A1	30.55	32.623	6.46	ASN
A2	31.866	36.144	5.858	GLY
A3	30.895	39.819	5.712	ARG
A4	28.343	40.73	3.055	THR
A5	27.377	44.156	1.787	PRO
A6	24.277	43.954	3.981	LEU
A7	26.478	43.604	7.104	HIS
A8	28.281	46.795	6.149	LEU
A9	25.156	48.749	5.374	ALA
A10	23.545	47.567	8.623	ALA
A11	26.59	48.353	10.724	ARG
A12	26.685	51.916	9.365	ASN
A13	22.968	52.521	9.529	GLY
A14	22.78	53.12	5.775	HIS
A15	19.061	52.778	5.508	LEU
A16	18.761	53.108	1.758	GLU
A17	21.5	50.55	0.991	VAL
A18	19.943	48.164	3.515	VAL
A19	16.565	48.592	1.764	LYS
A20	18.013	48.061	-1.678	LEU
A21	19.957	44.976	-0.623	LEU
A22	16.865	43.448	1.0	LEU
A23	14.768	44.152	-2.129	GLU
A24	17.488	42.603	-4.241	ALA
A25	17.248	39.414	-2.181	GLY
A26	20.253	39.621	0.132	ALA
A27	20.215	36.998	2.921	ASP
A28	18.945	38.891	5.957	VAL
A29	20.443	36.274	8.265	ASN
A30	23.905	35.896	6.686	ALA
A31	26.63	35.368	9.317	LYS
A32	30.024	37.047	9.275	ASP
A33	33.216	35.374	10.539	LYS
A34	32.222	36.233	14.116	ASN
A35	28.776	34.676	13.712	GLY
A36	27.02	38.087	13.572	ARG
A37	24.035	38.731	11.363	THR
A38	23.258	42.207	10.027	PRO
A39	20.755	42.563	12.913	LEU
A40	23.533	42.038	15.463	HIS
A41	25.527	44.842	13.895	LEU
A42	22.608	47.249	13.623	ALA
A43	21.605	46.483	17.204	ALA
A44	25.182	46.912	18.519	ARG
A45	25.437	50.311	16.869	ASN
A46	21.969	51.567	17.855	GLY
A47	20.387	51.836	14.429	HIS
A48	16.741	51.704	15.337	LEU
A49	15.333	52.163	11.842	GLU
A50	17.636	49.571	10.348	VAL
A51	16.692	47.188	13.123	VAL
A52	13.017	47.63	12.254	LYS
A53	13.7	47.117	8.531	LEU
A54	15.729	43.967	9.107	LEU
A55	13.075	42.585	11.47	LEU
A56	10.355	43.388	8.891	GLU
A57	12.422	41.504	6.331	ALA
A58	12.668	38.317	8.383	GLY
A59	15.722	38.76	10.551	ALA
A60	16.067	36.158	13.284	ASP
A61	15.652	38.233	16.412	VAL
A62	17.466	35.595	18.512	ASN
A63	20.398	34.715	16.228	ALA
A64	23.48	33.827	18.294	LYS
A65	27.018	34.831	17.362	ASP
A66	30.23	32.958	18.277	LYS
A67	30.115	34.296	21.805	ASN
A68	26.556	32.994	22.071	GLY
A69	25.276	36.571	22.081	ARG
A70	21.973	37.677	20.496	THR
A71	21.18	41.119	19.074	PRO
A72	19.556	41.927	22.434	LEU
A73	22.852	41.106	24.219	HIS
A74	24.695	43.549	21.968	LEU
A75	22.089	46.332	22.183	ALA
A76	22.086	45.923	25.965	ALA
A77	25.868	45.882	26.222	ARG
A78	25.99	49.131	24.307	ASN
A79	23.128	50.795	26.206	GLY
A80	20.765	51.304	23.274	HIS
A81	17.468	51.683	25.126	LEU
A82	15.229	52.194	22.07	GLU
A83	16.731	49.227	20.273	VAL
A84	16.37	47.101	23.386	VAL
A85	12.698	48.057	23.557	LYS
A86	12.1	47.186	19.909	LEU
A87	13.897	43.861	20.195	LEU
A88	11.808	42.803	23.237	LEU
A89	8.607	43.725	21.38	GLU
A90	9.812	41.698	18.385	ALA
A91	10.182	38.666	20.662	GLY
A92	13.767	38.726	21.812	ALA
A93	14.646	36.207	24.529	ASP
A94	15.175	38.375	27.62	VAL
A95	16.885	35.472	29.387	ASN
A96	19.17	34.349	26.583	ALA
A97	22.459	33.139	28.01	LYS
A98	25.729	33.664	26.189	ASP
A99	28.941	31.559	26.335	LYS
A100	29.531	32.639	29.923	ASN
A101	25.938	32.155	31.007	GLY
A102	25.344	35.912	30.927	ARG
A103	21.998	37.474	29.978	THR
A104	21.52	40.851	28.288	PRO
A105	20.866	42.278	31.75	LEU
A106	24.367	41.254	32.894	HIS
A107	26.091	42.9	29.955	LEU
A108	24.128	46.111	30.367	ALA
A109	25.002	46.232	34.06	ALA
A110	28.674	45.59	33.481	ARG
A111	28.782	48.529	31.123	ASN
A112	26.943	51.0	33.295	GLY
A113	23.648	51.024	31.474	HIS
A114	21.297	51.562	34.369	LEU
A115	18.208	52.491	32.406	GLU
A116	18.563	49.367	30.25	VAL
A117	19.071	47.286	33.397	VAL
A118	15.921	48.699	34.939	LYS
A119	13.951	48.03	31.734	LEU
A120	15.21	44.447	31.486	LEU
A121	14.465	43.708	35.164	LEU
A122	11.007	45.049	34.375	GLU
A123	10.551	42.966	31.204	ALA
A124	11.637	39.727	32.852	GLY
A125	10.222	40.137	36.354	ALA
A126	7.344	37.767	35.649	TYR