FMO DATABASE

FMODB ID: 17K1Z

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1396032.683812
FMO2-HF: Nuclear repulsion	1338717.375899
FMO2-HF: Total energy	-57315.307913
FMO2-MP2: Total energy	-57487.716611

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.
-5.87	-6.601	17.529	-8.422	-8.376	-0.046

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 : 0.043 / q_NPA : 0.006

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	-0.059	-0.018	2.535	1.011	2.527	0.586	-0.929	-1.174	-0.001
4	A	4	ALA	0	-0.003	-0.004	6.140	-0.095	-0.095	0.000	0.000	0.000	0.000
5	A	5	PHE	0	-0.045	-0.019	9.065	0.137	0.137	0.000	0.000	0.000	0.000
6	A	6	GLU	-1	-0.917	-0.953	12.938	-0.197	-0.197	0.000	0.000	0.000	0.000
7	A	7	ASN	0	-0.070	-0.040	16.467	0.048	0.048	0.000	0.000	0.000	0.000
8	A	8	GLU	-1	-0.830	-0.912	19.465	-0.126	-0.126	0.000	0.000	0.000	0.000
9	A	9	GLN	0	-0.038	-0.003	23.081	-0.009	-0.009	0.000	0.000	0.000	0.000
10	A	10	SER	0	-0.020	-0.009	26.024	0.002	0.002	0.000	0.000	0.000	0.000
11	A	11	SER	0	0.020	-0.019	29.553	-0.004	-0.004	0.000	0.000	0.000	0.000
12	A	12	THR	0	0.024	0.014	31.919	0.004	0.004	0.000	0.000	0.000	0.000
13	A	13	VAL	0	0.009	0.011	33.283	0.008	0.008	0.000	0.000	0.000	0.000
14	A	14	ALA	0	0.009	0.024	34.258	-0.001	-0.001	0.000	0.000	0.000	0.000
15	A	15	PRO	0	0.033	0.010	31.999	-0.006	-0.006	0.000	0.000	0.000	0.000
16	A	16	ALA	0	0.035	0.011	31.938	-0.007	-0.007	0.000	0.000	0.000	0.000
17	A	17	LYS	1	0.931	0.966	33.503	0.074	0.074	0.000	0.000	0.000	0.000
18	A	18	LEU	0	0.044	0.027	28.879	-0.005	-0.005	0.000	0.000	0.000	0.000
19	A	19	TYR	0	0.038	0.014	26.144	-0.006	-0.006	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.931	1.000	29.089	0.085	0.085	0.000	0.000	0.000	0.000
21	A	21	ALA	0	0.043	0.016	30.845	-0.005	-0.005	0.000	0.000	0.000	0.000
22	A	22	LEU	0	-0.048	-0.021	25.011	-0.010	-0.010	0.000	0.000	0.000	0.000
23	A	23	THR	0	-0.037	-0.036	25.508	-0.011	-0.011	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.885	0.934	27.413	0.091	0.091	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.786	-0.865	30.619	-0.110	-0.110	0.000	0.000	0.000	0.000
26	A	26	SER	0	-0.029	-0.002	26.488	-0.005	-0.005	0.000	0.000	0.000	0.000
27	A	27	ASP	-1	-0.799	-0.895	27.273	-0.180	-0.180	0.000	0.000	0.000	0.000
28	A	28	GLU	-1	-0.915	-0.963	29.136	-0.112	-0.112	0.000	0.000	0.000	0.000
29	A	29	ILE	0	-0.060	-0.022	30.220	0.003	0.003	0.000	0.000	0.000	0.000
30	A	30	VAL	0	0.026	-0.012	25.779	-0.001	-0.001	0.000	0.000	0.000	0.000
31	A	31	PRO	0	-0.020	-0.008	28.875	-0.004	-0.004	0.000	0.000	0.000	0.000
32	A	32	LYS	1	0.905	0.979	31.010	0.122	0.122	0.000	0.000	0.000	0.000
33	A	33	VAL	0	-0.095	-0.040	29.761	0.006	0.006	0.000	0.000	0.000	0.000
34	A	34	ILE	0	-0.072	-0.037	25.097	-0.007	-0.007	0.000	0.000	0.000	0.000
35	A	35	GLU	-1	-0.853	-0.931	29.141	-0.142	-0.142	0.000	0.000	0.000	0.000
36	A	36	PRO	0	0.015	0.008	27.425	0.002	0.002	0.000	0.000	0.000	0.000
37	A	37	ILE	0	-0.076	-0.012	24.723	-0.004	-0.004	0.000	0.000	0.000	0.000
38	A	38	GLN	0	-0.034	-0.023	28.523	0.019	0.019	0.000	0.000	0.000	0.000
39	A	39	SER	0	-0.047	-0.033	29.521	0.008	0.008	0.000	0.000	0.000	0.000
40	A	40	VAL	0	0.010	0.002	25.534	-0.017	-0.017	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.911	-0.956	27.252	-0.131	-0.131	0.000	0.000	0.000	0.000
42	A	42	ILE	0	-0.002	0.004	26.603	-0.016	-0.016	0.000	0.000	0.000	0.000
43	A	43	VAL	0	-0.047	-0.030	24.120	0.011	0.011	0.000	0.000	0.000	0.000
44	A	44	GLU	-1	-0.905	-0.960	23.547	-0.113	-0.113	0.000	0.000	0.000	0.000
45	A	45	GLY	0	0.012	0.018	25.741	-0.011	-0.011	0.000	0.000	0.000	0.000
46	A	46	ASN	0	-0.042	-0.040	27.212	0.000	0.000	0.000	0.000	0.000	0.000
47	A	47	GLY	0	0.019	0.003	27.615	0.006	0.006	0.000	0.000	0.000	0.000
48	A	48	GLY	0	0.012	0.030	26.809	-0.006	-0.006	0.000	0.000	0.000	0.000
49	A	49	PRO	0	-0.010	-0.031	22.183	-0.012	-0.012	0.000	0.000	0.000	0.000
50	A	50	GLY	0	-0.016	-0.002	20.915	0.014	0.014	0.000	0.000	0.000	0.000
51	A	51	THR	0	-0.040	-0.012	21.925	0.000	0.000	0.000	0.000	0.000	0.000
52	A	52	ILE	0	-0.006	0.011	19.927	-0.030	-0.030	0.000	0.000	0.000	0.000
53	A	53	LYS	1	0.824	0.889	21.796	0.209	0.209	0.000	0.000	0.000	0.000
54	A	54	LYS	1	0.957	0.985	22.039	0.149	0.149	0.000	0.000	0.000	0.000
55	A	55	ILE	0	-0.006	0.003	21.396	0.018	0.018	0.000	0.000	0.000	0.000
56	A	56	ILE	0	0.006	0.006	24.203	-0.018	-0.018	0.000	0.000	0.000	0.000
57	A	57	ALA	0	0.027	0.004	25.370	0.006	0.006	0.000	0.000	0.000	0.000
58	A	58	ILE	0	0.005	0.003	27.340	0.002	0.002	0.000	0.000	0.000	0.000
59	A	59	HIS	0	-0.031	0.002	24.692	0.007	0.007	0.000	0.000	0.000	0.000
60	A	60	ASP	-1	-0.908	-0.948	27.507	-0.168	-0.168	0.000	0.000	0.000	0.000
61	A	61	GLY	0	-0.036	-0.018	30.345	-0.002	-0.002	0.000	0.000	0.000	0.000
62	A	62	HIS	0	-0.032	-0.028	29.475	0.009	0.009	0.000	0.000	0.000	0.000
63	A	63	THR	0	-0.007	-0.009	28.737	-0.010	-0.010	0.000	0.000	0.000	0.000
64	A	64	SER	0	-0.016	0.008	23.625	0.000	0.000	0.000	0.000	0.000	0.000
65	A	65	PHE	0	-0.016	-0.031	20.637	0.016	0.016	0.000	0.000	0.000	0.000
66	A	66	VAL	0	0.026	0.024	17.561	-0.024	-0.024	0.000	0.000	0.000	0.000
67	A	67	LEU	0	-0.054	-0.022	17.602	0.038	0.038	0.000	0.000	0.000	0.000
68	A	68	HIS	0	0.036	0.015	17.338	-0.059	-0.059	0.000	0.000	0.000	0.000
69	A	69	LYS	1	0.998	1.014	15.881	0.282	0.282	0.000	0.000	0.000	0.000
70	A	70	LEU	0	-0.019	0.005	18.214	-0.038	-0.038	0.000	0.000	0.000	0.000
71	A	71	ASP	-1	-0.895	-0.960	15.549	-0.366	-0.366	0.000	0.000	0.000	0.000
72	A	72	ALA	0	-0.046	-0.048	18.662	0.037	0.037	0.000	0.000	0.000	0.000
73	A	73	ILE	0	0.016	0.007	21.467	-0.024	-0.024	0.000	0.000	0.000	0.000
74	A	74	ASP	-1	-0.848	-0.906	24.519	-0.065	-0.065	0.000	0.000	0.000	0.000
75	A	75	GLU	-1	-0.866	-0.952	27.104	-0.103	-0.103	0.000	0.000	0.000	0.000
76	A	76	ALA	0	-0.041	0.001	29.861	0.002	0.002	0.000	0.000	0.000	0.000
77	A	77	ASN	0	-0.109	-0.063	27.424	0.008	0.008	0.000	0.000	0.000	0.000
78	A	78	LEU	0	-0.049	-0.022	27.691	-0.007	-0.007	0.000	0.000	0.000	0.000
79	A	79	THR	0	-0.022	-0.023	22.903	-0.012	-0.012	0.000	0.000	0.000	0.000
80	A	80	TYR	0	0.003	-0.016	22.420	0.010	0.010	0.000	0.000	0.000	0.000
81	A	81	ASN	0	0.073	0.043	17.115	-0.025	-0.025	0.000	0.000	0.000	0.000
82	A	82	TYR	0	0.010	0.016	17.338	0.046	0.046	0.000	0.000	0.000	0.000
83	A	83	SER	0	0.011	-0.003	12.949	-0.104	-0.104	0.000	0.000	0.000	0.000
84	A	84	ILE	0	-0.053	-0.020	13.612	0.085	0.085	0.000	0.000	0.000	0.000
85	A	85	ILE	0	-0.001	-0.032	12.626	-0.135	-0.135	0.000	0.000	0.000	0.000
86	A	86	GLY	0	0.035	0.021	13.885	0.011	0.011	0.000	0.000	0.000	0.000
87	A	87	GLY	0	0.002	0.011	15.559	0.017	0.017	0.000	0.000	0.000	0.000
88	A	88	GLU	-1	-0.874	-0.943	16.732	-0.331	-0.331	0.000	0.000	0.000	0.000
89	A	89	GLY	0	-0.004	0.002	17.754	0.002	0.002	0.000	0.000	0.000	0.000
90	A	90	LEU	0	-0.083	-0.033	10.940	-0.054	-0.054	0.000	0.000	0.000	0.000
91	A	91	ASP	-1	-0.880	-0.937	11.011	-0.908	-0.908	0.000	0.000	0.000	0.000
92	A	92	GLU	-1	-0.838	-0.914	11.302	-0.684	-0.684	0.000	0.000	0.000	0.000
93	A	93	SER	0	-0.095	-0.060	8.004	-0.138	-0.138	0.000	0.000	0.000	0.000
94	A	94	LEU	0	-0.045	-0.030	6.488	-0.714	-0.714	0.000	0.000	0.000	0.000
95	A	95	GLU	-1	-0.940	-0.976	5.144	-0.498	-0.429	-0.001	-0.002	-0.065	0.000
96	A	96	LYS	1	0.931	0.963	7.452	1.203	1.203	0.000	0.000	0.000	0.000
97	A	97	ILE	0	-0.038	-0.003	8.179	-0.423	-0.423	0.000	0.000	0.000	0.000
98	A	98	SER	0	-0.026	-0.011	10.477	0.140	0.140	0.000	0.000	0.000	0.000
99	A	99	TYR	0	-0.054	-0.035	12.258	-0.090	-0.090	0.000	0.000	0.000	0.000
100	A	100	GLU	-1	-0.872	-0.934	14.345	-0.278	-0.278	0.000	0.000	0.000	0.000
101	A	101	SER	0	-0.002	-0.005	17.394	-0.006	-0.006	0.000	0.000	0.000	0.000
102	A	102	LYS	1	0.948	0.981	20.816	0.118	0.118	0.000	0.000	0.000	0.000
103	A	103	ILE	0	-0.063	-0.007	23.840	-0.005	-0.005	0.000	0.000	0.000	0.000
104	A	104	LEU	0	0.007	-0.013	26.126	0.013	0.013	0.000	0.000	0.000	0.000
105	A	105	PRO	0	0.020	-0.013	29.100	-0.004	-0.004	0.000	0.000	0.000	0.000
106	A	106	GLY	0	0.024	0.029	32.183	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	107	PRO	0	-0.028	-0.030	33.542	0.004	0.004	0.000	0.000	0.000	0.000
108	A	108	ASP	-1	-0.898	-0.946	36.918	-0.064	-0.064	0.000	0.000	0.000	0.000
109	A	109	GLY	0	-0.064	-0.026	38.472	-0.001	-0.001	0.000	0.000	0.000	0.000
110	A	110	GLY	0	0.047	0.037	35.508	-0.003	-0.003	0.000	0.000	0.000	0.000
111	A	111	SER	0	-0.069	-0.081	30.745	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	112	ILE	0	-0.005	-0.003	26.166	-0.001	-0.001	0.000	0.000	0.000	0.000
113	A	113	GLY	0	0.010	0.014	25.457	0.002	0.002	0.000	0.000	0.000	0.000
114	A	114	LYS	1	0.830	0.912	21.549	0.123	0.123	0.000	0.000	0.000	0.000
115	A	115	ILE	0	0.009	-0.007	17.480	0.000	0.000	0.000	0.000	0.000	0.000
116	A	116	ASN	0	0.022	0.010	13.776	-0.062	-0.062	0.000	0.000	0.000	0.000
117	A	117	VAL	0	0.001	0.003	11.978	-0.008	-0.008	0.000	0.000	0.000	0.000
118	A	118	LYS	1	0.871	0.920	8.602	0.449	0.449	0.000	0.000	0.000	0.000
119	A	119	PHE	0	0.003	0.005	7.285	0.132	0.132	0.000	0.000	0.000	0.000
120	A	120	HIS	0	0.005	0.009	4.044	-0.734	-0.681	-0.001	-0.051	-0.001	0.000
121	A	121	THR	0	-0.029	-0.021	2.057	1.607	2.101	4.431	-2.326	-2.598	0.004
122	A	122	LYS	1	0.907	0.945	2.144	-3.580	-3.720	4.129	-2.178	-1.812	-0.023
123	A	123	GLY	0	0.024	0.023	4.013	0.966	1.246	0.000	-0.101	-0.179	0.000
124	A	124	ASP	-1	-0.897	-0.941	1.881	-3.705	-6.852	8.386	-2.826	-2.413	-0.026
125	A	125	VAL	0	-0.029	-0.020	3.881	0.406	0.550	-0.001	-0.009	-0.134	0.000
126	A	126	LEU	0	-0.038	0.006	5.917	-0.555	-0.555	0.000	0.000	0.000	0.000
127	A	127	SER	0	0.043	0.006	6.915	0.306	0.306	0.000	0.000	0.000	0.000
128	A	128	GLU	-1	-0.825	-0.919	10.398	-0.384	-0.384	0.000	0.000	0.000	0.000
129	A	129	THR	0	0.005	0.012	13.418	0.027	0.027	0.000	0.000	0.000	0.000
130	A	130	VAL	0	0.022	0.005	9.994	0.052	0.052	0.000	0.000	0.000	0.000
131	A	131	ARG	1	0.970	0.979	8.301	0.523	0.523	0.000	0.000	0.000	0.000
132	A	132	ASP	-1	-0.917	-0.952	12.391	-0.281	-0.281	0.000	0.000	0.000	0.000
133	A	133	GLN	0	-0.073	-0.074	14.872	-0.004	-0.004	0.000	0.000	0.000	0.000
134	A	134	ALA	0	0.009	0.011	12.686	-0.006	-0.006	0.000	0.000	0.000	0.000
135	A	135	LYS	1	0.873	0.954	14.501	0.369	0.369	0.000	0.000	0.000	0.000
136	A	136	PHE	0	0.019	-0.006	18.235	0.005	0.005	0.000	0.000	0.000	0.000
137	A	137	LYS	1	0.927	0.980	12.870	0.810	0.810	0.000	0.000	0.000	0.000
138	A	138	GLY	0	0.040	0.033	16.409	-0.004	-0.004	0.000	0.000	0.000	0.000
139	A	139	LEU	0	-0.007	-0.013	17.215	0.020	0.020	0.000	0.000	0.000	0.000
140	A	140	GLY	0	0.007	0.013	20.508	0.032	0.032	0.000	0.000	0.000	0.000
141	A	141	LEU	0	0.032	0.021	21.266	0.025	0.025	0.000	0.000	0.000	0.000
142	A	142	PHE	0	0.053	0.007	22.555	0.025	0.025	0.000	0.000	0.000	0.000
143	A	143	LYS	1	0.950	0.969	24.294	0.239	0.239	0.000	0.000	0.000	0.000
144	A	144	ALA	0	-0.005	0.026	26.200	0.019	0.019	0.000	0.000	0.000	0.000
145	A	145	ILE	0	0.036	0.005	25.711	0.016	0.016	0.000	0.000	0.000	0.000
146	A	146	GLU	-1	-0.831	-0.886	28.572	-0.123	-0.123	0.000	0.000	0.000	0.000
147	A	147	GLY	0	0.069	0.035	30.426	0.013	0.013	0.000	0.000	0.000	0.000
148	A	148	TYR	0	-0.001	0.002	31.980	0.013	0.013	0.000	0.000	0.000	0.000
149	A	149	VAL	0	0.003	-0.016	32.496	0.010	0.010	0.000	0.000	0.000	0.000
150	A	150	LEU	0	-0.047	-0.012	34.395	0.009	0.009	0.000	0.000	0.000	0.000
151	A	151	ALA	0	-0.038	-0.030	36.198	0.008	0.008	0.000	0.000	0.000	0.000
152	A	152	HIS	1	0.800	0.910	37.153	0.109	0.109	0.000	0.000	0.000	0.000
153	A	153	PRO	0	0.040	0.021	38.504	-0.002	-0.002	0.000	0.000	0.000	0.000
154	A	154	ASP	-1	-0.998	-1.016	39.566	-0.072	-0.072	0.000	0.000	0.000	0.000
155	A	155	TYR	0	-0.090	-0.049	34.459	-0.001	-0.001	0.000	0.000	0.000	0.000

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