FMO DATABASE

FMODB ID: 3ZLGL

Calculation Name: 5J6C-A-Xray547

Preferred Name:

Target Type:

Ligand Name: flavin mononucleotide | imidazole

Ligand 3-letter code: FMN | IMD

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 5J6C

Chain ID: A

ChEMBL ID:

UniProt ID: C9YJL7

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	-1830050.982295
FMO2-HF: Nuclear repulsion	1760382.78156
FMO2-HF: Total energy	-69668.200734
FMO2-MP2: Total energy	-69872.655506

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:7:MET)

Summations of interaction energy for fragment #1(A:7: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.
81.697	87.423	2.173	-2.259	-5.638	-0.005

Interaction energy analysis for fragmet #1(A:7:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.929 / q_NPA : 0.961

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	9	GLY	0	0.051	0.023	3.816	5.967	7.520	-0.003	-0.597	-0.953	0.000
4	A	10	PHE	0	-0.032	-0.015	2.575	0.285	2.783	0.979	-1.085	-2.391	-0.005
5	A	11	LEU	0	0.064	0.020	2.277	7.470	8.938	1.194	-0.543	-2.119	0.000
101	A	107	LEU	0	-0.073	-0.039	3.586	-1.798	-1.591	0.003	-0.034	-0.175	0.000
6	A	12	LYS	1	0.851	0.917	5.901	35.685	35.685	0.000	0.000	0.000	0.000
7	A	13	LYS	1	0.957	0.976	6.684	39.182	39.182	0.000	0.000	0.000	0.000
8	A	14	ARG	1	0.956	1.009	7.837	27.076	27.076	0.000	0.000	0.000	0.000
9	A	15	ARG	1	0.860	0.918	9.940	20.882	20.882	0.000	0.000	0.000	0.000
10	A	16	SER	0	-0.013	-0.015	13.731	-0.493	-0.493	0.000	0.000	0.000	0.000
11	A	17	ILE	0	-0.052	-0.009	15.665	0.581	0.581	0.000	0.000	0.000	0.000
12	A	18	ARG	1	0.912	0.963	18.439	14.320	14.320	0.000	0.000	0.000	0.000
13	A	19	LYS	1	0.880	0.959	21.779	12.254	12.254	0.000	0.000	0.000	0.000
14	A	20	TYR	0	0.012	-0.008	19.460	-0.494	-0.494	0.000	0.000	0.000	0.000
15	A	21	LYS	1	0.849	0.908	22.571	13.417	13.417	0.000	0.000	0.000	0.000
16	A	22	ASP	-1	-0.935	-0.951	25.633	-10.447	-10.447	0.000	0.000	0.000	0.000
17	A	23	VAL	0	-0.046	-0.028	24.471	0.190	0.190	0.000	0.000	0.000	0.000
18	A	24	GLU	-1	-0.910	-0.954	24.927	-11.498	-11.498	0.000	0.000	0.000	0.000
19	A	25	VAL	0	-0.030	-0.022	19.148	-0.506	-0.506	0.000	0.000	0.000	0.000
20	A	26	GLU	-1	-0.713	-0.825	20.712	-14.689	-14.689	0.000	0.000	0.000	0.000
21	A	27	LYS	1	0.933	0.927	21.375	11.544	11.544	0.000	0.000	0.000	0.000
22	A	28	GLU	-1	-0.866	-0.925	18.334	-17.106	-17.106	0.000	0.000	0.000	0.000
23	A	29	LYS	1	0.840	0.929	16.932	16.366	16.366	0.000	0.000	0.000	0.000
24	A	30	LEU	0	0.048	0.030	16.825	-0.782	-0.782	0.000	0.000	0.000	0.000
25	A	31	ASP	-1	-0.833	-0.906	18.246	-13.284	-13.284	0.000	0.000	0.000	0.000
26	A	32	LYS	1	0.828	0.907	14.307	18.595	18.595	0.000	0.000	0.000	0.000
27	A	33	ILE	0	0.015	0.009	13.525	-0.771	-0.771	0.000	0.000	0.000	0.000
28	A	34	LEU	0	0.021	0.011	14.444	-0.213	-0.213	0.000	0.000	0.000	0.000
29	A	35	LYS	1	0.942	0.969	15.450	15.413	15.413	0.000	0.000	0.000	0.000
30	A	36	ALA	0	0.001	-0.002	10.422	-0.139	-0.139	0.000	0.000	0.000	0.000
31	A	37	ALA	0	-0.013	-0.007	12.079	-0.366	-0.366	0.000	0.000	0.000	0.000
32	A	38	LEU	0	-0.023	-0.017	14.158	0.328	0.328	0.000	0.000	0.000	0.000
33	A	39	LEU	0	-0.062	-0.031	12.437	0.545	0.545	0.000	0.000	0.000	0.000
34	A	40	ALA	0	-0.002	0.017	11.653	-0.941	-0.941	0.000	0.000	0.000	0.000
35	A	41	PRO	0	-0.028	-0.008	11.073	1.167	1.167	0.000	0.000	0.000	0.000
36	A	42	SER	0	0.009	-0.003	13.961	0.243	0.243	0.000	0.000	0.000	0.000
37	A	43	SER	0	0.021	0.008	16.989	0.247	0.247	0.000	0.000	0.000	0.000
38	A	44	LYS	1	0.908	0.941	19.569	11.066	11.066	0.000	0.000	0.000	0.000
39	A	45	GLY	0	0.006	0.014	19.555	0.314	0.314	0.000	0.000	0.000	0.000
40	A	46	LEU	0	-0.040	-0.025	20.611	0.100	0.100	0.000	0.000	0.000	0.000
41	A	47	ARG	1	0.892	0.960	17.855	13.880	13.880	0.000	0.000	0.000	0.000
42	A	48	THR	0	-0.013	-0.036	20.504	0.326	0.326	0.000	0.000	0.000	0.000
43	A	49	TRP	0	-0.041	-0.014	15.937	0.607	0.607	0.000	0.000	0.000	0.000
44	A	50	GLU	-1	-0.844	-0.900	20.488	-10.188	-10.188	0.000	0.000	0.000	0.000
45	A	51	PHE	0	-0.024	-0.027	16.683	-0.326	-0.326	0.000	0.000	0.000	0.000
46	A	52	ILE	0	0.021	0.019	21.476	0.318	0.318	0.000	0.000	0.000	0.000
47	A	53	VAL	0	-0.009	-0.007	21.227	-0.356	-0.356	0.000	0.000	0.000	0.000
48	A	54	VAL	0	-0.040	-0.028	23.430	0.503	0.503	0.000	0.000	0.000	0.000
49	A	55	ASP	-1	-0.827	-0.922	24.674	-11.064	-11.064	0.000	0.000	0.000	0.000
50	A	56	ASP	-1	-0.820	-0.909	26.887	-8.881	-8.881	0.000	0.000	0.000	0.000
51	A	57	LYS	1	0.952	0.976	29.951	9.425	9.425	0.000	0.000	0.000	0.000
52	A	58	GLU	-1	-0.881	-0.938	31.390	-8.443	-8.443	0.000	0.000	0.000	0.000
53	A	59	LYS	1	0.879	0.938	29.749	8.882	8.882	0.000	0.000	0.000	0.000
54	A	60	LEU	0	-0.024	-0.006	25.130	-0.148	-0.148	0.000	0.000	0.000	0.000
55	A	61	ILE	0	-0.025	-0.014	28.718	-0.213	-0.213	0.000	0.000	0.000	0.000
56	A	62	ASN	0	-0.008	0.006	31.692	-0.007	-0.007	0.000	0.000	0.000	0.000
57	A	63	LEU	0	0.013	0.003	26.171	-0.006	-0.006	0.000	0.000	0.000	0.000
58	A	64	SER	0	-0.110	-0.060	27.758	-0.154	-0.154	0.000	0.000	0.000	0.000
59	A	65	GLN	0	-0.015	-0.015	28.800	-0.196	-0.196	0.000	0.000	0.000	0.000
60	A	66	CYS	0	-0.028	-0.006	26.383	0.128	0.128	0.000	0.000	0.000	0.000
61	A	67	ARG	1	0.813	0.902	23.677	11.013	11.013	0.000	0.000	0.000	0.000
62	A	68	THR	0	-0.033	-0.029	30.241	-0.096	-0.096	0.000	0.000	0.000	0.000
63	A	69	LYS	1	0.888	0.942	32.543	8.197	8.197	0.000	0.000	0.000	0.000
64	A	70	GLY	0	0.014	0.017	29.533	-0.087	-0.087	0.000	0.000	0.000	0.000
65	A	71	GLY	0	-0.055	-0.054	25.330	-0.073	-0.073	0.000	0.000	0.000	0.000
66	A	72	GLY	0	0.076	0.034	24.157	-0.506	-0.506	0.000	0.000	0.000	0.000
67	A	73	PHE	0	0.009	0.015	25.815	-0.166	-0.166	0.000	0.000	0.000	0.000
68	A	74	PHE	0	0.000	-0.019	21.306	0.253	0.253	0.000	0.000	0.000	0.000
69	A	75	LEU	0	0.012	0.003	22.985	-0.171	-0.171	0.000	0.000	0.000	0.000
70	A	76	LYS	1	0.978	1.009	25.580	9.440	9.440	0.000	0.000	0.000	0.000
71	A	77	ASN	0	-0.053	-0.037	27.487	0.515	0.515	0.000	0.000	0.000	0.000
72	A	78	ALA	0	-0.024	-0.009	22.712	-0.305	-0.305	0.000	0.000	0.000	0.000
73	A	79	PRO	0	-0.010	0.019	22.606	0.294	0.294	0.000	0.000	0.000	0.000
74	A	80	LEU	0	0.018	0.011	19.527	0.103	0.103	0.000	0.000	0.000	0.000
75	A	81	ALA	0	-0.021	-0.010	20.618	-0.387	-0.387	0.000	0.000	0.000	0.000
76	A	82	ILE	0	-0.011	-0.002	16.881	0.184	0.184	0.000	0.000	0.000	0.000
77	A	83	VAL	0	-0.001	0.005	19.581	-0.360	-0.360	0.000	0.000	0.000	0.000
78	A	84	ILE	0	-0.038	-0.013	16.397	-0.025	-0.025	0.000	0.000	0.000	0.000
79	A	85	ILE	0	-0.012	-0.009	19.943	0.298	0.298	0.000	0.000	0.000	0.000
80	A	86	ALA	0	0.035	0.005	21.401	-0.457	-0.457	0.000	0.000	0.000	0.000
81	A	87	ASP	-1	-0.772	-0.870	23.297	-9.201	-9.201	0.000	0.000	0.000	0.000
82	A	88	LYS	1	0.783	0.889	26.283	9.066	9.066	0.000	0.000	0.000	0.000
83	A	89	GLU	-1	-0.893	-0.949	27.270	-8.363	-8.363	0.000	0.000	0.000	0.000
84	A	90	LYS	1	0.815	0.903	25.199	10.409	10.409	0.000	0.000	0.000	0.000
85	A	91	ASN	0	-0.014	-0.031	22.357	0.233	0.233	0.000	0.000	0.000	0.000
86	A	92	ASP	-1	-0.847	-0.908	25.424	-10.556	-10.556	0.000	0.000	0.000	0.000
87	A	93	VAL	0	-0.047	-0.015	20.450	-0.138	-0.138	0.000	0.000	0.000	0.000
88	A	94	TRP	0	0.026	0.001	20.232	-0.599	-0.599	0.000	0.000	0.000	0.000
89	A	95	ILE	0	-0.014	-0.003	18.920	-0.360	-0.360	0.000	0.000	0.000	0.000
90	A	96	GLU	-1	-0.848	-0.924	16.211	-13.715	-13.715	0.000	0.000	0.000	0.000
91	A	97	ASP	-1	-0.744	-0.842	15.071	-14.448	-14.448	0.000	0.000	0.000	0.000
92	A	98	ALA	0	-0.005	-0.005	15.390	-0.703	-0.703	0.000	0.000	0.000	0.000
93	A	99	SER	0	-0.031	-0.035	13.952	-0.553	-0.553	0.000	0.000	0.000	0.000
94	A	100	ILE	0	-0.034	-0.002	10.128	-1.320	-1.320	0.000	0.000	0.000	0.000
95	A	101	ALA	0	0.048	0.034	10.652	-1.376	-1.376	0.000	0.000	0.000	0.000
96	A	102	ALA	0	0.032	0.018	12.460	-0.582	-0.582	0.000	0.000	0.000	0.000
97	A	103	SER	0	-0.061	-0.046	8.382	-1.304	-1.304	0.000	0.000	0.000	0.000
98	A	104	TYR	0	-0.022	-0.021	7.261	-2.011	-2.011	0.000	0.000	0.000	0.000
99	A	105	ILE	0	0.030	0.022	8.962	-0.897	-0.897	0.000	0.000	0.000	0.000
100	A	106	GLN	0	-0.032	-0.028	10.159	-0.261	-0.261	0.000	0.000	0.000	0.000
102	A	108	GLN	0	-0.023	-0.020	7.554	-1.145	-1.145	0.000	0.000	0.000	0.000
103	A	109	ALA	0	0.051	0.019	9.849	0.415	0.415	0.000	0.000	0.000	0.000
104	A	110	HIS	0	-0.087	-0.042	7.193	1.942	1.942	0.000	0.000	0.000	0.000
105	A	111	GLU	-1	-0.981	-0.983	8.326	-31.318	-31.318	0.000	0.000	0.000	0.000
106	A	112	LEU	0	-0.021	0.000	9.568	0.687	0.687	0.000	0.000	0.000	0.000
107	A	113	GLY	0	-0.014	-0.002	12.507	1.672	1.672	0.000	0.000	0.000	0.000
108	A	114	LEU	0	-0.047	-0.009	14.066	1.362	1.362	0.000	0.000	0.000	0.000
109	A	115	GLY	0	-0.002	-0.007	14.193	-1.335	-1.335	0.000	0.000	0.000	0.000
110	A	116	SER	0	0.043	0.016	13.194	0.466	0.466	0.000	0.000	0.000	0.000
111	A	117	CYS	0	-0.116	-0.056	15.600	-0.531	-0.531	0.000	0.000	0.000	0.000
112	A	118	TRP	0	0.033	0.020	12.836	0.092	0.092	0.000	0.000	0.000	0.000
113	A	119	ILE	0	-0.031	-0.006	17.192	0.340	0.340	0.000	0.000	0.000	0.000
114	A	120	GLN	0	-0.065	-0.030	19.669	-0.404	-0.404	0.000	0.000	0.000	0.000
115	A	121	VAL	0	0.019	0.016	21.515	0.473	0.473	0.000	0.000	0.000	0.000
116	A	122	ARG	1	0.990	1.006	21.097	12.279	12.279	0.000	0.000	0.000	0.000
117	A	123	ASN	0	-0.024	-0.021	24.286	-0.231	-0.231	0.000	0.000	0.000	0.000
118	A	124	ARG	1	0.839	0.922	23.824	11.043	11.043	0.000	0.000	0.000	0.000
119	A	125	MET	0	0.050	0.044	27.776	-0.063	-0.063	0.000	0.000	0.000	0.000
120	A	126	TYR	0	0.013	0.017	30.992	-0.216	-0.216	0.000	0.000	0.000	0.000
121	A	127	ASP	-1	-0.811	-0.910	32.774	-7.763	-7.763	0.000	0.000	0.000	0.000
122	A	128	ASP	-1	-0.876	-0.943	35.474	-7.915	-7.915	0.000	0.000	0.000	0.000
123	A	129	ASN	0	-0.066	-0.020	37.667	0.200	0.200	0.000	0.000	0.000	0.000
124	A	130	ILE	0	-0.015	0.005	34.399	0.014	0.014	0.000	0.000	0.000	0.000
125	A	131	GLU	-1	-0.893	-0.957	30.815	-9.017	-9.017	0.000	0.000	0.000	0.000
126	A	132	ALA	0	-0.005	-0.016	27.850	0.065	0.065	0.000	0.000	0.000	0.000
127	A	133	ASP	-1	-0.761	-0.866	27.425	-9.679	-9.679	0.000	0.000	0.000	0.000
128	A	134	LYS	1	0.898	0.945	28.740	7.916	7.916	0.000	0.000	0.000	0.000
129	A	135	TYR	0	-0.025	-0.024	30.789	0.182	0.182	0.000	0.000	0.000	0.000
130	A	136	ILE	0	0.007	-0.009	25.873	0.041	0.041	0.000	0.000	0.000	0.000
131	A	137	ARG	1	0.836	0.888	29.266	9.019	9.019	0.000	0.000	0.000	0.000
132	A	138	GLU	-1	-0.861	-0.900	31.237	-7.703	-7.703	0.000	0.000	0.000	0.000
133	A	139	GLU	-1	-0.860	-0.926	31.352	-8.527	-8.527	0.000	0.000	0.000	0.000
134	A	140	LEU	0	-0.050	-0.035	27.064	-0.021	-0.021	0.000	0.000	0.000	0.000
135	A	141	LYS	1	0.898	0.961	31.161	7.707	7.707	0.000	0.000	0.000	0.000
136	A	142	VAL	0	0.025	0.022	28.301	0.013	0.013	0.000	0.000	0.000	0.000
137	A	143	PRO	0	0.016	0.003	31.169	0.147	0.147	0.000	0.000	0.000	0.000
138	A	144	SER	0	0.007	-0.003	31.780	-0.255	-0.255	0.000	0.000	0.000	0.000
139	A	145	LYS	1	0.937	0.975	30.146	9.036	9.036	0.000	0.000	0.000	0.000
140	A	146	TYR	0	-0.077	-0.060	26.230	-0.038	-0.038	0.000	0.000	0.000	0.000
141	A	147	SER	0	-0.046	-0.019	25.560	0.368	0.368	0.000	0.000	0.000	0.000
142	A	148	VAL	0	0.013	-0.003	23.690	-0.386	-0.386	0.000	0.000	0.000	0.000
143	A	149	GLU	-1	-0.782	-0.881	18.436	-12.723	-12.723	0.000	0.000	0.000	0.000
144	A	150	CYS	0	-0.064	-0.035	16.680	0.020	0.020	0.000	0.000	0.000	0.000
145	A	151	ILE	0	0.052	0.032	20.357	0.113	0.113	0.000	0.000	0.000	0.000
146	A	152	ILE	0	-0.024	-0.005	14.700	-0.465	-0.465	0.000	0.000	0.000	0.000
147	A	153	SER	0	0.016	-0.007	17.791	0.291	0.291	0.000	0.000	0.000	0.000
148	A	154	ILE	0	-0.016	-0.035	16.134	-1.118	-1.118	0.000	0.000	0.000	0.000
149	A	155	GLY	0	0.084	0.033	18.330	0.837	0.837	0.000	0.000	0.000	0.000
150	A	156	TYR	0	-0.021	-0.032	18.131	-1.274	-1.274	0.000	0.000	0.000	0.000
151	A	157	SER	0	0.004	-0.007	18.182	0.818	0.818	0.000	0.000	0.000	0.000
152	A	158	ASP	-1	-0.817	-0.910	20.216	-11.806	-11.806	0.000	0.000	0.000	0.000
153	A	159	GLU	-1	-0.824	-0.899	20.741	-13.484	-13.484	0.000	0.000	0.000	0.000
154	A	160	GLU	-1	-0.907	-0.939	19.359	-14.982	-14.982	0.000	0.000	0.000	0.000
155	A	161	LYS	1	0.828	0.894	16.339	15.184	15.184	0.000	0.000	0.000	0.000
156	A	162	LYS	1	0.985	1.007	16.012	16.160	16.160	0.000	0.000	0.000	0.000
157	A	163	ALA	0	0.022	0.011	11.095	-0.301	-0.301	0.000	0.000	0.000	0.000
158	A	164	TYR	0	-0.061	-0.027	11.152	1.625	1.625	0.000	0.000	0.000	0.000
159	A	165	ASN	0	-0.027	-0.036	11.826	-2.807	-2.807	0.000	0.000	0.000	0.000
160	A	166	ASP	-1	-0.799	-0.906	11.529	-27.378	-27.378	0.000	0.000	0.000	0.000
161	A	167	SER	0	-0.006	0.007	13.718	0.417	0.417	0.000	0.000	0.000	0.000
162	A	168	ASP	-1	-0.860	-0.923	14.254	-18.156	-18.156	0.000	0.000	0.000	0.000
163	A	169	LEU	0	-0.064	-0.014	9.970	-0.371	-0.371	0.000	0.000	0.000	0.000
164	A	170	ASP	-1	-0.764	-0.881	13.792	-14.384	-14.384	0.000	0.000	0.000	0.000
165	A	171	TYR	0	0.034	-0.007	12.839	0.088	0.088	0.000	0.000	0.000	0.000
166	A	172	LYS	1	0.874	0.943	16.719	14.314	14.314	0.000	0.000	0.000	0.000
167	A	173	LYS	1	0.865	0.928	15.936	15.796	15.796	0.000	0.000	0.000	0.000
168	A	174	VAL	0	-0.024	0.003	14.381	-0.306	-0.306	0.000	0.000	0.000	0.000
169	A	175	HIS	1	0.789	0.879	17.002	13.927	13.927	0.000	0.000	0.000	0.000
170	A	176	PHE	0	0.049	0.018	17.050	-0.648	-0.648	0.000	0.000	0.000	0.000
171	A	177	ASN	0	-0.013	-0.004	21.154	0.277	0.277	0.000	0.000	0.000	0.000
172	A	178	ASN	0	-0.020	-0.006	23.287	0.473	0.473	0.000	0.000	0.000	0.000
173	A	179	PHE	-1	-0.823	-0.883	22.658	-12.154	-12.154	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:7:MET)