FMO DATABASE

FMODB ID: 82GKY

Calculation Name: 1AX8-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1AX8

Chain ID: A

ChEMBL ID:

UniProt ID: P41159

Base Structure: X-ray

Registration Date: 2023-03-13

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	129
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1113548.175503
FMO2-HF: Nuclear repulsion	1062995.212052
FMO2-HF: Total energy	-50552.963451
FMO2-MP2: Total energy	-50699.422157

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:ILE)

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

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.
-16.112	-6.832	4.609	-4.371	-9.517	-0.023

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.016 / q_NPA : 0.007

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	LYS	1	0.864	0.920	3.665	-4.771	-2.594	0.011	-0.965	-1.223	0.004
4	A	6	VAL	0	0.116	0.069	2.695	-2.344	-1.155	0.458	-0.463	-1.184	0.000
5	A	7	GLN	0	0.005	0.023	2.605	-3.498	-1.781	0.824	-1.009	-1.532	-0.013
6	A	8	ASP	-1	-0.819	-0.895	5.840	1.011	1.011	0.000	0.000	0.000	0.000
7	A	9	ASP	-1	-0.896	-0.940	7.971	1.116	1.116	0.000	0.000	0.000	0.000
8	A	10	THR	0	-0.027	-0.034	7.472	-0.156	-0.156	0.000	0.000	0.000	0.000
9	A	11	LYS	1	0.829	0.899	9.883	0.264	0.264	0.000	0.000	0.000	0.000
10	A	12	THR	0	-0.069	-0.039	11.784	-0.020	-0.020	0.000	0.000	0.000	0.000
11	A	13	LEU	0	0.024	0.031	13.075	-0.018	-0.018	0.000	0.000	0.000	0.000
12	A	14	ILE	0	0.032	0.010	12.307	-0.015	-0.015	0.000	0.000	0.000	0.000
13	A	15	LYS	1	0.882	0.933	14.604	-0.111	-0.111	0.000	0.000	0.000	0.000
14	A	16	THR	0	-0.042	-0.009	17.379	0.006	0.006	0.000	0.000	0.000	0.000
15	A	17	ILE	0	0.011	-0.001	16.977	-0.005	-0.005	0.000	0.000	0.000	0.000
16	A	18	VAL	0	0.000	-0.001	19.256	-0.007	-0.007	0.000	0.000	0.000	0.000
17	A	19	THR	0	-0.055	-0.032	21.592	-0.002	-0.002	0.000	0.000	0.000	0.000
18	A	20	ARG	1	0.854	0.915	21.294	-0.087	-0.087	0.000	0.000	0.000	0.000
19	A	21	ILE	0	-0.002	-0.004	22.945	-0.002	-0.002	0.000	0.000	0.000	0.000
20	A	22	ASN	0	0.014	0.020	25.340	-0.010	-0.010	0.000	0.000	0.000	0.000
21	A	23	ASP	-1	-0.926	-0.960	27.148	0.046	0.046	0.000	0.000	0.000	0.000
22	A	24	ILE	0	-0.157	-0.064	27.977	0.001	0.001	0.000	0.000	0.000	0.000
23	A	39	LEU	0	-0.021	-0.025	31.298	-0.001	-0.001	0.000	0.000	0.000	0.000
24	A	40	ASP	-1	-0.911	-0.950	29.628	-0.040	-0.040	0.000	0.000	0.000	0.000
25	A	41	PHE	0	-0.030	-0.018	27.768	-0.004	-0.004	0.000	0.000	0.000	0.000
26	A	42	ILE	0	-0.040	-0.003	28.041	-0.006	-0.006	0.000	0.000	0.000	0.000
27	A	43	PRO	0	-0.001	0.004	25.670	-0.005	-0.005	0.000	0.000	0.000	0.000
28	A	44	GLY	0	0.060	0.023	22.985	0.008	0.008	0.000	0.000	0.000	0.000
29	A	45	LEU	0	-0.024	-0.018	23.662	-0.002	-0.002	0.000	0.000	0.000	0.000
30	A	46	HIS	0	-0.038	-0.015	20.465	0.001	0.001	0.000	0.000	0.000	0.000
31	A	47	PRO	0	0.022	0.036	18.074	-0.019	-0.019	0.000	0.000	0.000	0.000
32	A	48	ILE	0	0.006	-0.025	16.760	0.003	0.003	0.000	0.000	0.000	0.000
33	A	49	LEU	0	0.052	0.041	13.304	-0.027	-0.027	0.000	0.000	0.000	0.000
34	A	50	THR	0	-0.105	-0.059	10.834	-0.035	-0.035	0.000	0.000	0.000	0.000
35	A	51	LEU	0	0.088	0.041	5.693	0.049	0.049	0.000	0.000	0.000	0.000
36	A	52	SER	0	0.053	0.044	10.384	0.042	0.042	0.000	0.000	0.000	0.000
37	A	53	LYS	1	0.912	0.972	13.603	0.365	0.365	0.000	0.000	0.000	0.000
38	A	54	MET	0	-0.001	0.004	11.412	0.009	0.009	0.000	0.000	0.000	0.000
39	A	55	ASP	-1	-0.728	-0.843	13.523	-0.209	-0.209	0.000	0.000	0.000	0.000
40	A	56	GLN	0	-0.011	-0.005	15.240	0.036	0.036	0.000	0.000	0.000	0.000
41	A	57	THR	0	-0.024	-0.023	17.997	0.020	0.020	0.000	0.000	0.000	0.000
42	A	58	LEU	0	-0.025	-0.019	14.590	0.027	0.027	0.000	0.000	0.000	0.000
43	A	59	ALA	0	0.055	0.034	18.683	0.026	0.026	0.000	0.000	0.000	0.000
44	A	60	VAL	0	-0.005	-0.001	20.700	0.019	0.019	0.000	0.000	0.000	0.000
45	A	61	TYR	0	0.015	-0.019	20.638	0.019	0.019	0.000	0.000	0.000	0.000
46	A	62	GLN	0	-0.007	-0.011	19.349	-0.004	-0.004	0.000	0.000	0.000	0.000
47	A	63	GLN	0	-0.013	0.010	23.559	0.005	0.005	0.000	0.000	0.000	0.000
48	A	64	ILE	0	0.016	0.010	26.437	0.008	0.008	0.000	0.000	0.000	0.000
49	A	65	LEU	0	0.015	0.007	23.737	0.008	0.008	0.000	0.000	0.000	0.000
50	A	66	THR	0	-0.055	-0.044	26.730	0.011	0.011	0.000	0.000	0.000	0.000
51	A	67	SER	0	-0.080	-0.046	29.179	0.004	0.004	0.000	0.000	0.000	0.000
52	A	68	MET	0	-0.035	0.013	30.605	0.002	0.002	0.000	0.000	0.000	0.000
53	A	69	PRO	0	0.006	0.011	31.313	0.004	0.004	0.000	0.000	0.000	0.000
54	A	70	SER	0	0.051	0.008	31.414	0.003	0.003	0.000	0.000	0.000	0.000
55	A	71	ARG	1	0.903	0.935	30.619	-0.038	-0.038	0.000	0.000	0.000	0.000
56	A	72	ASN	0	0.076	0.039	28.120	0.008	0.008	0.000	0.000	0.000	0.000
57	A	73	VAL	0	0.038	0.039	26.816	0.001	0.001	0.000	0.000	0.000	0.000
58	A	74	ILE	0	0.006	0.002	26.410	-0.004	-0.004	0.000	0.000	0.000	0.000
59	A	75	GLN	0	-0.058	-0.022	24.030	-0.004	-0.004	0.000	0.000	0.000	0.000
60	A	76	ILE	0	0.053	0.024	22.261	0.006	0.006	0.000	0.000	0.000	0.000
61	A	77	SER	0	0.008	0.004	21.569	-0.012	-0.012	0.000	0.000	0.000	0.000
62	A	78	ASN	0	0.000	0.003	20.644	-0.006	-0.006	0.000	0.000	0.000	0.000
63	A	79	ASP	-1	-0.839	-0.907	18.594	0.081	0.081	0.000	0.000	0.000	0.000
64	A	80	LEU	0	-0.006	-0.018	17.047	-0.003	-0.003	0.000	0.000	0.000	0.000
65	A	81	GLU	-1	-0.785	-0.868	16.532	-0.095	-0.095	0.000	0.000	0.000	0.000
66	A	82	ASN	0	-0.059	-0.034	14.864	0.024	0.024	0.000	0.000	0.000	0.000
67	A	83	LEU	0	-0.020	-0.015	11.920	0.015	0.015	0.000	0.000	0.000	0.000
68	A	84	ARG	1	0.815	0.877	11.707	0.081	0.081	0.000	0.000	0.000	0.000
69	A	85	ASP	-1	-0.873	-0.927	11.802	-0.067	-0.067	0.000	0.000	0.000	0.000
70	A	86	LEU	0	-0.061	-0.029	7.829	-0.030	-0.030	0.000	0.000	0.000	0.000
71	A	87	LEU	0	0.007	-0.006	7.222	-0.271	-0.271	0.000	0.000	0.000	0.000
72	A	88	HIS	0	-0.006	-0.013	7.909	-0.273	-0.273	0.000	0.000	0.000	0.000
73	A	89	VAL	0	-0.007	0.000	5.271	-0.110	-0.110	0.000	0.000	0.000	0.000
74	A	90	LEU	0	-0.028	-0.010	2.481	-1.300	-0.695	1.338	-0.296	-1.647	-0.001
75	A	91	ALA	0	0.008	0.000	4.285	-0.951	-0.702	0.000	-0.045	-0.204	0.000
76	A	92	PHE	0	0.018	0.011	6.466	-0.103	-0.103	0.000	0.000	0.000	0.000
77	A	93	SER	0	-0.069	-0.047	2.730	-3.511	-1.116	1.044	-1.229	-2.210	-0.012
78	A	94	LYS	1	0.845	0.927	2.656	-0.020	0.872	0.933	-0.343	-1.482	-0.001
79	A	95	SER	0	-0.053	-0.017	4.194	0.453	0.509	0.001	-0.021	-0.035	0.000
80	A	146	CYS	0	-0.114	-0.069	7.684	0.133	0.133	0.000	0.000	0.000	0.000
81	A	97	HIS	0	0.024	0.006	9.429	0.013	0.013	0.000	0.000	0.000	0.000
82	A	98	LEU	0	-0.033	-0.025	9.709	-0.031	-0.031	0.000	0.000	0.000	0.000
83	A	99	PRO	0	-0.020	-0.018	13.407	0.033	0.033	0.000	0.000	0.000	0.000
84	A	100	GLU	-1	-0.937	-0.958	17.077	-0.145	-0.145	0.000	0.000	0.000	0.000
85	A	101	ALA	0	-0.027	-0.006	18.694	0.002	0.002	0.000	0.000	0.000	0.000
86	A	102	SER	0	-0.012	-0.004	20.190	0.020	0.020	0.000	0.000	0.000	0.000
87	A	103	GLY	0	0.019	0.017	23.799	-0.002	-0.002	0.000	0.000	0.000	0.000
88	A	104	LEU	0	-0.052	-0.034	26.178	0.001	0.001	0.000	0.000	0.000	0.000
89	A	105	GLU	-1	-0.919	-0.954	29.075	-0.056	-0.056	0.000	0.000	0.000	0.000
90	A	106	THR	0	-0.006	-0.002	32.377	0.005	0.005	0.000	0.000	0.000	0.000
91	A	107	LEU	0	0.011	0.001	29.984	-0.005	-0.005	0.000	0.000	0.000	0.000
92	A	108	ASP	-1	-0.855	-0.926	32.858	-0.047	-0.047	0.000	0.000	0.000	0.000
93	A	109	SER	0	-0.078	-0.046	32.396	-0.002	-0.002	0.000	0.000	0.000	0.000
94	A	110	LEU	0	0.002	-0.007	27.934	-0.004	-0.004	0.000	0.000	0.000	0.000
95	A	111	GLY	0	0.081	0.047	32.167	0.001	0.001	0.000	0.000	0.000	0.000
96	A	112	GLY	0	-0.023	-0.012	35.471	0.002	0.002	0.000	0.000	0.000	0.000
97	A	113	VAL	0	-0.055	-0.023	29.595	-0.002	-0.002	0.000	0.000	0.000	0.000
98	A	114	LEU	0	-0.013	-0.011	29.480	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	115	GLU	-1	-0.897	-0.949	33.249	-0.033	-0.033	0.000	0.000	0.000	0.000
100	A	116	ALA	0	-0.018	-0.017	35.990	-0.003	-0.003	0.000	0.000	0.000	0.000
101	A	117	SER	0	-0.036	-0.015	38.019	0.003	0.003	0.000	0.000	0.000	0.000
102	A	118	GLY	0	-0.011	-0.008	40.918	-0.001	-0.001	0.000	0.000	0.000	0.000
103	A	119	TYR	0	-0.038	-0.017	36.160	0.001	0.001	0.000	0.000	0.000	0.000
104	A	120	SER	0	-0.012	-0.027	36.161	0.001	0.001	0.000	0.000	0.000	0.000
105	A	121	THR	0	0.060	0.030	33.991	-0.002	-0.002	0.000	0.000	0.000	0.000
106	A	122	GLU	-1	-0.794	-0.891	31.730	-0.026	-0.026	0.000	0.000	0.000	0.000
107	A	123	VAL	0	0.013	0.004	30.683	-0.002	-0.002	0.000	0.000	0.000	0.000
108	A	124	VAL	0	0.001	0.027	30.733	-0.004	-0.004	0.000	0.000	0.000	0.000
109	A	125	ALA	0	0.008	0.001	28.115	-0.008	-0.008	0.000	0.000	0.000	0.000
110	A	126	LEU	0	-0.004	-0.011	26.289	-0.008	-0.008	0.000	0.000	0.000	0.000
111	A	127	SER	0	0.017	-0.004	25.865	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	128	ARG	1	0.817	0.904	25.782	0.072	0.072	0.000	0.000	0.000	0.000
113	A	129	LEU	0	0.016	0.028	20.389	-0.017	-0.017	0.000	0.000	0.000	0.000
114	A	130	GLN	0	-0.026	-0.036	21.344	-0.018	-0.018	0.000	0.000	0.000	0.000
115	A	131	GLY	0	0.067	0.040	21.388	-0.007	-0.007	0.000	0.000	0.000	0.000
116	A	132	SER	0	-0.037	-0.038	19.435	-0.021	-0.021	0.000	0.000	0.000	0.000
117	A	133	LEU	0	-0.021	-0.002	16.740	-0.031	-0.031	0.000	0.000	0.000	0.000
118	A	134	GLN	0	-0.007	-0.015	16.539	-0.024	-0.024	0.000	0.000	0.000	0.000
119	A	135	ASP	-1	-0.835	-0.906	17.357	-0.237	-0.237	0.000	0.000	0.000	0.000
120	A	136	MET	0	-0.017	-0.019	13.317	-0.038	-0.038	0.000	0.000	0.000	0.000
121	A	137	LEU	0	-0.048	-0.011	12.460	-0.059	-0.059	0.000	0.000	0.000	0.000
122	A	138	TRP	0	-0.029	-0.024	12.498	-0.037	-0.037	0.000	0.000	0.000	0.000
123	A	139	GLN	0	-0.018	-0.018	12.465	-0.093	-0.093	0.000	0.000	0.000	0.000
124	A	140	LEU	0	-0.007	-0.022	7.741	-0.104	-0.104	0.000	0.000	0.000	0.000
125	A	141	ASP	-1	-0.828	-0.897	7.386	-0.602	-0.602	0.000	0.000	0.000	0.000
126	A	142	LEU	0	-0.087	-0.036	9.186	-0.017	-0.017	0.000	0.000	0.000	0.000
127	A	143	SER	0	-0.030	-0.011	4.910	-0.167	-0.167	0.000	0.000	0.000	0.000
128	A	144	PRO	0	-0.004	0.031	6.301	0.030	0.030	0.000	0.000	0.000	0.000
129	A	145	GLY	0	0.052	0.017	6.896	-0.159	-0.159	0.000	0.000	0.000	0.000

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