FMO DATABASE

FMODB ID: QM3VY

Calculation Name: 7F76-B-Xray547

Preferred Name:

Target Type:

Ligand Name: flavin mononucleotide | isopropyl alcohol

Ligand 3-letter code: FMN | IPA

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 7F76

Chain ID: B

ChEMBL ID:

UniProt ID:

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	173
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1809075.608056
FMO2-HF: Nuclear repulsion	1741778.651895
FMO2-HF: Total energy	-67296.956162
FMO2-MP2: Total energy	-67494.213987

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:0:HIS)

Summations of interaction energy for fragment #1(A:0:HIS)

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.
-30.708	-27.003	2.198	-2.065	-3.839	-0.018

Interaction energy analysis for fragmet #1(A:0:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.849 / q_NPA : 0.904

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	2	GLN	0	-0.041	-0.018	3.863	2.195	3.429	-0.004	-0.418	-0.813	0.001
66	A	65	ASP	-1	-0.785	-0.879	4.999	-50.158	-50.085	-0.001	-0.010	-0.062	0.000
168	A	167	TYR	0	0.021	-0.005	2.195	-10.361	-8.075	2.204	-1.620	-2.870	-0.019
172	A	171	GLN	0	-0.093	-0.040	4.191	1.181	1.293	-0.001	-0.017	-0.094	0.000
4	A	3	LEU	0	-0.013	0.006	6.075	5.302	5.302	0.000	0.000	0.000	0.000
5	A	4	VAL	0	0.033	0.023	8.819	1.065	1.065	0.000	0.000	0.000	0.000
6	A	5	VAL	0	-0.023	-0.012	12.379	0.345	0.345	0.000	0.000	0.000	0.000
7	A	6	ILE	0	0.046	0.029	15.296	0.616	0.616	0.000	0.000	0.000	0.000
8	A	7	ASN	0	0.018	0.013	18.900	0.363	0.363	0.000	0.000	0.000	0.000
9	A	8	GLY	0	0.044	0.022	21.676	0.418	0.418	0.000	0.000	0.000	0.000
10	A	9	SER	0	-0.068	-0.023	24.607	0.806	0.806	0.000	0.000	0.000	0.000
11	A	10	PRO	0	0.075	0.038	26.819	-0.195	-0.195	0.000	0.000	0.000	0.000
12	A	11	ARG	1	0.921	0.957	29.092	9.721	9.721	0.000	0.000	0.000	0.000
13	A	12	LYS	1	0.967	0.968	28.320	9.782	9.782	0.000	0.000	0.000	0.000
14	A	13	SER	0	0.014	0.017	28.459	-0.275	-0.275	0.000	0.000	0.000	0.000
15	A	14	GLY	0	-0.045	-0.022	28.928	0.225	0.225	0.000	0.000	0.000	0.000
16	A	15	ARG	1	0.945	0.976	27.240	9.693	9.693	0.000	0.000	0.000	0.000
17	A	16	THR	0	0.039	0.014	23.081	-0.120	-0.120	0.000	0.000	0.000	0.000
18	A	17	ARG	1	0.891	0.952	22.410	12.247	12.247	0.000	0.000	0.000	0.000
19	A	18	ILE	0	-0.013	0.026	21.924	-0.523	-0.523	0.000	0.000	0.000	0.000
20	A	19	LEU	0	0.010	0.004	18.908	-0.511	-0.511	0.000	0.000	0.000	0.000
21	A	20	ALA	0	-0.006	-0.005	18.013	-0.879	-0.879	0.000	0.000	0.000	0.000
22	A	21	THR	0	0.043	0.001	16.881	-0.905	-0.905	0.000	0.000	0.000	0.000
23	A	22	PHE	0	-0.074	-0.028	16.352	-0.537	-0.537	0.000	0.000	0.000	0.000
24	A	23	ILE	0	0.012	-0.011	12.783	-0.958	-0.958	0.000	0.000	0.000	0.000
25	A	24	GLU	-1	-0.923	-0.967	12.353	-19.763	-19.763	0.000	0.000	0.000	0.000
26	A	25	LYS	1	0.910	0.947	12.182	14.165	14.165	0.000	0.000	0.000	0.000
27	A	26	GLU	-1	-0.931	-0.950	12.828	-20.287	-20.287	0.000	0.000	0.000	0.000
28	A	27	PHE	0	-0.063	-0.044	8.803	-1.441	-1.441	0.000	0.000	0.000	0.000
29	A	28	ASN	0	-0.044	-0.007	6.184	-2.037	-2.037	0.000	0.000	0.000	0.000
30	A	29	ALA	0	-0.013	0.006	7.925	-3.033	-3.033	0.000	0.000	0.000	0.000
31	A	30	LYS	1	0.988	0.978	10.293	23.958	23.958	0.000	0.000	0.000	0.000
32	A	31	ILE	0	0.010	0.014	12.553	0.321	0.321	0.000	0.000	0.000	0.000
33	A	32	ILE	0	0.006	0.005	16.059	0.173	0.173	0.000	0.000	0.000	0.000
34	A	33	ASP	-1	-0.701	-0.823	18.898	-12.763	-12.763	0.000	0.000	0.000	0.000
35	A	34	LEU	0	0.018	0.015	21.937	0.481	0.481	0.000	0.000	0.000	0.000
36	A	35	SER	0	-0.126	-0.077	25.019	0.673	0.673	0.000	0.000	0.000	0.000
37	A	36	GLU	-1	-0.957	-0.993	23.304	-12.859	-12.859	0.000	0.000	0.000	0.000
38	A	37	GLU	-1	-0.939	-0.954	27.112	-9.426	-9.426	0.000	0.000	0.000	0.000
39	A	38	THR	0	0.011	0.013	24.755	0.279	0.279	0.000	0.000	0.000	0.000
40	A	39	LEU	0	-0.042	-0.012	23.672	-0.067	-0.067	0.000	0.000	0.000	0.000
41	A	40	PRO	0	0.019	0.018	27.991	0.227	0.227	0.000	0.000	0.000	0.000
42	A	41	LEU	0	0.017	-0.001	30.719	-0.263	-0.263	0.000	0.000	0.000	0.000
43	A	42	TYR	0	0.014	0.011	30.675	0.090	0.090	0.000	0.000	0.000	0.000
44	A	43	ASN	0	0.001	-0.008	32.622	0.003	0.003	0.000	0.000	0.000	0.000
45	A	44	GLY	0	-0.007	0.000	33.189	0.203	0.203	0.000	0.000	0.000	0.000
46	A	45	GLU	-1	-0.933	-0.963	34.232	-8.266	-8.266	0.000	0.000	0.000	0.000
47	A	46	GLU	-1	-0.910	-0.963	33.423	-9.164	-9.164	0.000	0.000	0.000	0.000
48	A	47	TYR	0	0.018	0.009	32.672	-0.323	-0.323	0.000	0.000	0.000	0.000
49	A	48	GLN	0	-0.024	-0.036	30.919	-0.450	-0.450	0.000	0.000	0.000	0.000
50	A	49	GLY	0	-0.067	-0.037	28.377	-0.435	-0.435	0.000	0.000	0.000	0.000
51	A	50	GLU	-1	-0.877	-0.943	27.695	-11.119	-11.119	0.000	0.000	0.000	0.000
52	A	51	LEU	0	-0.052	-0.009	28.778	-0.142	-0.142	0.000	0.000	0.000	0.000
53	A	52	GLU	-1	-0.797	-0.886	25.230	-12.391	-12.391	0.000	0.000	0.000	0.000
54	A	53	HIS	0	0.032	0.014	23.761	-0.991	-0.991	0.000	0.000	0.000	0.000
55	A	54	VAL	0	0.004	0.008	23.373	-0.581	-0.581	0.000	0.000	0.000	0.000
56	A	55	ARG	1	0.833	0.908	23.106	11.931	11.931	0.000	0.000	0.000	0.000
57	A	56	ALA	0	0.030	0.018	19.843	-0.793	-0.793	0.000	0.000	0.000	0.000
58	A	57	LEU	0	-0.020	0.004	18.672	-1.241	-1.241	0.000	0.000	0.000	0.000
59	A	58	ARG	1	0.905	0.939	18.931	11.570	11.570	0.000	0.000	0.000	0.000
60	A	59	ASP	-1	-0.874	-0.942	17.343	-17.263	-17.263	0.000	0.000	0.000	0.000
61	A	60	THR	0	-0.088	-0.058	13.838	-1.814	-1.814	0.000	0.000	0.000	0.000
62	A	61	VAL	0	0.000	-0.011	13.817	-1.763	-1.763	0.000	0.000	0.000	0.000
63	A	62	LYS	1	0.823	0.899	14.561	15.323	15.323	0.000	0.000	0.000	0.000
64	A	63	LYS	1	0.844	0.915	11.554	18.687	18.687	0.000	0.000	0.000	0.000
65	A	64	ALA	0	-0.017	0.024	9.873	-2.748	-2.748	0.000	0.000	0.000	0.000
67	A	66	ALA	0	-0.023	-0.023	8.282	1.994	1.994	0.000	0.000	0.000	0.000
68	A	67	VAL	0	0.008	-0.001	10.183	-0.354	-0.354	0.000	0.000	0.000	0.000
69	A	68	ILE	0	-0.013	0.005	13.318	0.722	0.722	0.000	0.000	0.000	0.000
70	A	69	LEU	0	0.017	0.011	15.581	0.432	0.432	0.000	0.000	0.000	0.000
71	A	70	THR	0	-0.020	-0.039	18.672	0.551	0.551	0.000	0.000	0.000	0.000
72	A	71	SER	0	0.041	-0.014	21.165	0.272	0.272	0.000	0.000	0.000	0.000
73	A	72	PRO	0	-0.068	-0.009	24.984	0.020	0.020	0.000	0.000	0.000	0.000
74	A	73	GLU	-1	-0.787	-0.876	28.149	-10.011	-10.011	0.000	0.000	0.000	0.000
75	A	74	TYR	0	-0.058	-0.037	30.627	0.219	0.219	0.000	0.000	0.000	0.000
76	A	75	HIS	0	0.032	0.006	33.485	-0.102	-0.102	0.000	0.000	0.000	0.000
77	A	76	SER	0	0.000	0.007	34.138	0.101	0.101	0.000	0.000	0.000	0.000
78	A	77	GLY	0	0.055	0.034	31.598	0.011	0.011	0.000	0.000	0.000	0.000
79	A	78	MET	0	-0.013	-0.003	26.196	-0.221	-0.221	0.000	0.000	0.000	0.000
80	A	79	SER	0	-0.069	-0.048	27.798	0.415	0.415	0.000	0.000	0.000	0.000
81	A	80	GLY	0	0.057	0.015	29.465	-0.196	-0.196	0.000	0.000	0.000	0.000
82	A	81	ALA	0	0.017	0.013	28.325	-0.022	-0.022	0.000	0.000	0.000	0.000
83	A	82	LEU	0	0.036	0.007	22.409	-0.274	-0.274	0.000	0.000	0.000	0.000
84	A	83	LYS	1	0.810	0.874	25.868	10.363	10.363	0.000	0.000	0.000	0.000
85	A	84	ASN	0	0.008	0.006	28.168	0.172	0.172	0.000	0.000	0.000	0.000
86	A	85	ALA	0	0.009	0.002	23.678	-0.085	-0.085	0.000	0.000	0.000	0.000
87	A	86	LEU	0	-0.032	-0.037	21.657	-0.412	-0.412	0.000	0.000	0.000	0.000
88	A	87	ASP	-1	-0.797	-0.864	24.861	-10.853	-10.853	0.000	0.000	0.000	0.000
89	A	88	PHE	0	-0.006	0.011	25.406	0.162	0.162	0.000	0.000	0.000	0.000
90	A	89	LEU	0	-0.077	-0.021	20.192	-0.410	-0.410	0.000	0.000	0.000	0.000
91	A	90	SER	0	0.040	0.007	22.367	0.577	0.577	0.000	0.000	0.000	0.000
92	A	91	ASN	0	0.048	0.013	21.050	-0.668	-0.668	0.000	0.000	0.000	0.000
93	A	92	GLU	-1	-0.839	-0.892	20.172	-15.082	-15.082	0.000	0.000	0.000	0.000
94	A	93	GLN	0	-0.005	-0.001	18.094	-0.435	-0.435	0.000	0.000	0.000	0.000
95	A	94	PHE	0	0.026	-0.018	16.516	-1.455	-1.455	0.000	0.000	0.000	0.000
96	A	95	ALA	0	0.001	0.005	16.893	-0.434	-0.434	0.000	0.000	0.000	0.000
97	A	96	HIS	0	-0.044	-0.029	15.563	-1.131	-1.131	0.000	0.000	0.000	0.000
98	A	97	LYS	1	0.839	0.955	11.886	22.277	22.277	0.000	0.000	0.000	0.000
99	A	98	PRO	0	0.000	0.002	9.792	1.300	1.300	0.000	0.000	0.000	0.000
100	A	99	VAL	0	0.004	-0.002	12.649	-0.892	-0.892	0.000	0.000	0.000	0.000
101	A	100	GLY	0	0.036	0.023	15.055	0.740	0.740	0.000	0.000	0.000	0.000
102	A	101	LEU	0	-0.024	-0.011	16.317	0.193	0.193	0.000	0.000	0.000	0.000
103	A	102	ILE	0	0.002	-0.011	17.205	0.186	0.186	0.000	0.000	0.000	0.000
104	A	103	ALA	0	0.009	0.019	21.358	0.124	0.124	0.000	0.000	0.000	0.000
105	A	104	VAL	0	-0.044	-0.023	24.375	-0.063	-0.063	0.000	0.000	0.000	0.000
106	A	105	ALA	0	0.025	0.011	26.859	0.280	0.280	0.000	0.000	0.000	0.000
107	A	106	GLY	0	-0.030	-0.028	30.465	-0.027	-0.027	0.000	0.000	0.000	0.000
108	A	107	GLY	0	0.039	0.024	33.002	0.274	0.274	0.000	0.000	0.000	0.000
109	A	108	GLY	0	-0.014	-0.009	34.593	0.066	0.066	0.000	0.000	0.000	0.000
110	A	109	LYS	1	0.936	0.953	34.288	8.729	8.729	0.000	0.000	0.000	0.000
111	A	110	GLY	0	0.033	0.040	33.158	-0.029	-0.029	0.000	0.000	0.000	0.000
112	A	111	GLY	0	-0.002	-0.022	29.104	-0.233	-0.233	0.000	0.000	0.000	0.000
113	A	112	ILE	0	0.030	0.012	28.585	-0.400	-0.400	0.000	0.000	0.000	0.000
114	A	113	ASN	0	0.007	0.022	29.772	-0.204	-0.204	0.000	0.000	0.000	0.000
115	A	114	ALA	0	-0.005	-0.006	27.953	-0.139	-0.139	0.000	0.000	0.000	0.000
116	A	115	LEU	0	-0.001	-0.005	23.448	-0.321	-0.321	0.000	0.000	0.000	0.000
117	A	116	THR	0	0.005	-0.003	25.618	-0.347	-0.347	0.000	0.000	0.000	0.000
118	A	117	ASN	0	0.006	0.011	27.841	-0.191	-0.191	0.000	0.000	0.000	0.000
119	A	118	MET	0	-0.012	-0.016	22.439	0.061	0.061	0.000	0.000	0.000	0.000
120	A	119	ARG	1	0.828	0.911	20.633	13.496	13.496	0.000	0.000	0.000	0.000
121	A	120	THR	0	-0.048	-0.029	24.051	-0.095	-0.095	0.000	0.000	0.000	0.000
122	A	121	VAL	0	-0.010	-0.013	24.927	0.029	0.029	0.000	0.000	0.000	0.000
123	A	122	GLY	0	0.032	0.020	21.680	-0.166	-0.166	0.000	0.000	0.000	0.000
124	A	123	ARG	1	0.980	0.992	21.757	11.453	11.453	0.000	0.000	0.000	0.000
125	A	124	GLY	0	-0.058	-0.027	23.521	0.163	0.163	0.000	0.000	0.000	0.000
126	A	125	VAL	0	-0.027	-0.007	20.887	0.196	0.196	0.000	0.000	0.000	0.000
127	A	126	TYR	0	-0.043	-0.034	20.616	-0.569	-0.569	0.000	0.000	0.000	0.000
128	A	127	ALA	0	0.046	0.034	17.411	-0.604	-0.604	0.000	0.000	0.000	0.000
129	A	128	ASN	0	-0.059	-0.033	14.987	1.670	1.670	0.000	0.000	0.000	0.000
130	A	129	VAL	0	-0.038	-0.023	15.959	-0.956	-0.956	0.000	0.000	0.000	0.000
131	A	130	ILE	0	0.023	0.022	13.811	0.585	0.585	0.000	0.000	0.000	0.000
132	A	131	PRO	0	0.005	0.006	17.232	0.766	0.766	0.000	0.000	0.000	0.000
133	A	132	LYS	1	0.877	0.965	17.217	16.416	16.416	0.000	0.000	0.000	0.000
134	A	133	GLN	0	0.027	0.017	18.981	-0.685	-0.685	0.000	0.000	0.000	0.000
135	A	134	LEU	0	-0.016	-0.006	20.383	0.312	0.312	0.000	0.000	0.000	0.000
136	A	135	VAL	0	0.014	0.004	22.850	-0.021	-0.021	0.000	0.000	0.000	0.000
137	A	136	LEU	0	-0.011	-0.002	21.740	-0.001	-0.001	0.000	0.000	0.000	0.000
138	A	137	ASP	-1	-0.769	-0.906	25.921	-9.780	-9.780	0.000	0.000	0.000	0.000
139	A	138	PRO	0	-0.078	-0.061	28.953	-0.235	-0.235	0.000	0.000	0.000	0.000
140	A	139	HIS	0	0.061	0.032	29.949	0.139	0.139	0.000	0.000	0.000	0.000
141	A	140	CYS	0	-0.054	-0.008	25.412	-0.124	-0.124	0.000	0.000	0.000	0.000
142	A	141	PHE	0	-0.045	-0.040	24.065	-0.546	-0.546	0.000	0.000	0.000	0.000
143	A	142	ASP	-1	-0.741	-0.834	27.134	-9.820	-9.820	0.000	0.000	0.000	0.000
144	A	143	ARG	1	0.835	0.879	28.069	9.500	9.500	0.000	0.000	0.000	0.000
145	A	144	GLU	-1	-0.957	-0.953	30.181	-8.763	-8.763	0.000	0.000	0.000	0.000
146	A	145	ASN	0	-0.047	-0.048	28.396	0.045	0.045	0.000	0.000	0.000	0.000
147	A	146	TYR	0	-0.040	-0.013	23.837	-0.584	-0.584	0.000	0.000	0.000	0.000
148	A	147	THR	0	0.011	-0.012	23.196	-0.903	-0.903	0.000	0.000	0.000	0.000
149	A	148	LEU	0	-0.037	-0.008	19.771	0.403	0.403	0.000	0.000	0.000	0.000
150	A	149	THR	0	0.076	0.044	23.458	-0.200	-0.200	0.000	0.000	0.000	0.000
151	A	150	ASP	-1	-0.800	-0.907	22.504	-13.169	-13.169	0.000	0.000	0.000	0.000
152	A	151	ASP	-1	-0.875	-0.936	21.952	-12.148	-12.148	0.000	0.000	0.000	0.000
153	A	152	SER	0	-0.042	-0.037	22.493	-0.373	-0.373	0.000	0.000	0.000	0.000
154	A	153	LYS	1	0.854	0.932	18.392	13.266	13.266	0.000	0.000	0.000	0.000
155	A	154	LEU	0	0.004	0.018	17.621	-1.184	-1.184	0.000	0.000	0.000	0.000
156	A	155	LEU	0	-0.007	-0.013	18.366	-0.663	-0.663	0.000	0.000	0.000	0.000
157	A	156	VAL	0	-0.001	-0.008	15.768	-0.521	-0.521	0.000	0.000	0.000	0.000
158	A	157	LYS	1	0.885	0.927	11.794	21.480	21.480	0.000	0.000	0.000	0.000
159	A	158	GLY	0	0.029	0.018	13.834	-1.283	-1.283	0.000	0.000	0.000	0.000
160	A	159	VAL	0	-0.045	-0.034	15.686	-0.107	-0.107	0.000	0.000	0.000	0.000
161	A	160	ILE	0	0.003	0.005	9.394	-1.183	-1.183	0.000	0.000	0.000	0.000
162	A	161	ASP	-1	-0.848	-0.910	10.548	-26.538	-26.538	0.000	0.000	0.000	0.000
163	A	162	GLU	-1	-0.832	-0.926	11.085	-18.147	-18.147	0.000	0.000	0.000	0.000
164	A	163	LEU	0	-0.011	0.002	10.114	-0.692	-0.692	0.000	0.000	0.000	0.000
165	A	164	LYS	1	0.969	0.965	5.409	38.432	38.432	0.000	0.000	0.000	0.000
166	A	165	LEU	0	-0.061	-0.009	7.286	-2.532	-2.532	0.000	0.000	0.000	0.000
167	A	166	TYR	0	0.086	0.018	9.956	-0.044	-0.044	0.000	0.000	0.000	0.000
169	A	168	LYS	1	0.847	0.903	5.818	31.839	31.839	0.000	0.000	0.000	0.000
170	A	169	MET	0	-0.029	-0.006	7.385	0.762	0.762	0.000	0.000	0.000	0.000
171	A	170	HIS	0	0.026	0.024	9.644	1.977	1.977	0.000	0.000	0.000	0.000
173	A	172	TYR	-1	-0.952	-0.943	7.402	-21.449	-21.449	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:HIS)