FMO DATABASE

FMODB ID: 971K2

Calculation Name: 6I4Y-B-Xray547

Preferred Name: Maltose/maltodextrin-binding periplasmic protein

Target Type: SINGLE PROTEIN

Ligand Name: alpha-d-glucopyranose

Ligand 3-letter code: GLC

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 6I4Y

Chain ID: B

ChEMBL ID: CHEMBL4295571

UniProt ID: P0AEX9

Base Structure: X-ray

Registration Date: 2025-10-04

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	-1485883.562465
FMO2-HF: Nuclear repulsion	1417543.358026
FMO2-HF: Total energy	-68340.204439
FMO2-MP2: Total energy	-68537.829179

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:-1:ASP)

Summations of interaction energy for fragment #1(A:-1: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.
0.223	2.777	-0.027	-1.068	-1.459	0.002

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.027 / q_NPA : -0.009

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	1	MET	0	0.034	0.014	3.840	-0.944	1.430	-0.026	-1.066	-1.282	0.002
137	A	135	VAL	0	-0.006	-0.006	4.983	1.274	1.454	-0.001	-0.002	-0.177	0.000
4	A	2	LYS	1	0.829	0.912	6.505	4.502	4.502	0.000	0.000	0.000	0.000
5	A	3	ILE	0	-0.001	0.006	9.385	0.114	0.114	0.000	0.000	0.000	0.000
6	A	4	TRP	0	0.057	0.031	12.032	0.235	0.235	0.000	0.000	0.000	0.000
7	A	5	THR	0	-0.055	-0.054	13.959	-0.438	-0.438	0.000	0.000	0.000	0.000
8	A	6	SER	0	-0.046	0.000	16.272	0.083	0.083	0.000	0.000	0.000	0.000
9	A	7	GLU	-1	-0.892	-0.954	20.025	-1.089	-1.089	0.000	0.000	0.000	0.000
10	A	8	HIS	0	-0.012	-0.005	22.959	0.075	0.075	0.000	0.000	0.000	0.000
11	A	9	VAL	0	-0.012	-0.007	26.436	-0.010	-0.010	0.000	0.000	0.000	0.000
12	A	10	PHE	0	-0.009	0.004	27.176	0.028	0.028	0.000	0.000	0.000	0.000
13	A	11	ASP	-1	-0.879	-0.928	32.026	-0.383	-0.383	0.000	0.000	0.000	0.000
14	A	12	HIS	0	0.018	0.004	34.328	0.016	0.016	0.000	0.000	0.000	0.000
15	A	13	PRO	0	0.123	0.089	33.981	-0.030	-0.030	0.000	0.000	0.000	0.000
16	A	14	TRP	0	0.026	0.027	27.510	0.032	0.032	0.000	0.000	0.000	0.000
17	A	15	GLU	-1	-0.793	-0.891	31.871	-0.313	-0.313	0.000	0.000	0.000	0.000
18	A	16	THR	0	-0.054	-0.025	34.185	0.021	0.021	0.000	0.000	0.000	0.000
19	A	17	VAL	0	0.018	0.014	29.198	0.015	0.015	0.000	0.000	0.000	0.000
20	A	18	THR	0	0.028	-0.002	28.916	-0.003	-0.003	0.000	0.000	0.000	0.000
21	A	19	THR	0	-0.066	-0.046	30.371	0.028	0.028	0.000	0.000	0.000	0.000
22	A	20	ALA	0	-0.003	-0.011	32.739	0.021	0.021	0.000	0.000	0.000	0.000
23	A	21	ALA	0	-0.014	-0.006	27.311	0.014	0.014	0.000	0.000	0.000	0.000
24	A	22	MET	0	-0.043	-0.010	27.273	0.038	0.038	0.000	0.000	0.000	0.000
25	A	23	GLN	0	-0.038	-0.013	30.304	0.030	0.030	0.000	0.000	0.000	0.000
26	A	24	LYS	1	0.942	0.992	25.688	0.303	0.303	0.000	0.000	0.000	0.000
27	A	25	TYR	0	0.003	0.022	25.053	-0.017	-0.017	0.000	0.000	0.000	0.000
28	A	26	PRO	0	0.055	0.027	31.949	0.011	0.011	0.000	0.000	0.000	0.000
29	A	27	ASN	0	-0.010	-0.031	30.578	-0.014	-0.014	0.000	0.000	0.000	0.000
30	A	28	PRO	0	0.029	-0.009	34.111	0.006	0.006	0.000	0.000	0.000	0.000
31	A	29	MET	0	0.015	0.022	31.885	0.008	0.008	0.000	0.000	0.000	0.000
32	A	30	ASN	0	-0.056	-0.027	27.838	-0.028	-0.028	0.000	0.000	0.000	0.000
33	A	31	PRO	0	0.048	0.028	30.754	0.021	0.021	0.000	0.000	0.000	0.000
34	A	32	SER	0	0.019	0.015	28.529	0.013	0.013	0.000	0.000	0.000	0.000
35	A	33	VAL	0	-0.033	-0.008	27.085	0.033	0.033	0.000	0.000	0.000	0.000
36	A	34	VAL	0	0.006	-0.003	29.755	-0.004	-0.004	0.000	0.000	0.000	0.000
37	A	35	GLY	0	-0.003	0.002	30.797	0.008	0.008	0.000	0.000	0.000	0.000
38	A	36	VAL	0	-0.058	-0.020	28.291	0.008	0.008	0.000	0.000	0.000	0.000
39	A	37	ASP	-1	-0.857	-0.909	28.572	0.112	0.112	0.000	0.000	0.000	0.000
40	A	38	VAL	0	-0.078	-0.050	27.883	-0.011	-0.011	0.000	0.000	0.000	0.000
41	A	39	LEU	0	-0.048	-0.021	23.951	0.016	0.016	0.000	0.000	0.000	0.000
42	A	40	ASP	-1	-0.883	-0.949	26.327	0.166	0.166	0.000	0.000	0.000	0.000
43	A	41	ARG	1	0.885	0.929	27.486	0.024	0.024	0.000	0.000	0.000	0.000
44	A	42	HIS	0	0.051	0.047	27.879	0.006	0.006	0.000	0.000	0.000	0.000
45	A	43	ILE	0	-0.006	-0.007	28.676	-0.033	-0.033	0.000	0.000	0.000	0.000
46	A	44	ASP	-1	-0.768	-0.837	25.318	-0.114	-0.114	0.000	0.000	0.000	0.000
47	A	45	PRO	0	0.013	-0.026	27.659	-0.018	-0.018	0.000	0.000	0.000	0.000
48	A	46	SER	0	-0.108	-0.067	26.978	-0.026	-0.026	0.000	0.000	0.000	0.000
49	A	47	GLY	0	0.013	0.011	29.258	-0.028	-0.028	0.000	0.000	0.000	0.000
50	A	48	LYS	1	0.856	0.934	24.200	0.311	0.311	0.000	0.000	0.000	0.000
51	A	49	LEU	0	-0.026	-0.011	27.938	0.045	0.045	0.000	0.000	0.000	0.000
52	A	50	HIS	0	-0.015	-0.019	22.007	-0.016	-0.016	0.000	0.000	0.000	0.000
53	A	51	SER	0	-0.010	-0.014	24.552	0.028	0.028	0.000	0.000	0.000	0.000
54	A	52	HIS	0	0.010	0.016	20.761	-0.010	-0.010	0.000	0.000	0.000	0.000
55	A	53	ARG	1	0.878	0.921	23.241	0.099	0.099	0.000	0.000	0.000	0.000
56	A	54	LEU	0	0.003	0.014	23.135	0.035	0.035	0.000	0.000	0.000	0.000
57	A	55	LEU	0	0.002	0.005	23.673	-0.026	-0.026	0.000	0.000	0.000	0.000
58	A	56	SER	0	-0.065	-0.045	24.823	0.048	0.048	0.000	0.000	0.000	0.000
59	A	57	THR	0	0.021	0.001	25.245	-0.048	-0.048	0.000	0.000	0.000	0.000
60	A	58	GLU	-1	-0.946	-0.973	27.416	0.145	0.145	0.000	0.000	0.000	0.000
61	A	59	TRP	0	0.003	-0.013	23.309	-0.051	-0.051	0.000	0.000	0.000	0.000
62	A	60	GLY	0	0.027	0.016	29.615	0.012	0.012	0.000	0.000	0.000	0.000
63	A	61	LEU	0	0.011	0.008	30.805	-0.012	-0.012	0.000	0.000	0.000	0.000
64	A	62	PRO	0	0.031	0.014	34.025	0.019	0.019	0.000	0.000	0.000	0.000
65	A	63	SER	0	-0.067	-0.047	37.659	-0.012	-0.012	0.000	0.000	0.000	0.000
66	A	64	ILE	0	0.053	0.018	36.328	0.004	0.004	0.000	0.000	0.000	0.000
67	A	65	VAL	0	0.023	0.030	34.706	0.016	0.016	0.000	0.000	0.000	0.000
68	A	66	LYS	1	0.973	0.973	36.988	-0.061	-0.061	0.000	0.000	0.000	0.000
69	A	67	SER	0	-0.017	0.008	39.506	0.011	0.011	0.000	0.000	0.000	0.000
70	A	68	LEU	0	0.010	-0.001	31.789	0.013	0.013	0.000	0.000	0.000	0.000
71	A	69	ILE	0	0.001	-0.008	34.652	0.023	0.023	0.000	0.000	0.000	0.000
72	A	70	GLY	0	-0.017	0.004	35.853	0.010	0.010	0.000	0.000	0.000	0.000
73	A	71	ALA	0	-0.032	-0.005	35.403	0.013	0.013	0.000	0.000	0.000	0.000
74	A	72	ALA	0	-0.010	-0.018	30.442	0.035	0.035	0.000	0.000	0.000	0.000
75	A	73	ARG	1	0.938	0.973	24.667	-0.515	-0.515	0.000	0.000	0.000	0.000
76	A	74	THR	0	0.073	0.026	29.325	0.014	0.014	0.000	0.000	0.000	0.000
77	A	75	LYS	1	0.865	0.949	28.970	-0.168	-0.168	0.000	0.000	0.000	0.000
78	A	76	THR	0	-0.062	-0.021	23.247	0.036	0.036	0.000	0.000	0.000	0.000
79	A	77	TYR	0	0.016	-0.009	23.158	-0.047	-0.047	0.000	0.000	0.000	0.000
80	A	78	VAL	0	0.013	0.006	19.543	0.061	0.061	0.000	0.000	0.000	0.000
81	A	79	GLN	0	-0.006	0.013	18.777	0.050	0.050	0.000	0.000	0.000	0.000
82	A	80	GLU	-1	-0.869	-0.963	18.673	-0.208	-0.208	0.000	0.000	0.000	0.000
83	A	81	HIS	0	-0.047	-0.015	18.398	0.059	0.059	0.000	0.000	0.000	0.000
84	A	82	SER	0	0.000	-0.005	19.733	-0.074	-0.074	0.000	0.000	0.000	0.000
85	A	83	VAL	0	-0.005	-0.005	20.908	0.064	0.064	0.000	0.000	0.000	0.000
86	A	84	VAL	0	-0.013	-0.007	23.431	-0.069	-0.069	0.000	0.000	0.000	0.000
87	A	85	ASP	-1	-0.766	-0.873	26.107	-0.309	-0.309	0.000	0.000	0.000	0.000
88	A	86	PRO	0	-0.011	-0.019	27.848	-0.024	-0.024	0.000	0.000	0.000	0.000
89	A	87	VAL	0	-0.046	-0.026	30.831	0.009	0.009	0.000	0.000	0.000	0.000
90	A	88	GLU	-1	-0.950	-0.985	26.315	-0.511	-0.511	0.000	0.000	0.000	0.000
91	A	89	LYS	1	0.791	0.902	29.010	0.281	0.281	0.000	0.000	0.000	0.000
92	A	90	THR	0	0.023	0.007	24.089	-0.047	-0.047	0.000	0.000	0.000	0.000
93	A	91	MET	0	-0.036	-0.007	24.702	0.059	0.059	0.000	0.000	0.000	0.000
94	A	92	GLU	-1	-0.799	-0.872	16.942	-0.936	-0.936	0.000	0.000	0.000	0.000
95	A	93	LEU	0	-0.003	-0.010	19.440	0.110	0.110	0.000	0.000	0.000	0.000
96	A	94	LYS	1	0.891	0.942	13.076	0.542	0.542	0.000	0.000	0.000	0.000
97	A	95	SER	0	0.005	0.005	16.180	0.125	0.125	0.000	0.000	0.000	0.000
98	A	96	THR	0	0.020	-0.002	13.041	-0.134	-0.134	0.000	0.000	0.000	0.000
99	A	97	ASN	0	-0.023	-0.005	15.281	0.015	0.015	0.000	0.000	0.000	0.000
100	A	98	ILE	0	0.061	0.015	16.450	0.129	0.129	0.000	0.000	0.000	0.000
101	A	99	SER	0	-0.066	-0.030	18.840	0.045	0.045	0.000	0.000	0.000	0.000
102	A	100	PHE	0	0.001	-0.015	18.579	0.006	0.006	0.000	0.000	0.000	0.000
103	A	101	THR	0	0.056	0.035	13.019	0.066	0.066	0.000	0.000	0.000	0.000
104	A	102	ASN	0	-0.013	-0.006	13.557	0.281	0.281	0.000	0.000	0.000	0.000
105	A	103	MET	0	-0.080	-0.040	14.873	0.244	0.244	0.000	0.000	0.000	0.000
106	A	104	VAL	0	0.011	-0.005	13.075	0.021	0.021	0.000	0.000	0.000	0.000
107	A	105	SER	0	-0.052	-0.025	10.257	0.010	0.010	0.000	0.000	0.000	0.000
108	A	106	VAL	0	-0.041	-0.025	11.111	-0.191	-0.191	0.000	0.000	0.000	0.000
109	A	107	ASP	-1	-0.804	-0.871	10.440	0.292	0.292	0.000	0.000	0.000	0.000
110	A	108	GLU	-1	-0.911	-0.961	12.515	-1.074	-1.074	0.000	0.000	0.000	0.000
111	A	109	ARG	1	0.770	0.867	13.549	1.629	1.629	0.000	0.000	0.000	0.000
112	A	110	LEU	0	0.016	0.009	15.735	-0.126	-0.126	0.000	0.000	0.000	0.000
113	A	111	ILE	0	-0.010	-0.013	17.643	0.045	0.045	0.000	0.000	0.000	0.000
114	A	112	TYR	0	0.027	0.021	21.284	-0.026	-0.026	0.000	0.000	0.000	0.000
115	A	113	LYS	1	0.922	0.945	24.993	0.700	0.700	0.000	0.000	0.000	0.000
116	A	114	PRO	0	0.060	0.037	27.428	-0.012	-0.012	0.000	0.000	0.000	0.000
117	A	115	HIS	0	0.032	0.026	29.760	-0.045	-0.045	0.000	0.000	0.000	0.000
118	A	116	PRO	0	-0.063	-0.044	28.637	0.028	0.028	0.000	0.000	0.000	0.000
119	A	117	GLN	0	-0.035	-0.021	31.613	0.029	0.029	0.000	0.000	0.000	0.000
120	A	118	ASP	-1	-0.828	-0.917	34.371	-0.363	-0.363	0.000	0.000	0.000	0.000
121	A	119	PRO	0	-0.023	-0.017	34.871	-0.014	-0.014	0.000	0.000	0.000	0.000
122	A	120	GLU	-1	-0.910	-0.951	35.522	-0.296	-0.296	0.000	0.000	0.000	0.000
123	A	121	LYS	1	0.809	0.908	33.384	0.412	0.412	0.000	0.000	0.000	0.000
124	A	122	THR	0	-0.045	-0.036	28.497	-0.014	-0.014	0.000	0.000	0.000	0.000
125	A	123	VAL	0	-0.023	-0.007	24.951	-0.002	-0.002	0.000	0.000	0.000	0.000
126	A	124	LEU	0	-0.017	-0.007	22.222	0.031	0.031	0.000	0.000	0.000	0.000
127	A	125	THR	0	0.004	0.007	19.735	-0.034	-0.034	0.000	0.000	0.000	0.000
128	A	126	GLN	0	0.000	-0.008	18.431	0.080	0.080	0.000	0.000	0.000	0.000
129	A	127	GLU	-1	-0.840	-0.898	12.644	-2.823	-2.823	0.000	0.000	0.000	0.000
130	A	128	ALA	0	0.046	0.025	13.740	0.257	0.257	0.000	0.000	0.000	0.000
131	A	129	ILE	0	-0.063	-0.040	7.066	-0.754	-0.754	0.000	0.000	0.000	0.000
132	A	130	ILE	0	0.040	0.024	9.788	0.478	0.478	0.000	0.000	0.000	0.000
133	A	131	THR	0	-0.055	-0.006	6.369	-0.114	-0.114	0.000	0.000	0.000	0.000
134	A	132	VAL	0	-0.006	0.001	8.632	0.019	0.019	0.000	0.000	0.000	0.000
135	A	133	LYS	1	0.914	0.946	9.536	-1.885	-1.885	0.000	0.000	0.000	0.000
136	A	134	GLY	0	0.050	0.047	6.303	0.809	0.809	0.000	0.000	0.000	0.000
138	A	136	SER	0	0.047	0.018	6.042	-0.847	-0.847	0.000	0.000	0.000	0.000
139	A	137	LEU	0	0.061	0.016	7.416	0.402	0.402	0.000	0.000	0.000	0.000
140	A	138	SER	0	0.017	0.005	10.757	0.217	0.217	0.000	0.000	0.000	0.000
141	A	139	SER	0	0.053	0.024	8.332	0.614	0.614	0.000	0.000	0.000	0.000
142	A	140	TYR	0	0.016	0.003	10.788	0.302	0.302	0.000	0.000	0.000	0.000
143	A	141	LEU	0	0.016	0.006	12.407	0.018	0.018	0.000	0.000	0.000	0.000
144	A	142	GLU	-1	-0.901	-0.958	13.334	-0.537	-0.537	0.000	0.000	0.000	0.000
145	A	143	GLY	0	0.015	0.009	14.201	0.032	0.032	0.000	0.000	0.000	0.000
146	A	144	LEU	0	-0.029	-0.017	15.189	0.008	0.008	0.000	0.000	0.000	0.000
147	A	145	MET	0	-0.011	0.009	18.130	-0.060	-0.060	0.000	0.000	0.000	0.000
148	A	146	ALA	0	0.033	0.018	17.599	-0.017	-0.017	0.000	0.000	0.000	0.000
149	A	147	SER	0	-0.012	0.013	18.795	-0.043	-0.043	0.000	0.000	0.000	0.000
150	A	148	THR	0	-0.011	-0.027	20.550	-0.070	-0.070	0.000	0.000	0.000	0.000
151	A	149	ILE	0	0.013	0.009	23.129	-0.036	-0.036	0.000	0.000	0.000	0.000
152	A	150	SER	0	-0.037	-0.032	22.159	-0.012	-0.012	0.000	0.000	0.000	0.000
153	A	151	SER	0	0.020	0.011	24.571	-0.036	-0.036	0.000	0.000	0.000	0.000
154	A	152	ASN	0	0.023	-0.002	26.410	0.004	0.004	0.000	0.000	0.000	0.000
155	A	153	ALA	0	0.021	0.017	27.763	-0.027	-0.027	0.000	0.000	0.000	0.000
156	A	154	SER	0	-0.031	-0.020	28.699	-0.025	-0.025	0.000	0.000	0.000	0.000
157	A	155	LYS	1	0.927	0.974	28.267	-0.427	-0.427	0.000	0.000	0.000	0.000
158	A	156	GLY	0	0.000	0.004	32.529	-0.019	-0.019	0.000	0.000	0.000	0.000
159	A	157	ARG	1	0.913	0.947	27.940	-0.338	-0.338	0.000	0.000	0.000	0.000
160	A	158	GLU	-1	-0.911	-0.950	33.303	0.348	0.348	0.000	0.000	0.000	0.000
161	A	159	ALA	0	-0.016	-0.009	36.537	-0.013	-0.013	0.000	0.000	0.000	0.000
162	A	160	MET	0	-0.021	-0.009	37.931	-0.019	-0.019	0.000	0.000	0.000	0.000
163	A	161	GLU	-1	-0.894	-0.949	38.191	0.196	0.196	0.000	0.000	0.000	0.000
164	A	162	TRP	0	-0.043	-0.013	40.640	-0.014	-0.014	0.000	0.000	0.000	0.000
165	A	163	VAL	0	-0.032	-0.024	42.522	-0.010	-0.010	0.000	0.000	0.000	0.000
166	A	164	ILE	0	0.010	0.007	41.415	-0.011	-0.011	0.000	0.000	0.000	0.000
167	A	165	HIS	0	0.002	0.002	44.606	-0.006	-0.006	0.000	0.000	0.000	0.000
168	A	166	LYS	1	0.942	0.964	46.447	-0.127	-0.127	0.000	0.000	0.000	0.000
169	A	167	LEU	0	-0.020	-0.010	48.075	-0.006	-0.006	0.000	0.000	0.000	0.000
170	A	168	ASN	0	-0.044	-0.032	48.641	-0.006	-0.006	0.000	0.000	0.000	0.000
171	A	169	ALA	0	-0.032	-0.008	50.568	0.001	0.001	0.000	0.000	0.000	0.000
172	A	170	GLU	-1	-1.057	-1.015	52.659	0.086	0.086	0.000	0.000	0.000	0.000
173	A	171	ILE	-1	-0.973	-0.975	54.314	0.091	0.091	0.000	0.000	0.000	0.000

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