FMO DATABASE

FMODB ID: 7YZKK

Calculation Name: 1HNG-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1HNG

Chain ID: A

ChEMBL ID:

UniProt ID: P08921

Base Structure: X-ray

Registration Date: 2025-10-03

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	173
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1641950.957786
FMO2-HF: Nuclear repulsion	1570656.215757
FMO2-HF: Total energy	-71294.742029
FMO2-MP2: Total energy	-71497.975174

3D Structure Molmil

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:2:ASP)

Summations of interaction energy for fragment #1(A:2:ASP)

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.
-10.182	-4.066	1.174	-3.209	-4.081	-0.009

Interaction energy analysis for fragmet #1(A:2:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.063 / q_NPA : -0.041

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	4	GLY	0	0.048	0.037	3.822	6.981	9.858	-0.030	-1.278	-1.569	-0.002
19	A	20	ASN	0	-0.021	-0.037	4.727	-1.173	-1.085	-0.001	-0.002	-0.085	0.000
90	A	91	LYS	1	0.841	0.941	2.320	-20.683	-17.931	1.206	-1.812	-2.146	-0.007
91	A	92	ALA	0	0.035	0.025	4.107	2.913	3.312	-0.001	-0.117	-0.281	0.000
4	A	5	THR	0	-0.034	-0.010	6.530	-2.288	-2.288	0.000	0.000	0.000	0.000
5	A	6	VAL	0	0.002	0.005	10.360	0.675	0.675	0.000	0.000	0.000	0.000
6	A	7	TRP	0	0.020	0.001	13.187	-0.559	-0.559	0.000	0.000	0.000	0.000
7	A	8	GLY	0	0.047	0.021	16.751	0.070	0.070	0.000	0.000	0.000	0.000
8	A	9	ALA	0	0.020	0.015	20.007	-0.023	-0.023	0.000	0.000	0.000	0.000
9	A	10	LEU	0	-0.001	-0.008	23.784	-0.065	-0.065	0.000	0.000	0.000	0.000
10	A	11	GLY	0	-0.013	0.006	26.104	0.051	0.051	0.000	0.000	0.000	0.000
11	A	12	HIS	0	-0.036	-0.015	25.135	0.057	0.057	0.000	0.000	0.000	0.000
12	A	13	GLY	0	0.023	0.017	23.955	-0.075	-0.075	0.000	0.000	0.000	0.000
13	A	14	ILE	0	-0.047	-0.031	17.597	0.116	0.116	0.000	0.000	0.000	0.000
14	A	15	ASN	0	0.005	0.000	17.432	-0.242	-0.242	0.000	0.000	0.000	0.000
15	A	16	LEU	0	-0.017	-0.002	13.041	0.256	0.256	0.000	0.000	0.000	0.000
16	A	17	ASN	0	-0.010	-0.004	11.409	-0.370	-0.370	0.000	0.000	0.000	0.000
17	A	18	ILE	0	0.013	0.000	8.744	0.166	0.166	0.000	0.000	0.000	0.000
18	A	19	PRO	0	-0.045	-0.016	5.527	0.710	0.710	0.000	0.000	0.000	0.000
20	A	21	PHE	0	0.048	0.027	8.773	-0.452	-0.452	0.000	0.000	0.000	0.000
21	A	22	GLN	0	0.016	0.004	11.137	0.082	0.082	0.000	0.000	0.000	0.000
22	A	23	MET	0	-0.018	0.017	14.945	-0.270	-0.270	0.000	0.000	0.000	0.000
23	A	24	THR	0	0.031	0.006	17.332	0.068	0.068	0.000	0.000	0.000	0.000
24	A	25	ASP	-1	-0.853	-0.929	19.692	-0.237	-0.237	0.000	0.000	0.000	0.000
25	A	26	ASP	-1	-0.932	-0.951	19.181	-0.252	-0.252	0.000	0.000	0.000	0.000
26	A	27	ILE	0	-0.061	-0.017	14.817	-0.227	-0.227	0.000	0.000	0.000	0.000
27	A	28	ASP	-1	-0.853	-0.927	18.300	-0.980	-0.980	0.000	0.000	0.000	0.000
28	A	29	GLU	-1	-0.810	-0.893	16.674	-2.019	-2.019	0.000	0.000	0.000	0.000
29	A	30	VAL	0	-0.014	-0.003	12.799	-0.194	-0.194	0.000	0.000	0.000	0.000
30	A	31	ARG	1	0.825	0.915	13.029	2.885	2.885	0.000	0.000	0.000	0.000
31	A	32	TRP	0	0.008	-0.011	11.538	-0.821	-0.821	0.000	0.000	0.000	0.000
32	A	33	GLU	-1	-0.900	-0.959	12.456	-3.490	-3.490	0.000	0.000	0.000	0.000
33	A	34	ARG	1	0.893	0.927	12.837	0.950	0.950	0.000	0.000	0.000	0.000
34	A	35	GLY	0	0.024	0.013	13.868	0.334	0.334	0.000	0.000	0.000	0.000
35	A	36	SER	0	-0.018	-0.006	15.050	-0.296	-0.296	0.000	0.000	0.000	0.000
36	A	37	THR	0	-0.036	-0.013	17.404	0.270	0.270	0.000	0.000	0.000	0.000
37	A	38	LEU	0	0.027	0.023	16.883	-0.190	-0.190	0.000	0.000	0.000	0.000
38	A	39	VAL	0	-0.026	-0.022	16.783	0.263	0.263	0.000	0.000	0.000	0.000
39	A	40	ALA	0	-0.016	-0.017	17.391	0.280	0.280	0.000	0.000	0.000	0.000
40	A	41	GLU	-1	-0.848	-0.919	17.024	-2.034	-2.034	0.000	0.000	0.000	0.000
41	A	42	PHE	0	-0.010	0.006	18.234	0.223	0.223	0.000	0.000	0.000	0.000
42	A	43	LYS	1	0.883	0.899	18.953	1.264	1.264	0.000	0.000	0.000	0.000
43	A	44	ARG	1	0.822	0.907	20.415	0.515	0.515	0.000	0.000	0.000	0.000
44	A	45	LYS	1	0.914	0.956	23.522	0.703	0.703	0.000	0.000	0.000	0.000
45	A	46	MET	0	0.000	0.009	24.390	-0.013	-0.013	0.000	0.000	0.000	0.000
46	A	47	LYS	1	0.955	0.988	26.210	0.543	0.543	0.000	0.000	0.000	0.000
47	A	48	PRO	0	0.020	-0.001	22.600	-0.065	-0.065	0.000	0.000	0.000	0.000
48	A	49	PHE	0	-0.023	0.005	20.660	0.086	0.086	0.000	0.000	0.000	0.000
49	A	50	LEU	0	0.006	0.000	21.693	-0.060	-0.060	0.000	0.000	0.000	0.000
50	A	51	LYS	1	0.925	0.977	21.594	1.109	1.109	0.000	0.000	0.000	0.000
51	A	52	SER	0	-0.028	-0.023	23.526	0.075	0.075	0.000	0.000	0.000	0.000
52	A	53	GLY	0	0.061	0.026	25.456	0.001	0.001	0.000	0.000	0.000	0.000
53	A	54	ALA	0	0.034	0.025	24.698	0.078	0.078	0.000	0.000	0.000	0.000
54	A	55	PHE	0	-0.017	-0.005	20.580	0.025	0.025	0.000	0.000	0.000	0.000
55	A	56	GLU	-1	-0.830	-0.921	21.727	-0.028	-0.028	0.000	0.000	0.000	0.000
56	A	57	ILE	0	-0.010	0.002	17.153	-0.038	-0.038	0.000	0.000	0.000	0.000
57	A	58	LEU	0	0.013	0.005	19.049	0.061	0.061	0.000	0.000	0.000	0.000
58	A	59	ALA	0	0.012	0.005	19.650	-0.080	-0.080	0.000	0.000	0.000	0.000
59	A	60	ASN	0	-0.012	-0.027	16.628	-0.240	-0.240	0.000	0.000	0.000	0.000
60	A	61	GLY	0	0.040	0.010	15.466	0.031	0.031	0.000	0.000	0.000	0.000
61	A	62	ASP	-1	-0.806	-0.882	14.182	0.530	0.530	0.000	0.000	0.000	0.000
62	A	63	LEU	0	-0.006	0.006	15.048	-0.115	-0.115	0.000	0.000	0.000	0.000
63	A	64	LYS	1	0.834	0.915	16.919	0.202	0.202	0.000	0.000	0.000	0.000
64	A	65	ILE	0	0.005	0.000	17.635	-0.120	-0.120	0.000	0.000	0.000	0.000
65	A	66	LYS	1	0.853	0.917	21.554	0.393	0.393	0.000	0.000	0.000	0.000
66	A	67	ASN	0	0.003	-0.008	25.194	0.122	0.122	0.000	0.000	0.000	0.000
67	A	68	LEU	0	-0.041	0.003	19.991	-0.100	-0.100	0.000	0.000	0.000	0.000
68	A	69	THR	0	0.021	0.009	23.925	0.096	0.096	0.000	0.000	0.000	0.000
69	A	70	ARG	1	0.927	0.938	23.203	0.110	0.110	0.000	0.000	0.000	0.000
70	A	71	ASP	-1	-0.886	-0.935	22.345	-0.664	-0.664	0.000	0.000	0.000	0.000
71	A	72	ASP	-1	-0.857	-0.912	20.394	-0.781	-0.781	0.000	0.000	0.000	0.000
72	A	73	SER	0	-0.049	-0.011	17.978	-0.077	-0.077	0.000	0.000	0.000	0.000
73	A	74	GLY	0	0.025	0.019	15.150	-0.159	-0.159	0.000	0.000	0.000	0.000
74	A	75	THR	0	-0.044	-0.034	8.996	0.163	0.163	0.000	0.000	0.000	0.000
75	A	76	TYR	0	-0.009	-0.018	11.018	0.063	0.063	0.000	0.000	0.000	0.000
76	A	77	ASN	0	-0.036	-0.023	6.353	-0.185	-0.185	0.000	0.000	0.000	0.000
77	A	78	VAL	0	0.023	0.017	7.661	1.442	1.442	0.000	0.000	0.000	0.000
78	A	79	THR	0	-0.036	-0.027	7.535	-1.949	-1.949	0.000	0.000	0.000	0.000
79	A	80	VAL	0	0.007	0.008	9.811	0.867	0.867	0.000	0.000	0.000	0.000
80	A	81	TYR	0	0.015	-0.003	11.894	-0.670	-0.670	0.000	0.000	0.000	0.000
81	A	82	SER	0	0.052	0.004	14.738	0.198	0.198	0.000	0.000	0.000	0.000
82	A	83	THR	0	-0.005	-0.009	17.550	-0.149	-0.149	0.000	0.000	0.000	0.000
83	A	84	ASN	0	-0.015	0.011	19.084	0.013	0.013	0.000	0.000	0.000	0.000
84	A	85	GLY	0	0.023	0.014	18.499	-0.045	-0.045	0.000	0.000	0.000	0.000
85	A	86	THR	0	-0.034	-0.005	14.041	-0.250	-0.250	0.000	0.000	0.000	0.000
86	A	87	ARG	1	0.935	0.967	8.681	5.724	5.724	0.000	0.000	0.000	0.000
87	A	88	ILE	0	0.000	0.007	10.752	-0.383	-0.383	0.000	0.000	0.000	0.000
88	A	89	LEU	0	-0.012	-0.002	5.933	0.008	0.008	0.000	0.000	0.000	0.000
89	A	90	ASN	0	0.005	-0.016	4.993	0.739	0.739	0.000	0.000	0.000	0.000
92	A	93	LEU	0	-0.017	-0.017	6.042	2.593	2.593	0.000	0.000	0.000	0.000
93	A	94	ASP	-1	-0.849	-0.909	9.027	-1.262	-1.262	0.000	0.000	0.000	0.000
94	A	95	LEU	0	0.006	0.009	11.380	0.838	0.838	0.000	0.000	0.000	0.000
95	A	96	ARG	1	0.866	0.913	14.059	-0.080	-0.080	0.000	0.000	0.000	0.000
96	A	97	ILE	0	0.009	0.003	17.110	0.223	0.223	0.000	0.000	0.000	0.000
97	A	98	LEU	0	-0.035	-0.022	20.543	-0.014	-0.014	0.000	0.000	0.000	0.000
98	A	99	GLU	-1	-0.852	-0.928	23.087	0.009	0.009	0.000	0.000	0.000	0.000
99	A	100	MET	0	-0.020	-0.020	26.378	0.046	0.046	0.000	0.000	0.000	0.000
100	A	101	VAL	0	-0.004	-0.015	27.851	-0.051	-0.051	0.000	0.000	0.000	0.000
101	A	102	SER	0	0.025	0.033	30.099	-0.004	-0.004	0.000	0.000	0.000	0.000
102	A	103	LYS	1	0.842	0.888	33.773	-0.366	-0.366	0.000	0.000	0.000	0.000
103	A	104	PRO	0	-0.054	-0.035	34.389	-0.026	-0.026	0.000	0.000	0.000	0.000
104	A	105	MET	0	0.030	0.026	36.944	-0.011	-0.011	0.000	0.000	0.000	0.000
105	A	106	ILE	0	-0.037	-0.036	39.703	0.017	0.017	0.000	0.000	0.000	0.000
106	A	107	TYR	0	-0.002	-0.012	42.316	-0.014	-0.014	0.000	0.000	0.000	0.000
107	A	108	TRP	0	0.008	-0.024	45.047	0.012	0.012	0.000	0.000	0.000	0.000
108	A	109	GLU	-1	-0.798	-0.873	47.699	0.165	0.165	0.000	0.000	0.000	0.000
109	A	110	CYS	0	-0.045	-0.035	50.475	0.003	0.003	0.000	0.000	0.000	0.000
110	A	111	SER	0	-0.032	-0.020	53.025	0.001	0.001	0.000	0.000	0.000	0.000
111	A	112	ASN	0	-0.016	-0.014	48.947	0.002	0.002	0.000	0.000	0.000	0.000
112	A	113	ALA	0	0.036	0.034	49.733	0.011	0.011	0.000	0.000	0.000	0.000
113	A	114	THR	0	-0.031	-0.019	44.876	0.020	0.020	0.000	0.000	0.000	0.000
114	A	115	LEU	0	0.003	0.009	41.493	-0.008	-0.008	0.000	0.000	0.000	0.000
115	A	116	THR	0	-0.015	-0.009	40.773	0.008	0.008	0.000	0.000	0.000	0.000
116	A	117	CYS	0	-0.050	0.000	36.180	0.035	0.035	0.000	0.000	0.000	0.000
117	A	118	GLU	-1	-0.872	-0.922	37.381	0.203	0.203	0.000	0.000	0.000	0.000
118	A	119	VAL	0	-0.041	-0.013	32.487	0.021	0.021	0.000	0.000	0.000	0.000
119	A	120	LEU	0	0.076	0.050	35.335	-0.014	-0.014	0.000	0.000	0.000	0.000
120	A	121	GLU	-1	-0.842	-0.917	32.142	0.155	0.155	0.000	0.000	0.000	0.000
121	A	122	GLY	0	0.000	0.001	28.824	0.047	0.047	0.000	0.000	0.000	0.000
122	A	123	THR	0	-0.026	-0.018	24.190	-0.042	-0.042	0.000	0.000	0.000	0.000
123	A	124	ASP	-1	-0.871	-0.948	21.209	0.843	0.843	0.000	0.000	0.000	0.000
124	A	125	VAL	0	-0.015	0.011	24.457	0.110	0.110	0.000	0.000	0.000	0.000
125	A	126	GLU	-1	-0.902	-0.959	25.597	0.897	0.897	0.000	0.000	0.000	0.000
126	A	127	LEU	0	0.026	0.011	27.923	0.028	0.028	0.000	0.000	0.000	0.000
127	A	128	LYS	1	0.831	0.916	26.282	-0.897	-0.897	0.000	0.000	0.000	0.000
128	A	129	LEU	0	0.032	0.013	32.424	-0.020	-0.020	0.000	0.000	0.000	0.000
129	A	130	TYR	0	-0.036	-0.024	30.928	0.051	0.051	0.000	0.000	0.000	0.000
130	A	131	GLN	0	0.032	0.019	37.588	-0.023	-0.023	0.000	0.000	0.000	0.000
131	A	132	GLY	0	0.022	0.015	41.213	0.009	0.009	0.000	0.000	0.000	0.000
132	A	133	LYS	1	0.888	0.946	35.290	-0.703	-0.703	0.000	0.000	0.000	0.000
133	A	134	GLU	-1	-0.913	-0.944	37.318	0.540	0.540	0.000	0.000	0.000	0.000
134	A	135	HIS	0	-0.014	-0.001	32.413	0.006	0.006	0.000	0.000	0.000	0.000
135	A	136	LEU	0	-0.017	-0.001	35.669	-0.003	-0.003	0.000	0.000	0.000	0.000
136	A	137	ARG	1	0.910	0.947	34.750	-0.400	-0.400	0.000	0.000	0.000	0.000
137	A	138	SER	0	0.011	-0.012	29.649	0.033	0.033	0.000	0.000	0.000	0.000
138	A	139	LEU	0	0.001	-0.006	30.611	-0.024	-0.024	0.000	0.000	0.000	0.000
139	A	140	ARG	1	0.856	0.945	23.069	-0.795	-0.795	0.000	0.000	0.000	0.000
140	A	141	GLN	0	-0.023	-0.019	28.564	-0.082	-0.082	0.000	0.000	0.000	0.000
141	A	142	LYS	1	0.840	0.912	31.057	-0.188	-0.188	0.000	0.000	0.000	0.000
142	A	143	THR	0	0.090	0.039	33.535	-0.009	-0.009	0.000	0.000	0.000	0.000
143	A	144	MET	0	-0.083	-0.031	34.746	0.018	0.018	0.000	0.000	0.000	0.000
144	A	145	SER	0	0.036	0.013	37.270	0.001	0.001	0.000	0.000	0.000	0.000
145	A	146	TYR	0	-0.043	-0.039	39.746	0.022	0.022	0.000	0.000	0.000	0.000
146	A	147	GLN	0	-0.021	0.001	41.793	-0.005	-0.005	0.000	0.000	0.000	0.000
147	A	148	TRP	0	0.014	0.009	44.884	0.022	0.022	0.000	0.000	0.000	0.000
148	A	149	THR	0	0.019	0.007	45.626	-0.013	-0.013	0.000	0.000	0.000	0.000
149	A	150	ASN	0	-0.039	-0.031	45.679	-0.010	-0.010	0.000	0.000	0.000	0.000
150	A	151	LEU	0	0.070	0.039	47.801	0.013	0.013	0.000	0.000	0.000	0.000
151	A	152	ARG	1	0.938	0.974	46.471	-0.375	-0.375	0.000	0.000	0.000	0.000
152	A	153	ALA	0	-0.010	0.000	44.926	0.008	0.008	0.000	0.000	0.000	0.000
153	A	154	PRO	0	0.029	0.015	43.923	-0.006	-0.006	0.000	0.000	0.000	0.000
154	A	155	PHE	0	0.015	0.011	41.633	0.027	0.027	0.000	0.000	0.000	0.000
155	A	156	LYS	1	0.937	0.972	34.636	-0.636	-0.636	0.000	0.000	0.000	0.000
156	A	158	LYS	1	0.892	0.946	28.604	-0.851	-0.851	0.000	0.000	0.000	0.000
157	A	159	ALA	0	0.064	0.051	30.770	0.015	0.015	0.000	0.000	0.000	0.000
158	A	160	VAL	0	-0.050	-0.035	24.627	0.037	0.037	0.000	0.000	0.000	0.000
159	A	161	ASN	0	0.040	0.026	23.560	0.040	0.040	0.000	0.000	0.000	0.000
160	A	162	ARG	1	0.898	0.944	16.218	-1.474	-1.474	0.000	0.000	0.000	0.000
161	A	163	VAL	0	-0.005	0.009	20.241	0.136	0.136	0.000	0.000	0.000	0.000
162	A	164	SER	0	0.009	0.008	22.418	-0.094	-0.094	0.000	0.000	0.000	0.000
163	A	165	GLN	0	0.015	-0.017	26.038	0.060	0.060	0.000	0.000	0.000	0.000
164	A	166	GLU	-1	-0.895	-0.911	28.278	0.508	0.508	0.000	0.000	0.000	0.000
165	A	167	SER	0	-0.063	-0.057	32.105	0.028	0.028	0.000	0.000	0.000	0.000
166	A	168	GLU	-1	-0.778	-0.880	35.026	0.353	0.353	0.000	0.000	0.000	0.000
167	A	169	MET	0	-0.072	-0.049	38.723	0.038	0.038	0.000	0.000	0.000	0.000
168	A	170	GLU	-1	-0.847	-0.909	41.501	0.272	0.272	0.000	0.000	0.000	0.000
169	A	171	VAL	0	-0.043	-0.030	44.731	0.018	0.018	0.000	0.000	0.000	0.000
170	A	172	VAL	0	0.007	0.009	46.728	-0.011	-0.011	0.000	0.000	0.000	0.000
171	A	173	ASN	0	-0.048	-0.023	49.272	0.008	0.008	0.000	0.000	0.000	0.000
172	A	175	PRO	0	-0.030	-0.009	54.795	0.004	0.004	0.000	0.000	0.000	0.000
173	A	176	GLU	-2	-1.896	-1.935	58.511	0.375	0.375	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:ASP)