FMO DATABASE

FMODB ID: 4J3LN

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	OptH
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	-1124990.927305
FMO2-HF: Nuclear repulsion	1072542.276712
FMO2-HF: Total energy	-52448.650592
FMO2-MP2: Total energy	-52597.506726

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.
-1.955	0.445	0.029	-1.11	-1.319	0.004

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 : 0.024 / q_NPA : 0.012

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	3	ASP	-1	-0.916	-0.980	3.568	-3.437	-1.215	0.030	-1.100	-1.152	0.004
4	A	4	ASP	-1	-0.839	-0.902	4.505	-0.060	0.118	-0.001	-0.010	-0.167	0.000
5	A	5	TYR	0	-0.029	-0.022	6.012	0.531	0.531	0.000	0.000	0.000	0.000
6	A	6	ARG	1	0.965	0.967	7.545	0.911	0.911	0.000	0.000	0.000	0.000
7	A	7	TYR	0	0.042	0.033	9.987	0.192	0.192	0.000	0.000	0.000	0.000
8	A	8	ILE	0	0.024	0.000	7.632	0.137	0.137	0.000	0.000	0.000	0.000
9	A	9	HIS	0	0.013	0.011	10.604	0.112	0.112	0.000	0.000	0.000	0.000
10	A	10	PHE	0	-0.012	-0.008	12.688	0.077	0.077	0.000	0.000	0.000	0.000
11	A	11	LEU	0	-0.053	-0.029	12.729	0.060	0.060	0.000	0.000	0.000	0.000
12	A	12	THR	0	-0.012	-0.002	13.320	0.060	0.060	0.000	0.000	0.000	0.000
13	A	13	GLN	0	-0.011	-0.012	15.980	0.030	0.030	0.000	0.000	0.000	0.000
14	A	14	HIS	1	0.828	0.924	18.380	0.163	0.163	0.000	0.000	0.000	0.000
15	A	15	TYR	0	-0.006	0.002	18.034	0.011	0.011	0.000	0.000	0.000	0.000
16	A	16	ASP	-1	-0.798	-0.875	19.951	0.031	0.031	0.000	0.000	0.000	0.000
17	A	17	ALA	0	0.022	0.036	21.575	-0.005	-0.005	0.000	0.000	0.000	0.000
18	A	18	LYS	1	0.992	0.979	23.317	-0.064	-0.064	0.000	0.000	0.000	0.000
19	A	19	PRO	0	0.017	0.043	26.623	0.008	0.008	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.945	0.935	28.246	-0.022	-0.022	0.000	0.000	0.000	0.000
21	A	21	GLY	0	0.012	0.019	31.615	-0.001	-0.001	0.000	0.000	0.000	0.000
22	A	22	ARG	1	0.812	0.911	30.511	0.020	0.020	0.000	0.000	0.000	0.000
23	A	23	ASN	0	0.138	0.076	32.369	-0.004	-0.004	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.784	-0.927	33.077	-0.019	-0.019	0.000	0.000	0.000	0.000
25	A	25	GLU	-1	-0.969	-0.977	33.323	0.019	0.019	0.000	0.000	0.000	0.000
26	A	26	TYR	0	-0.054	-0.064	25.781	-0.002	-0.002	0.000	0.000	0.000	0.000
27	A	27	CYS	0	-0.040	-0.010	28.464	0.009	0.009	0.000	0.000	0.000	0.000
28	A	28	PHE	0	-0.032	-0.003	28.478	-0.003	-0.003	0.000	0.000	0.000	0.000
29	A	29	ASN	0	0.036	0.009	28.079	0.000	0.000	0.000	0.000	0.000	0.000
30	A	30	MET	0	-0.006	0.000	24.428	0.006	0.006	0.000	0.000	0.000	0.000
31	A	31	MET	0	0.008	0.015	23.698	-0.006	-0.006	0.000	0.000	0.000	0.000
32	A	32	LYS	1	0.960	0.990	24.116	-0.028	-0.028	0.000	0.000	0.000	0.000
33	A	33	ASN	0	-0.042	-0.034	21.977	0.006	0.006	0.000	0.000	0.000	0.000
34	A	34	ARG	1	0.800	0.891	18.625	0.021	0.021	0.000	0.000	0.000	0.000
35	A	35	ARG	1	0.875	0.945	18.994	-0.059	-0.059	0.000	0.000	0.000	0.000
36	A	36	LEU	0	0.015	0.018	20.344	-0.019	-0.019	0.000	0.000	0.000	0.000
37	A	37	THR	0	-0.010	-0.031	23.202	0.002	0.002	0.000	0.000	0.000	0.000
38	A	38	ARG	1	0.933	0.991	24.767	0.019	0.019	0.000	0.000	0.000	0.000
39	A	39	PRO	0	0.056	0.024	24.597	-0.006	-0.006	0.000	0.000	0.000	0.000
40	A	40	CYS	0	-0.045	0.010	26.747	-0.004	-0.004	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.923	0.987	22.200	0.134	0.134	0.000	0.000	0.000	0.000
42	A	42	ASP	-1	-0.855	-0.932	27.488	-0.066	-0.066	0.000	0.000	0.000	0.000
43	A	43	ARG	1	0.944	0.960	28.598	0.098	0.098	0.000	0.000	0.000	0.000
44	A	44	ASN	0	-0.059	-0.037	22.630	-0.029	-0.029	0.000	0.000	0.000	0.000
45	A	45	THR	0	-0.003	-0.003	25.469	0.017	0.017	0.000	0.000	0.000	0.000
46	A	46	PHE	0	-0.034	-0.011	21.680	-0.011	-0.011	0.000	0.000	0.000	0.000
47	A	47	ILE	0	0.036	0.012	21.542	0.005	0.005	0.000	0.000	0.000	0.000
48	A	48	HIS	1	0.778	0.855	23.402	0.034	0.034	0.000	0.000	0.000	0.000
49	A	49	GLY	0	0.029	0.021	25.348	-0.008	-0.008	0.000	0.000	0.000	0.000
50	A	50	ASN	0	0.043	0.022	22.290	0.004	0.004	0.000	0.000	0.000	0.000
51	A	51	LYS	1	1.028	1.010	14.063	-0.037	-0.037	0.000	0.000	0.000	0.000
52	A	52	ASN	0	-0.003	-0.007	18.216	-0.030	-0.030	0.000	0.000	0.000	0.000
53	A	53	ASP	-1	-0.844	-0.921	19.671	-0.073	-0.073	0.000	0.000	0.000	0.000
54	A	54	ILE	0	-0.025	-0.001	19.362	-0.010	-0.010	0.000	0.000	0.000	0.000
55	A	55	LYS	1	0.950	0.971	13.664	0.209	0.209	0.000	0.000	0.000	0.000
56	A	56	ALA	0	0.041	0.018	18.253	-0.022	-0.022	0.000	0.000	0.000	0.000
57	A	57	ILE	0	-0.032	-0.001	21.241	0.001	0.001	0.000	0.000	0.000	0.000
58	A	58	CYS	0	-0.125	-0.067	17.770	-0.005	-0.005	0.000	0.000	0.000	0.000
59	A	59	GLU	-1	-0.922	-0.942	19.657	-0.181	-0.181	0.000	0.000	0.000	0.000
60	A	60	ASP	-1	-0.864	-0.955	22.560	-0.139	-0.139	0.000	0.000	0.000	0.000
61	A	61	ARG	1	0.922	0.966	24.417	0.077	0.077	0.000	0.000	0.000	0.000
62	A	62	ASN	0	-0.001	-0.010	24.628	0.017	0.017	0.000	0.000	0.000	0.000
63	A	63	GLY	0	0.034	0.026	25.458	0.000	0.000	0.000	0.000	0.000	0.000
64	A	64	GLN	0	-0.023	-0.005	26.429	0.007	0.007	0.000	0.000	0.000	0.000
65	A	65	PRO	0	0.034	0.026	27.427	-0.007	-0.007	0.000	0.000	0.000	0.000
66	A	66	TYR	0	0.020	-0.005	28.132	0.014	0.014	0.000	0.000	0.000	0.000
67	A	67	ARG	1	0.940	0.954	28.773	0.144	0.144	0.000	0.000	0.000	0.000
68	A	68	GLY	0	0.014	0.018	29.636	-0.006	-0.006	0.000	0.000	0.000	0.000
69	A	69	ASP	-1	-0.872	-0.925	24.470	-0.237	-0.237	0.000	0.000	0.000	0.000
70	A	70	LEU	0	-0.082	-0.034	23.842	-0.019	-0.019	0.000	0.000	0.000	0.000
71	A	71	ARG	1	0.849	0.925	22.487	0.193	0.193	0.000	0.000	0.000	0.000
72	A	72	ILE	0	-0.017	-0.009	25.585	0.000	0.000	0.000	0.000	0.000	0.000
73	A	73	SER	0	-0.021	-0.017	26.420	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	74	LYS	1	0.907	0.967	27.788	0.104	0.104	0.000	0.000	0.000	0.000
75	A	75	SER	0	-0.020	-0.015	28.260	0.008	0.008	0.000	0.000	0.000	0.000
76	A	76	GLU	-1	-0.896	-0.946	29.583	-0.058	-0.058	0.000	0.000	0.000	0.000
77	A	77	PHE	0	-0.025	-0.021	24.324	0.002	0.002	0.000	0.000	0.000	0.000
78	A	78	GLN	0	0.057	0.033	28.893	0.001	0.001	0.000	0.000	0.000	0.000
79	A	79	ILE	0	-0.009	-0.019	27.034	-0.004	-0.004	0.000	0.000	0.000	0.000
80	A	80	THR	0	0.016	0.025	28.114	0.008	0.008	0.000	0.000	0.000	0.000
81	A	81	ILE	0	-0.011	0.009	28.270	-0.006	-0.006	0.000	0.000	0.000	0.000
82	A	83	LYS	1	0.988	0.977	30.015	0.049	0.049	0.000	0.000	0.000	0.000
83	A	84	HIS	0	-0.009	-0.010	31.623	0.009	0.009	0.000	0.000	0.000	0.000
84	A	85	LYS	1	0.897	0.955	33.346	0.021	0.021	0.000	0.000	0.000	0.000
85	A	86	GLY	0	0.001	-0.002	36.571	0.002	0.002	0.000	0.000	0.000	0.000
86	A	87	GLY	0	0.056	0.021	37.328	-0.003	-0.003	0.000	0.000	0.000	0.000
87	A	88	SER	0	-0.006	0.016	36.099	-0.003	-0.003	0.000	0.000	0.000	0.000
88	A	89	SER	0	0.057	0.032	31.220	-0.003	-0.003	0.000	0.000	0.000	0.000
89	A	90	ARG	1	0.937	0.955	31.240	0.018	0.018	0.000	0.000	0.000	0.000
90	A	91	PRO	0	0.023	-0.002	29.601	0.002	0.002	0.000	0.000	0.000	0.000
91	A	92	PRO	0	-0.028	-0.029	32.282	0.002	0.002	0.000	0.000	0.000	0.000
92	A	94	ARG	1	0.960	0.980	31.874	0.007	0.007	0.000	0.000	0.000	0.000
93	A	95	TYR	0	0.011	-0.014	28.847	-0.002	-0.002	0.000	0.000	0.000	0.000
94	A	96	GLY	0	-0.027	0.004	33.634	0.005	0.005	0.000	0.000	0.000	0.000
95	A	97	ALA	0	-0.005	-0.009	33.024	-0.005	-0.005	0.000	0.000	0.000	0.000
96	A	98	THR	0	-0.031	-0.013	33.260	0.001	0.001	0.000	0.000	0.000	0.000
97	A	99	GLU	-1	-0.962	-0.976	32.977	-0.020	-0.020	0.000	0.000	0.000	0.000
98	A	100	ASP	-1	-0.868	-0.946	32.901	-0.050	-0.050	0.000	0.000	0.000	0.000
99	A	101	SER	0	-0.062	-0.038	32.388	0.002	0.002	0.000	0.000	0.000	0.000
100	A	102	ARG	1	0.926	0.986	28.622	0.092	0.092	0.000	0.000	0.000	0.000
101	A	103	VAL	0	0.048	0.040	30.141	-0.002	-0.002	0.000	0.000	0.000	0.000
102	A	104	ILE	0	-0.060	-0.051	24.047	-0.001	-0.001	0.000	0.000	0.000	0.000
103	A	105	VAL	0	0.023	0.014	26.174	-0.003	-0.003	0.000	0.000	0.000	0.000
104	A	106	VAL	0	-0.031	-0.022	20.877	-0.001	-0.001	0.000	0.000	0.000	0.000
105	A	107	GLY	0	0.040	0.025	20.943	0.007	0.007	0.000	0.000	0.000	0.000
106	A	109	GLU	-1	-0.799	-0.904	12.597	-0.821	-0.821	0.000	0.000	0.000	0.000
107	A	110	ASN	0	0.034	0.012	11.162	0.061	0.061	0.000	0.000	0.000	0.000
108	A	111	GLY	0	0.012	0.014	13.822	0.001	0.001	0.000	0.000	0.000	0.000
109	A	112	LEU	0	-0.026	-0.011	10.701	0.074	0.074	0.000	0.000	0.000	0.000
110	A	113	PRO	0	0.001	0.008	14.663	-0.021	-0.021	0.000	0.000	0.000	0.000
111	A	114	VAL	0	0.003	-0.018	13.397	-0.014	-0.014	0.000	0.000	0.000	0.000
112	A	115	HIS	0	-0.030	-0.013	15.857	-0.011	-0.011	0.000	0.000	0.000	0.000
113	A	116	PHE	0	0.004	0.001	19.275	0.017	0.017	0.000	0.000	0.000	0.000
114	A	117	ASP	-1	-0.818	-0.893	22.253	-0.155	-0.155	0.000	0.000	0.000	0.000
115	A	118	GLU	-1	-0.833	-0.928	25.171	-0.099	-0.099	0.000	0.000	0.000	0.000
116	A	119	SER	0	-0.072	-0.050	27.703	0.012	0.012	0.000	0.000	0.000	0.000
117	A	120	PHE	0	0.016	0.019	29.801	0.007	0.007	0.000	0.000	0.000	0.000
118	A	121	ILE	0	-0.008	-0.007	31.512	0.005	0.005	0.000	0.000	0.000	0.000
119	A	122	THR	0	-0.015	-0.014	33.341	-0.001	-0.001	0.000	0.000	0.000	0.000
120	A	123	PRO	0	-0.003	0.005	36.102	0.003	0.003	0.000	0.000	0.000	0.000
121	A	124	ARG	1	0.981	0.983	38.835	0.046	0.046	0.000	0.000	0.000	0.000
122	A	125	HIS	0	0.030	0.037	39.498	0.003	0.003	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

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