FMO DATABASE

FMODB ID: G5281

Calculation Name: 2FB6-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2FB6

Chain ID: A

ChEMBL ID:

UniProt ID: Q8A7V2

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	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	116
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-951295.66081
FMO2-HF: Nuclear repulsion	904569.593308
FMO2-HF: Total energy	-46726.067502
FMO2-MP2: Total energy	-46858.193836

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:-1:ASN)

Summations of interaction energy for fragment #1(A:-1:ASN)

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.
-2.534	-0.282	-0.006	-1.106	-1.14	0.008

Interaction energy analysis for fragmet #1(A:-1:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.034 / q_NPA : 0.016

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	1	MET	0	0.008	-0.006	3.835	-1.718	0.424	-0.005	-1.103	-1.033	0.008
4	A	2	SER	0	0.001	0.002	6.376	-0.154	-0.154	0.000	0.000	0.000	0.000
5	A	3	ALA	0	0.008	0.007	5.037	-0.293	-0.183	-0.001	-0.003	-0.107	0.000
6	A	4	ASN	0	-0.036	-0.023	7.171	-0.379	-0.379	0.000	0.000	0.000	0.000
7	A	5	ASP	-1	-0.818	-0.900	10.209	0.859	0.859	0.000	0.000	0.000	0.000
8	A	6	LYS	1	0.840	0.901	12.563	-0.856	-0.856	0.000	0.000	0.000	0.000
9	A	7	LEU	0	-0.033	0.006	14.330	0.077	0.077	0.000	0.000	0.000	0.000
10	A	8	THR	0	-0.001	-0.033	17.057	-0.069	-0.069	0.000	0.000	0.000	0.000
11	A	9	ILE	0	-0.009	0.001	19.228	-0.001	-0.001	0.000	0.000	0.000	0.000
12	A	10	LEU	0	-0.004	0.006	22.833	-0.016	-0.016	0.000	0.000	0.000	0.000
13	A	11	TRP	0	0.030	0.006	24.818	-0.008	-0.008	0.000	0.000	0.000	0.000
14	A	12	THR	0	0.001	0.013	28.257	-0.011	-0.011	0.000	0.000	0.000	0.000
15	A	13	THR	0	-0.018	-0.013	31.038	-0.016	-0.016	0.000	0.000	0.000	0.000
16	A	14	ASP	-1	-0.855	-0.939	33.610	0.126	0.126	0.000	0.000	0.000	0.000
17	A	15	ASN	0	0.041	0.031	36.129	-0.003	-0.003	0.000	0.000	0.000	0.000
18	A	16	LYS	1	0.873	0.897	36.243	-0.094	-0.094	0.000	0.000	0.000	0.000
19	A	17	ASP	-1	-0.908	-0.933	37.205	0.117	0.117	0.000	0.000	0.000	0.000
20	A	18	THR	0	-0.002	-0.025	32.057	0.007	0.007	0.000	0.000	0.000	0.000
21	A	19	VAL	0	-0.031	-0.017	32.592	0.012	0.012	0.000	0.000	0.000	0.000
22	A	20	PHE	0	0.032	0.013	32.710	0.007	0.007	0.000	0.000	0.000	0.000
23	A	21	ASN	0	-0.034	-0.029	33.729	0.003	0.003	0.000	0.000	0.000	0.000
24	A	22	MET	0	-0.060	-0.005	26.408	0.007	0.007	0.000	0.000	0.000	0.000
25	A	23	LEU	0	-0.005	-0.016	27.452	0.015	0.015	0.000	0.000	0.000	0.000
26	A	24	ALA	0	0.058	0.026	28.016	0.018	0.018	0.000	0.000	0.000	0.000
27	A	25	MET	0	0.037	0.033	29.410	0.003	0.003	0.000	0.000	0.000	0.000
28	A	26	TYR	0	0.009	0.010	21.911	0.016	0.016	0.000	0.000	0.000	0.000
29	A	27	ALA	0	0.036	0.023	24.461	0.020	0.020	0.000	0.000	0.000	0.000
30	A	28	LEU	0	0.062	0.030	24.986	0.017	0.017	0.000	0.000	0.000	0.000
31	A	29	ASN	0	-0.066	-0.037	26.957	-0.010	-0.010	0.000	0.000	0.000	0.000
32	A	30	SER	0	-0.009	-0.026	21.772	0.011	0.011	0.000	0.000	0.000	0.000
33	A	31	LYS	1	0.865	0.947	20.071	-0.277	-0.277	0.000	0.000	0.000	0.000
34	A	32	ASN	0	-0.005	-0.010	23.338	-0.004	-0.004	0.000	0.000	0.000	0.000
35	A	33	ARG	1	0.835	0.926	24.893	-0.199	-0.199	0.000	0.000	0.000	0.000
36	A	34	GLY	0	0.000	0.015	20.908	-0.005	-0.005	0.000	0.000	0.000	0.000
37	A	35	TRP	0	-0.092	-0.047	19.418	0.023	0.023	0.000	0.000	0.000	0.000
38	A	36	TRP	0	-0.010	-0.003	14.094	0.087	0.087	0.000	0.000	0.000	0.000
39	A	37	LYS	1	0.885	0.938	13.718	-0.613	-0.613	0.000	0.000	0.000	0.000
40	A	38	HIS	0	-0.024	-0.008	13.647	-0.099	-0.099	0.000	0.000	0.000	0.000
41	A	39	ILE	0	0.037	0.014	17.365	0.060	0.060	0.000	0.000	0.000	0.000
42	A	40	ASN	0	-0.024	0.012	19.245	-0.065	-0.065	0.000	0.000	0.000	0.000
43	A	41	ILE	0	0.011	0.003	20.876	0.021	0.021	0.000	0.000	0.000	0.000
44	A	42	ILE	0	-0.004	0.003	21.213	-0.017	-0.017	0.000	0.000	0.000	0.000
45	A	43	LEU	0	0.019	0.013	25.343	-0.003	-0.003	0.000	0.000	0.000	0.000
46	A	44	TRP	0	0.027	-0.023	25.470	-0.007	-0.007	0.000	0.000	0.000	0.000
47	A	45	GLY	0	0.022	0.013	30.298	0.006	0.006	0.000	0.000	0.000	0.000
48	A	46	ALA	0	0.011	0.001	33.448	-0.005	-0.005	0.000	0.000	0.000	0.000
49	A	47	SER	0	-0.025	-0.026	31.210	-0.011	-0.011	0.000	0.000	0.000	0.000
50	A	48	VAL	0	0.020	0.009	32.584	-0.004	-0.004	0.000	0.000	0.000	0.000
51	A	49	LYS	1	0.943	0.980	34.958	-0.103	-0.103	0.000	0.000	0.000	0.000
52	A	50	LEU	0	0.025	0.031	36.015	-0.005	-0.005	0.000	0.000	0.000	0.000
53	A	51	VAL	0	0.013	0.004	33.210	-0.005	-0.005	0.000	0.000	0.000	0.000
54	A	52	ALA	0	-0.020	-0.009	36.667	-0.005	-0.005	0.000	0.000	0.000	0.000
55	A	53	ASN	0	-0.061	-0.048	39.114	-0.010	-0.010	0.000	0.000	0.000	0.000
56	A	54	ASP	-1	-0.780	-0.855	39.858	0.096	0.096	0.000	0.000	0.000	0.000
57	A	55	THR	0	0.044	0.013	40.019	0.006	0.006	0.000	0.000	0.000	0.000
58	A	56	GLN	0	0.035	0.024	40.582	0.005	0.005	0.000	0.000	0.000	0.000
59	A	57	VAL	0	0.011	0.000	35.242	0.005	0.005	0.000	0.000	0.000	0.000
60	A	58	GLN	0	-0.048	-0.031	35.821	0.004	0.004	0.000	0.000	0.000	0.000
61	A	59	THR	0	-0.021	-0.010	36.244	0.001	0.001	0.000	0.000	0.000	0.000
62	A	60	GLU	-1	-0.881	-0.943	33.361	0.146	0.146	0.000	0.000	0.000	0.000
63	A	61	ILE	0	-0.059	-0.028	31.163	0.011	0.011	0.000	0.000	0.000	0.000
64	A	62	LEU	0	0.003	0.006	31.518	0.007	0.007	0.000	0.000	0.000	0.000
65	A	63	GLU	-1	-0.894	-0.939	31.994	0.138	0.138	0.000	0.000	0.000	0.000
66	A	64	MET	0	-0.023	-0.027	28.061	0.016	0.016	0.000	0.000	0.000	0.000
67	A	65	LEU	0	-0.014	0.004	27.607	0.013	0.013	0.000	0.000	0.000	0.000
68	A	66	GLN	0	-0.052	-0.020	28.259	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	67	SER	0	-0.051	-0.024	27.029	0.004	0.004	0.000	0.000	0.000	0.000
70	A	68	GLY	0	0.006	-0.010	24.361	0.011	0.011	0.000	0.000	0.000	0.000
71	A	69	ILE	0	-0.101	-0.039	22.943	0.032	0.032	0.000	0.000	0.000	0.000
72	A	70	THR	0	-0.002	-0.015	21.439	-0.017	-0.017	0.000	0.000	0.000	0.000
73	A	71	ILE	0	0.026	0.000	23.750	0.018	0.018	0.000	0.000	0.000	0.000
74	A	72	GLU	-1	-0.701	-0.798	22.022	0.283	0.283	0.000	0.000	0.000	0.000
75	A	73	ALA	0	0.017	0.000	26.616	0.008	0.008	0.000	0.000	0.000	0.000
76	A	74	CYS	0	-0.024	0.001	29.085	-0.009	-0.009	0.000	0.000	0.000	0.000
77	A	75	GLN	0	0.008	0.002	29.954	-0.002	-0.002	0.000	0.000	0.000	0.000
78	A	76	ASP	-1	-0.804	-0.910	31.197	0.119	0.119	0.000	0.000	0.000	0.000
79	A	77	CYS	0	-0.061	-0.032	32.934	-0.005	-0.005	0.000	0.000	0.000	0.000
80	A	78	CYS	0	-0.025	-0.014	33.075	-0.006	-0.006	0.000	0.000	0.000	0.000
81	A	79	GLU	-1	-0.838	-0.896	35.755	0.085	0.085	0.000	0.000	0.000	0.000
82	A	80	ASN	0	-0.069	-0.052	36.864	-0.010	-0.010	0.000	0.000	0.000	0.000
83	A	81	PHE	0	-0.068	-0.051	36.214	-0.004	-0.004	0.000	0.000	0.000	0.000
84	A	82	GLY	0	0.026	0.033	40.334	-0.003	-0.003	0.000	0.000	0.000	0.000
85	A	83	VAL	0	-0.022	-0.020	37.383	-0.002	-0.002	0.000	0.000	0.000	0.000
86	A	84	ALA	0	0.024	0.018	36.181	0.004	0.004	0.000	0.000	0.000	0.000
87	A	85	SER	0	0.023	0.017	36.570	0.004	0.004	0.000	0.000	0.000	0.000
88	A	86	ILE	0	0.018	0.011	38.541	0.000	0.000	0.000	0.000	0.000	0.000
89	A	87	ILE	0	0.011	-0.007	32.985	0.003	0.003	0.000	0.000	0.000	0.000
90	A	88	THR	0	0.008	-0.015	33.474	0.006	0.006	0.000	0.000	0.000	0.000
91	A	89	ASN	0	-0.048	-0.029	34.598	0.000	0.000	0.000	0.000	0.000	0.000
92	A	90	LEU	0	-0.048	-0.006	34.775	-0.002	-0.002	0.000	0.000	0.000	0.000
93	A	91	GLY	0	0.006	0.009	32.458	0.004	0.004	0.000	0.000	0.000	0.000
94	A	92	ILE	0	-0.068	-0.020	29.225	0.012	0.012	0.000	0.000	0.000	0.000
95	A	93	THR	0	-0.016	-0.008	25.441	-0.012	-0.012	0.000	0.000	0.000	0.000
96	A	94	VAL	0	0.007	0.008	28.444	0.012	0.012	0.000	0.000	0.000	0.000
97	A	95	ARG	1	0.876	0.916	20.222	-0.254	-0.254	0.000	0.000	0.000	0.000
98	A	96	TYR	0	-0.014	-0.020	27.964	0.010	0.010	0.000	0.000	0.000	0.000
99	A	97	MET	0	0.000	0.009	22.711	0.007	0.007	0.000	0.000	0.000	0.000
100	A	98	GLY	0	-0.011	0.002	24.211	0.022	0.022	0.000	0.000	0.000	0.000
101	A	99	ILE	0	0.026	0.011	20.267	0.019	0.019	0.000	0.000	0.000	0.000
102	A	100	PRO	0	0.041	0.022	19.608	0.030	0.030	0.000	0.000	0.000	0.000
103	A	101	LEU	0	0.027	0.022	19.168	0.051	0.051	0.000	0.000	0.000	0.000
104	A	102	THR	0	-0.032	-0.024	19.403	0.034	0.034	0.000	0.000	0.000	0.000
105	A	103	GLU	-1	-0.903	-0.963	14.945	0.427	0.427	0.000	0.000	0.000	0.000
106	A	104	TYR	0	-0.076	-0.058	15.098	0.103	0.103	0.000	0.000	0.000	0.000
107	A	105	LEU	0	-0.004	-0.007	15.145	0.101	0.101	0.000	0.000	0.000	0.000
108	A	106	LYS	1	0.910	0.960	14.885	-0.235	-0.235	0.000	0.000	0.000	0.000
109	A	107	ASN	0	-0.078	-0.050	10.637	0.151	0.151	0.000	0.000	0.000	0.000
110	A	108	GLY	0	-0.012	0.013	10.524	0.325	0.325	0.000	0.000	0.000	0.000
111	A	109	GLU	-1	-0.856	-0.890	12.402	0.878	0.878	0.000	0.000	0.000	0.000
112	A	110	LYS	1	0.912	0.962	10.983	-1.543	-1.543	0.000	0.000	0.000	0.000
113	A	111	ILE	0	0.015	-0.007	15.853	-0.034	-0.034	0.000	0.000	0.000	0.000
114	A	112	LEU	0	0.001	0.017	19.298	-0.027	-0.027	0.000	0.000	0.000	0.000
115	A	113	SER	0	-0.011	-0.013	22.621	-0.005	-0.005	0.000	0.000	0.000	0.000
116	A	114	ILE	0	0.030	0.013	25.311	-0.021	-0.021	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-1:ASN)