A-1	58.742	-5.994	18.707	SER
A0	59.356	-3.337	21.377	HIS
A1	59.825	0.4	21.406	MET
A2	62.216	2.559	23.347	THR
A3	61.056	5.566	25.341	MET
A4	62.588	7.775	22.61	GLU
A5	60.558	6.027	19.935	GLN
A6	57.419	6.208	22.077	PHE
A7	57.691	9.961	22.619	LEU
A8	58.113	10.584	18.899	THR
A9	55.3	8.148	18.041	SER
A10	52.876	10.448	19.854	LEU
A11	53.396	13.125	17.21	ASP
A12	53.168	10.687	14.307	MET
A13	49.899	9.263	15.655	ILE
A14	48.46	12.74	16.156	ARG
A15	49.343	13.638	12.559	SER
A16	47.069	10.882	11.242	GLY
A17	44.04	12.047	13.24	CYS
A18	44.149	15.777	13.989	ALA
A19	43.48	16.839	10.359	PRO
A20	40.12	15.041	10.379	LYS
A21	38.808	17.381	13.111	PHE
A22	38.575	20.957	14.295	LYS
A23	40.755	21.0	17.417	LEU
A24	42.277	23.52	19.789	LYS
A25	46.024	23.318	20.399	THR
A26	45.566	23.98	24.119	GLU
A27	43.224	20.981	24.32	ASP
A28	45.722	18.704	22.58	LEU
A29	48.525	19.984	24.83	ASP
A30	46.447	19.079	27.89	ARG
A31	45.635	15.573	26.675	LEU
A32	49.315	15.113	25.786	ARG
A33	50.215	15.404	29.488	VAL
A34	47.242	13.312	30.603	GLY
A35	45.097	16.232	31.762	ASP
A36	41.561	15.275	30.725	PHE
A37	40.073	17.633	33.378	ASN
A38	38.155	19.932	31.051	PHE
A39	34.982	19.577	28.952	PRO
A40	35.693	18.011	25.57	PRO
A41	34.126	18.972	22.297	SER
A42	32.644	16.28	20.1	GLN
A43	35.603	16.77	17.776	ASP
A44	38.045	16.145	20.622	LEU
A45	36.189	13.007	21.647	MET
A46	36.169	11.713	18.083	CYS
A47	39.896	12.522	17.829	TYR
A48	40.469	10.104	20.724	THR
A49	38.487	7.467	18.807	LYS
A50	40.63	8.045	15.697	CYS
A51	43.776	7.555	17.796	VAL
A52	42.423	4.39	19.401	SER
A53	41.322	2.945	16.059	LEU
A54	44.878	3.415	14.827	MET
A55	46.111	1.577	17.968	ALA
A56	43.616	-1.229	17.367	GLY
A57	42.268	-1.056	20.916	THR
A58	38.673	-0.183	19.951	VAL
A59	36.331	-1.002	17.08	ASN
A60	34.375	1.55	15.013	LYS
A61	31.55	1.333	17.531	LYS
A62	34.057	2.538	20.163	GLY
A63	33.926	-0.727	22.095	GLU
A64	37.174	-1.238	24.003	PHE
A65	38.769	-4.658	23.479	ASN
A66	40.843	-5.447	26.587	ALA
A67	42.372	-8.743	25.414	PRO
A68	43.403	-7.104	22.125	LYS
A69	44.67	-4.005	23.923	ALA
A70	46.818	-6.221	26.179	LEU
A71	48.204	-7.989	23.112	ALA
A72	48.933	-4.67	21.382	GLN
A73	50.711	-3.043	24.346	LEU
A74	54.283	-3.836	23.136	PRO
A75	53.412	-2.042	19.872	HIS
A76	52.071	0.988	21.745	LEU
A77	54.175	1.69	24.85	VAL
A78	57.747	1.102	25.995	PRO
A79	58.557	-1.589	28.598	PRO
A80	58.782	1.194	31.235	GLU
A81	55.033	1.9	30.868	MET
A82	53.748	-1.652	30.393	MET
A83	52.674	-2.388	33.968	GLU
A84	50.961	0.987	34.404	MET
A85	49.137	0.364	31.136	SER
A86	48.156	-3.215	32.004	ARG
A87	46.783	-1.912	35.306	LYS
A88	44.771	0.798	33.526	SER
A89	43.469	-1.596	30.863	VAL
A90	42.046	-3.723	33.659	GLU
A91	40.602	-0.799	35.626	ALA
A92	39.023	0.801	32.556	CYS
A93	37.965	-2.194	30.472	ARG
A94	34.239	-1.735	31.17	ASP
A95	34.031	2.083	31.016	THR
A96	32.69	1.872	27.439	HIS
A97	29.614	-0.035	28.673	LYS
A98	28.251	3.118	30.35	GLN
A99	27.968	5.026	27.049	PHE
A100	26.226	4.399	23.722	LYS
A101	27.923	6.763	21.286	GLU
A102	31.26	5.619	19.85	SER
A103	33.343	8.789	20.332	CYS
A104	32.118	9.199	23.906	GLU
A105	32.849	5.527	24.662	ARG
A106	36.456	5.99	23.598	VAL
A107	36.971	9.407	25.171	TYR
A108	35.601	8.243	28.53	GLN
A109	37.877	5.19	28.38	THR
A110	40.925	7.369	27.64	ALA
A111	39.894	9.696	30.494	LYS
A112	39.654	6.637	32.765	CYS
A113	43.166	5.599	31.696	PHE
A114	44.434	9.097	32.533	SER
A115	42.802	9.015	35.969	GLU
A116	43.892	5.487	36.821	ASN
A117	47.452	6.041	35.653	ALA
A118	49.774	5.506	38.621	ASP
A119	52.473	7.411	36.733	GLY
A120	52.633	10.038	34.015	GLN
A121	50.104	9.414	31.254	PHE
A122	50.551	10.786	27.735	MET
A123	47.994	10.874	24.938	TRP
A124	48.974	11.398	21.276	PRO