FMO DATABASE

FMODB ID: RQR18

Calculation Name: 2BDZ-A-Xray547

Preferred Name:

Target Type:

Ligand Name: n-[n-[1-hydroxycarboxyethyl-carbonyl]leucylamino-butyl]-guanidine

Ligand 3-letter code: E64

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2BDZ

Chain ID: A

ChEMBL ID:

UniProt ID: P84346

Base Structure: X-ray

Registration Date: 2025-10-03

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	209
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2542476.180697
FMO2-HF: Nuclear repulsion	2459995.978277
FMO2-HF: Total energy	-82480.202419
FMO2-MP2: Total energy	-82720.741951

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:1:TYR)

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

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.
66.387	78.564	9.616	-6.375	-15.414	-0.037

Interaction energy analysis for fragmet #1(A:1:TYR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.845 / q_NPA : 0.922

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	3	GLU	-1	-0.762	-0.869	2.340	-38.882	-36.369	1.923	-1.722	-2.714	-0.023
4	A	4	SER	0	-0.025	-0.020	4.219	2.552	2.772	-0.001	-0.002	-0.216	0.000
117	A	119	ILE	0	-0.027	-0.014	1.995	-5.451	-4.314	1.960	-0.892	-2.204	-0.002
118	A	120	SER	0	0.002	-0.023	4.749	-3.566	-3.388	-0.001	-0.004	-0.172	0.000
120	A	122	ILE	0	-0.021	-0.012	2.942	-2.309	-0.835	2.773	-0.721	-3.525	0.006
121	A	123	GLN	0	-0.026	-0.022	2.512	-3.126	-1.414	0.646	-0.510	-1.849	-0.003
122	A	124	ALA	0	-0.005	0.017	4.297	0.071	0.253	0.001	-0.026	-0.156	0.000
124	A	126	ALA	0	-0.061	-0.021	2.440	-0.480	0.090	0.996	-0.585	-0.981	-0.004
125	A	127	ASN	0	-0.067	-0.023	4.364	-0.160	-0.060	-0.001	-0.025	-0.074	0.000
164	A	166	TYR	0	-0.080	-0.047	2.415	-1.684	1.278	1.281	-1.426	-2.817	-0.016
189	A	191	ARG	1	0.804	0.898	3.127	29.690	30.819	0.039	-0.462	-0.706	0.005
5	A	5	ILE	0	-0.032	-0.009	5.713	-2.354	-2.354	0.000	0.000	0.000	0.000
6	A	6	ASP	-1	-0.740	-0.847	7.763	-18.076	-18.076	0.000	0.000	0.000	0.000
7	A	7	TRP	0	0.009	-0.022	8.195	1.775	1.775	0.000	0.000	0.000	0.000
8	A	8	ARG	1	0.799	0.878	12.538	18.197	18.197	0.000	0.000	0.000	0.000
9	A	9	GLU	-1	-0.900	-0.942	12.526	-21.013	-21.013	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.895	0.955	8.926	27.555	27.555	0.000	0.000	0.000	0.000
11	A	11	GLY	0	0.025	0.023	14.552	0.408	0.408	0.000	0.000	0.000	0.000
12	A	12	ALA	0	-0.043	-0.030	14.372	0.673	0.673	0.000	0.000	0.000	0.000
13	A	13	VAL	0	0.006	-0.009	15.219	-0.200	-0.200	0.000	0.000	0.000	0.000
14	A	14	THR	0	-0.012	-0.026	17.954	0.373	0.373	0.000	0.000	0.000	0.000
15	A	15	PRO	0	0.033	0.007	21.403	-0.311	-0.311	0.000	0.000	0.000	0.000
16	A	16	VAL	0	-0.042	0.001	22.164	-0.115	-0.115	0.000	0.000	0.000	0.000
17	A	17	LYS	1	0.811	0.913	24.375	12.107	12.107	0.000	0.000	0.000	0.000
18	A	18	ASN	0	-0.003	-0.034	26.776	-0.227	-0.227	0.000	0.000	0.000	0.000
19	A	19	GLN	0	0.044	0.031	27.368	-0.132	-0.132	0.000	0.000	0.000	0.000
20	A	20	ASN	0	-0.003	0.026	30.216	0.230	0.230	0.000	0.000	0.000	0.000
21	A	21	PRO	0	0.006	-0.015	33.006	0.071	0.071	0.000	0.000	0.000	0.000
22	A	22	CYS	0	-0.068	-0.025	32.506	-0.258	-0.258	0.000	0.000	0.000	0.000
23	A	23	GLY	0	0.095	0.055	31.141	-0.304	-0.304	0.000	0.000	0.000	0.000
24	A	24	SER	0	0.017	-0.022	29.817	-0.188	-0.188	0.000	0.000	0.000	0.000
25	A	25	CYS	0	-0.074	-0.013	25.067	-0.198	-0.198	0.000	0.000	0.000	0.000
26	A	26	TRP	0	0.031	0.022	24.257	-0.612	-0.612	0.000	0.000	0.000	0.000
27	A	27	ALA	0	0.020	0.018	24.054	-0.387	-0.387	0.000	0.000	0.000	0.000
28	A	28	PHE	0	-0.018	-0.020	23.881	-0.289	-0.289	0.000	0.000	0.000	0.000
29	A	29	SER	0	-0.063	-0.013	19.476	-0.544	-0.544	0.000	0.000	0.000	0.000
30	A	30	THR	0	0.060	0.010	19.333	-0.976	-0.976	0.000	0.000	0.000	0.000
31	A	31	VAL	0	0.019	0.024	20.246	-0.595	-0.595	0.000	0.000	0.000	0.000
32	A	32	ALA	0	-0.020	-0.002	18.776	-0.251	-0.251	0.000	0.000	0.000	0.000
33	A	33	THR	0	-0.075	-0.056	15.567	-0.811	-0.811	0.000	0.000	0.000	0.000
34	A	34	ILE	0	0.004	0.005	17.232	-0.497	-0.497	0.000	0.000	0.000	0.000
35	A	35	GLU	-1	-0.746	-0.847	19.985	-12.892	-12.892	0.000	0.000	0.000	0.000
36	A	36	GLY	0	0.031	0.022	15.843	-0.028	-0.028	0.000	0.000	0.000	0.000
37	A	37	ILE	0	-0.002	-0.011	14.081	-0.540	-0.540	0.000	0.000	0.000	0.000
38	A	38	ASN	0	0.032	0.005	16.461	0.269	0.269	0.000	0.000	0.000	0.000
39	A	39	LYS	1	0.830	0.951	16.868	15.610	15.610	0.000	0.000	0.000	0.000
40	A	40	ILE	0	-0.053	-0.035	11.967	0.131	0.131	0.000	0.000	0.000	0.000
41	A	41	ILE	0	-0.014	0.008	15.438	-0.196	-0.196	0.000	0.000	0.000	0.000
42	A	42	THR	0	-0.022	-0.030	17.905	0.754	0.754	0.000	0.000	0.000	0.000
43	A	43	GLY	0	0.036	0.027	19.439	0.644	0.644	0.000	0.000	0.000	0.000
44	A	44	GLN	0	-0.043	-0.024	20.555	0.415	0.415	0.000	0.000	0.000	0.000
45	A	45	LEU	0	-0.018	-0.001	19.303	-0.287	-0.287	0.000	0.000	0.000	0.000
46	A	46	ILE	0	-0.002	-0.008	22.052	0.552	0.552	0.000	0.000	0.000	0.000
47	A	47	SER	0	-0.015	-0.003	24.043	-0.437	-0.437	0.000	0.000	0.000	0.000
48	A	48	LEU	0	-0.038	-0.011	23.208	0.494	0.494	0.000	0.000	0.000	0.000
49	A	49	SER	0	-0.004	-0.029	26.639	0.000	0.000	0.000	0.000	0.000	0.000
50	A	50	GLU	-1	-0.729	-0.870	25.222	-11.483	-11.483	0.000	0.000	0.000	0.000
51	A	51	GLN	0	-0.043	-0.031	28.678	0.035	0.035	0.000	0.000	0.000	0.000
52	A	52	GLU	-1	-0.741	-0.857	30.848	-9.432	-9.432	0.000	0.000	0.000	0.000
53	A	53	LEU	0	-0.018	-0.002	25.863	0.129	0.129	0.000	0.000	0.000	0.000
54	A	54	LEU	0	-0.017	0.007	30.524	0.156	0.156	0.000	0.000	0.000	0.000
55	A	55	ASP	-1	-0.693	-0.793	32.809	-8.065	-8.065	0.000	0.000	0.000	0.000
56	A	56	CYS	0	-0.053	-0.007	33.599	0.256	0.256	0.000	0.000	0.000	0.000
57	A	57	GLU	-1	-0.742	-0.821	28.933	-10.064	-10.064	0.000	0.000	0.000	0.000
58	A	58	ARG	1	0.786	0.881	32.388	7.992	7.992	0.000	0.000	0.000	0.000
59	A	59	ARG	1	0.869	0.954	29.445	10.191	10.191	0.000	0.000	0.000	0.000
60	A	60	SER	0	-0.011	-0.017	29.402	-0.098	-0.098	0.000	0.000	0.000	0.000
61	A	61	HIS	1	0.837	0.898	31.765	9.357	9.357	0.000	0.000	0.000	0.000
62	A	62	GLY	0	0.072	0.037	33.380	0.188	0.188	0.000	0.000	0.000	0.000
63	A	64	ASP	-1	-0.867	-0.917	34.108	-8.294	-8.294	0.000	0.000	0.000	0.000
64	A	65	GLY	0	0.012	0.007	30.202	-0.093	-0.093	0.000	0.000	0.000	0.000
65	A	66	GLY	0	-0.002	-0.036	29.024	0.282	0.282	0.000	0.000	0.000	0.000
66	A	67	TYR	0	0.010	0.019	25.992	-0.200	-0.200	0.000	0.000	0.000	0.000
67	A	68	GLN	0	0.025	0.028	18.909	0.415	0.415	0.000	0.000	0.000	0.000
68	A	69	THR	0	0.031	0.028	22.223	0.005	0.005	0.000	0.000	0.000	0.000
69	A	70	THR	0	0.005	-0.026	23.644	-0.041	-0.041	0.000	0.000	0.000	0.000
70	A	71	SER	0	-0.006	-0.006	24.698	0.107	0.107	0.000	0.000	0.000	0.000
71	A	72	LEU	0	0.007	-0.008	19.074	0.050	0.050	0.000	0.000	0.000	0.000
72	A	73	GLN	0	-0.038	-0.035	23.067	-0.260	-0.260	0.000	0.000	0.000	0.000
73	A	74	TYR	0	-0.068	-0.048	25.746	0.328	0.328	0.000	0.000	0.000	0.000
74	A	75	VAL	0	-0.002	-0.004	23.914	0.262	0.262	0.000	0.000	0.000	0.000
75	A	76	VAL	0	-0.021	-0.004	23.337	-0.100	-0.100	0.000	0.000	0.000	0.000
76	A	77	ASP	-1	-0.848	-0.918	25.884	-10.193	-10.193	0.000	0.000	0.000	0.000
77	A	78	ASN	0	-0.068	-0.033	29.337	0.557	0.557	0.000	0.000	0.000	0.000
78	A	79	GLY	0	0.016	0.013	27.301	0.174	0.174	0.000	0.000	0.000	0.000
79	A	80	VAL	0	-0.081	-0.048	25.530	0.178	0.178	0.000	0.000	0.000	0.000
80	A	81	HIS	0	0.003	0.000	28.608	-0.091	-0.091	0.000	0.000	0.000	0.000
81	A	82	THR	0	0.051	0.019	29.029	-0.204	-0.204	0.000	0.000	0.000	0.000
82	A	83	GLU	-1	-0.849	-0.934	28.704	-10.115	-10.115	0.000	0.000	0.000	0.000
83	A	84	ARG	1	0.817	0.885	29.281	10.159	10.159	0.000	0.000	0.000	0.000
84	A	85	GLU	-1	-0.722	-0.835	33.384	-8.339	-8.339	0.000	0.000	0.000	0.000
85	A	86	TYR	0	-0.082	-0.075	33.022	0.328	0.328	0.000	0.000	0.000	0.000
86	A	87	PRO	0	0.051	0.047	32.995	-0.313	-0.313	0.000	0.000	0.000	0.000
87	A	88	TYR	0	-0.024	-0.032	31.774	0.085	0.085	0.000	0.000	0.000	0.000
88	A	89	GLU	-1	-0.841	-0.920	33.901	-7.622	-7.622	0.000	0.000	0.000	0.000
89	A	90	LYS	1	0.887	0.954	34.515	8.749	8.749	0.000	0.000	0.000	0.000
90	A	91	LYS	1	0.976	0.993	35.792	7.587	7.587	0.000	0.000	0.000	0.000
91	A	92	GLN	0	0.008	0.003	35.966	0.072	0.072	0.000	0.000	0.000	0.000
92	A	93	GLY	0	0.010	0.010	37.890	0.232	0.232	0.000	0.000	0.000	0.000
93	A	94	ARG	1	0.844	0.893	39.719	7.114	7.114	0.000	0.000	0.000	0.000
94	A	96	ARG	1	0.783	0.844	37.875	8.051	8.051	0.000	0.000	0.000	0.000
95	A	97	ALA	0	0.050	0.025	35.002	0.047	0.047	0.000	0.000	0.000	0.000
96	A	98	LYS	1	0.939	0.961	36.530	7.130	7.130	0.000	0.000	0.000	0.000
97	A	99	ASP	-1	-0.792	-0.868	39.501	-7.131	-7.131	0.000	0.000	0.000	0.000
98	A	100	LYS	1	0.851	0.943	36.149	8.276	8.276	0.000	0.000	0.000	0.000
99	A	101	LYS	1	0.804	0.881	38.060	7.737	7.737	0.000	0.000	0.000	0.000
100	A	102	GLY	0	0.007	0.018	35.677	0.014	0.014	0.000	0.000	0.000	0.000
101	A	103	PRO	0	-0.017	-0.021	30.740	-0.090	-0.090	0.000	0.000	0.000	0.000
102	A	104	LYS	1	0.867	0.949	29.865	9.526	9.526	0.000	0.000	0.000	0.000
103	A	105	VAL	0	-0.027	-0.003	23.116	-0.136	-0.136	0.000	0.000	0.000	0.000
104	A	106	TYR	0	0.077	0.031	25.493	0.184	0.184	0.000	0.000	0.000	0.000
105	A	107	ILE	0	-0.079	-0.031	20.414	-0.542	-0.542	0.000	0.000	0.000	0.000
106	A	108	THR	0	0.051	0.017	21.306	0.283	0.283	0.000	0.000	0.000	0.000
107	A	109	GLY	0	0.032	0.018	20.878	0.348	0.348	0.000	0.000	0.000	0.000
108	A	110	TYR	0	-0.033	-0.018	17.853	-0.402	-0.402	0.000	0.000	0.000	0.000
109	A	111	LYS	1	0.959	0.991	11.615	22.529	22.529	0.000	0.000	0.000	0.000
110	A	112	TYR	0	0.017	0.009	15.854	-0.237	-0.237	0.000	0.000	0.000	0.000
111	A	113	VAL	0	-0.045	-0.029	10.412	-1.067	-1.067	0.000	0.000	0.000	0.000
112	A	114	PRO	0	-0.019	-0.014	11.286	0.985	0.985	0.000	0.000	0.000	0.000
113	A	115	ALA	0	0.035	0.032	12.461	-0.948	-0.948	0.000	0.000	0.000	0.000
114	A	116	ASN	0	-0.058	-0.048	14.185	0.041	0.041	0.000	0.000	0.000	0.000
115	A	117	ASP	-1	-0.817	-0.895	8.183	-26.000	-26.000	0.000	0.000	0.000	0.000
116	A	118	GLU	-1	-0.780	-0.866	5.455	-28.870	-28.870	0.000	0.000	0.000	0.000
119	A	121	LEU	0	-0.004	0.001	7.453	-0.292	-0.292	0.000	0.000	0.000	0.000
123	A	125	ILE	0	0.008	-0.006	6.736	0.152	0.152	0.000	0.000	0.000	0.000
126	A	128	GLN	0	0.006	-0.001	7.519	2.817	2.817	0.000	0.000	0.000	0.000
127	A	129	PRO	0	-0.021	-0.006	10.018	-0.669	-0.669	0.000	0.000	0.000	0.000
128	A	130	VAL	0	-0.023	-0.002	10.298	0.585	0.585	0.000	0.000	0.000	0.000
129	A	131	SER	0	-0.008	0.001	13.210	0.651	0.651	0.000	0.000	0.000	0.000
130	A	132	VAL	0	0.009	-0.015	13.876	-0.571	-0.571	0.000	0.000	0.000	0.000
131	A	133	VAL	0	0.008	0.014	17.133	0.762	0.762	0.000	0.000	0.000	0.000
132	A	134	THR	0	-0.010	-0.017	18.592	-0.493	-0.493	0.000	0.000	0.000	0.000
133	A	135	ASP	-1	-0.860	-0.930	21.015	-10.571	-10.571	0.000	0.000	0.000	0.000
134	A	136	SER	0	-0.037	-0.041	23.720	-0.036	-0.036	0.000	0.000	0.000	0.000
135	A	137	ARG	1	0.893	0.951	25.727	10.617	10.617	0.000	0.000	0.000	0.000
136	A	138	GLY	0	0.017	0.015	27.205	0.397	0.397	0.000	0.000	0.000	0.000
137	A	139	ARG	1	0.918	0.941	28.204	8.793	8.793	0.000	0.000	0.000	0.000
138	A	140	GLY	0	0.045	0.026	26.733	0.012	0.012	0.000	0.000	0.000	0.000
139	A	141	PHE	0	0.049	0.032	20.768	-0.188	-0.188	0.000	0.000	0.000	0.000
140	A	142	GLN	0	0.015	-0.008	25.213	0.168	0.168	0.000	0.000	0.000	0.000
141	A	143	PHE	0	-0.027	-0.015	28.307	0.066	0.066	0.000	0.000	0.000	0.000
142	A	144	TYR	0	0.005	0.029	19.334	0.131	0.131	0.000	0.000	0.000	0.000
143	A	145	LYS	1	0.825	0.887	24.669	10.334	10.334	0.000	0.000	0.000	0.000
144	A	146	GLY	0	0.048	0.013	21.697	-0.068	-0.068	0.000	0.000	0.000	0.000
145	A	147	GLY	0	-0.001	0.011	19.167	0.276	0.276	0.000	0.000	0.000	0.000
146	A	148	ILE	0	-0.043	-0.012	13.095	-0.294	-0.294	0.000	0.000	0.000	0.000
147	A	149	TYR	0	0.002	-0.029	16.747	0.538	0.538	0.000	0.000	0.000	0.000
148	A	150	GLU	-1	-0.825	-0.919	16.804	-15.204	-15.204	0.000	0.000	0.000	0.000
149	A	151	GLY	0	-0.011	0.007	18.499	-0.006	-0.006	0.000	0.000	0.000	0.000
150	A	152	PRO	0	0.009	0.007	21.649	0.077	0.077	0.000	0.000	0.000	0.000
151	A	153	CYS	0	-0.089	-0.030	16.460	-0.314	-0.314	0.000	0.000	0.000	0.000
152	A	154	GLY	0	0.043	0.044	23.077	-0.052	-0.052	0.000	0.000	0.000	0.000
153	A	155	THR	0	-0.047	-0.049	19.720	-0.474	-0.474	0.000	0.000	0.000	0.000
154	A	156	ASN	0	-0.009	0.009	22.254	-0.265	-0.265	0.000	0.000	0.000	0.000
155	A	157	THR	0	-0.012	-0.012	20.467	0.190	0.190	0.000	0.000	0.000	0.000
156	A	158	ASP	-1	-0.827	-0.904	23.869	-10.608	-10.608	0.000	0.000	0.000	0.000
157	A	159	HIS	0	-0.020	-0.013	24.117	0.345	0.345	0.000	0.000	0.000	0.000
158	A	160	ALA	0	0.021	0.006	21.702	-0.567	-0.567	0.000	0.000	0.000	0.000
159	A	161	VAL	0	0.008	0.002	18.128	0.324	0.324	0.000	0.000	0.000	0.000
160	A	162	THR	0	0.026	0.025	15.209	-0.050	-0.050	0.000	0.000	0.000	0.000
161	A	163	ALA	0	-0.003	0.004	11.590	0.158	0.158	0.000	0.000	0.000	0.000
162	A	164	VAL	0	0.003	-0.015	12.290	-0.612	-0.612	0.000	0.000	0.000	0.000
163	A	165	GLY	0	0.063	0.018	9.073	-0.345	-0.345	0.000	0.000	0.000	0.000
165	A	167	GLY	0	0.042	0.021	7.108	-0.811	-0.811	0.000	0.000	0.000	0.000
166	A	168	LYS	1	0.860	0.912	5.636	26.052	26.052	0.000	0.000	0.000	0.000
167	A	169	THR	0	0.040	0.022	6.685	-0.068	-0.068	0.000	0.000	0.000	0.000
168	A	170	TYR	0	-0.012	-0.001	8.914	1.306	1.306	0.000	0.000	0.000	0.000
169	A	171	LEU	0	0.051	0.023	8.582	-2.440	-2.440	0.000	0.000	0.000	0.000
170	A	172	LEU	0	-0.046	-0.023	10.907	1.710	1.710	0.000	0.000	0.000	0.000
171	A	173	LEU	0	0.009	0.001	13.210	-0.710	-0.710	0.000	0.000	0.000	0.000
172	A	174	LYS	1	0.859	0.929	15.915	14.393	14.393	0.000	0.000	0.000	0.000
173	A	175	ASN	0	0.028	0.025	18.557	0.006	0.006	0.000	0.000	0.000	0.000
174	A	176	SER	0	0.009	-0.012	21.922	-0.142	-0.142	0.000	0.000	0.000	0.000
175	A	177	TRP	0	0.000	-0.001	25.012	0.405	0.405	0.000	0.000	0.000	0.000
176	A	178	GLY	0	0.028	0.019	27.009	0.377	0.377	0.000	0.000	0.000	0.000
177	A	179	PRO	0	0.002	-0.012	26.108	-0.208	-0.208	0.000	0.000	0.000	0.000
178	A	180	ASN	0	-0.035	-0.034	27.174	-0.162	-0.162	0.000	0.000	0.000	0.000
179	A	181	TRP	0	0.013	0.032	21.872	0.010	0.010	0.000	0.000	0.000	0.000
180	A	182	GLY	0	0.021	0.009	23.589	-0.374	-0.374	0.000	0.000	0.000	0.000
181	A	183	GLU	-1	-0.750	-0.823	18.543	-14.357	-14.357	0.000	0.000	0.000	0.000
182	A	184	LYS	1	0.877	0.922	21.928	10.407	10.407	0.000	0.000	0.000	0.000
183	A	185	GLY	0	0.011	0.012	23.784	-0.058	-0.058	0.000	0.000	0.000	0.000
184	A	186	TYR	0	-0.019	-0.010	17.540	-0.538	-0.538	0.000	0.000	0.000	0.000
185	A	187	ILE	0	0.025	0.006	18.060	0.619	0.619	0.000	0.000	0.000	0.000
186	A	188	ARG	1	0.819	0.896	14.279	15.017	15.017	0.000	0.000	0.000	0.000
187	A	189	ILE	0	0.035	0.023	14.473	0.911	0.911	0.000	0.000	0.000	0.000
188	A	190	LYS	1	0.880	0.936	12.941	14.102	14.102	0.000	0.000	0.000	0.000
190	A	192	ALA	0	-0.024	-0.004	10.354	0.860	0.860	0.000	0.000	0.000	0.000
191	A	193	SER	0	0.029	0.020	8.096	-1.630	-1.630	0.000	0.000	0.000	0.000
192	A	194	GLY	0	0.036	0.014	7.272	1.356	1.356	0.000	0.000	0.000	0.000
193	A	195	ARG	1	0.968	0.985	8.520	18.161	18.161	0.000	0.000	0.000	0.000
194	A	196	SER	0	0.030	0.009	11.969	1.173	1.173	0.000	0.000	0.000	0.000
195	A	197	LYS	1	0.996	0.995	13.842	11.907	11.907	0.000	0.000	0.000	0.000
196	A	198	GLY	0	0.045	0.036	13.459	-0.214	-0.214	0.000	0.000	0.000	0.000
197	A	199	THR	0	-0.014	-0.037	14.320	1.167	1.167	0.000	0.000	0.000	0.000
198	A	201	GLY	0	0.073	0.040	18.333	0.316	0.316	0.000	0.000	0.000	0.000
199	A	202	VAL	0	-0.005	0.023	13.491	-0.177	-0.177	0.000	0.000	0.000	0.000
200	A	203	TYR	0	-0.048	-0.039	9.331	-1.150	-1.150	0.000	0.000	0.000	0.000
201	A	204	THR	0	-0.018	-0.016	14.293	-0.026	-0.026	0.000	0.000	0.000	0.000
202	A	205	SER	0	-0.017	-0.030	17.743	0.316	0.316	0.000	0.000	0.000	0.000
203	A	206	SER	0	0.016	0.014	13.909	0.475	0.475	0.000	0.000	0.000	0.000
204	A	207	PHE	0	0.018	0.007	15.686	-0.134	-0.134	0.000	0.000	0.000	0.000
205	A	208	PHE	0	0.013	0.004	11.025	-0.543	-0.543	0.000	0.000	0.000	0.000
206	A	209	PRO	0	0.027	0.017	14.831	0.351	0.351	0.000	0.000	0.000	0.000
207	A	210	ILE	0	-0.018	-0.012	15.450	-1.224	-1.224	0.000	0.000	0.000	0.000
208	A	211	LYS	1	0.835	0.913	17.028	14.577	14.577	0.000	0.000	0.000	0.000
209	A	212	GLY	-1	-0.834	-0.907	18.542	-14.239	-14.239	0.000	0.000	0.000	0.000

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