FMO DATABASE

FMODB ID: 5YQKZ

Calculation Name: 4YGU-D-Xray547

Preferred Name:

Target Type:

Ligand Name: triethylene glycol | di(hydroxyethyl)ether | 1,2-ethanediol

Ligand 3-letter code: PGE | PEG | EDO

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4YGU

Chain ID: D

ChEMBL ID:

UniProt ID:

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	-1763460.207658
FMO2-HF: Nuclear repulsion	1696010.379323
FMO2-HF: Total energy	-67449.828336
FMO2-MP2: Total energy	-67647.47528

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:28:LYS)

Summations of interaction energy for fragment #1(A:28: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.
-169.132	-168.913	43.896	-22.963	-21.147	-0.275

Interaction energy analysis for fragmet #1(A:28:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 2 / q_Mulliken : 1.556 / q_NPA : 1.760

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	30	SER	0	0.024	-0.003	3.504	-0.778	1.175	-0.003	-0.796	-1.153	-0.003
35	A	62	GLU	-1	-0.832	-0.919	1.819	-191.423	-194.409	23.886	-10.948	-9.951	-0.133
36	A	63	GLY	0	0.052	0.023	2.977	3.278	4.481	0.249	-0.496	-0.955	-0.002
37	A	64	ARG	1	0.917	0.964	2.409	70.140	73.449	2.837	-2.594	-3.552	-0.030
38	A	65	GLU	-1	-0.737	-0.856	1.698	-151.126	-154.598	16.929	-8.114	-5.343	-0.107
73	A	100	THR	0	-0.020	0.003	4.655	3.144	3.232	-0.001	-0.002	-0.084	0.000
75	A	102	TRP	0	-0.009	-0.007	3.930	-0.368	-0.244	-0.001	-0.013	-0.109	0.000
4	A	31	GLU	-1	-0.853	-0.905	5.517	-46.512	-46.512	0.000	0.000	0.000	0.000
5	A	32	VAL	0	0.006	-0.006	8.899	-0.719	-0.719	0.000	0.000	0.000	0.000
6	A	33	ARG	1	0.739	0.842	11.400	46.507	46.507	0.000	0.000	0.000	0.000
7	A	34	LYS	1	0.864	0.934	15.167	27.598	27.598	0.000	0.000	0.000	0.000
8	A	35	VAL	0	0.013	0.011	18.352	0.254	0.254	0.000	0.000	0.000	0.000
9	A	36	ASP	-1	-0.872	-0.931	20.311	-24.196	-24.196	0.000	0.000	0.000	0.000
10	A	37	ALA	0	0.008	-0.003	22.958	-0.813	-0.813	0.000	0.000	0.000	0.000
11	A	38	PHE	0	-0.007	-0.006	18.980	0.440	0.440	0.000	0.000	0.000	0.000
12	A	39	SER	0	0.016	0.012	24.649	0.290	0.290	0.000	0.000	0.000	0.000
13	A	40	SER	0	0.004	0.005	24.422	0.840	0.840	0.000	0.000	0.000	0.000
14	A	41	ILE	0	-0.020	-0.010	18.048	-0.767	-0.767	0.000	0.000	0.000	0.000
15	A	42	GLU	-1	-0.837	-0.893	21.317	-23.785	-23.785	0.000	0.000	0.000	0.000
16	A	43	ILE	0	-0.025	-0.020	15.889	-1.379	-1.379	0.000	0.000	0.000	0.000
17	A	44	THR	0	0.014	0.002	18.727	1.077	1.077	0.000	0.000	0.000	0.000
18	A	45	SER	0	-0.015	-0.028	13.700	-1.835	-1.835	0.000	0.000	0.000	0.000
19	A	46	VAL	0	-0.035	-0.007	11.644	1.958	1.958	0.000	0.000	0.000	0.000
20	A	47	GLY	0	-0.006	-0.011	9.969	-3.823	-3.823	0.000	0.000	0.000	0.000
21	A	48	THR	0	0.003	0.017	8.371	3.493	3.493	0.000	0.000	0.000	0.000
22	A	49	ILE	0	-0.030	-0.020	9.309	-4.844	-4.844	0.000	0.000	0.000	0.000
23	A	50	HIS	0	0.010	0.015	7.915	4.948	4.948	0.000	0.000	0.000	0.000
24	A	51	PHE	0	0.041	0.011	12.415	-0.873	-0.873	0.000	0.000	0.000	0.000
25	A	52	THR	0	-0.066	-0.050	15.395	-0.340	-0.340	0.000	0.000	0.000	0.000
26	A	53	GLN	0	0.020	0.006	17.269	-0.429	-0.429	0.000	0.000	0.000	0.000
27	A	54	SER	0	-0.011	-0.024	19.992	0.203	0.203	0.000	0.000	0.000	0.000
28	A	55	ASP	-1	-0.879	-0.933	21.835	-22.444	-22.444	0.000	0.000	0.000	0.000
29	A	56	THR	0	-0.093	-0.035	19.677	0.195	0.195	0.000	0.000	0.000	0.000
30	A	57	TYR	0	0.002	0.012	20.080	-0.813	-0.813	0.000	0.000	0.000	0.000
31	A	58	SER	0	-0.084	-0.052	15.667	-1.378	-1.378	0.000	0.000	0.000	0.000
32	A	59	PHE	0	0.070	0.027	11.947	-0.267	-0.267	0.000	0.000	0.000	0.000
33	A	60	ARG	1	0.935	0.978	5.313	71.013	71.013	0.000	0.000	0.000	0.000
34	A	61	ILE	0	0.017	0.018	7.554	0.073	0.073	0.000	0.000	0.000	0.000
39	A	66	LYS	1	0.871	0.945	5.402	55.454	55.454	0.000	0.000	0.000	0.000
40	A	67	TYR	0	0.012	-0.003	7.051	6.597	6.597	0.000	0.000	0.000	0.000
41	A	68	VAL	0	0.049	0.045	5.443	4.229	4.229	0.000	0.000	0.000	0.000
42	A	69	LYS	1	0.856	0.902	7.475	67.336	67.336	0.000	0.000	0.000	0.000
43	A	70	ASN	0	-0.009	-0.008	10.744	4.691	4.691	0.000	0.000	0.000	0.000
44	A	71	THR	0	0.028	0.017	11.208	2.561	2.561	0.000	0.000	0.000	0.000
45	A	72	GLU	-1	-0.976	-0.986	13.490	-29.789	-29.789	0.000	0.000	0.000	0.000
46	A	73	THR	0	-0.011	0.000	14.594	-1.439	-1.439	0.000	0.000	0.000	0.000
47	A	74	THR	0	-0.023	-0.007	17.672	0.700	0.700	0.000	0.000	0.000	0.000
48	A	75	VAL	0	0.024	0.014	21.290	-0.414	-0.414	0.000	0.000	0.000	0.000
49	A	76	LYS	1	0.935	0.969	23.851	23.649	23.649	0.000	0.000	0.000	0.000
50	A	77	ASP	-1	-0.879	-0.935	27.357	-19.907	-19.907	0.000	0.000	0.000	0.000
51	A	78	GLY	0	0.027	0.026	27.294	0.260	0.260	0.000	0.000	0.000	0.000
52	A	79	ARG	1	0.812	0.897	24.280	22.004	22.004	0.000	0.000	0.000	0.000
53	A	80	LEU	0	-0.030	-0.012	17.237	-0.339	-0.339	0.000	0.000	0.000	0.000
54	A	81	LEU	0	0.001	0.006	21.137	0.012	0.012	0.000	0.000	0.000	0.000
55	A	82	ILE	0	0.008	-0.014	14.524	-1.548	-1.548	0.000	0.000	0.000	0.000
56	A	83	GLY	0	0.035	0.020	17.310	1.146	1.146	0.000	0.000	0.000	0.000
57	A	84	PHE	0	-0.054	-0.026	13.666	-2.634	-2.634	0.000	0.000	0.000	0.000
58	A	85	LYS	1	0.900	0.960	14.229	39.950	39.950	0.000	0.000	0.000	0.000
59	A	86	ASP	-1	-0.869	-0.931	17.216	-30.898	-30.898	0.000	0.000	0.000	0.000
60	A	87	LYS	1	0.972	0.992	18.680	22.768	22.768	0.000	0.000	0.000	0.000
61	A	88	LYS	1	0.897	0.948	15.145	36.119	36.119	0.000	0.000	0.000	0.000
62	A	89	ASN	0	0.034	0.003	18.471	-1.446	-1.446	0.000	0.000	0.000	0.000
63	A	90	LYS	1	1.009	1.001	19.908	24.985	24.985	0.000	0.000	0.000	0.000
64	A	91	SER	0	0.077	0.033	15.641	-1.549	-1.549	0.000	0.000	0.000	0.000
65	A	92	ARG	1	0.852	0.927	14.764	25.690	25.690	0.000	0.000	0.000	0.000
66	A	93	ARG	0	-0.016	0.003	14.258	0.208	0.208	0.000	0.000	0.000	0.000
67	A	94	ASN	0	-0.026	-0.014	11.627	0.368	0.368	0.000	0.000	0.000	0.000
68	A	95	GLN	0	0.027	-0.002	14.614	0.771	0.771	0.000	0.000	0.000	0.000
69	A	96	LYS	1	0.933	0.966	13.821	32.846	32.846	0.000	0.000	0.000	0.000
70	A	97	ASP	-1	-0.822	-0.906	8.290	-59.919	-59.919	0.000	0.000	0.000	0.000
71	A	98	GLY	0	-0.020	-0.023	8.284	3.720	3.720	0.000	0.000	0.000	0.000
72	A	99	VAL	0	-0.072	-0.025	6.004	-9.128	-9.128	0.000	0.000	0.000	0.000
74	A	101	ILE	0	0.004	-0.010	6.541	-3.409	-3.409	0.000	0.000	0.000	0.000
76	A	103	ILE	0	-0.002	-0.001	10.997	0.225	0.225	0.000	0.000	0.000	0.000
77	A	104	SER	0	-0.002	0.005	14.792	-0.142	-0.142	0.000	0.000	0.000	0.000
78	A	105	ALA	0	0.031	0.007	17.718	0.159	0.159	0.000	0.000	0.000	0.000
79	A	106	PRO	0	0.047	0.034	21.498	-0.196	-0.196	0.000	0.000	0.000	0.000
80	A	107	ASP	-1	-0.815	-0.903	24.668	-20.433	-20.433	0.000	0.000	0.000	0.000
81	A	108	LEU	0	-0.072	-0.042	21.063	-1.047	-1.047	0.000	0.000	0.000	0.000
82	A	109	LYS	1	0.925	0.955	24.905	20.658	20.658	0.000	0.000	0.000	0.000
83	A	110	GLU	-1	-0.917	-0.957	26.132	-20.237	-20.237	0.000	0.000	0.000	0.000
84	A	111	VAL	0	-0.028	-0.002	20.341	-1.071	-1.071	0.000	0.000	0.000	0.000
85	A	112	GLU	-1	-0.796	-0.881	22.644	-22.031	-22.031	0.000	0.000	0.000	0.000
86	A	113	PHE	0	-0.037	-0.015	15.701	-1.094	-1.094	0.000	0.000	0.000	0.000
87	A	114	THR	0	0.004	-0.002	20.754	1.308	1.308	0.000	0.000	0.000	0.000
88	A	115	GLY	0	0.009	-0.012	17.890	-0.879	-0.879	0.000	0.000	0.000	0.000
89	A	116	VAL	0	-0.099	-0.046	15.278	1.485	1.485	0.000	0.000	0.000	0.000
90	A	117	GLY	0	0.040	0.027	13.563	-2.638	-2.638	0.000	0.000	0.000	0.000
91	A	118	GLU	-1	-0.834	-0.904	13.031	-37.579	-37.579	0.000	0.000	0.000	0.000
92	A	119	PHE	0	-0.015	-0.019	13.868	-2.341	-2.341	0.000	0.000	0.000	0.000
93	A	120	ASN	0	0.020	-0.003	12.375	3.527	3.527	0.000	0.000	0.000	0.000
94	A	121	CYS	0	-0.047	-0.025	15.413	-1.042	-1.042	0.000	0.000	0.000	0.000
95	A	122	GLU	-1	-0.855	-0.943	14.824	-30.316	-30.316	0.000	0.000	0.000	0.000
96	A	123	LYS	1	0.836	0.923	14.232	35.289	35.289	0.000	0.000	0.000	0.000
97	A	124	PRO	0	0.021	0.016	19.481	-0.063	-0.063	0.000	0.000	0.000	0.000
98	A	125	LEU	0	-0.048	0.000	21.554	-0.601	-0.601	0.000	0.000	0.000	0.000
99	A	126	LYS	1	0.968	0.978	24.014	19.364	19.364	0.000	0.000	0.000	0.000
100	A	127	LEU	0	-0.031	-0.010	24.478	-0.246	-0.246	0.000	0.000	0.000	0.000
101	A	128	ASP	-1	-0.843	-0.904	28.724	-16.868	-16.868	0.000	0.000	0.000	0.000
102	A	129	GLU	-1	-0.868	-0.939	31.859	-16.906	-16.906	0.000	0.000	0.000	0.000
103	A	130	VAL	0	-0.025	-0.011	25.273	-0.540	-0.540	0.000	0.000	0.000	0.000
104	A	131	SER	0	-0.035	-0.027	27.464	0.531	0.531	0.000	0.000	0.000	0.000
105	A	132	PHE	0	0.046	0.015	21.594	-0.944	-0.944	0.000	0.000	0.000	0.000
106	A	133	GLU	-1	-0.808	-0.889	25.352	-20.228	-20.228	0.000	0.000	0.000	0.000
107	A	134	VAL	0	-0.013	0.004	21.765	-1.071	-1.071	0.000	0.000	0.000	0.000
108	A	135	LYS	1	0.819	0.898	23.400	23.189	23.189	0.000	0.000	0.000	0.000
109	A	136	GLY	0	-0.023	-0.019	22.464	-1.153	-1.153	0.000	0.000	0.000	0.000
110	A	137	VAL	0	-0.061	-0.047	19.726	1.005	1.005	0.000	0.000	0.000	0.000
111	A	138	GLY	0	0.026	0.034	18.554	-1.468	-1.468	0.000	0.000	0.000	0.000
112	A	139	GLU	-1	-0.870	-0.926	17.546	-29.170	-29.170	0.000	0.000	0.000	0.000
113	A	140	VAL	0	-0.033	-0.029	18.081	-1.458	-1.458	0.000	0.000	0.000	0.000
114	A	141	ASN	0	0.003	-0.001	16.498	2.669	2.669	0.000	0.000	0.000	0.000
115	A	142	VAL	0	-0.024	-0.027	18.850	-1.091	-1.091	0.000	0.000	0.000	0.000
116	A	143	ALA	0	0.045	0.028	19.997	1.096	1.096	0.000	0.000	0.000	0.000
117	A	144	ASP	-1	-0.909	-0.961	21.896	-21.154	-21.154	0.000	0.000	0.000	0.000
118	A	145	LEU	0	-0.003	0.007	24.046	-0.604	-0.604	0.000	0.000	0.000	0.000
119	A	146	THR	0	-0.018	-0.010	26.249	0.970	0.970	0.000	0.000	0.000	0.000
120	A	147	CYS	0	-0.089	-0.041	29.229	-0.435	-0.435	0.000	0.000	0.000	0.000
121	A	148	ASN	0	0.020	0.008	31.231	0.519	0.519	0.000	0.000	0.000	0.000
122	A	149	VAL	0	-0.024	-0.021	33.158	0.390	0.390	0.000	0.000	0.000	0.000
123	A	150	LEU	0	0.045	0.030	27.538	-0.680	-0.680	0.000	0.000	0.000	0.000
124	A	151	LYS	1	0.866	0.934	30.073	18.097	18.097	0.000	0.000	0.000	0.000
125	A	152	VAL	0	0.032	0.014	27.051	-0.788	-0.788	0.000	0.000	0.000	0.000
126	A	153	ALA	0	-0.023	-0.019	28.320	0.819	0.819	0.000	0.000	0.000	0.000
127	A	154	LEU	0	-0.004	0.020	25.658	-0.735	-0.735	0.000	0.000	0.000	0.000
128	A	155	ARG	1	0.848	0.882	27.374	20.196	20.196	0.000	0.000	0.000	0.000
129	A	156	GLY	0	-0.019	-0.007	26.694	-0.867	-0.867	0.000	0.000	0.000	0.000
130	A	157	VAL	0	-0.052	-0.041	24.058	0.731	0.731	0.000	0.000	0.000	0.000
131	A	158	GLY	0	-0.012	0.021	23.231	-0.689	-0.689	0.000	0.000	0.000	0.000
132	A	159	SER	0	0.000	-0.018	22.598	1.364	1.364	0.000	0.000	0.000	0.000
133	A	160	ALA	0	-0.016	-0.022	22.496	-0.910	-0.910	0.000	0.000	0.000	0.000
134	A	161	ASP	-1	-0.889	-0.935	22.107	-22.583	-22.583	0.000	0.000	0.000	0.000
135	A	162	ILE	0	0.003	-0.002	22.740	-0.841	-0.841	0.000	0.000	0.000	0.000
136	A	163	HIS	0	-0.036	-0.014	24.898	1.332	1.332	0.000	0.000	0.000	0.000
137	A	164	VAL	0	0.000	-0.018	26.442	-0.476	-0.476	0.000	0.000	0.000	0.000
138	A	165	VAL	0	0.001	0.011	29.171	0.673	0.673	0.000	0.000	0.000	0.000
139	A	166	CYS	0	-0.044	-0.013	32.034	-0.251	-0.251	0.000	0.000	0.000	0.000
140	A	167	ASP	-1	-0.865	-0.922	34.238	-15.219	-15.219	0.000	0.000	0.000	0.000
141	A	168	TYR	0	-0.193	-0.127	36.132	0.270	0.270	0.000	0.000	0.000	0.000
142	A	169	LEU	0	0.070	0.038	31.658	-0.538	-0.538	0.000	0.000	0.000	0.000
143	A	170	SER	0	-0.028	-0.002	33.641	0.404	0.404	0.000	0.000	0.000	0.000
144	A	171	ALA	0	0.047	0.009	32.182	-0.696	-0.696	0.000	0.000	0.000	0.000
145	A	172	GLN	0	0.006	0.020	32.374	0.244	0.244	0.000	0.000	0.000	0.000
146	A	173	MET	0	0.021	0.026	29.424	-0.751	-0.751	0.000	0.000	0.000	0.000
147	A	174	GLY	0	0.023	0.001	31.805	0.693	0.693	0.000	0.000	0.000	0.000
148	A	175	GLY	0	-0.020	-0.013	30.427	0.065	0.065	0.000	0.000	0.000	0.000
149	A	176	VAL	0	-0.038	-0.027	28.727	0.597	0.597	0.000	0.000	0.000	0.000
150	A	177	GLY	0	0.056	0.038	26.344	-0.552	-0.552	0.000	0.000	0.000	0.000
151	A	178	SER	0	-0.038	-0.037	26.092	0.912	0.912	0.000	0.000	0.000	0.000
152	A	179	VAL	0	0.030	0.019	26.270	-0.808	-0.808	0.000	0.000	0.000	0.000
153	A	180	THR	0	-0.009	0.005	26.370	1.047	1.047	0.000	0.000	0.000	0.000
154	A	181	LEU	0	0.002	0.001	27.319	-0.488	-0.488	0.000	0.000	0.000	0.000
155	A	182	SER	0	-0.011	-0.004	28.073	0.456	0.456	0.000	0.000	0.000	0.000
156	A	183	GLY	0	0.076	0.051	30.211	-0.375	-0.375	0.000	0.000	0.000	0.000
157	A	184	SER	0	-0.113	-0.084	32.134	0.777	0.777	0.000	0.000	0.000	0.000
158	A	185	ALA	0	0.026	0.009	34.273	-0.395	-0.395	0.000	0.000	0.000	0.000
159	A	186	GLY	0	0.004	-0.002	36.303	0.348	0.348	0.000	0.000	0.000	0.000
160	A	187	ARG	1	0.961	0.981	38.959	14.974	14.974	0.000	0.000	0.000	0.000
161	A	188	ALA	0	0.021	0.001	36.661	-0.465	-0.465	0.000	0.000	0.000	0.000
162	A	189	ASP	-1	-0.846	-0.878	37.853	-14.693	-14.693	0.000	0.000	0.000	0.000
163	A	190	ILE	0	-0.020	-0.013	34.774	-0.498	-0.498	0.000	0.000	0.000	0.000
164	A	191	SER	0	-0.037	-0.023	36.126	0.430	0.430	0.000	0.000	0.000	0.000
165	A	192	LYS	1	0.884	0.936	34.533	16.524	16.524	0.000	0.000	0.000	0.000
166	A	193	GLY	0	-0.013	0.002	36.313	0.483	0.483	0.000	0.000	0.000	0.000
167	A	194	GLY	0	-0.041	-0.003	34.073	0.177	0.177	0.000	0.000	0.000	0.000
168	A	195	ILE	0	-0.008	-0.017	32.912	0.341	0.341	0.000	0.000	0.000	0.000
169	A	196	GLY	0	-0.009	-0.001	31.204	-0.302	-0.302	0.000	0.000	0.000	0.000
170	A	197	GLY	0	-0.015	-0.018	30.673	0.661	0.661	0.000	0.000	0.000	0.000
171	A	198	VAL	0	0.003	-0.017	30.975	-0.394	-0.394	0.000	0.000	0.000	0.000
172	A	199	ASN	0	-0.029	0.004	30.402	0.677	0.677	0.000	0.000	0.000	0.000
173	A	200	THR	0	0.073	0.020	31.612	-0.453	-0.453	0.000	0.000	0.000	0.000
174	A	201	ASP	-1	-0.895	-0.928	34.130	-16.653	-16.653	0.000	0.000	0.000	0.000
175	A	202	ASN	0	-0.070	-0.043	31.743	0.609	0.609	0.000	0.000	0.000	0.000
176	A	203	LEU	0	-0.008	0.009	32.588	-0.339	-0.339	0.000	0.000	0.000	0.000
177	A	204	LYS	1	0.868	0.938	34.550	15.857	15.857	0.000	0.000	0.000	0.000
178	A	205	ILE	0	-0.002	-0.017	37.213	-0.399	-0.399	0.000	0.000	0.000	0.000
179	A	206	GLY	-1	-0.922	-0.937	39.719	-13.574	-13.574	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:28:LYS)