A32	19.761	50.897	8.744	LEU
A33	16.42	49.451	7.555	PRO
A34	13.951	52.029	6.331	GLU
A35	10.37	52.139	5.24	GLY
A36	7.048	51.192	6.721	LYS
A37	5.224	47.986	5.715	ILE
A38	1.994	48.944	4.001	MET
A39	-0.996	46.863	5.144	PRO
A40	-3.13	44.966	2.661	ASN
A41	-0.767	45.766	-0.197	THR
A42	1.463	43.461	-2.271	VAL
A43	4.59	44.461	-4.206	PHE
A44	4.505	42.958	-7.706	VAL
A45	7.817	42.964	-9.536	GLY
A46	8.968	41.469	-12.774	GLY
A47	6.132	43.141	-14.69	ILE
A48	7.032	42.579	-18.372	ASP
A49	6.072	44.801	-21.313	VAL
A50	3.847	41.95	-22.721	ARG
A51	1.707	42.093	-19.538	MET
A52	-1.204	44.435	-18.673	ASP
A53	-2.783	45.949	-15.527	GLU
A54	-6.136	44.311	-16.281	THR
A55	-4.937	40.704	-16.074	GLU
A56	-3.138	41.479	-12.801	ILE
A57	-6.284	43.131	-11.429	ARG
A58	-8.482	40.194	-12.508	SER
A59	-6.116	37.658	-10.952	PHE
A60	-5.77	39.369	-7.609	PHE
A61	-9.568	39.532	-7.249	ALA
A62	-9.294	35.909	-5.991	ARG
A63	-8.012	37.413	-2.701	TYR
A64	-10.431	40.282	-2.266	GLY
A65	-11.752	43.579	-3.552	SER
A66	-8.849	45.219	-5.337	VAL
A67	-8.503	48.916	-4.534	LYS
A68	-5.641	49.784	-6.898	GLU
A69	-3.159	48.153	-9.303	VAL
A70	-0.507	50.887	-9.437	LYS
A71	2.432	50.455	-11.816	ILE
A72	5.407	52.681	-11.022	ILE
A73	6.727	54.843	-13.914	THR
A74	9.528	57.341	-14.374	ASP
A75	8.854	60.991	-15.124	ARG
A76	8.605	60.26	-18.856	THR
A77	5.929	57.634	-18.329	GLY
A78	8.293	54.631	-18.785	VAL
A79	7.42	51.649	-16.551	SER
A80	9.927	50.672	-13.917	LYS
A81	8.675	47.094	-14.208	GLY
A82	7.007	46.861	-10.778	TYR
A83	3.864	47.967	-9.028	GLY
A84	1.531	47.488	-6.088	PHE
A85	-1.82	45.782	-5.611	VAL
A86	-3.853	47.031	-2.652	SER
A87	-7.123	45.712	-1.173	PHE
A88	-10.187	47.109	0.554	TYR
A89	-10.455	43.969	2.648	ASN
A90	-7.854	42.553	5.047	ASP
A91	-5.655	40.057	3.245	VAL
A92	-2.85	37.827	4.502	ASP
A93	0.032	39.343	2.519	VAL
A94	2.411	36.604	3.733	GLN
A95	0.19	33.974	2.131	LYS
A96	-0.371	35.958	-1.081	ILE
A97	3.351	36.37	-1.669	VAL
A98	3.727	32.567	-1.717	GLU
A99	1.654	32.402	-4.914	SER
A100	3.206	31.336	-8.212	GLN
A101	1.573	33.775	-10.628	ILE
A102	2.706	33.669	-14.271	ASN
A103	1.773	35.92	-17.199	PHE
A104	3.257	35.943	-20.734	HIS
A105	5.964	33.401	-19.875	GLY
A106	7.23	35.263	-16.801	LYS
A107	6.725	34.652	-13.049	LYS
A108	5.738	37.648	-10.947	LEU
A109	8.129	38.568	-8.158	LYS
A110	6.055	39.157	-5.048	LEU
A111	6.827	40.701	-1.666	GLY
A112	5.411	42.736	1.233	PRO
A113	5.002	46.408	0.188	ALA
A114	7.422	48.843	1.854	ILE
A115	7.062	52.66	1.539	ARG
A116	10.16	54.684	2.134	LYS
A117	10.169	58.491	2.6	GLN
A123	5.856	66.272	-7.953	HIS