FMO DATABASE

FMODB ID: 85MYY

Calculation Name: 1ICX-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1ICX

Chain ID: A

ChEMBL ID:

UniProt ID: P52778

Base Structure: X-ray

Registration Date: 2023-09-20

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	155
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1395210.383867
FMO2-HF: Nuclear repulsion	1337893.195976
FMO2-HF: Total energy	-57317.187891
FMO2-MP2: Total energy	-57489.356

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:GLY)

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

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.
-7.69	-2.607	5.941	-5.424	-5.598	-0.039

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.023 / q_NPA : 0.009

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	PHE	0	-0.006	0.000	2.666	0.874	2.291	0.300	-0.778	-0.939	-0.001
4	A	4	ALA	0	-0.013	-0.005	6.106	0.045	0.045	0.000	0.000	0.000	0.000
5	A	5	PHE	0	-0.030	-0.017	9.163	0.120	0.120	0.000	0.000	0.000	0.000
6	A	6	GLU	-1	-0.818	-0.891	12.961	-0.139	-0.139	0.000	0.000	0.000	0.000
7	A	7	ASN	0	-0.056	-0.028	16.122	0.012	0.012	0.000	0.000	0.000	0.000
8	A	8	GLU	-1	-0.863	-0.937	19.218	-0.081	-0.081	0.000	0.000	0.000	0.000
9	A	9	GLN	0	-0.026	-0.012	22.948	-0.012	-0.012	0.000	0.000	0.000	0.000
10	A	10	SER	0	0.016	0.018	26.157	0.003	0.003	0.000	0.000	0.000	0.000
11	A	11	SER	0	-0.036	-0.046	29.734	-0.003	-0.003	0.000	0.000	0.000	0.000
12	A	12	THR	0	0.051	0.016	32.214	0.004	0.004	0.000	0.000	0.000	0.000
13	A	13	VAL	0	-0.011	0.008	33.386	0.006	0.006	0.000	0.000	0.000	0.000
14	A	14	ALA	0	0.033	0.028	34.071	-0.001	-0.001	0.000	0.000	0.000	0.000
15	A	15	PRO	0	-0.008	-0.008	31.876	-0.004	-0.004	0.000	0.000	0.000	0.000
16	A	16	ALA	0	0.036	0.014	31.964	-0.005	-0.005	0.000	0.000	0.000	0.000
17	A	17	LYS	1	0.895	0.947	33.592	0.053	0.053	0.000	0.000	0.000	0.000
18	A	18	LEU	0	0.036	0.027	28.971	-0.004	-0.004	0.000	0.000	0.000	0.000
19	A	19	TYR	0	0.032	-0.006	26.078	-0.006	-0.006	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.824	0.910	29.283	0.063	0.063	0.000	0.000	0.000	0.000
21	A	21	ALA	0	0.028	0.013	31.252	-0.003	-0.003	0.000	0.000	0.000	0.000
22	A	22	LEU	0	-0.033	-0.019	25.225	-0.008	-0.008	0.000	0.000	0.000	0.000
23	A	23	THR	0	-0.017	-0.015	25.641	-0.008	-0.008	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.915	0.971	27.731	0.053	0.053	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.756	-0.837	30.969	-0.073	-0.073	0.000	0.000	0.000	0.000
26	A	26	SER	0	-0.002	0.001	26.771	-0.005	-0.005	0.000	0.000	0.000	0.000
27	A	27	ASP	-1	-0.784	-0.891	27.523	-0.127	-0.127	0.000	0.000	0.000	0.000
28	A	28	GLU	-1	-0.849	-0.910	29.467	-0.083	-0.083	0.000	0.000	0.000	0.000
29	A	29	ILE	0	-0.020	-0.008	30.899	0.002	0.002	0.000	0.000	0.000	0.000
30	A	30	VAL	0	0.020	0.004	26.171	-0.001	-0.001	0.000	0.000	0.000	0.000
31	A	31	PRO	0	0.031	0.007	29.317	-0.003	-0.003	0.000	0.000	0.000	0.000
32	A	32	LYS	1	0.747	0.876	31.501	0.088	0.088	0.000	0.000	0.000	0.000
33	A	33	VAL	0	-0.084	-0.040	30.246	0.005	0.005	0.000	0.000	0.000	0.000
34	A	34	ILE	0	-0.063	-0.029	25.692	-0.008	-0.008	0.000	0.000	0.000	0.000
35	A	35	GLU	-1	-0.875	-0.930	29.631	-0.111	-0.111	0.000	0.000	0.000	0.000
36	A	36	PRO	0	0.014	0.006	27.933	0.002	0.002	0.000	0.000	0.000	0.000
37	A	37	ILE	0	-0.051	-0.025	24.954	-0.002	-0.002	0.000	0.000	0.000	0.000
38	A	38	GLN	0	-0.027	-0.009	28.823	0.015	0.015	0.000	0.000	0.000	0.000
39	A	39	SER	0	-0.044	-0.048	29.721	0.007	0.007	0.000	0.000	0.000	0.000
40	A	40	VAL	0	0.011	0.004	25.806	-0.014	-0.014	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.836	-0.884	27.488	-0.103	-0.103	0.000	0.000	0.000	0.000
42	A	42	ILE	0	-0.022	-0.014	26.780	-0.010	-0.010	0.000	0.000	0.000	0.000
43	A	43	VAL	0	-0.056	-0.033	24.264	0.006	0.006	0.000	0.000	0.000	0.000
44	A	44	GLU	-1	-0.905	-0.949	23.043	-0.064	-0.064	0.000	0.000	0.000	0.000
45	A	45	GLY	0	0.025	0.019	25.743	-0.007	-0.007	0.000	0.000	0.000	0.000
46	A	46	ASN	0	-0.034	-0.032	27.213	0.002	0.002	0.000	0.000	0.000	0.000
47	A	47	GLY	0	0.012	0.012	28.195	0.005	0.005	0.000	0.000	0.000	0.000
48	A	48	GLY	0	0.020	0.019	27.198	-0.006	-0.006	0.000	0.000	0.000	0.000
49	A	49	PRO	0	0.001	0.000	22.831	-0.010	-0.010	0.000	0.000	0.000	0.000
50	A	50	GLY	0	-0.029	-0.005	21.107	0.011	0.011	0.000	0.000	0.000	0.000
51	A	51	THR	0	-0.048	-0.041	21.912	-0.005	-0.005	0.000	0.000	0.000	0.000
52	A	52	ILE	0	-0.005	0.006	19.831	-0.021	-0.021	0.000	0.000	0.000	0.000
53	A	53	LYS	1	0.822	0.879	22.118	0.141	0.141	0.000	0.000	0.000	0.000
54	A	54	LYS	1	0.880	0.947	22.388	0.106	0.106	0.000	0.000	0.000	0.000
55	A	55	ILE	0	0.001	0.000	21.744	0.016	0.016	0.000	0.000	0.000	0.000
56	A	56	ILE	0	0.004	0.007	24.460	-0.016	-0.016	0.000	0.000	0.000	0.000
57	A	57	ALA	0	-0.003	-0.014	25.714	0.002	0.002	0.000	0.000	0.000	0.000
58	A	58	ILE	0	0.017	0.000	27.617	0.004	0.004	0.000	0.000	0.000	0.000
59	A	59	HIS	0	-0.007	0.006	25.777	-0.005	-0.005	0.000	0.000	0.000	0.000
60	A	60	ASP	-1	-0.956	-0.973	28.023	-0.147	-0.147	0.000	0.000	0.000	0.000
61	A	61	GLY	0	-0.017	-0.015	31.182	0.003	0.003	0.000	0.000	0.000	0.000
62	A	62	HIS	0	-0.032	-0.016	29.783	0.009	0.009	0.000	0.000	0.000	0.000
63	A	63	THR	0	-0.023	-0.005	29.482	-0.005	-0.005	0.000	0.000	0.000	0.000
64	A	64	SER	0	-0.049	-0.035	24.299	0.005	0.005	0.000	0.000	0.000	0.000
65	A	65	PHE	0	-0.001	-0.017	21.287	0.012	0.012	0.000	0.000	0.000	0.000
66	A	66	VAL	0	-0.009	0.011	17.967	-0.022	-0.022	0.000	0.000	0.000	0.000
67	A	67	LEU	0	-0.032	-0.009	17.833	0.033	0.033	0.000	0.000	0.000	0.000
68	A	68	HIS	0	0.031	0.012	17.610	-0.041	-0.041	0.000	0.000	0.000	0.000
69	A	69	LYS	1	0.912	0.956	16.777	0.152	0.152	0.000	0.000	0.000	0.000
70	A	70	LEU	0	0.005	0.017	18.503	-0.026	-0.026	0.000	0.000	0.000	0.000
71	A	71	ASP	-1	-0.830	-0.895	15.804	-0.192	-0.192	0.000	0.000	0.000	0.000
72	A	72	ALA	0	-0.033	-0.033	18.890	0.031	0.031	0.000	0.000	0.000	0.000
73	A	73	ILE	0	-0.018	-0.015	21.668	-0.021	-0.021	0.000	0.000	0.000	0.000
74	A	74	ASP	-1	-0.781	-0.876	24.737	-0.016	-0.016	0.000	0.000	0.000	0.000
75	A	75	GLU	-1	-0.863	-0.947	27.353	-0.056	-0.056	0.000	0.000	0.000	0.000
76	A	76	ALA	0	-0.048	-0.007	30.082	0.000	0.000	0.000	0.000	0.000	0.000
77	A	77	ASN	0	-0.064	-0.046	26.928	0.001	0.001	0.000	0.000	0.000	0.000
78	A	78	LEU	0	-0.011	0.017	27.871	-0.005	-0.005	0.000	0.000	0.000	0.000
79	A	79	THR	0	-0.009	-0.012	23.341	-0.006	-0.006	0.000	0.000	0.000	0.000
80	A	80	TYR	0	-0.019	-0.010	22.737	0.009	0.009	0.000	0.000	0.000	0.000
81	A	81	ASN	0	0.040	0.020	17.542	-0.022	-0.022	0.000	0.000	0.000	0.000
82	A	82	TYR	0	-0.032	-0.005	17.476	0.039	0.039	0.000	0.000	0.000	0.000
83	A	83	SER	0	0.023	-0.005	13.344	-0.080	-0.080	0.000	0.000	0.000	0.000
84	A	84	ILE	0	-0.026	-0.004	14.286	0.061	0.061	0.000	0.000	0.000	0.000
85	A	85	ILE	0	-0.003	-0.028	13.008	-0.112	-0.112	0.000	0.000	0.000	0.000
86	A	86	GLY	0	0.048	0.026	14.107	0.013	0.013	0.000	0.000	0.000	0.000
87	A	87	GLY	0	0.001	0.009	15.752	0.025	0.025	0.000	0.000	0.000	0.000
88	A	88	GLU	-1	-0.824	-0.893	17.120	-0.276	-0.276	0.000	0.000	0.000	0.000
89	A	89	GLY	0	0.007	0.003	18.090	-0.003	-0.003	0.000	0.000	0.000	0.000
90	A	90	LEU	0	-0.066	-0.028	10.875	-0.045	-0.045	0.000	0.000	0.000	0.000
91	A	91	ASP	-1	-0.851	-0.905	11.580	-0.740	-0.740	0.000	0.000	0.000	0.000
92	A	92	GLU	-1	-0.780	-0.886	11.190	-0.744	-0.744	0.000	0.000	0.000	0.000
93	A	93	SER	0	-0.069	-0.059	8.398	-0.098	-0.098	0.000	0.000	0.000	0.000
94	A	94	LEU	0	-0.037	-0.029	6.675	-0.620	-0.620	0.000	0.000	0.000	0.000
95	A	95	GLU	-1	-0.930	-0.966	5.048	-0.164	-0.164	0.000	0.000	0.000	0.000
96	A	96	LYS	1	0.875	0.933	7.821	0.904	0.904	0.000	0.000	0.000	0.000
97	A	97	ILE	0	-0.037	-0.007	8.679	-0.339	-0.339	0.000	0.000	0.000	0.000
98	A	98	SER	0	-0.014	-0.015	10.739	0.131	0.131	0.000	0.000	0.000	0.000
99	A	99	TYR	0	-0.039	-0.045	12.519	-0.077	-0.077	0.000	0.000	0.000	0.000
100	A	100	GLU	-1	-0.840	-0.905	13.673	-0.137	-0.137	0.000	0.000	0.000	0.000
101	A	101	SER	0	0.007	0.012	17.289	-0.009	-0.009	0.000	0.000	0.000	0.000
102	A	102	LYS	1	0.820	0.901	20.712	0.065	0.065	0.000	0.000	0.000	0.000
103	A	103	ILE	0	-0.039	-0.001	24.012	-0.006	-0.006	0.000	0.000	0.000	0.000
104	A	104	LEU	0	0.014	0.008	25.995	0.011	0.011	0.000	0.000	0.000	0.000
105	A	105	PRO	0	0.038	-0.012	29.173	-0.004	-0.004	0.000	0.000	0.000	0.000
106	A	106	GLY	0	0.011	0.020	31.857	-0.002	-0.002	0.000	0.000	0.000	0.000
107	A	107	PRO	0	-0.015	-0.018	33.829	0.004	0.004	0.000	0.000	0.000	0.000
108	A	108	ASP	-1	-0.913	-0.955	37.143	-0.043	-0.043	0.000	0.000	0.000	0.000
109	A	109	GLY	0	-0.031	-0.003	38.934	-0.001	-0.001	0.000	0.000	0.000	0.000
110	A	110	GLY	0	0.014	0.012	35.678	-0.002	-0.002	0.000	0.000	0.000	0.000
111	A	111	SER	0	-0.058	-0.052	30.872	0.001	0.001	0.000	0.000	0.000	0.000
112	A	112	ILE	0	0.001	-0.011	26.573	-0.003	-0.003	0.000	0.000	0.000	0.000
113	A	113	GLY	0	0.001	0.010	25.732	0.004	0.004	0.000	0.000	0.000	0.000
114	A	114	LYS	1	0.826	0.913	20.813	0.092	0.092	0.000	0.000	0.000	0.000
115	A	115	ILE	0	0.012	-0.008	17.479	0.005	0.005	0.000	0.000	0.000	0.000
116	A	116	ASN	0	-0.036	-0.025	13.201	-0.075	-0.075	0.000	0.000	0.000	0.000
117	A	117	VAL	0	0.001	-0.001	12.531	0.003	0.003	0.000	0.000	0.000	0.000
118	A	118	LYS	1	0.838	0.892	8.684	0.207	0.207	0.000	0.000	0.000	0.000
119	A	119	PHE	0	0.018	0.017	7.503	0.049	0.049	0.000	0.000	0.000	0.000
120	A	120	HIS	0	-0.005	0.000	4.676	-0.443	-0.412	-0.001	-0.038	0.008	0.000
121	A	121	THR	0	0.004	-0.015	2.358	-0.991	0.484	2.136	-1.797	-1.813	-0.008
122	A	122	LYS	1	0.792	0.880	2.139	-5.135	-4.786	3.243	-1.859	-1.733	-0.024
123	A	123	GLY	0	0.037	0.018	3.787	0.781	0.994	0.002	-0.067	-0.147	0.000
124	A	124	ASP	-1	-0.926	-0.955	3.167	-1.848	-0.336	0.261	-0.876	-0.897	-0.006
125	A	125	VAL	0	-0.041	-0.029	4.031	0.404	0.490	0.000	-0.009	-0.077	0.000
126	A	126	LEU	0	-0.025	0.015	5.598	-0.370	-0.370	0.000	0.000	0.000	0.000
127	A	127	SER	0	0.035	0.018	6.681	0.324	0.324	0.000	0.000	0.000	0.000
128	A	128	GLU	-1	-0.798	-0.901	10.156	-0.364	-0.364	0.000	0.000	0.000	0.000
129	A	129	THR	0	-0.025	-0.009	13.278	0.034	0.034	0.000	0.000	0.000	0.000
130	A	130	VAL	0	0.028	0.019	9.765	0.037	0.037	0.000	0.000	0.000	0.000
131	A	131	ARG	1	0.850	0.904	8.435	0.479	0.479	0.000	0.000	0.000	0.000
132	A	132	ASP	-1	-0.827	-0.901	12.401	-0.220	-0.220	0.000	0.000	0.000	0.000
133	A	133	GLN	0	0.027	-0.002	14.918	0.015	0.015	0.000	0.000	0.000	0.000
134	A	134	ALA	0	0.005	0.004	12.703	0.018	0.018	0.000	0.000	0.000	0.000
135	A	135	LYS	1	0.787	0.895	14.625	0.291	0.291	0.000	0.000	0.000	0.000
136	A	136	PHE	0	0.013	0.001	18.313	0.016	0.016	0.000	0.000	0.000	0.000
137	A	137	LYS	1	0.885	0.946	14.255	0.586	0.586	0.000	0.000	0.000	0.000
138	A	138	GLY	0	0.034	0.047	16.373	-0.012	-0.012	0.000	0.000	0.000	0.000
139	A	139	LEU	0	0.008	-0.012	17.061	0.031	0.031	0.000	0.000	0.000	0.000
140	A	140	GLY	0	-0.003	0.006	20.769	0.025	0.025	0.000	0.000	0.000	0.000
141	A	141	LEU	0	0.023	0.011	21.473	0.020	0.020	0.000	0.000	0.000	0.000
142	A	142	PHE	0	0.060	0.019	22.910	0.020	0.020	0.000	0.000	0.000	0.000
143	A	143	LYS	1	0.920	0.948	24.020	0.174	0.174	0.000	0.000	0.000	0.000
144	A	144	ALA	0	0.010	0.028	26.528	0.013	0.013	0.000	0.000	0.000	0.000
145	A	145	ILE	0	0.022	0.007	26.155	0.013	0.013	0.000	0.000	0.000	0.000
146	A	146	GLU	-1	-0.867	-0.905	28.738	-0.092	-0.092	0.000	0.000	0.000	0.000
147	A	147	GLY	0	0.060	0.027	30.493	0.010	0.010	0.000	0.000	0.000	0.000
148	A	148	TYR	0	-0.004	-0.002	32.161	0.010	0.010	0.000	0.000	0.000	0.000
149	A	149	VAL	0	-0.018	-0.023	33.137	0.008	0.008	0.000	0.000	0.000	0.000
150	A	150	LEU	0	-0.032	-0.015	34.548	0.007	0.007	0.000	0.000	0.000	0.000
151	A	151	ALA	0	-0.015	0.000	36.398	0.006	0.006	0.000	0.000	0.000	0.000
152	A	152	HIS	1	0.826	0.917	37.193	0.082	0.082	0.000	0.000	0.000	0.000
153	A	153	PRO	0	0.058	0.031	38.787	-0.001	-0.001	0.000	0.000	0.000	0.000
154	A	154	ASP	-1	-0.984	-0.992	39.850	-0.047	-0.047	0.000	0.000	0.000	0.000
155	A	155	TYR	0	-0.082	-0.054	34.741	0.002	0.002	0.000	0.000	0.000	0.000

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