A1	12.856	16.686	32.935	ALA
A2	10.382	15.331	30.396	LEU
A3	8.056	18.355	30.328	TRP
A4	10.892	20.697	29.229	GLN
A5	12.322	18.199	26.691	PHE
A6	8.947	17.658	25.007	ASN
A7	8.614	21.495	24.872	GLY
A8	12.034	21.83	23.208	MET
A9	11.154	19.281	20.477	ILE
A10	7.919	21.205	19.825	LYS
A11	9.946	24.434	19.651	CYS
A12	12.106	22.986	16.832	LYS
A13	9.391	20.83	15.167	ILE
A14	6.135	22.713	15.743	PRO
A15	4.1	20.173	13.771	SER
A16	4.991	17.308	16.155	SER
A17	3.413	15.744	19.214	GLU
A18	6.685	14.342	20.591	PRO
A19	5.224	11.816	23.027	LEU
A20	3.417	10.183	20.133	LEU
A21	5.947	10.721	17.294	ASP
A22	9.359	10.225	19.064	PHE
A23	8.59	7.704	21.713	ASN
A24	9.416	4.139	20.837	ASN
A25	11.269	4.773	17.564	TYR
A26	14.269	2.65	16.563	GLY
A27	16.555	1.074	19.127	CYS
A28	17.25	4.166	21.231	TYR
A29	14.308	6.59	21.179	CYS
A30	12.376	5.553	24.25	GLY
A31	13.113	3.558	27.401	LEU
A32	16.46	1.832	27.113	GLY
A33	18.582	1.708	24.014	GLY
A34	20.907	-1.052	22.845	SER
A35	22.366	-2.408	19.645	GLY
A36	23.187	-0.508	16.48	THR
A37	20.967	2.523	15.838	PRO
A38	18.732	1.877	12.829	VAL
A39	18.979	5.382	11.313	ASP
A40	20.132	8.951	11.922	ASP
A41	17.134	9.804	14.083	LEU
A42	17.978	6.7	16.218	ASP
A43	21.605	7.98	16.422	ARG
A44	20.193	11.28	17.741	CYS
A45	18.545	9.301	20.505	CYS
A46	21.665	7.221	21.089	GLN
A47	23.724	10.403	21.569	THR
A48	21.032	11.75	23.903	HIS
A49	21.013	8.57	26.015	ASP
A50	24.837	8.775	26.28	ASN
A51	24.531	12.445	27.292	CYS
A52	22.349	11.498	30.287	TYR
A53	24.816	8.779	31.409	LYS
A54	27.565	11.336	31.224	GLN
A55	25.635	13.889	33.247	ALA
A56	25.381	11.307	35.966	LYS
A57	29.181	11.31	36.289	LYS
A58	29.446	15.11	36.775	LEU
A59	30.569	16.065	40.302	ASP
A60	28.02	18.88	40.244	SER
A61	25.153	16.515	39.509	CYS
A62	26.33	13.891	41.994	LYS
A63	26.631	16.279	44.926	VAL
A64	23.17	17.694	44.062	LEU
A65	21.931	14.024	43.945	VAL
A66	20.338	14.789	40.617	ASP
A67	18.36	12.636	38.222	ASN
A68	18.571	13.808	34.552	PRO
A69	15.032	12.512	34.098	TYR
A70	13.752	14.871	36.853	THR
A71	16.18	17.796	36.351	ASN
A72	14.381	21.121	36.663	ASN
A73	16.482	23.379	34.363	TYR
A74	14.918	26.408	32.666	SER
A75	14.752	27.049	28.931	TYR
A76	12.97	29.402	26.53	SER
A77	11.639	29.073	22.979	CYS
A78	11.289	32.037	20.623	SER
A79	11.168	31.921	16.836	ASN
A80	11.775	28.149	16.946	ASN
A81	15.102	28.637	18.718	GLU
A82	15.897	27.138	22.09	ILE
A83	17.884	28.942	24.717	THR
A84	18.967	27.266	27.924	CYS
A85	18.805	29.718	30.824	SER
A86	21.922	31.414	32.083	SER
A87	20.518	31.015	35.563	GLU
A88	20.964	27.211	35.285	ASN
A89	23.567	25.696	37.612	ASN
A90	26.375	23.593	36.181	ALA
A91	24.418	20.293	36.31	CYS
A92	21.117	21.76	35.115	GLU
A93	22.978	23.471	32.334	ALA
A94	24.578	20.185	31.245	PHE
A95	21.131	18.425	31.075	ILE
A96	19.558	21.328	29.224	CYS
A97	22.295	21.156	26.574	ASN
A98	21.805	17.353	26.183	CYS
A99	18.081	18.05	25.568	ASP
A100	18.744	21.036	23.28	ARG
A101	21.249	19.143	21.097	ASN
A102	18.82	16.231	20.695	ALA
A103	15.889	18.457	19.762	ALA
A104	18.0	20.133	17.081	ILE
A105	19.252	16.761	15.898	CYS
A106	15.661	15.473	15.64	PHE
A107	14.783	18.475	13.492	SER
A108	17.657	17.916	11.062	LYS
A109	17.228	14.234	10.18	VAL
A110	14.737	12.203	8.188	PRO
A111	11.911	10.315	9.942	TYR
A112	11.506	6.699	8.752	ASN
A113	8.093	5.552	9.903	LYS
A114	9.077	1.962	9.281	GLU
A115	11.371	2.296	12.31	HIS
A116	8.591	3.282	14.684	LYS
A117	7.77	0.612	17.301	ASN
A118	10.671	-1.615	16.216	LEU
A119	10.868	-5.12	17.697	ASP
A120	13.872	-4.918	20.073	LYS
A121	14.963	-8.204	18.735	LYS
A122	16.473	-6.186	15.874	ASN
A123	18.637	-4.346	18.436	CYS