FMO DATABASE

FMODB ID: 5RK5Z

Calculation Name: 2FCR-A-Xray547

Preferred Name:

Target Type:

Ligand Name: flavin mononucleotide

Ligand 3-letter code: FMN

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2FCR

Chain ID: A

ChEMBL ID:

UniProt ID: P14070

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	-1781762.73403
FMO2-HF: Nuclear repulsion	1715244.70759
FMO2-HF: Total energy	-66518.026441
FMO2-MP2: Total energy	-66711.824307

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:LYS)

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

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.
-1006.268	-997.363	41.965	-25.409	-25.461	-0.294

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 2 / q_Mulliken : 1.563 / q_NPA : 1.777

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	GLY	0	0.059	0.027	3.075	-11.029	-8.643	0.101	-1.178	-1.310	-0.007
4	A	4	ILE	0	-0.041	-0.028	5.397	5.889	5.933	-0.001	-0.002	-0.040	0.000
26	A	26	ALA	0	-0.030	-0.031	3.786	-6.164	-5.862	0.000	-0.121	-0.181	0.000
27	A	27	LYS	1	0.778	0.877	1.964	34.224	34.930	5.243	-2.775	-3.174	-0.040
28	A	28	ALA	0	0.034	0.032	2.651	-21.523	-18.211	1.019	-2.030	-2.301	-0.022
29	A	29	ASP	-1	-0.843	-0.896	1.812	-199.980	-198.125	15.756	-8.722	-8.890	-0.109
30	A	30	ALA	0	-0.064	-0.042	3.317	11.295	11.517	0.021	-0.060	-0.183	-0.001
46	A	46	TYR	0	-0.130	-0.093	2.362	-21.519	-18.092	1.301	-1.555	-3.173	-0.017
47	A	47	ASP	-1	-0.882	-0.934	1.709	-149.107	-152.757	18.527	-8.929	-5.947	-0.098
48	A	48	LEU	0	-0.019	-0.014	4.489	11.677	11.857	-0.001	-0.027	-0.152	0.000
173	A	173	VAL	-1	-0.833	-0.886	4.349	-72.626	-72.505	-0.001	-0.010	-0.110	0.000
5	A	5	PHE	0	0.032	0.026	7.640	0.068	0.068	0.000	0.000	0.000	0.000
6	A	6	PHE	0	-0.003	-0.008	11.532	1.923	1.923	0.000	0.000	0.000	0.000
7	A	7	SER	0	0.040	0.007	14.945	0.776	0.776	0.000	0.000	0.000	0.000
8	A	8	THR	0	-0.026	-0.026	18.398	0.829	0.829	0.000	0.000	0.000	0.000
9	A	9	SER	0	0.037	0.029	21.179	0.696	0.696	0.000	0.000	0.000	0.000
10	A	10	THR	0	-0.034	-0.027	24.799	0.220	0.220	0.000	0.000	0.000	0.000
11	A	11	GLY	0	0.004	0.008	21.377	0.247	0.247	0.000	0.000	0.000	0.000
12	A	12	ASN	0	0.032	0.010	20.399	-0.900	-0.900	0.000	0.000	0.000	0.000
13	A	13	THR	0	0.025	0.002	17.415	-0.395	-0.395	0.000	0.000	0.000	0.000
14	A	14	THR	0	-0.004	0.005	15.512	-1.301	-1.301	0.000	0.000	0.000	0.000
15	A	15	GLU	-1	-0.901	-0.947	15.463	-29.367	-29.367	0.000	0.000	0.000	0.000
16	A	16	VAL	0	0.007	0.000	16.314	-1.413	-1.413	0.000	0.000	0.000	0.000
17	A	17	ALA	0	0.016	0.020	12.505	-2.263	-2.263	0.000	0.000	0.000	0.000
18	A	18	ASP	-1	-0.864	-0.947	11.438	-46.116	-46.116	0.000	0.000	0.000	0.000
19	A	19	PHE	0	-0.066	-0.029	11.945	-2.428	-2.428	0.000	0.000	0.000	0.000
20	A	20	ILE	0	0.037	0.027	9.944	-1.534	-1.534	0.000	0.000	0.000	0.000
21	A	21	GLY	0	0.080	0.037	7.918	-3.819	-3.819	0.000	0.000	0.000	0.000
22	A	22	LYS	1	0.767	0.883	8.155	48.658	48.658	0.000	0.000	0.000	0.000
23	A	23	THR	0	-0.047	-0.030	10.763	0.112	0.112	0.000	0.000	0.000	0.000
24	A	24	LEU	0	0.033	0.022	6.544	-0.412	-0.412	0.000	0.000	0.000	0.000
25	A	25	GLY	0	-0.022	-0.007	6.506	-5.031	-5.031	0.000	0.000	0.000	0.000
31	A	31	PRO	0	-0.016	-0.007	6.983	-1.997	-1.997	0.000	0.000	0.000	0.000
32	A	32	ILE	0	-0.016	0.005	8.173	2.366	2.366	0.000	0.000	0.000	0.000
33	A	33	ASP	-1	-0.776	-0.872	11.551	-32.467	-32.467	0.000	0.000	0.000	0.000
34	A	34	VAL	0	0.007	-0.021	15.125	-0.742	-0.742	0.000	0.000	0.000	0.000
35	A	35	ASP	-1	-0.895	-0.915	16.446	-27.049	-27.049	0.000	0.000	0.000	0.000
36	A	36	ASP	-1	-0.972	-0.975	15.220	-34.247	-34.247	0.000	0.000	0.000	0.000
37	A	37	VAL	0	-0.080	-0.033	13.057	-1.293	-1.293	0.000	0.000	0.000	0.000
38	A	38	THR	0	-0.061	-0.036	15.541	1.453	1.453	0.000	0.000	0.000	0.000
39	A	39	ASP	-1	-0.880	-0.946	14.266	-36.701	-36.701	0.000	0.000	0.000	0.000
40	A	40	PRO	0	0.025	0.020	13.804	-2.909	-2.909	0.000	0.000	0.000	0.000
41	A	41	GLN	0	-0.039	-0.051	13.114	-3.387	-3.387	0.000	0.000	0.000	0.000
42	A	42	ALA	0	0.041	0.027	9.411	-2.502	-2.502	0.000	0.000	0.000	0.000
43	A	43	LEU	0	-0.021	-0.013	7.880	-6.286	-6.286	0.000	0.000	0.000	0.000
44	A	44	LYS	1	0.892	0.945	8.530	38.483	38.483	0.000	0.000	0.000	0.000
45	A	45	ASP	-1	-0.976	-0.963	5.593	-62.727	-62.727	0.000	0.000	0.000	0.000
49	A	49	LEU	0	-0.033	0.006	6.354	-9.740	-9.740	0.000	0.000	0.000	0.000
50	A	50	PHE	0	0.005	-0.007	8.528	4.962	4.962	0.000	0.000	0.000	0.000
51	A	51	LEU	0	-0.014	-0.010	10.883	-1.327	-1.327	0.000	0.000	0.000	0.000
52	A	52	GLY	0	0.045	0.018	13.789	1.897	1.897	0.000	0.000	0.000	0.000
53	A	53	ALA	0	0.029	0.008	16.165	0.120	0.120	0.000	0.000	0.000	0.000
54	A	54	PRO	0	-0.054	0.005	19.786	0.282	0.282	0.000	0.000	0.000	0.000
55	A	55	THR	0	0.005	-0.010	23.259	-0.119	-0.119	0.000	0.000	0.000	0.000
56	A	56	TRP	0	-0.028	-0.012	26.074	0.902	0.902	0.000	0.000	0.000	0.000
57	A	57	ASN	0	-0.065	-0.024	29.256	1.249	1.249	0.000	0.000	0.000	0.000
58	A	58	THR	0	0.005	-0.008	31.328	-0.285	-0.285	0.000	0.000	0.000	0.000
59	A	59	GLY	0	0.011	0.012	33.199	0.504	0.504	0.000	0.000	0.000	0.000
60	A	60	ALA	0	-0.050	-0.011	31.319	0.334	0.334	0.000	0.000	0.000	0.000
61	A	61	ASP	-1	-0.959	-0.976	31.733	-19.454	-19.454	0.000	0.000	0.000	0.000
62	A	62	THR	0	0.015	0.010	28.430	-0.384	-0.384	0.000	0.000	0.000	0.000
63	A	63	GLU	-1	-0.982	-0.989	26.815	-20.112	-20.112	0.000	0.000	0.000	0.000
64	A	64	ARG	1	0.769	0.854	26.587	22.454	22.454	0.000	0.000	0.000	0.000
65	A	65	SER	0	-0.034	-0.038	23.109	-0.006	-0.006	0.000	0.000	0.000	0.000
66	A	66	GLY	0	-0.005	-0.006	25.187	0.174	0.174	0.000	0.000	0.000	0.000
67	A	67	THR	0	-0.064	-0.049	22.018	-0.639	-0.639	0.000	0.000	0.000	0.000
68	A	68	SER	0	0.020	-0.025	20.552	0.687	0.687	0.000	0.000	0.000	0.000
69	A	69	TRP	0	-0.052	-0.041	14.495	-0.745	-0.745	0.000	0.000	0.000	0.000
70	A	70	ASP	-1	-0.781	-0.862	20.815	-24.358	-24.358	0.000	0.000	0.000	0.000
71	A	71	GLU	-1	-0.843	-0.897	22.302	-26.066	-26.066	0.000	0.000	0.000	0.000
72	A	72	PHE	0	0.043	0.011	14.862	-0.284	-0.284	0.000	0.000	0.000	0.000
73	A	73	LEU	0	-0.021	-0.025	18.945	-0.847	-0.847	0.000	0.000	0.000	0.000
74	A	74	TYR	0	-0.103	-0.085	21.099	0.347	0.347	0.000	0.000	0.000	0.000
75	A	75	ASP	-1	-0.909	-0.957	23.451	-22.876	-22.876	0.000	0.000	0.000	0.000
76	A	76	LYS	1	0.802	0.897	18.286	29.571	29.571	0.000	0.000	0.000	0.000
77	A	77	LEU	0	-0.020	0.005	16.023	-0.963	-0.963	0.000	0.000	0.000	0.000
78	A	78	PRO	0	-0.026	-0.023	18.397	-0.654	-0.654	0.000	0.000	0.000	0.000
79	A	79	GLU	-1	-0.955	-0.972	18.681	-28.325	-28.325	0.000	0.000	0.000	0.000
80	A	80	VAL	0	-0.074	-0.019	13.326	-0.516	-0.516	0.000	0.000	0.000	0.000
81	A	81	ASP	-1	-0.940	-0.960	16.226	-33.198	-33.198	0.000	0.000	0.000	0.000
82	A	82	MET	0	-0.003	-0.015	11.187	-2.078	-2.078	0.000	0.000	0.000	0.000
83	A	83	LYS	1	0.938	0.976	13.505	29.913	29.913	0.000	0.000	0.000	0.000
84	A	84	ASP	-1	-0.980	-0.992	13.088	-35.931	-35.931	0.000	0.000	0.000	0.000
85	A	85	LEU	0	-0.023	0.009	7.805	-0.811	-0.811	0.000	0.000	0.000	0.000
86	A	86	PRO	0	-0.032	-0.007	8.792	3.082	3.082	0.000	0.000	0.000	0.000
87	A	87	VAL	0	0.019	-0.004	10.160	-4.613	-4.613	0.000	0.000	0.000	0.000
88	A	88	ALA	0	0.019	0.016	12.523	3.396	3.396	0.000	0.000	0.000	0.000
89	A	89	ILE	0	0.004	0.010	14.032	-1.545	-1.545	0.000	0.000	0.000	0.000
90	A	90	PHE	0	-0.022	-0.005	13.093	1.086	1.086	0.000	0.000	0.000	0.000
91	A	91	GLY	0	0.030	0.006	18.033	-0.310	-0.310	0.000	0.000	0.000	0.000
92	A	92	LEU	0	-0.033	-0.024	19.848	0.434	0.434	0.000	0.000	0.000	0.000
93	A	93	GLY	0	0.005	-0.018	23.341	0.353	0.353	0.000	0.000	0.000	0.000
94	A	94	ASP	-1	-0.838	-0.918	27.159	-19.202	-19.202	0.000	0.000	0.000	0.000
95	A	95	ALA	0	0.003	-0.013	30.539	0.179	0.179	0.000	0.000	0.000	0.000
96	A	96	GLU	-1	-0.953	-0.962	32.593	-16.523	-16.523	0.000	0.000	0.000	0.000
97	A	97	GLY	0	-0.058	-0.033	34.773	0.575	0.575	0.000	0.000	0.000	0.000
98	A	98	TYR	0	-0.074	-0.048	32.358	0.532	0.532	0.000	0.000	0.000	0.000
99	A	99	PRO	0	0.031	0.025	33.588	-0.555	-0.555	0.000	0.000	0.000	0.000
100	A	100	ASP	-1	-0.853	-0.932	35.406	-16.545	-16.545	0.000	0.000	0.000	0.000
101	A	101	ASN	0	-0.092	-0.068	32.308	0.362	0.362	0.000	0.000	0.000	0.000
102	A	102	PHE	0	0.042	0.039	27.760	-0.871	-0.871	0.000	0.000	0.000	0.000
103	A	103	CYS	0	-0.037	0.009	24.798	-0.681	-0.681	0.000	0.000	0.000	0.000
104	A	104	ASP	-1	-0.716	-0.842	25.856	-21.151	-21.151	0.000	0.000	0.000	0.000
105	A	105	ALA	0	-0.004	-0.003	23.697	-0.030	-0.030	0.000	0.000	0.000	0.000
106	A	106	ILE	0	-0.040	-0.003	20.978	-0.873	-0.873	0.000	0.000	0.000	0.000
107	A	107	GLU	-1	-0.757	-0.865	22.102	-22.667	-22.667	0.000	0.000	0.000	0.000
108	A	108	GLU	-1	-0.736	-0.822	23.895	-24.033	-24.033	0.000	0.000	0.000	0.000
109	A	109	ILE	0	0.040	0.020	17.485	-0.457	-0.457	0.000	0.000	0.000	0.000
110	A	110	HIS	0	-0.024	-0.035	19.390	-1.467	-1.467	0.000	0.000	0.000	0.000
111	A	111	ASP	-1	-0.778	-0.850	20.396	-24.795	-24.795	0.000	0.000	0.000	0.000
112	A	112	CYS	0	-0.047	-0.017	20.937	0.345	0.345	0.000	0.000	0.000	0.000
113	A	113	PHE	0	0.043	0.005	13.263	-0.649	-0.649	0.000	0.000	0.000	0.000
114	A	114	ALA	0	0.012	0.019	17.848	-0.486	-0.486	0.000	0.000	0.000	0.000
115	A	115	LYS	1	0.803	0.905	19.723	26.135	26.135	0.000	0.000	0.000	0.000
116	A	116	GLN	0	-0.043	-0.024	17.474	2.605	2.605	0.000	0.000	0.000	0.000
117	A	117	GLY	0	-0.025	-0.018	17.158	-1.187	-1.187	0.000	0.000	0.000	0.000
118	A	118	ALA	0	0.034	0.032	13.982	-0.826	-0.826	0.000	0.000	0.000	0.000
119	A	119	LYS	1	0.881	0.945	14.000	37.741	37.741	0.000	0.000	0.000	0.000
120	A	120	PRO	0	0.011	0.003	14.551	-2.401	-2.401	0.000	0.000	0.000	0.000
121	A	121	VAL	0	-0.066	-0.029	12.433	0.664	0.664	0.000	0.000	0.000	0.000
122	A	122	GLY	0	0.013	0.001	15.896	-0.458	-0.458	0.000	0.000	0.000	0.000
123	A	123	PHE	0	-0.005	0.003	17.406	0.647	0.647	0.000	0.000	0.000	0.000
124	A	124	SER	0	-0.053	-0.038	21.003	0.153	0.153	0.000	0.000	0.000	0.000
125	A	125	ASN	0	0.003	-0.018	23.511	0.958	0.958	0.000	0.000	0.000	0.000
126	A	126	PRO	0	-0.017	0.004	27.178	-0.318	-0.318	0.000	0.000	0.000	0.000
127	A	127	ASP	-1	-0.876	-0.930	29.453	-18.791	-18.791	0.000	0.000	0.000	0.000
128	A	128	ASP	-1	-0.884	-0.921	26.324	-23.554	-23.554	0.000	0.000	0.000	0.000
129	A	129	TYR	0	-0.036	-0.033	25.989	-0.571	-0.571	0.000	0.000	0.000	0.000
130	A	130	ASP	-1	-0.930	-0.952	31.426	-17.369	-17.369	0.000	0.000	0.000	0.000
131	A	131	TYR	0	-0.100	-0.069	30.867	-0.375	-0.375	0.000	0.000	0.000	0.000
132	A	132	GLU	-1	-0.958	-0.960	35.175	-15.894	-15.894	0.000	0.000	0.000	0.000
133	A	133	GLU	-1	-1.028	-1.016	34.790	-16.925	-16.925	0.000	0.000	0.000	0.000
134	A	134	SER	0	0.010	-0.030	29.167	-0.475	-0.475	0.000	0.000	0.000	0.000
135	A	135	LYS	1	0.835	0.919	29.814	19.467	19.467	0.000	0.000	0.000	0.000
136	A	136	SER	0	-0.056	-0.033	25.595	-0.503	-0.503	0.000	0.000	0.000	0.000
137	A	137	VAL	0	0.016	0.024	26.670	-0.922	-0.922	0.000	0.000	0.000	0.000
138	A	138	ARG	1	0.763	0.829	25.827	23.492	23.492	0.000	0.000	0.000	0.000
139	A	139	ASP	-1	-0.973	-1.001	27.975	-21.904	-21.904	0.000	0.000	0.000	0.000
140	A	140	GLY	0	-0.025	-0.010	29.549	-0.158	-0.158	0.000	0.000	0.000	0.000
141	A	141	LYS	1	0.863	0.952	23.833	23.907	23.907	0.000	0.000	0.000	0.000
142	A	142	PHE	0	0.079	0.037	24.405	0.232	0.232	0.000	0.000	0.000	0.000
143	A	143	LEU	0	-0.067	-0.047	22.911	-1.032	-1.032	0.000	0.000	0.000	0.000
144	A	144	GLY	0	0.042	0.012	19.718	-1.396	-1.396	0.000	0.000	0.000	0.000
145	A	145	LEU	0	-0.029	0.001	18.805	1.384	1.384	0.000	0.000	0.000	0.000
146	A	146	PRO	0	0.018	0.028	20.865	-0.746	-0.746	0.000	0.000	0.000	0.000
147	A	147	LEU	0	-0.012	-0.030	19.513	-0.264	-0.264	0.000	0.000	0.000	0.000
148	A	148	ASP	-1	-0.724	-0.833	23.957	-20.689	-20.689	0.000	0.000	0.000	0.000
149	A	149	MET	0	-0.028	-0.019	21.949	-0.523	-0.523	0.000	0.000	0.000	0.000
150	A	150	VAL	0	-0.041	-0.008	26.373	0.166	0.166	0.000	0.000	0.000	0.000
151	A	151	ASN	0	-0.072	-0.075	29.996	1.082	1.082	0.000	0.000	0.000	0.000
152	A	152	ASP	-1	-0.965	-0.964	27.727	-21.670	-21.670	0.000	0.000	0.000	0.000
153	A	153	GLN	0	-0.012	-0.025	29.625	-0.453	-0.453	0.000	0.000	0.000	0.000
154	A	154	ILE	0	-0.056	-0.030	26.007	0.060	0.060	0.000	0.000	0.000	0.000
155	A	155	PRO	0	-0.049	-0.011	25.092	-0.527	-0.527	0.000	0.000	0.000	0.000
156	A	156	MET	0	0.075	0.046	18.462	-1.289	-1.289	0.000	0.000	0.000	0.000
157	A	157	GLU	-1	-0.861	-0.947	19.036	-28.678	-28.678	0.000	0.000	0.000	0.000
158	A	158	LYS	1	0.884	0.927	19.238	23.325	23.325	0.000	0.000	0.000	0.000
159	A	159	ARG	1	0.795	0.893	21.558	25.392	25.392	0.000	0.000	0.000	0.000
160	A	160	VAL	0	0.027	0.016	15.651	-0.712	-0.712	0.000	0.000	0.000	0.000
161	A	161	ALA	0	0.005	0.002	15.832	-1.848	-1.848	0.000	0.000	0.000	0.000
162	A	162	GLY	0	0.029	0.019	16.525	-1.429	-1.429	0.000	0.000	0.000	0.000
163	A	163	TRP	0	-0.031	-0.023	14.737	-0.994	-0.994	0.000	0.000	0.000	0.000
164	A	164	VAL	0	0.010	0.002	11.590	-1.325	-1.325	0.000	0.000	0.000	0.000
165	A	165	GLU	-1	-0.956	-0.982	13.194	-36.561	-36.561	0.000	0.000	0.000	0.000
166	A	166	ALA	0	-0.022	0.004	15.246	-0.312	-0.312	0.000	0.000	0.000	0.000
167	A	167	VAL	0	0.055	0.030	11.250	0.117	0.117	0.000	0.000	0.000	0.000
168	A	168	VAL	0	-0.031	0.000	9.405	-1.904	-1.904	0.000	0.000	0.000	0.000
169	A	169	SER	0	-0.089	-0.057	11.536	0.223	0.223	0.000	0.000	0.000	0.000
170	A	170	GLU	-1	-0.924	-0.968	14.445	-33.811	-33.811	0.000	0.000	0.000	0.000
171	A	171	THR	0	-0.044	-0.047	9.446	-0.895	-0.895	0.000	0.000	0.000	0.000
172	A	172	GLY	0	-0.052	-0.016	10.231	-0.580	-0.580	0.000	0.000	0.000	0.000

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