FMO DATABASE

FMODB ID: G5NY1

Calculation Name: 1BVO-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1BVO

Chain ID: A

ChEMBL ID:

UniProt ID: Q17034

Base Structure: X-ray

Registration Date: 2023-09-21

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	175
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1831367.290179
FMO2-HF: Nuclear repulsion	1762283.329352
FMO2-HF: Total energy	-69083.960827
FMO2-MP2: Total energy	-69284.574147

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:48:PRO)

Summations of interaction energy for fragment #1(A:48:PRO)

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.
-3.248	-3.378	22.067	-11.428	-10.505	-0.029

Interaction energy analysis for fragmet #1(A:48:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.028 / 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	50	VAL	0	0.036	0.008	3.795	0.246	2.326	-0.026	-1.006	-1.046	0.005
4	A	51	GLU	-1	-0.852	-0.909	7.007	0.256	0.256	0.000	0.000	0.000	0.000
5	A	52	ILE	0	-0.030	-0.026	9.613	0.027	0.027	0.000	0.000	0.000	0.000
6	A	53	THR	0	0.014	0.008	12.113	0.019	0.019	0.000	0.000	0.000	0.000
7	A	54	GLU	-1	-0.845	-0.904	14.641	0.026	0.026	0.000	0.000	0.000	0.000
8	A	55	GLN	0	0.100	0.048	16.791	-0.041	-0.041	0.000	0.000	0.000	0.000
9	A	56	PRO	0	-0.012	-0.006	19.403	0.023	0.023	0.000	0.000	0.000	0.000
10	A	57	HIS	0	0.050	0.036	22.186	-0.009	-0.009	0.000	0.000	0.000	0.000
11	A	58	PRO	0	0.025	0.012	25.440	-0.007	-0.007	0.000	0.000	0.000	0.000
12	A	59	LYS	1	0.920	0.950	26.943	0.069	0.069	0.000	0.000	0.000	0.000
13	A	60	ALA	0	0.007	0.003	29.058	0.008	0.008	0.000	0.000	0.000	0.000
14	A	61	LEU	0	-0.027	-0.012	27.960	0.005	0.005	0.000	0.000	0.000	0.000
15	A	62	ARG	1	0.889	0.965	31.045	0.053	0.053	0.000	0.000	0.000	0.000
16	A	63	PHE	0	0.005	0.017	28.311	-0.001	-0.001	0.000	0.000	0.000	0.000
17	A	64	ARG	1	0.818	0.891	32.063	0.063	0.063	0.000	0.000	0.000	0.000
18	A	65	TYR	0	0.074	0.026	33.191	-0.008	-0.008	0.000	0.000	0.000	0.000
19	A	66	GLU	-1	-0.876	-0.930	34.596	-0.085	-0.085	0.000	0.000	0.000	0.000
20	A	67	CYS	0	-0.059	-0.037	35.735	0.004	0.004	0.000	0.000	0.000	0.000
21	A	68	GLU	-1	-0.845	-0.933	37.385	-0.057	-0.057	0.000	0.000	0.000	0.000
22	A	69	GLY	0	-0.005	0.022	37.292	0.004	0.004	0.000	0.000	0.000	0.000
23	A	70	ARG	1	0.924	0.969	35.352	0.050	0.050	0.000	0.000	0.000	0.000
24	A	71	SER	0	0.037	0.006	31.909	-0.002	-0.002	0.000	0.000	0.000	0.000
25	A	72	ALA	0	-0.023	-0.008	29.662	-0.004	-0.004	0.000	0.000	0.000	0.000
26	A	73	GLY	0	-0.045	-0.019	30.633	0.001	0.001	0.000	0.000	0.000	0.000
27	A	74	SER	0	-0.009	-0.011	26.350	-0.006	-0.006	0.000	0.000	0.000	0.000
28	A	75	ILE	0	-0.013	0.010	23.273	0.006	0.006	0.000	0.000	0.000	0.000
29	A	76	PRO	0	-0.004	0.012	24.482	0.002	0.002	0.000	0.000	0.000	0.000
30	A	77	GLY	0	0.064	0.025	22.831	-0.015	-0.015	0.000	0.000	0.000	0.000
31	A	78	VAL	0	-0.004	-0.031	21.761	0.003	0.003	0.000	0.000	0.000	0.000
32	A	79	ASN	0	-0.050	-0.035	21.912	0.002	0.002	0.000	0.000	0.000	0.000
33	A	80	THR	0	-0.076	0.000	25.518	0.010	0.010	0.000	0.000	0.000	0.000
34	A	81	THR	0	0.006	-0.002	27.456	-0.002	-0.002	0.000	0.000	0.000	0.000
35	A	82	ALA	0	-0.079	-0.039	30.395	-0.003	-0.003	0.000	0.000	0.000	0.000
36	A	83	GLU	-1	-0.887	-0.949	33.591	0.019	0.019	0.000	0.000	0.000	0.000
37	A	84	GLN	0	-0.007	-0.003	26.533	0.000	0.000	0.000	0.000	0.000	0.000
38	A	85	LYS	1	0.962	0.983	28.410	0.004	0.004	0.000	0.000	0.000	0.000
39	A	86	THR	0	0.016	0.016	23.099	0.005	0.005	0.000	0.000	0.000	0.000
40	A	87	PHE	0	-0.028	-0.031	22.023	-0.010	-0.010	0.000	0.000	0.000	0.000
41	A	88	PRO	0	0.014	0.015	18.872	0.012	0.012	0.000	0.000	0.000	0.000
42	A	89	SER	0	-0.002	-0.003	15.656	0.012	0.012	0.000	0.000	0.000	0.000
43	A	90	ILE	0	-0.011	0.009	10.005	-0.030	-0.030	0.000	0.000	0.000	0.000
44	A	91	GLN	0	-0.004	-0.017	8.960	0.184	0.184	0.000	0.000	0.000	0.000
45	A	92	VAL	0	0.000	0.015	4.006	-0.346	-0.168	0.002	-0.039	-0.141	0.000
46	A	93	HIS	1	0.841	0.909	3.951	-1.537	-0.802	0.001	-0.428	-0.308	-0.001
47	A	94	GLY	0	0.031	0.014	1.917	1.982	-2.678	18.050	-8.854	-4.536	-0.027
48	A	95	TYR	0	-0.014	-0.022	2.498	-2.127	-1.396	0.618	0.019	-1.367	-0.002
49	A	96	ARG	1	0.944	0.973	4.114	-1.089	-0.991	0.001	-0.029	-0.070	0.000
50	A	97	GLY	0	0.063	0.027	7.666	-0.065	-0.065	0.000	0.000	0.000	0.000
51	A	98	ARG	1	0.843	0.916	9.492	0.012	0.012	0.000	0.000	0.000	0.000
52	A	99	ALA	0	0.046	0.005	7.383	-0.040	-0.040	0.000	0.000	0.000	0.000
53	A	100	VAL	0	0.017	0.039	9.375	0.070	0.070	0.000	0.000	0.000	0.000
54	A	101	VAL	0	-0.023	-0.019	9.990	-0.124	-0.124	0.000	0.000	0.000	0.000
55	A	102	VAL	0	0.024	0.014	12.000	0.080	0.080	0.000	0.000	0.000	0.000
56	A	103	VAL	0	0.007	0.001	14.200	-0.055	-0.055	0.000	0.000	0.000	0.000
57	A	104	SER	0	-0.007	-0.014	16.607	0.037	0.037	0.000	0.000	0.000	0.000
58	A	105	CYS	0	0.030	0.030	19.076	-0.012	-0.012	0.000	0.000	0.000	0.000
59	A	106	VAL	0	0.024	0.023	18.302	-0.006	-0.006	0.000	0.000	0.000	0.000
60	A	107	THR	0	0.031	0.005	21.574	0.016	0.016	0.000	0.000	0.000	0.000
61	A	108	LYS	1	0.887	0.940	22.723	0.118	0.118	0.000	0.000	0.000	0.000
62	A	109	GLU	-1	-0.888	-0.983	23.859	-0.183	-0.183	0.000	0.000	0.000	0.000
63	A	110	GLY	0	0.081	0.042	23.363	-0.016	-0.016	0.000	0.000	0.000	0.000
64	A	111	PRO	0	0.011	0.009	19.038	-0.008	-0.008	0.000	0.000	0.000	0.000
65	A	112	GLU	-1	-0.896	-0.942	18.106	-0.497	-0.497	0.000	0.000	0.000	0.000
66	A	113	HIS	1	0.789	0.908	18.182	0.368	0.368	0.000	0.000	0.000	0.000
67	A	114	LYS	1	1.050	1.017	20.217	0.204	0.204	0.000	0.000	0.000	0.000
68	A	115	PRO	0	-0.008	0.010	21.563	0.010	0.010	0.000	0.000	0.000	0.000
69	A	116	HIS	0	0.022	0.013	23.090	0.014	0.014	0.000	0.000	0.000	0.000
70	A	117	PRO	0	0.038	0.019	25.272	-0.005	-0.005	0.000	0.000	0.000	0.000
71	A	118	HIS	0	0.007	0.019	26.934	0.002	0.002	0.000	0.000	0.000	0.000
72	A	119	ASN	0	0.026	0.027	25.640	-0.026	-0.026	0.000	0.000	0.000	0.000
73	A	120	LEU	0	-0.010	-0.005	20.555	0.010	0.010	0.000	0.000	0.000	0.000
74	A	121	VAL	0	-0.022	-0.019	24.583	0.000	0.000	0.000	0.000	0.000	0.000
75	A	122	GLY	0	0.061	0.000	24.816	0.001	0.001	0.000	0.000	0.000	0.000
76	A	123	LYS	1	0.857	0.924	25.587	0.038	0.038	0.000	0.000	0.000	0.000
77	A	124	GLU	-1	-0.939	-0.970	20.900	-0.059	-0.059	0.000	0.000	0.000	0.000
78	A	125	GLY	0	0.132	0.065	20.712	-0.012	-0.012	0.000	0.000	0.000	0.000
79	A	126	CYS	0	-0.112	-0.029	21.418	-0.025	-0.025	0.000	0.000	0.000	0.000
80	A	127	LYS	1	0.990	0.985	23.138	0.135	0.135	0.000	0.000	0.000	0.000
81	A	128	LYS	1	0.963	0.977	23.809	0.121	0.121	0.000	0.000	0.000	0.000
82	A	129	GLY	0	-0.010	-0.001	25.025	-0.011	-0.011	0.000	0.000	0.000	0.000
83	A	130	VAL	0	0.022	0.029	19.081	-0.012	-0.012	0.000	0.000	0.000	0.000
84	A	131	CYS	0	-0.034	-0.008	19.681	0.027	0.027	0.000	0.000	0.000	0.000
85	A	132	THR	0	-0.034	-0.010	15.697	-0.040	-0.040	0.000	0.000	0.000	0.000
86	A	133	VAL	0	0.010	0.020	15.187	0.028	0.028	0.000	0.000	0.000	0.000
87	A	134	GLU	-1	-0.829	-0.910	13.447	-0.093	-0.093	0.000	0.000	0.000	0.000
88	A	135	ILE	0	-0.046	-0.015	8.751	0.023	0.023	0.000	0.000	0.000	0.000
89	A	136	ASN	0	0.044	0.044	12.621	0.067	0.067	0.000	0.000	0.000	0.000
90	A	137	SER	0	0.065	-0.003	11.528	0.051	0.051	0.000	0.000	0.000	0.000
91	A	138	THR	0	-0.021	-0.014	11.624	0.076	0.076	0.000	0.000	0.000	0.000
92	A	139	THR	0	-0.007	-0.030	12.011	0.103	0.103	0.000	0.000	0.000	0.000
93	A	140	MET	0	-0.059	0.037	7.686	0.047	0.047	0.000	0.000	0.000	0.000
94	A	141	SER	0	0.001	-0.008	9.663	-0.027	-0.027	0.000	0.000	0.000	0.000
95	A	142	TYR	0	-0.007	-0.002	12.374	-0.011	-0.011	0.000	0.000	0.000	0.000
96	A	143	THR	0	0.005	0.003	14.857	-0.006	-0.006	0.000	0.000	0.000	0.000
97	A	144	PHE	0	-0.002	-0.008	14.511	0.001	0.001	0.000	0.000	0.000	0.000
98	A	145	ASN	0	0.064	0.029	19.694	0.001	0.001	0.000	0.000	0.000	0.000
99	A	146	ASN	0	-0.085	-0.066	22.936	0.006	0.006	0.000	0.000	0.000	0.000
100	A	147	LEU	0	0.069	0.037	19.581	-0.007	-0.007	0.000	0.000	0.000	0.000
101	A	148	GLY	0	0.027	0.013	23.619	0.007	0.007	0.000	0.000	0.000	0.000
102	A	149	ILE	0	0.002	-0.001	24.579	-0.011	-0.011	0.000	0.000	0.000	0.000
103	A	150	GLN	0	-0.019	-0.017	27.470	0.009	0.009	0.000	0.000	0.000	0.000
104	A	151	CYS	0	-0.051	-0.030	29.669	-0.008	-0.008	0.000	0.000	0.000	0.000
105	A	152	VAL	0	0.065	0.045	30.330	0.008	0.008	0.000	0.000	0.000	0.000
106	A	153	LYS	1	0.946	0.965	32.987	0.076	0.076	0.000	0.000	0.000	0.000
107	A	154	LYS	1	0.979	0.964	36.117	0.089	0.089	0.000	0.000	0.000	0.000
108	A	155	LYS	1	0.909	0.959	37.131	0.069	0.069	0.000	0.000	0.000	0.000
109	A	156	ASP	-1	-0.788	-0.902	35.220	-0.091	-0.091	0.000	0.000	0.000	0.000
110	A	157	VAL	0	-0.039	-0.002	31.531	-0.006	-0.006	0.000	0.000	0.000	0.000
111	A	158	GLU	-1	-0.868	-0.937	32.017	-0.133	-0.133	0.000	0.000	0.000	0.000
112	A	159	GLU	-1	-0.926	-0.966	32.449	-0.115	-0.115	0.000	0.000	0.000	0.000
113	A	160	ALA	0	0.048	0.021	29.976	-0.006	-0.006	0.000	0.000	0.000	0.000
114	A	161	LEU	0	-0.016	-0.020	26.985	-0.012	-0.012	0.000	0.000	0.000	0.000
115	A	162	ARG	1	0.852	0.937	28.128	0.115	0.115	0.000	0.000	0.000	0.000
116	A	163	LEU	0	-0.017	-0.027	28.572	-0.008	-0.008	0.000	0.000	0.000	0.000
117	A	164	ARG	1	0.804	0.907	22.071	0.208	0.208	0.000	0.000	0.000	0.000
118	A	165	GLN	0	0.038	0.011	23.908	-0.026	-0.026	0.000	0.000	0.000	0.000
119	A	166	GLU	-1	-0.923	-0.956	25.016	-0.148	-0.148	0.000	0.000	0.000	0.000
120	A	167	ILE	0	-0.067	-0.028	21.550	-0.003	-0.003	0.000	0.000	0.000	0.000
121	A	168	ARG	1	0.914	0.965	20.483	0.266	0.266	0.000	0.000	0.000	0.000
122	A	169	VAL	0	-0.014	0.002	18.241	-0.031	-0.031	0.000	0.000	0.000	0.000
123	A	170	ASP	-1	-0.785	-0.910	18.532	-0.328	-0.328	0.000	0.000	0.000	0.000
124	A	171	PRO	0	-0.079	-0.049	15.269	-0.030	-0.030	0.000	0.000	0.000	0.000
125	A	172	PHE	0	0.049	-0.005	14.416	-0.068	-0.068	0.000	0.000	0.000	0.000
126	A	173	ARG	1	0.907	1.000	14.621	0.554	0.554	0.000	0.000	0.000	0.000
127	A	174	THR	0	0.036	0.020	19.025	0.024	0.024	0.000	0.000	0.000	0.000
128	A	175	GLY	0	-0.047	-0.016	22.186	0.028	0.028	0.000	0.000	0.000	0.000
129	A	176	PHE	0	0.021	-0.027	23.430	0.000	0.000	0.000	0.000	0.000	0.000
130	A	177	GLY	0	-0.019	0.002	27.455	0.015	0.015	0.000	0.000	0.000	0.000
131	A	178	HIS	0	-0.013	-0.037	26.289	0.015	0.015	0.000	0.000	0.000	0.000
132	A	179	ALA	0	-0.015	-0.005	30.257	0.007	0.007	0.000	0.000	0.000	0.000
133	A	180	LYS	1	1.003	1.010	31.954	0.155	0.155	0.000	0.000	0.000	0.000
134	A	181	GLU	-1	-0.970	-0.967	33.857	-0.124	-0.124	0.000	0.000	0.000	0.000
135	A	182	PRO	0	0.038	0.003	33.779	-0.005	-0.005	0.000	0.000	0.000	0.000
136	A	183	GLY	0	-0.073	-0.037	34.590	0.000	0.000	0.000	0.000	0.000	0.000
137	A	184	SER	0	-0.002	0.002	32.694	0.002	0.002	0.000	0.000	0.000	0.000
138	A	185	ILE	0	-0.023	0.003	29.012	-0.007	-0.007	0.000	0.000	0.000	0.000
139	A	186	ASP	-1	-0.791	-0.902	30.394	-0.108	-0.108	0.000	0.000	0.000	0.000
140	A	187	LEU	0	-0.066	-0.034	30.295	-0.005	-0.005	0.000	0.000	0.000	0.000
141	A	188	ASN	0	-0.039	-0.033	31.999	0.010	0.010	0.000	0.000	0.000	0.000
142	A	189	ALA	0	-0.010	-0.001	27.897	0.006	0.006	0.000	0.000	0.000	0.000
143	A	190	VAL	0	-0.027	0.005	24.082	-0.006	-0.006	0.000	0.000	0.000	0.000
144	A	191	ARG	1	0.845	0.935	20.034	0.258	0.258	0.000	0.000	0.000	0.000
145	A	192	LEU	0	0.011	0.009	18.254	-0.001	-0.001	0.000	0.000	0.000	0.000
146	A	193	CYS	0	-0.071	-0.021	15.368	-0.051	-0.051	0.000	0.000	0.000	0.000
147	A	194	PHE	0	0.040	0.013	11.782	0.060	0.060	0.000	0.000	0.000	0.000
148	A	195	GLN	0	0.023	0.001	10.616	-0.085	-0.085	0.000	0.000	0.000	0.000
149	A	196	VAL	0	0.028	0.015	5.736	0.151	0.151	0.000	0.000	0.000	0.000
150	A	197	PHE	0	-0.015	-0.001	7.577	-0.233	-0.233	0.000	0.000	0.000	0.000
151	A	198	LEU	0	0.027	-0.004	2.641	-0.436	0.149	0.316	-0.214	-0.687	-0.001
152	A	199	GLU	-1	-0.851	-0.946	7.056	-0.039	-0.039	0.000	0.000	0.000	0.000
153	A	200	GLY	0	-0.004	-0.004	9.049	-0.036	-0.036	0.000	0.000	0.000	0.000
154	A	201	GLN	0	0.039	0.026	10.579	0.059	0.059	0.000	0.000	0.000	0.000
155	A	202	GLN	0	-0.019	-0.003	13.212	0.017	0.017	0.000	0.000	0.000	0.000
156	A	203	ARG	1	0.993	0.976	15.657	0.004	0.004	0.000	0.000	0.000	0.000
157	A	204	GLY	0	-0.046	-0.019	15.537	0.004	0.004	0.000	0.000	0.000	0.000
158	A	205	ARG	1	0.896	0.955	15.446	0.160	0.160	0.000	0.000	0.000	0.000
159	A	206	PHE	0	-0.034	-0.026	10.511	0.000	0.000	0.000	0.000	0.000	0.000
160	A	207	THR	0	-0.032	-0.018	10.598	0.006	0.006	0.000	0.000	0.000	0.000
161	A	208	GLU	-1	-0.846	-0.905	6.078	-0.797	-0.797	0.000	0.000	0.000	0.000
162	A	209	PRO	0	-0.063	-0.005	7.153	-0.046	-0.046	0.000	0.000	0.000	0.000
163	A	210	LEU	0	-0.006	0.004	2.152	-1.155	-1.032	3.105	-0.877	-2.350	-0.003
164	A	211	THR	0	-0.018	-0.023	5.505	0.574	0.574	0.000	0.000	0.000	0.000
165	A	212	PRO	0	-0.052	-0.023	7.966	-0.017	-0.017	0.000	0.000	0.000	0.000
166	A	213	VAL	0	0.036	0.035	9.394	-0.018	-0.018	0.000	0.000	0.000	0.000
167	A	214	VAL	0	-0.044	-0.031	12.066	0.089	0.089	0.000	0.000	0.000	0.000
168	A	215	SER	0	0.025	0.028	15.751	0.004	0.004	0.000	0.000	0.000	0.000
169	A	216	ASP	-1	-0.889	-0.954	17.803	-0.176	-0.176	0.000	0.000	0.000	0.000
170	A	217	ILE	0	-0.094	-0.058	20.904	-0.006	-0.006	0.000	0.000	0.000	0.000
171	A	218	ILE	0	0.004	0.017	22.239	0.017	0.017	0.000	0.000	0.000	0.000
172	A	219	TYR	0	-0.037	-0.043	25.790	-0.007	-0.007	0.000	0.000	0.000	0.000
173	A	220	ASP	-1	-0.859	-0.936	29.548	-0.075	-0.075	0.000	0.000	0.000	0.000
174	A	221	LYS	1	0.927	0.981	31.967	0.049	0.049	0.000	0.000	0.000	0.000
175	A	222	LYS	1	0.942	0.961	34.187	0.052	0.052	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:48:PRO)