FMO DATABASE

FMODB ID: NN12Q

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1830490.783295
FMO2-HF: Nuclear repulsion	1761404.100852
FMO2-HF: Total energy	-69086.682443
FMO2-MP2: Total energy	-69287.036599

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.
-7.302	-0.792	9.373	-6.099	-9.785	-0.041

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 : -0.017 / q_NPA : -0.024

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	0.022	0.003	3.871	-0.934	0.977	-0.020	-1.040	-0.851	0.002
4	A	51	GLU	-1	-0.793	-0.888	7.115	0.367	0.367	0.000	0.000	0.000	0.000
5	A	52	ILE	0	-0.022	-0.012	9.978	-0.006	-0.006	0.000	0.000	0.000	0.000
6	A	53	THR	0	-0.036	-0.025	12.684	0.035	0.035	0.000	0.000	0.000	0.000
7	A	54	GLU	-1	-0.746	-0.815	15.086	-0.014	-0.014	0.000	0.000	0.000	0.000
8	A	55	GLN	0	0.086	0.023	17.640	-0.051	-0.051	0.000	0.000	0.000	0.000
9	A	56	PRO	0	-0.021	-0.016	19.276	0.008	0.008	0.000	0.000	0.000	0.000
10	A	57	HIS	0	0.030	0.012	22.127	0.004	0.004	0.000	0.000	0.000	0.000
11	A	58	PRO	0	0.050	0.022	25.580	-0.005	-0.005	0.000	0.000	0.000	0.000
12	A	59	LYS	1	0.896	0.945	27.108	0.043	0.043	0.000	0.000	0.000	0.000
13	A	60	ALA	0	0.006	0.019	28.787	0.003	0.003	0.000	0.000	0.000	0.000
14	A	61	LEU	0	-0.001	-0.002	27.894	0.003	0.003	0.000	0.000	0.000	0.000
15	A	62	ARG	1	0.834	0.935	30.959	0.048	0.048	0.000	0.000	0.000	0.000
16	A	63	PHE	0	0.028	-0.002	28.213	-0.003	-0.003	0.000	0.000	0.000	0.000
17	A	64	ARG	1	0.814	0.894	31.908	0.061	0.061	0.000	0.000	0.000	0.000
18	A	65	TYR	0	0.055	0.015	33.217	-0.005	-0.005	0.000	0.000	0.000	0.000
19	A	66	GLU	-1	-0.925	-0.958	34.551	-0.077	-0.077	0.000	0.000	0.000	0.000
20	A	67	CYS	0	-0.015	-0.017	35.712	0.001	0.001	0.000	0.000	0.000	0.000
21	A	68	GLU	-1	-0.828	-0.905	37.349	-0.052	-0.052	0.000	0.000	0.000	0.000
22	A	69	GLY	0	0.020	0.019	37.920	0.002	0.002	0.000	0.000	0.000	0.000
23	A	70	ARG	1	0.893	0.954	35.230	0.051	0.051	0.000	0.000	0.000	0.000
24	A	71	SER	0	0.028	0.004	31.715	-0.002	-0.002	0.000	0.000	0.000	0.000
25	A	72	ALA	0	-0.018	-0.007	29.363	-0.005	-0.005	0.000	0.000	0.000	0.000
26	A	73	GLY	0	-0.042	-0.023	30.310	0.006	0.006	0.000	0.000	0.000	0.000
27	A	74	SER	0	-0.018	-0.025	26.413	-0.006	-0.006	0.000	0.000	0.000	0.000
28	A	75	ILE	0	-0.023	-0.005	23.051	0.009	0.009	0.000	0.000	0.000	0.000
29	A	76	PRO	0	0.002	0.005	24.438	-0.005	-0.005	0.000	0.000	0.000	0.000
30	A	77	GLY	0	0.024	0.000	22.970	-0.008	-0.008	0.000	0.000	0.000	0.000
31	A	78	VAL	0	-0.028	-0.034	22.172	0.006	0.006	0.000	0.000	0.000	0.000
32	A	79	ASN	0	-0.048	-0.040	22.319	0.014	0.014	0.000	0.000	0.000	0.000
33	A	80	THR	0	-0.079	-0.007	25.679	0.003	0.003	0.000	0.000	0.000	0.000
34	A	81	THR	0	0.024	-0.005	27.877	0.003	0.003	0.000	0.000	0.000	0.000
35	A	82	ALA	0	-0.040	-0.017	31.151	-0.004	-0.004	0.000	0.000	0.000	0.000
36	A	83	GLU	-1	-0.885	-0.951	34.006	-0.017	-0.017	0.000	0.000	0.000	0.000
37	A	84	GLN	0	-0.085	-0.031	27.087	0.001	0.001	0.000	0.000	0.000	0.000
38	A	85	LYS	1	0.976	0.995	28.718	0.038	0.038	0.000	0.000	0.000	0.000
39	A	86	THR	0	0.011	-0.015	23.364	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	87	PHE	0	-0.007	-0.022	22.217	-0.001	-0.001	0.000	0.000	0.000	0.000
41	A	88	PRO	0	0.011	0.019	18.929	0.002	0.002	0.000	0.000	0.000	0.000
42	A	89	SER	0	-0.010	-0.003	16.390	-0.006	-0.006	0.000	0.000	0.000	0.000
43	A	90	ILE	0	-0.042	-0.008	10.469	0.008	0.008	0.000	0.000	0.000	0.000
44	A	91	GLN	0	0.020	-0.005	9.451	0.058	0.058	0.000	0.000	0.000	0.000
45	A	92	VAL	0	0.018	0.017	3.899	-0.241	-0.092	0.002	-0.031	-0.121	0.000
46	A	93	HIS	1	0.777	0.875	4.561	-0.204	0.048	-0.001	-0.073	-0.178	0.000
47	A	94	GLY	0	0.066	0.025	2.312	-1.271	-0.762	5.828	-3.330	-3.007	-0.026
48	A	95	TYR	0	-0.007	-0.024	2.561	-3.835	-1.689	1.789	-0.845	-3.090	-0.014
49	A	96	ARG	1	0.895	0.926	3.863	0.178	0.294	0.005	-0.027	-0.094	0.000
50	A	97	GLY	0	0.039	0.034	7.501	-0.007	-0.007	0.000	0.000	0.000	0.000
51	A	98	ARG	1	0.769	0.860	9.589	0.274	0.274	0.000	0.000	0.000	0.000
52	A	99	ALA	0	0.030	0.016	7.560	-0.081	-0.081	0.000	0.000	0.000	0.000
53	A	100	VAL	0	0.005	0.023	9.541	0.082	0.082	0.000	0.000	0.000	0.000
54	A	101	VAL	0	0.000	-0.008	9.832	-0.114	-0.114	0.000	0.000	0.000	0.000
55	A	102	VAL	0	0.007	0.016	11.880	0.070	0.070	0.000	0.000	0.000	0.000
56	A	103	VAL	0	0.002	-0.004	14.011	-0.032	-0.032	0.000	0.000	0.000	0.000
57	A	104	SER	0	0.022	0.001	16.662	0.033	0.033	0.000	0.000	0.000	0.000
58	A	105	CYS	0	-0.002	0.016	19.363	-0.002	-0.002	0.000	0.000	0.000	0.000
59	A	106	VAL	0	0.005	0.000	18.863	-0.004	-0.004	0.000	0.000	0.000	0.000
60	A	107	THR	0	0.000	-0.007	21.890	0.008	0.008	0.000	0.000	0.000	0.000
61	A	108	LYS	1	0.806	0.896	22.770	0.053	0.053	0.000	0.000	0.000	0.000
62	A	109	GLU	-1	-0.794	-0.911	24.144	-0.077	-0.077	0.000	0.000	0.000	0.000
63	A	110	GLY	0	0.038	0.023	23.661	-0.013	-0.013	0.000	0.000	0.000	0.000
64	A	111	PRO	0	0.005	0.013	18.864	-0.005	-0.005	0.000	0.000	0.000	0.000
65	A	112	GLU	-1	-0.860	-0.934	18.634	-0.180	-0.180	0.000	0.000	0.000	0.000
66	A	113	HIS	1	0.800	0.899	18.069	0.154	0.154	0.000	0.000	0.000	0.000
67	A	114	LYS	1	0.914	0.951	20.480	0.104	0.104	0.000	0.000	0.000	0.000
68	A	115	PRO	0	0.032	0.015	21.177	0.002	0.002	0.000	0.000	0.000	0.000
69	A	116	HIS	0	0.009	0.007	22.962	0.011	0.011	0.000	0.000	0.000	0.000
70	A	117	PRO	0	0.000	-0.001	25.583	-0.007	-0.007	0.000	0.000	0.000	0.000
71	A	118	HIS	0	-0.012	-0.014	27.137	-0.003	-0.003	0.000	0.000	0.000	0.000
72	A	119	ASN	0	0.014	0.019	25.954	-0.020	-0.020	0.000	0.000	0.000	0.000
73	A	120	LEU	0	-0.020	-0.005	20.349	0.009	0.009	0.000	0.000	0.000	0.000
74	A	121	VAL	0	-0.024	-0.019	24.421	-0.002	-0.002	0.000	0.000	0.000	0.000
75	A	122	GLY	0	0.079	0.012	24.984	0.000	0.000	0.000	0.000	0.000	0.000
76	A	123	LYS	1	0.840	0.915	25.995	0.085	0.085	0.000	0.000	0.000	0.000
77	A	124	GLU	-1	-0.823	-0.896	20.931	-0.148	-0.148	0.000	0.000	0.000	0.000
78	A	125	GLY	0	0.081	0.029	20.428	-0.007	-0.007	0.000	0.000	0.000	0.000
79	A	126	CYS	0	-0.131	-0.033	21.334	-0.014	-0.014	0.000	0.000	0.000	0.000
80	A	127	LYS	1	0.964	0.965	23.547	0.159	0.159	0.000	0.000	0.000	0.000
81	A	128	LYS	1	0.896	0.941	24.164	0.117	0.117	0.000	0.000	0.000	0.000
82	A	129	GLY	0	0.020	0.023	25.372	-0.003	-0.003	0.000	0.000	0.000	0.000
83	A	130	VAL	0	-0.027	0.003	19.191	-0.006	-0.006	0.000	0.000	0.000	0.000
84	A	131	CYS	0	-0.010	-0.003	19.176	0.011	0.011	0.000	0.000	0.000	0.000
85	A	132	THR	0	-0.056	-0.039	15.607	-0.035	-0.035	0.000	0.000	0.000	0.000
86	A	133	VAL	0	0.018	0.022	15.024	0.027	0.027	0.000	0.000	0.000	0.000
87	A	134	GLU	-1	-0.791	-0.872	13.675	-0.310	-0.310	0.000	0.000	0.000	0.000
88	A	135	ILE	0	-0.039	-0.017	8.538	0.030	0.030	0.000	0.000	0.000	0.000
89	A	136	ASN	0	0.053	0.030	12.440	0.008	0.008	0.000	0.000	0.000	0.000
90	A	137	SER	0	0.048	0.013	11.179	0.000	0.000	0.000	0.000	0.000	0.000
91	A	138	THR	0	0.013	0.015	11.087	-0.001	-0.001	0.000	0.000	0.000	0.000
92	A	139	THR	0	0.006	-0.028	11.879	0.023	0.023	0.000	0.000	0.000	0.000
93	A	140	MET	0	-0.054	0.025	7.009	-0.023	-0.023	0.000	0.000	0.000	0.000
94	A	141	SER	0	0.042	0.029	9.464	-0.016	-0.016	0.000	0.000	0.000	0.000
95	A	142	TYR	0	0.003	-0.007	12.122	-0.003	-0.003	0.000	0.000	0.000	0.000
96	A	143	THR	0	0.032	0.010	14.776	-0.001	-0.001	0.000	0.000	0.000	0.000
97	A	144	PHE	0	0.012	0.009	14.578	0.008	0.008	0.000	0.000	0.000	0.000
98	A	145	ASN	0	0.014	-0.004	19.870	0.002	0.002	0.000	0.000	0.000	0.000
99	A	146	ASN	0	-0.051	-0.022	23.181	0.011	0.011	0.000	0.000	0.000	0.000
100	A	147	LEU	0	0.069	0.055	19.552	-0.006	-0.006	0.000	0.000	0.000	0.000
101	A	148	GLY	0	0.017	0.004	23.617	0.010	0.010	0.000	0.000	0.000	0.000
102	A	149	ILE	0	0.002	0.003	25.113	-0.009	-0.009	0.000	0.000	0.000	0.000
103	A	150	GLN	0	0.013	0.008	27.537	0.006	0.006	0.000	0.000	0.000	0.000
104	A	151	CYS	0	-0.047	-0.010	29.866	-0.004	-0.004	0.000	0.000	0.000	0.000
105	A	152	VAL	0	0.068	0.033	30.754	0.004	0.004	0.000	0.000	0.000	0.000
106	A	153	LYS	1	0.837	0.893	33.447	0.067	0.067	0.000	0.000	0.000	0.000
107	A	154	LYS	1	0.868	0.913	35.489	0.058	0.058	0.000	0.000	0.000	0.000
108	A	155	LYS	1	0.934	0.968	37.195	0.048	0.048	0.000	0.000	0.000	0.000
109	A	156	ASP	-1	-0.720	-0.841	34.978	-0.068	-0.068	0.000	0.000	0.000	0.000
110	A	157	VAL	0	-0.028	-0.002	31.829	-0.005	-0.005	0.000	0.000	0.000	0.000
111	A	158	GLU	-1	-0.789	-0.896	31.910	-0.086	-0.086	0.000	0.000	0.000	0.000
112	A	159	GLU	-1	-0.840	-0.898	32.719	-0.097	-0.097	0.000	0.000	0.000	0.000
113	A	160	ALA	0	0.050	0.021	29.909	-0.006	-0.006	0.000	0.000	0.000	0.000
114	A	161	LEU	0	-0.020	-0.015	26.996	-0.010	-0.010	0.000	0.000	0.000	0.000
115	A	162	ARG	1	0.761	0.867	27.981	0.091	0.091	0.000	0.000	0.000	0.000
116	A	163	LEU	0	-0.006	-0.010	28.632	-0.009	-0.009	0.000	0.000	0.000	0.000
117	A	164	ARG	1	0.838	0.913	22.470	0.145	0.145	0.000	0.000	0.000	0.000
118	A	165	GLN	0	0.009	0.003	23.881	-0.017	-0.017	0.000	0.000	0.000	0.000
119	A	166	GLU	-1	-0.854	-0.913	25.323	-0.123	-0.123	0.000	0.000	0.000	0.000
120	A	167	ILE	0	-0.061	-0.028	22.111	-0.002	-0.002	0.000	0.000	0.000	0.000
121	A	168	ARG	1	0.930	0.959	21.160	0.177	0.177	0.000	0.000	0.000	0.000
122	A	169	VAL	0	-0.004	0.009	18.265	-0.022	-0.022	0.000	0.000	0.000	0.000
123	A	170	ASP	-1	-0.780	-0.910	19.255	-0.190	-0.190	0.000	0.000	0.000	0.000
124	A	171	PRO	0	-0.068	-0.038	15.090	-0.020	-0.020	0.000	0.000	0.000	0.000
125	A	172	PHE	0	0.052	0.012	15.202	-0.052	-0.052	0.000	0.000	0.000	0.000
126	A	173	ARG	1	0.902	0.967	14.682	0.353	0.353	0.000	0.000	0.000	0.000
127	A	174	THR	0	0.052	0.045	19.785	0.030	0.030	0.000	0.000	0.000	0.000
128	A	175	GLY	0	-0.002	-0.001	22.533	0.019	0.019	0.000	0.000	0.000	0.000
129	A	176	PHE	0	0.000	-0.019	23.315	0.007	0.007	0.000	0.000	0.000	0.000
130	A	177	GLY	0	0.010	0.002	27.861	0.008	0.008	0.000	0.000	0.000	0.000
131	A	178	HIS	0	0.048	0.005	26.470	0.011	0.011	0.000	0.000	0.000	0.000
132	A	179	ALA	0	-0.041	-0.012	30.491	0.004	0.004	0.000	0.000	0.000	0.000
133	A	180	LYS	1	0.870	0.934	32.097	0.090	0.090	0.000	0.000	0.000	0.000
134	A	181	GLU	-1	-0.905	-0.939	34.210	-0.053	-0.053	0.000	0.000	0.000	0.000
135	A	182	PRO	0	0.025	0.008	34.295	-0.001	-0.001	0.000	0.000	0.000	0.000
136	A	183	GLY	0	-0.041	-0.021	35.255	0.000	0.000	0.000	0.000	0.000	0.000
137	A	184	SER	0	0.001	-0.002	32.901	-0.001	-0.001	0.000	0.000	0.000	0.000
138	A	185	ILE	0	-0.025	-0.002	29.302	-0.002	-0.002	0.000	0.000	0.000	0.000
139	A	186	ASP	-1	-0.762	-0.877	30.601	-0.056	-0.056	0.000	0.000	0.000	0.000
140	A	187	LEU	0	-0.027	-0.006	30.505	-0.007	-0.007	0.000	0.000	0.000	0.000
141	A	188	ASN	0	-0.049	-0.026	32.278	0.001	0.001	0.000	0.000	0.000	0.000
142	A	189	ALA	0	0.007	0.001	28.105	0.004	0.004	0.000	0.000	0.000	0.000
143	A	190	VAL	0	-0.019	0.002	24.030	-0.004	-0.004	0.000	0.000	0.000	0.000
144	A	191	ARG	1	0.832	0.930	19.943	0.106	0.106	0.000	0.000	0.000	0.000
145	A	192	LEU	0	0.033	0.017	18.169	-0.006	-0.006	0.000	0.000	0.000	0.000
146	A	193	CYS	0	-0.025	-0.002	14.709	-0.009	-0.009	0.000	0.000	0.000	0.000
147	A	194	PHE	0	0.003	-0.001	11.811	0.018	0.018	0.000	0.000	0.000	0.000
148	A	195	GLN	0	0.038	0.005	10.515	-0.035	-0.035	0.000	0.000	0.000	0.000
149	A	196	VAL	0	0.021	0.013	5.911	0.098	0.098	0.000	0.000	0.000	0.000
150	A	197	PHE	0	0.000	0.006	7.473	-0.176	-0.176	0.000	0.000	0.000	0.000
151	A	198	LEU	0	0.016	-0.001	3.064	-0.537	0.111	0.133	-0.151	-0.630	0.000
152	A	199	GLU	-1	-0.861	-0.940	7.519	-0.255	-0.255	0.000	0.000	0.000	0.000
153	A	200	GLY	0	-0.004	0.017	8.970	-0.038	-0.038	0.000	0.000	0.000	0.000
154	A	201	GLN	0	0.006	-0.007	10.104	0.033	0.033	0.000	0.000	0.000	0.000
155	A	202	GLN	0	0.044	0.027	13.153	0.036	0.036	0.000	0.000	0.000	0.000
156	A	203	ARG	1	0.938	0.959	15.065	0.155	0.155	0.000	0.000	0.000	0.000
157	A	204	GLY	0	-0.005	-0.003	15.608	0.033	0.033	0.000	0.000	0.000	0.000
158	A	205	ARG	1	0.861	0.937	15.022	0.234	0.234	0.000	0.000	0.000	0.000
159	A	206	PHE	0	0.004	-0.006	10.884	-0.015	-0.015	0.000	0.000	0.000	0.000
160	A	207	THR	0	-0.031	-0.017	11.141	0.004	0.004	0.000	0.000	0.000	0.000
161	A	208	GLU	-1	-0.836	-0.915	6.336	-0.671	-0.671	0.000	0.000	0.000	0.000
162	A	209	PRO	0	-0.069	-0.013	7.133	-0.121	-0.121	0.000	0.000	0.000	0.000
163	A	210	LEU	0	0.007	-0.001	2.352	-1.359	-0.580	1.637	-0.602	-1.814	-0.003
164	A	211	THR	0	-0.020	-0.016	5.704	0.569	0.569	0.000	0.000	0.000	0.000
165	A	212	PRO	0	-0.025	-0.012	8.287	-0.071	-0.071	0.000	0.000	0.000	0.000
166	A	213	VAL	0	-0.005	0.009	9.016	0.046	0.046	0.000	0.000	0.000	0.000
167	A	214	VAL	0	-0.031	-0.024	11.845	0.018	0.018	0.000	0.000	0.000	0.000
168	A	215	SER	0	-0.007	-0.006	15.558	0.021	0.021	0.000	0.000	0.000	0.000
169	A	216	ASP	-1	-0.850	-0.916	17.824	-0.048	-0.048	0.000	0.000	0.000	0.000
170	A	217	ILE	0	-0.070	-0.023	21.101	-0.013	-0.013	0.000	0.000	0.000	0.000
171	A	218	ILE	0	0.005	0.015	22.419	0.009	0.009	0.000	0.000	0.000	0.000
172	A	219	TYR	0	0.019	-0.018	25.811	-0.004	-0.004	0.000	0.000	0.000	0.000
173	A	220	ASP	-1	-0.736	-0.830	29.507	-0.054	-0.054	0.000	0.000	0.000	0.000
174	A	221	LYS	1	0.822	0.925	31.951	0.046	0.046	0.000	0.000	0.000	0.000
175	A	222	LYS	1	0.916	0.925	34.309	0.035	0.035	0.000	0.000	0.000	0.000

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