A1	-1.385	3.684	30.754	SER
A2	0.99	0.811	31.6	VAL
A3	3.934	2.646	33.225	ILE
A4	7.451	1.382	32.38	GLU
A5	8.887	0.38	35.744	ILE
A6	12.65	0.613	36.225	ASN
A7	14.973	0.66	39.237	ASP
A8	14.803	4.47	39.366	GLU
A9	11.053	5.028	39.389	ASN
A10	10.262	1.798	41.27	PHE
A11	9.756	3.158	44.784	ASP
A12	8.098	6.207	43.256	GLU
A13	5.34	4.007	41.759	VAL
A14	5.148	1.129	44.257	ILE
A15	5.887	2.497	47.749	LYS
A16	4.134	5.843	47.257	LYS
A17	0.676	4.741	46.098	SER
A18	-2.355	3.669	48.129	ASP
A19	-3.874	1.977	45.041	LYS
A20	-3.218	-1.6	43.949	VAL
A21	-0.278	-1.885	41.578	VAL
A22	-0.401	-4.747	39.079	VAL
A23	3.117	-5.5	37.816	VAL
A24	3.818	-7.517	34.669	ASP
A25	7.135	-9.266	34.275	PHE
A26	8.025	-9.83	30.654	TRP
A27	10.787	-10.07	28.051	ALA
A28	10.865	-9.647	24.276	GLU
A29	11.665	-13.332	23.641	TRP
A30	8.697	-14.641	25.598	CYS
A31	5.772	-15.73	23.45	GLY
A32	3.3	-16.402	26.294	PRO
A33	3.967	-12.833	27.434	CYS
A34	2.517	-11.591	24.14	ARG
A35	-0.853	-13.008	25.249	MET
A36	-0.856	-10.875	28.423	ILE
A37	0.52	-7.607	26.917	ALA
A38	-2.695	-6.502	25.172	PRO
A39	-4.903	-7.558	28.122	ILE
A40	-2.956	-5.632	30.773	ILE
A41	-3.265	-2.644	28.44	GLU
A42	-7.049	-3.13	28.133	GLU
A43	-7.572	-3.407	31.884	LEU
A44	-5.534	-0.223	32.36	ALA
A45	-8.367	1.386	30.315	GLU
A46	-11.303	-0.271	32.094	GLU
A47	-9.965	0.884	35.507	TYR
A48	-9.945	4.67	35.188	ALA
A49	-6.865	5.265	37.325	GLY
A50	-8.45	3.012	39.934	LYS
A51	-5.59	0.5	39.696	VAL
A52	-2.067	1.259	38.526	VAL
A53	-0.564	-1.035	35.87	PHE
A54	3.172	-1.386	35.335	GLY
A55	5.695	-3.378	33.332	LYS
A56	9.1	-4.74	34.282	VAL
A57	11.454	-6.048	31.572	ASN
A58	13.299	-8.887	33.292	VAL
A59	16.207	-8.571	30.89	ASP
A60	16.788	-4.848	31.537	GLU
A61	16.127	-5.362	35.247	ASN
A62	17.264	-8.921	36.146	PRO
A63	17.893	-7.949	39.78	GLU
A64	14.393	-6.713	40.687	ILE
A65	13.028	-9.97	39.311	ALA
A66	15.517	-11.58	41.644	ALA
A67	14.273	-9.706	44.711	LYS
A68	10.655	-10.915	44.382	TYR
A69	11.623	-14.41	43.278	GLY
A70	10.337	-14.396	39.722	ILE
A71	11.259	-17.915	38.594	MET
A72	9.487	-17.726	35.213	SER
A73	7.556	-15.392	32.901	ILE
A74	4.886	-14.263	32.376	PRO
A75	3.993	-13.51	35.989	THR
A76	1.831	-10.788	37.543	LEU
A77	2.503	-9.438	41.062	LEU
A78	-0.159	-7.476	42.958	PHE
A79	1.394	-4.814	45.185	PHE
A80	-0.498	-3.112	47.999	LYS
A81	1.205	-0.595	50.285	ASN
A82	4.678	-1.508	49.021	GLY
A83	4.372	-5.221	49.786	LYS
A84	3.383	-8.124	47.53	VAL
A85	-0.148	-9.376	48.286	VAL
A86	-0.729	-11.71	45.306	ASP
A87	1.076	-13.605	42.532	GLN
A88	-0.251	-14.975	39.23	LEU
A89	2.034	-17.288	37.271	VAL
A90	1.23	-17.982	33.62	GLY
A91	-1.158	-16.322	31.146	ALA
A92	-4.847	-16.25	32.131	ARG
A93	-8.103	-15.011	30.469	PRO
A94	-9.018	-11.313	30.872	LYS
A95	-12.037	-12.3	32.97	GLU
A96	-9.979	-14.35	35.399	ALA
A97	-7.603	-11.411	35.992	LEU
A98	-10.55	-9.113	36.71	LYS
A99	-11.714	-11.711	39.267	GLU
A100	-8.474	-11.589	41.266	ARG
A101	-8.211	-7.837	41.042	ILE
A102	-11.636	-7.046	42.526	LYS
A103	-10.616	-8.567	45.867	LYS
A104	-7.976	-5.858	46.369	TYR
A105	-9.961	-2.793	45.217	LEU