FMO DATABASE

FMODB ID: QMZQY

Calculation Name: 5LS0-B-Xray547

Preferred Name:

Target Type:

Ligand Name: di(hydroxyethyl)ether

Ligand 3-letter code: PEG

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 5LS0

Chain ID: B

ChEMBL ID:

UniProt ID: Q93V56

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	179
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2017308.72159
FMO2-HF: Nuclear repulsion	1945295.841736
FMO2-HF: Total energy	-72012.879854
FMO2-MP2: Total energy	-72222.499208

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:30:SER)

Summations of interaction energy for fragment #1(A:30: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.
-94.204	-92.834	-0.019	-0.565	-0.785	-0.001

Interaction energy analysis for fragmet #1(A:30:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.847 / q_NPA : 0.903

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	32	ALA	0	0.005	0.009	3.851	1.339	2.709	-0.019	-0.565	-0.785	-0.001
4	A	33	ALA	0	0.011	0.001	6.702	1.241	1.241	0.000	0.000	0.000	0.000
5	A	34	HIS	0	0.053	0.024	8.991	1.596	1.596	0.000	0.000	0.000	0.000
6	A	35	PRO	0	0.001	-0.008	12.596	0.189	0.189	0.000	0.000	0.000	0.000
7	A	36	TRP	0	0.025	0.006	14.646	0.324	0.324	0.000	0.000	0.000	0.000
8	A	37	HIS	1	0.863	0.939	14.092	18.849	18.849	0.000	0.000	0.000	0.000
9	A	38	ASP	-1	-0.838	-0.905	9.552	-28.044	-28.044	0.000	0.000	0.000	0.000
10	A	39	LEU	0	-0.041	-0.010	11.254	-1.555	-1.555	0.000	0.000	0.000	0.000
11	A	40	GLU	-1	-0.907	-0.966	12.870	-18.145	-18.145	0.000	0.000	0.000	0.000
12	A	41	ILE	0	0.061	0.031	15.228	0.156	0.156	0.000	0.000	0.000	0.000
13	A	42	GLY	0	0.067	0.045	17.961	0.617	0.617	0.000	0.000	0.000	0.000
14	A	43	PRO	0	-0.037	-0.042	18.486	0.614	0.614	0.000	0.000	0.000	0.000
15	A	44	GLY	0	-0.022	-0.001	21.269	0.545	0.545	0.000	0.000	0.000	0.000
16	A	45	ALA	0	-0.012	0.022	23.005	0.585	0.585	0.000	0.000	0.000	0.000
17	A	46	PRO	0	0.041	0.015	24.880	-0.019	-0.019	0.000	0.000	0.000	0.000
18	A	47	GLN	0	0.009	-0.006	27.372	-0.125	-0.125	0.000	0.000	0.000	0.000
19	A	48	ILE	0	-0.067	-0.054	24.063	0.215	0.215	0.000	0.000	0.000	0.000
20	A	49	PHE	0	-0.012	0.000	22.144	-0.340	-0.340	0.000	0.000	0.000	0.000
21	A	50	ASN	0	-0.056	-0.043	16.628	0.705	0.705	0.000	0.000	0.000	0.000
22	A	51	VAL	0	0.009	-0.009	19.969	0.307	0.307	0.000	0.000	0.000	0.000
23	A	52	VAL	0	-0.009	0.000	16.992	-0.485	-0.485	0.000	0.000	0.000	0.000
24	A	53	VAL	0	-0.024	-0.007	19.689	0.769	0.769	0.000	0.000	0.000	0.000
25	A	54	GLU	-1	-0.830	-0.929	21.369	-13.308	-13.308	0.000	0.000	0.000	0.000
26	A	55	ILE	0	-0.075	-0.043	23.590	0.076	0.076	0.000	0.000	0.000	0.000
27	A	56	THR	0	-0.032	-0.023	25.768	0.036	0.036	0.000	0.000	0.000	0.000
28	A	57	LYS	1	0.941	0.972	27.743	9.613	9.613	0.000	0.000	0.000	0.000
29	A	58	GLY	0	0.015	-0.001	31.030	-0.001	-0.001	0.000	0.000	0.000	0.000
30	A	59	SER	0	-0.042	-0.008	30.001	0.223	0.223	0.000	0.000	0.000	0.000
31	A	60	LYS	1	0.966	0.979	32.151	8.298	8.298	0.000	0.000	0.000	0.000
32	A	61	VAL	0	-0.038	-0.014	28.856	0.201	0.201	0.000	0.000	0.000	0.000
33	A	62	LYS	1	0.872	0.930	28.324	10.761	10.761	0.000	0.000	0.000	0.000
34	A	63	TYR	0	0.007	-0.024	24.842	0.038	0.038	0.000	0.000	0.000	0.000
35	A	64	GLU	-1	-0.805	-0.893	25.104	-10.905	-10.905	0.000	0.000	0.000	0.000
36	A	65	LEU	0	0.023	0.014	18.507	-0.560	-0.560	0.000	0.000	0.000	0.000
37	A	66	ASP	-1	-0.838	-0.892	20.777	-14.246	-14.246	0.000	0.000	0.000	0.000
38	A	67	LYS	1	0.856	0.909	19.885	11.520	11.520	0.000	0.000	0.000	0.000
39	A	68	LYS	1	0.910	0.966	19.656	13.294	13.294	0.000	0.000	0.000	0.000
40	A	69	THR	0	-0.080	-0.087	17.150	-0.985	-0.985	0.000	0.000	0.000	0.000
41	A	70	GLY	0	-0.015	0.003	15.499	-1.530	-1.530	0.000	0.000	0.000	0.000
42	A	71	LEU	0	-0.031	-0.017	15.257	-0.471	-0.471	0.000	0.000	0.000	0.000
43	A	72	ILE	0	0.011	0.011	17.767	0.567	0.567	0.000	0.000	0.000	0.000
44	A	73	LYS	1	0.874	0.941	20.829	11.566	11.566	0.000	0.000	0.000	0.000
45	A	74	VAL	0	0.004	-0.012	23.995	0.135	0.135	0.000	0.000	0.000	0.000
46	A	75	ASP	-1	-0.872	-0.910	27.380	-10.336	-10.336	0.000	0.000	0.000	0.000
47	A	76	ARG	1	0.817	0.882	29.702	9.731	9.731	0.000	0.000	0.000	0.000
48	A	77	ILE	0	-0.034	-0.012	32.295	-0.184	-0.184	0.000	0.000	0.000	0.000
49	A	78	LEU	0	0.016	0.006	34.587	0.164	0.164	0.000	0.000	0.000	0.000
50	A	79	TYR	0	0.038	0.010	36.937	0.073	0.073	0.000	0.000	0.000	0.000
51	A	80	SER	0	0.029	0.030	40.388	0.284	0.284	0.000	0.000	0.000	0.000
52	A	81	SER	0	-0.084	-0.041	40.441	-0.224	-0.224	0.000	0.000	0.000	0.000
53	A	82	VAL	0	0.012	0.004	38.317	0.131	0.131	0.000	0.000	0.000	0.000
54	A	83	VAL	0	-0.027	-0.018	35.427	-0.127	-0.127	0.000	0.000	0.000	0.000
55	A	84	TYR	0	0.076	0.039	31.798	0.181	0.181	0.000	0.000	0.000	0.000
56	A	85	PRO	0	0.011	0.018	33.968	-0.126	-0.126	0.000	0.000	0.000	0.000
57	A	86	HIS	0	-0.009	-0.017	31.464	0.354	0.354	0.000	0.000	0.000	0.000
58	A	87	ASN	0	0.026	0.002	26.302	0.015	0.015	0.000	0.000	0.000	0.000
59	A	88	TYR	0	0.018	-0.007	27.403	0.323	0.323	0.000	0.000	0.000	0.000
60	A	89	GLY	0	0.027	0.017	24.044	-0.400	-0.400	0.000	0.000	0.000	0.000
61	A	90	PHE	0	0.052	0.046	18.597	0.200	0.200	0.000	0.000	0.000	0.000
62	A	91	VAL	0	0.016	0.020	21.716	-0.642	-0.642	0.000	0.000	0.000	0.000
63	A	92	PRO	0	-0.045	-0.005	16.823	0.086	0.086	0.000	0.000	0.000	0.000
64	A	93	ARG	1	0.804	0.881	12.106	22.111	22.111	0.000	0.000	0.000	0.000
65	A	94	THR	0	0.023	0.010	19.430	0.643	0.643	0.000	0.000	0.000	0.000
66	A	95	LEU	0	-0.075	-0.036	22.994	-0.601	-0.601	0.000	0.000	0.000	0.000
67	A	96	CYS	0	0.018	0.025	25.637	0.333	0.333	0.000	0.000	0.000	0.000
68	A	97	GLU	-1	-0.796	-0.908	29.375	-9.731	-9.731	0.000	0.000	0.000	0.000
69	A	98	ASP	-1	-0.825	-0.897	29.867	-10.557	-10.557	0.000	0.000	0.000	0.000
70	A	99	ASN	0	-0.141	-0.075	27.582	-0.142	-0.142	0.000	0.000	0.000	0.000
71	A	100	ASP	-1	-0.802	-0.886	25.570	-12.636	-12.636	0.000	0.000	0.000	0.000
72	A	101	PRO	0	-0.059	-0.037	21.874	0.090	0.090	0.000	0.000	0.000	0.000
73	A	102	ILE	0	0.042	0.009	24.459	0.309	0.309	0.000	0.000	0.000	0.000
74	A	103	ASP	-1	-0.754	-0.862	25.939	-11.410	-11.410	0.000	0.000	0.000	0.000
75	A	104	VAL	0	-0.054	-0.040	25.754	0.329	0.329	0.000	0.000	0.000	0.000
76	A	105	LEU	0	-0.026	-0.004	27.956	-0.138	-0.138	0.000	0.000	0.000	0.000
77	A	106	VAL	0	-0.006	-0.015	25.517	0.153	0.153	0.000	0.000	0.000	0.000
78	A	107	ILE	0	-0.050	-0.029	28.975	0.108	0.108	0.000	0.000	0.000	0.000
79	A	108	MET	0	-0.045	-0.018	25.481	-0.358	-0.358	0.000	0.000	0.000	0.000
80	A	109	GLN	0	-0.064	-0.046	30.893	0.310	0.310	0.000	0.000	0.000	0.000
81	A	110	GLU	-1	-0.913	-0.949	28.161	-10.077	-10.077	0.000	0.000	0.000	0.000
82	A	111	PRO	0	-0.030	-0.007	28.303	-0.149	-0.149	0.000	0.000	0.000	0.000
83	A	112	VAL	0	0.014	-0.004	22.161	-0.311	-0.311	0.000	0.000	0.000	0.000
84	A	113	LEU	0	0.007	0.012	21.249	0.309	0.309	0.000	0.000	0.000	0.000
85	A	114	PRO	0	0.037	0.014	21.465	-0.435	-0.435	0.000	0.000	0.000	0.000
86	A	115	GLY	0	-0.030	-0.009	17.840	-0.472	-0.472	0.000	0.000	0.000	0.000
87	A	116	CYS	0	-0.079	-0.019	16.356	-1.284	-1.284	0.000	0.000	0.000	0.000
88	A	117	PHE	0	-0.008	-0.007	13.060	0.265	0.265	0.000	0.000	0.000	0.000
89	A	118	LEU	0	-0.014	0.004	18.075	-0.021	-0.021	0.000	0.000	0.000	0.000
90	A	119	ARG	1	0.871	0.895	19.770	13.651	13.651	0.000	0.000	0.000	0.000
91	A	120	ALA	0	-0.008	-0.007	22.013	0.501	0.501	0.000	0.000	0.000	0.000
92	A	121	ARG	1	0.858	0.926	25.504	9.876	9.876	0.000	0.000	0.000	0.000
93	A	122	ALA	0	0.019	0.019	28.524	0.160	0.160	0.000	0.000	0.000	0.000
94	A	123	ILE	0	-0.031	-0.016	30.655	0.160	0.160	0.000	0.000	0.000	0.000
95	A	124	GLY	0	0.029	0.007	34.106	0.358	0.358	0.000	0.000	0.000	0.000
96	A	125	LEU	0	-0.026	-0.002	34.082	-0.324	-0.324	0.000	0.000	0.000	0.000
97	A	126	MET	0	-0.015	-0.002	35.832	0.379	0.379	0.000	0.000	0.000	0.000
98	A	127	PRO	0	0.030	0.026	36.997	-0.191	-0.191	0.000	0.000	0.000	0.000
99	A	128	MET	0	-0.057	-0.027	37.204	0.192	0.192	0.000	0.000	0.000	0.000
100	A	129	ILE	0	0.025	0.033	38.800	-0.126	-0.126	0.000	0.000	0.000	0.000
101	A	130	ASP	-1	-0.802	-0.878	37.448	-8.433	-8.433	0.000	0.000	0.000	0.000
102	A	131	GLN	0	0.012	-0.012	39.691	0.045	0.045	0.000	0.000	0.000	0.000
103	A	132	GLY	0	-0.025	-0.011	41.930	0.071	0.071	0.000	0.000	0.000	0.000
104	A	133	GLU	-1	-0.921	-0.952	37.430	-8.305	-8.305	0.000	0.000	0.000	0.000
105	A	134	LYS	1	0.809	0.897	33.923	9.391	9.391	0.000	0.000	0.000	0.000
106	A	135	ASP	-1	-0.812	-0.921	34.086	-9.578	-9.578	0.000	0.000	0.000	0.000
107	A	136	ASP	-1	-0.876	-0.945	34.433	-8.798	-8.798	0.000	0.000	0.000	0.000
108	A	137	LYS	1	0.759	0.875	31.845	9.431	9.431	0.000	0.000	0.000	0.000
109	A	138	ILE	0	-0.009	0.002	29.207	0.318	0.318	0.000	0.000	0.000	0.000
110	A	139	ILE	0	-0.030	-0.016	31.362	-0.100	-0.100	0.000	0.000	0.000	0.000
111	A	140	ALA	0	0.042	0.008	28.621	0.018	0.018	0.000	0.000	0.000	0.000
112	A	141	VAL	0	-0.001	0.016	30.145	0.171	0.171	0.000	0.000	0.000	0.000
113	A	142	CYS	0	-0.018	0.009	24.515	-0.370	-0.370	0.000	0.000	0.000	0.000
114	A	143	VAL	0	-0.039	-0.033	24.632	0.381	0.381	0.000	0.000	0.000	0.000
115	A	144	ASP	-1	-0.803	-0.889	22.592	-13.431	-13.431	0.000	0.000	0.000	0.000
116	A	145	ASP	-1	-0.753	-0.859	25.676	-10.088	-10.088	0.000	0.000	0.000	0.000
117	A	146	PRO	0	-0.072	-0.052	28.569	0.201	0.201	0.000	0.000	0.000	0.000
118	A	147	GLU	-1	-0.951	-0.966	31.336	-8.378	-8.378	0.000	0.000	0.000	0.000
119	A	148	TYR	0	-0.007	-0.020	31.357	0.185	0.185	0.000	0.000	0.000	0.000
120	A	149	LYS	1	0.946	0.991	29.290	10.499	10.499	0.000	0.000	0.000	0.000
121	A	150	HIS	0	-0.015	-0.015	30.903	-0.151	-0.151	0.000	0.000	0.000	0.000
122	A	151	TYR	0	-0.035	0.016	34.258	0.198	0.198	0.000	0.000	0.000	0.000
123	A	152	THR	0	-0.083	-0.056	33.757	-0.325	-0.325	0.000	0.000	0.000	0.000
124	A	153	ASP	-1	-0.744	-0.889	35.775	-8.021	-8.021	0.000	0.000	0.000	0.000
125	A	154	ILE	0	0.037	0.019	36.853	0.087	0.087	0.000	0.000	0.000	0.000
126	A	155	LYS	1	0.817	0.898	38.954	7.757	7.757	0.000	0.000	0.000	0.000
127	A	156	GLU	-1	-0.829	-0.900	38.351	-8.082	-8.082	0.000	0.000	0.000	0.000
128	A	157	LEU	0	-0.021	0.002	36.634	-0.014	-0.014	0.000	0.000	0.000	0.000
129	A	158	PRO	0	0.003	-0.008	40.712	0.200	0.200	0.000	0.000	0.000	0.000
130	A	159	PRO	0	0.045	0.015	42.806	-0.100	-0.100	0.000	0.000	0.000	0.000
131	A	160	HIS	0	-0.029	-0.009	43.173	0.077	0.077	0.000	0.000	0.000	0.000
132	A	161	ARG	1	0.817	0.883	37.362	8.133	8.133	0.000	0.000	0.000	0.000
133	A	162	LEU	0	0.054	0.032	39.076	-0.134	-0.134	0.000	0.000	0.000	0.000
134	A	163	SER	0	-0.020	-0.004	41.334	-0.014	-0.014	0.000	0.000	0.000	0.000
135	A	164	GLU	-1	-0.841	-0.909	39.370	-7.967	-7.967	0.000	0.000	0.000	0.000
136	A	165	ILE	0	-0.002	-0.001	36.318	-0.092	-0.092	0.000	0.000	0.000	0.000
137	A	166	ARG	1	0.839	0.890	39.105	7.008	7.008	0.000	0.000	0.000	0.000
138	A	167	ARG	1	0.855	0.939	41.727	6.906	6.906	0.000	0.000	0.000	0.000
139	A	168	PHE	0	-0.008	-0.010	35.124	0.034	0.034	0.000	0.000	0.000	0.000
140	A	169	PHE	0	0.020	-0.006	33.281	-0.068	-0.068	0.000	0.000	0.000	0.000
141	A	170	GLU	-1	-0.805	-0.882	39.210	-7.002	-7.002	0.000	0.000	0.000	0.000
142	A	171	ASP	-1	-0.862	-0.938	42.262	-6.958	-6.958	0.000	0.000	0.000	0.000
143	A	172	TYR	0	-0.081	-0.046	34.471	-0.045	-0.045	0.000	0.000	0.000	0.000
144	A	173	LYS	1	0.827	0.896	35.958	8.678	8.678	0.000	0.000	0.000	0.000
145	A	174	LYS	1	0.889	0.953	40.363	6.999	6.999	0.000	0.000	0.000	0.000
146	A	175	ASN	0	-0.061	-0.044	43.392	0.228	0.228	0.000	0.000	0.000	0.000
147	A	176	GLU	-1	-0.807	-0.885	37.593	-8.646	-8.646	0.000	0.000	0.000	0.000
148	A	177	ASN	0	-0.086	-0.052	42.296	0.097	0.097	0.000	0.000	0.000	0.000
149	A	178	LYS	1	0.820	0.914	38.495	8.193	8.193	0.000	0.000	0.000	0.000
150	A	179	GLU	-1	-0.937	-0.960	43.266	-6.767	-6.767	0.000	0.000	0.000	0.000
151	A	180	VAL	0	-0.014	-0.012	39.364	-0.169	-0.169	0.000	0.000	0.000	0.000
152	A	181	ALA	0	-0.020	0.000	42.348	0.163	0.163	0.000	0.000	0.000	0.000
153	A	182	VAL	0	0.011	0.007	40.338	-0.145	-0.145	0.000	0.000	0.000	0.000
154	A	183	ASN	0	-0.054	-0.024	42.175	0.169	0.169	0.000	0.000	0.000	0.000
155	A	184	ASP	-1	-0.876	-0.932	42.701	-6.954	-6.954	0.000	0.000	0.000	0.000
156	A	185	PHE	0	-0.023	-0.025	38.315	-0.072	-0.072	0.000	0.000	0.000	0.000
157	A	186	LEU	0	-0.013	-0.001	39.441	0.200	0.200	0.000	0.000	0.000	0.000
158	A	187	PRO	0	0.028	-0.001	38.912	-0.177	-0.177	0.000	0.000	0.000	0.000
159	A	188	SER	0	-0.030	-0.002	35.224	-0.201	-0.201	0.000	0.000	0.000	0.000
160	A	189	GLU	-1	-0.878	-0.939	34.844	-8.464	-8.464	0.000	0.000	0.000	0.000
161	A	190	SER	0	0.054	0.017	35.619	-0.126	-0.126	0.000	0.000	0.000	0.000
162	A	191	ALA	0	-0.024	0.003	32.924	-0.151	-0.151	0.000	0.000	0.000	0.000
163	A	192	VAL	0	-0.004	-0.012	30.748	-0.346	-0.346	0.000	0.000	0.000	0.000
164	A	193	GLU	-1	-0.930	-0.969	31.288	-8.758	-8.758	0.000	0.000	0.000	0.000
165	A	194	ALA	0	-0.001	0.003	32.410	-0.167	-0.167	0.000	0.000	0.000	0.000
166	A	195	ILE	0	-0.040	-0.007	26.268	-0.326	-0.326	0.000	0.000	0.000	0.000
167	A	196	GLN	0	-0.021	-0.028	27.149	-0.442	-0.442	0.000	0.000	0.000	0.000
168	A	197	TYR	0	0.007	0.011	28.283	-0.272	-0.272	0.000	0.000	0.000	0.000
169	A	198	SER	0	0.011	-0.003	27.069	-0.280	-0.280	0.000	0.000	0.000	0.000
170	A	199	MET	0	-0.030	-0.009	23.593	-0.517	-0.517	0.000	0.000	0.000	0.000
171	A	200	ASP	-1	-0.870	-0.924	24.545	-11.422	-11.422	0.000	0.000	0.000	0.000
172	A	201	LEU	0	0.034	0.020	26.655	-0.177	-0.177	0.000	0.000	0.000	0.000
173	A	202	TYR	0	0.019	0.021	16.989	-0.648	-0.648	0.000	0.000	0.000	0.000
174	A	203	ALA	0	-0.017	-0.014	22.308	-0.530	-0.530	0.000	0.000	0.000	0.000
175	A	204	GLU	-1	-0.886	-0.939	23.362	-10.651	-10.651	0.000	0.000	0.000	0.000
176	A	205	TYR	0	-0.051	-0.028	25.501	-0.040	-0.040	0.000	0.000	0.000	0.000
177	A	206	ILE	0	-0.107	-0.053	19.054	-0.270	-0.270	0.000	0.000	0.000	0.000
178	A	207	LEU	0	-0.109	-0.042	17.230	-0.937	-0.937	0.000	0.000	0.000	0.000
179	A	208	HIS	0	-0.052	-0.009	20.320	-0.370	-0.370	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:30:SER)