FMO DATABASE

FMODB ID: R5QR8

Calculation Name: 1IQV-A-Xray372

Preferred Name:
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Target Type:
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Ligand Name:
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ligand 3-letter code:
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PDB ID: 1IQV

Chain ID: A

ChEMBL ID:
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UniProt ID: O59230

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	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	166
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1693446.157436
FMO2-HF: Nuclear repulsion	1627971.499302
FMO2-HF: Total energy	-65474.658134
FMO2-MP2: Total energy	-65666.721014

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:18:ILE)

Summations of interaction energy for fragment #1(A:18: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.
-7.636	-5.624	8.272	-4.978	-5.306	-0.003

Interaction energy analysis for fragmet #1(A:18:ILE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.027 / q_NPA : -0.012

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	20	VAL	0	0.032	0.007	3.697	1.047	2.614	-0.013	-0.646	-0.908	0.004
4	A	21	MET	0	-0.048	-0.019	6.000	-0.090	-0.090	0.000	0.000	0.000	0.000
5	A	22	GLY	0	0.026	0.020	5.978	-0.293	-0.293	0.000	0.000	0.000	0.000
6	A	23	ARG	1	0.787	0.873	7.013	-0.404	-0.404	0.000	0.000	0.000	0.000
7	A	24	TRP	0	-0.007	-0.021	8.175	-0.092	-0.092	0.000	0.000	0.000	0.000
8	A	25	SER	0	0.019	-0.012	6.218	-0.302	-0.302	0.000	0.000	0.000	0.000
9	A	26	THR	0	-0.037	-0.052	6.315	0.269	0.269	0.000	0.000	0.000	0.000
10	A	27	GLU	-1	-0.847	-0.878	6.970	-1.600	-1.600	0.000	0.000	0.000	0.000
11	A	28	ASP	-1	-0.865	-0.910	8.874	-0.622	-0.622	0.000	0.000	0.000	0.000
12	A	29	VAL	0	-0.132	-0.064	11.319	0.138	0.138	0.000	0.000	0.000	0.000
13	A	30	GLU	-1	-0.797	-0.894	13.080	-0.339	-0.339	0.000	0.000	0.000	0.000
14	A	31	VAL	0	-0.048	-0.022	15.000	0.037	0.037	0.000	0.000	0.000	0.000
15	A	32	LYS	1	0.832	0.893	17.675	0.262	0.262	0.000	0.000	0.000	0.000
16	A	33	ASP	-1	-0.753	-0.832	21.247	-0.111	-0.111	0.000	0.000	0.000	0.000
17	A	34	PRO	0	0.034	-0.003	21.592	-0.012	-0.012	0.000	0.000	0.000	0.000
18	A	35	SER	0	-0.061	-0.054	22.709	0.000	0.000	0.000	0.000	0.000	0.000
19	A	36	LEU	0	-0.029	-0.035	19.870	0.011	0.011	0.000	0.000	0.000	0.000
20	A	37	LYS	1	0.910	0.963	16.554	0.333	0.333	0.000	0.000	0.000	0.000
21	A	38	PRO	0	0.003	0.006	16.546	-0.033	-0.033	0.000	0.000	0.000	0.000
22	A	39	TYR	0	-0.022	-0.019	17.180	0.003	0.003	0.000	0.000	0.000	0.000
23	A	40	ILE	0	-0.038	-0.013	13.348	0.037	0.037	0.000	0.000	0.000	0.000
24	A	41	ASN	0	-0.009	-0.011	8.840	-0.121	-0.121	0.000	0.000	0.000	0.000
25	A	42	LEU	0	-0.013	-0.016	8.723	0.078	0.078	0.000	0.000	0.000	0.000
26	A	43	GLU	-1	-0.818	-0.899	6.115	-1.491	-1.491	0.000	0.000	0.000	0.000
27	A	44	PRO	0	-0.040	-0.005	1.854	-0.040	-0.770	8.022	-4.181	-3.111	-0.008
28	A	45	ARG	1	0.983	0.984	2.670	-3.620	-2.445	0.263	-0.151	-1.287	0.001
29	A	64	VAL	0	-0.012	-0.006	12.937	0.020	0.020	0.000	0.000	0.000	0.000
30	A	65	HIS	1	0.943	0.987	7.196	0.131	0.131	0.000	0.000	0.000	0.000
31	A	66	ILE	0	0.074	0.028	10.549	0.104	0.104	0.000	0.000	0.000	0.000
32	A	67	VAL	0	0.056	0.039	9.473	0.045	0.045	0.000	0.000	0.000	0.000
33	A	68	GLU	-1	-0.904	-0.957	8.644	0.591	0.591	0.000	0.000	0.000	0.000
34	A	69	ARG	1	0.876	0.935	11.777	-0.024	-0.024	0.000	0.000	0.000	0.000
35	A	70	LEU	0	0.029	0.019	14.605	0.004	0.004	0.000	0.000	0.000	0.000
36	A	71	ILE	0	0.024	0.009	11.815	0.011	0.011	0.000	0.000	0.000	0.000
37	A	72	ASN	0	-0.017	-0.019	15.063	0.020	0.020	0.000	0.000	0.000	0.000
38	A	73	LYS	1	0.800	0.893	17.774	-0.094	-0.094	0.000	0.000	0.000	0.000
39	A	74	VAL	0	0.013	0.013	18.808	-0.010	-0.010	0.000	0.000	0.000	0.000
40	A	75	MET	0	-0.060	-0.032	17.519	-0.003	-0.003	0.000	0.000	0.000	0.000
41	A	76	ARG	1	0.849	0.929	21.024	-0.134	-0.134	0.000	0.000	0.000	0.000
42	A	77	SER	0	-0.013	0.003	23.852	-0.021	-0.021	0.000	0.000	0.000	0.000
43	A	78	GLY	0	0.024	0.004	25.126	-0.008	-0.008	0.000	0.000	0.000	0.000
44	A	79	GLY	0	0.032	0.031	25.210	0.013	0.013	0.000	0.000	0.000	0.000
45	A	80	SER	0	-0.045	-0.020	27.031	0.012	0.012	0.000	0.000	0.000	0.000
46	A	98	SER	0	0.116	0.057	20.287	-0.004	-0.004	0.000	0.000	0.000	0.000
47	A	99	LYS	1	0.986	0.965	21.417	-0.176	-0.176	0.000	0.000	0.000	0.000
48	A	100	LYS	1	1.011	1.003	12.954	-0.572	-0.572	0.000	0.000	0.000	0.000
49	A	101	VAL	0	0.049	0.024	16.571	0.028	0.028	0.000	0.000	0.000	0.000
50	A	102	ARG	1	0.981	1.001	17.649	-0.216	-0.216	0.000	0.000	0.000	0.000
51	A	103	ALA	0	0.019	0.011	17.906	-0.010	-0.010	0.000	0.000	0.000	0.000
52	A	104	TYR	0	-0.015	-0.011	9.960	0.048	0.048	0.000	0.000	0.000	0.000
53	A	105	GLU	-1	-0.842	-0.948	15.105	0.543	0.543	0.000	0.000	0.000	0.000
54	A	106	VAL	0	-0.033	-0.001	17.300	-0.031	-0.031	0.000	0.000	0.000	0.000
55	A	107	VAL	0	0.010	-0.003	13.965	-0.030	-0.030	0.000	0.000	0.000	0.000
56	A	108	LYS	1	0.890	0.949	11.036	-0.788	-0.788	0.000	0.000	0.000	0.000
57	A	109	GLU	-1	-0.819	-0.901	15.011	0.169	0.169	0.000	0.000	0.000	0.000
58	A	110	ALA	0	0.026	0.010	18.337	-0.035	-0.035	0.000	0.000	0.000	0.000
59	A	111	PHE	0	-0.002	-0.013	11.507	-0.039	-0.039	0.000	0.000	0.000	0.000
60	A	112	LYS	1	0.870	0.926	16.157	-0.315	-0.315	0.000	0.000	0.000	0.000
61	A	113	ILE	0	-0.009	0.001	17.883	-0.034	-0.034	0.000	0.000	0.000	0.000
62	A	114	ILE	0	0.004	0.000	18.216	-0.019	-0.019	0.000	0.000	0.000	0.000
63	A	115	GLU	-1	-0.814	-0.865	15.015	-0.061	-0.061	0.000	0.000	0.000	0.000
64	A	116	LYS	1	0.913	0.961	19.198	-0.033	-0.033	0.000	0.000	0.000	0.000
65	A	117	ARG	1	0.938	0.973	22.058	-0.046	-0.046	0.000	0.000	0.000	0.000
66	A	118	THR	0	-0.017	-0.013	21.189	-0.015	-0.015	0.000	0.000	0.000	0.000
67	A	119	GLY	0	0.016	0.016	21.464	-0.012	-0.012	0.000	0.000	0.000	0.000
68	A	120	LYS	1	0.886	0.943	18.829	0.088	0.088	0.000	0.000	0.000	0.000
69	A	121	ASN	0	0.083	0.036	11.003	0.107	0.107	0.000	0.000	0.000	0.000
70	A	122	PRO	0	0.020	0.001	13.616	-0.003	-0.003	0.000	0.000	0.000	0.000
71	A	123	ILE	0	-0.002	-0.001	9.132	0.039	0.039	0.000	0.000	0.000	0.000
72	A	124	GLN	0	0.024	0.021	13.443	-0.035	-0.035	0.000	0.000	0.000	0.000
73	A	125	VAL	0	-0.009	0.001	15.636	0.023	0.023	0.000	0.000	0.000	0.000
74	A	126	LEU	0	-0.016	-0.010	14.039	0.023	0.023	0.000	0.000	0.000	0.000
75	A	127	VAL	0	-0.008	-0.004	14.633	0.018	0.018	0.000	0.000	0.000	0.000
76	A	128	TRP	0	0.049	0.030	17.508	0.022	0.022	0.000	0.000	0.000	0.000
77	A	129	ALA	0	-0.010	-0.003	20.513	0.014	0.014	0.000	0.000	0.000	0.000
78	A	130	ILE	0	-0.048	-0.039	16.824	0.016	0.016	0.000	0.000	0.000	0.000
79	A	131	GLU	-1	-0.856	-0.950	20.281	-0.176	-0.176	0.000	0.000	0.000	0.000
80	A	132	ASN	0	-0.063	-0.029	22.723	0.001	0.001	0.000	0.000	0.000	0.000
81	A	133	ALA	0	-0.021	-0.021	24.074	0.009	0.009	0.000	0.000	0.000	0.000
82	A	134	ALA	0	-0.027	-0.001	23.289	0.011	0.011	0.000	0.000	0.000	0.000
83	A	135	PRO	0	-0.040	-0.010	25.378	-0.007	-0.007	0.000	0.000	0.000	0.000
84	A	136	ARG	1	0.855	0.866	28.109	0.055	0.055	0.000	0.000	0.000	0.000
85	A	137	GLH	0	-0.057	-0.061	29.893	-0.001	-0.001	0.000	0.000	0.000	0.000
86	A	138	ASP	-1	-0.783	-0.891	31.206	-0.002	-0.002	0.000	0.000	0.000	0.000
87	A	139	THR	0	-0.038	-0.005	33.475	-0.001	-0.001	0.000	0.000	0.000	0.000
88	A	140	THR	0	0.007	0.004	35.821	0.004	0.004	0.000	0.000	0.000	0.000
89	A	141	SER	0	-0.039	-0.027	37.992	-0.001	-0.001	0.000	0.000	0.000	0.000
90	A	142	VAL	0	-0.002	-0.008	40.946	0.002	0.002	0.000	0.000	0.000	0.000
91	A	143	MET	0	-0.058	-0.013	44.037	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	144	PHE	0	0.014	0.024	46.548	0.002	0.002	0.000	0.000	0.000	0.000
93	A	145	GLY	0	0.035	0.011	49.451	-0.001	-0.001	0.000	0.000	0.000	0.000
94	A	146	GLY	0	0.031	0.008	52.482	0.001	0.001	0.000	0.000	0.000	0.000
95	A	147	ILE	0	-0.014	-0.007	49.738	0.000	0.000	0.000	0.000	0.000	0.000
96	A	148	ARG	1	0.890	0.931	42.248	-0.007	-0.007	0.000	0.000	0.000	0.000
97	A	149	TYR	0	0.019	0.011	45.830	-0.002	-0.002	0.000	0.000	0.000	0.000
98	A	150	HIS	0	0.034	0.024	39.579	0.004	0.004	0.000	0.000	0.000	0.000
99	A	151	VAL	0	0.048	0.029	40.616	-0.002	-0.002	0.000	0.000	0.000	0.000
100	A	152	ALA	0	0.029	0.026	38.005	0.001	0.001	0.000	0.000	0.000	0.000
101	A	153	VAL	0	-0.040	-0.028	34.081	0.000	0.000	0.000	0.000	0.000	0.000
102	A	154	ASP	-1	-0.893	-0.945	30.673	-0.044	-0.044	0.000	0.000	0.000	0.000
103	A	155	ILE	0	-0.070	-0.017	27.325	0.007	0.007	0.000	0.000	0.000	0.000
104	A	156	SER	0	0.065	0.028	25.392	-0.007	-0.007	0.000	0.000	0.000	0.000
105	A	157	PRO	0	0.102	0.038	22.048	0.006	0.006	0.000	0.000	0.000	0.000
106	A	158	LEU	0	0.018	0.001	18.414	0.002	0.002	0.000	0.000	0.000	0.000
107	A	159	ARG	1	0.857	0.928	21.312	0.009	0.009	0.000	0.000	0.000	0.000
108	A	160	ARG	1	0.876	0.948	23.702	0.089	0.089	0.000	0.000	0.000	0.000
109	A	161	LEU	0	0.026	0.017	17.315	0.008	0.008	0.000	0.000	0.000	0.000
110	A	162	ASP	-1	-0.845	-0.895	20.828	0.074	0.074	0.000	0.000	0.000	0.000
111	A	163	VAL	0	0.016	0.000	21.705	0.015	0.015	0.000	0.000	0.000	0.000
112	A	164	ALA	0	0.052	0.036	21.901	0.009	0.009	0.000	0.000	0.000	0.000
113	A	165	LEU	0	-0.001	-0.019	16.747	0.013	0.013	0.000	0.000	0.000	0.000
114	A	166	ARG	1	0.853	0.919	20.932	-0.037	-0.037	0.000	0.000	0.000	0.000
115	A	167	ASN	0	0.046	0.013	23.699	0.014	0.014	0.000	0.000	0.000	0.000
116	A	168	ILE	0	0.025	0.030	20.970	0.003	0.003	0.000	0.000	0.000	0.000
117	A	169	ALA	0	-0.012	-0.007	21.656	0.007	0.007	0.000	0.000	0.000	0.000
118	A	170	LEU	0	-0.003	-0.007	23.470	0.006	0.006	0.000	0.000	0.000	0.000
119	A	171	GLY	0	0.042	0.024	27.035	0.001	0.001	0.000	0.000	0.000	0.000
120	A	172	ALA	0	-0.038	-0.013	24.457	0.000	0.000	0.000	0.000	0.000	0.000
121	A	173	SER	0	-0.012	-0.016	26.331	0.005	0.005	0.000	0.000	0.000	0.000
122	A	174	ALA	0	0.006	0.007	27.640	0.001	0.001	0.000	0.000	0.000	0.000
123	A	175	LYS	1	0.775	0.877	27.451	-0.037	-0.037	0.000	0.000	0.000	0.000
124	A	176	CYS	0	-0.082	-0.013	27.954	0.004	0.004	0.000	0.000	0.000	0.000
125	A	177	TYR	0	0.004	0.003	30.108	-0.002	-0.002	0.000	0.000	0.000	0.000
126	A	178	ARG	1	0.974	0.997	32.719	-0.042	-0.042	0.000	0.000	0.000	0.000
127	A	179	THR	0	-0.068	-0.044	32.528	-0.006	-0.006	0.000	0.000	0.000	0.000
128	A	180	LYS	1	0.971	0.980	33.991	-0.049	-0.049	0.000	0.000	0.000	0.000
129	A	181	MET	0	0.000	0.028	28.926	0.001	0.001	0.000	0.000	0.000	0.000
130	A	182	SER	0	0.010	-0.026	26.184	0.009	0.009	0.000	0.000	0.000	0.000
131	A	183	PHE	0	0.033	-0.020	23.412	-0.005	-0.005	0.000	0.000	0.000	0.000
132	A	184	ALA	0	0.012	0.000	21.451	-0.006	-0.006	0.000	0.000	0.000	0.000
133	A	185	GLU	-1	-0.799	-0.873	22.668	0.077	0.077	0.000	0.000	0.000	0.000
134	A	186	ALA	0	0.008	0.016	25.223	-0.015	-0.015	0.000	0.000	0.000	0.000
135	A	187	LEU	0	0.010	-0.015	18.830	-0.011	-0.011	0.000	0.000	0.000	0.000
136	A	188	ALA	0	0.003	-0.002	21.520	-0.015	-0.015	0.000	0.000	0.000	0.000
137	A	189	GLU	-1	-0.853	-0.926	22.470	0.013	0.013	0.000	0.000	0.000	0.000
138	A	190	GLU	-1	-0.813	-0.884	24.437	0.006	0.006	0.000	0.000	0.000	0.000
139	A	191	ILE	0	-0.020	-0.013	18.495	-0.011	-0.011	0.000	0.000	0.000	0.000
140	A	192	ILE	0	0.028	0.011	22.591	-0.018	-0.018	0.000	0.000	0.000	0.000
141	A	193	LEU	0	-0.004	0.015	24.371	-0.012	-0.012	0.000	0.000	0.000	0.000
142	A	194	ALA	0	0.006	0.013	24.231	-0.007	-0.007	0.000	0.000	0.000	0.000
143	A	195	ALA	0	-0.022	-0.009	22.393	-0.010	-0.010	0.000	0.000	0.000	0.000
144	A	196	ASN	0	-0.090	-0.059	24.327	-0.017	-0.017	0.000	0.000	0.000	0.000
145	A	197	LYS	1	0.904	0.972	27.641	0.083	0.083	0.000	0.000	0.000	0.000
146	A	198	ASP	-1	-0.738	-0.855	29.651	-0.013	-0.013	0.000	0.000	0.000	0.000
147	A	199	PRO	0	0.013	-0.004	31.250	0.004	0.004	0.000	0.000	0.000	0.000
148	A	200	LYS	1	0.848	0.910	32.635	0.014	0.014	0.000	0.000	0.000	0.000
149	A	201	SER	0	-0.065	-0.037	27.706	0.004	0.004	0.000	0.000	0.000	0.000
150	A	202	TYR	0	0.035	0.023	28.591	-0.003	-0.003	0.000	0.000	0.000	0.000
151	A	203	ALA	0	-0.008	-0.016	25.836	-0.002	-0.002	0.000	0.000	0.000	0.000
152	A	204	TYR	0	0.009	0.006	27.867	-0.007	-0.007	0.000	0.000	0.000	0.000
153	A	205	SER	0	0.008	-0.011	29.279	-0.002	-0.002	0.000	0.000	0.000	0.000
154	A	206	LYS	1	0.829	0.891	30.466	-0.013	-0.013	0.000	0.000	0.000	0.000
155	A	207	LYS	1	0.814	0.922	28.144	0.050	0.050	0.000	0.000	0.000	0.000
156	A	208	LEU	0	-0.016	-0.014	30.691	-0.002	-0.002	0.000	0.000	0.000	0.000
157	A	209	GLU	-1	-0.879	-0.928	33.924	0.006	0.006	0.000	0.000	0.000	0.000
158	A	210	ILE	0	0.003	0.000	30.823	0.000	0.000	0.000	0.000	0.000	0.000
159	A	211	GLU	-1	-0.688	-0.806	31.142	-0.050	-0.050	0.000	0.000	0.000	0.000
160	A	212	ARG	1	0.959	1.006	35.025	0.011	0.011	0.000	0.000	0.000	0.000
161	A	213	ILE	0	0.013	0.005	37.881	0.000	0.000	0.000	0.000	0.000	0.000
162	A	214	ALA	0	0.007	0.001	36.131	0.001	0.001	0.000	0.000	0.000	0.000
163	A	215	GLU	-1	-0.828	-0.885	37.515	-0.038	-0.038	0.000	0.000	0.000	0.000
164	A	216	SER	0	-0.038	-0.021	39.858	0.000	0.000	0.000	0.000	0.000	0.000
165	A	217	SER	0	-0.098	-0.050	41.017	0.003	0.003	0.000	0.000	0.000	0.000
166	A	218	ARG	1	0.870	0.946	37.003	0.036	0.036	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:18:ILE)