FMO DATABASE

FMODB ID: G6G31

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1396766.599506
FMO2-HF: Nuclear repulsion	1339450.129515
FMO2-HF: Total energy	-57316.469991
FMO2-MP2: Total energy	-57488.794437

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.
-8.007	-7.401	16.216	-8.571	-8.252	-0.038

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 : 0.037 / q_NPA : 0.004

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	-0.039	-0.008	2.767	1.018	2.486	0.251	-0.713	-1.006	-0.001
4	A	4	ALA	0	-0.002	0.000	6.132	-0.073	-0.073	0.000	0.000	0.000	0.000
5	A	5	PHE	0	-0.038	-0.018	9.122	0.144	0.144	0.000	0.000	0.000	0.000
6	A	6	GLU	-1	-0.893	-0.936	12.929	-0.204	-0.204	0.000	0.000	0.000	0.000
7	A	7	ASN	0	-0.068	-0.037	16.459	0.036	0.036	0.000	0.000	0.000	0.000
8	A	8	GLU	-1	-0.848	-0.925	19.456	-0.121	-0.121	0.000	0.000	0.000	0.000
9	A	9	GLN	0	-0.022	-0.005	23.072	-0.007	-0.007	0.000	0.000	0.000	0.000
10	A	10	SER	0	0.018	0.015	26.015	0.003	0.003	0.000	0.000	0.000	0.000
11	A	11	SER	0	-0.022	-0.046	29.544	-0.004	-0.004	0.000	0.000	0.000	0.000
12	A	12	THR	0	0.040	0.017	31.909	0.005	0.005	0.000	0.000	0.000	0.000
13	A	13	VAL	0	-0.003	0.012	33.318	0.007	0.007	0.000	0.000	0.000	0.000
14	A	14	ALA	0	0.028	0.026	34.258	-0.001	-0.001	0.000	0.000	0.000	0.000
15	A	15	PRO	0	0.026	0.004	31.900	-0.005	-0.005	0.000	0.000	0.000	0.000
16	A	16	ALA	0	0.032	0.011	31.938	-0.007	-0.007	0.000	0.000	0.000	0.000
17	A	17	LYS	1	0.940	0.971	33.511	0.070	0.070	0.000	0.000	0.000	0.000
18	A	18	LEU	0	0.031	0.023	28.925	-0.005	-0.005	0.000	0.000	0.000	0.000
19	A	19	TYR	0	0.033	-0.008	25.962	-0.006	-0.006	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.805	0.905	29.096	0.089	0.089	0.000	0.000	0.000	0.000
21	A	21	ALA	0	0.024	0.010	30.851	-0.004	-0.004	0.000	0.000	0.000	0.000
22	A	22	LEU	0	-0.034	-0.017	25.045	-0.009	-0.009	0.000	0.000	0.000	0.000
23	A	23	THR	0	-0.022	-0.014	25.381	-0.011	-0.011	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.915	0.958	27.418	0.086	0.086	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.739	-0.823	30.622	-0.102	-0.102	0.000	0.000	0.000	0.000
26	A	26	SER	0	0.007	0.010	26.481	-0.004	-0.004	0.000	0.000	0.000	0.000
27	A	27	ASP	-1	-0.789	-0.884	27.230	-0.170	-0.170	0.000	0.000	0.000	0.000
28	A	28	GLU	-1	-0.864	-0.931	29.140	-0.105	-0.105	0.000	0.000	0.000	0.000
29	A	29	ILE	0	-0.042	-0.017	30.461	0.004	0.004	0.000	0.000	0.000	0.000
30	A	30	VAL	0	0.025	-0.010	25.696	-0.001	-0.001	0.000	0.000	0.000	0.000
31	A	31	PRO	0	-0.017	-0.004	28.885	-0.003	-0.003	0.000	0.000	0.000	0.000
32	A	32	LYS	1	0.822	0.932	31.019	0.116	0.116	0.000	0.000	0.000	0.000
33	A	33	VAL	0	-0.085	-0.036	29.866	0.005	0.005	0.000	0.000	0.000	0.000
34	A	34	ILE	0	-0.073	-0.040	25.045	-0.006	-0.006	0.000	0.000	0.000	0.000
35	A	35	GLU	-1	-0.866	-0.937	29.155	-0.131	-0.131	0.000	0.000	0.000	0.000
36	A	36	PRO	0	0.016	0.010	27.417	0.002	0.002	0.000	0.000	0.000	0.000
37	A	37	ILE	0	-0.064	-0.024	24.525	-0.004	-0.004	0.000	0.000	0.000	0.000
38	A	38	GLN	0	-0.027	-0.003	28.531	0.017	0.017	0.000	0.000	0.000	0.000
39	A	39	SER	0	-0.047	-0.041	29.528	0.008	0.008	0.000	0.000	0.000	0.000
40	A	40	VAL	0	0.015	0.001	25.537	-0.015	-0.015	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.862	-0.929	27.227	-0.131	-0.131	0.000	0.000	0.000	0.000
42	A	42	ILE	0	-0.003	-0.001	26.599	-0.015	-0.015	0.000	0.000	0.000	0.000
43	A	43	VAL	0	-0.044	-0.030	24.191	0.011	0.011	0.000	0.000	0.000	0.000
44	A	44	GLU	-1	-0.901	-0.954	23.328	-0.114	-0.114	0.000	0.000	0.000	0.000
45	A	45	GLY	0	0.020	0.018	25.731	-0.010	-0.010	0.000	0.000	0.000	0.000
46	A	46	ASN	0	-0.054	-0.051	27.201	0.004	0.004	0.000	0.000	0.000	0.000
47	A	47	GLY	0	0.031	0.007	27.614	0.007	0.007	0.000	0.000	0.000	0.000
48	A	48	GLY	0	0.018	0.041	26.802	-0.005	-0.005	0.000	0.000	0.000	0.000
49	A	49	PRO	0	0.003	-0.010	22.146	-0.012	-0.012	0.000	0.000	0.000	0.000
50	A	50	GLY	0	-0.016	-0.004	20.906	0.013	0.013	0.000	0.000	0.000	0.000
51	A	51	THR	0	-0.067	-0.037	21.913	0.000	0.000	0.000	0.000	0.000	0.000
52	A	52	ILE	0	0.002	0.012	19.803	-0.030	-0.030	0.000	0.000	0.000	0.000
53	A	53	LYS	1	0.802	0.878	21.791	0.197	0.197	0.000	0.000	0.000	0.000
54	A	54	LYS	1	0.896	0.962	22.036	0.136	0.136	0.000	0.000	0.000	0.000
55	A	55	ILE	0	-0.003	0.004	21.365	0.018	0.018	0.000	0.000	0.000	0.000
56	A	56	ILE	0	-0.002	0.006	24.206	-0.017	-0.017	0.000	0.000	0.000	0.000
57	A	57	ALA	0	0.030	0.004	25.352	0.006	0.006	0.000	0.000	0.000	0.000
58	A	58	ILE	0	0.016	0.011	27.347	0.001	0.001	0.000	0.000	0.000	0.000
59	A	59	HIS	0	-0.028	0.003	25.200	0.001	0.001	0.000	0.000	0.000	0.000
60	A	60	ASP	-1	-0.922	-0.959	27.518	-0.155	-0.155	0.000	0.000	0.000	0.000
61	A	61	GLY	0	-0.031	-0.013	30.354	-0.002	-0.002	0.000	0.000	0.000	0.000
62	A	62	HIS	0	-0.030	-0.026	29.419	0.009	0.009	0.000	0.000	0.000	0.000
63	A	63	THR	0	-0.015	-0.010	28.743	-0.006	-0.006	0.000	0.000	0.000	0.000
64	A	64	SER	0	-0.065	-0.033	23.690	0.002	0.002	0.000	0.000	0.000	0.000
65	A	65	PHE	0	-0.016	-0.028	21.046	0.013	0.013	0.000	0.000	0.000	0.000
66	A	66	VAL	0	0.011	0.021	17.564	-0.024	-0.024	0.000	0.000	0.000	0.000
67	A	67	LEU	0	-0.039	-0.016	17.608	0.036	0.036	0.000	0.000	0.000	0.000
68	A	68	HIS	0	0.024	0.012	17.337	-0.054	-0.054	0.000	0.000	0.000	0.000
69	A	69	LYS	1	0.941	0.975	16.056	0.288	0.288	0.000	0.000	0.000	0.000
70	A	70	LEU	0	-0.009	0.002	18.211	-0.035	-0.035	0.000	0.000	0.000	0.000
71	A	71	ASP	-1	-0.862	-0.919	15.593	-0.346	-0.346	0.000	0.000	0.000	0.000
72	A	72	ALA	0	-0.028	-0.029	18.655	0.034	0.034	0.000	0.000	0.000	0.000
73	A	73	ILE	0	0.010	0.003	21.462	-0.022	-0.022	0.000	0.000	0.000	0.000
74	A	74	ASP	-1	-0.807	-0.896	24.517	-0.064	-0.064	0.000	0.000	0.000	0.000
75	A	75	GLU	-1	-0.871	-0.952	27.103	-0.099	-0.099	0.000	0.000	0.000	0.000
76	A	76	ALA	0	-0.039	0.004	29.862	0.002	0.002	0.000	0.000	0.000	0.000
77	A	77	ASN	0	-0.131	-0.073	27.284	0.006	0.006	0.000	0.000	0.000	0.000
78	A	78	LEU	0	-0.037	-0.016	27.691	-0.006	-0.006	0.000	0.000	0.000	0.000
79	A	79	THR	0	-0.003	-0.015	22.888	-0.012	-0.012	0.000	0.000	0.000	0.000
80	A	80	TYR	0	0.012	0.002	22.356	0.012	0.012	0.000	0.000	0.000	0.000
81	A	81	ASN	0	0.038	0.020	17.182	-0.020	-0.020	0.000	0.000	0.000	0.000
82	A	82	TYR	0	0.016	0.022	17.361	0.050	0.050	0.000	0.000	0.000	0.000
83	A	83	SER	0	0.016	-0.003	12.939	-0.099	-0.099	0.000	0.000	0.000	0.000
84	A	84	ILE	0	-0.047	-0.018	13.619	0.080	0.080	0.000	0.000	0.000	0.000
85	A	85	ILE	0	0.007	-0.032	12.627	-0.128	-0.128	0.000	0.000	0.000	0.000
86	A	86	GLY	0	0.042	0.025	13.881	0.010	0.010	0.000	0.000	0.000	0.000
87	A	87	GLY	0	0.006	0.012	15.556	0.017	0.017	0.000	0.000	0.000	0.000
88	A	88	GLU	-1	-0.818	-0.906	16.735	-0.307	-0.307	0.000	0.000	0.000	0.000
89	A	89	GLY	0	-0.004	0.002	17.765	0.001	0.001	0.000	0.000	0.000	0.000
90	A	90	LEU	0	-0.084	-0.032	10.646	-0.050	-0.050	0.000	0.000	0.000	0.000
91	A	91	ASP	-1	-0.881	-0.931	11.057	-0.832	-0.832	0.000	0.000	0.000	0.000
92	A	92	GLU	-1	-0.797	-0.902	11.310	-0.670	-0.670	0.000	0.000	0.000	0.000
93	A	93	SER	0	-0.087	-0.065	7.993	-0.095	-0.095	0.000	0.000	0.000	0.000
94	A	94	LEU	0	-0.060	-0.034	6.495	-0.656	-0.656	0.000	0.000	0.000	0.000
95	A	95	GLU	-1	-0.929	-0.967	5.021	-0.407	-0.407	0.000	0.000	0.000	0.000
96	A	96	LYS	1	0.888	0.938	7.454	1.320	1.320	0.000	0.000	0.000	0.000
97	A	97	ILE	0	-0.041	-0.006	8.184	-0.400	-0.400	0.000	0.000	0.000	0.000
98	A	98	SER	0	-0.028	-0.024	10.491	0.136	0.136	0.000	0.000	0.000	0.000
99	A	99	TYR	0	-0.054	-0.047	12.264	-0.083	-0.083	0.000	0.000	0.000	0.000
100	A	100	GLU	-1	-0.831	-0.900	13.952	-0.305	-0.305	0.000	0.000	0.000	0.000
101	A	101	SER	0	-0.011	-0.009	17.394	0.000	0.000	0.000	0.000	0.000	0.000
102	A	102	LYS	1	0.933	0.973	20.816	0.112	0.112	0.000	0.000	0.000	0.000
103	A	103	ILE	0	-0.076	-0.016	23.840	-0.005	-0.005	0.000	0.000	0.000	0.000
104	A	104	LEU	0	0.005	-0.003	25.893	0.012	0.012	0.000	0.000	0.000	0.000
105	A	105	PRO	0	0.028	-0.011	29.100	-0.003	-0.003	0.000	0.000	0.000	0.000
106	A	106	GLY	0	0.014	0.022	32.183	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	107	PRO	0	-0.026	-0.027	33.534	0.004	0.004	0.000	0.000	0.000	0.000
108	A	108	ASP	-1	-0.906	-0.954	36.910	-0.059	-0.059	0.000	0.000	0.000	0.000
109	A	109	GLY	0	-0.057	-0.021	38.473	-0.001	-0.001	0.000	0.000	0.000	0.000
110	A	110	GLY	0	0.046	0.040	35.500	-0.003	-0.003	0.000	0.000	0.000	0.000
111	A	111	SER	0	-0.073	-0.070	30.821	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	112	ILE	0	0.001	-0.006	26.310	-0.001	-0.001	0.000	0.000	0.000	0.000
113	A	113	GLY	0	0.018	0.024	25.454	0.002	0.002	0.000	0.000	0.000	0.000
114	A	114	LYS	1	0.859	0.927	21.558	0.127	0.127	0.000	0.000	0.000	0.000
115	A	115	ILE	0	0.009	-0.011	17.568	0.000	0.000	0.000	0.000	0.000	0.000
116	A	116	ASN	0	-0.031	-0.020	13.391	-0.090	-0.090	0.000	0.000	0.000	0.000
117	A	117	VAL	0	0.007	0.003	12.233	-0.007	-0.007	0.000	0.000	0.000	0.000
118	A	118	LYS	1	0.838	0.889	8.631	0.398	0.398	0.000	0.000	0.000	0.000
119	A	119	PHE	0	-0.001	0.004	7.277	0.103	0.103	0.000	0.000	0.000	0.000
120	A	120	HIS	0	0.015	0.015	4.049	-0.555	-0.514	-0.001	-0.049	0.010	0.000
121	A	121	THR	0	-0.010	-0.001	2.131	-0.536	0.967	3.783	-2.648	-2.638	0.015
122	A	122	LYS	1	0.871	0.926	2.138	-3.814	-3.970	4.204	-2.212	-1.836	-0.024
123	A	123	GLY	0	0.027	0.025	4.020	0.838	1.100	0.000	-0.094	-0.169	0.000
124	A	124	ASP	-1	-0.917	-0.958	1.900	-3.773	-6.428	7.980	-2.844	-2.481	-0.028
125	A	125	VAL	0	-0.037	-0.026	3.889	0.404	0.547	-0.001	-0.011	-0.132	0.000
126	A	126	LEU	0	-0.017	0.016	5.912	-0.498	-0.498	0.000	0.000	0.000	0.000
127	A	127	SER	0	0.048	0.014	6.908	0.283	0.283	0.000	0.000	0.000	0.000
128	A	128	GLU	-1	-0.770	-0.880	10.391	-0.358	-0.358	0.000	0.000	0.000	0.000
129	A	129	THR	0	-0.019	-0.007	13.411	0.022	0.022	0.000	0.000	0.000	0.000
130	A	130	VAL	0	0.019	0.012	9.801	0.040	0.040	0.000	0.000	0.000	0.000
131	A	131	ARG	1	0.900	0.924	8.414	0.452	0.452	0.000	0.000	0.000	0.000
132	A	132	ASP	-1	-0.830	-0.902	12.382	-0.228	-0.228	0.000	0.000	0.000	0.000
133	A	133	GLN	0	-0.045	-0.047	14.861	-0.002	-0.002	0.000	0.000	0.000	0.000
134	A	134	ALA	0	-0.005	0.003	12.684	-0.008	-0.008	0.000	0.000	0.000	0.000
135	A	135	LYS	1	0.790	0.906	14.490	0.320	0.320	0.000	0.000	0.000	0.000
136	A	136	PHE	0	0.024	-0.001	18.223	0.002	0.002	0.000	0.000	0.000	0.000
137	A	137	LYS	1	0.934	0.980	13.394	0.702	0.702	0.000	0.000	0.000	0.000
138	A	138	GLY	0	0.043	0.048	16.397	-0.006	-0.006	0.000	0.000	0.000	0.000
139	A	139	LEU	0	-0.011	-0.017	17.203	0.020	0.020	0.000	0.000	0.000	0.000
140	A	140	GLY	0	0.014	0.016	20.534	0.030	0.030	0.000	0.000	0.000	0.000
141	A	141	LEU	0	0.035	0.022	21.284	0.025	0.025	0.000	0.000	0.000	0.000
142	A	142	PHE	0	0.049	0.005	22.569	0.025	0.025	0.000	0.000	0.000	0.000
143	A	143	LYS	1	0.924	0.954	24.054	0.210	0.210	0.000	0.000	0.000	0.000
144	A	144	ALA	0	-0.011	0.022	26.217	0.018	0.018	0.000	0.000	0.000	0.000
145	A	145	ILE	0	0.031	0.007	25.758	0.015	0.015	0.000	0.000	0.000	0.000
146	A	146	GLU	-1	-0.832	-0.881	28.587	-0.115	-0.115	0.000	0.000	0.000	0.000
147	A	147	GLY	0	0.061	0.032	30.443	0.012	0.012	0.000	0.000	0.000	0.000
148	A	148	TYR	0	-0.002	-0.004	31.996	0.012	0.012	0.000	0.000	0.000	0.000
149	A	149	VAL	0	-0.010	-0.019	32.319	0.009	0.009	0.000	0.000	0.000	0.000
150	A	150	LEU	0	-0.049	-0.014	34.413	0.009	0.009	0.000	0.000	0.000	0.000
151	A	151	ALA	0	-0.031	-0.018	36.214	0.007	0.007	0.000	0.000	0.000	0.000
152	A	152	HIS	1	0.811	0.910	36.838	0.102	0.102	0.000	0.000	0.000	0.000
153	A	153	PRO	0	0.046	0.025	38.517	-0.002	-0.002	0.000	0.000	0.000	0.000
154	A	154	ASP	-1	-0.996	-1.004	39.579	-0.067	-0.067	0.000	0.000	0.000	0.000
155	A	155	TYR	0	-0.088	-0.060	34.426	0.000	0.000	0.000	0.000	0.000	0.000

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