FMO DATABASE

FMODB ID: MRG3Z

Calculation Name: 2BV8-B-Xray547

Preferred Name:

Target Type:

Ligand Name: phycocyanobilin | phycoerythrobilin | n-methyl asparagine

Ligand 3-letter code: CYC | PEB | MEN

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2BV8

Chain ID: B

ChEMBL ID:

UniProt ID: Q6B8L6

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1523968.709854
FMO2-HF: Nuclear repulsion	1458831.81306
FMO2-HF: Total energy	-65136.896794
FMO2-MP2: Total energy	-65322.551796

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:MET)

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

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.
-145.75	-139.392	5.683	-3.585	-8.454	-0.021

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.813 / q_NPA : 0.903

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	ASP	-1	-0.758	-0.857	3.697	-36.302	-33.913	-0.010	-1.000	-1.379	-0.005
92	A	92	TYR	0	0.008	-0.001	4.738	-2.613	-2.520	-0.001	-0.002	-0.089	0.000
99	A	99	ALA	0	-0.039	-0.008	5.609	-0.232	-0.170	-0.001	-0.006	-0.054	0.000
103	A	103	SER	0	-0.020	-0.011	3.232	-8.364	-6.906	0.063	-0.786	-0.735	-0.005
104	A	104	VAL	0	-0.021	-0.024	2.534	-3.147	-2.527	4.076	-1.200	-3.496	-0.007
105	A	105	LEU	0	0.001	0.007	3.550	2.763	2.875	0.032	0.011	-0.155	0.000
107	A	107	ASP	-1	-0.927	-0.977	3.772	-53.038	-52.532	0.001	-0.191	-0.316	-0.001
108	A	108	ARG	1	0.855	0.921	2.970	46.922	48.040	1.523	-0.411	-2.230	-0.003
4	A	4	ALA	0	0.032	0.005	5.624	-0.653	-0.653	0.000	0.000	0.000	0.000
5	A	5	PHE	0	0.017	-0.001	8.964	1.878	1.878	0.000	0.000	0.000	0.000
6	A	6	ALA	0	-0.011	-0.015	6.078	0.899	0.899	0.000	0.000	0.000	0.000
7	A	7	LYS	1	0.826	0.913	7.942	32.621	32.621	0.000	0.000	0.000	0.000
8	A	8	VAL	0	0.015	0.003	8.926	2.011	2.011	0.000	0.000	0.000	0.000
9	A	9	VAL	0	-0.006	-0.001	11.120	1.708	1.708	0.000	0.000	0.000	0.000
10	A	10	ALA	0	0.010	0.010	8.387	1.530	1.530	0.000	0.000	0.000	0.000
11	A	11	GLN	0	-0.050	-0.038	10.486	1.989	1.989	0.000	0.000	0.000	0.000
12	A	12	ALA	0	-0.022	0.000	13.110	1.589	1.589	0.000	0.000	0.000	0.000
13	A	13	ASP	-1	-0.900	-0.947	12.773	-20.996	-20.996	0.000	0.000	0.000	0.000
14	A	14	ALA	0	-0.019	-0.011	13.115	1.248	1.248	0.000	0.000	0.000	0.000
15	A	15	ARG	1	0.755	0.860	15.020	18.457	18.457	0.000	0.000	0.000	0.000
16	A	16	GLY	0	-0.015	0.006	17.825	1.015	1.015	0.000	0.000	0.000	0.000
17	A	17	GLU	-1	-0.912	-0.932	18.628	-14.280	-14.280	0.000	0.000	0.000	0.000
18	A	18	PHE	0	-0.014	-0.014	18.407	-0.850	-0.850	0.000	0.000	0.000	0.000
19	A	19	LEU	0	-0.005	-0.003	15.202	0.032	0.032	0.000	0.000	0.000	0.000
20	A	20	SER	0	0.008	-0.009	19.506	0.858	0.858	0.000	0.000	0.000	0.000
21	A	21	ASN	0	0.038	-0.010	21.491	-0.710	-0.710	0.000	0.000	0.000	0.000
22	A	22	THR	0	0.035	0.024	22.699	0.018	0.018	0.000	0.000	0.000	0.000
23	A	23	GLN	0	0.040	0.038	17.169	0.506	0.506	0.000	0.000	0.000	0.000
24	A	24	LEU	0	-0.014	-0.004	18.017	-0.694	-0.694	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.903	-0.948	19.497	-13.186	-13.186	0.000	0.000	0.000	0.000
26	A	26	ALA	0	-0.009	-0.007	18.188	-0.132	-0.132	0.000	0.000	0.000	0.000
27	A	27	LEU	0	0.005	-0.002	13.064	-0.416	-0.416	0.000	0.000	0.000	0.000
28	A	28	ALA	0	0.005	0.002	16.355	-0.211	-0.211	0.000	0.000	0.000	0.000
29	A	29	ASN	0	-0.036	-0.024	19.217	0.654	0.654	0.000	0.000	0.000	0.000
30	A	30	MET	0	-0.004	0.005	11.839	-0.193	-0.193	0.000	0.000	0.000	0.000
31	A	31	ILE	0	-0.058	-0.019	14.951	-0.252	-0.252	0.000	0.000	0.000	0.000
32	A	32	ALA	0	-0.043	-0.015	17.461	0.402	0.402	0.000	0.000	0.000	0.000
33	A	33	GLU	-1	-0.860	-0.919	16.233	-16.381	-16.381	0.000	0.000	0.000	0.000
34	A	34	GLY	0	0.034	0.016	16.159	-0.124	-0.124	0.000	0.000	0.000	0.000
35	A	35	ASN	0	-0.021	-0.025	16.761	-0.655	-0.655	0.000	0.000	0.000	0.000
36	A	36	LYS	1	0.932	0.963	19.157	12.430	12.430	0.000	0.000	0.000	0.000
37	A	37	ARG	1	0.754	0.838	12.229	20.047	20.047	0.000	0.000	0.000	0.000
38	A	38	LEU	0	-0.018	-0.013	13.885	-0.507	-0.507	0.000	0.000	0.000	0.000
39	A	39	ASP	-1	-0.905	-0.957	15.923	-12.836	-12.836	0.000	0.000	0.000	0.000
40	A	40	ILE	0	-0.015	-0.004	16.307	0.294	0.294	0.000	0.000	0.000	0.000
41	A	41	VAL	0	0.021	0.006	11.858	0.061	0.061	0.000	0.000	0.000	0.000
42	A	42	ASN	0	-0.029	-0.013	14.971	-0.003	-0.003	0.000	0.000	0.000	0.000
43	A	43	ARG	1	0.885	0.951	17.615	12.050	12.050	0.000	0.000	0.000	0.000
44	A	44	ILE	0	0.035	0.012	14.748	0.269	0.269	0.000	0.000	0.000	0.000
45	A	45	ASN	0	-0.052	-0.042	13.185	-0.195	-0.195	0.000	0.000	0.000	0.000
46	A	46	SER	0	-0.073	-0.039	16.457	0.480	0.480	0.000	0.000	0.000	0.000
47	A	47	ASN	0	-0.027	-0.012	19.936	0.751	0.751	0.000	0.000	0.000	0.000
48	A	48	ALA	0	0.021	0.029	16.844	0.272	0.272	0.000	0.000	0.000	0.000
49	A	49	SER	0	0.013	-0.002	18.694	0.102	0.102	0.000	0.000	0.000	0.000
50	A	50	ALA	0	0.003	0.012	21.262	0.355	0.355	0.000	0.000	0.000	0.000
51	A	51	ILE	0	0.037	0.025	19.154	0.328	0.328	0.000	0.000	0.000	0.000
52	A	52	VAL	0	0.029	0.026	18.442	0.225	0.225	0.000	0.000	0.000	0.000
53	A	53	SER	0	-0.031	-0.037	21.350	0.399	0.399	0.000	0.000	0.000	0.000
54	A	54	ASN	0	-0.032	-0.016	24.886	0.633	0.633	0.000	0.000	0.000	0.000
55	A	55	SER	0	0.041	0.018	23.107	0.356	0.356	0.000	0.000	0.000	0.000
56	A	56	ALA	0	0.005	0.005	24.214	0.200	0.200	0.000	0.000	0.000	0.000
57	A	57	ARG	1	0.865	0.920	25.952	9.684	9.684	0.000	0.000	0.000	0.000
58	A	58	ALA	0	0.018	0.013	28.496	0.316	0.316	0.000	0.000	0.000	0.000
59	A	59	LEU	0	0.037	0.023	25.286	0.252	0.252	0.000	0.000	0.000	0.000
60	A	60	PHE	0	-0.025	-0.048	26.360	0.178	0.178	0.000	0.000	0.000	0.000
61	A	61	ALA	0	-0.028	-0.003	31.215	0.301	0.301	0.000	0.000	0.000	0.000
62	A	62	GLU	-1	-0.865	-0.927	30.865	-9.430	-9.430	0.000	0.000	0.000	0.000
63	A	63	GLN	0	0.025	0.026	29.191	0.040	0.040	0.000	0.000	0.000	0.000
64	A	64	PRO	0	0.044	0.027	32.502	-0.162	-0.162	0.000	0.000	0.000	0.000
65	A	65	GLN	0	0.018	-0.006	34.718	-0.155	-0.155	0.000	0.000	0.000	0.000
66	A	66	LEU	0	-0.027	-0.005	28.134	-0.036	-0.036	0.000	0.000	0.000	0.000
67	A	67	ILE	0	-0.023	-0.018	30.640	-0.141	-0.141	0.000	0.000	0.000	0.000
68	A	68	GLN	0	0.003	0.021	33.035	0.179	0.179	0.000	0.000	0.000	0.000
69	A	69	PRO	0	-0.001	-0.027	35.572	-0.203	-0.203	0.000	0.000	0.000	0.000
70	A	70	GLY	0	-0.014	-0.003	35.817	0.115	0.115	0.000	0.000	0.000	0.000
71	A	71	GLY	0	0.045	0.047	33.380	-0.160	-0.160	0.000	0.000	0.000	0.000
72	A	72	ASN	0	0.026	0.021	26.574	-0.334	-0.334	0.000	0.000	0.000	0.000
73	A	73	ALA	0	0.065	0.030	27.418	-0.247	-0.247	0.000	0.000	0.000	0.000
74	A	74	TYR	0	0.014	0.025	28.553	0.098	0.098	0.000	0.000	0.000	0.000
75	A	75	THR	0	-0.065	-0.043	30.621	-0.201	-0.201	0.000	0.000	0.000	0.000
76	A	76	ASN	0	0.073	0.018	29.346	-0.264	-0.264	0.000	0.000	0.000	0.000
77	A	77	ARG	1	0.970	0.991	25.267	10.488	10.488	0.000	0.000	0.000	0.000
78	A	78	ARG	1	0.843	0.918	25.084	9.287	9.287	0.000	0.000	0.000	0.000
79	A	79	MET	0	0.028	0.037	25.051	-0.434	-0.434	0.000	0.000	0.000	0.000
80	A	80	ALA	0	0.003	-0.006	23.367	-0.315	-0.315	0.000	0.000	0.000	0.000
81	A	81	ALA	0	-0.032	-0.012	20.881	-0.471	-0.471	0.000	0.000	0.000	0.000
82	A	82	CYS	0	0.047	0.030	20.207	-0.500	-0.500	0.000	0.000	0.000	0.000
83	A	83	LEU	0	0.009	-0.001	20.668	-0.380	-0.380	0.000	0.000	0.000	0.000
84	A	84	ARG	1	0.852	0.908	16.372	14.349	14.349	0.000	0.000	0.000	0.000
85	A	85	ASP	-1	-0.767	-0.849	16.132	-15.931	-15.931	0.000	0.000	0.000	0.000
86	A	86	MET	0	-0.049	-0.015	15.933	-0.548	-0.548	0.000	0.000	0.000	0.000
87	A	87	GLU	-1	-0.882	-0.952	14.533	-15.964	-15.964	0.000	0.000	0.000	0.000
88	A	88	ILE	0	-0.083	-0.040	11.107	-1.036	-1.036	0.000	0.000	0.000	0.000
89	A	89	VAL	0	0.052	0.017	11.196	-1.581	-1.581	0.000	0.000	0.000	0.000
90	A	90	LEU	0	0.016	0.021	12.408	-0.968	-0.968	0.000	0.000	0.000	0.000
91	A	91	ARG	1	0.898	0.951	8.476	20.259	20.259	0.000	0.000	0.000	0.000
93	A	93	VAL	0	0.019	0.015	8.653	-2.041	-2.041	0.000	0.000	0.000	0.000
94	A	94	SER	0	-0.034	-0.021	10.103	-0.401	-0.401	0.000	0.000	0.000	0.000
95	A	95	TYR	0	-0.037	-0.026	5.266	-0.459	-0.459	0.000	0.000	0.000	0.000
96	A	96	ALA	0	0.006	0.006	6.662	-2.113	-2.113	0.000	0.000	0.000	0.000
97	A	97	GLU	-1	-0.853	-0.933	8.013	-18.965	-18.965	0.000	0.000	0.000	0.000
98	A	98	ILE	0	-0.027	-0.017	7.422	0.540	0.540	0.000	0.000	0.000	0.000
100	A	100	GLY	0	0.046	0.027	7.467	-0.441	-0.441	0.000	0.000	0.000	0.000
101	A	101	ASP	-1	-0.806	-0.890	5.701	-41.670	-41.670	0.000	0.000	0.000	0.000
102	A	102	SER	0	0.005	-0.019	6.542	-0.991	-0.991	0.000	0.000	0.000	0.000
106	A	106	ASP	-1	-0.753	-0.853	7.001	-26.447	-26.447	0.000	0.000	0.000	0.000
109	A	109	CYS	0	-0.067	-0.015	6.968	3.081	3.081	0.000	0.000	0.000	0.000
110	A	110	LEU	0	0.002	0.019	10.004	2.021	2.021	0.000	0.000	0.000	0.000
111	A	111	ASN	0	-0.009	-0.004	10.675	3.115	3.115	0.000	0.000	0.000	0.000
112	A	112	GLY	0	0.022	0.023	12.559	-0.093	-0.093	0.000	0.000	0.000	0.000
113	A	113	LEU	0	-0.016	0.013	14.343	1.177	1.177	0.000	0.000	0.000	0.000
114	A	114	ARG	1	0.883	0.942	16.625	16.210	16.210	0.000	0.000	0.000	0.000
115	A	115	GLU	-1	-0.863	-0.943	18.602	-15.437	-15.437	0.000	0.000	0.000	0.000
116	A	116	THR	0	-0.047	-0.031	17.634	0.687	0.687	0.000	0.000	0.000	0.000
117	A	117	TYR	0	-0.058	-0.066	18.389	0.587	0.587	0.000	0.000	0.000	0.000
118	A	118	GLN	0	-0.011	-0.012	22.176	0.436	0.436	0.000	0.000	0.000	0.000
119	A	119	ALA	0	-0.028	-0.008	23.175	0.562	0.562	0.000	0.000	0.000	0.000
120	A	120	LEU	0	-0.072	-0.034	21.065	0.438	0.438	0.000	0.000	0.000	0.000
121	A	121	GLY	0	-0.025	0.001	25.268	0.414	0.414	0.000	0.000	0.000	0.000
122	A	122	THR	0	-0.079	-0.053	23.146	0.341	0.341	0.000	0.000	0.000	0.000
123	A	123	PRO	0	-0.019	-0.015	25.379	-0.233	-0.233	0.000	0.000	0.000	0.000
124	A	124	GLY	0	0.111	0.049	23.139	-0.085	-0.085	0.000	0.000	0.000	0.000
125	A	125	SER	0	0.010	0.005	23.588	-0.280	-0.280	0.000	0.000	0.000	0.000
126	A	126	SER	0	-0.015	-0.030	26.077	0.037	0.037	0.000	0.000	0.000	0.000
127	A	127	VAL	0	-0.007	-0.001	19.815	0.037	0.037	0.000	0.000	0.000	0.000
128	A	128	ALA	0	0.033	0.022	21.538	-0.348	-0.348	0.000	0.000	0.000	0.000
129	A	129	VAL	0	-0.010	-0.001	22.608	-0.061	-0.061	0.000	0.000	0.000	0.000
130	A	130	ALA	0	-0.008	-0.018	22.031	0.084	0.084	0.000	0.000	0.000	0.000
131	A	131	ILE	0	-0.028	-0.014	17.518	-0.137	-0.137	0.000	0.000	0.000	0.000
132	A	132	GLU	-1	-0.801	-0.904	20.439	-13.453	-13.453	0.000	0.000	0.000	0.000
133	A	133	LYS	1	0.838	0.922	22.811	10.387	10.387	0.000	0.000	0.000	0.000
134	A	134	MET	0	-0.034	0.002	17.590	0.065	0.065	0.000	0.000	0.000	0.000
135	A	135	LYS	1	0.790	0.912	19.879	13.268	13.268	0.000	0.000	0.000	0.000
136	A	136	GLU	-1	-0.928	-0.972	21.034	-10.661	-10.661	0.000	0.000	0.000	0.000
137	A	137	ALA	0	-0.034	-0.017	22.719	0.196	0.196	0.000	0.000	0.000	0.000
138	A	138	SER	0	0.012	-0.020	18.849	-0.004	-0.004	0.000	0.000	0.000	0.000
139	A	139	VAL	0	-0.004	-0.005	20.721	-0.129	-0.129	0.000	0.000	0.000	0.000
140	A	140	SER	0	-0.032	-0.013	22.469	0.432	0.432	0.000	0.000	0.000	0.000
141	A	141	ASP	-1	-0.886	-0.945	22.275	-11.679	-11.679	0.000	0.000	0.000	0.000
142	A	142	ALA	0	-0.070	-0.037	20.389	0.122	0.122	0.000	0.000	0.000	0.000
143	A	143	ASN	0	-0.033	-0.007	22.285	-0.155	-0.155	0.000	0.000	0.000	0.000
144	A	144	ASP	-1	-0.875	-0.917	25.790	-9.453	-9.453	0.000	0.000	0.000	0.000
145	A	145	SER	0	-0.019	-0.013	26.467	-0.183	-0.183	0.000	0.000	0.000	0.000
146	A	146	SER	0	-0.015	-0.006	28.425	0.119	0.119	0.000	0.000	0.000	0.000
147	A	147	GLY	0	-0.009	-0.003	27.513	-0.313	-0.313	0.000	0.000	0.000	0.000
148	A	148	THR	0	-0.025	0.001	23.798	-0.382	-0.382	0.000	0.000	0.000	0.000
149	A	149	PRO	0	-0.024	-0.023	26.032	0.379	0.379	0.000	0.000	0.000	0.000
150	A	150	SER	0	-0.015	0.001	27.971	-0.292	-0.292	0.000	0.000	0.000	0.000
151	A	151	GLY	0	0.019	-0.006	28.618	0.127	0.127	0.000	0.000	0.000	0.000
152	A	152	ASP	-1	-0.825	-0.883	26.845	-11.413	-11.413	0.000	0.000	0.000	0.000
153	A	153	CYS	0	0.018	0.010	22.364	-0.375	-0.375	0.000	0.000	0.000	0.000
154	A	154	SER	0	-0.015	-0.025	22.378	-0.667	-0.667	0.000	0.000	0.000	0.000
155	A	155	SER	0	0.010	-0.002	19.737	-0.156	-0.156	0.000	0.000	0.000	0.000
156	A	156	LEU	0	0.004	0.013	16.442	-0.434	-0.434	0.000	0.000	0.000	0.000
157	A	157	SER	0	-0.001	-0.012	18.124	-0.695	-0.695	0.000	0.000	0.000	0.000
158	A	158	ALA	0	-0.018	-0.003	20.155	-0.056	-0.056	0.000	0.000	0.000	0.000
159	A	159	GLU	-1	-0.768	-0.816	12.863	-21.016	-21.016	0.000	0.000	0.000	0.000
160	A	160	LEU	0	0.057	0.025	15.141	-0.695	-0.695	0.000	0.000	0.000	0.000
161	A	161	GLY	0	-0.019	-0.018	16.129	-0.251	-0.251	0.000	0.000	0.000	0.000
162	A	162	THR	0	0.013	-0.001	14.915	0.019	0.019	0.000	0.000	0.000	0.000
163	A	163	TYR	0	-0.084	-0.070	10.259	-1.574	-1.574	0.000	0.000	0.000	0.000
164	A	164	PHE	0	0.023	-0.001	13.539	-0.541	-0.541	0.000	0.000	0.000	0.000
165	A	165	ASP	-1	-0.809	-0.885	16.324	-14.116	-14.116	0.000	0.000	0.000	0.000
166	A	166	ARG	1	0.780	0.873	10.598	24.176	24.176	0.000	0.000	0.000	0.000
167	A	167	ALA	0	0.022	0.002	13.929	-0.029	-0.029	0.000	0.000	0.000	0.000
168	A	168	ALA	0	-0.013	-0.015	15.348	0.438	0.438	0.000	0.000	0.000	0.000
169	A	169	SER	0	-0.044	-0.034	17.817	0.828	0.828	0.000	0.000	0.000	0.000
170	A	170	ALA	0	-0.046	-0.020	15.245	0.181	0.181	0.000	0.000	0.000	0.000
171	A	171	VAL	0	-0.040	-0.016	17.203	-0.032	-0.032	0.000	0.000	0.000	0.000
172	A	172	SER	-1	-0.890	-0.921	19.490	-12.765	-12.765	0.000	0.000	0.000	0.000

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