FMO DATABASE

FMODB ID: GV4V1

Calculation Name: 3EIY-A-Xray547

Preferred Name:

Target Type:

Ligand Name: pyrophosphate 2- | tetraethylene glycol | di(hydroxyethyl)ether | potassium ion

Ligand 3-letter code: POP | PG4 | PEG | K

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3EIY

Chain ID: A

ChEMBL ID:

UniProt ID: Q3JUV5

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	-1775510.364902
FMO2-HF: Nuclear repulsion	1709166.843649
FMO2-HF: Total energy	-66343.521252
FMO2-MP2: Total energy	-66538.191025

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:2:SER)

Summations of interaction energy for fragment #1(A:2:SER)

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.
-110.921	-104.11	1.104	-3.657	-4.257	-0.032

Interaction energy analysis for fragmet #1(A:2:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.870 / q_NPA : 0.920

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	4	SER	0	0.054	0.037	3.188	0.286	2.737	0.043	-1.146	-1.348	-0.006
4	A	5	ASN	0	-0.053	-0.020	3.400	-1.701	-0.526	0.007	-0.579	-0.603	-0.003
5	A	6	VAL	0	-0.006	0.015	4.610	4.259	4.428	-0.001	-0.023	-0.145	0.000
35	A	36	ALA	0	-0.034	-0.009	5.077	-6.403	-6.425	-0.001	-0.002	0.026	0.000
37	A	38	GLY	0	-0.098	-0.036	2.693	-7.893	-7.379	0.566	-0.524	-0.556	-0.003
38	A	39	LEU	0	-0.008	-0.013	2.759	-8.580	-6.056	0.490	-1.383	-1.631	-0.020
6	A	7	PRO	0	0.018	0.003	6.899	1.623	1.623	0.000	0.000	0.000	0.000
7	A	8	ALA	0	0.086	0.067	10.680	0.174	0.174	0.000	0.000	0.000	0.000
8	A	9	GLY	0	0.020	-0.014	13.223	0.949	0.949	0.000	0.000	0.000	0.000
9	A	10	LYS	1	0.802	0.919	14.013	19.570	19.570	0.000	0.000	0.000	0.000
10	A	11	ASP	-1	-0.879	-0.943	17.144	-13.075	-13.075	0.000	0.000	0.000	0.000
11	A	12	LEU	0	-0.025	0.017	16.400	0.012	0.012	0.000	0.000	0.000	0.000
12	A	13	PRO	0	0.026	0.011	20.693	0.423	0.423	0.000	0.000	0.000	0.000
13	A	14	GLN	0	0.017	0.003	21.371	-0.365	-0.365	0.000	0.000	0.000	0.000
14	A	15	ASP	-1	-0.836	-0.876	19.178	-16.060	-16.060	0.000	0.000	0.000	0.000
15	A	16	PHE	0	0.072	0.017	16.035	-0.678	-0.678	0.000	0.000	0.000	0.000
16	A	17	ASN	0	-0.111	-0.071	11.355	1.141	1.141	0.000	0.000	0.000	0.000
17	A	18	VAL	0	0.025	0.007	12.324	-0.161	-0.161	0.000	0.000	0.000	0.000
18	A	19	ILE	0	-0.023	-0.009	5.669	-1.452	-1.452	0.000	0.000	0.000	0.000
19	A	20	ILE	0	-0.025	-0.009	9.376	1.589	1.589	0.000	0.000	0.000	0.000
20	A	21	GLU	-1	-0.822	-0.922	10.270	-26.699	-26.699	0.000	0.000	0.000	0.000
21	A	22	ILE	0	-0.013	-0.003	11.997	0.377	0.377	0.000	0.000	0.000	0.000
22	A	23	PRO	0	-0.010	0.003	14.917	0.496	0.496	0.000	0.000	0.000	0.000
23	A	24	ALA	0	0.025	0.021	17.172	0.546	0.546	0.000	0.000	0.000	0.000
24	A	25	GLN	0	-0.017	-0.018	20.799	0.115	0.115	0.000	0.000	0.000	0.000
25	A	26	SER	0	-0.045	-0.013	18.974	0.319	0.319	0.000	0.000	0.000	0.000
26	A	27	GLU	-1	-0.861	-0.936	21.006	-11.752	-11.752	0.000	0.000	0.000	0.000
27	A	28	PRO	0	-0.017	0.013	21.090	-0.621	-0.621	0.000	0.000	0.000	0.000
28	A	29	VAL	0	-0.033	-0.019	17.705	0.320	0.320	0.000	0.000	0.000	0.000
29	A	30	LYS	1	0.828	0.901	15.828	17.693	17.693	0.000	0.000	0.000	0.000
30	A	31	TYR	0	-0.006	-0.012	12.624	-0.277	-0.277	0.000	0.000	0.000	0.000
31	A	32	GLU	-1	-0.780	-0.868	12.112	-18.737	-18.737	0.000	0.000	0.000	0.000
32	A	33	ALA	0	-0.055	-0.035	6.668	-1.480	-1.480	0.000	0.000	0.000	0.000
33	A	34	ASP	-1	-0.775	-0.884	7.599	-32.177	-32.177	0.000	0.000	0.000	0.000
34	A	35	LYS	1	0.885	0.926	5.582	23.440	23.440	0.000	0.000	0.000	0.000
36	A	37	LEU	0	-0.031	-0.017	6.196	-1.754	-1.754	0.000	0.000	0.000	0.000
39	A	40	LEU	0	-0.006	-0.010	5.547	1.178	1.178	0.000	0.000	0.000	0.000
40	A	41	VAL	0	0.002	0.002	8.625	0.688	0.688	0.000	0.000	0.000	0.000
41	A	42	VAL	0	-0.022	-0.013	11.719	0.361	0.361	0.000	0.000	0.000	0.000
42	A	43	ASP	-1	-0.820	-0.880	15.385	-15.784	-15.784	0.000	0.000	0.000	0.000
43	A	44	ARG	1	0.800	0.872	17.141	15.029	15.029	0.000	0.000	0.000	0.000
44	A	45	PHE	0	-0.008	-0.006	20.011	-0.393	-0.393	0.000	0.000	0.000	0.000
45	A	46	ILE	0	-0.019	-0.006	21.076	0.236	0.236	0.000	0.000	0.000	0.000
46	A	47	GLY	0	0.018	0.008	24.178	0.366	0.366	0.000	0.000	0.000	0.000
47	A	48	THR	0	-0.055	-0.046	27.716	0.328	0.328	0.000	0.000	0.000	0.000
48	A	49	GLY	0	-0.027	-0.009	27.098	0.284	0.284	0.000	0.000	0.000	0.000
49	A	50	MET	0	-0.054	-0.018	27.112	-0.004	-0.004	0.000	0.000	0.000	0.000
50	A	51	ARG	1	0.850	0.907	23.979	11.514	11.514	0.000	0.000	0.000	0.000
51	A	52	TYR	0	0.073	0.041	19.879	0.306	0.306	0.000	0.000	0.000	0.000
52	A	53	PRO	0	-0.019	-0.004	22.763	-0.082	-0.082	0.000	0.000	0.000	0.000
53	A	54	VAL	0	-0.020	-0.021	21.500	0.274	0.274	0.000	0.000	0.000	0.000
54	A	55	ASN	0	-0.016	-0.013	16.583	-0.444	-0.444	0.000	0.000	0.000	0.000
55	A	56	TYR	0	-0.009	-0.025	16.681	0.641	0.641	0.000	0.000	0.000	0.000
56	A	57	GLY	0	0.057	0.032	13.046	-1.099	-1.099	0.000	0.000	0.000	0.000
57	A	58	PHE	0	0.043	0.036	7.556	-0.240	-0.240	0.000	0.000	0.000	0.000
58	A	59	ILE	0	0.008	0.019	11.726	-1.693	-1.693	0.000	0.000	0.000	0.000
59	A	60	PRO	0	-0.046	-0.007	8.397	-0.331	-0.331	0.000	0.000	0.000	0.000
60	A	61	GLN	0	-0.044	-0.057	7.905	4.706	4.706	0.000	0.000	0.000	0.000
61	A	62	THR	0	-0.027	-0.022	11.587	2.317	2.317	0.000	0.000	0.000	0.000
62	A	63	LEU	0	-0.062	-0.021	14.167	-1.431	-1.431	0.000	0.000	0.000	0.000
63	A	64	SER	0	0.042	-0.005	16.857	1.195	1.195	0.000	0.000	0.000	0.000
64	A	65	GLY	0	-0.047	-0.032	20.002	-0.110	-0.110	0.000	0.000	0.000	0.000
65	A	66	ASP	-1	-0.855	-0.927	19.661	-15.547	-15.547	0.000	0.000	0.000	0.000
66	A	67	GLY	0	-0.047	-0.017	18.524	0.176	0.176	0.000	0.000	0.000	0.000
67	A	68	ASP	-1	-0.899	-0.934	15.340	-20.877	-20.877	0.000	0.000	0.000	0.000
68	A	69	PRO	0	-0.110	-0.077	11.495	0.139	0.139	0.000	0.000	0.000	0.000
69	A	70	VAL	0	0.028	0.015	14.706	0.735	0.735	0.000	0.000	0.000	0.000
70	A	71	ASP	-1	-0.735	-0.835	15.913	-18.636	-18.636	0.000	0.000	0.000	0.000
71	A	72	VAL	0	-0.083	-0.056	16.252	1.057	1.057	0.000	0.000	0.000	0.000
72	A	73	LEU	0	-0.005	0.005	17.289	-0.499	-0.499	0.000	0.000	0.000	0.000
73	A	74	VAL	0	-0.021	-0.017	16.175	0.389	0.389	0.000	0.000	0.000	0.000
74	A	75	ILE	0	0.017	0.010	19.407	0.120	0.120	0.000	0.000	0.000	0.000
75	A	76	THR	0	-0.002	-0.043	19.135	-0.244	-0.244	0.000	0.000	0.000	0.000
76	A	77	PRO	0	-0.037	-0.013	22.399	0.219	0.219	0.000	0.000	0.000	0.000
77	A	78	PHE	0	0.018	0.005	21.757	0.412	0.412	0.000	0.000	0.000	0.000
78	A	79	PRO	0	0.003	0.023	19.445	-0.429	-0.429	0.000	0.000	0.000	0.000
79	A	80	LEU	0	-0.008	0.004	14.587	-0.129	-0.129	0.000	0.000	0.000	0.000
80	A	81	LEU	0	0.009	0.003	11.715	0.070	0.070	0.000	0.000	0.000	0.000
81	A	82	ALA	0	0.055	0.039	11.656	-1.193	-1.193	0.000	0.000	0.000	0.000
82	A	83	GLY	0	0.008	0.005	7.430	-0.598	-0.598	0.000	0.000	0.000	0.000
83	A	84	SER	0	-0.111	-0.061	6.346	-3.573	-3.573	0.000	0.000	0.000	0.000
84	A	85	VAL	0	0.007	-0.007	6.847	-0.566	-0.566	0.000	0.000	0.000	0.000
85	A	86	VAL	0	-0.011	-0.001	9.428	1.630	1.630	0.000	0.000	0.000	0.000
86	A	87	ARG	1	0.781	0.853	13.205	15.489	15.489	0.000	0.000	0.000	0.000
87	A	88	ALA	0	-0.031	-0.025	15.499	0.905	0.905	0.000	0.000	0.000	0.000
88	A	89	ARG	1	0.826	0.916	18.095	11.963	11.963	0.000	0.000	0.000	0.000
89	A	90	ALA	0	0.037	0.009	21.408	-0.046	-0.046	0.000	0.000	0.000	0.000
90	A	91	LEU	0	-0.088	-0.031	23.289	0.418	0.418	0.000	0.000	0.000	0.000
91	A	92	GLY	0	0.007	-0.007	25.368	0.597	0.597	0.000	0.000	0.000	0.000
92	A	93	MET	0	-0.038	-0.002	24.885	-0.570	-0.570	0.000	0.000	0.000	0.000
93	A	94	LEU	0	-0.018	-0.009	25.714	0.630	0.630	0.000	0.000	0.000	0.000
94	A	95	LYS	1	0.881	0.937	26.423	9.544	9.544	0.000	0.000	0.000	0.000
95	A	96	MET	0	-0.027	-0.020	24.689	0.562	0.562	0.000	0.000	0.000	0.000
96	A	97	THR	0	-0.016	-0.016	28.759	-0.045	-0.045	0.000	0.000	0.000	0.000
97	A	98	ASP	-1	-0.788	-0.907	24.773	-12.430	-12.430	0.000	0.000	0.000	0.000
98	A	99	GLU	-1	-0.843	-0.907	25.520	-11.840	-11.840	0.000	0.000	0.000	0.000
99	A	100	SER	0	-0.025	-0.010	24.456	0.091	0.091	0.000	0.000	0.000	0.000
100	A	101	GLY	0	-0.017	0.002	26.396	-0.063	-0.063	0.000	0.000	0.000	0.000
101	A	102	VAL	0	-0.053	-0.037	26.704	0.172	0.172	0.000	0.000	0.000	0.000
102	A	103	ASP	-1	-0.775	-0.867	22.964	-14.199	-14.199	0.000	0.000	0.000	0.000
103	A	104	ALA	0	-0.007	-0.013	23.603	0.578	0.578	0.000	0.000	0.000	0.000
104	A	105	LYS	1	0.813	0.891	20.107	14.148	14.148	0.000	0.000	0.000	0.000
105	A	106	LEU	0	-0.005	-0.012	19.963	0.786	0.786	0.000	0.000	0.000	0.000
106	A	107	VAL	0	-0.018	-0.007	21.664	-0.201	-0.201	0.000	0.000	0.000	0.000
107	A	108	ALA	0	0.029	0.010	19.689	0.232	0.232	0.000	0.000	0.000	0.000
108	A	109	VAL	0	0.007	0.011	21.366	0.197	0.197	0.000	0.000	0.000	0.000
109	A	110	PRO	0	0.028	0.001	18.586	-0.511	-0.511	0.000	0.000	0.000	0.000
110	A	111	HIS	0	0.039	0.025	19.211	0.755	0.755	0.000	0.000	0.000	0.000
111	A	112	ASP	-1	-0.744	-0.868	21.145	-11.616	-11.616	0.000	0.000	0.000	0.000
112	A	113	LYS	1	0.880	0.923	23.258	11.780	11.780	0.000	0.000	0.000	0.000
113	A	114	VAL	0	-0.046	-0.012	17.410	-0.122	-0.122	0.000	0.000	0.000	0.000
114	A	115	CYS	0	-0.013	-0.001	20.739	0.127	0.127	0.000	0.000	0.000	0.000
115	A	116	PRO	0	0.068	0.041	22.969	0.292	0.292	0.000	0.000	0.000	0.000
116	A	117	MET	0	-0.032	-0.018	25.858	0.174	0.174	0.000	0.000	0.000	0.000
117	A	118	THR	0	-0.006	-0.016	23.876	0.075	0.075	0.000	0.000	0.000	0.000
118	A	119	ALA	0	0.022	0.024	26.580	0.060	0.060	0.000	0.000	0.000	0.000
119	A	120	ASN	0	-0.043	-0.024	28.118	0.193	0.193	0.000	0.000	0.000	0.000
120	A	121	LEU	0	-0.013	0.019	26.855	0.254	0.254	0.000	0.000	0.000	0.000
121	A	122	LYS	1	0.881	0.931	28.326	9.516	9.516	0.000	0.000	0.000	0.000
122	A	123	SER	0	0.007	-0.008	29.152	-0.244	-0.244	0.000	0.000	0.000	0.000
123	A	124	ILE	0	0.034	0.011	27.846	-0.043	-0.043	0.000	0.000	0.000	0.000
124	A	125	ASP	-1	-0.898	-0.948	30.070	-9.021	-9.021	0.000	0.000	0.000	0.000
125	A	126	ASP	-1	-0.847	-0.914	31.429	-9.314	-9.314	0.000	0.000	0.000	0.000
126	A	127	VAL	0	-0.033	-0.004	28.082	-0.038	-0.038	0.000	0.000	0.000	0.000
127	A	128	PRO	0	0.002	-0.008	30.490	0.274	0.274	0.000	0.000	0.000	0.000
128	A	129	ALA	0	0.036	0.016	32.505	-0.210	-0.210	0.000	0.000	0.000	0.000
129	A	130	TYR	0	0.070	0.024	31.160	-0.198	-0.198	0.000	0.000	0.000	0.000
130	A	131	LEU	0	-0.009	0.008	26.810	-0.119	-0.119	0.000	0.000	0.000	0.000
131	A	132	LYS	1	0.870	0.939	29.337	9.140	9.140	0.000	0.000	0.000	0.000
132	A	133	ASP	-1	-0.890	-0.949	30.799	-9.009	-9.009	0.000	0.000	0.000	0.000
133	A	134	GLN	0	-0.047	-0.031	29.411	-0.301	-0.301	0.000	0.000	0.000	0.000
134	A	135	ILE	0	-0.017	-0.005	25.390	-0.224	-0.224	0.000	0.000	0.000	0.000
135	A	136	LYS	1	0.857	0.916	27.751	8.909	8.909	0.000	0.000	0.000	0.000
136	A	137	HIS	0	0.006	-0.002	30.397	-0.231	-0.231	0.000	0.000	0.000	0.000
137	A	138	PHE	0	-0.002	-0.008	23.054	0.050	0.050	0.000	0.000	0.000	0.000
138	A	139	PHE	0	0.020	-0.002	21.879	-0.166	-0.166	0.000	0.000	0.000	0.000
139	A	140	GLU	-1	-0.839	-0.908	27.417	-9.212	-9.212	0.000	0.000	0.000	0.000
140	A	141	GLN	0	-0.059	-0.024	29.950	0.397	0.397	0.000	0.000	0.000	0.000
141	A	142	TYR	0	0.030	0.009	22.133	-0.154	-0.154	0.000	0.000	0.000	0.000
142	A	143	LYS	1	0.850	0.922	24.158	12.347	12.347	0.000	0.000	0.000	0.000
143	A	144	ALA	0	0.000	0.005	27.913	0.137	0.137	0.000	0.000	0.000	0.000
144	A	145	LEU	0	-0.039	-0.018	30.434	0.341	0.341	0.000	0.000	0.000	0.000
145	A	146	GLU	-1	-0.806	-0.888	25.120	-12.507	-12.507	0.000	0.000	0.000	0.000
146	A	147	LYS	1	0.939	0.950	29.399	9.285	9.285	0.000	0.000	0.000	0.000
147	A	148	GLY	0	0.000	-0.002	29.851	-0.252	-0.252	0.000	0.000	0.000	0.000
148	A	149	LYS	1	0.862	0.947	23.262	12.762	12.762	0.000	0.000	0.000	0.000
149	A	150	TRP	0	-0.053	-0.018	29.005	0.396	0.396	0.000	0.000	0.000	0.000
150	A	151	VAL	0	0.041	0.008	27.178	-0.387	-0.387	0.000	0.000	0.000	0.000
151	A	152	LYS	1	0.788	0.892	30.159	9.620	9.620	0.000	0.000	0.000	0.000
152	A	153	VAL	0	0.017	0.007	30.147	-0.247	-0.247	0.000	0.000	0.000	0.000
153	A	154	GLU	-1	-0.837	-0.880	31.593	-9.173	-9.173	0.000	0.000	0.000	0.000
154	A	155	GLY	0	-0.018	-0.015	32.101	0.351	0.351	0.000	0.000	0.000	0.000
155	A	156	TRP	0	-0.017	-0.011	27.639	-0.425	-0.425	0.000	0.000	0.000	0.000
156	A	157	ASP	-1	-0.825	-0.904	29.694	-9.741	-9.741	0.000	0.000	0.000	0.000
157	A	158	GLY	0	0.049	0.024	29.575	-0.248	-0.248	0.000	0.000	0.000	0.000
158	A	159	ILE	0	0.003	-0.012	26.758	-0.316	-0.316	0.000	0.000	0.000	0.000
159	A	160	ASP	-1	-0.902	-0.945	27.174	-10.633	-10.633	0.000	0.000	0.000	0.000
160	A	161	ALA	0	-0.002	0.007	28.369	-0.255	-0.255	0.000	0.000	0.000	0.000
161	A	162	ALA	0	0.034	0.014	23.748	-0.385	-0.385	0.000	0.000	0.000	0.000
162	A	163	HIS	0	0.015	-0.012	23.454	-0.918	-0.918	0.000	0.000	0.000	0.000
163	A	164	LYS	1	0.818	0.903	24.328	11.362	11.362	0.000	0.000	0.000	0.000
164	A	165	GLU	-1	-0.831	-0.886	21.512	-14.586	-14.586	0.000	0.000	0.000	0.000
165	A	166	ILE	0	-0.023	-0.008	18.793	-0.679	-0.679	0.000	0.000	0.000	0.000
166	A	167	THR	0	-0.059	-0.045	20.060	-0.682	-0.682	0.000	0.000	0.000	0.000
167	A	168	ASP	-1	-0.816	-0.894	21.983	-12.669	-12.669	0.000	0.000	0.000	0.000
168	A	169	GLY	0	0.061	0.038	19.173	-0.300	-0.300	0.000	0.000	0.000	0.000
169	A	170	VAL	0	-0.032	-0.033	16.580	-1.159	-1.159	0.000	0.000	0.000	0.000
170	A	171	ALA	0	-0.075	-0.034	17.975	-0.430	-0.430	0.000	0.000	0.000	0.000
171	A	172	ASN	0	0.017	0.002	19.571	0.230	0.230	0.000	0.000	0.000	0.000
172	A	173	PHE	0	-0.012	0.011	10.177	-1.071	-1.071	0.000	0.000	0.000	0.000
173	A	174	LYS	1	0.837	0.922	15.533	16.253	16.253	0.000	0.000	0.000	0.000
174	A	175	LYS	0	0.004	0.022	17.442	0.942	0.942	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:SER)