FMO DATABASE

FMODB ID: VVZN1

Calculation Name: 1ELP-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1ELP

Chain ID: A

ChEMBL ID:

UniProt ID: P08209

Base Structure: X-ray

Registration Date: 2025-09-02

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	-2025282.558427
FMO2-HF: Nuclear repulsion	1951485.163422
FMO2-HF: Total energy	-73797.395005
FMO2-MP2: Total energy	-74010.010056

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:GLY)

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

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.
-106.986	-99.46	6.659	-7.362	-6.826	-0.074

Interaction energy analysis for fragmet #1(A:1:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.819 / q_NPA : 0.910

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	3	ILE	0	0.009	0.020	3.831	4.730	6.064	-0.018	-0.621	-0.695	-0.003
19	A	19	SER	0	0.057	0.014	3.949	-3.018	-2.809	-0.001	-0.076	-0.132	0.000
20	A	20	SER	0	-0.031	-0.013	3.093	-16.368	-15.082	0.037	-0.833	-0.491	-0.008
39	A	39	SER	0	-0.011	-0.011	2.444	-10.368	-9.183	1.768	-1.622	-1.331	-0.017
40	A	40	GLY	0	-0.001	0.014	2.496	-20.414	-18.366	2.435	-2.703	-1.780	-0.027
41	A	41	CYS	0	-0.057	-0.026	3.554	8.861	8.767	0.009	0.047	0.038	0.000
42	A	42	TRP	0	0.005	-0.010	3.086	-3.791	-2.956	0.081	-0.322	-0.595	-0.002
80	A	80	LEU	0	0.007	0.022	2.121	-6.165	-5.442	2.348	-1.232	-1.840	-0.017
4	A	4	THR	0	0.015	0.008	6.750	0.911	0.911	0.000	0.000	0.000	0.000
5	A	5	PHE	0	0.023	-0.009	10.072	0.867	0.867	0.000	0.000	0.000	0.000
6	A	6	TYR	0	0.050	0.011	13.340	-0.200	-0.200	0.000	0.000	0.000	0.000
7	A	7	GLU	-1	-0.783	-0.884	16.929	-13.992	-13.992	0.000	0.000	0.000	0.000
8	A	8	ASP	-1	-0.826	-0.895	20.234	-12.496	-12.496	0.000	0.000	0.000	0.000
9	A	9	ARG	1	0.980	0.987	20.186	11.522	11.522	0.000	0.000	0.000	0.000
10	A	10	GLY	0	-0.022	-0.012	20.669	0.330	0.330	0.000	0.000	0.000	0.000
11	A	11	PHE	0	-0.040	-0.031	15.236	0.299	0.299	0.000	0.000	0.000	0.000
12	A	12	GLN	0	-0.034	0.000	18.578	0.345	0.345	0.000	0.000	0.000	0.000
13	A	13	GLY	0	0.044	0.021	20.678	-0.378	-0.378	0.000	0.000	0.000	0.000
14	A	14	ARG	1	0.818	0.906	20.129	14.597	14.597	0.000	0.000	0.000	0.000
15	A	15	HIS	0	0.003	0.001	15.619	-1.045	-1.045	0.000	0.000	0.000	0.000
16	A	16	TYR	0	-0.009	-0.020	12.602	0.759	0.759	0.000	0.000	0.000	0.000
17	A	17	GLU	-1	-0.819	-0.886	8.643	-34.526	-34.526	0.000	0.000	0.000	0.000
18	A	18	CYS	0	-0.064	-0.022	7.848	2.388	2.388	0.000	0.000	0.000	0.000
21	A	21	ASP	-1	-0.789	-0.905	5.660	-30.395	-30.395	0.000	0.000	0.000	0.000
22	A	22	HIS	0	0.014	0.015	8.704	2.681	2.681	0.000	0.000	0.000	0.000
23	A	23	SER	0	0.016	0.016	11.818	0.339	0.339	0.000	0.000	0.000	0.000
24	A	24	ASN	0	0.063	0.007	15.282	1.192	1.192	0.000	0.000	0.000	0.000
25	A	25	LEU	0	0.015	0.004	12.225	-0.156	-0.156	0.000	0.000	0.000	0.000
26	A	26	GLN	0	0.018	0.007	16.332	0.674	0.674	0.000	0.000	0.000	0.000
27	A	27	PRO	0	-0.033	-0.010	18.721	0.494	0.494	0.000	0.000	0.000	0.000
28	A	28	TYR	0	-0.015	-0.004	16.186	0.667	0.667	0.000	0.000	0.000	0.000
29	A	29	LEU	0	-0.036	-0.011	15.134	-0.101	-0.101	0.000	0.000	0.000	0.000
30	A	30	GLY	0	-0.013	-0.010	18.937	0.165	0.165	0.000	0.000	0.000	0.000
31	A	31	ARG	1	0.776	0.883	20.783	13.798	13.798	0.000	0.000	0.000	0.000
32	A	32	CYS	0	-0.061	-0.024	15.180	-0.973	-0.973	0.000	0.000	0.000	0.000
33	A	33	ASN	0	-0.042	-0.044	18.461	0.533	0.533	0.000	0.000	0.000	0.000
34	A	34	SER	0	-0.044	-0.021	17.080	0.269	0.269	0.000	0.000	0.000	0.000
35	A	35	VAL	0	0.000	-0.004	10.740	-0.560	-0.560	0.000	0.000	0.000	0.000
36	A	36	ARG	1	0.852	0.931	10.277	22.779	22.779	0.000	0.000	0.000	0.000
37	A	37	VAL	0	-0.027	-0.004	5.418	-2.405	-2.405	0.000	0.000	0.000	0.000
38	A	38	ASP	-1	-0.890	-0.947	6.195	-30.044	-30.044	0.000	0.000	0.000	0.000
43	A	43	MET	0	-0.054	0.006	7.505	3.089	3.089	0.000	0.000	0.000	0.000
44	A	44	ILE	0	-0.019	-0.007	10.597	-1.569	-1.569	0.000	0.000	0.000	0.000
45	A	45	TYR	0	0.036	0.008	12.894	0.477	0.477	0.000	0.000	0.000	0.000
46	A	46	GLU	-1	-0.775	-0.874	16.434	-13.331	-13.331	0.000	0.000	0.000	0.000
47	A	47	GLN	0	-0.031	-0.030	19.724	0.422	0.422	0.000	0.000	0.000	0.000
48	A	48	PRO	0	0.033	0.014	18.548	-0.983	-0.983	0.000	0.000	0.000	0.000
49	A	49	ASN	0	-0.061	-0.045	17.633	-0.131	-0.131	0.000	0.000	0.000	0.000
50	A	50	TYR	0	-0.012	-0.012	12.571	-0.021	-0.021	0.000	0.000	0.000	0.000
51	A	51	LEU	0	0.015	0.029	17.088	0.469	0.469	0.000	0.000	0.000	0.000
52	A	52	GLY	0	0.037	0.012	20.185	-0.297	-0.297	0.000	0.000	0.000	0.000
53	A	53	PRO	0	-0.058	-0.031	21.112	-0.345	-0.345	0.000	0.000	0.000	0.000
54	A	54	GLN	0	0.047	0.031	16.566	-1.418	-1.418	0.000	0.000	0.000	0.000
55	A	55	TYR	0	0.002	0.007	15.074	1.109	1.109	0.000	0.000	0.000	0.000
56	A	56	PHE	0	0.026	-0.003	10.355	-1.423	-1.423	0.000	0.000	0.000	0.000
57	A	57	LEU	0	-0.023	-0.002	9.716	1.167	1.167	0.000	0.000	0.000	0.000
58	A	58	ARG	1	0.859	0.911	7.875	21.844	21.844	0.000	0.000	0.000	0.000
59	A	59	ARG	1	0.899	0.973	7.043	33.271	33.271	0.000	0.000	0.000	0.000
60	A	60	GLY	0	0.021	0.013	8.078	2.774	2.774	0.000	0.000	0.000	0.000
61	A	61	ASP	-1	-0.843	-0.907	10.925	-22.888	-22.888	0.000	0.000	0.000	0.000
62	A	62	TYR	0	-0.023	-0.034	10.721	1.826	1.826	0.000	0.000	0.000	0.000
63	A	63	PRO	0	0.030	0.011	15.476	-0.070	-0.070	0.000	0.000	0.000	0.000
64	A	64	ASP	-1	-0.848	-0.940	18.689	-13.493	-13.493	0.000	0.000	0.000	0.000
65	A	65	TYR	0	0.049	0.026	18.421	-0.581	-0.581	0.000	0.000	0.000	0.000
66	A	66	GLN	0	-0.012	-0.007	19.343	-0.610	-0.610	0.000	0.000	0.000	0.000
67	A	67	GLN	0	-0.038	-0.001	16.987	-0.109	-0.109	0.000	0.000	0.000	0.000
68	A	68	TRP	0	-0.010	0.005	14.849	-0.960	-0.960	0.000	0.000	0.000	0.000
69	A	69	MET	0	-0.072	-0.050	16.724	0.269	0.269	0.000	0.000	0.000	0.000
70	A	70	GLY	0	0.005	0.009	19.757	0.193	0.193	0.000	0.000	0.000	0.000
71	A	71	LEU	0	-0.029	-0.030	20.485	0.646	0.646	0.000	0.000	0.000	0.000
72	A	72	ASN	0	-0.059	-0.048	22.423	0.079	0.079	0.000	0.000	0.000	0.000
73	A	73	ASP	-1	-0.791	-0.878	20.686	-13.753	-13.753	0.000	0.000	0.000	0.000
74	A	74	SER	0	-0.036	-0.016	20.636	-0.232	-0.232	0.000	0.000	0.000	0.000
75	A	75	ILE	0	-0.001	-0.009	14.194	-0.357	-0.357	0.000	0.000	0.000	0.000
76	A	76	ARG	1	0.870	0.941	17.649	14.034	14.034	0.000	0.000	0.000	0.000
77	A	77	SER	0	-0.047	-0.013	14.582	-0.141	-0.141	0.000	0.000	0.000	0.000
78	A	78	CYS	0	-0.030	0.002	9.988	-0.121	-0.121	0.000	0.000	0.000	0.000
79	A	79	ARG	1	0.844	0.928	8.952	25.073	25.073	0.000	0.000	0.000	0.000
81	A	81	ILE	0	-0.054	-0.040	5.931	4.185	4.185	0.000	0.000	0.000	0.000
82	A	82	PRO	0	-0.045	-0.009	7.083	-3.450	-3.450	0.000	0.000	0.000	0.000
83	A	83	HIS	0	0.044	0.010	7.416	2.032	2.032	0.000	0.000	0.000	0.000
84	A	84	ALA	0	0.004	0.004	9.221	0.768	0.768	0.000	0.000	0.000	0.000
85	A	85	GLY	0	-0.029	-0.018	12.696	0.074	0.074	0.000	0.000	0.000	0.000
86	A	87	SER	0	-0.045	-0.047	15.126	1.192	1.192	0.000	0.000	0.000	0.000
87	A	88	HIS	0	-0.020	-0.017	14.060	-0.058	-0.058	0.000	0.000	0.000	0.000
88	A	89	ARG	1	0.776	0.862	18.876	13.397	13.397	0.000	0.000	0.000	0.000
89	A	90	LEU	0	-0.005	0.003	20.843	-0.352	-0.352	0.000	0.000	0.000	0.000
90	A	91	ARG	1	0.838	0.907	23.669	11.353	11.353	0.000	0.000	0.000	0.000
91	A	92	LEU	0	0.030	0.007	25.364	-0.223	-0.223	0.000	0.000	0.000	0.000
92	A	93	TYR	0	0.011	-0.001	28.651	0.206	0.206	0.000	0.000	0.000	0.000
93	A	94	GLU	-1	-0.760	-0.874	31.908	-8.330	-8.330	0.000	0.000	0.000	0.000
94	A	95	ARG	1	0.837	0.903	34.873	8.106	8.106	0.000	0.000	0.000	0.000
95	A	96	GLU	-1	-0.743	-0.848	33.265	-9.498	-9.498	0.000	0.000	0.000	0.000
96	A	97	ASP	-1	-0.847	-0.897	33.181	-8.829	-8.829	0.000	0.000	0.000	0.000
97	A	98	TYR	0	0.021	0.002	28.823	0.129	0.129	0.000	0.000	0.000	0.000
98	A	99	ARG	1	0.827	0.919	33.329	8.756	8.756	0.000	0.000	0.000	0.000
99	A	100	GLY	0	-0.026	-0.020	36.295	-0.097	-0.097	0.000	0.000	0.000	0.000
100	A	101	GLN	0	-0.024	-0.009	35.807	0.110	0.110	0.000	0.000	0.000	0.000
101	A	102	MET	0	-0.018	0.002	31.296	-0.326	-0.326	0.000	0.000	0.000	0.000
102	A	103	ILE	0	-0.004	0.003	29.689	0.232	0.232	0.000	0.000	0.000	0.000
103	A	104	GLU	-1	-0.768	-0.863	27.187	-11.611	-11.611	0.000	0.000	0.000	0.000
104	A	105	ILE	0	-0.029	-0.008	24.147	0.232	0.232	0.000	0.000	0.000	0.000
105	A	106	THR	0	0.037	0.005	22.679	-0.292	-0.292	0.000	0.000	0.000	0.000
106	A	107	GLU	-1	-0.897	-0.947	21.888	-12.277	-12.277	0.000	0.000	0.000	0.000
107	A	108	ASP	-1	-0.827	-0.882	18.899	-16.409	-16.409	0.000	0.000	0.000	0.000
108	A	109	CYS	0	-0.040	-0.003	21.787	0.729	0.729	0.000	0.000	0.000	0.000
109	A	110	SER	0	0.050	0.016	24.398	-0.142	-0.142	0.000	0.000	0.000	0.000
110	A	111	SER	0	0.010	-0.036	25.371	0.035	0.035	0.000	0.000	0.000	0.000
111	A	112	LEU	0	-0.009	-0.004	27.434	0.172	0.172	0.000	0.000	0.000	0.000
112	A	113	GLN	0	0.045	0.016	29.701	0.323	0.323	0.000	0.000	0.000	0.000
113	A	114	ASP	-1	-0.867	-0.906	32.362	-9.167	-9.167	0.000	0.000	0.000	0.000
114	A	115	ARG	1	0.835	0.923	29.007	10.644	10.644	0.000	0.000	0.000	0.000
115	A	116	PHE	0	0.001	-0.027	28.330	0.093	0.093	0.000	0.000	0.000	0.000
116	A	117	HIS	1	0.874	0.962	33.473	8.849	8.849	0.000	0.000	0.000	0.000
117	A	118	PHE	0	0.036	0.032	31.893	0.189	0.189	0.000	0.000	0.000	0.000
118	A	119	ASN	0	0.007	-0.013	32.612	-0.218	-0.218	0.000	0.000	0.000	0.000
119	A	120	GLU	-1	-0.906	-0.957	31.275	-9.327	-9.327	0.000	0.000	0.000	0.000
120	A	121	ILE	0	-0.051	-0.014	28.102	0.113	0.113	0.000	0.000	0.000	0.000
121	A	122	HIS	0	-0.001	-0.012	29.752	-0.312	-0.312	0.000	0.000	0.000	0.000
122	A	123	SER	0	-0.066	-0.032	29.147	-0.046	-0.046	0.000	0.000	0.000	0.000
123	A	124	LEU	0	-0.011	-0.012	23.443	-0.016	-0.016	0.000	0.000	0.000	0.000
124	A	125	ASN	0	0.017	0.003	25.025	-0.363	-0.363	0.000	0.000	0.000	0.000
125	A	126	VAL	0	-0.005	0.011	18.725	0.153	0.153	0.000	0.000	0.000	0.000
126	A	127	LEU	0	0.021	0.016	21.146	-0.302	-0.302	0.000	0.000	0.000	0.000
127	A	128	GLU	-1	-0.787	-0.856	18.902	-14.543	-14.543	0.000	0.000	0.000	0.000
128	A	129	GLY	0	0.067	0.033	14.890	0.083	0.083	0.000	0.000	0.000	0.000
129	A	130	SER	0	-0.002	-0.001	12.243	1.005	1.005	0.000	0.000	0.000	0.000
130	A	131	TRP	0	-0.027	-0.027	14.620	-0.234	-0.234	0.000	0.000	0.000	0.000
131	A	132	VAL	0	-0.016	-0.006	14.392	-0.574	-0.574	0.000	0.000	0.000	0.000
132	A	133	LEU	0	0.005	0.014	17.161	0.623	0.623	0.000	0.000	0.000	0.000
133	A	134	TYR	0	0.024	-0.002	16.753	-0.547	-0.547	0.000	0.000	0.000	0.000
134	A	135	GLU	-1	-0.816	-0.915	22.555	-10.815	-10.815	0.000	0.000	0.000	0.000
135	A	136	LEU	0	-0.003	0.002	25.335	0.574	0.574	0.000	0.000	0.000	0.000
136	A	137	PRO	0	0.014	0.015	25.369	-0.494	-0.494	0.000	0.000	0.000	0.000
137	A	138	ASN	0	-0.067	-0.049	24.570	-0.215	-0.215	0.000	0.000	0.000	0.000
138	A	139	TYR	0	-0.033	-0.016	19.702	-0.380	-0.380	0.000	0.000	0.000	0.000
139	A	140	ARG	1	0.979	0.996	20.900	11.827	11.827	0.000	0.000	0.000	0.000
140	A	141	GLY	0	0.046	0.021	23.225	0.192	0.192	0.000	0.000	0.000	0.000
141	A	142	ARG	1	0.911	0.955	22.413	12.426	12.426	0.000	0.000	0.000	0.000
142	A	143	GLN	0	0.039	0.025	16.826	-0.633	-0.633	0.000	0.000	0.000	0.000
143	A	144	TYR	0	-0.053	-0.017	19.087	0.156	0.156	0.000	0.000	0.000	0.000
144	A	145	LEU	0	-0.009	-0.012	12.888	-0.222	-0.222	0.000	0.000	0.000	0.000
145	A	146	LEU	0	-0.022	0.006	16.514	0.626	0.626	0.000	0.000	0.000	0.000
146	A	147	ARG	1	0.954	0.972	13.178	19.074	19.074	0.000	0.000	0.000	0.000
147	A	148	PRO	0	0.033	0.009	15.486	0.898	0.898	0.000	0.000	0.000	0.000
148	A	149	GLY	0	0.026	0.028	18.434	-0.223	-0.223	0.000	0.000	0.000	0.000
149	A	150	GLU	-1	-0.965	-0.978	21.849	-11.575	-11.575	0.000	0.000	0.000	0.000
150	A	151	TYR	0	-0.051	-0.045	19.415	-0.323	-0.323	0.000	0.000	0.000	0.000
151	A	152	ARG	1	0.788	0.867	26.057	9.798	9.798	0.000	0.000	0.000	0.000
152	A	153	ARG	1	0.863	0.890	28.986	11.079	11.079	0.000	0.000	0.000	0.000
153	A	154	TYR	0	0.080	0.032	27.579	-0.387	-0.387	0.000	0.000	0.000	0.000
154	A	155	HIS	0	-0.008	0.022	26.648	-0.197	-0.197	0.000	0.000	0.000	0.000
155	A	156	ASP	-1	-0.805	-0.900	25.124	-11.803	-11.803	0.000	0.000	0.000	0.000
156	A	157	TRP	0	-0.012	0.008	21.694	-0.624	-0.624	0.000	0.000	0.000	0.000
157	A	158	GLY	0	-0.019	-0.018	21.919	-0.586	-0.586	0.000	0.000	0.000	0.000
158	A	159	ALA	0	-0.015	0.001	23.991	0.060	0.060	0.000	0.000	0.000	0.000
159	A	160	MET	0	-0.023	-0.026	26.151	0.274	0.274	0.000	0.000	0.000	0.000
160	A	161	ASN	0	-0.011	-0.021	29.317	0.330	0.330	0.000	0.000	0.000	0.000
161	A	162	ALA	0	0.078	0.041	29.234	-0.400	-0.400	0.000	0.000	0.000	0.000
162	A	163	LYS	1	0.873	0.954	29.948	10.222	10.222	0.000	0.000	0.000	0.000
163	A	164	VAL	0	-0.031	-0.014	25.309	-0.462	-0.462	0.000	0.000	0.000	0.000
164	A	165	GLY	0	0.020	0.014	26.539	0.414	0.414	0.000	0.000	0.000	0.000
165	A	166	SER	0	-0.058	-0.043	23.408	-0.055	-0.055	0.000	0.000	0.000	0.000
166	A	167	LEU	0	0.015	0.021	21.414	-0.259	-0.259	0.000	0.000	0.000	0.000
167	A	168	ARG	1	0.891	0.954	14.996	18.089	18.089	0.000	0.000	0.000	0.000
168	A	169	ARG	1	0.882	0.931	16.321	15.604	15.604	0.000	0.000	0.000	0.000
169	A	170	VAL	0	-0.053	-0.025	10.055	-0.426	-0.426	0.000	0.000	0.000	0.000
170	A	171	ILE	0	0.007	0.006	12.023	-0.804	-0.804	0.000	0.000	0.000	0.000
171	A	172	ASP	-1	-0.766	-0.907	6.136	-42.625	-42.625	0.000	0.000	0.000	0.000
172	A	173	ILE	0	-0.072	-0.034	8.539	2.703	2.703	0.000	0.000	0.000	0.000
173	A	174	TYR	-1	-0.814	-0.897	5.945	-39.778	-39.778	0.000	0.000	0.000	0.000

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