FMO DATABASE

FMODB ID: KVJQ3

Calculation Name: 3RYK-A-Xray547

Preferred Name:

Target Type:

Ligand Name: thymidine-5'-diphosphate | pyrophosphate 2-

Ligand 3-letter code: TYD | POP

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3RYK

Chain ID: A

ChEMBL ID:

UniProt ID: A0A1S0

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	175
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1880511.245023
FMO2-HF: Nuclear repulsion	1811422.075961
FMO2-HF: Total energy	-69089.169061
FMO2-MP2: Total energy	-69293.287273

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:ALA)

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

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.
21.341	23.541	3.14	-1.952	-3.387	-0.016

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.833 / q_NPA : 0.914

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	LYS	1	0.938	0.971	3.312	38.675	40.249	0.047	-0.873	-0.748	-0.003
18	A	17	ARG	1	0.867	0.922	2.809	44.879	45.813	0.112	-0.333	-0.713	-0.004
19	A	18	LEU	0	0.044	0.043	4.923	2.036	2.164	-0.001	-0.010	-0.117	0.000
32	A	31	ASN	0	-0.035	-0.033	4.742	2.995	3.067	-0.001	-0.004	-0.067	0.000
35	A	34	VAL	0	-0.036	-0.010	2.245	-2.838	-3.351	2.984	-0.725	-1.746	-0.009
36	A	35	LEU	0	0.025	0.020	4.755	0.458	0.463	-0.001	-0.007	0.004	0.000
4	A	3	VAL	0	0.042	0.023	6.047	2.860	2.860	0.000	0.000	0.000	0.000
5	A	4	ILE	0	-0.070	-0.020	9.551	-0.360	-0.360	0.000	0.000	0.000	0.000
6	A	5	GLU	-1	-0.788	-0.880	12.563	-15.557	-15.557	0.000	0.000	0.000	0.000
7	A	6	THR	0	-0.036	-0.033	14.126	-1.230	-1.230	0.000	0.000	0.000	0.000
8	A	7	ASN	0	-0.002	0.003	16.351	0.161	0.161	0.000	0.000	0.000	0.000
9	A	8	PHE	0	0.038	0.008	19.940	-0.341	-0.341	0.000	0.000	0.000	0.000
10	A	9	THR	0	0.002	0.021	20.351	0.228	0.228	0.000	0.000	0.000	0.000
11	A	10	ASP	-1	-0.842	-0.924	17.840	-15.398	-15.398	0.000	0.000	0.000	0.000
12	A	11	ALA	0	-0.016	0.003	16.776	-0.893	-0.893	0.000	0.000	0.000	0.000
13	A	12	LYS	1	0.897	0.954	11.928	20.737	20.737	0.000	0.000	0.000	0.000
14	A	13	LEU	0	0.016	0.034	14.247	-0.158	-0.158	0.000	0.000	0.000	0.000
15	A	14	LEU	0	-0.009	-0.018	9.024	-1.673	-1.673	0.000	0.000	0.000	0.000
16	A	15	GLU	-1	-0.858	-0.940	8.409	-26.397	-26.397	0.000	0.000	0.000	0.000
17	A	16	PRO	0	0.001	0.013	5.836	-8.209	-8.209	0.000	0.000	0.000	0.000
20	A	19	PHE	0	-0.058	-0.031	5.024	-4.341	-4.341	0.000	0.000	0.000	0.000
21	A	20	GLY	0	0.023	0.012	9.625	1.611	1.611	0.000	0.000	0.000	0.000
22	A	21	ASP	-1	-0.830	-0.904	13.099	-18.892	-18.892	0.000	0.000	0.000	0.000
23	A	22	ASP	-1	-0.904	-0.946	16.315	-14.651	-14.651	0.000	0.000	0.000	0.000
24	A	23	ARG	1	0.833	0.899	18.575	16.414	16.414	0.000	0.000	0.000	0.000
25	A	24	GLY	0	0.016	0.017	17.884	0.429	0.429	0.000	0.000	0.000	0.000
26	A	25	PHE	0	-0.037	-0.030	11.878	-0.859	-0.859	0.000	0.000	0.000	0.000
27	A	26	PHE	0	0.052	0.039	8.006	0.761	0.761	0.000	0.000	0.000	0.000
28	A	27	THR	0	-0.047	-0.069	6.907	-2.186	-2.186	0.000	0.000	0.000	0.000
29	A	28	GLU	-1	-0.876	-0.909	4.929	-42.774	-42.774	0.000	0.000	0.000	0.000
30	A	29	SER	0	-0.009	-0.006	6.500	-3.302	-3.302	0.000	0.000	0.000	0.000
31	A	30	TYR	0	0.055	0.018	8.546	1.180	1.180	0.000	0.000	0.000	0.000
33	A	32	LYS	1	0.944	0.979	6.502	16.669	16.669	0.000	0.000	0.000	0.000
34	A	33	LYS	1	1.030	1.016	6.299	34.371	34.371	0.000	0.000	0.000	0.000
37	A	36	GLU	-1	-0.896	-0.943	7.641	-20.116	-20.116	0.000	0.000	0.000	0.000
38	A	37	THR	0	-0.088	-0.057	5.854	-0.546	-0.546	0.000	0.000	0.000	0.000
39	A	38	LEU	0	-0.064	-0.025	5.159	0.243	0.243	0.000	0.000	0.000	0.000
40	A	39	GLY	0	0.021	0.008	8.524	1.776	1.776	0.000	0.000	0.000	0.000
41	A	40	VAL	0	-0.071	-0.032	10.416	1.582	1.582	0.000	0.000	0.000	0.000
42	A	41	THR	0	0.024	0.005	11.682	-0.965	-0.965	0.000	0.000	0.000	0.000
43	A	42	HIS	0	0.032	0.017	13.378	0.437	0.437	0.000	0.000	0.000	0.000
44	A	43	SER	0	-0.037	-0.025	14.146	-1.224	-1.224	0.000	0.000	0.000	0.000
45	A	44	PHE	0	0.002	-0.012	12.886	0.550	0.550	0.000	0.000	0.000	0.000
46	A	45	VAL	0	-0.007	0.006	17.422	-0.119	-0.119	0.000	0.000	0.000	0.000
47	A	46	GLN	0	0.019	0.000	20.503	0.698	0.698	0.000	0.000	0.000	0.000
48	A	47	ASP	-1	-0.845	-0.904	17.489	-17.581	-17.581	0.000	0.000	0.000	0.000
49	A	48	ASN	0	-0.013	0.009	20.357	1.152	1.152	0.000	0.000	0.000	0.000
50	A	49	VAL	0	0.004	-0.013	21.257	-0.737	-0.737	0.000	0.000	0.000	0.000
51	A	50	SER	0	-0.025	-0.006	23.465	0.705	0.705	0.000	0.000	0.000	0.000
52	A	51	TYR	0	0.028	-0.003	25.455	-0.277	-0.277	0.000	0.000	0.000	0.000
53	A	52	SER	0	-0.017	-0.019	27.663	0.437	0.437	0.000	0.000	0.000	0.000
54	A	53	ALA	0	0.036	0.032	29.660	-0.216	-0.216	0.000	0.000	0.000	0.000
55	A	54	GLU	-1	-0.874	-0.926	32.227	-8.648	-8.648	0.000	0.000	0.000	0.000
56	A	55	ALA	0	-0.015	0.007	31.085	-0.295	-0.295	0.000	0.000	0.000	0.000
57	A	56	GLY	0	0.053	0.010	31.489	0.333	0.333	0.000	0.000	0.000	0.000
58	A	57	THR	0	-0.043	-0.022	30.902	0.339	0.339	0.000	0.000	0.000	0.000
59	A	58	ILE	0	-0.023	-0.015	30.583	-0.413	-0.413	0.000	0.000	0.000	0.000
60	A	59	ARG	1	0.846	0.929	27.942	10.523	10.523	0.000	0.000	0.000	0.000
61	A	60	GLY	0	0.005	0.010	28.810	-0.442	-0.442	0.000	0.000	0.000	0.000
62	A	61	LEU	0	-0.011	-0.003	28.239	0.180	0.180	0.000	0.000	0.000	0.000
63	A	62	HIS	0	0.030	0.030	27.171	-0.080	-0.080	0.000	0.000	0.000	0.000
64	A	63	PHE	0	0.027	-0.014	27.662	-0.318	-0.318	0.000	0.000	0.000	0.000
65	A	64	GLN	0	-0.064	-0.022	27.655	0.442	0.442	0.000	0.000	0.000	0.000
66	A	65	LYS	1	0.875	0.927	28.939	8.672	8.672	0.000	0.000	0.000	0.000
67	A	66	ASN	0	0.039	0.006	28.514	-0.213	-0.213	0.000	0.000	0.000	0.000
68	A	67	PRO	0	-0.037	-0.024	31.332	0.282	0.282	0.000	0.000	0.000	0.000
69	A	68	LYS	1	0.931	0.983	28.678	8.998	8.998	0.000	0.000	0.000	0.000
70	A	69	ALA	0	0.033	0.032	26.572	-0.171	-0.171	0.000	0.000	0.000	0.000
71	A	70	GLN	0	-0.051	-0.036	22.845	-0.274	-0.274	0.000	0.000	0.000	0.000
72	A	71	THR	0	-0.059	-0.036	17.222	0.129	0.129	0.000	0.000	0.000	0.000
73	A	72	LYS	1	0.828	0.898	18.888	12.732	12.732	0.000	0.000	0.000	0.000
74	A	73	LEU	0	-0.013	-0.001	11.144	-0.612	-0.612	0.000	0.000	0.000	0.000
75	A	74	ILE	0	-0.006	0.003	15.699	0.232	0.232	0.000	0.000	0.000	0.000
76	A	75	GLN	0	0.038	0.004	13.188	-2.558	-2.558	0.000	0.000	0.000	0.000
77	A	76	VAL	0	-0.017	-0.003	16.374	1.140	1.140	0.000	0.000	0.000	0.000
78	A	77	MET	0	-0.037	-0.013	15.500	-1.131	-1.131	0.000	0.000	0.000	0.000
79	A	78	GLN	0	-0.008	-0.018	18.831	-0.114	-0.114	0.000	0.000	0.000	0.000
80	A	79	GLY	0	0.056	0.038	21.951	0.267	0.267	0.000	0.000	0.000	0.000
81	A	80	ALA	0	0.002	-0.019	21.765	-0.845	-0.845	0.000	0.000	0.000	0.000
82	A	81	ILE	0	-0.022	-0.003	21.111	0.732	0.732	0.000	0.000	0.000	0.000
83	A	82	TYR	0	0.033	0.017	22.967	-0.724	-0.724	0.000	0.000	0.000	0.000
84	A	83	ASP	-1	-0.812	-0.916	21.417	-13.889	-13.889	0.000	0.000	0.000	0.000
85	A	84	VAL	0	0.030	0.012	23.550	-0.212	-0.212	0.000	0.000	0.000	0.000
86	A	85	ILE	0	-0.026	-0.012	20.627	0.009	0.009	0.000	0.000	0.000	0.000
87	A	86	VAL	0	0.033	0.006	24.675	0.077	0.077	0.000	0.000	0.000	0.000
88	A	87	ASP	-1	-0.723	-0.807	26.003	-11.818	-11.818	0.000	0.000	0.000	0.000
89	A	88	LEU	0	0.004	-0.007	27.328	0.444	0.444	0.000	0.000	0.000	0.000
90	A	89	ARG	1	0.757	0.840	22.997	12.914	12.914	0.000	0.000	0.000	0.000
91	A	90	LYS	1	0.981	0.982	29.935	8.109	8.109	0.000	0.000	0.000	0.000
92	A	91	ASP	-1	-0.923	-0.960	31.218	-9.258	-9.258	0.000	0.000	0.000	0.000
93	A	92	SER	0	-0.072	-0.039	27.159	-0.112	-0.112	0.000	0.000	0.000	0.000
94	A	93	PRO	0	-0.004	-0.005	27.602	0.267	0.267	0.000	0.000	0.000	0.000
95	A	94	THR	0	-0.053	-0.040	25.780	-0.050	-0.050	0.000	0.000	0.000	0.000
96	A	95	PHE	0	0.017	0.012	28.622	0.008	0.008	0.000	0.000	0.000	0.000
97	A	96	LYS	1	0.888	0.956	30.883	8.825	8.825	0.000	0.000	0.000	0.000
98	A	97	GLN	0	-0.018	0.007	28.054	-0.330	-0.330	0.000	0.000	0.000	0.000
99	A	98	TRP	0	0.011	-0.004	26.861	-0.473	-0.473	0.000	0.000	0.000	0.000
100	A	99	ARG	1	0.796	0.873	20.388	14.946	14.946	0.000	0.000	0.000	0.000
101	A	100	GLY	0	0.043	0.029	24.324	-0.031	-0.031	0.000	0.000	0.000	0.000
102	A	101	TYR	0	-0.021	-0.023	19.129	-0.505	-0.505	0.000	0.000	0.000	0.000
103	A	102	ILE	0	0.013	0.007	20.778	0.381	0.381	0.000	0.000	0.000	0.000
104	A	103	LEU	0	-0.023	0.004	16.442	-1.069	-1.069	0.000	0.000	0.000	0.000
105	A	104	SER	0	0.010	-0.018	17.672	1.076	1.076	0.000	0.000	0.000	0.000
106	A	105	ALA	0	0.043	0.030	17.013	-1.142	-1.142	0.000	0.000	0.000	0.000
107	A	106	ASP	-1	-0.916	-0.958	16.514	-16.814	-16.814	0.000	0.000	0.000	0.000
108	A	107	ASN	0	-0.037	-0.032	14.921	-1.465	-1.465	0.000	0.000	0.000	0.000
109	A	108	HIS	1	0.877	0.944	11.559	20.137	20.137	0.000	0.000	0.000	0.000
110	A	109	ARG	1	0.900	0.971	12.090	20.948	20.948	0.000	0.000	0.000	0.000
111	A	110	GLN	0	-0.037	-0.046	10.696	0.768	0.768	0.000	0.000	0.000	0.000
112	A	111	LEU	0	-0.018	0.004	13.636	-0.619	-0.619	0.000	0.000	0.000	0.000
113	A	112	LEU	0	-0.032	-0.005	13.245	0.366	0.366	0.000	0.000	0.000	0.000
114	A	113	VAL	0	0.020	-0.002	15.302	0.415	0.415	0.000	0.000	0.000	0.000
115	A	114	PRO	0	0.020	0.010	19.010	0.026	0.026	0.000	0.000	0.000	0.000
116	A	115	LYS	1	0.900	0.946	20.407	13.417	13.417	0.000	0.000	0.000	0.000
117	A	116	GLY	0	-0.005	-0.010	23.572	0.022	0.022	0.000	0.000	0.000	0.000
118	A	117	PHE	0	-0.009	-0.005	23.121	0.110	0.110	0.000	0.000	0.000	0.000
119	A	118	ALA	0	-0.011	0.012	25.877	0.137	0.137	0.000	0.000	0.000	0.000
120	A	119	HIS	0	-0.058	-0.057	22.267	-0.070	-0.070	0.000	0.000	0.000	0.000
121	A	120	GLY	0	0.054	0.026	25.395	0.412	0.412	0.000	0.000	0.000	0.000
122	A	121	PHE	0	-0.033	-0.006	24.204	-0.309	-0.309	0.000	0.000	0.000	0.000
123	A	122	CYS	0	0.019	0.019	26.537	0.602	0.602	0.000	0.000	0.000	0.000
124	A	123	THR	0	-0.037	-0.025	27.008	-0.439	-0.439	0.000	0.000	0.000	0.000
125	A	124	LEU	0	-0.008	-0.002	24.792	0.395	0.395	0.000	0.000	0.000	0.000
126	A	125	VAL	0	-0.010	0.001	26.204	0.267	0.267	0.000	0.000	0.000	0.000
127	A	126	PRO	0	0.019	0.005	28.807	-0.155	-0.155	0.000	0.000	0.000	0.000
128	A	127	HIS	0	-0.009	0.016	28.750	-0.476	-0.476	0.000	0.000	0.000	0.000
129	A	128	THR	0	0.026	0.015	23.902	-0.574	-0.574	0.000	0.000	0.000	0.000
130	A	129	ILE	0	-0.047	-0.026	22.252	0.395	0.395	0.000	0.000	0.000	0.000
131	A	130	VAL	0	0.038	0.024	20.839	-0.791	-0.791	0.000	0.000	0.000	0.000
132	A	131	MET	0	-0.006	0.001	17.205	0.053	0.053	0.000	0.000	0.000	0.000
133	A	132	TYR	0	0.003	-0.010	17.776	-0.560	-0.560	0.000	0.000	0.000	0.000
134	A	133	LYS	1	0.860	0.937	13.210	19.480	19.480	0.000	0.000	0.000	0.000
135	A	134	VAL	0	0.003	-0.005	17.885	-0.107	-0.107	0.000	0.000	0.000	0.000
136	A	135	ASP	-1	-0.799	-0.895	18.520	-14.281	-14.281	0.000	0.000	0.000	0.000
137	A	136	GLU	-1	-0.853	-0.917	20.192	-10.831	-10.831	0.000	0.000	0.000	0.000
138	A	137	TYR	0	0.012	0.006	24.016	-0.144	-0.144	0.000	0.000	0.000	0.000
139	A	138	TYR	0	-0.103	-0.065	26.214	0.243	0.243	0.000	0.000	0.000	0.000
140	A	139	SER	0	-0.002	-0.010	28.366	0.331	0.331	0.000	0.000	0.000	0.000
141	A	140	ALA	0	0.016	-0.004	31.843	0.026	0.026	0.000	0.000	0.000	0.000
142	A	141	ASP	-1	-0.926	-0.952	34.543	-8.122	-8.122	0.000	0.000	0.000	0.000
143	A	142	HIS	0	0.011	0.009	32.205	-0.085	-0.085	0.000	0.000	0.000	0.000
144	A	143	ASP	-1	-0.815	-0.884	31.648	-10.000	-10.000	0.000	0.000	0.000	0.000
145	A	144	SER	0	-0.002	-0.010	32.045	0.414	0.414	0.000	0.000	0.000	0.000
146	A	145	GLY	0	0.031	0.000	31.809	-0.366	-0.366	0.000	0.000	0.000	0.000
147	A	146	VAL	0	-0.016	0.003	32.630	0.180	0.180	0.000	0.000	0.000	0.000
148	A	147	LEU	0	-0.020	0.003	33.639	-0.244	-0.244	0.000	0.000	0.000	0.000
149	A	148	TRP	0	0.048	0.014	33.463	-0.136	-0.136	0.000	0.000	0.000	0.000
150	A	149	ASN	0	-0.024	-0.007	34.489	-0.210	-0.210	0.000	0.000	0.000	0.000
151	A	150	ASP	-1	-0.738	-0.874	35.764	-8.271	-8.271	0.000	0.000	0.000	0.000
152	A	151	LYS	1	0.923	0.941	37.195	7.161	7.161	0.000	0.000	0.000	0.000
153	A	152	GLU	-1	-0.912	-0.949	37.344	-8.075	-8.075	0.000	0.000	0.000	0.000
154	A	153	LEU	0	-0.046	-0.020	31.830	-0.200	-0.200	0.000	0.000	0.000	0.000
155	A	154	ALA	0	-0.036	-0.017	34.044	-0.169	-0.169	0.000	0.000	0.000	0.000
156	A	155	ILE	0	-0.001	0.013	30.394	-0.134	-0.134	0.000	0.000	0.000	0.000
157	A	156	PRO	0	-0.025	-0.003	31.044	0.211	0.211	0.000	0.000	0.000	0.000
158	A	157	TRP	0	-0.024	-0.031	28.218	-0.491	-0.491	0.000	0.000	0.000	0.000
159	A	158	PRO	0	-0.031	-0.015	29.458	0.276	0.276	0.000	0.000	0.000	0.000
160	A	159	VAL	0	-0.009	-0.018	32.645	0.093	0.093	0.000	0.000	0.000	0.000
161	A	160	THR	0	0.003	0.011	35.608	-0.009	-0.009	0.000	0.000	0.000	0.000
162	A	161	SER	0	-0.040	-0.033	38.974	0.211	0.211	0.000	0.000	0.000	0.000
163	A	162	PRO	0	0.017	0.028	35.288	0.033	0.033	0.000	0.000	0.000	0.000
164	A	163	ILE	0	0.014	0.014	35.326	0.251	0.251	0.000	0.000	0.000	0.000
165	A	164	LEU	0	0.007	0.002	34.267	-0.292	-0.292	0.000	0.000	0.000	0.000
166	A	165	SER	0	-0.060	-0.064	35.583	0.314	0.314	0.000	0.000	0.000	0.000
167	A	166	ASP	-1	-0.834	-0.939	37.423	-7.572	-7.572	0.000	0.000	0.000	0.000
168	A	167	LYS	1	0.917	0.958	34.587	8.958	8.958	0.000	0.000	0.000	0.000
169	A	168	ASP	-1	-0.808	-0.887	32.895	-9.471	-9.471	0.000	0.000	0.000	0.000
170	A	169	ARG	1	0.849	0.928	36.130	7.999	7.999	0.000	0.000	0.000	0.000
171	A	170	ILE	0	-0.010	0.001	39.350	0.181	0.181	0.000	0.000	0.000	0.000
172	A	171	LEU	0	-0.058	0.004	33.616	0.030	0.030	0.000	0.000	0.000	0.000
173	A	172	PRO	0	-0.016	-0.001	36.701	0.153	0.153	0.000	0.000	0.000	0.000
174	A	173	LEU	0	-0.023	-0.022	37.556	-0.181	-0.181	0.000	0.000	0.000	0.000
175	A	174	LEU	-1	-0.959	-0.967	33.515	-8.545	-8.545	0.000	0.000	0.000	0.000

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