A0	8.564	12.943	57.313	SER
A1	11.74	11.913	55.561	LEU
A2	11.363	9.434	52.628	ASN
A3	13.463	6.294	51.936	ALA
A4	14.169	3.629	49.383	ILE
A5	15.171	0.164	50.664	ILE
A6	17.517	-1.763	48.324	ILE
A7	17.87	-5.28	49.757	ASP
A8	16.885	-8.724	48.471	ASP
A9	16.812	-10.497	51.831	HIS
A10	13.213	-11.189	52.953	PRO
A11	13.803	-11.052	56.725	LEU
A12	15.85	-7.868	56.663	ALA
A13	13.43	-6.188	54.256	ILE
A14	10.618	-6.638	56.742	ALA
A15	12.751	-5.595	59.741	ALA
A16	14.028	-2.452	58.039	ILE
A17	10.551	-1.477	56.756	ARG
A18	9.079	-1.857	60.262	ASN
A19	11.974	0.127	61.749	LEU
A20	11.516	3.043	59.344	LEU
A21	7.707	3.226	59.779	ILE
A22	8.107	3.176	63.622	LYS
A23	10.47	6.161	63.232	ASN
A24	8.262	8.357	61.027	ASP
A25	10.121	7.633	57.794	ILE
A26	8.046	6.846	54.712	GLU
A27	9.086	4.174	52.203	ILE
A28	8.824	5.273	48.585	LEU
A29	10.007	2.04	47.032	ALA
A30	11.602	-1.266	47.832	GLU
A31	14.089	-2.709	45.3	LEU
A32	15.539	-6.22	45.221	THR
A33	18.263	-5.621	42.622	GLU
A34	20.72	-2.886	41.727	GLY
A35	19.959	-2.564	37.987	GLY
A36	17.072	-0.117	38.482	SER
A37	18.393	1.619	41.612	ALA
A38	20.035	4.781	40.212	VAL
A39	16.974	5.482	38.029	GLN
A40	14.457	4.859	40.865	ARG
A41	16.443	7.133	43.203	VAL
A42	16.71	9.843	40.575	GLU
A43	12.999	9.706	39.81	THR
A44	11.572	9.292	43.337	LEU
A45	14.038	11.598	45.04	LYS
A46	14.228	9.902	48.521	PRO
A47	16.067	11.522	51.409	ASP
A48	17.512	8.129	52.459	ILE
A49	18.696	5.126	50.49	VAL
A50	19.571	1.915	52.364	ILE
A51	21.734	-0.4	50.246	ILE
A52	22.585	-3.98	51.111	ASP
A53	26.134	-4.843	50.02	VAL
A54	25.04	-8.128	48.44	ASP
A55	22.251	-6.754	46.213	ILE
A56	22.214	-8.717	42.888	PRO
A57	22.626	-6.941	39.52	GLY
A58	24.632	-3.733	39.715	VAL
A59	26.553	-4.156	42.912	ASN
A60	25.701	-2.265	46.104	GLY
A61	28.892	-0.254	46.329	ILE
A62	28.694	0.541	42.594	GLN
A63	25.2	1.918	43.164	VAL
A64	26.622	4.148	45.948	LEU
A65	29.443	5.303	43.691	GLU
A66	27.203	6.031	40.738	THR
A67	24.714	7.979	42.907	LEU
A68	27.465	10.2	44.246	ARG
A69	28.959	10.642	40.766	LYS
A70	25.469	11.752	39.636	ARG
A71	25.352	14.3	42.505	GLN
A72	22.775	12.595	44.718	TYR
A73	22.976	14.573	47.969	SER
A74	20.866	12.439	50.274	GLY
A75	21.722	9.982	53.027	ILE
A76	23.122	6.612	51.941	ILE
A77	23.535	3.843	54.559	ILE
A78	25.175	0.617	53.461	ILE
A79	24.063	-2.531	55.307	VAL
A80	25.668	-5.961	55.483	SER
A81	24.481	-9.3	56.877	ALA
A82	27.829	-9.516	58.744	LYS
A86	36.525	-4.239	57.624	PHE
A87	34.527	-3.041	54.544	TYR
A88	33.249	0.102	56.297	GLY
A89	36.38	2.034	55.281	LYS
A90	35.794	1.45	51.573	HIS
A91	32.159	2.601	51.921	CYS
A92	33.319	5.736	53.756	ALA
A93	35.818	6.498	50.992	ASP
A94	33.067	5.997	48.417	ALA
A95	30.889	8.631	50.127	GLY
A96	28.376	6.643	52.176	ALA
A97	26.994	8.297	55.331	ASN
A98	27.208	5.004	57.235	GLY
A99	27.845	1.292	57.13	PHE
A100	25.927	-0.956	59.542	VAL
A101	26.132	-4.661	60.224	SER
A102	22.583	-6.132	60.393	LYS
A103	23.658	-8.939	62.768	LYS
A104	23.635	-6.602	65.787	GLU
A105	20.036	-5.493	65.097	GLY
A106	18.066	-2.552	63.806	MET
A107	18.974	0.025	66.42	ASN
A108	22.212	0.718	64.537	ASN
A109	20.459	1.593	61.23	ILE
A110	18.268	4.222	62.885	ILE
A111	21.33	5.559	64.817	ALA
A112	23.174	5.861	61.52	ALA
A113	20.285	7.776	59.911	ILE
A114	20.129	10.088	62.947	GLU
A115	23.87	10.648	62.804	ALA
A116	23.585	11.47	59.108	ALA
A117	20.709	13.929	59.578	LYS
A118	22.896	15.687	62.153	ASN
A119	25.831	15.979	59.739	GLY
A120	27.843	13.011	61.011	TYR
A121	28.782	9.583	59.703	CYS
A122	28.395	6.232	61.434	TYR
A123	30.989	3.511	60.581	PHE
A124	32.502	0.521	62.373	PRO
A125	35.432	1.307	64.692	PHE
A126	38.477	-0.935	65.054	SER
A127	40.77	-0.167	67.932	LEU
A128	43.374	-2.677	66.667	ASN
A129	44.509	-0.154	64.017	ARG
A130	45.695	2.093	66.874	PHE
A131	46.285	-0.134	69.987	VAL