FMO DATABASE

FMODB ID: QM2RY

Calculation Name: 6JEX-A-Xray547

Preferred Name:

Target Type:

Ligand Name: l-[(n-hydroxyamino)carbonyl]phenylalanine | zinc ion

Ligand 3-letter code: LHY | ZN

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 6JEX

Chain ID: A

ChEMBL ID:

UniProt ID:

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	172
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1809252.186782
FMO2-HF: Nuclear repulsion	1740357.206498
FMO2-HF: Total energy	-68894.980284
FMO2-MP2: Total energy	-69094.650012

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:ALA)

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

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.
-165.585	-162.802	0.124	-1.718	-1.188	-0.011

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.804 / q_NPA : 0.889

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	LEU	0	0.022	0.016	3.046	-18.184	-15.401	0.124	-1.718	-1.188	-0.011
4	A	5	PRO	0	-0.048	-0.020	5.796	1.866	1.866	0.000	0.000	0.000	0.000
5	A	6	ILE	0	0.046	0.020	7.668	2.356	2.356	0.000	0.000	0.000	0.000
6	A	7	LEU	0	-0.065	-0.018	11.015	0.541	0.541	0.000	0.000	0.000	0.000
7	A	8	SER	0	0.024	0.010	14.081	0.464	0.464	0.000	0.000	0.000	0.000
8	A	9	PHE	0	0.012	0.017	16.477	0.781	0.781	0.000	0.000	0.000	0.000
9	A	10	PRO	0	-0.089	-0.062	20.233	-0.037	-0.037	0.000	0.000	0.000	0.000
10	A	11	ASP	-1	-0.740	-0.862	16.914	-17.538	-17.538	0.000	0.000	0.000	0.000
11	A	12	PRO	0	-0.001	-0.008	19.799	0.212	0.212	0.000	0.000	0.000	0.000
12	A	13	ARG	1	0.790	0.866	14.048	20.572	20.572	0.000	0.000	0.000	0.000
13	A	14	LEU	0	-0.003	0.005	17.247	0.031	0.031	0.000	0.000	0.000	0.000
14	A	15	ARG	1	0.671	0.799	20.403	12.915	12.915	0.000	0.000	0.000	0.000
15	A	16	THR	0	-0.060	-0.029	20.833	0.788	0.788	0.000	0.000	0.000	0.000
16	A	17	ILE	0	-0.025	-0.003	23.133	-0.163	-0.163	0.000	0.000	0.000	0.000
17	A	18	ALA	0	0.002	0.009	21.881	-0.107	-0.107	0.000	0.000	0.000	0.000
18	A	19	LYS	1	0.817	0.906	22.876	13.635	13.635	0.000	0.000	0.000	0.000
19	A	20	PRO	0	0.000	-0.013	23.371	-0.567	-0.567	0.000	0.000	0.000	0.000
20	A	21	VAL	0	-0.004	0.002	20.963	-0.269	-0.269	0.000	0.000	0.000	0.000
21	A	22	GLU	-1	-0.858	-0.916	23.636	-12.011	-12.011	0.000	0.000	0.000	0.000
22	A	23	GLU	-1	-0.912	-0.960	24.664	-10.835	-10.835	0.000	0.000	0.000	0.000
23	A	24	VAL	0	-0.050	-0.014	21.856	-0.658	-0.658	0.000	0.000	0.000	0.000
24	A	25	THR	0	0.019	-0.013	20.462	0.092	0.092	0.000	0.000	0.000	0.000
25	A	26	ASP	-1	-0.825	-0.925	17.937	-16.032	-16.032	0.000	0.000	0.000	0.000
26	A	27	GLU	-1	-0.871	-0.912	15.153	-17.768	-17.768	0.000	0.000	0.000	0.000
27	A	28	ILE	0	-0.074	-0.036	14.856	-1.414	-1.414	0.000	0.000	0.000	0.000
28	A	29	ARG	1	0.851	0.922	16.122	13.846	13.846	0.000	0.000	0.000	0.000
29	A	30	GLN	0	-0.058	-0.027	8.971	1.505	1.505	0.000	0.000	0.000	0.000
30	A	31	LEU	0	-0.024	-0.006	11.498	-1.848	-1.848	0.000	0.000	0.000	0.000
31	A	32	ALA	0	0.045	0.010	12.373	-1.139	-1.139	0.000	0.000	0.000	0.000
32	A	33	ALA	0	0.026	0.023	11.619	-0.136	-0.136	0.000	0.000	0.000	0.000
33	A	34	ASP	-1	-0.855	-0.924	7.401	-38.867	-38.867	0.000	0.000	0.000	0.000
34	A	35	MET	0	-0.081	-0.018	8.811	-2.447	-2.447	0.000	0.000	0.000	0.000
35	A	36	PHE	0	0.032	0.019	11.506	0.240	0.240	0.000	0.000	0.000	0.000
36	A	37	GLU	-1	-0.910	-0.956	7.058	-29.993	-29.993	0.000	0.000	0.000	0.000
37	A	38	THR	0	-0.068	-0.061	7.663	-3.045	-3.045	0.000	0.000	0.000	0.000
38	A	39	MET	0	-0.052	-0.002	8.847	1.261	1.261	0.000	0.000	0.000	0.000
39	A	40	TYR	0	-0.046	-0.076	11.184	0.683	0.683	0.000	0.000	0.000	0.000
40	A	41	ALA	0	-0.037	-0.016	7.812	1.038	1.038	0.000	0.000	0.000	0.000
41	A	42	ALA	0	-0.070	-0.003	9.757	0.592	0.592	0.000	0.000	0.000	0.000
42	A	43	PRO	0	-0.031	-0.008	11.506	0.743	0.743	0.000	0.000	0.000	0.000
43	A	44	GLY	0	-0.034	-0.043	13.912	0.941	0.941	0.000	0.000	0.000	0.000
44	A	45	ILE	0	0.037	0.022	16.500	-0.360	-0.360	0.000	0.000	0.000	0.000
45	A	46	GLY	0	0.026	0.001	18.239	0.684	0.684	0.000	0.000	0.000	0.000
46	A	47	LEU	0	-0.038	-0.016	12.179	-1.089	-1.089	0.000	0.000	0.000	0.000
47	A	48	ALA	0	0.069	0.044	16.718	0.056	0.056	0.000	0.000	0.000	0.000
48	A	49	ALA	0	0.014	-0.005	15.150	-1.000	-1.000	0.000	0.000	0.000	0.000
49	A	50	SER	0	0.009	-0.019	15.173	-1.101	-1.101	0.000	0.000	0.000	0.000
50	A	51	GLN	0	0.024	-0.008	14.919	-0.120	-0.120	0.000	0.000	0.000	0.000
51	A	52	VAL	0	-0.033	-0.011	10.277	-1.291	-1.291	0.000	0.000	0.000	0.000
52	A	53	ASP	-1	-0.819	-0.894	11.737	-21.035	-21.035	0.000	0.000	0.000	0.000
53	A	54	ARG	1	0.922	0.979	12.270	22.853	22.853	0.000	0.000	0.000	0.000
54	A	55	HIS	0	0.020	-0.007	15.244	0.941	0.941	0.000	0.000	0.000	0.000
55	A	56	ILE	0	-0.020	-0.009	18.114	0.941	0.941	0.000	0.000	0.000	0.000
56	A	57	GLN	0	-0.029	-0.022	20.027	-0.208	-0.208	0.000	0.000	0.000	0.000
57	A	58	LEU	0	0.026	0.005	16.285	0.470	0.470	0.000	0.000	0.000	0.000
58	A	59	ILE	0	-0.010	-0.005	18.857	-0.670	-0.670	0.000	0.000	0.000	0.000
59	A	60	VAL	0	-0.014	0.004	14.695	0.507	0.507	0.000	0.000	0.000	0.000
60	A	61	MET	0	-0.003	-0.020	18.164	0.260	0.260	0.000	0.000	0.000	0.000
61	A	62	ASP	-1	-0.739	-0.812	18.267	-15.722	-15.722	0.000	0.000	0.000	0.000
62	A	63	LEU	0	-0.025	-0.024	20.139	-0.109	-0.109	0.000	0.000	0.000	0.000
63	A	64	SER	0	-0.049	-0.026	20.944	0.484	0.484	0.000	0.000	0.000	0.000
64	A	65	GLU	-1	-0.980	-0.995	21.457	-12.147	-12.147	0.000	0.000	0.000	0.000
65	A	66	SER	0	-0.056	-0.034	20.697	-0.235	-0.235	0.000	0.000	0.000	0.000
66	A	67	LYS	1	0.813	0.931	11.300	22.743	22.743	0.000	0.000	0.000	0.000
67	A	68	ASP	-1	-0.874	-0.956	17.679	-14.004	-14.004	0.000	0.000	0.000	0.000
68	A	69	GLU	-1	-0.922	-0.949	20.453	-11.669	-11.669	0.000	0.000	0.000	0.000
69	A	70	PRO	0	-0.056	-0.017	17.825	-0.204	-0.204	0.000	0.000	0.000	0.000
70	A	71	MET	0	-0.016	-0.015	19.781	0.699	0.699	0.000	0.000	0.000	0.000
71	A	72	VAL	0	-0.019	-0.027	18.983	-0.880	-0.880	0.000	0.000	0.000	0.000
72	A	73	PHE	0	-0.004	-0.009	21.580	0.826	0.826	0.000	0.000	0.000	0.000
73	A	74	ILE	0	0.001	-0.002	20.774	-0.636	-0.636	0.000	0.000	0.000	0.000
74	A	75	ASN	0	-0.022	-0.017	23.981	0.222	0.222	0.000	0.000	0.000	0.000
75	A	76	PRO	0	0.005	0.011	24.996	0.454	0.454	0.000	0.000	0.000	0.000
76	A	77	LYS	1	0.929	0.963	27.944	9.801	9.801	0.000	0.000	0.000	0.000
77	A	78	VAL	0	0.024	0.010	30.502	-0.087	-0.087	0.000	0.000	0.000	0.000
78	A	79	THR	0	-0.010	-0.012	32.443	0.199	0.199	0.000	0.000	0.000	0.000
79	A	80	PRO	0	-0.008	0.009	36.140	-0.031	-0.031	0.000	0.000	0.000	0.000
80	A	81	LEU	0	-0.033	-0.016	37.716	0.210	0.210	0.000	0.000	0.000	0.000
81	A	82	THR	0	-0.022	-0.018	39.845	0.281	0.281	0.000	0.000	0.000	0.000
82	A	83	GLU	-1	-0.951	-0.971	40.688	-7.324	-7.324	0.000	0.000	0.000	0.000
83	A	84	GLU	-1	-0.972	-0.974	41.193	-7.722	-7.722	0.000	0.000	0.000	0.000
84	A	85	THR	0	-0.046	-0.033	37.516	-0.136	-0.136	0.000	0.000	0.000	0.000
85	A	86	GLN	0	-0.026	-0.023	32.908	0.099	0.099	0.000	0.000	0.000	0.000
86	A	87	PRO	0	0.007	0.011	34.886	-0.256	-0.256	0.000	0.000	0.000	0.000
87	A	88	TYR	0	-0.012	-0.013	26.661	-0.159	-0.159	0.000	0.000	0.000	0.000
88	A	89	GLU	-1	-0.797	-0.878	27.892	-10.473	-10.473	0.000	0.000	0.000	0.000
89	A	90	GLU	-1	-0.725	-0.828	25.838	-12.252	-12.252	0.000	0.000	0.000	0.000
90	A	91	GLY	0	0.041	0.004	22.837	0.215	0.215	0.000	0.000	0.000	0.000
91	A	92	CYS	-1	-0.935	-0.844	19.555	-16.483	-16.483	0.000	0.000	0.000	0.000
92	A	93	LEU	0	0.045	0.029	13.582	-0.168	-0.168	0.000	0.000	0.000	0.000
93	A	94	SER	0	0.034	-0.019	15.278	-0.966	-0.966	0.000	0.000	0.000	0.000
94	A	95	VAL	0	-0.101	-0.053	17.067	0.705	0.705	0.000	0.000	0.000	0.000
95	A	96	PRO	0	0.049	0.032	16.069	0.574	0.574	0.000	0.000	0.000	0.000
96	A	97	GLN	0	0.001	-0.015	17.756	1.115	1.115	0.000	0.000	0.000	0.000
97	A	98	ILE	0	-0.089	-0.034	20.898	0.956	0.956	0.000	0.000	0.000	0.000
98	A	99	TYR	0	0.043	0.019	21.301	-0.521	-0.521	0.000	0.000	0.000	0.000
99	A	100	ASP	-1	-0.900	-0.948	26.272	-9.635	-9.635	0.000	0.000	0.000	0.000
100	A	101	LYS	1	0.772	0.864	29.526	9.837	9.837	0.000	0.000	0.000	0.000
101	A	102	VAL	0	-0.045	-0.020	29.056	0.105	0.105	0.000	0.000	0.000	0.000
102	A	103	ASP	-1	-0.810	-0.890	32.162	-8.745	-8.745	0.000	0.000	0.000	0.000
103	A	104	ARG	1	0.781	0.849	27.343	11.172	11.172	0.000	0.000	0.000	0.000
104	A	105	PRO	0	-0.003	-0.002	34.444	0.132	0.132	0.000	0.000	0.000	0.000
105	A	106	SER	0	0.019	0.000	35.035	-0.270	-0.270	0.000	0.000	0.000	0.000
106	A	107	ARG	1	0.840	0.915	35.820	7.923	7.923	0.000	0.000	0.000	0.000
107	A	108	VAL	0	-0.026	-0.015	32.142	0.152	0.152	0.000	0.000	0.000	0.000
108	A	109	LYS	1	0.829	0.896	35.234	8.685	8.685	0.000	0.000	0.000	0.000
109	A	110	ILE	0	-0.016	-0.020	28.822	-0.171	-0.171	0.000	0.000	0.000	0.000
110	A	111	GLU	-1	-0.848	-0.910	31.940	-8.976	-8.976	0.000	0.000	0.000	0.000
111	A	112	ALA	0	-0.024	-0.009	26.863	-0.318	-0.318	0.000	0.000	0.000	0.000
112	A	113	ILE	0	-0.007	0.009	25.755	0.407	0.407	0.000	0.000	0.000	0.000
113	A	114	ASN	0	0.077	0.033	24.481	-0.533	-0.533	0.000	0.000	0.000	0.000
114	A	115	LEU	0	0.031	-0.010	18.621	0.010	0.010	0.000	0.000	0.000	0.000
115	A	116	GLU	-1	-0.899	-0.940	22.457	-13.038	-13.038	0.000	0.000	0.000	0.000
116	A	117	GLY	0	-0.044	-0.017	25.584	0.421	0.421	0.000	0.000	0.000	0.000
117	A	118	GLN	0	-0.054	-0.023	27.411	0.631	0.631	0.000	0.000	0.000	0.000
118	A	119	ALA	0	0.013	0.000	29.018	-0.338	-0.338	0.000	0.000	0.000	0.000
119	A	120	PHE	0	-0.038	-0.020	26.573	0.265	0.265	0.000	0.000	0.000	0.000
120	A	121	GLU	-1	-0.849	-0.925	32.122	-8.764	-8.764	0.000	0.000	0.000	0.000
121	A	122	ILE	0	-0.020	-0.002	29.772	0.093	0.093	0.000	0.000	0.000	0.000
122	A	123	GLU	-1	-0.863	-0.924	34.210	-8.248	-8.248	0.000	0.000	0.000	0.000
123	A	124	ALA	0	-0.004	-0.005	31.618	-0.156	-0.156	0.000	0.000	0.000	0.000
124	A	125	ASP	-1	-0.854	-0.929	33.644	-9.014	-9.014	0.000	0.000	0.000	0.000
125	A	126	GLY	0	0.033	0.021	32.164	-0.342	-0.342	0.000	0.000	0.000	0.000
126	A	127	LEU	0	0.016	0.000	25.141	-0.024	-0.024	0.000	0.000	0.000	0.000
127	A	128	LEU	0	0.048	0.029	26.611	-0.393	-0.393	0.000	0.000	0.000	0.000
128	A	129	ALA	0	0.022	0.025	28.563	-0.245	-0.245	0.000	0.000	0.000	0.000
129	A	130	VAL	0	0.004	0.010	27.359	-0.109	-0.109	0.000	0.000	0.000	0.000
130	A	131	CYS	0	-0.031	-0.005	22.945	-0.413	-0.413	0.000	0.000	0.000	0.000
131	A	132	ILE	0	0.045	0.015	24.858	-0.422	-0.422	0.000	0.000	0.000	0.000
132	A	133	GLN	0	-0.046	-0.045	26.590	0.085	0.085	0.000	0.000	0.000	0.000
133	A	134	HIS	1	0.765	0.828	20.955	14.165	14.165	0.000	0.000	0.000	0.000
134	A	135	GLU	-1	-0.817	-0.939	19.962	-16.308	-16.308	0.000	0.000	0.000	0.000
135	A	136	MET	0	0.005	0.004	22.971	-0.269	-0.269	0.000	0.000	0.000	0.000
136	A	137	ASP	-1	-0.780	-0.836	25.939	-11.037	-11.037	0.000	0.000	0.000	0.000
137	A	138	HIS	0	0.027	-0.011	19.777	0.216	0.216	0.000	0.000	0.000	0.000
138	A	139	LEU	0	-0.040	0.005	21.078	-0.268	-0.268	0.000	0.000	0.000	0.000
139	A	140	ASN	0	-0.069	-0.044	23.496	0.543	0.543	0.000	0.000	0.000	0.000
140	A	141	GLY	0	0.033	0.049	23.767	0.442	0.442	0.000	0.000	0.000	0.000
141	A	142	LYS	1	0.809	0.880	24.827	11.012	11.012	0.000	0.000	0.000	0.000
142	A	143	LEU	0	0.050	0.012	21.362	-0.542	-0.542	0.000	0.000	0.000	0.000
143	A	144	PHE	0	0.054	0.028	22.686	0.521	0.521	0.000	0.000	0.000	0.000
144	A	145	VAL	0	0.002	-0.008	24.933	0.518	0.518	0.000	0.000	0.000	0.000
145	A	146	ASP	-1	-0.803	-0.863	27.444	-11.393	-11.393	0.000	0.000	0.000	0.000
146	A	147	TYR	0	-0.034	-0.029	29.116	0.558	0.558	0.000	0.000	0.000	0.000
147	A	148	LEU	0	-0.008	0.025	28.765	0.338	0.338	0.000	0.000	0.000	0.000
148	A	149	SER	0	0.030	0.010	32.612	0.024	0.024	0.000	0.000	0.000	0.000
149	A	150	PRO	0	0.043	0.003	33.191	-0.287	-0.287	0.000	0.000	0.000	0.000
150	A	151	LEU	0	0.036	0.018	32.571	-0.301	-0.301	0.000	0.000	0.000	0.000
151	A	152	LYS	1	0.897	0.958	31.034	9.349	9.349	0.000	0.000	0.000	0.000
152	A	153	ARG	1	0.923	0.957	27.852	9.925	9.925	0.000	0.000	0.000	0.000
153	A	154	GLN	0	-0.030	-0.017	27.929	-0.280	-0.280	0.000	0.000	0.000	0.000
154	A	155	ARG	1	0.972	0.974	28.153	9.883	9.883	0.000	0.000	0.000	0.000
155	A	156	ALA	0	0.019	0.011	25.101	-0.302	-0.302	0.000	0.000	0.000	0.000
156	A	157	ARG	1	0.949	0.982	23.787	10.866	10.866	0.000	0.000	0.000	0.000
157	A	158	GLU	-1	-0.892	-0.932	23.602	-11.317	-11.317	0.000	0.000	0.000	0.000
158	A	159	LYS	1	0.893	0.954	22.692	13.106	13.106	0.000	0.000	0.000	0.000
159	A	160	VAL	0	0.017	0.017	18.488	-0.441	-0.441	0.000	0.000	0.000	0.000
160	A	161	GLU	-1	-0.785	-0.874	19.173	-16.293	-16.293	0.000	0.000	0.000	0.000
161	A	162	LYS	1	0.822	0.892	20.025	11.519	11.519	0.000	0.000	0.000	0.000
162	A	163	ILE	0	-0.018	-0.007	16.459	-0.251	-0.251	0.000	0.000	0.000	0.000
163	A	164	VAL	0	0.023	0.015	14.777	-0.953	-0.953	0.000	0.000	0.000	0.000
164	A	165	ARG	1	0.888	0.912	15.487	13.534	13.534	0.000	0.000	0.000	0.000
165	A	166	GLN	0	-0.040	-0.004	17.869	0.682	0.682	0.000	0.000	0.000	0.000
166	A	167	ARG	1	0.998	0.996	12.208	21.916	21.916	0.000	0.000	0.000	0.000
167	A	168	GLU	-1	-0.866	-0.917	12.151	-27.109	-27.109	0.000	0.000	0.000	0.000
168	A	169	ARG	1	0.874	0.929	14.095	15.163	15.163	0.000	0.000	0.000	0.000
169	A	170	GLU	-1	-0.918	-0.967	12.439	-19.703	-19.703	0.000	0.000	0.000	0.000
170	A	171	LYS	1	0.764	0.872	7.760	27.516	27.516	0.000	0.000	0.000	0.000
171	A	172	VAL	0	-0.095	-0.044	11.969	-0.441	-0.441	0.000	0.000	0.000	0.000
172	A	173	ALA	-1	-0.942	-0.944	14.432	-18.931	-18.931	0.000	0.000	0.000	0.000

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