FMO DATABASE

FMODB ID: 145VZ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1112013.891869
FMO2-HF: Nuclear repulsion	1061462.144707
FMO2-HF: Total energy	-50551.747162
FMO2-MP2: Total energy	-50698.404546

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.
-15.51	-7.096	4.093	-4.083	-8.425	-0.007

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 : 0.049 / q_NPA : 0.017

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	0.975	0.977	3.570	-6.913	-4.198	0.017	-1.212	-1.521	0.007
4	A	6	VAL	0	0.074	0.067	2.502	-2.465	-1.261	1.149	-0.643	-1.710	0.000
5	A	7	GLN	0	0.019	0.012	2.938	-2.766	-0.951	0.259	-0.913	-1.161	-0.006
6	A	8	ASP	-1	-0.899	-0.950	5.598	1.236	1.236	0.000	0.000	0.000	0.000
7	A	9	ASP	-1	-0.904	-0.960	7.621	1.032	1.032	0.000	0.000	0.000	0.000
8	A	10	THR	0	-0.032	-0.029	7.329	-0.215	-0.215	0.000	0.000	0.000	0.000
9	A	11	LYS	1	0.829	0.895	9.635	0.196	0.196	0.000	0.000	0.000	0.000
10	A	12	THR	0	-0.054	-0.034	11.517	-0.040	-0.040	0.000	0.000	0.000	0.000
11	A	13	LEU	0	0.029	0.030	12.853	-0.025	-0.025	0.000	0.000	0.000	0.000
12	A	14	ILE	0	0.040	0.013	12.502	-0.018	-0.018	0.000	0.000	0.000	0.000
13	A	15	LYS	1	0.920	0.961	14.012	-0.124	-0.124	0.000	0.000	0.000	0.000
14	A	16	THR	0	-0.027	-0.002	17.377	0.001	0.001	0.000	0.000	0.000	0.000
15	A	17	ILE	0	0.018	0.003	17.233	-0.003	-0.003	0.000	0.000	0.000	0.000
16	A	18	VAL	0	-0.006	0.003	19.232	-0.008	-0.008	0.000	0.000	0.000	0.000
17	A	19	THR	0	-0.047	-0.030	21.707	-0.001	-0.001	0.000	0.000	0.000	0.000
18	A	20	ARG	1	0.854	0.921	20.794	-0.067	-0.067	0.000	0.000	0.000	0.000
19	A	21	ILE	0	-0.024	-0.019	23.024	-0.002	-0.002	0.000	0.000	0.000	0.000
20	A	22	ASN	0	-0.019	0.009	25.085	-0.011	-0.011	0.000	0.000	0.000	0.000
21	A	23	ASP	-1	-0.951	-0.977	27.903	0.047	0.047	0.000	0.000	0.000	0.000
22	A	24	ILE	0	-0.120	-0.035	28.310	0.000	0.000	0.000	0.000	0.000	0.000
23	A	39	LEU	0	-0.029	-0.033	31.306	-0.001	-0.001	0.000	0.000	0.000	0.000
24	A	40	ASP	-1	-0.898	-0.938	29.669	-0.036	-0.036	0.000	0.000	0.000	0.000
25	A	41	PHE	0	-0.040	-0.030	27.890	-0.004	-0.004	0.000	0.000	0.000	0.000
26	A	42	ILE	0	-0.066	-0.007	28.244	-0.007	-0.007	0.000	0.000	0.000	0.000
27	A	43	PRO	0	0.021	0.014	25.818	-0.005	-0.005	0.000	0.000	0.000	0.000
28	A	44	GLY	0	0.072	0.035	23.229	0.007	0.007	0.000	0.000	0.000	0.000
29	A	45	LEU	0	-0.047	-0.044	23.891	-0.002	-0.002	0.000	0.000	0.000	0.000
30	A	46	HIS	0	-0.034	-0.024	20.551	-0.008	-0.008	0.000	0.000	0.000	0.000
31	A	47	PRO	0	0.042	0.055	18.607	-0.018	-0.018	0.000	0.000	0.000	0.000
32	A	48	ILE	0	-0.074	-0.041	17.506	-0.008	-0.008	0.000	0.000	0.000	0.000
33	A	49	LEU	0	0.093	0.025	14.009	-0.009	-0.009	0.000	0.000	0.000	0.000
34	A	50	THR	0	-0.090	-0.025	11.485	-0.045	-0.045	0.000	0.000	0.000	0.000
35	A	51	LEU	0	0.076	0.015	6.038	0.040	0.040	0.000	0.000	0.000	0.000
36	A	52	SER	0	0.040	0.018	10.673	0.041	0.041	0.000	0.000	0.000	0.000
37	A	53	LYS	1	0.912	0.975	13.963	0.358	0.358	0.000	0.000	0.000	0.000
38	A	54	MET	0	-0.012	0.021	11.098	0.019	0.019	0.000	0.000	0.000	0.000
39	A	55	ASP	-1	-0.738	-0.856	13.578	-0.260	-0.260	0.000	0.000	0.000	0.000
40	A	56	GLN	0	-0.004	-0.010	15.344	0.038	0.038	0.000	0.000	0.000	0.000
41	A	57	THR	0	-0.013	-0.004	18.088	0.033	0.033	0.000	0.000	0.000	0.000
42	A	58	LEU	0	-0.020	-0.017	14.672	0.029	0.029	0.000	0.000	0.000	0.000
43	A	59	ALA	0	0.031	0.020	18.854	0.027	0.027	0.000	0.000	0.000	0.000
44	A	60	VAL	0	0.016	0.008	20.754	0.020	0.020	0.000	0.000	0.000	0.000
45	A	61	TYR	0	0.032	-0.014	20.899	0.019	0.019	0.000	0.000	0.000	0.000
46	A	62	GLN	0	-0.004	0.002	19.978	-0.002	-0.002	0.000	0.000	0.000	0.000
47	A	63	GLN	0	-0.009	0.005	23.728	0.004	0.004	0.000	0.000	0.000	0.000
48	A	64	ILE	0	0.011	0.011	26.516	0.008	0.008	0.000	0.000	0.000	0.000
49	A	65	LEU	0	0.006	-0.009	24.289	0.009	0.009	0.000	0.000	0.000	0.000
50	A	66	THR	0	-0.035	-0.019	26.793	0.011	0.011	0.000	0.000	0.000	0.000
51	A	67	SER	0	-0.091	-0.044	29.212	0.006	0.006	0.000	0.000	0.000	0.000
52	A	68	MET	0	-0.019	0.012	30.547	0.002	0.002	0.000	0.000	0.000	0.000
53	A	69	PRO	0	-0.007	0.006	31.305	0.003	0.003	0.000	0.000	0.000	0.000
54	A	70	SER	0	0.055	0.009	31.498	0.003	0.003	0.000	0.000	0.000	0.000
55	A	71	ARG	1	0.983	0.980	30.968	-0.036	-0.036	0.000	0.000	0.000	0.000
56	A	72	ASN	0	0.013	-0.001	28.357	0.004	0.004	0.000	0.000	0.000	0.000
57	A	73	VAL	0	0.068	0.061	26.894	0.002	0.002	0.000	0.000	0.000	0.000
58	A	74	ILE	0	0.020	0.014	26.370	-0.004	-0.004	0.000	0.000	0.000	0.000
59	A	75	GLN	0	-0.033	-0.004	24.242	-0.005	-0.005	0.000	0.000	0.000	0.000
60	A	76	ILE	0	0.023	-0.005	22.449	0.005	0.005	0.000	0.000	0.000	0.000
61	A	77	SER	0	0.006	-0.008	21.699	-0.012	-0.012	0.000	0.000	0.000	0.000
62	A	78	ASN	0	-0.008	0.006	21.083	-0.022	-0.022	0.000	0.000	0.000	0.000
63	A	79	ASP	-1	-0.863	-0.932	18.384	0.070	0.070	0.000	0.000	0.000	0.000
64	A	80	LEU	0	-0.036	-0.036	17.039	-0.010	-0.010	0.000	0.000	0.000	0.000
65	A	81	GLU	-1	-0.858	-0.928	16.876	-0.129	-0.129	0.000	0.000	0.000	0.000
66	A	82	ASN	0	0.009	0.013	14.543	-0.014	-0.014	0.000	0.000	0.000	0.000
67	A	83	LEU	0	-0.031	-0.025	11.820	0.000	0.000	0.000	0.000	0.000	0.000
68	A	84	ARG	1	0.873	0.913	11.971	0.118	0.118	0.000	0.000	0.000	0.000
69	A	85	ASP	-1	-0.859	-0.911	11.950	-0.139	-0.139	0.000	0.000	0.000	0.000
70	A	86	LEU	0	-0.061	-0.034	7.583	-0.081	-0.081	0.000	0.000	0.000	0.000
71	A	87	LEU	0	-0.006	-0.006	7.309	-0.282	-0.282	0.000	0.000	0.000	0.000
72	A	88	HIS	0	0.001	-0.016	8.181	-0.254	-0.254	0.000	0.000	0.000	0.000
73	A	89	VAL	0	-0.021	-0.003	5.167	-0.100	-0.100	0.000	0.000	0.000	0.000
74	A	90	LEU	0	-0.014	-0.008	2.302	-0.944	-0.966	2.249	-0.403	-1.824	-0.003
75	A	91	ALA	0	0.035	0.009	4.663	-0.602	-0.473	-0.001	-0.006	-0.122	0.000
76	A	92	PHE	0	-0.009	0.013	7.262	-0.036	-0.036	0.000	0.000	0.000	0.000
77	A	93	SER	0	-0.055	-0.029	3.042	-2.352	-0.650	0.225	-0.721	-1.207	-0.006
78	A	94	LYS	1	0.858	0.925	2.882	0.456	1.304	0.196	-0.181	-0.863	0.001
79	A	95	SER	0	-0.048	-0.019	4.809	0.376	0.399	-0.001	-0.004	-0.017	0.000
80	A	146	CYS	0	-0.073	-0.024	8.343	0.041	0.041	0.000	0.000	0.000	0.000
81	A	97	HIS	0	0.006	-0.004	10.066	0.032	0.032	0.000	0.000	0.000	0.000
82	A	98	LEU	0	-0.028	-0.012	10.347	-0.011	-0.011	0.000	0.000	0.000	0.000
83	A	99	PRO	0	-0.033	-0.022	13.900	0.028	0.028	0.000	0.000	0.000	0.000
84	A	100	GLU	-1	-0.910	-0.941	17.591	-0.173	-0.173	0.000	0.000	0.000	0.000
85	A	101	ALA	0	-0.055	-0.025	19.122	0.002	0.002	0.000	0.000	0.000	0.000
86	A	102	SER	0	0.002	-0.001	20.747	0.017	0.017	0.000	0.000	0.000	0.000
87	A	103	GLY	0	0.003	0.004	24.228	-0.003	-0.003	0.000	0.000	0.000	0.000
88	A	104	LEU	0	-0.083	-0.039	26.549	0.002	0.002	0.000	0.000	0.000	0.000
89	A	105	GLU	-1	-0.918	-0.965	29.467	-0.066	-0.066	0.000	0.000	0.000	0.000
90	A	106	THR	0	-0.004	-0.009	32.500	0.004	0.004	0.000	0.000	0.000	0.000
91	A	107	LEU	0	-0.001	-0.014	30.308	-0.005	-0.005	0.000	0.000	0.000	0.000
92	A	108	ASP	-1	-0.866	-0.931	33.261	-0.051	-0.051	0.000	0.000	0.000	0.000
93	A	109	SER	0	-0.043	-0.020	33.227	0.001	0.001	0.000	0.000	0.000	0.000
94	A	110	LEU	0	-0.050	-0.031	28.654	-0.003	-0.003	0.000	0.000	0.000	0.000
95	A	111	GLY	0	0.067	0.042	32.783	0.001	0.001	0.000	0.000	0.000	0.000
96	A	112	GLY	0	0.015	0.003	35.897	0.001	0.001	0.000	0.000	0.000	0.000
97	A	113	VAL	0	-0.046	-0.019	30.133	0.000	0.000	0.000	0.000	0.000	0.000
98	A	114	LEU	0	0.018	0.000	29.628	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	115	GLU	-1	-0.890	-0.931	33.393	-0.040	-0.040	0.000	0.000	0.000	0.000
100	A	116	ALA	0	-0.015	-0.015	36.372	-0.003	-0.003	0.000	0.000	0.000	0.000
101	A	117	SER	0	-0.026	-0.003	38.333	0.003	0.003	0.000	0.000	0.000	0.000
102	A	118	GLY	0	-0.036	-0.028	40.836	0.000	0.000	0.000	0.000	0.000	0.000
103	A	119	TYR	0	-0.015	-0.013	36.291	0.001	0.001	0.000	0.000	0.000	0.000
104	A	120	SER	0	0.035	0.038	36.076	-0.002	-0.002	0.000	0.000	0.000	0.000
105	A	121	THR	0	0.099	0.040	34.329	-0.001	-0.001	0.000	0.000	0.000	0.000
106	A	122	GLU	-1	-0.903	-0.968	32.275	-0.031	-0.031	0.000	0.000	0.000	0.000
107	A	123	VAL	0	-0.003	-0.003	31.185	-0.001	-0.001	0.000	0.000	0.000	0.000
108	A	124	VAL	0	0.014	0.031	31.054	-0.003	-0.003	0.000	0.000	0.000	0.000
109	A	125	ALA	0	-0.004	-0.010	28.583	-0.008	-0.008	0.000	0.000	0.000	0.000
110	A	126	LEU	0	0.005	-0.012	26.340	-0.008	-0.008	0.000	0.000	0.000	0.000
111	A	127	SER	0	0.022	-0.003	26.207	0.000	0.000	0.000	0.000	0.000	0.000
112	A	128	ARG	1	0.791	0.884	26.083	0.078	0.078	0.000	0.000	0.000	0.000
113	A	129	LEU	0	-0.023	0.005	20.483	-0.014	-0.014	0.000	0.000	0.000	0.000
114	A	130	GLN	0	-0.004	-0.016	21.510	-0.017	-0.017	0.000	0.000	0.000	0.000
115	A	131	GLY	0	0.068	0.049	21.585	-0.007	-0.007	0.000	0.000	0.000	0.000
116	A	132	SER	0	0.003	-0.020	19.552	-0.011	-0.011	0.000	0.000	0.000	0.000
117	A	133	LEU	0	-0.027	0.000	16.893	-0.031	-0.031	0.000	0.000	0.000	0.000
118	A	134	GLN	0	-0.010	-0.019	16.663	-0.023	-0.023	0.000	0.000	0.000	0.000
119	A	135	ASP	-1	-0.877	-0.939	17.620	-0.215	-0.215	0.000	0.000	0.000	0.000
120	A	136	MET	0	-0.047	-0.028	13.206	-0.038	-0.038	0.000	0.000	0.000	0.000
121	A	137	LEU	0	-0.039	-0.019	12.661	-0.058	-0.058	0.000	0.000	0.000	0.000
122	A	138	TRP	0	-0.030	-0.018	12.500	-0.043	-0.043	0.000	0.000	0.000	0.000
123	A	139	GLN	0	0.044	0.030	12.671	-0.079	-0.079	0.000	0.000	0.000	0.000
124	A	140	LEU	0	-0.008	-0.014	8.144	-0.103	-0.103	0.000	0.000	0.000	0.000
125	A	141	ASP	-1	-0.857	-0.906	7.692	-0.555	-0.555	0.000	0.000	0.000	0.000
126	A	142	LEU	0	-0.089	-0.038	9.678	0.017	0.017	0.000	0.000	0.000	0.000
127	A	143	SER	0	-0.072	-0.031	5.399	-0.199	-0.199	0.000	0.000	0.000	0.000
128	A	144	PRO	0	-0.009	0.018	6.655	0.070	0.070	0.000	0.000	0.000	0.000
129	A	145	GLY	0	0.024	0.005	7.311	-0.139	-0.139	0.000	0.000	0.000	0.000

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