FMO DATABASE

FMODB ID: KV9K3

Calculation Name: 1U3E-M-Xray547

Preferred Name:

Target Type:

Ligand Name: 2-amino-2-hydroxymethyl-propane-1,3-diol | 1,2-ethanediol | manganese (ii) ion | strontium ion

Ligand 3-letter code: TRS | EDO | MN | SR

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1U3E

Chain ID: M

ChEMBL ID:

UniProt ID: P34081

Base Structure: X-ray

Registration Date: 2025-10-05

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	174
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1491469.153425
FMO2-HF: Nuclear repulsion	1422439.39945
FMO2-HF: Total energy	-69029.753975
FMO2-MP2: Total energy	-69232.066857

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.
119.399	130.191	10.551	-7.237	-14.104	-0.064

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 : 0.757 / q_NPA : 0.891

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	TRP	0	0.038	0.004	2.876	6.298	9.267	1.808	-1.251	-3.526	-0.003
4	A	4	LYS	1	0.890	0.944	5.364	29.700	29.722	-0.001	-0.002	-0.019	0.000
16	A	16	SER	0	0.077	0.039	2.492	-5.453	-4.172	1.670	-0.998	-1.953	-0.002
17	A	17	ASN	0	0.025	0.004	2.639	-8.407	-6.080	1.175	-1.492	-2.010	-0.017
18	A	18	THR	0	0.011	-0.007	2.192	1.572	2.688	3.141	-1.248	-3.009	-0.009
19	A	19	GLY	0	0.029	0.010	4.652	3.893	3.967	-0.001	-0.011	-0.061	0.000
20	A	20	GLU	-1	-0.923	-0.960	2.653	-43.409	-40.406	2.759	-2.235	-3.526	-0.033
5	A	5	ASP	-1	-0.808	-0.897	8.973	-21.576	-21.576	0.000	0.000	0.000	0.000
6	A	6	ILE	0	-0.069	-0.024	11.663	0.092	0.092	0.000	0.000	0.000	0.000
7	A	7	LYS	1	0.945	0.959	13.525	19.598	19.598	0.000	0.000	0.000	0.000
8	A	8	GLY	0	-0.039	-0.016	16.726	0.493	0.493	0.000	0.000	0.000	0.000
9	A	9	TYR	0	-0.049	-0.039	16.392	1.108	1.108	0.000	0.000	0.000	0.000
10	A	10	GLU	-1	-0.712	-0.851	15.515	-16.398	-16.398	0.000	0.000	0.000	0.000
11	A	11	GLY	0	0.011	0.013	15.274	0.958	0.958	0.000	0.000	0.000	0.000
12	A	12	HIS	0	-0.080	-0.028	16.710	0.344	0.344	0.000	0.000	0.000	0.000
13	A	13	TYR	0	-0.039	-0.042	13.425	0.221	0.221	0.000	0.000	0.000	0.000
14	A	14	GLN	0	0.009	0.006	8.912	-0.921	-0.921	0.000	0.000	0.000	0.000
15	A	15	VAL	0	-0.021	-0.014	7.841	0.781	0.781	0.000	0.000	0.000	0.000
21	A	21	VAL	0	-0.001	-0.014	5.912	-0.109	-0.109	0.000	0.000	0.000	0.000
22	A	22	TYR	0	-0.002	0.007	8.025	0.700	0.700	0.000	0.000	0.000	0.000
23	A	23	SER	0	-0.033	-0.012	9.939	0.937	0.937	0.000	0.000	0.000	0.000
24	A	24	ILE	0	0.058	0.029	12.907	-0.073	-0.073	0.000	0.000	0.000	0.000
25	A	25	LYS	1	0.958	0.982	14.663	13.082	13.082	0.000	0.000	0.000	0.000
26	A	26	SER	0	-0.036	-0.029	15.688	0.575	0.575	0.000	0.000	0.000	0.000
27	A	27	GLY	0	0.046	0.040	14.671	0.310	0.310	0.000	0.000	0.000	0.000
28	A	28	LYS	1	0.957	0.983	11.791	13.833	13.833	0.000	0.000	0.000	0.000
29	A	29	THR	0	0.050	0.012	6.732	-0.060	-0.060	0.000	0.000	0.000	0.000
30	A	30	LEU	0	-0.081	-0.040	10.014	1.250	1.250	0.000	0.000	0.000	0.000
31	A	31	LYS	1	0.989	0.993	11.211	13.662	13.662	0.000	0.000	0.000	0.000
32	A	32	HIS	1	0.822	0.895	8.598	22.659	22.659	0.000	0.000	0.000	0.000
33	A	33	GLN	0	0.009	0.005	13.419	0.222	0.222	0.000	0.000	0.000	0.000
34	A	34	ILE	0	0.041	0.013	14.149	-0.532	-0.532	0.000	0.000	0.000	0.000
35	A	35	PRO	0	-0.014	-0.001	17.979	0.525	0.525	0.000	0.000	0.000	0.000
36	A	36	LYS	1	1.010	0.992	21.517	9.374	9.374	0.000	0.000	0.000	0.000
37	A	37	ASP	-1	-0.796	-0.878	21.331	-12.373	-12.373	0.000	0.000	0.000	0.000
38	A	38	GLY	0	0.036	0.014	19.449	-0.151	-0.151	0.000	0.000	0.000	0.000
39	A	39	TYR	0	-0.031	-0.015	17.254	-0.843	-0.843	0.000	0.000	0.000	0.000
40	A	40	HIS	0	0.019	0.013	11.884	-0.710	-0.710	0.000	0.000	0.000	0.000
41	A	41	ARG	1	0.834	0.901	14.777	12.613	12.613	0.000	0.000	0.000	0.000
42	A	42	ILE	0	0.014	0.021	12.749	-0.277	-0.277	0.000	0.000	0.000	0.000
43	A	43	GLY	0	0.020	0.011	15.885	0.497	0.497	0.000	0.000	0.000	0.000
44	A	44	LEU	0	-0.015	0.004	14.594	-0.488	-0.488	0.000	0.000	0.000	0.000
45	A	45	PHE	0	0.016	-0.006	18.632	0.649	0.649	0.000	0.000	0.000	0.000
46	A	46	LYS	1	0.898	0.933	20.819	12.440	12.440	0.000	0.000	0.000	0.000
47	A	47	GLY	0	0.030	0.022	23.337	0.356	0.356	0.000	0.000	0.000	0.000
48	A	48	GLY	0	0.009	0.005	25.840	0.349	0.349	0.000	0.000	0.000	0.000
49	A	49	LYS	1	0.952	0.975	26.544	9.645	9.645	0.000	0.000	0.000	0.000
50	A	50	GLY	0	0.036	0.032	22.956	-0.430	-0.430	0.000	0.000	0.000	0.000
51	A	51	LYS	1	0.931	0.964	22.062	12.571	12.571	0.000	0.000	0.000	0.000
52	A	52	THR	0	0.001	-0.003	19.912	-0.550	-0.550	0.000	0.000	0.000	0.000
53	A	53	PHE	0	-0.003	-0.003	16.783	0.259	0.259	0.000	0.000	0.000	0.000
54	A	54	GLN	0	0.013	-0.001	16.522	-0.164	-0.164	0.000	0.000	0.000	0.000
55	A	55	VAL	0	0.015	0.008	9.969	-0.223	-0.223	0.000	0.000	0.000	0.000
56	A	56	HIS	0	0.044	0.018	11.993	-1.458	-1.458	0.000	0.000	0.000	0.000
57	A	57	ARG	1	0.940	0.977	13.325	14.027	14.027	0.000	0.000	0.000	0.000
58	A	58	LEU	0	-0.002	0.011	12.147	-0.142	-0.142	0.000	0.000	0.000	0.000
59	A	59	VAL	0	0.027	0.034	8.304	-0.626	-0.626	0.000	0.000	0.000	0.000
60	A	60	ALA	0	0.046	0.009	10.507	-0.788	-0.788	0.000	0.000	0.000	0.000
61	A	61	ILE	0	-0.008	-0.003	13.498	0.373	0.373	0.000	0.000	0.000	0.000
62	A	62	HIS	0	-0.044	-0.024	10.314	1.535	1.535	0.000	0.000	0.000	0.000
63	A	63	PHE	0	-0.010	-0.016	6.280	-1.472	-1.472	0.000	0.000	0.000	0.000
64	A	64	CYS	0	-0.056	-0.006	10.393	-0.839	-0.839	0.000	0.000	0.000	0.000
65	A	65	GLU	-1	-0.856	-0.923	13.458	-18.903	-18.903	0.000	0.000	0.000	0.000
66	A	66	GLY	0	0.017	0.001	16.364	0.259	0.259	0.000	0.000	0.000	0.000
67	A	67	TYR	0	-0.088	-0.045	18.803	0.368	0.368	0.000	0.000	0.000	0.000
68	A	68	GLU	-1	-0.838	-0.930	20.539	-12.031	-12.031	0.000	0.000	0.000	0.000
69	A	69	GLU	-1	-0.937	-0.966	24.238	-10.530	-10.530	0.000	0.000	0.000	0.000
70	A	70	GLY	0	-0.025	-0.010	26.550	0.191	0.191	0.000	0.000	0.000	0.000
71	A	71	LEU	0	-0.076	-0.011	22.775	0.055	0.055	0.000	0.000	0.000	0.000
72	A	72	VAL	0	-0.044	-0.037	22.233	-0.228	-0.228	0.000	0.000	0.000	0.000
73	A	73	VAL	0	-0.014	-0.008	15.590	-0.296	-0.296	0.000	0.000	0.000	0.000
74	A	74	ASP	-1	-0.799	-0.881	18.910	-14.277	-14.277	0.000	0.000	0.000	0.000
75	A	75	HIS	1	0.784	0.877	14.079	16.413	16.413	0.000	0.000	0.000	0.000
76	A	76	LYS	1	0.910	0.957	14.608	20.179	20.179	0.000	0.000	0.000	0.000
77	A	77	ASP	-1	-0.744	-0.847	15.726	-16.955	-16.955	0.000	0.000	0.000	0.000
78	A	78	GLY	0	-0.036	-0.010	18.860	0.570	0.570	0.000	0.000	0.000	0.000
79	A	79	ASN	0	-0.025	-0.013	14.737	0.623	0.623	0.000	0.000	0.000	0.000
80	A	80	LYS	1	0.891	0.940	15.395	12.287	12.287	0.000	0.000	0.000	0.000
81	A	81	ASP	-1	-0.816	-0.897	12.894	-16.798	-16.798	0.000	0.000	0.000	0.000
82	A	82	ASN	0	-0.055	-0.032	10.916	-3.288	-3.288	0.000	0.000	0.000	0.000
83	A	83	ASN	0	-0.036	-0.030	9.330	1.397	1.397	0.000	0.000	0.000	0.000
84	A	84	LEU	0	0.072	0.050	6.078	-1.883	-1.883	0.000	0.000	0.000	0.000
85	A	85	SER	0	0.021	-0.006	7.562	1.234	1.234	0.000	0.000	0.000	0.000
86	A	86	THR	0	0.017	0.014	8.363	1.956	1.956	0.000	0.000	0.000	0.000
87	A	87	ASN	0	-0.029	-0.026	10.818	2.780	2.780	0.000	0.000	0.000	0.000
88	A	88	LEU	0	-0.044	-0.009	11.453	1.791	1.791	0.000	0.000	0.000	0.000
89	A	89	ARG	1	0.850	0.898	14.174	14.074	14.074	0.000	0.000	0.000	0.000
90	A	90	TRP	0	-0.032	0.002	16.352	1.025	1.025	0.000	0.000	0.000	0.000
91	A	91	VAL	0	-0.004	-0.008	19.626	0.318	0.318	0.000	0.000	0.000	0.000
92	A	92	THR	0	0.070	0.041	22.972	0.185	0.185	0.000	0.000	0.000	0.000
93	A	93	GLN	0	0.047	-0.003	26.550	-0.012	-0.012	0.000	0.000	0.000	0.000
94	A	94	LYS	1	0.887	0.943	27.948	9.128	9.128	0.000	0.000	0.000	0.000
95	A	95	ILE	0	0.096	0.042	25.661	0.044	0.044	0.000	0.000	0.000	0.000
96	A	96	ASN	0	-0.021	-0.004	23.678	-0.275	-0.275	0.000	0.000	0.000	0.000
97	A	97	VAL	0	0.015	0.009	26.190	0.070	0.070	0.000	0.000	0.000	0.000
98	A	98	GLU	-1	-0.833	-0.920	29.688	-9.566	-9.566	0.000	0.000	0.000	0.000
99	A	99	ASN	0	0.019	0.024	24.943	-0.033	-0.033	0.000	0.000	0.000	0.000
100	A	100	GLN	0	-0.021	-0.014	27.045	0.030	0.030	0.000	0.000	0.000	0.000
101	A	101	MET	0	-0.032	-0.018	28.879	0.287	0.287	0.000	0.000	0.000	0.000
102	A	102	SER	0	-0.010	0.004	29.789	0.221	0.221	0.000	0.000	0.000	0.000
103	A	103	ARG	1	0.903	0.940	24.499	11.759	11.759	0.000	0.000	0.000	0.000
104	A	104	GLY	0	0.036	0.037	29.929	0.067	0.067	0.000	0.000	0.000	0.000
105	A	105	THR	0	-0.086	-0.049	28.047	-0.059	-0.059	0.000	0.000	0.000	0.000
106	A	106	LEU	0	-0.013	0.000	30.398	-0.120	-0.120	0.000	0.000	0.000	0.000
107	A	107	ASN	0	-0.003	0.001	32.394	0.399	0.399	0.000	0.000	0.000	0.000
108	A	108	VAL	0	0.090	0.036	35.129	-0.024	-0.024	0.000	0.000	0.000	0.000
109	A	109	SER	0	0.048	0.027	38.240	0.126	0.126	0.000	0.000	0.000	0.000
110	A	110	LYS	1	0.922	0.948	37.991	7.476	7.476	0.000	0.000	0.000	0.000
111	A	111	ALA	0	0.016	0.009	38.717	0.119	0.119	0.000	0.000	0.000	0.000
112	A	112	GLN	0	0.028	0.003	40.601	0.202	0.202	0.000	0.000	0.000	0.000
113	A	113	GLN	0	0.027	0.020	43.052	0.023	0.023	0.000	0.000	0.000	0.000
114	A	114	ILE	0	0.000	-0.005	40.793	0.146	0.146	0.000	0.000	0.000	0.000
115	A	115	ALA	0	0.006	0.018	44.554	0.122	0.122	0.000	0.000	0.000	0.000
116	A	116	LYS	1	0.964	0.980	46.179	6.148	6.148	0.000	0.000	0.000	0.000
117	A	117	ILE	0	-0.002	0.009	47.381	0.143	0.143	0.000	0.000	0.000	0.000
118	A	118	LYS	1	0.989	0.973	43.149	6.898	6.898	0.000	0.000	0.000	0.000
119	A	119	ASN	0	-0.047	-0.020	47.150	-0.029	-0.029	0.000	0.000	0.000	0.000
120	A	120	GLN	0	-0.064	-0.015	50.491	0.206	0.206	0.000	0.000	0.000	0.000
121	A	121	LYS	1	0.957	0.974	53.108	5.686	5.686	0.000	0.000	0.000	0.000
122	A	122	PRO	0	0.062	0.034	55.831	0.065	0.065	0.000	0.000	0.000	0.000
123	A	123	ILE	0	-0.053	-0.022	59.048	-0.004	-0.004	0.000	0.000	0.000	0.000
124	A	124	ILE	0	0.044	0.026	62.519	-0.003	-0.003	0.000	0.000	0.000	0.000
125	A	125	VAL	0	-0.050	-0.027	66.110	-0.011	-0.011	0.000	0.000	0.000	0.000
126	A	126	ILE	0	0.040	0.016	68.748	0.013	0.013	0.000	0.000	0.000	0.000
127	A	127	SER	0	-0.020	-0.022	72.305	-0.030	-0.030	0.000	0.000	0.000	0.000
128	A	128	PRO	0	-0.040	-0.027	75.145	0.019	0.019	0.000	0.000	0.000	0.000
129	A	129	ASP	-1	-0.858	-0.932	78.404	-3.997	-3.997	0.000	0.000	0.000	0.000
130	A	130	GLY	0	0.009	0.011	77.484	0.037	0.037	0.000	0.000	0.000	0.000
131	A	131	ILE	0	-0.011	0.010	74.314	-0.042	-0.042	0.000	0.000	0.000	0.000
132	A	132	GLU	-1	-0.940	-0.972	70.874	-4.376	-4.376	0.000	0.000	0.000	0.000
133	A	133	LYS	1	0.923	0.963	66.629	4.615	4.615	0.000	0.000	0.000	0.000
134	A	134	GLU	-1	-0.842	-0.896	61.670	-4.983	-4.983	0.000	0.000	0.000	0.000
135	A	135	TYR	0	0.026	-0.007	62.863	0.003	0.003	0.000	0.000	0.000	0.000
136	A	136	PRO	0	0.042	0.008	57.547	-0.045	-0.045	0.000	0.000	0.000	0.000
137	A	137	SER	0	-0.010	-0.024	56.907	-0.074	-0.074	0.000	0.000	0.000	0.000
138	A	138	THR	0	0.043	0.020	58.947	0.057	0.057	0.000	0.000	0.000	0.000
139	A	139	LYS	1	0.907	0.951	56.643	5.478	5.478	0.000	0.000	0.000	0.000
140	A	140	CYS	0	0.023	0.031	59.898	0.064	0.064	0.000	0.000	0.000	0.000
141	A	141	ALA	0	0.096	0.049	61.571	0.062	0.062	0.000	0.000	0.000	0.000
142	A	142	CYS	0	-0.102	-0.044	63.473	0.069	0.069	0.000	0.000	0.000	0.000
143	A	143	GLU	-1	-0.967	-0.969	61.551	-5.016	-5.016	0.000	0.000	0.000	0.000
144	A	144	GLU	-1	-0.918	-0.968	64.805	-4.687	-4.687	0.000	0.000	0.000	0.000
145	A	145	LEU	0	-0.022	-0.005	67.301	0.072	0.072	0.000	0.000	0.000	0.000
146	A	146	GLY	0	0.043	0.054	68.739	0.054	0.054	0.000	0.000	0.000	0.000
147	A	147	LEU	0	-0.080	-0.036	67.327	0.048	0.048	0.000	0.000	0.000	0.000
148	A	148	THR	0	0.002	-0.013	66.149	-0.045	-0.045	0.000	0.000	0.000	0.000
149	A	149	ARG	1	1.010	0.975	56.790	5.338	5.338	0.000	0.000	0.000	0.000
150	A	150	GLY	0	0.006	0.020	62.654	-0.031	-0.031	0.000	0.000	0.000	0.000
151	A	151	LYS	1	0.871	0.943	63.599	4.720	4.720	0.000	0.000	0.000	0.000
152	A	152	VAL	0	0.056	0.030	64.349	0.016	0.016	0.000	0.000	0.000	0.000
153	A	153	THR	0	-0.042	-0.039	59.860	-0.043	-0.043	0.000	0.000	0.000	0.000
154	A	154	ASP	-1	-0.857	-0.941	62.936	-4.837	-4.837	0.000	0.000	0.000	0.000
155	A	155	VAL	0	-0.067	-0.024	65.440	0.016	0.016	0.000	0.000	0.000	0.000
156	A	156	LEU	0	-0.049	-0.010	61.527	0.008	0.008	0.000	0.000	0.000	0.000
157	A	157	LYS	1	0.840	0.919	57.437	5.278	5.278	0.000	0.000	0.000	0.000
158	A	158	GLY	0	0.050	0.046	63.679	-0.003	-0.003	0.000	0.000	0.000	0.000
159	A	159	HIS	0	0.007	0.008	62.166	0.094	0.094	0.000	0.000	0.000	0.000
160	A	160	ARG	1	0.887	0.936	67.602	4.528	4.528	0.000	0.000	0.000	0.000
161	A	161	ILE	0	0.111	0.056	69.929	-0.050	-0.050	0.000	0.000	0.000	0.000
162	A	162	HIS	0	0.006	0.014	72.387	0.035	0.035	0.000	0.000	0.000	0.000
163	A	163	HIS	0	-0.019	-0.025	69.554	-0.047	-0.047	0.000	0.000	0.000	0.000
164	A	164	LYS	1	0.874	0.927	70.469	4.428	4.428	0.000	0.000	0.000	0.000
165	A	165	GLY	0	0.064	0.044	74.812	0.023	0.023	0.000	0.000	0.000	0.000
166	A	166	TYR	0	0.077	0.052	71.801	0.013	0.013	0.000	0.000	0.000	0.000
167	A	167	THR	0	-0.027	-0.041	71.215	-0.043	-0.043	0.000	0.000	0.000	0.000
168	A	168	PHE	0	0.045	0.012	66.178	-0.021	-0.021	0.000	0.000	0.000	0.000
169	A	169	ARG	1	0.933	0.968	65.585	4.531	4.531	0.000	0.000	0.000	0.000
170	A	170	TYR	0	0.016	-0.004	59.152	-0.053	-0.053	0.000	0.000	0.000	0.000
171	A	171	LYS	1	0.877	0.937	60.329	5.051	5.051	0.000	0.000	0.000	0.000
172	A	172	LEU	0	-0.037	-0.017	59.419	-0.108	-0.108	0.000	0.000	0.000	0.000
173	A	173	ASN	0	-0.056	-0.037	57.561	0.075	0.075	0.000	0.000	0.000	0.000
174	A	174	GLY	-1	-0.892	-0.931	54.150	-5.589	-5.589	0.000	0.000	0.000	0.000

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