FMO DATABASE

FMODB ID: YVYV2

Calculation Name: 1AGI-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1AGI

Chain ID: A

ChEMBL ID:

UniProt ID: P10152

Base Structure: X-ray

Registration Date: 2023-09-21

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	122
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1130929.869781
FMO2-HF: Nuclear repulsion	1078480.206817
FMO2-HF: Total energy	-52449.662964
FMO2-MP2: Total energy	-52598.591949

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:ALA)

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

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.
-1.46	0.891	0.084	-1.282	-1.154	0.003

Interaction energy analysis for fragmet #1(A:1:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.028 / q_NPA : 0.014

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	3	ASP	-1	-0.878	-0.956	3.325	-3.317	-0.966	0.084	-1.282	-1.154	0.003
4	A	4	ASP	-1	-0.816	-0.909	4.904	0.065	0.065	0.000	0.000	0.000	0.000
5	A	5	TYR	0	-0.023	-0.005	6.405	0.425	0.425	0.000	0.000	0.000	0.000
6	A	6	ARG	1	0.903	0.928	7.735	0.919	0.919	0.000	0.000	0.000	0.000
7	A	7	TYR	0	0.015	0.017	10.332	0.178	0.178	0.000	0.000	0.000	0.000
8	A	8	ILE	0	0.029	0.007	8.151	0.118	0.118	0.000	0.000	0.000	0.000
9	A	9	HIS	0	0.014	0.026	11.140	0.124	0.124	0.000	0.000	0.000	0.000
10	A	10	PHE	0	0.001	0.005	13.298	0.069	0.069	0.000	0.000	0.000	0.000
11	A	11	LEU	0	-0.042	-0.026	13.180	0.056	0.056	0.000	0.000	0.000	0.000
12	A	12	THR	0	-0.027	-0.026	13.771	0.054	0.054	0.000	0.000	0.000	0.000
13	A	13	GLN	0	0.011	0.002	16.417	0.052	0.052	0.000	0.000	0.000	0.000
14	A	14	HIS	1	0.849	0.936	18.890	0.179	0.179	0.000	0.000	0.000	0.000
15	A	15	TYR	0	-0.003	-0.002	18.427	0.014	0.014	0.000	0.000	0.000	0.000
16	A	16	ASP	-1	-0.753	-0.853	20.266	0.001	0.001	0.000	0.000	0.000	0.000
17	A	17	ALA	0	0.029	0.036	21.723	-0.001	-0.001	0.000	0.000	0.000	0.000
18	A	18	LYS	1	0.980	0.977	23.556	-0.049	-0.049	0.000	0.000	0.000	0.000
19	A	19	PRO	0	0.035	0.049	26.998	0.008	0.008	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.909	0.914	28.725	-0.010	-0.010	0.000	0.000	0.000	0.000
21	A	21	GLY	0	0.033	0.042	31.704	0.000	0.000	0.000	0.000	0.000	0.000
22	A	22	ARG	1	0.787	0.869	30.806	0.026	0.026	0.000	0.000	0.000	0.000
23	A	23	ASN	0	0.114	0.057	32.439	-0.005	-0.005	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.755	-0.900	33.190	-0.030	-0.030	0.000	0.000	0.000	0.000
25	A	25	GLU	-1	-0.905	-0.940	33.200	0.000	0.000	0.000	0.000	0.000	0.000
26	A	26	TYR	0	0.015	-0.034	26.409	-0.003	-0.003	0.000	0.000	0.000	0.000
27	A	27	CYS	0	-0.060	-0.019	28.840	0.007	0.007	0.000	0.000	0.000	0.000
28	A	28	PHE	0	-0.017	-0.008	28.841	-0.005	-0.005	0.000	0.000	0.000	0.000
29	A	29	ASN	0	-0.047	-0.024	28.427	-0.001	-0.001	0.000	0.000	0.000	0.000
30	A	30	MET	0	-0.020	0.003	24.451	0.001	0.001	0.000	0.000	0.000	0.000
31	A	31	MET	0	0.003	0.015	24.111	-0.008	-0.008	0.000	0.000	0.000	0.000
32	A	32	LYS	1	0.958	0.986	24.649	-0.008	-0.008	0.000	0.000	0.000	0.000
33	A	33	ASN	0	-0.046	-0.032	22.414	0.005	0.005	0.000	0.000	0.000	0.000
34	A	34	ARG	1	0.757	0.853	19.249	0.051	0.051	0.000	0.000	0.000	0.000
35	A	35	ARG	1	0.909	0.953	19.383	-0.016	-0.016	0.000	0.000	0.000	0.000
36	A	36	LEU	0	-0.009	0.016	20.550	-0.012	-0.012	0.000	0.000	0.000	0.000
37	A	37	THR	0	-0.010	-0.026	23.606	0.006	0.006	0.000	0.000	0.000	0.000
38	A	38	ARG	1	0.927	0.965	24.752	0.058	0.058	0.000	0.000	0.000	0.000
39	A	39	PRO	0	0.073	0.040	24.963	-0.007	-0.007	0.000	0.000	0.000	0.000
40	A	40	CYS	0	-0.068	-0.010	26.927	-0.003	-0.003	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.881	0.962	22.216	0.152	0.152	0.000	0.000	0.000	0.000
42	A	42	ASP	-1	-0.798	-0.880	27.684	-0.072	-0.072	0.000	0.000	0.000	0.000
43	A	43	ARG	1	0.882	0.935	29.113	0.108	0.108	0.000	0.000	0.000	0.000
44	A	44	ASN	0	-0.014	-0.015	23.061	-0.029	-0.029	0.000	0.000	0.000	0.000
45	A	45	THR	0	-0.009	-0.017	25.841	0.017	0.017	0.000	0.000	0.000	0.000
46	A	46	PHE	0	-0.031	-0.013	22.245	-0.011	-0.011	0.000	0.000	0.000	0.000
47	A	47	ILE	0	0.042	0.019	21.941	0.009	0.009	0.000	0.000	0.000	0.000
48	A	48	HIS	1	0.808	0.884	24.050	0.044	0.044	0.000	0.000	0.000	0.000
49	A	49	GLY	0	0.060	0.037	25.618	-0.005	-0.005	0.000	0.000	0.000	0.000
50	A	50	ASN	0	0.015	-0.005	22.155	0.009	0.009	0.000	0.000	0.000	0.000
51	A	51	LYS	1	1.004	1.005	13.822	0.001	0.001	0.000	0.000	0.000	0.000
52	A	52	ASN	0	-0.023	-0.020	18.033	-0.024	-0.024	0.000	0.000	0.000	0.000
53	A	53	ASP	-1	-0.753	-0.849	19.627	-0.064	-0.064	0.000	0.000	0.000	0.000
54	A	54	ILE	0	-0.008	0.010	20.107	-0.008	-0.008	0.000	0.000	0.000	0.000
55	A	55	LYS	1	0.863	0.925	15.448	0.160	0.160	0.000	0.000	0.000	0.000
56	A	56	ALA	0	0.009	0.004	18.542	-0.018	-0.018	0.000	0.000	0.000	0.000
57	A	57	ILE	0	-0.001	0.010	21.414	0.006	0.006	0.000	0.000	0.000	0.000
58	A	58	CYS	0	-0.110	-0.056	17.832	-0.007	-0.007	0.000	0.000	0.000	0.000
59	A	59	GLU	-1	-0.842	-0.892	19.724	-0.150	-0.150	0.000	0.000	0.000	0.000
60	A	60	ASP	-1	-0.795	-0.894	22.576	-0.126	-0.126	0.000	0.000	0.000	0.000
61	A	61	ARG	1	0.849	0.926	23.501	0.066	0.066	0.000	0.000	0.000	0.000
62	A	62	ASN	0	0.011	0.008	24.694	0.015	0.015	0.000	0.000	0.000	0.000
63	A	63	GLY	0	0.037	0.026	25.791	-0.001	-0.001	0.000	0.000	0.000	0.000
64	A	64	GLN	0	0.004	0.003	26.671	0.011	0.011	0.000	0.000	0.000	0.000
65	A	65	PRO	0	0.034	0.025	27.356	-0.008	-0.008	0.000	0.000	0.000	0.000
66	A	66	TYR	0	0.012	-0.013	28.122	0.013	0.013	0.000	0.000	0.000	0.000
67	A	67	ARG	1	0.847	0.889	28.796	0.138	0.138	0.000	0.000	0.000	0.000
68	A	68	GLY	0	0.035	0.040	29.446	0.001	0.001	0.000	0.000	0.000	0.000
69	A	69	ASP	-1	-0.907	-0.942	24.451	-0.218	-0.218	0.000	0.000	0.000	0.000
70	A	70	LEU	0	-0.077	-0.029	23.770	-0.020	-0.020	0.000	0.000	0.000	0.000
71	A	71	ARG	1	0.784	0.872	22.562	0.171	0.171	0.000	0.000	0.000	0.000
72	A	72	ILE	0	-0.012	-0.004	25.428	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	73	SER	0	-0.017	-0.029	26.585	-0.002	-0.002	0.000	0.000	0.000	0.000
74	A	74	LYS	1	0.844	0.915	27.824	0.092	0.092	0.000	0.000	0.000	0.000
75	A	75	SER	0	-0.010	-0.020	28.447	0.007	0.007	0.000	0.000	0.000	0.000
76	A	76	GLU	-1	-0.865	-0.901	29.902	-0.055	-0.055	0.000	0.000	0.000	0.000
77	A	77	PHE	0	-0.021	-0.024	24.852	0.002	0.002	0.000	0.000	0.000	0.000
78	A	78	GLN	0	0.047	0.035	29.319	0.002	0.002	0.000	0.000	0.000	0.000
79	A	79	ILE	0	-0.013	-0.016	27.610	-0.002	-0.002	0.000	0.000	0.000	0.000
80	A	80	THR	0	-0.022	0.000	28.579	0.009	0.009	0.000	0.000	0.000	0.000
81	A	81	ILE	0	0.014	0.020	28.661	-0.006	-0.006	0.000	0.000	0.000	0.000
82	A	83	LYS	1	0.888	0.908	30.394	0.061	0.061	0.000	0.000	0.000	0.000
83	A	84	HIS	0	-0.019	-0.012	31.906	0.009	0.009	0.000	0.000	0.000	0.000
84	A	85	LYS	1	0.821	0.907	33.675	0.033	0.033	0.000	0.000	0.000	0.000
85	A	86	GLY	0	0.016	0.011	37.150	0.001	0.001	0.000	0.000	0.000	0.000
86	A	87	GLY	0	0.051	0.020	38.024	-0.004	-0.004	0.000	0.000	0.000	0.000
87	A	88	SER	0	-0.020	-0.002	35.437	-0.002	-0.002	0.000	0.000	0.000	0.000
88	A	89	SER	0	0.062	0.024	31.438	-0.004	-0.004	0.000	0.000	0.000	0.000
89	A	90	ARG	1	0.934	0.970	31.392	0.034	0.034	0.000	0.000	0.000	0.000
90	A	91	PRO	0	0.037	0.010	29.707	0.003	0.003	0.000	0.000	0.000	0.000
91	A	92	PRO	0	-0.031	-0.023	32.491	0.001	0.001	0.000	0.000	0.000	0.000
92	A	94	ARG	1	0.940	0.978	32.150	0.020	0.020	0.000	0.000	0.000	0.000
93	A	95	TYR	0	0.036	-0.005	29.091	-0.001	-0.001	0.000	0.000	0.000	0.000
94	A	96	GLY	0	-0.039	-0.008	33.916	0.006	0.006	0.000	0.000	0.000	0.000
95	A	97	ALA	0	0.004	0.004	33.620	-0.006	-0.006	0.000	0.000	0.000	0.000
96	A	98	THR	0	-0.015	-0.017	33.634	0.001	0.001	0.000	0.000	0.000	0.000
97	A	99	GLU	-1	-0.908	-0.939	33.375	-0.027	-0.027	0.000	0.000	0.000	0.000
98	A	100	ASP	-1	-0.806	-0.889	33.344	-0.052	-0.052	0.000	0.000	0.000	0.000
99	A	101	SER	0	-0.081	-0.066	33.121	0.002	0.002	0.000	0.000	0.000	0.000
100	A	102	ARG	1	0.858	0.932	31.010	0.087	0.087	0.000	0.000	0.000	0.000
101	A	103	VAL	0	0.057	0.046	30.571	-0.002	-0.002	0.000	0.000	0.000	0.000
102	A	104	ILE	0	-0.048	-0.021	24.651	-0.001	-0.001	0.000	0.000	0.000	0.000
103	A	105	VAL	0	0.038	0.015	26.349	-0.001	-0.001	0.000	0.000	0.000	0.000
104	A	106	VAL	0	-0.027	-0.011	21.000	-0.002	-0.002	0.000	0.000	0.000	0.000
105	A	107	GLY	0	0.052	0.029	21.097	0.008	0.008	0.000	0.000	0.000	0.000
106	A	109	GLU	-1	-0.785	-0.888	13.693	-0.691	-0.691	0.000	0.000	0.000	0.000
107	A	110	ASN	0	0.009	-0.001	11.189	0.057	0.057	0.000	0.000	0.000	0.000
108	A	111	GLY	0	0.047	0.038	13.777	0.018	0.018	0.000	0.000	0.000	0.000
109	A	112	LEU	0	-0.031	-0.014	11.355	0.068	0.068	0.000	0.000	0.000	0.000
110	A	113	PRO	0	0.000	0.000	14.751	-0.023	-0.023	0.000	0.000	0.000	0.000
111	A	114	VAL	0	-0.004	-0.022	13.502	-0.017	-0.017	0.000	0.000	0.000	0.000
112	A	115	HIS	0	0.004	0.001	16.055	-0.017	-0.017	0.000	0.000	0.000	0.000
113	A	116	PHE	0	0.003	-0.010	19.593	0.015	0.015	0.000	0.000	0.000	0.000
114	A	117	ASP	-1	-0.776	-0.842	22.734	-0.153	-0.153	0.000	0.000	0.000	0.000
115	A	118	GLU	-1	-0.771	-0.874	25.564	-0.106	-0.106	0.000	0.000	0.000	0.000
116	A	119	SER	0	-0.064	-0.053	28.108	0.014	0.014	0.000	0.000	0.000	0.000
117	A	120	PHE	0	0.018	0.010	29.815	0.008	0.008	0.000	0.000	0.000	0.000
118	A	121	ILE	0	0.023	0.014	31.742	0.004	0.004	0.000	0.000	0.000	0.000
119	A	122	THR	0	-0.019	-0.003	33.479	-0.003	-0.003	0.000	0.000	0.000	0.000
120	A	123	PRO	0	0.016	0.010	36.293	0.003	0.003	0.000	0.000	0.000	0.000
121	A	124	ARG	1	0.848	0.891	37.736	0.048	0.048	0.000	0.000	0.000	0.000
122	A	125	HIS	0	0.043	0.032	39.846	0.004	0.004	0.000	0.000	0.000	0.000

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