FMO DATABASE

FMODB ID: Q1KQY

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1694998.04533
FMO2-HF: Nuclear repulsion	1629523.001135
FMO2-HF: Total energy	-65475.044195
FMO2-MP2: Total energy	-65667.055473

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.
-10.788	-7.492	4.586	-3.051	-4.831	0.006

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 : 0.037 / q_NPA : -0.007

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	0.027	0.018	3.877	1.017	2.572	-0.011	-0.676	-0.869	0.002
4	A	21	MET	0	-0.064	-0.031	5.946	-0.244	-0.244	0.000	0.000	0.000	0.000
5	A	22	GLY	0	0.027	0.024	6.038	-0.314	-0.314	0.000	0.000	0.000	0.000
6	A	23	ARG	1	0.802	0.905	7.021	-0.436	-0.436	0.000	0.000	0.000	0.000
7	A	24	TRP	0	-0.026	-0.046	8.444	-0.121	-0.121	0.000	0.000	0.000	0.000
8	A	25	SER	0	0.016	-0.037	6.043	-0.351	-0.351	0.000	0.000	0.000	0.000
9	A	26	THR	0	-0.049	-0.070	6.530	0.326	0.326	0.000	0.000	0.000	0.000
10	A	27	GLU	-1	-0.838	-0.861	7.301	-1.748	-1.748	0.000	0.000	0.000	0.000
11	A	28	ASP	-1	-0.882	-0.928	9.099	-0.635	-0.635	0.000	0.000	0.000	0.000
12	A	29	VAL	0	-0.112	-0.051	11.420	0.128	0.128	0.000	0.000	0.000	0.000
13	A	30	GLU	-1	-0.783	-0.889	13.238	-0.289	-0.289	0.000	0.000	0.000	0.000
14	A	31	VAL	0	-0.046	-0.014	15.336	0.044	0.044	0.000	0.000	0.000	0.000
15	A	32	LYS	1	0.794	0.872	17.868	0.215	0.215	0.000	0.000	0.000	0.000
16	A	33	ASP	-1	-0.718	-0.826	21.506	-0.073	-0.073	0.000	0.000	0.000	0.000
17	A	34	PRO	0	0.035	0.004	21.935	-0.009	-0.009	0.000	0.000	0.000	0.000
18	A	35	SER	0	-0.063	-0.053	23.260	0.002	0.002	0.000	0.000	0.000	0.000
19	A	36	LEU	0	-0.043	-0.040	19.637	0.016	0.016	0.000	0.000	0.000	0.000
20	A	37	LYS	1	0.919	0.953	16.796	0.295	0.295	0.000	0.000	0.000	0.000
21	A	38	PRO	0	0.006	0.011	16.917	-0.029	-0.029	0.000	0.000	0.000	0.000
22	A	39	TYR	0	-0.022	-0.012	17.017	0.010	0.010	0.000	0.000	0.000	0.000
23	A	40	ILE	0	-0.029	-0.021	13.375	0.042	0.042	0.000	0.000	0.000	0.000
24	A	41	ASN	0	0.011	0.000	9.268	-0.069	-0.069	0.000	0.000	0.000	0.000
25	A	42	LEU	0	0.023	0.001	9.086	0.118	0.118	0.000	0.000	0.000	0.000
26	A	43	GLU	-1	-0.845	-0.887	6.812	-1.307	-1.307	0.000	0.000	0.000	0.000
27	A	44	PRO	0	-0.042	-0.010	2.189	-0.561	-0.329	4.256	-1.979	-2.509	0.001
28	A	45	ARG	1	0.983	0.994	2.653	-5.503	-3.994	0.341	-0.396	-1.453	0.003
29	A	64	VAL	0	0.011	-0.001	12.552	0.032	0.032	0.000	0.000	0.000	0.000
30	A	65	HIS	1	0.884	0.942	7.390	-0.190	-0.190	0.000	0.000	0.000	0.000
31	A	66	ILE	0	0.055	0.026	10.613	0.094	0.094	0.000	0.000	0.000	0.000
32	A	67	VAL	0	0.048	0.031	9.734	0.028	0.028	0.000	0.000	0.000	0.000
33	A	68	GLU	-1	-0.841	-0.924	9.386	0.960	0.960	0.000	0.000	0.000	0.000
34	A	69	ARG	1	0.861	0.924	12.194	-0.152	-0.152	0.000	0.000	0.000	0.000
35	A	70	LEU	0	0.040	0.026	15.025	-0.008	-0.008	0.000	0.000	0.000	0.000
36	A	71	ILE	0	0.017	0.006	11.970	-0.001	-0.001	0.000	0.000	0.000	0.000
37	A	72	ASN	0	0.001	-0.020	15.103	0.010	0.010	0.000	0.000	0.000	0.000
38	A	73	LYS	1	0.801	0.902	17.953	-0.173	-0.173	0.000	0.000	0.000	0.000
39	A	74	VAL	0	0.027	0.026	19.025	-0.015	-0.015	0.000	0.000	0.000	0.000
40	A	75	MET	0	-0.066	-0.029	17.896	-0.015	-0.015	0.000	0.000	0.000	0.000
41	A	76	ARG	1	0.857	0.928	21.369	-0.194	-0.194	0.000	0.000	0.000	0.000
42	A	77	SER	0	0.028	0.010	23.940	-0.024	-0.024	0.000	0.000	0.000	0.000
43	A	78	GLY	0	0.022	0.029	25.390	-0.017	-0.017	0.000	0.000	0.000	0.000
44	A	79	GLY	0	0.025	0.020	25.424	0.019	0.019	0.000	0.000	0.000	0.000
45	A	80	SER	0	0.005	0.012	26.758	0.016	0.016	0.000	0.000	0.000	0.000
46	A	98	SER	0	0.112	0.057	19.733	-0.006	-0.006	0.000	0.000	0.000	0.000
47	A	99	LYS	1	0.977	0.967	20.914	-0.212	-0.212	0.000	0.000	0.000	0.000
48	A	100	LYS	1	0.940	0.965	12.371	-0.783	-0.783	0.000	0.000	0.000	0.000
49	A	101	VAL	0	0.045	0.025	16.151	0.041	0.041	0.000	0.000	0.000	0.000
50	A	102	ARG	1	0.926	0.964	17.477	-0.240	-0.240	0.000	0.000	0.000	0.000
51	A	103	ALA	0	0.008	0.000	18.097	-0.018	-0.018	0.000	0.000	0.000	0.000
52	A	104	TYR	0	0.014	0.005	10.072	0.028	0.028	0.000	0.000	0.000	0.000
53	A	105	GLU	-1	-0.815	-0.935	14.819	0.591	0.591	0.000	0.000	0.000	0.000
54	A	106	VAL	0	-0.033	-0.002	17.176	-0.043	-0.043	0.000	0.000	0.000	0.000
55	A	107	VAL	0	0.013	-0.001	14.127	-0.038	-0.038	0.000	0.000	0.000	0.000
56	A	108	LYS	1	0.874	0.958	11.439	-0.855	-0.855	0.000	0.000	0.000	0.000
57	A	109	GLU	-1	-0.812	-0.905	15.295	0.165	0.165	0.000	0.000	0.000	0.000
58	A	110	ALA	0	0.017	0.012	18.470	-0.038	-0.038	0.000	0.000	0.000	0.000
59	A	111	PHE	0	-0.004	-0.014	11.631	-0.037	-0.037	0.000	0.000	0.000	0.000
60	A	112	LYS	1	0.879	0.929	16.216	-0.292	-0.292	0.000	0.000	0.000	0.000
61	A	113	ILE	0	-0.005	0.002	18.177	-0.037	-0.037	0.000	0.000	0.000	0.000
62	A	114	ILE	0	0.005	0.002	18.345	-0.020	-0.020	0.000	0.000	0.000	0.000
63	A	115	GLU	-1	-0.791	-0.856	15.176	-0.078	-0.078	0.000	0.000	0.000	0.000
64	A	116	LYS	1	0.909	0.945	19.298	-0.015	-0.015	0.000	0.000	0.000	0.000
65	A	117	ARG	1	0.905	0.954	22.287	-0.059	-0.059	0.000	0.000	0.000	0.000
66	A	118	THR	0	-0.032	-0.024	21.373	-0.014	-0.014	0.000	0.000	0.000	0.000
67	A	119	GLY	0	0.000	0.015	21.657	-0.013	-0.013	0.000	0.000	0.000	0.000
68	A	120	LYS	1	0.921	0.955	18.746	0.083	0.083	0.000	0.000	0.000	0.000
69	A	121	ASN	0	0.080	0.035	10.951	0.125	0.125	0.000	0.000	0.000	0.000
70	A	122	PRO	0	0.009	0.004	13.756	0.002	0.002	0.000	0.000	0.000	0.000
71	A	123	ILE	0	-0.001	0.000	9.204	0.053	0.053	0.000	0.000	0.000	0.000
72	A	124	GLN	0	0.020	0.015	13.550	-0.035	-0.035	0.000	0.000	0.000	0.000
73	A	125	VAL	0	-0.005	0.004	16.057	0.021	0.021	0.000	0.000	0.000	0.000
74	A	126	LEU	0	-0.009	-0.012	14.151	0.024	0.024	0.000	0.000	0.000	0.000
75	A	127	VAL	0	-0.015	-0.003	14.842	0.019	0.019	0.000	0.000	0.000	0.000
76	A	128	TRP	0	0.045	0.024	17.530	0.018	0.018	0.000	0.000	0.000	0.000
77	A	129	ALA	0	-0.019	-0.008	20.448	0.012	0.012	0.000	0.000	0.000	0.000
78	A	130	ILE	0	-0.038	-0.032	16.822	0.016	0.016	0.000	0.000	0.000	0.000
79	A	131	GLU	-1	-0.808	-0.911	20.522	-0.131	-0.131	0.000	0.000	0.000	0.000
80	A	132	ASN	0	-0.058	-0.033	22.846	-0.001	-0.001	0.000	0.000	0.000	0.000
81	A	133	ALA	0	-0.002	-0.009	23.985	0.006	0.006	0.000	0.000	0.000	0.000
82	A	134	ALA	0	-0.018	0.003	23.143	0.012	0.012	0.000	0.000	0.000	0.000
83	A	135	PRO	0	-0.044	-0.006	25.264	-0.010	-0.010	0.000	0.000	0.000	0.000
84	A	136	ARG	1	0.863	0.878	27.959	0.034	0.034	0.000	0.000	0.000	0.000
85	A	137	GLH	0	-0.048	-0.057	29.781	-0.002	-0.002	0.000	0.000	0.000	0.000
86	A	138	ASP	-1	-0.771	-0.871	31.161	0.029	0.029	0.000	0.000	0.000	0.000
87	A	139	THR	0	-0.042	-0.011	33.547	-0.003	-0.003	0.000	0.000	0.000	0.000
88	A	140	THR	0	0.018	0.025	35.961	0.006	0.006	0.000	0.000	0.000	0.000
89	A	141	SER	0	-0.029	-0.025	38.023	-0.003	-0.003	0.000	0.000	0.000	0.000
90	A	142	VAL	0	0.017	0.003	40.883	0.002	0.002	0.000	0.000	0.000	0.000
91	A	143	MET	0	-0.035	-0.013	43.942	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	144	PHE	0	0.037	0.017	46.807	0.002	0.002	0.000	0.000	0.000	0.000
93	A	145	GLY	0	0.041	0.016	50.063	-0.001	-0.001	0.000	0.000	0.000	0.000
94	A	146	GLY	0	0.000	-0.004	52.734	0.001	0.001	0.000	0.000	0.000	0.000
95	A	147	ILE	0	-0.004	0.013	50.046	0.000	0.000	0.000	0.000	0.000	0.000
96	A	148	ARG	1	0.827	0.909	42.347	-0.024	-0.024	0.000	0.000	0.000	0.000
97	A	149	TYR	0	0.049	0.023	45.905	-0.002	-0.002	0.000	0.000	0.000	0.000
98	A	150	HIS	0	0.000	-0.005	39.345	0.005	0.005	0.000	0.000	0.000	0.000
99	A	151	VAL	0	0.044	0.027	40.883	-0.002	-0.002	0.000	0.000	0.000	0.000
100	A	152	ALA	0	0.009	0.005	38.097	0.003	0.003	0.000	0.000	0.000	0.000
101	A	153	VAL	0	-0.054	-0.023	33.973	0.000	0.000	0.000	0.000	0.000	0.000
102	A	154	ASP	-1	-0.851	-0.943	30.274	-0.010	-0.010	0.000	0.000	0.000	0.000
103	A	155	ILE	0	-0.101	-0.034	27.159	0.009	0.009	0.000	0.000	0.000	0.000
104	A	156	SER	0	0.094	0.051	25.814	-0.005	-0.005	0.000	0.000	0.000	0.000
105	A	157	PRO	0	0.062	0.026	21.960	0.010	0.010	0.000	0.000	0.000	0.000
106	A	158	LEU	0	0.013	-0.001	18.564	0.007	0.007	0.000	0.000	0.000	0.000
107	A	159	ARG	1	0.839	0.908	21.492	-0.021	-0.021	0.000	0.000	0.000	0.000
108	A	160	ARG	1	0.799	0.892	23.451	0.050	0.050	0.000	0.000	0.000	0.000
109	A	161	LEU	0	0.028	0.010	17.116	0.008	0.008	0.000	0.000	0.000	0.000
110	A	162	ASP	-1	-0.827	-0.871	20.713	0.140	0.140	0.000	0.000	0.000	0.000
111	A	163	VAL	0	0.034	0.009	21.981	0.014	0.014	0.000	0.000	0.000	0.000
112	A	164	ALA	0	0.057	0.050	21.793	0.006	0.006	0.000	0.000	0.000	0.000
113	A	165	LEU	0	0.000	-0.014	16.734	0.012	0.012	0.000	0.000	0.000	0.000
114	A	166	ARG	1	0.842	0.909	21.014	-0.083	-0.083	0.000	0.000	0.000	0.000
115	A	167	ASN	0	0.015	0.002	23.833	0.007	0.007	0.000	0.000	0.000	0.000
116	A	168	ILE	0	0.030	0.021	21.050	0.003	0.003	0.000	0.000	0.000	0.000
117	A	169	ALA	0	-0.008	-0.005	21.706	0.005	0.005	0.000	0.000	0.000	0.000
118	A	170	LEU	0	0.008	-0.005	23.537	0.004	0.004	0.000	0.000	0.000	0.000
119	A	171	GLY	0	0.043	0.024	27.196	-0.002	-0.002	0.000	0.000	0.000	0.000
120	A	172	ALA	0	-0.033	-0.009	24.431	-0.002	-0.002	0.000	0.000	0.000	0.000
121	A	173	SER	0	-0.043	-0.039	26.390	0.000	0.000	0.000	0.000	0.000	0.000
122	A	174	ALA	0	0.020	0.006	27.895	-0.003	-0.003	0.000	0.000	0.000	0.000
123	A	175	LYS	1	0.768	0.875	27.596	-0.063	-0.063	0.000	0.000	0.000	0.000
124	A	176	CYS	0	-0.076	-0.020	28.243	0.001	0.001	0.000	0.000	0.000	0.000
125	A	177	TYR	0	-0.005	-0.011	30.381	-0.004	-0.004	0.000	0.000	0.000	0.000
126	A	178	ARG	1	0.961	0.997	33.041	-0.059	-0.059	0.000	0.000	0.000	0.000
127	A	179	THR	0	-0.054	-0.043	32.696	-0.007	-0.007	0.000	0.000	0.000	0.000
128	A	180	LYS	1	0.987	0.985	34.165	-0.058	-0.058	0.000	0.000	0.000	0.000
129	A	181	MET	0	-0.010	0.034	28.896	0.002	0.002	0.000	0.000	0.000	0.000
130	A	182	SER	0	0.025	-0.025	26.189	0.011	0.011	0.000	0.000	0.000	0.000
131	A	183	PHE	0	0.001	-0.021	23.752	-0.002	-0.002	0.000	0.000	0.000	0.000
132	A	184	ALA	0	0.026	0.012	21.689	-0.003	-0.003	0.000	0.000	0.000	0.000
133	A	185	GLU	-1	-0.803	-0.872	22.803	0.085	0.085	0.000	0.000	0.000	0.000
134	A	186	ALA	0	0.050	0.033	25.352	-0.015	-0.015	0.000	0.000	0.000	0.000
135	A	187	LEU	0	0.007	-0.017	19.115	-0.009	-0.009	0.000	0.000	0.000	0.000
136	A	188	ALA	0	-0.006	-0.009	21.731	-0.013	-0.013	0.000	0.000	0.000	0.000
137	A	189	GLU	-1	-0.848	-0.920	22.657	0.030	0.030	0.000	0.000	0.000	0.000
138	A	190	GLU	-1	-0.819	-0.871	24.476	0.033	0.033	0.000	0.000	0.000	0.000
139	A	191	ILE	0	-0.010	-0.010	18.561	-0.010	-0.010	0.000	0.000	0.000	0.000
140	A	192	ILE	0	0.027	0.013	22.599	-0.018	-0.018	0.000	0.000	0.000	0.000
141	A	193	LEU	0	-0.008	0.009	24.548	-0.013	-0.013	0.000	0.000	0.000	0.000
142	A	194	ALA	0	0.005	0.011	24.251	-0.008	-0.008	0.000	0.000	0.000	0.000
143	A	195	ALA	0	-0.025	-0.007	22.370	-0.010	-0.010	0.000	0.000	0.000	0.000
144	A	196	ASN	0	-0.085	-0.058	24.289	-0.019	-0.019	0.000	0.000	0.000	0.000
145	A	197	LYS	1	0.908	0.972	27.697	0.060	0.060	0.000	0.000	0.000	0.000
146	A	198	ASP	-1	-0.734	-0.846	29.682	0.001	0.001	0.000	0.000	0.000	0.000
147	A	199	PRO	0	-0.009	-0.016	31.286	0.006	0.006	0.000	0.000	0.000	0.000
148	A	200	LYS	1	0.846	0.902	32.684	0.002	0.002	0.000	0.000	0.000	0.000
149	A	201	SER	0	-0.058	-0.029	27.807	0.005	0.005	0.000	0.000	0.000	0.000
150	A	202	TYR	0	0.016	0.022	28.652	-0.004	-0.004	0.000	0.000	0.000	0.000
151	A	203	ALA	0	-0.010	-0.019	26.009	-0.001	-0.001	0.000	0.000	0.000	0.000
152	A	204	TYR	0	0.009	-0.002	28.058	-0.006	-0.006	0.000	0.000	0.000	0.000
153	A	205	SER	0	0.002	-0.012	29.429	-0.002	-0.002	0.000	0.000	0.000	0.000
154	A	206	LYS	1	0.838	0.892	30.433	-0.039	-0.039	0.000	0.000	0.000	0.000
155	A	207	LYS	1	0.813	0.925	28.026	0.023	0.023	0.000	0.000	0.000	0.000
156	A	208	LEU	0	0.009	-0.008	30.660	-0.003	-0.003	0.000	0.000	0.000	0.000
157	A	209	GLU	-1	-0.894	-0.933	33.911	0.027	0.027	0.000	0.000	0.000	0.000
158	A	210	ILE	0	0.011	0.004	30.780	-0.001	-0.001	0.000	0.000	0.000	0.000
159	A	211	GLU	-1	-0.701	-0.815	30.982	-0.025	-0.025	0.000	0.000	0.000	0.000
160	A	212	ARG	1	0.963	1.005	34.918	-0.008	-0.008	0.000	0.000	0.000	0.000
161	A	213	ILE	0	0.007	0.010	37.877	-0.001	-0.001	0.000	0.000	0.000	0.000
162	A	214	ALA	0	0.009	0.008	35.994	0.000	0.000	0.000	0.000	0.000	0.000
163	A	215	GLU	-1	-0.806	-0.872	37.816	-0.019	-0.019	0.000	0.000	0.000	0.000
164	A	216	SER	0	-0.057	-0.037	40.087	-0.001	-0.001	0.000	0.000	0.000	0.000
165	A	217	SER	0	-0.048	-0.030	40.637	0.002	0.002	0.000	0.000	0.000	0.000
166	A	218	ARG	1	0.854	0.941	36.883	0.018	0.018	0.000	0.000	0.000	0.000

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