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
B34	32.222	36.233	14.116	ASN
B35	28.776	34.676	13.712	GLY
B36	27.02	38.087	13.572	ARG
B37	24.035	38.731	11.363	THR
B38	23.258	42.207	10.027	PRO
B39	20.755	42.563	12.913	LEU
B40	23.533	42.038	15.463	HIS
B41	25.527	44.842	13.895	LEU
B42	22.608	47.249	13.623	ALA
B43	21.605	46.483	17.204	ALA
B44	25.182	46.912	18.519	ARG
B45	25.437	50.311	16.869	ASN
B46	21.969	51.567	17.855	GLY
B47	20.387	51.836	14.429	HIS
B48	16.741	51.704	15.337	LEU
B49	15.333	52.163	11.842	GLU
B50	17.636	49.571	10.348	VAL
B51	16.692	47.188	13.123	VAL
B52	13.017	47.63	12.254	LYS
B53	13.7	47.117	8.531	LEU
B54	15.729	43.967	9.107	LEU
B55	13.075	42.585	11.47	LEU
B56	10.355	43.388	8.891	GLU
B57	12.422	41.504	6.331	ALA
B58	12.668	38.317	8.383	GLY
B59	15.722	38.76	10.551	ALA
B60	16.067	36.158	13.284	ASP
B61	15.652	38.233	16.412	VAL
B62	17.466	35.595	18.512	ASN
B63	20.398	34.715	16.228	ALA
B64	23.48	33.827	18.294	LYS
B65	27.018	34.831	17.362	ASP
B66	30.23	32.958	18.277	LYS
C67	30.115	34.296	21.805	ASN
C68	26.556	32.994	22.071	GLY
C69	25.276	36.571	22.081	ARG
C70	21.973	37.677	20.496	THR
C71	21.18	41.119	19.074	PRO
C72	19.556	41.927	22.434	LEU
C73	22.852	41.106	24.219	HIS
C74	24.695	43.549	21.968	LEU
C75	22.089	46.332	22.183	ALA
C76	22.086	45.923	25.965	ALA
C77	25.868	45.882	26.222	ARG
C78	25.99	49.131	24.307	ASN
C79	23.128	50.795	26.206	GLY
C80	20.765	51.304	23.274	HIS
C81	17.468	51.683	25.126	LEU
C82	15.229	52.194	22.07	GLU
C83	16.731	49.227	20.273	VAL
C84	16.37	47.101	23.386	VAL
C85	12.698	48.057	23.557	LYS
C86	12.1	47.186	19.909	LEU
C87	13.897	43.861	20.195	LEU
C88	11.808	42.803	23.237	LEU
C89	8.607	43.725	21.38	GLU
C90	9.812	41.698	18.385	ALA
C91	10.182	38.666	20.662	GLY
C92	13.767	38.726	21.812	ALA
C93	14.646	36.207	24.529	ASP
C94	15.175	38.375	27.62	VAL
C95	16.885	35.472	29.387	ASN
C96	19.17	34.349	26.583	ALA
C97	22.459	33.139	28.01	LYS
C98	25.729	33.664	26.189	ASP
C99	28.941	31.559	26.335	LYS