FMO DATABASE

FMODB ID: 9L1N2

Calculation Name: 1VQ2-A-Xray547

Preferred Name:

Target Type:

Ligand Name: 3,4-dihydro-2'-deoxyuridine-5'-monophosphate | zinc ion

Ligand 3-letter code: DDN | ZN

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1VQ2

Chain ID: A

ChEMBL ID:

UniProt ID: P16006

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1745306.463491
FMO2-HF: Nuclear repulsion	1677029.598204
FMO2-HF: Total energy	-68276.865286
FMO2-MP2: Total energy	-68471.281885

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.
-106.069	-97.209	23.537	-14.542	-17.854	-0.163

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 : 0.779 / q_NPA : 0.892

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	ALA	0	0.103	0.053	3.784	0.191	1.521	0.002	-0.490	-0.842	0.001
5	A	5	THR	0	-0.060	-0.014	3.135	3.498	4.145	0.054	-0.140	-0.561	0.000
6	A	6	VAL	0	0.039	0.017	2.306	1.789	2.398	2.632	-0.899	-2.342	-0.003
7	A	7	LEU	0	0.018	0.017	4.873	3.928	4.014	-0.001	-0.015	-0.070	0.000
9	A	9	ILE	0	0.007	0.005	3.753	1.112	1.442	0.010	-0.055	-0.285	0.000
29	A	29	GLU	-1	-0.795	-0.917	2.059	-149.114	-148.059	16.789	-9.698	-8.147	-0.124
32	A	32	GLY	0	-0.038	-0.011	2.188	0.785	1.273	1.204	-0.909	-0.782	-0.003
33	A	33	ARG	1	0.937	0.954	2.511	28.505	31.952	1.764	-2.072	-3.138	-0.031
34	A	34	ILE	0	-0.001	0.001	2.385	-0.937	-0.391	1.084	-0.183	-1.447	-0.003
35	A	35	ILE	0	-0.026	-0.017	4.787	2.800	2.880	-0.001	-0.009	-0.070	0.000
106	A	126	TYR	0	-0.038	-0.028	3.331	2.422	2.664	0.000	-0.072	-0.170	0.000
4	A	4	SER	0	0.048	0.019	6.037	0.395	0.395	0.000	0.000	0.000	0.000
8	A	8	GLN	0	0.008	-0.010	8.071	4.768	4.768	0.000	0.000	0.000	0.000
10	A	10	ALA	0	0.004	0.002	7.751	2.052	2.052	0.000	0.000	0.000	0.000
11	A	11	TYR	0	-0.003	-0.059	9.910	1.548	1.548	0.000	0.000	0.000	0.000
12	A	12	LEU	0	-0.016	0.014	9.658	1.455	1.455	0.000	0.000	0.000	0.000
13	A	13	VAL	0	0.012	0.005	9.641	1.138	1.138	0.000	0.000	0.000	0.000
14	A	14	SER	0	-0.027	-0.032	12.445	1.408	1.408	0.000	0.000	0.000	0.000
15	A	15	GLN	0	-0.042	-0.033	15.472	1.642	1.642	0.000	0.000	0.000	0.000
16	A	16	GLU	-1	-0.908	-0.938	15.588	-14.137	-14.137	0.000	0.000	0.000	0.000
17	A	17	SER	0	-0.035	-0.010	18.109	0.991	0.991	0.000	0.000	0.000	0.000
18	A	18	LYS	1	0.909	0.946	20.166	12.776	12.776	0.000	0.000	0.000	0.000
19	A	19	CYS	0	-0.074	-0.014	23.068	0.579	0.579	0.000	0.000	0.000	0.000
20	A	20	CYS	0	-0.028	-0.025	24.829	-0.064	-0.064	0.000	0.000	0.000	0.000
21	A	21	SER	0	0.061	0.027	26.797	0.200	0.200	0.000	0.000	0.000	0.000
22	A	22	TRP	0	0.031	-0.020	21.577	-0.199	-0.199	0.000	0.000	0.000	0.000
23	A	23	LYS	1	0.807	0.919	18.898	12.632	12.632	0.000	0.000	0.000	0.000
24	A	24	VAL	0	-0.013	-0.015	16.490	-0.580	-0.580	0.000	0.000	0.000	0.000
25	A	25	GLY	0	0.050	0.011	13.635	0.430	0.430	0.000	0.000	0.000	0.000
26	A	26	ALA	0	-0.046	-0.020	11.541	-0.786	-0.786	0.000	0.000	0.000	0.000
27	A	27	VAL	0	-0.002	-0.005	5.319	-0.045	-0.045	0.000	0.000	0.000	0.000
28	A	28	ILE	0	0.020	0.016	8.392	-1.186	-1.186	0.000	0.000	0.000	0.000
30	A	30	LYS	1	0.985	0.993	6.085	27.406	27.406	0.000	0.000	0.000	0.000
31	A	31	ASN	0	0.008	0.003	6.613	-2.882	-2.882	0.000	0.000	0.000	0.000
36	A	36	SER	0	0.008	-0.005	8.471	2.788	2.788	0.000	0.000	0.000	0.000
37	A	37	THR	0	-0.051	-0.029	7.966	-2.818	-2.818	0.000	0.000	0.000	0.000
38	A	38	GLY	0	0.081	0.044	10.639	1.320	1.320	0.000	0.000	0.000	0.000
39	A	39	TYR	0	0.024	0.010	13.703	-0.863	-0.863	0.000	0.000	0.000	0.000
40	A	40	ASN	0	0.011	0.003	16.375	-0.120	-0.120	0.000	0.000	0.000	0.000
41	A	41	GLY	0	0.020	0.011	20.030	0.137	0.137	0.000	0.000	0.000	0.000
42	A	42	SER	0	-0.004	-0.020	22.829	-0.195	-0.195	0.000	0.000	0.000	0.000
43	A	43	PRO	0	0.009	0.015	24.311	-0.352	-0.352	0.000	0.000	0.000	0.000
44	A	44	ALA	0	0.029	0.011	25.473	0.235	0.235	0.000	0.000	0.000	0.000
45	A	45	GLY	0	-0.019	-0.010	26.871	0.208	0.208	0.000	0.000	0.000	0.000
46	A	46	GLY	0	-0.022	0.003	29.065	0.332	0.332	0.000	0.000	0.000	0.000
47	A	47	VAL	0	0.016	0.017	29.367	-0.198	-0.198	0.000	0.000	0.000	0.000
48	A	48	ASN	0	-0.006	0.007	25.961	-0.557	-0.557	0.000	0.000	0.000	0.000
49	A	49	CYS	0	-0.010	0.035	26.798	0.293	0.293	0.000	0.000	0.000	0.000
50	A	50	CYS	0	-0.040	-0.024	27.577	0.141	0.141	0.000	0.000	0.000	0.000
51	A	51	ASP	-1	-0.816	-0.910	29.354	-9.546	-9.546	0.000	0.000	0.000	0.000
52	A	52	TYR	0	0.012	0.000	31.761	0.332	0.332	0.000	0.000	0.000	0.000
53	A	53	ALA	0	0.021	-0.001	31.818	0.235	0.235	0.000	0.000	0.000	0.000
54	A	54	ALA	0	-0.029	-0.014	33.635	0.195	0.195	0.000	0.000	0.000	0.000
55	A	55	GLU	-1	-0.972	-0.985	35.543	-7.963	-7.963	0.000	0.000	0.000	0.000
56	A	56	GLN	0	-0.074	-0.034	36.828	0.324	0.324	0.000	0.000	0.000	0.000
57	A	57	GLY	0	-0.019	0.002	38.298	0.102	0.102	0.000	0.000	0.000	0.000
58	A	58	TRP	0	0.003	-0.013	32.311	-0.172	-0.172	0.000	0.000	0.000	0.000
59	A	59	LEU	0	-0.053	-0.020	31.410	-0.210	-0.210	0.000	0.000	0.000	0.000
60	A	60	LEU	0	0.053	0.039	34.865	0.280	0.280	0.000	0.000	0.000	0.000
61	A	61	ASN	0	-0.027	-0.035	34.403	-0.481	-0.481	0.000	0.000	0.000	0.000
62	A	62	LYS	-1	-0.781	-0.853	33.208	-9.028	-9.028	0.000	0.000	0.000	0.000
63	A	83	ARG	2	1.555	1.742	30.215	18.426	18.426	0.000	0.000	0.000	0.000
64	A	84	PHE	0	0.091	0.033	30.049	0.206	0.206	0.000	0.000	0.000	0.000
65	A	85	VAL	0	0.050	0.045	29.620	-0.368	-0.368	0.000	0.000	0.000	0.000
66	A	86	LEU	0	-0.036	-0.014	30.212	0.307	0.307	0.000	0.000	0.000	0.000
67	A	87	ALA	0	0.036	0.024	32.305	-0.084	-0.084	0.000	0.000	0.000	0.000
68	A	88	LYS	1	0.799	0.850	34.062	9.025	9.025	0.000	0.000	0.000	0.000
69	A	89	GLU	-1	-0.939	-0.962	35.958	-7.577	-7.577	0.000	0.000	0.000	0.000
70	A	90	HIS	0	0.032	0.012	36.365	-0.066	-0.066	0.000	0.000	0.000	0.000
71	A	91	ARG	1	0.822	0.895	28.034	10.472	10.472	0.000	0.000	0.000	0.000
72	A	92	SER	0	-0.054	-0.023	33.099	-0.291	-0.291	0.000	0.000	0.000	0.000
73	A	93	ALA	0	0.073	0.036	34.884	-0.152	-0.152	0.000	0.000	0.000	0.000
74	A	94	HIS	0	-0.027	-0.022	27.433	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	95	SER	0	-0.004	-0.022	30.489	-0.348	-0.348	0.000	0.000	0.000	0.000
76	A	96	GLU	-1	-0.918	-0.937	31.502	-8.534	-8.534	0.000	0.000	0.000	0.000
77	A	97	TRP	0	-0.005	0.006	28.721	-0.115	-0.115	0.000	0.000	0.000	0.000
78	A	98	SER	0	-0.029	-0.036	27.130	-0.219	-0.219	0.000	0.000	0.000	0.000
79	A	99	SER	0	-0.030	-0.041	28.388	-0.372	-0.372	0.000	0.000	0.000	0.000
80	A	100	LYS	1	0.873	0.946	29.698	8.581	8.581	0.000	0.000	0.000	0.000
81	A	101	ASN	0	-0.063	-0.034	29.274	0.300	0.300	0.000	0.000	0.000	0.000
82	A	102	GLU	-1	-0.748	-0.858	24.467	-11.805	-11.805	0.000	0.000	0.000	0.000
83	A	103	ILE	0	0.016	0.026	21.091	-0.159	-0.159	0.000	0.000	0.000	0.000
84	A	104	HIS	0	0.010	-0.013	20.103	-0.270	-0.270	0.000	0.000	0.000	0.000
85	A	105	ALA	0	0.007	0.022	15.260	-0.194	-0.194	0.000	0.000	0.000	0.000
86	A	106	GLU	-1	-0.806	-0.950	14.873	-17.745	-17.745	0.000	0.000	0.000	0.000
87	A	107	LEU	0	0.000	-0.003	15.955	-0.499	-0.499	0.000	0.000	0.000	0.000
88	A	108	ASN	0	0.033	0.005	17.033	0.372	0.372	0.000	0.000	0.000	0.000
89	A	109	ALA	0	-0.014	0.012	12.384	-0.158	-0.158	0.000	0.000	0.000	0.000
90	A	110	ILE	0	-0.012	-0.001	14.363	-0.578	-0.578	0.000	0.000	0.000	0.000
91	A	111	LEU	0	-0.004	-0.003	16.650	0.339	0.339	0.000	0.000	0.000	0.000
92	A	112	PHE	0	0.047	0.030	13.118	0.190	0.190	0.000	0.000	0.000	0.000
93	A	113	ALA	0	-0.017	-0.009	14.210	-0.010	-0.010	0.000	0.000	0.000	0.000
94	A	114	ALA	0	-0.045	-0.022	15.910	0.321	0.321	0.000	0.000	0.000	0.000
95	A	115	GLU	-1	-0.982	-0.985	19.598	-13.207	-13.207	0.000	0.000	0.000	0.000
96	A	116	ASN	0	-0.032	-0.020	15.202	1.058	1.058	0.000	0.000	0.000	0.000
97	A	117	GLY	0	0.016	0.021	18.294	-0.112	-0.112	0.000	0.000	0.000	0.000
98	A	118	SER	0	-0.079	-0.034	13.508	-0.580	-0.580	0.000	0.000	0.000	0.000
99	A	119	SER	0	-0.001	-0.014	15.096	-0.936	-0.936	0.000	0.000	0.000	0.000
100	A	120	ILE	0	0.037	0.003	12.245	-1.840	-1.840	0.000	0.000	0.000	0.000
101	A	121	GLU	-1	-0.836	-0.904	13.557	-19.950	-19.950	0.000	0.000	0.000	0.000
102	A	122	GLY	0	-0.026	-0.014	12.989	-0.980	-0.980	0.000	0.000	0.000	0.000
103	A	123	ALA	0	-0.077	-0.024	9.383	-2.814	-2.814	0.000	0.000	0.000	0.000
104	A	124	THR	0	-0.009	-0.009	6.200	1.291	1.291	0.000	0.000	0.000	0.000
105	A	125	MET	0	-0.014	0.006	8.008	-1.989	-1.989	0.000	0.000	0.000	0.000
107	A	127	VAL	0	0.020	0.002	9.416	0.882	0.882	0.000	0.000	0.000	0.000
108	A	128	THR	0	0.020	0.017	12.464	-0.192	-0.192	0.000	0.000	0.000	0.000
109	A	129	LEU	0	0.022	0.019	14.383	0.363	0.363	0.000	0.000	0.000	0.000
110	A	130	SER	0	-0.017	-0.012	17.161	-0.282	-0.282	0.000	0.000	0.000	0.000
111	A	131	PRO	0	0.030	0.031	16.884	0.740	0.740	0.000	0.000	0.000	0.000
112	A	132	CYS	0	-0.010	0.030	19.631	0.454	0.454	0.000	0.000	0.000	0.000
113	A	133	PRO	0	0.041	0.003	22.783	-0.413	-0.413	0.000	0.000	0.000	0.000
114	A	134	ASP	-1	-0.814	-0.915	24.779	-11.729	-11.729	0.000	0.000	0.000	0.000
115	A	135	CYS	0	0.013	0.006	19.310	-0.226	-0.226	0.000	0.000	0.000	0.000
116	A	136	ALA	0	-0.014	-0.005	19.912	-0.697	-0.697	0.000	0.000	0.000	0.000
117	A	137	LYS	1	0.856	0.924	20.898	11.268	11.268	0.000	0.000	0.000	0.000
118	A	138	ALA	0	0.007	0.014	21.006	0.022	0.022	0.000	0.000	0.000	0.000
119	A	139	ILE	0	-0.010	-0.019	15.552	-0.430	-0.430	0.000	0.000	0.000	0.000
120	A	140	ALA	0	-0.014	0.009	18.099	-0.575	-0.575	0.000	0.000	0.000	0.000
121	A	141	GLN	0	0.004	0.011	20.286	0.082	0.082	0.000	0.000	0.000	0.000
122	A	142	SER	0	-0.059	-0.046	16.844	-0.348	-0.348	0.000	0.000	0.000	0.000
123	A	143	GLY	0	0.047	0.023	17.448	-0.336	-0.336	0.000	0.000	0.000	0.000
124	A	144	ILE	0	-0.060	-0.030	11.698	-1.287	-1.287	0.000	0.000	0.000	0.000
125	A	145	LYS	1	0.885	0.932	12.354	20.443	20.443	0.000	0.000	0.000	0.000
126	A	146	LYS	1	0.804	0.916	7.499	34.957	34.957	0.000	0.000	0.000	0.000
127	A	147	LEU	0	0.015	0.018	11.026	-1.156	-1.156	0.000	0.000	0.000	0.000
128	A	148	VAL	0	-0.042	-0.025	8.092	0.248	0.248	0.000	0.000	0.000	0.000
129	A	149	TYR	0	0.017	0.006	11.005	-0.480	-0.480	0.000	0.000	0.000	0.000
130	A	150	CYS	0	-0.097	-0.026	13.422	-0.127	-0.127	0.000	0.000	0.000	0.000
131	A	151	GLU	-1	-0.793	-0.891	14.944	-14.952	-14.952	0.000	0.000	0.000	0.000
132	A	152	THR	0	-0.019	-0.023	18.647	-0.525	-0.525	0.000	0.000	0.000	0.000
133	A	153	TYR	0	0.007	-0.005	21.330	0.604	0.604	0.000	0.000	0.000	0.000
134	A	154	ASP	-1	-0.797	-0.882	23.177	-10.675	-10.675	0.000	0.000	0.000	0.000
135	A	155	LYS	1	0.918	0.976	26.264	10.900	10.900	0.000	0.000	0.000	0.000
136	A	156	ASN	0	-0.026	-0.022	22.299	0.585	0.585	0.000	0.000	0.000	0.000
137	A	157	LYS	1	0.889	0.959	26.388	11.571	11.571	0.000	0.000	0.000	0.000
138	A	158	PRO	0	0.049	0.004	26.295	-0.543	-0.543	0.000	0.000	0.000	0.000
139	A	159	GLY	0	0.098	0.050	25.150	0.368	0.368	0.000	0.000	0.000	0.000
140	A	160	TRP	0	-0.066	-0.033	17.511	0.003	0.003	0.000	0.000	0.000	0.000
141	A	161	ASP	-1	-0.786	-0.889	19.544	-15.489	-15.489	0.000	0.000	0.000	0.000
142	A	162	ASP	-1	-0.879	-0.936	21.283	-12.808	-12.808	0.000	0.000	0.000	0.000
143	A	163	ILE	0	-0.046	-0.031	22.216	-0.008	-0.008	0.000	0.000	0.000	0.000
144	A	164	LEU	0	-0.023	-0.003	16.950	-0.186	-0.186	0.000	0.000	0.000	0.000
145	A	165	ARG	1	0.881	0.922	19.606	15.476	15.476	0.000	0.000	0.000	0.000
146	A	166	ASN	0	-0.021	-0.016	20.764	-0.056	-0.056	0.000	0.000	0.000	0.000
147	A	167	ALA	0	-0.016	0.010	20.416	0.420	0.420	0.000	0.000	0.000	0.000
148	A	168	GLY	0	-0.025	-0.009	19.717	-0.380	-0.380	0.000	0.000	0.000	0.000
149	A	169	ILE	0	-0.069	-0.016	14.428	-1.071	-1.071	0.000	0.000	0.000	0.000
150	A	170	GLU	-1	-0.842	-0.925	11.320	-26.234	-26.234	0.000	0.000	0.000	0.000
151	A	171	VAL	0	0.007	-0.008	13.805	-1.116	-1.116	0.000	0.000	0.000	0.000
152	A	172	PHE	0	-0.041	-0.017	11.623	0.447	0.447	0.000	0.000	0.000	0.000
153	A	173	ASN	0	-0.032	-0.021	13.634	-0.050	-0.050	0.000	0.000	0.000	0.000
154	A	174	VAL	0	-0.023	-0.017	10.089	-1.000	-1.000	0.000	0.000	0.000	0.000
155	A	175	PRO	0	0.063	0.041	13.450	0.311	0.311	0.000	0.000	0.000	0.000
156	A	176	LYS	1	0.914	0.930	15.252	15.804	15.804	0.000	0.000	0.000	0.000
157	A	177	LYS	1	0.959	0.987	15.893	15.478	15.478	0.000	0.000	0.000	0.000
158	A	178	ASN	0	-0.082	-0.046	12.484	0.577	0.577	0.000	0.000	0.000	0.000
159	A	179	LEU	0	-0.054	-0.018	10.829	-2.127	-2.127	0.000	0.000	0.000	0.000
160	A	180	ASN	0	-0.010	-0.002	12.636	0.131	0.131	0.000	0.000	0.000	0.000
161	A	181	LYS	1	0.935	0.957	8.833	25.099	25.099	0.000	0.000	0.000	0.000
162	A	182	LEU	0	-0.003	0.021	12.042	0.000	0.000	0.000	0.000	0.000	0.000
163	A	183	ASN	0	0.015	0.000	14.941	0.449	0.449	0.000	0.000	0.000	0.000
164	A	184	TRP	0	0.017	-0.023	14.535	0.003	0.003	0.000	0.000	0.000	0.000
165	A	185	GLU	-1	-0.889	-0.927	19.804	-11.824	-11.824	0.000	0.000	0.000	0.000
166	A	186	ASN	0	-0.108	-0.057	20.132	0.321	0.321	0.000	0.000	0.000	0.000
167	A	187	ILE	0	-0.066	-0.014	15.878	-0.432	-0.432	0.000	0.000	0.000	0.000
168	A	188	ASN	0	0.003	0.006	19.210	0.606	0.606	0.000	0.000	0.000	0.000
169	A	189	GLU	-1	-0.718	-0.849	18.298	-17.125	-17.125	0.000	0.000	0.000	0.000
170	A	190	PHE	0	-0.007	0.024	21.106	0.137	0.137	0.000	0.000	0.000	0.000
171	A	191	CYS	0	-0.052	-0.031	24.022	-0.053	-0.053	0.000	0.000	0.000	0.000
172	A	192	GLY	0	0.043	0.027	26.810	0.337	0.337	0.000	0.000	0.000	0.000
173	A	193	GLU	-2	-1.703	-1.821	30.139	-18.097	-18.097	0.000	0.000	0.000	0.000

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