FMO DATABASE

FMODB ID: YNQZ2

Calculation Name: 1EBA-A-Xray372

Preferred Name: Erythropoietin receptor

Target Type: SINGLE PROTEIN

Ligand Name: 3,5 dibromotyrosine

ligand 3-letter code: DBY

PDB ID: 1EBA

Chain ID: A

ChEMBL ID: CHEMBL1817

UniProt ID: P19235

Base Structure: X-ray

Registration Date: 2023-09-26

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptHSide
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	213
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2241033.911227
FMO2-HF: Nuclear repulsion	2157884.680137
FMO2-HF: Total energy	-83149.23109
FMO2-MP2: Total energy	-83391.85893

3D Structure

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:10:LYS)

Summations of interaction energy for fragment #1(A:10: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.
-7.755	-2.894	1.124	-2.288	-3.698	-0.008

Interaction energy analysis for fragmet #1(A:10:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 1.026 / q_NPA : 0.999

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	12	GLU	-1	-0.822	-0.921	3.318	-25.682	-23.555	0.005	-0.873	-1.260	0.002
4	A	13	SER	0	-0.012	-0.006	2.642	-2.281	-0.345	1.101	-1.220	-1.817	-0.010
5	A	14	LYS	1	0.932	0.951	3.374	51.934	52.732	0.018	-0.195	-0.621	0.000
6	A	15	ALA	0	0.011	0.014	6.040	2.886	2.886	0.000	0.000	0.000	0.000
7	A	16	ALA	0	0.022	0.015	7.679	2.446	2.446	0.000	0.000	0.000	0.000
8	A	17	LEU	0	-0.074	-0.042	7.386	1.443	1.443	0.000	0.000	0.000	0.000
9	A	18	LEU	0	-0.041	-0.022	9.629	1.321	1.321	0.000	0.000	0.000	0.000
10	A	19	ALA	0	-0.011	0.028	12.339	1.374	1.374	0.000	0.000	0.000	0.000
11	A	20	ALA	0	-0.028	-0.021	14.251	0.345	0.345	0.000	0.000	0.000	0.000
12	A	21	ARG	1	0.964	0.995	17.182	15.283	15.283	0.000	0.000	0.000	0.000
13	A	22	GLY	0	0.012	-0.002	19.307	0.223	0.223	0.000	0.000	0.000	0.000
14	A	23	PRO	0	-0.027	-0.024	23.058	-0.220	-0.220	0.000	0.000	0.000	0.000
15	A	24	GLU	-1	-0.883	-0.927	23.509	-11.312	-11.312	0.000	0.000	0.000	0.000
16	A	25	GLU	-1	-0.796	-0.893	23.942	-9.736	-9.736	0.000	0.000	0.000	0.000
17	A	26	LEU	0	-0.037	0.004	24.496	-0.346	-0.346	0.000	0.000	0.000	0.000
18	A	27	LEU	0	-0.025	-0.012	20.300	0.165	0.165	0.000	0.000	0.000	0.000
19	A	28	CYS	0	-0.045	-0.017	24.157	0.009	0.009	0.000	0.000	0.000	0.000
20	A	29	PHE	0	-0.017	-0.010	19.718	-0.108	-0.108	0.000	0.000	0.000	0.000
21	A	30	THR	0	0.006	0.008	24.200	0.090	0.090	0.000	0.000	0.000	0.000
22	A	31	GLU	-1	-0.899	-0.942	20.414	-12.424	-12.424	0.000	0.000	0.000	0.000
23	A	32	ARG	1	0.792	0.866	20.962	11.437	11.437	0.000	0.000	0.000	0.000
24	A	33	LEU	0	-0.051	-0.028	26.543	0.037	0.037	0.000	0.000	0.000	0.000
25	A	34	GLU	-1	-0.972	-0.980	29.110	-8.447	-8.447	0.000	0.000	0.000	0.000
26	A	35	ASP	-1	-0.792	-0.894	25.701	-10.364	-10.364	0.000	0.000	0.000	0.000
27	A	36	LEU	0	0.041	0.001	26.836	0.092	0.092	0.000	0.000	0.000	0.000
28	A	37	VAL	0	-0.025	-0.004	22.366	0.092	0.092	0.000	0.000	0.000	0.000
29	A	39	PHE	0	-0.031	-0.039	18.653	-0.233	-0.233	0.000	0.000	0.000	0.000
30	A	40	TRP	0	0.011	0.009	22.953	0.218	0.218	0.000	0.000	0.000	0.000
31	A	41	GLU	-1	-0.828	-0.918	17.182	-16.080	-16.080	0.000	0.000	0.000	0.000
32	A	42	GLU	-1	-0.702	-0.789	21.637	-10.364	-10.364	0.000	0.000	0.000	0.000
33	A	43	ALA	0	-0.021	-0.012	21.814	-0.608	-0.608	0.000	0.000	0.000	0.000
34	A	44	ALA	0	0.025	0.013	22.262	0.355	0.355	0.000	0.000	0.000	0.000
35	A	45	SER	0	0.044	0.000	24.004	0.386	0.386	0.000	0.000	0.000	0.000
36	A	46	ALA	0	-0.021	-0.001	27.679	0.068	0.068	0.000	0.000	0.000	0.000
37	A	47	GLY	0	0.003	-0.001	29.111	0.253	0.253	0.000	0.000	0.000	0.000
38	A	48	VAL	0	-0.023	-0.005	28.474	0.339	0.339	0.000	0.000	0.000	0.000
39	A	49	GLY	0	0.022	0.023	27.841	-0.427	-0.427	0.000	0.000	0.000	0.000
40	A	50	PRO	0	-0.002	-0.015	27.266	0.189	0.189	0.000	0.000	0.000	0.000
41	A	51	GLY	0	-0.029	-0.005	29.308	0.209	0.209	0.000	0.000	0.000	0.000
42	A	52	ASN	0	-0.039	-0.016	31.761	0.217	0.217	0.000	0.000	0.000	0.000
43	A	53	TYR	0	-0.057	-0.053	28.554	0.330	0.330	0.000	0.000	0.000	0.000
44	A	54	SER	0	-0.005	0.006	32.998	0.054	0.054	0.000	0.000	0.000	0.000
45	A	55	PHE	0	0.041	0.011	28.780	0.010	0.010	0.000	0.000	0.000	0.000
46	A	56	SER	0	-0.011	-0.021	33.405	0.120	0.120	0.000	0.000	0.000	0.000
47	A	57	TYR	0	-0.070	-0.080	34.577	-0.197	-0.197	0.000	0.000	0.000	0.000
48	A	58	GLN	0	0.037	0.036	36.721	0.214	0.214	0.000	0.000	0.000	0.000
49	A	59	LEU	0	0.008	-0.025	36.712	-0.201	-0.201	0.000	0.000	0.000	0.000
50	A	60	GLU	-1	-0.887	-0.950	39.726	-6.641	-6.641	0.000	0.000	0.000	0.000
51	A	61	ASP	-1	-0.925	-0.957	42.462	-6.129	-6.129	0.000	0.000	0.000	0.000
52	A	62	GLU	-1	-0.984	-0.968	42.536	-6.691	-6.691	0.000	0.000	0.000	0.000
53	A	63	PRO	0	-0.061	-0.043	43.799	-0.044	-0.044	0.000	0.000	0.000	0.000
54	A	64	TRP	0	-0.051	-0.012	37.939	-0.223	-0.223	0.000	0.000	0.000	0.000
55	A	65	LYS	1	0.850	0.921	38.534	7.475	7.475	0.000	0.000	0.000	0.000
56	A	66	LEU	0	-0.035	-0.026	35.406	-0.114	-0.114	0.000	0.000	0.000	0.000
57	A	67	CYS	0	-0.011	0.018	24.697	0.097	0.097	0.000	0.000	0.000	0.000
58	A	68	ARG	1	0.943	0.968	30.643	9.182	9.182	0.000	0.000	0.000	0.000
59	A	69	LEU	0	0.004	0.011	27.655	-0.232	-0.232	0.000	0.000	0.000	0.000
60	A	70	HIS	0	-0.032	-0.013	24.618	0.284	0.284	0.000	0.000	0.000	0.000
61	A	71	GLN	0	0.054	0.015	22.715	0.348	0.348	0.000	0.000	0.000	0.000
62	A	72	ALA	0	-0.025	-0.001	18.341	-0.136	-0.136	0.000	0.000	0.000	0.000
63	A	73	PRO	0	0.015	0.010	15.933	0.169	0.169	0.000	0.000	0.000	0.000
64	A	74	THR	0	0.002	-0.030	14.032	-0.704	-0.704	0.000	0.000	0.000	0.000
65	A	75	ALA	0	0.000	-0.008	9.239	-0.134	-0.134	0.000	0.000	0.000	0.000
66	A	76	ARG	1	0.890	0.942	11.347	14.936	14.936	0.000	0.000	0.000	0.000
67	A	77	GLY	0	-0.015	-0.001	13.383	0.698	0.698	0.000	0.000	0.000	0.000
68	A	78	ALA	0	-0.049	-0.007	16.272	0.925	0.925	0.000	0.000	0.000	0.000
69	A	79	VAL	0	-0.006	0.010	17.715	-0.652	-0.652	0.000	0.000	0.000	0.000
70	A	80	ARG	1	0.873	0.925	14.381	16.122	16.122	0.000	0.000	0.000	0.000
71	A	81	PHE	0	-0.010	-0.010	20.853	-0.031	-0.031	0.000	0.000	0.000	0.000
72	A	82	TRP	0	0.027	0.002	21.588	0.003	0.003	0.000	0.000	0.000	0.000
73	A	84	SER	0	-0.007	0.002	25.673	-0.243	-0.243	0.000	0.000	0.000	0.000
74	A	85	LEU	0	0.001	-0.002	27.509	0.172	0.172	0.000	0.000	0.000	0.000
75	A	86	PRO	0	-0.025	-0.002	30.424	-0.173	-0.173	0.000	0.000	0.000	0.000
76	A	87	THR	0	0.079	0.024	31.737	0.122	0.122	0.000	0.000	0.000	0.000
77	A	88	ALA	0	-0.042	-0.018	33.362	0.045	0.045	0.000	0.000	0.000	0.000
78	A	89	ASP	-1	-0.788	-0.841	35.070	-7.453	-7.453	0.000	0.000	0.000	0.000
79	A	90	THR	0	-0.022	-0.036	30.839	-0.153	-0.153	0.000	0.000	0.000	0.000
80	A	91	SER	0	0.035	0.018	33.745	-0.055	-0.055	0.000	0.000	0.000	0.000
81	A	92	SER	0	-0.001	-0.017	33.260	-0.133	-0.133	0.000	0.000	0.000	0.000
82	A	93	PHE	0	-0.036	-0.017	34.874	-0.046	-0.046	0.000	0.000	0.000	0.000
83	A	94	VAL	0	-0.020	0.021	37.427	0.094	0.094	0.000	0.000	0.000	0.000
84	A	95	PRO	0	-0.035	-0.016	36.934	-0.190	-0.190	0.000	0.000	0.000	0.000
85	A	96	LEU	0	0.033	0.022	32.799	0.098	0.098	0.000	0.000	0.000	0.000
86	A	97	GLU	-1	-0.817	-0.893	35.284	-7.372	-7.372	0.000	0.000	0.000	0.000
87	A	98	LEU	0	-0.001	-0.008	30.412	-0.060	-0.060	0.000	0.000	0.000	0.000
88	A	99	ARG	1	0.805	0.873	34.482	7.495	7.495	0.000	0.000	0.000	0.000
89	A	100	VAL	0	0.024	0.026	30.480	-0.064	-0.064	0.000	0.000	0.000	0.000
90	A	101	THR	0	-0.001	-0.003	33.798	0.070	0.070	0.000	0.000	0.000	0.000
91	A	102	ALA	0	0.011	0.011	34.459	-0.171	-0.171	0.000	0.000	0.000	0.000
92	A	103	ALA	0	0.037	0.004	35.428	0.228	0.228	0.000	0.000	0.000	0.000
93	A	104	SER	0	-0.086	-0.034	37.801	0.168	0.168	0.000	0.000	0.000	0.000
94	A	105	GLY	0	0.005	0.001	39.652	0.159	0.159	0.000	0.000	0.000	0.000
95	A	106	ALA	0	-0.018	-0.004	37.630	0.033	0.033	0.000	0.000	0.000	0.000
96	A	107	PRO	0	0.027	0.004	36.860	-0.172	-0.172	0.000	0.000	0.000	0.000
97	A	108	ARG	1	0.764	0.861	27.429	10.043	10.043	0.000	0.000	0.000	0.000
98	A	109	TYR	0	-0.023	-0.016	26.869	-0.181	-0.181	0.000	0.000	0.000	0.000
99	A	110	HIS	0	-0.016	-0.010	32.817	0.332	0.332	0.000	0.000	0.000	0.000
100	A	111	ARG	1	0.828	0.896	26.641	9.594	9.594	0.000	0.000	0.000	0.000
101	A	112	VAL	0	0.026	0.017	33.457	0.032	0.032	0.000	0.000	0.000	0.000
102	A	113	ILE	0	-0.034	-0.015	29.519	-0.105	-0.105	0.000	0.000	0.000	0.000
103	A	114	HIS	0	0.063	0.036	32.341	0.068	0.068	0.000	0.000	0.000	0.000
104	A	115	ILE	0	0.047	0.025	29.546	-0.202	-0.202	0.000	0.000	0.000	0.000
105	A	116	ASN	0	-0.029	-0.023	29.379	-0.258	-0.258	0.000	0.000	0.000	0.000
106	A	117	GLU	-1	-0.904	-0.957	30.161	-8.394	-8.394	0.000	0.000	0.000	0.000
107	A	118	VAL	0	-0.086	-0.033	25.799	-0.227	-0.227	0.000	0.000	0.000	0.000
108	A	119	VAL	0	0.027	0.007	24.541	-0.250	-0.250	0.000	0.000	0.000	0.000
109	A	120	LEU	0	-0.078	-0.032	17.512	-0.186	-0.186	0.000	0.000	0.000	0.000
110	A	121	LEU	0	0.011	0.011	20.517	-0.218	-0.218	0.000	0.000	0.000	0.000
111	A	122	ASP	-1	-0.788	-0.859	17.882	-13.304	-13.304	0.000	0.000	0.000	0.000
112	A	123	ALA	0	-0.061	-0.041	15.042	0.353	0.353	0.000	0.000	0.000	0.000
113	A	124	PRO	0	-0.020	-0.014	17.155	0.243	0.243	0.000	0.000	0.000	0.000
114	A	125	VAL	0	0.022	0.007	17.803	-0.690	-0.690	0.000	0.000	0.000	0.000
115	A	126	GLY	0	-0.010	-0.008	19.745	0.423	0.423	0.000	0.000	0.000	0.000
116	A	127	LEU	0	-0.016	0.010	17.493	0.473	0.473	0.000	0.000	0.000	0.000
117	A	128	VAL	0	-0.023	-0.009	20.404	-0.327	-0.327	0.000	0.000	0.000	0.000
118	A	129	ALA	0	-0.011	-0.019	22.481	0.151	0.151	0.000	0.000	0.000	0.000
119	A	130	ARG	1	0.856	0.938	24.316	8.964	8.964	0.000	0.000	0.000	0.000
120	A	131	LEU	0	0.003	-0.006	27.633	-0.112	-0.112	0.000	0.000	0.000	0.000
121	A	132	ALA	0	-0.064	-0.023	30.358	0.097	0.097	0.000	0.000	0.000	0.000
122	A	133	ASP	-1	-0.907	-0.954	33.524	-8.064	-8.064	0.000	0.000	0.000	0.000
123	A	134	GLU	-1	-0.849	-0.904	36.493	-7.676	-7.676	0.000	0.000	0.000	0.000
124	A	135	SER	0	-0.084	-0.075	35.692	-0.155	-0.155	0.000	0.000	0.000	0.000
125	A	136	GLY	0	0.032	0.026	33.585	-0.047	-0.047	0.000	0.000	0.000	0.000
126	A	137	HIS	0	-0.034	-0.021	31.228	-0.445	-0.445	0.000	0.000	0.000	0.000
127	A	138	VAL	0	0.013	0.017	24.670	-0.048	-0.048	0.000	0.000	0.000	0.000
128	A	139	VAL	0	-0.051	-0.027	28.126	0.082	0.082	0.000	0.000	0.000	0.000
129	A	140	LEU	0	-0.027	-0.014	22.395	-0.224	-0.224	0.000	0.000	0.000	0.000
130	A	141	ARG	1	0.883	0.921	24.920	9.257	9.257	0.000	0.000	0.000	0.000
131	A	142	TRP	0	-0.005	0.005	22.185	-0.441	-0.441	0.000	0.000	0.000	0.000
132	A	143	LEU	0	-0.002	0.009	23.346	0.490	0.490	0.000	0.000	0.000	0.000
133	A	144	PRO	0	0.030	0.004	22.975	-0.380	-0.380	0.000	0.000	0.000	0.000
134	A	145	PRO	0	0.015	0.007	20.935	-0.075	-0.075	0.000	0.000	0.000	0.000
135	A	146	PRO	0	-0.007	-0.007	20.713	0.421	0.421	0.000	0.000	0.000	0.000
136	A	147	GLU	-1	-0.962	-0.980	23.633	-10.279	-10.279	0.000	0.000	0.000	0.000
137	A	148	THR	0	0.043	0.033	24.372	-0.027	-0.027	0.000	0.000	0.000	0.000
138	A	149	PRO	0	-0.017	-0.006	26.919	0.162	0.162	0.000	0.000	0.000	0.000
139	A	150	MET	0	0.008	-0.010	29.463	-0.066	-0.066	0.000	0.000	0.000	0.000
140	A	151	THR	0	0.091	0.033	28.146	0.029	0.029	0.000	0.000	0.000	0.000
141	A	152	SER	0	-0.058	-0.035	29.631	-0.165	-0.165	0.000	0.000	0.000	0.000
142	A	153	HIS	0	0.035	0.015	31.225	0.081	0.081	0.000	0.000	0.000	0.000
143	A	154	ILE	0	0.005	0.015	24.809	-0.099	-0.099	0.000	0.000	0.000	0.000
144	A	155	ARG	1	0.833	0.914	26.326	9.371	9.371	0.000	0.000	0.000	0.000
145	A	156	TYR	0	0.002	-0.019	22.329	-0.462	-0.462	0.000	0.000	0.000	0.000
146	A	157	GLU	-1	-0.789	-0.879	19.693	-11.882	-11.882	0.000	0.000	0.000	0.000
147	A	158	VAL	0	-0.015	-0.008	20.097	-0.455	-0.455	0.000	0.000	0.000	0.000
148	A	159	ASP	-1	-0.844	-0.894	16.437	-14.123	-14.123	0.000	0.000	0.000	0.000
149	A	160	VAL	0	-0.016	-0.013	18.433	-0.148	-0.148	0.000	0.000	0.000	0.000
150	A	161	SER	0	0.043	0.027	16.001	-0.170	-0.170	0.000	0.000	0.000	0.000
151	A	162	ALA	0	0.005	-0.016	18.093	0.166	0.166	0.000	0.000	0.000	0.000
152	A	163	GLY	0	-0.009	-0.008	17.624	-0.391	-0.391	0.000	0.000	0.000	0.000
153	A	164	ASN	0	-0.054	-0.055	18.646	0.057	0.057	0.000	0.000	0.000	0.000
154	A	165	GLY	0	0.038	0.030	21.213	0.063	0.063	0.000	0.000	0.000	0.000
155	A	166	ALA	0	0.011	0.024	18.873	0.219	0.219	0.000	0.000	0.000	0.000
156	A	167	GLY	0	-0.014	-0.020	19.907	0.537	0.537	0.000	0.000	0.000	0.000
157	A	168	SER	0	-0.059	-0.019	21.639	-0.043	-0.043	0.000	0.000	0.000	0.000
158	A	169	VAL	0	0.037	0.014	19.785	-0.278	-0.278	0.000	0.000	0.000	0.000
159	A	170	GLN	0	0.019	0.017	20.951	0.480	0.480	0.000	0.000	0.000	0.000
160	A	171	ARG	1	0.817	0.881	15.339	13.398	13.398	0.000	0.000	0.000	0.000
161	A	172	VAL	0	-0.024	0.002	22.485	0.354	0.354	0.000	0.000	0.000	0.000
162	A	173	GLU	-1	-0.853	-0.914	24.308	-9.541	-9.541	0.000	0.000	0.000	0.000
163	A	174	ILE	0	-0.065	-0.036	25.207	0.210	0.210	0.000	0.000	0.000	0.000
164	A	175	LEU	0	0.030	0.008	27.793	-0.037	-0.037	0.000	0.000	0.000	0.000
165	A	176	GLU	-1	-0.816	-0.918	29.318	-8.417	-8.417	0.000	0.000	0.000	0.000
166	A	177	GLY	0	-0.034	0.001	29.531	0.313	0.313	0.000	0.000	0.000	0.000
167	A	178	ARG	1	0.785	0.892	30.425	8.058	8.058	0.000	0.000	0.000	0.000
168	A	179	THR	0	0.000	-0.005	26.292	-0.074	-0.074	0.000	0.000	0.000	0.000
169	A	180	GLU	-1	-0.769	-0.881	27.137	-8.964	-8.964	0.000	0.000	0.000	0.000
170	A	181	CYS	0	-0.025	-0.013	25.831	0.113	0.113	0.000	0.000	0.000	0.000
171	A	182	VAL	0	-0.013	0.016	27.497	-0.202	-0.202	0.000	0.000	0.000	0.000
172	A	183	LEU	0	-0.006	0.000	24.033	0.089	0.089	0.000	0.000	0.000	0.000
173	A	184	SER	0	0.035	-0.004	28.709	0.004	0.004	0.000	0.000	0.000	0.000
174	A	185	ASN	0	-0.038	-0.005	27.609	0.085	0.085	0.000	0.000	0.000	0.000
175	A	186	LEU	0	-0.012	-0.001	25.146	-0.204	-0.204	0.000	0.000	0.000	0.000
176	A	187	ARG	1	0.957	0.984	24.556	11.434	11.434	0.000	0.000	0.000	0.000
177	A	188	GLY	0	0.101	0.061	28.339	-0.202	-0.202	0.000	0.000	0.000	0.000
178	A	189	ARG	1	0.907	0.955	28.551	9.370	9.370	0.000	0.000	0.000	0.000
179	A	190	THR	0	-0.062	-0.031	23.577	-0.274	-0.274	0.000	0.000	0.000	0.000
180	A	191	ARG	1	0.922	0.975	17.457	14.645	14.645	0.000	0.000	0.000	0.000
181	A	192	TYR	0	0.017	0.006	20.172	-0.236	-0.236	0.000	0.000	0.000	0.000
182	A	193	THR	0	-0.014	-0.008	13.929	0.174	0.174	0.000	0.000	0.000	0.000
183	A	194	PHE	0	0.030	0.017	17.335	0.219	0.219	0.000	0.000	0.000	0.000
184	A	195	ALA	0	0.056	0.013	14.446	-0.544	-0.544	0.000	0.000	0.000	0.000
185	A	196	VAL	0	-0.012	0.006	16.436	0.274	0.274	0.000	0.000	0.000	0.000
186	A	197	ARG	1	0.820	0.893	16.490	12.396	12.396	0.000	0.000	0.000	0.000
187	A	198	ALA	0	0.034	-0.003	18.514	0.512	0.512	0.000	0.000	0.000	0.000
188	A	199	ARG	1	0.842	0.905	21.034	9.518	9.518	0.000	0.000	0.000	0.000
189	A	200	MET	0	0.011	0.023	23.798	0.296	0.296	0.000	0.000	0.000	0.000
190	A	201	ALA	0	-0.009	0.001	27.127	-0.054	-0.054	0.000	0.000	0.000	0.000
191	A	202	GLU	-1	-0.731	-0.820	29.439	-8.965	-8.965	0.000	0.000	0.000	0.000
192	A	203	PRO	0	-0.058	-0.052	32.915	0.063	0.063	0.000	0.000	0.000	0.000
193	A	204	SER	0	-0.010	-0.012	34.898	0.024	0.024	0.000	0.000	0.000	0.000
194	A	205	PHE	0	0.007	0.002	29.884	0.013	0.013	0.000	0.000	0.000	0.000
195	A	206	GLY	0	0.069	0.046	28.898	0.077	0.077	0.000	0.000	0.000	0.000
196	A	207	GLY	0	-0.003	0.004	25.364	-0.062	-0.062	0.000	0.000	0.000	0.000
197	A	208	PHE	0	-0.070	-0.037	20.310	-0.076	-0.076	0.000	0.000	0.000	0.000
198	A	209	TRP	0	-0.047	-0.017	18.751	0.008	0.008	0.000	0.000	0.000	0.000
199	A	210	SER	0	0.058	0.032	17.063	-0.172	-0.172	0.000	0.000	0.000	0.000
200	A	211	ALA	0	-0.041	-0.015	12.041	-0.299	-0.299	0.000	0.000	0.000	0.000
201	A	212	TRP	0	-0.001	-0.020	11.372	0.792	0.792	0.000	0.000	0.000	0.000
202	A	213	SER	0	0.038	0.029	12.925	-0.285	-0.285	0.000	0.000	0.000	0.000
203	A	214	GLU	-1	-0.948	-0.969	11.088	-19.562	-19.562	0.000	0.000	0.000	0.000
204	A	215	PRO	0	-0.027	-0.019	11.348	0.871	0.871	0.000	0.000	0.000	0.000
205	A	216	VAL	0	0.004	0.008	14.366	0.037	0.037	0.000	0.000	0.000	0.000
206	A	217	SER	0	-0.055	-0.041	16.464	-0.232	-0.232	0.000	0.000	0.000	0.000
207	A	218	LEU	0	-0.018	-0.008	18.460	0.190	0.190	0.000	0.000	0.000	0.000
208	A	219	LEU	0	-0.043	-0.030	22.166	-0.189	-0.189	0.000	0.000	0.000	0.000
209	A	220	THR	0	0.041	0.019	24.839	0.117	0.117	0.000	0.000	0.000	0.000
210	A	221	PRO	0	0.053	0.017	27.853	-0.084	-0.084	0.000	0.000	0.000	0.000
211	A	222	SER	0	-0.097	-0.084	31.372	-0.211	-0.211	0.000	0.000	0.000	0.000
212	A	223	ASP	-1	-0.892	-0.932	33.052	-8.241	-8.241	0.000	0.000	0.000	0.000
213	A	224	LEU	0	0.013	0.028	33.229	0.111	0.111	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:10:LYS)