FMO DATABASE

FMODB ID: 892NY

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1832150.213933
FMO2-HF: Nuclear repulsion	1763064.801961
FMO2-HF: Total energy	-69085.411972
FMO2-MP2: Total energy	-69285.886752

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.
-3.195	-2.777	22.562	-11.499	-11.483	-0.039

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 : 0.003 / q_NPA : -0.032

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	0.017	0.004	3.795	0.179	1.939	-0.028	-0.825	-0.906	0.003
4	A	51	GLU	-1	-0.846	-0.901	6.960	0.530	0.530	0.000	0.000	0.000	0.000
5	A	52	ILE	0	-0.035	-0.031	9.516	-0.022	-0.022	0.000	0.000	0.000	0.000
6	A	53	THR	0	0.016	0.002	12.176	0.021	0.021	0.000	0.000	0.000	0.000
7	A	54	GLU	-1	-0.814	-0.851	14.567	0.062	0.062	0.000	0.000	0.000	0.000
8	A	55	GLN	0	0.081	0.026	17.501	-0.047	-0.047	0.000	0.000	0.000	0.000
9	A	56	PRO	0	-0.013	-0.004	19.304	0.011	0.011	0.000	0.000	0.000	0.000
10	A	57	HIS	0	0.043	0.028	22.134	-0.005	-0.005	0.000	0.000	0.000	0.000
11	A	58	PRO	0	0.027	0.010	25.177	-0.009	-0.009	0.000	0.000	0.000	0.000
12	A	59	LYS	1	0.867	0.928	26.865	0.028	0.028	0.000	0.000	0.000	0.000
13	A	60	ALA	0	-0.023	-0.010	28.974	0.005	0.005	0.000	0.000	0.000	0.000
14	A	61	LEU	0	-0.018	-0.007	28.096	0.003	0.003	0.000	0.000	0.000	0.000
15	A	62	ARG	1	0.865	0.962	31.128	0.030	0.030	0.000	0.000	0.000	0.000
16	A	63	PHE	0	0.026	0.003	28.174	-0.001	-0.001	0.000	0.000	0.000	0.000
17	A	64	ARG	1	0.806	0.888	32.159	0.039	0.039	0.000	0.000	0.000	0.000
18	A	65	TYR	0	0.060	0.013	33.285	-0.006	-0.006	0.000	0.000	0.000	0.000
19	A	66	GLU	-1	-0.889	-0.938	34.618	-0.066	-0.066	0.000	0.000	0.000	0.000
20	A	67	CYS	0	-0.034	-0.029	35.823	0.002	0.002	0.000	0.000	0.000	0.000
21	A	68	GLU	-1	-0.856	-0.922	37.371	-0.036	-0.036	0.000	0.000	0.000	0.000
22	A	69	GLY	0	0.003	0.020	37.364	0.003	0.003	0.000	0.000	0.000	0.000
23	A	70	ARG	1	0.933	0.969	35.472	0.032	0.032	0.000	0.000	0.000	0.000
24	A	71	SER	0	0.033	0.006	31.762	-0.002	-0.002	0.000	0.000	0.000	0.000
25	A	72	ALA	0	-0.019	-0.008	29.778	-0.003	-0.003	0.000	0.000	0.000	0.000
26	A	73	GLY	0	-0.040	-0.014	30.694	0.002	0.002	0.000	0.000	0.000	0.000
27	A	74	SER	0	-0.016	-0.029	26.474	-0.007	-0.007	0.000	0.000	0.000	0.000
28	A	75	ILE	0	-0.025	-0.001	23.351	0.005	0.005	0.000	0.000	0.000	0.000
29	A	76	PRO	0	0.003	0.010	24.542	0.002	0.002	0.000	0.000	0.000	0.000
30	A	77	GLY	0	0.054	0.027	22.793	-0.009	-0.009	0.000	0.000	0.000	0.000
31	A	78	VAL	0	-0.019	-0.034	21.635	-0.002	-0.002	0.000	0.000	0.000	0.000
32	A	79	ASN	0	-0.057	-0.045	22.060	0.001	0.001	0.000	0.000	0.000	0.000
33	A	80	THR	0	-0.074	-0.002	25.444	0.004	0.004	0.000	0.000	0.000	0.000
34	A	81	THR	0	0.021	-0.006	27.410	-0.002	-0.002	0.000	0.000	0.000	0.000
35	A	82	ALA	0	-0.079	-0.033	30.346	-0.004	-0.004	0.000	0.000	0.000	0.000
36	A	83	GLU	-1	-0.882	-0.943	33.560	0.030	0.030	0.000	0.000	0.000	0.000
37	A	84	GLN	0	-0.047	-0.014	26.813	0.003	0.003	0.000	0.000	0.000	0.000
38	A	85	LYS	1	0.973	0.992	28.456	-0.012	-0.012	0.000	0.000	0.000	0.000
39	A	86	THR	0	-0.014	-0.030	23.057	0.003	0.003	0.000	0.000	0.000	0.000
40	A	87	PHE	0	-0.010	-0.028	22.069	-0.011	-0.011	0.000	0.000	0.000	0.000
41	A	88	PRO	0	0.012	0.016	18.962	0.014	0.014	0.000	0.000	0.000	0.000
42	A	89	SER	0	-0.004	0.005	15.750	0.006	0.006	0.000	0.000	0.000	0.000
43	A	90	ILE	0	0.007	0.011	10.351	-0.009	-0.009	0.000	0.000	0.000	0.000
44	A	91	GLN	0	0.016	-0.017	9.098	0.182	0.182	0.000	0.000	0.000	0.000
45	A	92	VAL	0	0.007	0.021	3.930	-0.257	-0.062	0.003	-0.044	-0.154	0.000
46	A	93	HIS	1	0.794	0.876	3.949	-1.806	-1.143	0.001	-0.356	-0.309	0.000
47	A	94	GLY	0	0.060	0.031	1.969	3.553	-1.261	18.090	-8.634	-4.642	-0.031
48	A	95	TYR	0	-0.019	-0.029	2.322	-3.890	-2.528	1.826	-0.657	-2.532	-0.008
49	A	96	ARG	1	0.903	0.943	3.749	-0.392	-0.275	0.006	-0.018	-0.105	0.000
50	A	97	GLY	0	0.042	0.022	7.312	-0.075	-0.075	0.000	0.000	0.000	0.000
51	A	98	ARG	1	0.789	0.868	9.262	0.161	0.161	0.000	0.000	0.000	0.000
52	A	99	ALA	0	0.057	0.024	7.341	-0.080	-0.080	0.000	0.000	0.000	0.000
53	A	100	VAL	0	0.012	0.037	9.343	0.081	0.081	0.000	0.000	0.000	0.000
54	A	101	VAL	0	-0.023	-0.022	10.025	-0.096	-0.096	0.000	0.000	0.000	0.000
55	A	102	VAL	0	0.000	0.008	12.052	0.060	0.060	0.000	0.000	0.000	0.000
56	A	103	VAL	0	0.015	0.005	14.295	-0.035	-0.035	0.000	0.000	0.000	0.000
57	A	104	SER	0	-0.005	-0.017	16.698	0.022	0.022	0.000	0.000	0.000	0.000
58	A	105	CYS	0	0.022	0.029	19.191	-0.003	-0.003	0.000	0.000	0.000	0.000
59	A	106	VAL	0	0.009	0.018	18.654	-0.008	-0.008	0.000	0.000	0.000	0.000
60	A	107	THR	0	-0.001	-0.006	21.707	0.013	0.013	0.000	0.000	0.000	0.000
61	A	108	LYS	1	0.784	0.879	22.863	0.068	0.068	0.000	0.000	0.000	0.000
62	A	109	GLU	-1	-0.781	-0.926	23.953	-0.109	-0.109	0.000	0.000	0.000	0.000
63	A	110	GLY	0	0.053	0.023	23.668	-0.014	-0.014	0.000	0.000	0.000	0.000
64	A	111	PRO	0	0.011	0.007	19.081	-0.006	-0.006	0.000	0.000	0.000	0.000
65	A	112	GLU	-1	-0.894	-0.934	18.630	-0.338	-0.338	0.000	0.000	0.000	0.000
66	A	113	HIS	1	0.804	0.913	18.316	0.230	0.230	0.000	0.000	0.000	0.000
67	A	114	LYS	1	0.970	0.960	20.653	0.153	0.153	0.000	0.000	0.000	0.000
68	A	115	PRO	0	0.000	0.008	21.601	0.011	0.011	0.000	0.000	0.000	0.000
69	A	116	HIS	0	0.021	0.004	23.222	0.010	0.010	0.000	0.000	0.000	0.000
70	A	117	PRO	0	0.012	-0.001	25.394	-0.004	-0.004	0.000	0.000	0.000	0.000
71	A	118	HIS	0	0.012	0.013	26.958	-0.002	-0.002	0.000	0.000	0.000	0.000
72	A	119	ASN	0	0.021	0.028	25.750	-0.022	-0.022	0.000	0.000	0.000	0.000
73	A	120	LEU	0	-0.008	0.000	20.647	0.010	0.010	0.000	0.000	0.000	0.000
74	A	121	VAL	0	-0.014	-0.015	24.670	-0.004	-0.004	0.000	0.000	0.000	0.000
75	A	122	GLY	0	0.064	-0.006	24.870	0.004	0.004	0.000	0.000	0.000	0.000
76	A	123	LYS	1	0.836	0.905	25.631	0.028	0.028	0.000	0.000	0.000	0.000
77	A	124	GLU	-1	-0.909	-0.952	20.881	-0.067	-0.067	0.000	0.000	0.000	0.000
78	A	125	GLY	0	0.142	0.067	20.745	-0.008	-0.008	0.000	0.000	0.000	0.000
79	A	126	CYS	0	-0.156	-0.016	21.465	-0.019	-0.019	0.000	0.000	0.000	0.000
80	A	127	LYS	1	1.000	0.981	23.201	0.126	0.126	0.000	0.000	0.000	0.000
81	A	128	LYS	1	0.940	0.973	23.882	0.110	0.110	0.000	0.000	0.000	0.000
82	A	129	GLY	0	-0.015	0.003	25.115	-0.008	-0.008	0.000	0.000	0.000	0.000
83	A	130	VAL	0	0.003	0.021	19.174	-0.006	-0.006	0.000	0.000	0.000	0.000
84	A	131	CYS	0	-0.013	-0.017	19.760	0.015	0.015	0.000	0.000	0.000	0.000
85	A	132	THR	0	-0.023	-0.008	15.624	-0.032	-0.032	0.000	0.000	0.000	0.000
86	A	133	VAL	0	0.009	0.014	15.236	0.022	0.022	0.000	0.000	0.000	0.000
87	A	134	GLU	-1	-0.790	-0.873	13.496	-0.161	-0.161	0.000	0.000	0.000	0.000
88	A	135	ILE	0	-0.048	-0.018	8.775	0.034	0.034	0.000	0.000	0.000	0.000
89	A	136	ASN	0	0.055	0.040	12.595	0.021	0.021	0.000	0.000	0.000	0.000
90	A	137	SER	0	0.059	0.006	11.138	0.047	0.047	0.000	0.000	0.000	0.000
91	A	138	THR	0	0.001	0.003	11.248	0.031	0.031	0.000	0.000	0.000	0.000
92	A	139	THR	0	0.000	-0.025	11.524	0.072	0.072	0.000	0.000	0.000	0.000
93	A	140	MET	0	-0.065	0.028	7.395	0.045	0.045	0.000	0.000	0.000	0.000
94	A	141	SER	0	0.016	0.013	9.668	0.023	0.023	0.000	0.000	0.000	0.000
95	A	142	TYR	0	0.009	0.002	12.419	-0.028	-0.028	0.000	0.000	0.000	0.000
96	A	143	THR	0	0.028	0.007	14.858	0.010	0.010	0.000	0.000	0.000	0.000
97	A	144	PHE	0	-0.014	-0.011	14.334	-0.007	-0.007	0.000	0.000	0.000	0.000
98	A	145	ASN	0	0.055	0.025	19.731	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	146	ASN	0	-0.062	-0.035	22.988	0.001	0.001	0.000	0.000	0.000	0.000
100	A	147	LEU	0	0.072	0.043	19.645	-0.008	-0.008	0.000	0.000	0.000	0.000
101	A	148	GLY	0	0.031	0.015	23.681	0.009	0.009	0.000	0.000	0.000	0.000
102	A	149	ILE	0	-0.003	0.000	24.838	-0.010	-0.010	0.000	0.000	0.000	0.000
103	A	150	GLN	0	-0.019	-0.017	27.562	0.005	0.005	0.000	0.000	0.000	0.000
104	A	151	CYS	0	-0.041	-0.015	29.770	-0.006	-0.006	0.000	0.000	0.000	0.000
105	A	152	VAL	0	0.053	0.035	30.589	0.005	0.005	0.000	0.000	0.000	0.000
106	A	153	LYS	1	0.897	0.958	33.099	0.058	0.058	0.000	0.000	0.000	0.000
107	A	154	LYS	1	0.979	0.963	36.237	0.058	0.058	0.000	0.000	0.000	0.000
108	A	155	LYS	1	0.920	0.963	37.256	0.048	0.048	0.000	0.000	0.000	0.000
109	A	156	ASP	-1	-0.763	-0.899	35.331	-0.068	-0.068	0.000	0.000	0.000	0.000
110	A	157	VAL	0	-0.036	-0.003	31.821	-0.005	-0.005	0.000	0.000	0.000	0.000
111	A	158	GLU	-1	-0.865	-0.933	32.140	-0.102	-0.102	0.000	0.000	0.000	0.000
112	A	159	GLU	-1	-0.827	-0.910	32.570	-0.099	-0.099	0.000	0.000	0.000	0.000
113	A	160	ALA	0	0.047	0.026	30.093	-0.006	-0.006	0.000	0.000	0.000	0.000
114	A	161	LEU	0	-0.016	-0.018	27.082	-0.010	-0.010	0.000	0.000	0.000	0.000
115	A	162	ARG	1	0.775	0.877	28.247	0.095	0.095	0.000	0.000	0.000	0.000
116	A	163	LEU	0	-0.020	-0.021	28.586	-0.010	-0.010	0.000	0.000	0.000	0.000
117	A	164	ARG	1	0.801	0.895	22.310	0.150	0.150	0.000	0.000	0.000	0.000
118	A	165	GLN	0	0.040	0.014	24.016	-0.021	-0.021	0.000	0.000	0.000	0.000
119	A	166	GLU	-1	-0.878	-0.930	25.121	-0.130	-0.130	0.000	0.000	0.000	0.000
120	A	167	ILE	0	-0.050	-0.030	21.714	-0.005	-0.005	0.000	0.000	0.000	0.000
121	A	168	ARG	1	0.910	0.969	20.996	0.222	0.222	0.000	0.000	0.000	0.000
122	A	169	VAL	0	-0.012	0.001	18.195	-0.026	-0.026	0.000	0.000	0.000	0.000
123	A	170	ASP	-1	-0.780	-0.910	18.645	-0.247	-0.247	0.000	0.000	0.000	0.000
124	A	171	PRO	0	-0.076	-0.041	15.227	-0.026	-0.026	0.000	0.000	0.000	0.000
125	A	172	PHE	0	0.050	0.002	15.038	-0.053	-0.053	0.000	0.000	0.000	0.000
126	A	173	ARG	1	0.904	0.992	14.748	0.469	0.469	0.000	0.000	0.000	0.000
127	A	174	THR	0	0.056	0.043	19.712	0.026	0.026	0.000	0.000	0.000	0.000
128	A	175	GLY	0	-0.030	-0.003	22.912	0.022	0.022	0.000	0.000	0.000	0.000
129	A	176	PHE	0	0.039	-0.013	23.602	0.002	0.002	0.000	0.000	0.000	0.000
130	A	177	GLY	0	0.010	0.014	27.900	0.013	0.013	0.000	0.000	0.000	0.000
131	A	178	HIS	0	0.028	-0.019	26.006	0.013	0.013	0.000	0.000	0.000	0.000
132	A	179	ALA	0	-0.043	-0.018	30.693	0.006	0.006	0.000	0.000	0.000	0.000
133	A	180	LYS	1	0.906	0.965	32.155	0.119	0.119	0.000	0.000	0.000	0.000
134	A	181	GLU	-1	-0.916	-0.938	34.282	-0.081	-0.081	0.000	0.000	0.000	0.000
135	A	182	PRO	0	0.032	0.006	34.082	-0.003	-0.003	0.000	0.000	0.000	0.000
136	A	183	GLY	0	-0.069	-0.039	34.727	0.000	0.000	0.000	0.000	0.000	0.000
137	A	184	SER	0	-0.027	-0.011	32.984	0.001	0.001	0.000	0.000	0.000	0.000
138	A	185	ILE	0	-0.030	-0.006	29.124	-0.004	-0.004	0.000	0.000	0.000	0.000
139	A	186	ASP	-1	-0.759	-0.870	30.529	-0.062	-0.062	0.000	0.000	0.000	0.000
140	A	187	LEU	0	-0.061	-0.029	30.426	-0.004	-0.004	0.000	0.000	0.000	0.000
141	A	188	ASN	0	-0.044	-0.033	32.107	0.007	0.007	0.000	0.000	0.000	0.000
142	A	189	ALA	0	-0.011	0.000	28.059	0.007	0.007	0.000	0.000	0.000	0.000
143	A	190	VAL	0	-0.007	0.010	24.283	-0.006	-0.006	0.000	0.000	0.000	0.000
144	A	191	ARG	1	0.850	0.939	20.111	0.137	0.137	0.000	0.000	0.000	0.000
145	A	192	LEU	0	0.019	0.013	18.349	-0.007	-0.007	0.000	0.000	0.000	0.000
146	A	193	CYS	0	-0.046	-0.021	14.539	-0.019	-0.019	0.000	0.000	0.000	0.000
147	A	194	PHE	0	0.027	0.012	11.917	0.034	0.034	0.000	0.000	0.000	0.000
148	A	195	GLN	0	0.017	-0.002	10.746	-0.056	-0.056	0.000	0.000	0.000	0.000
149	A	196	VAL	0	0.035	0.014	5.974	0.112	0.112	0.000	0.000	0.000	0.000
150	A	197	PHE	0	-0.005	-0.001	7.670	-0.200	-0.200	0.000	0.000	0.000	0.000
151	A	198	LEU	0	0.008	-0.009	2.495	-0.518	0.067	0.539	-0.263	-0.861	0.000
152	A	199	GLU	-1	-0.851	-0.942	7.036	-0.165	-0.165	0.000	0.000	0.000	0.000
153	A	200	GLY	0	0.016	0.009	8.856	-0.070	-0.070	0.000	0.000	0.000	0.000
154	A	201	GLN	0	0.020	0.017	10.351	0.030	0.030	0.000	0.000	0.000	0.000
155	A	202	GLN	0	-0.011	-0.001	13.026	0.028	0.028	0.000	0.000	0.000	0.000
156	A	203	ARG	1	0.985	0.972	15.339	0.095	0.095	0.000	0.000	0.000	0.000
157	A	204	GLY	0	-0.022	-0.010	15.434	0.018	0.018	0.000	0.000	0.000	0.000
158	A	205	ARG	1	0.876	0.947	15.428	0.208	0.208	0.000	0.000	0.000	0.000
159	A	206	PHE	0	-0.026	-0.016	10.584	-0.016	-0.016	0.000	0.000	0.000	0.000
160	A	207	THR	0	-0.016	-0.006	11.244	0.028	0.028	0.000	0.000	0.000	0.000
161	A	208	GLU	-1	-0.874	-0.927	6.508	-0.813	-0.813	0.000	0.000	0.000	0.000
162	A	209	PRO	0	-0.045	0.013	7.200	-0.035	-0.035	0.000	0.000	0.000	0.000
163	A	210	LEU	0	0.002	-0.003	2.241	-1.307	-0.757	2.125	-0.702	-1.974	-0.003
164	A	211	THR	0	-0.019	-0.021	5.728	0.531	0.531	0.000	0.000	0.000	0.000
165	A	212	PRO	0	-0.041	-0.019	8.667	0.008	0.008	0.000	0.000	0.000	0.000
166	A	213	VAL	0	0.015	0.025	9.259	0.005	0.005	0.000	0.000	0.000	0.000
167	A	214	VAL	0	-0.040	-0.026	12.201	0.050	0.050	0.000	0.000	0.000	0.000
168	A	215	SER	0	0.039	0.029	15.797	0.016	0.016	0.000	0.000	0.000	0.000
169	A	216	ASP	-1	-0.887	-0.936	17.803	-0.051	-0.051	0.000	0.000	0.000	0.000
170	A	217	ILE	0	-0.077	-0.043	20.887	-0.010	-0.010	0.000	0.000	0.000	0.000
171	A	218	ILE	0	0.008	0.014	22.342	0.014	0.014	0.000	0.000	0.000	0.000
172	A	219	TYR	0	0.001	-0.028	25.900	-0.010	-0.010	0.000	0.000	0.000	0.000
173	A	220	ASP	-1	-0.826	-0.911	29.661	-0.041	-0.041	0.000	0.000	0.000	0.000
174	A	221	LYS	1	0.929	0.979	32.075	0.017	0.017	0.000	0.000	0.000	0.000
175	A	222	LYS	1	0.968	0.978	34.286	0.023	0.023	0.000	0.000	0.000	0.000

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