FMO DATABASE

FMODB ID: 5J3NZ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1127702.822258
FMO2-HF: Nuclear repulsion	1075253.413158
FMO2-HF: Total energy	-52449.4091
FMO2-MP2: Total energy	-52598.312309

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.
-1.408	0.927	0.017	-1.061	-1.291	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 : 0.011

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	-0.908	-0.978	3.636	-3.028	-0.867	0.018	-1.051	-1.128	0.004
4	A	4	ASP	-1	-0.802	-0.895	4.618	-0.053	0.121	-0.001	-0.010	-0.163	0.000
5	A	5	TYR	0	-0.037	-0.020	6.148	0.510	0.510	0.000	0.000	0.000	0.000
6	A	6	ARG	1	0.938	0.953	7.598	0.907	0.907	0.000	0.000	0.000	0.000
7	A	7	TYR	0	0.047	0.030	10.099	0.189	0.189	0.000	0.000	0.000	0.000
8	A	8	ILE	0	0.013	-0.001	7.646	0.132	0.132	0.000	0.000	0.000	0.000
9	A	9	HIS	0	0.008	0.013	10.638	0.125	0.125	0.000	0.000	0.000	0.000
10	A	10	PHE	0	-0.010	-0.005	12.719	0.074	0.074	0.000	0.000	0.000	0.000
11	A	11	LEU	0	-0.050	-0.026	12.717	0.058	0.058	0.000	0.000	0.000	0.000
12	A	12	THR	0	-0.023	-0.017	13.329	0.058	0.058	0.000	0.000	0.000	0.000
13	A	13	GLN	0	0.017	0.001	15.991	0.049	0.049	0.000	0.000	0.000	0.000
14	A	14	HIS	1	0.847	0.931	18.410	0.159	0.159	0.000	0.000	0.000	0.000
15	A	15	TYR	0	-0.004	0.006	18.034	0.010	0.010	0.000	0.000	0.000	0.000
16	A	16	ASP	-1	-0.767	-0.858	19.964	0.029	0.029	0.000	0.000	0.000	0.000
17	A	17	ALA	0	0.026	0.032	21.512	-0.005	-0.005	0.000	0.000	0.000	0.000
18	A	18	LYS	1	0.995	0.983	23.329	-0.061	-0.061	0.000	0.000	0.000	0.000
19	A	19	PRO	0	0.034	0.054	26.628	0.008	0.008	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.910	0.914	28.248	-0.019	-0.019	0.000	0.000	0.000	0.000
21	A	21	GLY	0	0.027	0.028	31.610	-0.001	-0.001	0.000	0.000	0.000	0.000
22	A	22	ARG	1	0.762	0.873	30.503	0.020	0.020	0.000	0.000	0.000	0.000
23	A	23	ASN	0	0.122	0.061	32.378	-0.004	-0.004	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.751	-0.891	33.082	-0.019	-0.019	0.000	0.000	0.000	0.000
25	A	25	GLU	-1	-0.925	-0.961	32.950	0.017	0.017	0.000	0.000	0.000	0.000
26	A	26	TYR	0	0.002	-0.039	25.852	-0.002	-0.002	0.000	0.000	0.000	0.000
27	A	27	CYS	0	-0.052	-0.010	28.450	0.008	0.008	0.000	0.000	0.000	0.000
28	A	28	PHE	0	-0.027	-0.006	28.476	-0.002	-0.002	0.000	0.000	0.000	0.000
29	A	29	ASN	0	-0.032	-0.013	28.123	0.002	0.002	0.000	0.000	0.000	0.000
30	A	30	MET	0	-0.003	0.005	24.169	0.005	0.005	0.000	0.000	0.000	0.000
31	A	31	MET	0	0.008	0.017	23.692	-0.006	-0.006	0.000	0.000	0.000	0.000
32	A	32	LYS	1	0.951	0.985	24.109	-0.029	-0.029	0.000	0.000	0.000	0.000
33	A	33	ASN	0	-0.041	-0.037	22.062	0.007	0.007	0.000	0.000	0.000	0.000
34	A	34	ARG	1	0.776	0.873	18.772	0.024	0.024	0.000	0.000	0.000	0.000
35	A	35	ARG	1	0.870	0.947	18.964	-0.059	-0.059	0.000	0.000	0.000	0.000
36	A	36	LEU	0	0.011	0.014	20.162	-0.019	-0.019	0.000	0.000	0.000	0.000
37	A	37	THR	0	-0.008	-0.030	23.204	0.002	0.002	0.000	0.000	0.000	0.000
38	A	38	ARG	1	0.922	0.986	24.671	0.021	0.021	0.000	0.000	0.000	0.000
39	A	39	PRO	0	0.073	0.030	24.594	-0.006	-0.006	0.000	0.000	0.000	0.000
40	A	40	CYS	0	-0.073	-0.002	26.752	-0.004	-0.004	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.896	0.971	21.868	0.131	0.131	0.000	0.000	0.000	0.000
42	A	42	ASP	-1	-0.785	-0.879	27.506	-0.062	-0.062	0.000	0.000	0.000	0.000
43	A	43	ARG	1	0.908	0.942	28.610	0.098	0.098	0.000	0.000	0.000	0.000
44	A	44	ASN	0	-0.040	-0.020	22.661	-0.028	-0.028	0.000	0.000	0.000	0.000
45	A	45	THR	0	-0.007	-0.016	25.478	0.016	0.016	0.000	0.000	0.000	0.000
46	A	46	PHE	0	-0.031	-0.011	21.785	-0.010	-0.010	0.000	0.000	0.000	0.000
47	A	47	ILE	0	0.036	0.012	21.433	0.005	0.005	0.000	0.000	0.000	0.000
48	A	48	HIS	1	0.806	0.877	23.430	0.034	0.034	0.000	0.000	0.000	0.000
49	A	49	GLY	0	0.030	0.022	25.345	-0.008	-0.008	0.000	0.000	0.000	0.000
50	A	50	ASN	0	0.022	0.000	22.102	0.014	0.014	0.000	0.000	0.000	0.000
51	A	51	LYS	1	1.027	1.014	13.780	-0.025	-0.025	0.000	0.000	0.000	0.000
52	A	52	ASN	0	-0.017	-0.018	18.301	-0.027	-0.027	0.000	0.000	0.000	0.000
53	A	53	ASP	-1	-0.770	-0.866	19.693	-0.069	-0.069	0.000	0.000	0.000	0.000
54	A	54	ILE	0	0.001	0.016	19.652	-0.009	-0.009	0.000	0.000	0.000	0.000
55	A	55	LYS	1	0.877	0.931	15.082	0.193	0.193	0.000	0.000	0.000	0.000
56	A	56	ALA	0	0.020	0.004	18.289	-0.020	-0.020	0.000	0.000	0.000	0.000
57	A	57	ILE	0	-0.029	-0.002	21.284	0.002	0.002	0.000	0.000	0.000	0.000
58	A	58	CYS	0	-0.128	-0.069	17.854	-0.004	-0.004	0.000	0.000	0.000	0.000
59	A	59	GLU	-1	-0.856	-0.899	19.551	-0.173	-0.173	0.000	0.000	0.000	0.000
60	A	60	ASP	-1	-0.795	-0.902	22.619	-0.136	-0.136	0.000	0.000	0.000	0.000
61	A	61	ARG	1	0.851	0.935	23.751	0.076	0.076	0.000	0.000	0.000	0.000
62	A	62	ASN	0	0.006	-0.005	24.621	0.016	0.016	0.000	0.000	0.000	0.000
63	A	63	GLY	0	0.037	0.027	25.508	0.000	0.000	0.000	0.000	0.000	0.000
64	A	64	GLN	0	0.000	0.004	26.479	0.009	0.009	0.000	0.000	0.000	0.000
65	A	65	PRO	0	0.042	0.030	27.491	-0.007	-0.007	0.000	0.000	0.000	0.000
66	A	66	TYR	0	-0.003	-0.015	28.194	0.014	0.014	0.000	0.000	0.000	0.000
67	A	67	ARG	1	0.893	0.928	28.864	0.140	0.140	0.000	0.000	0.000	0.000
68	A	68	GLY	0	0.025	0.022	29.733	-0.006	-0.006	0.000	0.000	0.000	0.000
69	A	69	ASP	-1	-0.878	-0.929	24.617	-0.229	-0.229	0.000	0.000	0.000	0.000
70	A	70	LEU	0	-0.081	-0.030	23.814	-0.018	-0.018	0.000	0.000	0.000	0.000
71	A	71	ARG	1	0.810	0.892	22.700	0.180	0.180	0.000	0.000	0.000	0.000
72	A	72	ILE	0	-0.023	-0.013	25.637	0.001	0.001	0.000	0.000	0.000	0.000
73	A	73	SER	0	-0.025	-0.025	26.422	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	74	LYS	1	0.861	0.937	27.828	0.103	0.103	0.000	0.000	0.000	0.000
75	A	75	SER	0	-0.013	-0.020	28.313	0.007	0.007	0.000	0.000	0.000	0.000
76	A	76	GLU	-1	-0.869	-0.906	29.613	-0.055	-0.055	0.000	0.000	0.000	0.000
77	A	77	PHE	0	-0.040	-0.027	24.394	0.002	0.002	0.000	0.000	0.000	0.000
78	A	78	GLN	0	0.062	0.046	28.924	0.002	0.002	0.000	0.000	0.000	0.000
79	A	79	ILE	0	-0.007	-0.023	27.067	-0.003	-0.003	0.000	0.000	0.000	0.000
80	A	80	THR	0	-0.009	0.012	28.146	0.008	0.008	0.000	0.000	0.000	0.000
81	A	81	ILE	0	-0.008	0.008	28.298	-0.005	-0.005	0.000	0.000	0.000	0.000
82	A	83	LYS	1	0.900	0.918	30.040	0.053	0.053	0.000	0.000	0.000	0.000
83	A	84	HIS	0	-0.021	-0.018	31.626	0.008	0.008	0.000	0.000	0.000	0.000
84	A	85	LYS	1	0.853	0.925	33.362	0.021	0.021	0.000	0.000	0.000	0.000
85	A	86	GLY	0	0.006	0.000	36.579	0.002	0.002	0.000	0.000	0.000	0.000
86	A	87	GLY	0	0.046	0.016	37.341	-0.003	-0.003	0.000	0.000	0.000	0.000
87	A	88	SER	0	-0.006	0.023	35.753	-0.003	-0.003	0.000	0.000	0.000	0.000
88	A	89	SER	0	0.074	0.029	31.237	-0.004	-0.004	0.000	0.000	0.000	0.000
89	A	90	ARG	1	0.924	0.957	31.239	0.018	0.018	0.000	0.000	0.000	0.000
90	A	91	PRO	0	0.038	0.002	29.499	0.002	0.002	0.000	0.000	0.000	0.000
91	A	92	PRO	0	-0.026	-0.028	32.267	0.002	0.002	0.000	0.000	0.000	0.000
92	A	94	ARG	1	0.944	0.976	31.869	0.007	0.007	0.000	0.000	0.000	0.000
93	A	95	TYR	0	0.016	-0.016	28.870	-0.002	-0.002	0.000	0.000	0.000	0.000
94	A	96	GLY	0	-0.027	-0.004	33.642	0.005	0.005	0.000	0.000	0.000	0.000
95	A	97	ALA	0	-0.010	-0.011	33.152	-0.005	-0.005	0.000	0.000	0.000	0.000
96	A	98	THR	0	-0.017	-0.009	33.283	0.001	0.001	0.000	0.000	0.000	0.000
97	A	99	GLU	-1	-0.902	-0.941	33.007	-0.019	-0.019	0.000	0.000	0.000	0.000
98	A	100	ASP	-1	-0.809	-0.907	32.945	-0.047	-0.047	0.000	0.000	0.000	0.000
99	A	101	SER	0	-0.078	-0.062	32.439	0.002	0.002	0.000	0.000	0.000	0.000
100	A	102	ARG	1	0.876	0.947	30.045	0.086	0.086	0.000	0.000	0.000	0.000
101	A	103	VAL	0	0.063	0.050	30.163	-0.001	-0.001	0.000	0.000	0.000	0.000
102	A	104	ILE	0	-0.052	-0.028	24.115	0.000	0.000	0.000	0.000	0.000	0.000
103	A	105	VAL	0	0.035	0.015	26.352	-0.003	-0.003	0.000	0.000	0.000	0.000
104	A	106	VAL	0	-0.032	-0.020	20.961	-0.001	-0.001	0.000	0.000	0.000	0.000
105	A	107	GLY	0	0.051	0.026	21.026	0.006	0.006	0.000	0.000	0.000	0.000
106	A	109	GLU	-1	-0.788	-0.891	13.393	-0.726	-0.726	0.000	0.000	0.000	0.000
107	A	110	ASN	0	0.019	0.007	11.534	0.062	0.062	0.000	0.000	0.000	0.000
108	A	111	GLY	0	0.023	0.016	13.891	0.003	0.003	0.000	0.000	0.000	0.000
109	A	112	LEU	0	-0.005	-0.001	11.290	0.071	0.071	0.000	0.000	0.000	0.000
110	A	113	PRO	0	-0.006	0.004	14.715	-0.019	-0.019	0.000	0.000	0.000	0.000
111	A	114	VAL	0	-0.003	-0.023	13.357	-0.013	-0.013	0.000	0.000	0.000	0.000
112	A	115	HIS	0	-0.018	-0.006	15.931	-0.008	-0.008	0.000	0.000	0.000	0.000
113	A	116	PHE	0	0.012	0.001	19.344	0.015	0.015	0.000	0.000	0.000	0.000
114	A	117	ASP	-1	-0.787	-0.866	22.315	-0.150	-0.150	0.000	0.000	0.000	0.000
115	A	118	GLU	-1	-0.784	-0.886	25.308	-0.094	-0.094	0.000	0.000	0.000	0.000
116	A	119	SER	0	-0.080	-0.060	27.759	0.012	0.012	0.000	0.000	0.000	0.000
117	A	120	PHE	0	0.004	0.005	29.848	0.007	0.007	0.000	0.000	0.000	0.000
118	A	121	ILE	0	0.004	-0.003	31.579	0.005	0.005	0.000	0.000	0.000	0.000
119	A	122	THR	0	-0.006	-0.008	33.345	-0.003	-0.003	0.000	0.000	0.000	0.000
120	A	123	PRO	0	0.012	0.015	36.166	0.003	0.003	0.000	0.000	0.000	0.000
121	A	124	ARG	1	0.878	0.912	37.774	0.046	0.046	0.000	0.000	0.000	0.000
122	A	125	HIS	0	0.042	0.042	39.548	0.003	0.003	0.000	0.000	0.000	0.000

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