FMO DATABASE

FMODB ID: 76Z5K

Calculation Name: 2A1V-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2A1V

Chain ID: A

ChEMBL ID:

UniProt ID: Q9RRT5

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	138
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1250730.848084
FMO2-HF: Nuclear repulsion	1196716.334535
FMO2-HF: Total energy	-54014.51355
FMO2-MP2: Total energy	-54173.601361

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:3:LEU)

Summations of interaction energy for fragment #1(A:3:LEU)

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.
-7.378	-3.617	1.365	-2.231	-2.893	-0.015

Interaction energy analysis for fragmet #1(A:3:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.017 / q_NPA : -0.010

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	5	THR	0	0.061	0.049	2.496	-4.529	-0.910	1.366	-2.223	-2.761	-0.015
4	A	6	PRO	0	0.014	-0.018	4.506	0.438	0.580	-0.001	-0.008	-0.132	0.000
5	A	7	MET	0	-0.079	-0.029	7.382	0.281	0.281	0.000	0.000	0.000	0.000
6	A	8	GLN	0	-0.013	-0.022	9.873	0.306	0.306	0.000	0.000	0.000	0.000
7	A	9	THR	0	-0.025	-0.002	10.870	0.152	0.152	0.000	0.000	0.000	0.000
8	A	10	VAL	0	0.051	0.003	12.787	-0.097	-0.097	0.000	0.000	0.000	0.000
9	A	11	ASP	-1	-0.882	-0.937	11.166	-0.843	-0.843	0.000	0.000	0.000	0.000
10	A	12	ASP	-1	-0.750	-0.871	8.213	-2.075	-2.075	0.000	0.000	0.000	0.000
11	A	13	LEU	0	-0.040	-0.008	9.633	-0.165	-0.165	0.000	0.000	0.000	0.000
12	A	14	ARG	1	0.849	0.888	12.534	0.622	0.622	0.000	0.000	0.000	0.000
13	A	15	SER	0	-0.028	-0.011	7.774	-0.202	-0.202	0.000	0.000	0.000	0.000
14	A	16	VAL	0	-0.021	0.002	8.193	-0.017	-0.017	0.000	0.000	0.000	0.000
15	A	17	CYS	0	-0.070	-0.062	9.856	0.195	0.195	0.000	0.000	0.000	0.000
16	A	18	ASP	-1	-0.900	-0.946	11.732	-0.625	-0.625	0.000	0.000	0.000	0.000
17	A	19	GLU	-1	-0.885	-0.919	7.581	-1.211	-1.211	0.000	0.000	0.000	0.000
18	A	20	LEU	0	-0.102	-0.043	11.978	0.131	0.131	0.000	0.000	0.000	0.000
19	A	21	PRO	0	0.000	-0.006	14.800	0.027	0.027	0.000	0.000	0.000	0.000
20	A	22	HIS	0	0.006	-0.007	18.012	-0.014	-0.014	0.000	0.000	0.000	0.000
21	A	23	SER	0	0.041	0.048	17.097	0.021	0.021	0.000	0.000	0.000	0.000
22	A	24	LEU	0	-0.011	-0.013	19.436	0.015	0.015	0.000	0.000	0.000	0.000
23	A	25	GLU	-1	-0.756	-0.844	17.421	-0.548	-0.548	0.000	0.000	0.000	0.000
24	A	26	THR	0	-0.086	-0.053	21.674	0.044	0.044	0.000	0.000	0.000	0.000
25	A	27	PHE	0	0.096	0.041	22.180	-0.028	-0.028	0.000	0.000	0.000	0.000
26	A	28	PRO	0	-0.105	-0.046	26.939	0.017	0.017	0.000	0.000	0.000	0.000
27	A	29	PHE	0	-0.035	-0.016	27.950	0.014	0.014	0.000	0.000	0.000	0.000
28	A	30	ASP	-1	-0.892	-0.946	31.352	-0.164	-0.164	0.000	0.000	0.000	0.000
29	A	31	ASP	-1	-0.870	-0.903	28.972	-0.244	-0.244	0.000	0.000	0.000	0.000
30	A	32	GLU	-1	-0.922	-0.963	25.234	-0.262	-0.262	0.000	0.000	0.000	0.000
31	A	33	THR	0	-0.064	-0.068	24.457	-0.040	-0.040	0.000	0.000	0.000	0.000
32	A	34	LEU	0	-0.028	0.011	18.377	0.018	0.018	0.000	0.000	0.000	0.000
33	A	35	VAL	0	-0.077	-0.057	22.354	-0.011	-0.011	0.000	0.000	0.000	0.000
34	A	36	PHE	0	0.068	0.039	16.445	0.019	0.019	0.000	0.000	0.000	0.000
35	A	37	LYS	1	0.919	0.947	20.790	0.262	0.262	0.000	0.000	0.000	0.000
36	A	38	VAL	0	0.033	0.023	20.772	-0.013	-0.013	0.000	0.000	0.000	0.000
37	A	39	GLY	0	-0.015	-0.015	22.602	0.023	0.023	0.000	0.000	0.000	0.000
38	A	40	TYR	0	-0.018	-0.031	25.281	-0.009	-0.009	0.000	0.000	0.000	0.000
39	A	41	LEU	0	0.050	0.012	26.494	-0.008	-0.008	0.000	0.000	0.000	0.000
40	A	42	SER	0	-0.019	-0.004	28.983	-0.004	-0.004	0.000	0.000	0.000	0.000
41	A	43	LYS	1	0.755	0.858	30.165	0.138	0.138	0.000	0.000	0.000	0.000
42	A	44	SER	0	0.042	0.042	25.677	-0.004	-0.004	0.000	0.000	0.000	0.000
43	A	45	ARG	1	0.804	0.886	25.844	0.183	0.183	0.000	0.000	0.000	0.000
44	A	46	MET	0	0.031	0.018	24.078	-0.008	-0.008	0.000	0.000	0.000	0.000
45	A	47	TYR	0	-0.004	-0.023	16.560	0.015	0.015	0.000	0.000	0.000	0.000
46	A	48	ALA	0	0.033	0.047	18.508	-0.020	-0.020	0.000	0.000	0.000	0.000
47	A	49	LEU	0	-0.027	-0.011	20.461	0.025	0.025	0.000	0.000	0.000	0.000
48	A	50	THR	0	-0.027	-0.039	18.268	-0.028	-0.028	0.000	0.000	0.000	0.000
49	A	51	ASP	-1	-0.775	-0.871	21.469	-0.297	-0.297	0.000	0.000	0.000	0.000
50	A	52	ILE	0	-0.016	-0.028	19.787	-0.022	-0.022	0.000	0.000	0.000	0.000
51	A	53	THR	0	-0.011	0.000	21.721	-0.004	-0.004	0.000	0.000	0.000	0.000
52	A	54	GLN	0	-0.145	-0.068	22.893	0.017	0.017	0.000	0.000	0.000	0.000
53	A	55	ASP	-1	-0.912	-0.936	19.100	-0.478	-0.478	0.000	0.000	0.000	0.000
54	A	56	PRO	0	-0.013	-0.015	18.598	0.037	0.037	0.000	0.000	0.000	0.000
55	A	57	LEU	0	0.032	0.018	15.639	0.023	0.023	0.000	0.000	0.000	0.000
56	A	58	ARG	1	0.890	0.950	19.116	0.328	0.328	0.000	0.000	0.000	0.000
57	A	59	LEU	0	0.040	0.046	15.453	0.010	0.010	0.000	0.000	0.000	0.000
58	A	60	SER	0	-0.026	0.000	19.427	0.030	0.030	0.000	0.000	0.000	0.000
59	A	61	LEU	0	0.025	0.005	17.678	-0.016	-0.016	0.000	0.000	0.000	0.000
60	A	62	LYS	1	0.822	0.914	21.470	0.258	0.258	0.000	0.000	0.000	0.000
61	A	63	VAL	0	0.001	-0.009	21.010	-0.024	-0.024	0.000	0.000	0.000	0.000
62	A	64	ASP	-1	-0.857	-0.941	23.432	-0.132	-0.132	0.000	0.000	0.000	0.000
63	A	65	PRO	0	-0.038	-0.031	25.811	-0.005	-0.005	0.000	0.000	0.000	0.000
64	A	66	GLU	-1	-0.936	-0.947	27.963	-0.101	-0.101	0.000	0.000	0.000	0.000
65	A	67	ARG	1	0.845	0.880	16.957	0.270	0.270	0.000	0.000	0.000	0.000
66	A	68	GLY	0	-0.014	-0.014	24.238	-0.016	-0.016	0.000	0.000	0.000	0.000
67	A	69	GLU	-1	-0.863	-0.905	25.417	-0.152	-0.152	0.000	0.000	0.000	0.000
68	A	70	GLU	-1	-0.868	-0.935	24.357	-0.144	-0.144	0.000	0.000	0.000	0.000
69	A	71	LEU	0	-0.051	-0.032	19.509	-0.007	-0.007	0.000	0.000	0.000	0.000
70	A	72	ARG	1	0.792	0.861	23.332	0.168	0.168	0.000	0.000	0.000	0.000
71	A	73	GLN	0	-0.027	-0.007	25.986	0.007	0.007	0.000	0.000	0.000	0.000
72	A	74	ALA	0	-0.033	-0.019	22.516	0.008	0.008	0.000	0.000	0.000	0.000
73	A	75	HIS	0	-0.009	-0.001	18.490	-0.014	-0.014	0.000	0.000	0.000	0.000
74	A	76	PRO	0	0.027	0.017	23.058	-0.018	-0.018	0.000	0.000	0.000	0.000
75	A	77	GLN	0	-0.061	-0.037	24.474	0.002	0.002	0.000	0.000	0.000	0.000
76	A	78	SER	0	0.008	-0.002	20.019	0.008	0.008	0.000	0.000	0.000	0.000
77	A	79	ILE	0	-0.033	-0.012	19.634	-0.037	-0.037	0.000	0.000	0.000	0.000
78	A	80	ALA	0	0.039	0.033	23.176	0.029	0.029	0.000	0.000	0.000	0.000
79	A	81	PRO	0	-0.004	-0.027	26.002	-0.012	-0.012	0.000	0.000	0.000	0.000
80	A	82	GLY	0	0.014	0.014	26.710	-0.006	-0.006	0.000	0.000	0.000	0.000
81	A	83	TYR	0	0.011	0.009	27.115	0.029	0.029	0.000	0.000	0.000	0.000
82	A	84	HIS	0	0.000	0.009	28.928	-0.005	-0.005	0.000	0.000	0.000	0.000
83	A	85	LEU	0	0.014	0.025	26.495	0.001	0.001	0.000	0.000	0.000	0.000
84	A	86	ASN	0	0.002	-0.008	30.706	0.016	0.016	0.000	0.000	0.000	0.000
85	A	87	LYS	1	0.956	0.956	30.192	0.182	0.182	0.000	0.000	0.000	0.000
86	A	88	LYS	1	0.907	0.950	30.767	0.137	0.137	0.000	0.000	0.000	0.000
87	A	89	HIS	0	-0.008	-0.006	27.905	-0.006	-0.006	0.000	0.000	0.000	0.000
88	A	90	TRP	0	0.021	0.028	23.009	-0.008	-0.008	0.000	0.000	0.000	0.000
89	A	91	VAL	0	0.021	0.018	22.199	0.026	0.026	0.000	0.000	0.000	0.000
90	A	92	THR	0	-0.013	-0.029	22.618	-0.009	-0.009	0.000	0.000	0.000	0.000
91	A	93	VAL	0	0.028	0.004	17.601	0.032	0.032	0.000	0.000	0.000	0.000
92	A	94	THR	0	0.001	0.007	19.261	-0.020	-0.020	0.000	0.000	0.000	0.000
93	A	95	LEU	0	-0.050	-0.019	14.031	-0.008	-0.008	0.000	0.000	0.000	0.000
94	A	96	ASP	-1	-0.780	-0.874	15.730	-0.451	-0.451	0.000	0.000	0.000	0.000
95	A	97	GLY	0	-0.001	0.007	13.269	0.020	0.020	0.000	0.000	0.000	0.000
96	A	98	THR	0	-0.092	-0.055	14.273	0.038	0.038	0.000	0.000	0.000	0.000
97	A	99	VAL	0	0.004	0.007	15.426	0.051	0.051	0.000	0.000	0.000	0.000
98	A	100	PRO	0	-0.008	-0.015	12.286	-0.092	-0.092	0.000	0.000	0.000	0.000
99	A	101	ALA	0	0.061	0.029	7.941	0.020	0.020	0.000	0.000	0.000	0.000
100	A	102	GLU	-1	-0.813	-0.888	8.049	-0.242	-0.242	0.000	0.000	0.000	0.000
101	A	103	LEU	0	-0.029	-0.007	9.400	0.033	0.033	0.000	0.000	0.000	0.000
102	A	104	LEU	0	0.018	0.004	11.793	0.031	0.031	0.000	0.000	0.000	0.000
103	A	105	GLY	0	0.065	0.034	9.740	0.009	0.009	0.000	0.000	0.000	0.000
104	A	106	GLU	-1	-0.815	-0.869	10.801	-0.265	-0.265	0.000	0.000	0.000	0.000
105	A	107	LEU	0	-0.007	0.006	12.693	0.090	0.090	0.000	0.000	0.000	0.000
106	A	108	LEU	0	-0.010	0.005	12.417	0.093	0.093	0.000	0.000	0.000	0.000
107	A	109	ARG	1	0.819	0.868	8.784	0.980	0.980	0.000	0.000	0.000	0.000
108	A	110	GLY	0	0.035	0.019	14.454	0.083	0.083	0.000	0.000	0.000	0.000
109	A	111	SER	0	-0.042	-0.038	17.622	0.078	0.078	0.000	0.000	0.000	0.000
110	A	112	TYR	0	0.022	-0.019	16.846	0.055	0.055	0.000	0.000	0.000	0.000
111	A	113	LEU	0	0.005	0.005	16.862	0.051	0.051	0.000	0.000	0.000	0.000
112	A	114	LEU	0	-0.005	0.018	19.976	0.045	0.045	0.000	0.000	0.000	0.000
113	A	115	VAL	0	0.001	-0.011	22.382	0.036	0.036	0.000	0.000	0.000	0.000
114	A	116	THR	0	-0.047	-0.014	21.201	0.033	0.033	0.000	0.000	0.000	0.000
115	A	117	LYS	1	0.825	0.922	22.589	0.162	0.162	0.000	0.000	0.000	0.000
116	A	118	LYS	1	0.883	0.931	25.997	0.142	0.142	0.000	0.000	0.000	0.000
117	A	119	GLY	0	-0.023	-0.005	27.367	0.012	0.012	0.000	0.000	0.000	0.000
118	A	120	PHE	0	-0.012	0.003	25.833	0.005	0.005	0.000	0.000	0.000	0.000
119	A	121	THR	0	-0.026	-0.023	29.271	0.006	0.006	0.000	0.000	0.000	0.000
120	A	122	LYS	1	0.997	0.981	29.505	0.043	0.043	0.000	0.000	0.000	0.000
121	A	123	ALA	0	-0.012	-0.012	29.909	0.002	0.002	0.000	0.000	0.000	0.000
122	A	124	GLU	-1	-0.658	-0.804	29.488	-0.114	-0.114	0.000	0.000	0.000	0.000
123	A	125	ARG	1	0.878	0.949	24.505	0.118	0.118	0.000	0.000	0.000	0.000
124	A	126	LYS	1	0.931	0.978	25.838	0.033	0.033	0.000	0.000	0.000	0.000
125	A	127	GLU	-1	-0.917	-0.923	27.773	-0.081	-0.081	0.000	0.000	0.000	0.000
126	A	128	LEU	0	-0.009	0.007	24.602	0.002	0.002	0.000	0.000	0.000	0.000
127	A	129	GLY	0	0.026	0.019	23.809	-0.004	-0.004	0.000	0.000	0.000	0.000
128	A	130	LEU	0	-0.080	-0.052	21.457	-0.014	-0.014	0.000	0.000	0.000	0.000
129	A	131	PRO	0	0.015	0.017	17.485	0.024	0.024	0.000	0.000	0.000	0.000
130	A	132	ASP	-1	-0.935	-0.975	20.529	-0.099	-0.099	0.000	0.000	0.000	0.000
131	A	133	SER	0	-0.003	-0.013	17.507	-0.006	-0.006	0.000	0.000	0.000	0.000
132	A	134	LEU	0	0.005	-0.008	12.960	0.010	0.010	0.000	0.000	0.000	0.000
133	A	135	GLU	-1	-0.898	-0.934	12.027	0.214	0.214	0.000	0.000	0.000	0.000
134	A	136	GLY	0	0.053	0.031	8.152	-0.144	-0.144	0.000	0.000	0.000	0.000
135	A	137	GLY	0	-0.015	0.004	7.448	-0.317	-0.317	0.000	0.000	0.000	0.000
136	A	138	SER	0	0.017	0.006	4.927	0.408	0.408	0.000	0.000	0.000	0.000
137	A	139	HIS	0	-0.002	-0.001	6.857	-0.243	-0.243	0.000	0.000	0.000	0.000
138	A	140	HIS	1	0.813	0.895	8.561	-0.087	-0.087	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:LEU)