FMO DATABASE

FMODB ID: LVYY9

Calculation Name: 3TEO-A-Xray547

Preferred Name:

Target Type:

Ligand Name: 3,6,9,12,15,18,21,24,27,30,33,36,39-tridecaoxahentetracontane-1,41-diol

Ligand 3-letter code: PE3

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3TEO

Chain ID: A

ChEMBL ID:

UniProt ID: G0WXL9

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	202
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2171647.770036
FMO2-HF: Nuclear repulsion	2090539.970826
FMO2-HF: Total energy	-81107.79921
FMO2-MP2: Total energy	-81346.565389

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:VAL)

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

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.
-105.048	-104.85	14.899	-8.519	-6.579	-0.1

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.799 / q_NPA : 0.883

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	GLU	-1	-0.797	-0.884	1.691	-112.415	-113.190	14.731	-8.329	-5.627	-0.099
4	A	5	TYR	0	-0.022	-0.005	4.021	8.382	8.790	0.000	-0.061	-0.347	0.000
5	A	6	ILE	0	0.014	0.004	2.731	6.072	6.637	0.168	-0.129	-0.605	-0.001
6	A	7	ASP	-1	-0.878	-0.949	6.218	-33.879	-33.879	0.000	0.000	0.000	0.000
7	A	8	SER	0	-0.066	-0.029	8.504	4.558	4.558	0.000	0.000	0.000	0.000
8	A	9	GLU	-1	-0.874	-0.953	9.395	-21.549	-21.549	0.000	0.000	0.000	0.000
9	A	10	LEU	0	-0.018	-0.014	9.145	2.529	2.529	0.000	0.000	0.000	0.000
10	A	11	LYS	1	0.984	0.998	12.062	24.376	24.376	0.000	0.000	0.000	0.000
11	A	12	ARG	1	0.940	0.986	13.622	22.341	22.341	0.000	0.000	0.000	0.000
12	A	13	LEU	0	0.000	0.004	14.583	1.434	1.434	0.000	0.000	0.000	0.000
13	A	14	GLU	-1	-0.850	-0.919	16.178	-15.804	-15.804	0.000	0.000	0.000	0.000
14	A	15	ASP	-1	-0.900	-0.958	18.153	-15.534	-15.534	0.000	0.000	0.000	0.000
15	A	16	TYR	0	-0.132	-0.090	19.370	0.806	0.806	0.000	0.000	0.000	0.000
16	A	17	ALA	0	-0.005	-0.012	20.387	0.769	0.769	0.000	0.000	0.000	0.000
17	A	18	LEU	0	0.007	0.005	21.831	0.726	0.726	0.000	0.000	0.000	0.000
18	A	19	ARG	1	0.846	0.937	23.481	13.096	13.096	0.000	0.000	0.000	0.000
19	A	20	ARG	1	0.861	0.926	25.645	11.015	11.015	0.000	0.000	0.000	0.000
20	A	21	VAL	0	-0.021	0.002	26.560	0.389	0.389	0.000	0.000	0.000	0.000
21	A	22	LYS	1	0.777	0.869	19.951	15.653	15.653	0.000	0.000	0.000	0.000
22	A	23	GLY	0	0.004	0.023	26.672	-0.014	-0.014	0.000	0.000	0.000	0.000
23	A	24	ILE	0	-0.029	-0.005	23.178	0.092	0.092	0.000	0.000	0.000	0.000
24	A	25	PRO	0	-0.002	0.010	27.529	0.211	0.211	0.000	0.000	0.000	0.000
25	A	26	ASN	0	0.007	0.000	28.203	-0.473	-0.473	0.000	0.000	0.000	0.000
26	A	27	ASN	0	0.054	0.008	25.443	-0.131	-0.131	0.000	0.000	0.000	0.000
27	A	28	ARG	1	0.904	0.960	28.380	9.716	9.716	0.000	0.000	0.000	0.000
28	A	29	ARG	1	0.879	0.953	30.392	10.375	10.375	0.000	0.000	0.000	0.000
29	A	30	LEU	0	0.050	0.038	33.770	0.322	0.322	0.000	0.000	0.000	0.000
30	A	31	TRP	0	0.014	-0.004	35.744	-0.093	-0.093	0.000	0.000	0.000	0.000
31	A	32	VAL	0	0.017	0.001	38.021	0.136	0.136	0.000	0.000	0.000	0.000
32	A	33	LEU	0	-0.011	0.018	40.484	-0.053	-0.053	0.000	0.000	0.000	0.000
33	A	34	THR	0	-0.018	-0.037	41.419	0.073	0.073	0.000	0.000	0.000	0.000
34	A	35	CYS	-1	-0.748	-0.763	44.450	-6.580	-6.580	0.000	0.000	0.000	0.000
35	A	36	MET	0	-0.021	-0.016	43.543	-0.202	-0.202	0.000	0.000	0.000	0.000
36	A	37	ASP	-1	-0.782	-0.847	44.099	-6.605	-6.605	0.000	0.000	0.000	0.000
37	A	38	GLU	-1	-0.826	-0.919	42.803	-6.867	-6.867	0.000	0.000	0.000	0.000
38	A	39	ARG	1	0.742	0.822	42.600	6.123	6.123	0.000	0.000	0.000	0.000
39	A	40	VAL	0	-0.020	-0.004	42.521	-0.046	-0.046	0.000	0.000	0.000	0.000
40	A	41	HIS	1	0.848	0.937	38.764	7.378	7.378	0.000	0.000	0.000	0.000
41	A	42	ILE	0	0.081	0.028	37.436	-0.081	-0.081	0.000	0.000	0.000	0.000
42	A	43	GLU	-1	-0.866	-0.925	32.038	-9.499	-9.499	0.000	0.000	0.000	0.000
43	A	44	GLN	0	-0.031	-0.025	35.626	-0.081	-0.081	0.000	0.000	0.000	0.000
44	A	45	SER	0	-0.072	-0.040	36.478	0.105	0.105	0.000	0.000	0.000	0.000
45	A	46	LEU	0	0.011	-0.006	37.469	0.179	0.179	0.000	0.000	0.000	0.000
46	A	47	GLY	0	-0.022	0.009	35.464	-0.067	-0.067	0.000	0.000	0.000	0.000
47	A	48	ILE	0	-0.106	-0.046	32.541	-0.216	-0.216	0.000	0.000	0.000	0.000
48	A	49	GLN	0	-0.012	-0.011	27.492	-0.188	-0.188	0.000	0.000	0.000	0.000
49	A	50	PRO	0	0.066	0.026	27.217	0.073	0.073	0.000	0.000	0.000	0.000
50	A	51	ASP	-1	-0.850	-0.888	24.135	-12.513	-12.513	0.000	0.000	0.000	0.000
51	A	52	ASP	-1	-0.852	-0.948	27.740	-10.816	-10.816	0.000	0.000	0.000	0.000
52	A	53	ALA	0	-0.007	-0.005	30.305	0.156	0.156	0.000	0.000	0.000	0.000
53	A	54	HIS	0	-0.042	0.003	31.487	0.074	0.074	0.000	0.000	0.000	0.000
54	A	55	ILE	0	0.027	0.005	35.121	0.264	0.264	0.000	0.000	0.000	0.000
55	A	56	TYR	0	-0.068	-0.050	37.548	0.004	0.004	0.000	0.000	0.000	0.000
56	A	57	ARG	1	0.867	0.912	39.212	7.733	7.733	0.000	0.000	0.000	0.000
57	A	58	ASN	0	-0.009	-0.009	42.709	0.025	0.025	0.000	0.000	0.000	0.000
58	A	59	ALA	0	0.036	0.004	46.298	-0.010	-0.010	0.000	0.000	0.000	0.000
59	A	60	GLY	0	0.041	-0.009	49.120	0.112	0.112	0.000	0.000	0.000	0.000
60	A	61	GLY	0	0.042	0.019	47.442	0.077	0.077	0.000	0.000	0.000	0.000
61	A	62	ILE	0	-0.013	0.002	48.451	0.006	0.006	0.000	0.000	0.000	0.000
62	A	63	VAL	0	-0.002	0.005	49.276	-0.122	-0.122	0.000	0.000	0.000	0.000
63	A	64	THR	0	0.010	0.004	48.221	0.120	0.120	0.000	0.000	0.000	0.000
64	A	65	ASP	-1	-0.843	-0.931	49.382	-6.415	-6.415	0.000	0.000	0.000	0.000
65	A	66	ASP	-1	-0.717	-0.825	44.650	-7.309	-7.309	0.000	0.000	0.000	0.000
66	A	67	ALA	0	0.002	0.019	44.794	-0.210	-0.210	0.000	0.000	0.000	0.000
67	A	68	ILE	0	0.027	0.010	44.852	-0.160	-0.160	0.000	0.000	0.000	0.000
68	A	69	ARG	1	0.844	0.926	41.052	7.298	7.298	0.000	0.000	0.000	0.000
69	A	70	SER	0	-0.027	-0.024	40.843	-0.227	-0.227	0.000	0.000	0.000	0.000
70	A	71	ALA	0	0.013	0.008	40.638	-0.218	-0.218	0.000	0.000	0.000	0.000
71	A	72	SER	0	-0.024	-0.008	41.861	-0.161	-0.161	0.000	0.000	0.000	0.000
72	A	73	LEU	0	0.010	0.012	38.972	-0.132	-0.132	0.000	0.000	0.000	0.000
73	A	74	THR	0	0.002	-0.012	35.997	-0.240	-0.240	0.000	0.000	0.000	0.000
74	A	75	THR	0	-0.043	-0.045	37.154	-0.156	-0.156	0.000	0.000	0.000	0.000
75	A	76	ASN	0	-0.093	-0.049	38.861	-0.097	-0.097	0.000	0.000	0.000	0.000
76	A	77	PHE	0	-0.013	0.000	36.876	-0.078	-0.078	0.000	0.000	0.000	0.000
77	A	78	PHE	0	-0.041	-0.019	33.301	-0.330	-0.330	0.000	0.000	0.000	0.000
78	A	79	GLY	0	0.015	0.019	33.342	-0.296	-0.296	0.000	0.000	0.000	0.000
79	A	80	THR	0	-0.034	-0.032	35.021	-0.221	-0.221	0.000	0.000	0.000	0.000
80	A	81	LYS	1	0.814	0.880	36.455	8.589	8.589	0.000	0.000	0.000	0.000
81	A	82	GLU	-1	-0.932	-0.954	38.214	-7.949	-7.949	0.000	0.000	0.000	0.000
82	A	83	ILE	0	0.008	0.000	39.450	-0.119	-0.119	0.000	0.000	0.000	0.000
83	A	84	ILE	0	-0.004	-0.002	39.726	0.179	0.179	0.000	0.000	0.000	0.000
84	A	85	VAL	0	0.000	0.007	43.025	-0.059	-0.059	0.000	0.000	0.000	0.000
85	A	86	VAL	0	-0.015	-0.012	42.807	0.045	0.045	0.000	0.000	0.000	0.000
86	A	87	THR	0	0.059	0.037	45.813	-0.070	-0.070	0.000	0.000	0.000	0.000
87	A	88	HIS	1	0.716	0.759	47.726	6.377	6.377	0.000	0.000	0.000	0.000
88	A	89	THR	0	-0.023	-0.048	49.684	0.100	0.100	0.000	0.000	0.000	0.000
89	A	90	ASP	-1	-0.823	-0.896	51.594	-5.874	-5.874	0.000	0.000	0.000	0.000
90	A	91	CYS	0	-0.023	0.027	52.115	-0.072	-0.072	0.000	0.000	0.000	0.000
91	A	92	GLY	0	0.081	0.032	52.547	0.112	0.112	0.000	0.000	0.000	0.000
92	A	93	MET	0	-0.007	-0.011	53.109	0.100	0.100	0.000	0.000	0.000	0.000
93	A	94	LEU	0	-0.006	0.002	55.908	0.083	0.083	0.000	0.000	0.000	0.000
94	A	95	ARG	1	0.769	0.877	56.420	5.558	5.558	0.000	0.000	0.000	0.000
95	A	96	PHE	0	0.019	0.029	57.249	0.038	0.038	0.000	0.000	0.000	0.000
96	A	97	THR	0	0.029	0.018	60.928	-0.058	-0.058	0.000	0.000	0.000	0.000
97	A	98	GLY	0	0.075	0.029	61.519	-0.006	-0.006	0.000	0.000	0.000	0.000
98	A	99	GLU	0	-0.074	-0.084	62.364	0.037	0.037	0.000	0.000	0.000	0.000
99	A	100	GLU	-1	-0.893	-0.948	63.693	-4.907	-4.907	0.000	0.000	0.000	0.000
100	A	101	VAL	0	-0.017	-0.006	58.600	0.011	0.011	0.000	0.000	0.000	0.000
101	A	102	ALA	0	0.026	0.016	61.968	-0.017	-0.017	0.000	0.000	0.000	0.000
102	A	103	LYS	1	1.000	0.993	63.861	4.548	4.548	0.000	0.000	0.000	0.000
103	A	104	TYR	0	0.005	0.023	59.006	0.053	0.053	0.000	0.000	0.000	0.000
104	A	105	PHE	0	0.006	-0.001	56.913	0.004	0.004	0.000	0.000	0.000	0.000
105	A	106	ILE	0	0.028	0.023	62.934	0.016	0.016	0.000	0.000	0.000	0.000
106	A	107	SER	0	-0.117	-0.064	65.774	0.049	0.049	0.000	0.000	0.000	0.000
107	A	108	LYS	1	0.885	0.932	60.821	5.162	5.162	0.000	0.000	0.000	0.000
108	A	109	GLY	0	0.001	0.011	64.743	-0.033	-0.033	0.000	0.000	0.000	0.000
109	A	110	ILE	0	-0.046	-0.016	60.711	-0.011	-0.011	0.000	0.000	0.000	0.000
110	A	111	LYS	1	0.956	0.975	63.930	4.764	4.764	0.000	0.000	0.000	0.000
111	A	112	PRO	0	0.022	-0.003	63.232	-0.054	-0.054	0.000	0.000	0.000	0.000
112	A	113	THR	0	0.009	0.000	63.236	-0.041	-0.041	0.000	0.000	0.000	0.000
113	A	114	GLU	-1	-0.921	-0.961	63.384	-4.809	-4.809	0.000	0.000	0.000	0.000
114	A	115	VAL	0	-0.049	-0.010	58.142	-0.065	-0.065	0.000	0.000	0.000	0.000
115	A	116	GLN	0	0.006	-0.008	55.158	-0.001	-0.001	0.000	0.000	0.000	0.000
116	A	117	LEU	0	-0.014	-0.010	55.433	-0.094	-0.094	0.000	0.000	0.000	0.000
117	A	118	ASP	-1	-0.813	-0.906	50.322	-6.468	-6.468	0.000	0.000	0.000	0.000
118	A	119	PRO	0	-0.056	-0.040	50.787	0.050	0.050	0.000	0.000	0.000	0.000
119	A	120	LEU	0	-0.027	0.001	45.454	-0.026	-0.026	0.000	0.000	0.000	0.000
120	A	121	LEU	0	-0.045	-0.008	49.615	-0.003	-0.003	0.000	0.000	0.000	0.000
121	A	122	PRO	0	0.078	0.036	51.962	0.109	0.109	0.000	0.000	0.000	0.000
122	A	123	ALA	0	-0.054	-0.037	54.993	0.136	0.136	0.000	0.000	0.000	0.000
123	A	124	PHE	0	-0.029	-0.008	54.772	0.097	0.097	0.000	0.000	0.000	0.000
124	A	125	ARG	1	0.887	0.941	56.958	5.372	5.372	0.000	0.000	0.000	0.000
125	A	126	ILE	0	-0.007	0.011	59.998	-0.022	-0.022	0.000	0.000	0.000	0.000
126	A	127	SER	0	-0.013	-0.013	62.558	0.050	0.050	0.000	0.000	0.000	0.000
127	A	128	SER	0	-0.006	-0.003	65.485	0.066	0.066	0.000	0.000	0.000	0.000
128	A	129	GLU	-1	-0.931	-0.964	65.447	-4.740	-4.740	0.000	0.000	0.000	0.000
129	A	130	GLU	-1	-0.848	-0.930	65.512	-4.707	-4.707	0.000	0.000	0.000	0.000
130	A	131	ASP	-1	-0.864	-0.937	62.827	-5.061	-5.061	0.000	0.000	0.000	0.000
131	A	132	PHE	0	-0.032	-0.021	59.198	-0.111	-0.111	0.000	0.000	0.000	0.000
132	A	133	ILE	0	-0.041	-0.022	60.722	-0.100	-0.100	0.000	0.000	0.000	0.000
133	A	134	LYS	1	0.914	0.962	60.854	4.925	4.925	0.000	0.000	0.000	0.000
134	A	135	TRP	0	-0.010	-0.001	53.627	-0.093	-0.093	0.000	0.000	0.000	0.000
135	A	136	PHE	0	0.024	0.004	56.199	-0.151	-0.151	0.000	0.000	0.000	0.000
136	A	137	LYS	1	0.809	0.917	53.651	5.794	5.794	0.000	0.000	0.000	0.000
137	A	138	PHE	0	0.065	0.029	56.637	-0.083	-0.083	0.000	0.000	0.000	0.000
138	A	139	TYR	0	-0.011	-0.033	52.657	0.031	0.031	0.000	0.000	0.000	0.000
139	A	140	GLU	-1	-0.905	-0.949	59.232	-4.925	-4.925	0.000	0.000	0.000	0.000
140	A	141	ASP	-1	-0.789	-0.856	61.794	-4.989	-4.989	0.000	0.000	0.000	0.000
141	A	142	LEU	0	-0.092	-0.054	57.101	0.018	0.018	0.000	0.000	0.000	0.000
142	A	143	GLY	0	-0.034	-0.007	61.487	-0.008	-0.008	0.000	0.000	0.000	0.000
143	A	144	VAL	0	-0.061	-0.017	57.430	0.004	0.004	0.000	0.000	0.000	0.000
144	A	145	LYS	1	0.982	0.979	60.881	4.908	4.908	0.000	0.000	0.000	0.000
145	A	146	SER	0	-0.011	-0.011	57.768	-0.033	-0.033	0.000	0.000	0.000	0.000
146	A	147	PRO	0	0.048	0.026	52.495	-0.013	-0.013	0.000	0.000	0.000	0.000
147	A	148	ASP	-1	-0.739	-0.838	53.121	-6.014	-6.014	0.000	0.000	0.000	0.000
148	A	149	GLU	-1	-0.820	-0.917	54.276	-5.402	-5.402	0.000	0.000	0.000	0.000
149	A	150	MET	0	0.012	0.020	52.868	-0.029	-0.029	0.000	0.000	0.000	0.000
150	A	151	ALA	0	-0.014	0.001	50.006	-0.081	-0.081	0.000	0.000	0.000	0.000
151	A	152	LEU	0	-0.028	-0.023	51.199	-0.078	-0.078	0.000	0.000	0.000	0.000
152	A	153	LYS	1	0.947	0.988	53.553	5.514	5.514	0.000	0.000	0.000	0.000
153	A	154	GLY	0	0.029	0.006	50.711	0.000	0.000	0.000	0.000	0.000	0.000
154	A	155	VAL	0	-0.022	-0.018	48.319	-0.071	-0.071	0.000	0.000	0.000	0.000
155	A	156	GLU	-1	-0.893	-0.943	50.464	-5.763	-5.763	0.000	0.000	0.000	0.000
156	A	157	ILE	0	0.039	0.020	52.149	-0.032	-0.032	0.000	0.000	0.000	0.000
157	A	158	LEU	0	-0.030	-0.022	46.478	-0.045	-0.045	0.000	0.000	0.000	0.000
158	A	159	ARG	1	0.862	0.922	49.028	6.323	6.323	0.000	0.000	0.000	0.000
159	A	160	ASN	0	-0.029	-0.034	50.846	-0.026	-0.026	0.000	0.000	0.000	0.000
160	A	161	HIS	0	0.006	0.017	50.258	-0.015	-0.015	0.000	0.000	0.000	0.000
161	A	162	PRO	0	0.004	-0.009	50.677	-0.115	-0.115	0.000	0.000	0.000	0.000
162	A	163	LEU	0	-0.016	-0.005	47.351	-0.076	-0.076	0.000	0.000	0.000	0.000
163	A	164	ILE	0	0.005	0.009	44.531	-0.204	-0.204	0.000	0.000	0.000	0.000
164	A	165	PRO	0	0.010	0.018	42.608	0.173	0.173	0.000	0.000	0.000	0.000
165	A	166	LYS	1	0.862	0.917	45.045	6.501	6.501	0.000	0.000	0.000	0.000
166	A	167	ASP	-1	-0.830	-0.895	40.983	-7.792	-7.792	0.000	0.000	0.000	0.000
167	A	168	VAL	0	-0.057	-0.017	41.028	-0.121	-0.121	0.000	0.000	0.000	0.000
168	A	169	ARG	1	0.927	0.973	42.078	7.511	7.511	0.000	0.000	0.000	0.000
169	A	170	ILE	0	0.037	0.021	43.160	-0.100	-0.100	0.000	0.000	0.000	0.000
170	A	171	THR	0	-0.011	-0.002	44.245	0.246	0.246	0.000	0.000	0.000	0.000
171	A	172	GLY	0	0.036	0.015	46.153	-0.054	-0.054	0.000	0.000	0.000	0.000
172	A	173	TYR	0	-0.036	-0.029	43.391	0.102	0.102	0.000	0.000	0.000	0.000
173	A	174	VAL	0	-0.018	0.011	47.942	0.026	0.026	0.000	0.000	0.000	0.000
174	A	175	TYR	0	0.020	-0.005	41.905	-0.100	-0.100	0.000	0.000	0.000	0.000
175	A	176	GLU	-1	-0.762	-0.852	47.001	-6.092	-6.092	0.000	0.000	0.000	0.000
176	A	177	VAL	0	-0.004	-0.013	47.094	-0.119	-0.119	0.000	0.000	0.000	0.000
177	A	178	GLU	-1	-0.830	-0.881	48.417	-6.145	-6.145	0.000	0.000	0.000	0.000
178	A	179	THR	0	-0.074	-0.059	47.356	0.034	0.034	0.000	0.000	0.000	0.000
179	A	180	HIS	0	-0.016	0.013	42.790	-0.245	-0.245	0.000	0.000	0.000	0.000
180	A	181	ARG	1	0.954	0.990	43.059	6.446	6.446	0.000	0.000	0.000	0.000
181	A	182	LEU	0	0.021	0.015	42.459	0.141	0.141	0.000	0.000	0.000	0.000
182	A	183	ARG	1	0.796	0.861	46.006	6.023	6.023	0.000	0.000	0.000	0.000
183	A	184	LYS	1	0.895	0.934	49.104	5.989	5.989	0.000	0.000	0.000	0.000
184	A	185	PRO	0	-0.008	-0.009	50.207	0.108	0.108	0.000	0.000	0.000	0.000
185	A	186	ASN	0	-0.039	-0.032	53.317	0.021	0.021	0.000	0.000	0.000	0.000
186	A	187	GLN	0	0.016	0.028	52.467	0.081	0.081	0.000	0.000	0.000	0.000
187	A	188	ILE	0	-0.010	-0.006	54.386	-0.101	-0.101	0.000	0.000	0.000	0.000
188	A	189	ILE	0	0.117	0.062	53.581	0.066	0.066	0.000	0.000	0.000	0.000
189	A	190	TYR	0	-0.062	-0.045	51.373	0.058	0.058	0.000	0.000	0.000	0.000
190	A	191	ASN	0	0.000	-0.005	57.881	-0.001	-0.001	0.000	0.000	0.000	0.000
191	A	192	GLU	-1	-0.948	-0.967	58.874	-5.356	-5.356	0.000	0.000	0.000	0.000
192	A	193	THR	0	-0.003	-0.034	56.596	0.058	0.058	0.000	0.000	0.000	0.000
193	A	194	SER	0	-0.039	-0.004	60.039	0.013	0.013	0.000	0.000	0.000	0.000
194	A	195	LYS	1	0.889	0.948	62.655	4.945	4.945	0.000	0.000	0.000	0.000
195	A	196	PHE	0	-0.009	0.003	64.989	-0.036	-0.036	0.000	0.000	0.000	0.000
196	A	197	GLU	-1	-0.908	-0.964	62.005	-5.183	-5.183	0.000	0.000	0.000	0.000
197	A	198	HIS	0	-0.050	-0.016	66.019	0.033	0.033	0.000	0.000	0.000	0.000
198	A	199	GLY	0	0.050	0.034	63.102	-0.050	-0.050	0.000	0.000	0.000	0.000
199	A	200	THR	0	-0.040	-0.030	61.286	0.069	0.069	0.000	0.000	0.000	0.000
200	A	201	ILE	0	-0.019	-0.010	62.350	-0.045	-0.045	0.000	0.000	0.000	0.000
201	A	202	VAL	0	0.023	0.015	57.649	-0.003	-0.003	0.000	0.000	0.000	0.000
202	A	203	LYS	0	-0.017	-0.004	57.828	-0.358	-0.358	0.000	0.000	0.000	0.000

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