FMO DATABASE

FMODB ID: KGVR3

Calculation Name: 2FI9-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2FI9

Chain ID: A

ChEMBL ID:

UniProt ID: Q8RIU4

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:

Apendix: None

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
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	118
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-951992.693863
FMO2-HF: Nuclear repulsion	906782.709717
FMO2-HF: Total energy	-45209.984145
FMO2-MP2: Total energy	-45341.67203

3D Structure Molmil

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:11:HIS)

Summations of interaction energy for fragment #1(A:11:HIS)

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.
-8.462	1.185	10.304	-7.525	-12.43	-0.033

Interaction energy analysis for fragmet #1(A:11:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.023 / q_NPA : 0.009

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	13	PRO	0	-0.015	0.003	3.457	1.026	3.883	0.275	-1.101	-2.032	0.005
4	A	14	GLY	0	0.074	0.047	4.640	-1.040	-0.938	-0.001	-0.006	-0.095	0.000
5	A	15	ARG	1	0.829	0.921	6.838	0.351	0.351	0.000	0.000	0.000	0.000
6	A	16	ALA	0	0.011	0.002	8.114	-0.122	-0.122	0.000	0.000	0.000	0.000
7	A	17	PRO	0	0.010	0.003	10.050	0.080	0.080	0.000	0.000	0.000	0.000
8	A	18	ILE	0	-0.029	-0.017	7.995	0.023	0.023	0.000	0.000	0.000	0.000
9	A	19	ASP	-1	-0.871	-0.939	10.630	0.288	0.288	0.000	0.000	0.000	0.000
10	A	20	ALA	0	-0.071	-0.043	11.635	-0.049	-0.049	0.000	0.000	0.000	0.000
11	A	21	TYR	0	0.046	0.029	11.526	0.076	0.076	0.000	0.000	0.000	0.000
12	A	22	GLY	0	-0.007	0.009	13.517	-0.095	-0.095	0.000	0.000	0.000	0.000
13	A	23	ASN	0	-0.039	-0.042	13.889	0.014	0.014	0.000	0.000	0.000	0.000
14	A	24	GLY	0	0.062	0.043	14.157	0.051	0.051	0.000	0.000	0.000	0.000
15	A	25	GLY	0	-0.040	-0.028	10.324	0.222	0.222	0.000	0.000	0.000	0.000
16	A	26	PHE	0	-0.024	-0.006	7.469	-0.256	-0.256	0.000	0.000	0.000	0.000
17	A	27	ARG	1	0.935	0.971	7.969	-0.318	-0.318	0.000	0.000	0.000	0.000
18	A	28	PHE	0	0.059	0.019	2.434	-0.703	0.233	0.516	-0.435	-1.018	0.002
19	A	29	ALA	0	0.032	0.033	6.453	-0.180	-0.180	0.000	0.000	0.000	0.000
20	A	30	ASP	-1	-0.945	-0.967	8.257	0.041	0.041	0.000	0.000	0.000	0.000
21	A	31	MET	0	-0.073	-0.021	2.280	-0.441	0.062	0.896	-0.447	-0.953	-0.002
22	A	32	SER	0	-0.048	-0.035	6.885	0.131	0.131	0.000	0.000	0.000	0.000
23	A	33	HIS	0	-0.028	-0.010	3.593	0.652	1.331	0.033	-0.265	-0.447	0.002
24	A	34	ARG	1	0.937	0.976	4.961	-4.000	-4.000	0.000	0.000	0.000	0.000
25	A	35	GLY	0	0.065	0.012	8.930	0.359	0.359	0.000	0.000	0.000	0.000
26	A	36	SER	0	0.014	-0.002	9.191	0.066	0.066	0.000	0.000	0.000	0.000
27	A	37	ILE	0	-0.021	0.003	5.416	0.545	0.545	0.000	0.000	0.000	0.000
28	A	38	ILE	0	0.004	0.014	7.298	-0.657	-0.657	0.000	0.000	0.000	0.000
29	A	39	CYS	0	-0.048	-0.017	6.789	0.714	0.714	0.000	0.000	0.000	0.000
30	A	40	ILE	0	0.037	0.014	6.801	-0.226	-0.226	0.000	0.000	0.000	0.000
31	A	41	PRO	0	0.002	-0.010	7.957	0.106	0.106	0.000	0.000	0.000	0.000
32	A	42	SER	0	-0.052	-0.051	5.757	-0.249	-0.249	0.000	0.000	0.000	0.000
33	A	43	GLY	0	-0.012	-0.003	3.567	-1.636	-1.383	0.003	-0.077	-0.179	0.000
34	A	44	ILE	0	-0.056	-0.022	3.323	-2.228	-1.250	0.023	-0.329	-0.672	0.000
35	A	45	TYR	0	-0.030	-0.031	2.095	-0.689	2.462	8.560	-4.834	-6.877	-0.040
36	A	46	GLY	0	0.000	-0.001	4.103	-1.239	-1.051	-0.001	-0.031	-0.157	0.000
37	A	47	ILE	0	-0.039	-0.028	6.010	-0.851	-0.851	0.000	0.000	0.000	0.000
38	A	48	ASP	-1	-0.923	-0.965	9.566	0.948	0.948	0.000	0.000	0.000	0.000
39	A	49	MET	0	-0.050	0.009	12.286	-0.136	-0.136	0.000	0.000	0.000	0.000
40	A	50	THR	0	0.024	0.002	15.074	0.030	0.030	0.000	0.000	0.000	0.000
41	A	51	GLY	0	-0.013	-0.015	18.199	-0.037	-0.037	0.000	0.000	0.000	0.000
42	A	52	PRO	0	-0.018	-0.011	18.397	0.033	0.033	0.000	0.000	0.000	0.000
43	A	53	VAL	0	-0.044	-0.020	19.458	-0.005	-0.005	0.000	0.000	0.000	0.000
44	A	54	PRO	0	-0.013	0.008	17.203	0.005	0.005	0.000	0.000	0.000	0.000
45	A	55	THR	0	0.002	-0.036	17.741	-0.083	-0.083	0.000	0.000	0.000	0.000
46	A	56	GLN	0	0.018	-0.026	18.383	0.020	0.020	0.000	0.000	0.000	0.000
47	A	57	GLU	-1	-0.895	-0.944	15.317	0.009	0.009	0.000	0.000	0.000	0.000
48	A	58	ASP	-1	-0.814	-0.857	14.172	0.486	0.486	0.000	0.000	0.000	0.000
49	A	59	ILE	0	-0.024	-0.015	13.311	0.079	0.079	0.000	0.000	0.000	0.000
50	A	60	SER	0	-0.034	-0.029	12.952	-0.100	-0.100	0.000	0.000	0.000	0.000
51	A	61	ARG	1	1.008	1.005	5.593	2.300	2.300	0.000	0.000	0.000	0.000
52	A	62	VAL	0	0.002	0.001	10.878	-0.066	-0.066	0.000	0.000	0.000	0.000
53	A	63	LEU	0	-0.019	-0.013	12.945	-0.044	-0.044	0.000	0.000	0.000	0.000
54	A	64	GLU	-1	-0.951	-0.980	11.422	-0.796	-0.796	0.000	0.000	0.000	0.000
55	A	65	GLU	-1	-0.801	-0.866	7.905	-1.286	-1.286	0.000	0.000	0.000	0.000
56	A	66	SER	0	0.022	0.002	12.852	0.061	0.061	0.000	0.000	0.000	0.000
57	A	67	ASP	-1	-0.954	-0.963	16.255	-0.263	-0.263	0.000	0.000	0.000	0.000
58	A	68	GLN	0	-0.083	-0.044	13.403	-0.027	-0.027	0.000	0.000	0.000	0.000
59	A	69	ILE	0	-0.061	-0.026	11.863	0.059	0.059	0.000	0.000	0.000	0.000
60	A	70	GLU	-1	-0.904	-0.941	16.099	-0.023	-0.023	0.000	0.000	0.000	0.000
61	A	71	VAL	0	-0.043	-0.023	18.350	0.012	0.012	0.000	0.000	0.000	0.000
62	A	72	LEU	0	-0.009	0.002	14.825	0.018	0.018	0.000	0.000	0.000	0.000
63	A	73	LEU	0	-0.034	-0.014	16.381	-0.015	-0.015	0.000	0.000	0.000	0.000
64	A	74	ILE	0	0.018	-0.003	15.961	0.067	0.067	0.000	0.000	0.000	0.000
65	A	75	GLY	0	0.029	0.000	16.113	-0.046	-0.046	0.000	0.000	0.000	0.000
66	A	76	THR	0	-0.029	-0.018	16.686	0.058	0.058	0.000	0.000	0.000	0.000
67	A	77	GLY	0	0.046	0.007	18.014	-0.028	-0.028	0.000	0.000	0.000	0.000
68	A	78	VAL	0	-0.043	-0.032	19.094	-0.011	-0.011	0.000	0.000	0.000	0.000
69	A	79	GLU	-1	-0.895	-0.940	21.964	0.218	0.218	0.000	0.000	0.000	0.000
70	A	80	LEU	0	-0.034	0.012	23.112	0.025	0.025	0.000	0.000	0.000	0.000
71	A	81	LEU	0	0.000	0.000	22.725	-0.026	-0.026	0.000	0.000	0.000	0.000
72	A	82	ARG	1	0.948	0.970	24.557	-0.133	-0.133	0.000	0.000	0.000	0.000
73	A	83	LEU	0	0.064	0.045	21.317	0.014	0.014	0.000	0.000	0.000	0.000
74	A	84	PRO	0	0.045	0.019	23.298	-0.023	-0.023	0.000	0.000	0.000	0.000
75	A	85	GLU	-1	-0.858	-0.927	25.825	0.056	0.056	0.000	0.000	0.000	0.000
76	A	86	GLU	-1	-0.863	-0.947	25.166	0.075	0.075	0.000	0.000	0.000	0.000
77	A	87	LEU	0	0.006	-0.004	20.045	-0.019	-0.019	0.000	0.000	0.000	0.000
78	A	88	ARG	1	0.770	0.886	22.738	-0.099	-0.099	0.000	0.000	0.000	0.000
79	A	89	VAL	0	-0.004	0.004	25.197	-0.011	-0.011	0.000	0.000	0.000	0.000
80	A	90	LEU	0	0.025	0.019	20.796	-0.012	-0.012	0.000	0.000	0.000	0.000
81	A	91	LEU	0	0.024	0.003	17.988	-0.022	-0.022	0.000	0.000	0.000	0.000
82	A	92	TRP	0	0.040	0.023	21.591	-0.023	-0.023	0.000	0.000	0.000	0.000
83	A	93	GLU	-1	-0.971	-0.991	23.820	-0.080	-0.080	0.000	0.000	0.000	0.000
84	A	94	LYS	1	0.825	0.918	17.783	0.236	0.236	0.000	0.000	0.000	0.000
85	A	95	ARG	1	0.792	0.893	21.186	0.048	0.048	0.000	0.000	0.000	0.000
86	A	96	ILE	0	0.029	0.035	16.791	0.002	0.002	0.000	0.000	0.000	0.000
87	A	97	SER	0	-0.063	-0.025	21.004	0.019	0.019	0.000	0.000	0.000	0.000
88	A	98	SER	0	0.014	-0.013	20.717	0.010	0.010	0.000	0.000	0.000	0.000
89	A	99	ASP	-1	-0.916	-0.960	21.122	0.160	0.160	0.000	0.000	0.000	0.000
90	A	100	THR	0	-0.073	-0.040	20.828	0.027	0.027	0.000	0.000	0.000	0.000
91	A	101	MET	0	-0.011	0.002	20.138	-0.020	-0.020	0.000	0.000	0.000	0.000
92	A	102	SER	0	0.036	0.024	20.379	0.038	0.038	0.000	0.000	0.000	0.000
93	A	103	THR	0	0.020	-0.033	14.408	-0.031	-0.031	0.000	0.000	0.000	0.000
94	A	104	GLY	0	-0.008	-0.005	16.434	0.019	0.019	0.000	0.000	0.000	0.000
95	A	105	ALA	0	-0.030	-0.016	18.235	-0.011	-0.011	0.000	0.000	0.000	0.000
96	A	106	ALA	0	0.063	0.039	16.453	-0.022	-0.022	0.000	0.000	0.000	0.000
97	A	107	VAL	0	0.014	0.012	12.722	-0.003	-0.003	0.000	0.000	0.000	0.000
98	A	108	ARG	1	0.892	0.941	15.188	-0.349	-0.349	0.000	0.000	0.000	0.000
99	A	109	THR	0	0.012	-0.005	18.231	-0.037	-0.037	0.000	0.000	0.000	0.000
100	A	110	PHE	0	0.008	-0.008	10.925	-0.018	-0.018	0.000	0.000	0.000	0.000
101	A	111	ASN	0	-0.015	-0.013	13.726	0.005	0.005	0.000	0.000	0.000	0.000
102	A	112	VAL	0	-0.016	0.001	16.105	-0.031	-0.031	0.000	0.000	0.000	0.000
103	A	113	LEU	0	0.022	0.002	18.463	-0.024	-0.024	0.000	0.000	0.000	0.000
104	A	114	LEU	0	-0.019	-0.010	12.542	-0.029	-0.029	0.000	0.000	0.000	0.000
105	A	115	ALA	0	-0.032	-0.013	16.643	-0.031	-0.031	0.000	0.000	0.000	0.000
106	A	116	GLU	-1	-0.949	-0.958	19.101	0.085	0.085	0.000	0.000	0.000	0.000
107	A	117	ASP	-1	-0.958	-0.967	18.577	0.021	0.021	0.000	0.000	0.000	0.000
108	A	118	ARG	1	0.866	0.931	19.599	-0.097	-0.097	0.000	0.000	0.000	0.000
109	A	119	ALA	0	0.064	0.040	16.481	0.023	0.023	0.000	0.000	0.000	0.000
110	A	120	VAL	0	-0.045	-0.022	15.104	-0.002	-0.002	0.000	0.000	0.000	0.000
111	A	121	ALA	0	0.033	0.018	12.804	0.015	0.015	0.000	0.000	0.000	0.000
112	A	122	ALA	0	-0.015	-0.013	11.986	-0.044	-0.044	0.000	0.000	0.000	0.000
113	A	123	LEU	0	0.000	0.020	11.299	0.148	0.148	0.000	0.000	0.000	0.000
114	A	124	LEU	0	-0.022	-0.023	10.300	-0.157	-0.157	0.000	0.000	0.000	0.000
115	A	125	PHE	0	0.063	0.023	11.804	0.205	0.205	0.000	0.000	0.000	0.000
116	A	126	ALA	0	-0.002	0.019	11.392	-0.083	-0.083	0.000	0.000	0.000	0.000
117	A	127	VAL	0	-0.020	0.005	13.344	-0.090	-0.090	0.000	0.000	0.000	0.000
118	A	128	GLU	-1	-0.926	-0.954	15.871	0.631	0.631	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:11:HIS)