FMO DATABASE

FMODB ID: 89VGY

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

Total energy (hartree)

FMO2-HF: Electronic energy	-953753.883882
FMO2-HF: Nuclear repulsion	907027.748145
FMO2-HF: Total energy	-46726.135737
FMO2-MP2: Total energy	-46858.251892

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.
-1.94	0.323	0.004	-1.025	-1.242	0.006

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 : 0.048 / q_NPA : 0.033

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

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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	-0.022	-0.018	3.859	-1.913	0.228	0.005	-1.021	-1.125	0.006
4	A	2	SER	0	-0.005	0.001	5.769	-0.048	-0.048	0.000	0.000	0.000	0.000
5	A	3	ALA	0	0.008	0.009	5.063	-0.171	-0.049	-0.001	-0.004	-0.117	0.000
6	A	4	ASN	0	-0.053	-0.032	7.207	-0.124	-0.124	0.000	0.000	0.000	0.000
7	A	5	ASP	-1	-0.815	-0.895	10.420	0.536	0.536	0.000	0.000	0.000	0.000
8	A	6	LYS	1	0.796	0.888	12.787	-0.883	-0.883	0.000	0.000	0.000	0.000
9	A	7	LEU	0	-0.025	0.020	14.488	0.097	0.097	0.000	0.000	0.000	0.000
10	A	8	THR	0	-0.012	-0.046	16.867	-0.047	-0.047	0.000	0.000	0.000	0.000
11	A	9	ILE	0	0.006	0.009	19.141	-0.005	-0.005	0.000	0.000	0.000	0.000
12	A	10	LEU	0	0.002	0.012	22.826	-0.016	-0.016	0.000	0.000	0.000	0.000
13	A	11	TRP	0	0.036	0.017	24.775	-0.012	-0.012	0.000	0.000	0.000	0.000
14	A	12	THR	0	0.015	0.027	28.230	-0.011	-0.011	0.000	0.000	0.000	0.000
15	A	13	THR	0	0.007	-0.006	30.964	-0.018	-0.018	0.000	0.000	0.000	0.000
16	A	14	ASP	-1	-0.851	-0.940	33.730	0.142	0.142	0.000	0.000	0.000	0.000
17	A	15	ASN	0	0.000	0.000	36.257	-0.003	-0.003	0.000	0.000	0.000	0.000
18	A	16	LYS	1	0.853	0.888	36.158	-0.097	-0.097	0.000	0.000	0.000	0.000
19	A	17	ASP	-1	-0.880	-0.912	37.052	0.118	0.118	0.000	0.000	0.000	0.000
20	A	18	THR	0	0.014	-0.011	31.897	0.004	0.004	0.000	0.000	0.000	0.000
21	A	19	VAL	0	-0.038	-0.016	32.457	0.012	0.012	0.000	0.000	0.000	0.000
22	A	20	PHE	0	0.028	0.008	32.599	0.006	0.006	0.000	0.000	0.000	0.000
23	A	21	ASN	0	-0.051	-0.037	33.680	-0.001	-0.001	0.000	0.000	0.000	0.000
24	A	22	MET	0	-0.042	-0.003	26.121	0.005	0.005	0.000	0.000	0.000	0.000
25	A	23	LEU	0	-0.002	-0.001	27.577	0.011	0.011	0.000	0.000	0.000	0.000
26	A	24	ALA	0	0.051	0.020	27.908	0.015	0.015	0.000	0.000	0.000	0.000
27	A	25	MET	0	0.040	0.033	29.239	0.000	0.000	0.000	0.000	0.000	0.000
28	A	26	TYR	0	0.007	0.008	22.239	0.009	0.009	0.000	0.000	0.000	0.000
29	A	27	ALA	0	0.031	0.024	24.502	0.013	0.013	0.000	0.000	0.000	0.000
30	A	28	LEU	0	0.054	0.024	25.090	0.008	0.008	0.000	0.000	0.000	0.000
31	A	29	ASN	0	-0.061	-0.034	27.118	-0.018	-0.018	0.000	0.000	0.000	0.000
32	A	30	SER	0	-0.011	-0.029	21.899	0.001	0.001	0.000	0.000	0.000	0.000
33	A	31	LYS	1	0.828	0.924	20.339	-0.218	-0.218	0.000	0.000	0.000	0.000
34	A	32	ASN	0	0.005	-0.006	23.530	-0.012	-0.012	0.000	0.000	0.000	0.000
35	A	33	ARG	1	0.823	0.918	24.936	-0.150	-0.150	0.000	0.000	0.000	0.000
36	A	34	GLY	0	-0.011	0.000	20.911	-0.008	-0.008	0.000	0.000	0.000	0.000
37	A	35	TRP	0	-0.081	-0.039	19.156	0.015	0.015	0.000	0.000	0.000	0.000
38	A	36	TRP	0	-0.010	-0.006	14.311	0.074	0.074	0.000	0.000	0.000	0.000
39	A	37	LYS	1	0.894	0.941	13.247	-0.336	-0.336	0.000	0.000	0.000	0.000
40	A	38	HIS	0	-0.003	0.005	13.849	-0.067	-0.067	0.000	0.000	0.000	0.000
41	A	39	ILE	0	0.027	0.007	17.566	0.057	0.057	0.000	0.000	0.000	0.000
42	A	40	ASN	0	-0.035	0.006	19.038	-0.063	-0.063	0.000	0.000	0.000	0.000
43	A	41	ILE	0	0.008	0.000	20.793	0.026	0.026	0.000	0.000	0.000	0.000
44	A	42	ILE	0	-0.004	0.000	20.981	-0.018	-0.018	0.000	0.000	0.000	0.000
45	A	43	LEU	0	0.014	0.008	25.365	-0.003	-0.003	0.000	0.000	0.000	0.000
46	A	44	TRP	0	0.020	-0.014	25.395	-0.004	-0.004	0.000	0.000	0.000	0.000
47	A	45	GLY	0	0.029	0.005	29.972	0.007	0.007	0.000	0.000	0.000	0.000
48	A	46	ALA	0	0.011	0.013	33.224	-0.007	-0.007	0.000	0.000	0.000	0.000
49	A	47	SER	0	-0.034	-0.024	31.075	-0.013	-0.013	0.000	0.000	0.000	0.000
50	A	48	VAL	0	0.032	0.008	32.467	-0.006	-0.006	0.000	0.000	0.000	0.000
51	A	49	LYS	1	0.927	0.972	34.773	-0.127	-0.127	0.000	0.000	0.000	0.000
52	A	50	LEU	0	0.012	0.025	35.685	-0.007	-0.007	0.000	0.000	0.000	0.000
53	A	51	VAL	0	0.016	0.005	33.062	-0.007	-0.007	0.000	0.000	0.000	0.000
54	A	52	ALA	0	-0.007	0.000	36.483	-0.006	-0.006	0.000	0.000	0.000	0.000
55	A	53	ASN	0	-0.070	-0.050	39.006	-0.011	-0.011	0.000	0.000	0.000	0.000
56	A	54	ASP	-1	-0.775	-0.861	39.607	0.099	0.099	0.000	0.000	0.000	0.000
57	A	55	THR	0	0.046	0.016	39.774	0.006	0.006	0.000	0.000	0.000	0.000
58	A	56	GLN	0	0.027	0.036	40.493	0.003	0.003	0.000	0.000	0.000	0.000
59	A	57	VAL	0	0.026	0.001	34.999	0.004	0.004	0.000	0.000	0.000	0.000
60	A	58	GLN	0	-0.045	-0.035	35.450	0.002	0.002	0.000	0.000	0.000	0.000
61	A	59	THR	0	-0.027	-0.016	36.154	-0.001	-0.001	0.000	0.000	0.000	0.000
62	A	60	GLU	-1	-0.879	-0.945	33.066	0.135	0.135	0.000	0.000	0.000	0.000
63	A	61	ILE	0	-0.057	-0.029	30.909	0.010	0.010	0.000	0.000	0.000	0.000
64	A	62	LEU	0	0.009	0.016	31.414	0.005	0.005	0.000	0.000	0.000	0.000
65	A	63	GLU	-1	-0.894	-0.943	31.787	0.113	0.113	0.000	0.000	0.000	0.000
66	A	64	MET	0	-0.010	-0.009	27.872	0.012	0.012	0.000	0.000	0.000	0.000
67	A	65	LEU	0	-0.003	0.009	27.489	0.009	0.009	0.000	0.000	0.000	0.000
68	A	66	GLN	0	-0.049	-0.023	28.286	-0.004	-0.004	0.000	0.000	0.000	0.000
69	A	67	SER	0	-0.047	-0.022	27.118	-0.002	-0.002	0.000	0.000	0.000	0.000
70	A	68	GLY	0	0.020	0.004	24.484	0.003	0.003	0.000	0.000	0.000	0.000
71	A	69	ILE	0	-0.080	-0.033	22.813	0.031	0.031	0.000	0.000	0.000	0.000
72	A	70	THR	0	-0.008	-0.023	21.040	-0.017	-0.017	0.000	0.000	0.000	0.000
73	A	71	ILE	0	0.025	0.008	23.412	0.023	0.023	0.000	0.000	0.000	0.000
74	A	72	GLU	-1	-0.700	-0.807	21.787	0.348	0.348	0.000	0.000	0.000	0.000
75	A	73	ALA	0	0.015	0.001	26.406	0.004	0.004	0.000	0.000	0.000	0.000
76	A	74	CYS	0	-0.008	0.010	28.943	-0.005	-0.005	0.000	0.000	0.000	0.000
77	A	75	GLN	0	-0.008	-0.001	29.717	-0.004	-0.004	0.000	0.000	0.000	0.000
78	A	76	ASP	-1	-0.814	-0.917	30.876	0.175	0.175	0.000	0.000	0.000	0.000
79	A	77	CYS	0	-0.052	-0.031	32.709	-0.009	-0.009	0.000	0.000	0.000	0.000
80	A	78	CYS	0	-0.027	-0.021	32.822	-0.009	-0.009	0.000	0.000	0.000	0.000
81	A	79	GLU	-1	-0.831	-0.878	35.725	0.119	0.119	0.000	0.000	0.000	0.000
82	A	80	ASN	0	-0.051	-0.041	36.861	-0.013	-0.013	0.000	0.000	0.000	0.000
83	A	81	PHE	0	-0.054	-0.041	36.151	-0.004	-0.004	0.000	0.000	0.000	0.000
84	A	82	GLY	0	0.009	0.019	40.382	-0.004	-0.004	0.000	0.000	0.000	0.000
85	A	83	VAL	0	-0.007	-0.010	37.314	-0.004	-0.004	0.000	0.000	0.000	0.000
86	A	84	ALA	0	0.016	0.012	36.202	0.002	0.002	0.000	0.000	0.000	0.000
87	A	85	SER	0	0.024	0.023	36.548	0.004	0.004	0.000	0.000	0.000	0.000
88	A	86	ILE	0	0.017	0.014	38.601	-0.001	-0.001	0.000	0.000	0.000	0.000
89	A	87	ILE	0	-0.004	-0.014	32.742	0.001	0.001	0.000	0.000	0.000	0.000
90	A	88	THR	0	0.008	-0.014	33.809	0.006	0.006	0.000	0.000	0.000	0.000
91	A	89	ASN	0	-0.044	-0.028	34.834	-0.001	-0.001	0.000	0.000	0.000	0.000
92	A	90	LEU	0	-0.053	-0.012	34.714	-0.004	-0.004	0.000	0.000	0.000	0.000
93	A	91	GLY	0	0.007	0.009	32.463	0.003	0.003	0.000	0.000	0.000	0.000
94	A	92	ILE	0	-0.062	-0.015	28.964	0.012	0.012	0.000	0.000	0.000	0.000
95	A	93	THR	0	-0.002	-0.015	25.286	-0.011	-0.011	0.000	0.000	0.000	0.000
96	A	94	VAL	0	-0.006	-0.005	27.972	0.019	0.019	0.000	0.000	0.000	0.000
97	A	95	ARG	1	0.851	0.907	20.437	-0.321	-0.321	0.000	0.000	0.000	0.000
98	A	96	TYR	0	-0.010	-0.031	28.325	0.012	0.012	0.000	0.000	0.000	0.000
99	A	97	MET	0	-0.019	0.010	22.422	0.012	0.012	0.000	0.000	0.000	0.000
100	A	98	GLY	0	0.003	0.008	24.065	0.030	0.030	0.000	0.000	0.000	0.000
101	A	99	ILE	0	0.027	0.021	20.642	0.027	0.027	0.000	0.000	0.000	0.000
102	A	100	PRO	0	0.017	0.003	19.890	0.048	0.048	0.000	0.000	0.000	0.000
103	A	101	LEU	0	0.034	0.024	19.095	0.062	0.062	0.000	0.000	0.000	0.000
104	A	102	THR	0	-0.043	-0.032	19.610	0.040	0.040	0.000	0.000	0.000	0.000
105	A	103	GLU	-1	-0.877	-0.952	15.063	0.740	0.740	0.000	0.000	0.000	0.000
106	A	104	TYR	0	-0.075	-0.056	14.940	0.139	0.139	0.000	0.000	0.000	0.000
107	A	105	LEU	0	-0.011	-0.003	15.010	0.110	0.110	0.000	0.000	0.000	0.000
108	A	106	LYS	1	0.902	0.958	14.844	-0.443	-0.443	0.000	0.000	0.000	0.000
109	A	107	ASN	0	-0.083	-0.051	10.673	0.269	0.269	0.000	0.000	0.000	0.000
110	A	108	GLY	0	-0.009	0.010	10.432	0.350	0.350	0.000	0.000	0.000	0.000
111	A	109	GLU	-1	-0.797	-0.870	12.338	0.930	0.930	0.000	0.000	0.000	0.000
112	A	110	LYS	1	0.908	0.948	10.750	-1.593	-1.593	0.000	0.000	0.000	0.000
113	A	111	ILE	0	-0.006	-0.006	15.902	-0.070	-0.070	0.000	0.000	0.000	0.000
114	A	112	LEU	0	0.014	0.009	19.217	-0.029	-0.029	0.000	0.000	0.000	0.000
115	A	113	SER	0	-0.015	-0.011	22.542	-0.009	-0.009	0.000	0.000	0.000	0.000
116	A	114	ILE	0	0.006	0.002	25.193	-0.025	-0.025	0.000	0.000	0.000	0.000

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