A2	89.77	62.8	86.83	SER
A3	90.87	59.57	84.86	SER
A4	88.9	56.4	85.75	HIS
A5	89.07	53.1	83.65	PRO
A6	85.28	53.44	82.99	ILE
A7	85.9	56.2	80.39	PHE
A8	87.59	53.66	78.08	HIS
A9	86.45	50.16	79.3	ARG
A10	82.73	51.16	79.61	GLY
A11	79.78	51.02	77.18	GLU
A12	78.98	53.94	75.03	PHE
A13	76.1	54.5	72.66	SER
A14	76.61	55.12	68.89	VAL
A15	74.7	58.52	69.47	CYS
A16	74.54	60.67	72.43	ASP
A17	71.15	61.74	73.84	SER
A18	69.2	63.89	76.32	VAL
A19	65.93	62.94	78.17	SER
A20	63.11	65.37	79.32	VAL
A21	59.7	65.8	80.99	TRP
A22	57.66	67.94	78.48	VAL
A23	54.66	69.71	80.26	GLY
A24	53.98	72.72	77.95	ASP
A25	52.97	70.85	74.78	LYS
A26	50.13	72.48	72.7	THR
A27	50.37	71.12	69.17	THR
A28	51.46	67.61	68.09	ALA
A29	50.95	65.49	65.07	THR
A30	48.83	62.44	65.39	ASP
A31	48.65	58.9	64.08	ILE
A32	46.98	60.12	60.86	LYS
A33	49.61	62.87	60.35	GLY
A34	47.1	65.78	61.11	LYS
A35	48.17	68.58	63.55	GLU
A36	46.22	68.26	66.71	VAL
A37	45.74	70.49	69.78	MET
A38	46.99	68.77	73.04	VAL
A39	45.0	69.53	76.31	LEU
A40	47.0	70.81	79.35	GLY
A41	45.26	68.82	82.1	GLU
A42	43.4	65.44	82.01	VAL
A43	41.05	63.69	84.52	ASN
A44	39.94	60.14	85.76	ILE
A45	36.55	60.57	87.5	ASN
A46	38.16	62.94	90.0	ASN
A47	40.88	65.61	90.23	SER
A48	43.06	66.78	87.29	VAL
A49	46.57	65.5	86.36	PHE
A50	48.76	68.06	84.33	LYS
A51	49.36	66.18	81.06	GLN
A52	53.04	65.33	80.77	TYR
A53	55.01	63.42	78.19	PHE
A54	58.46	61.87	78.57	PHE
A55	60.61	62.58	75.66	GLU
A56	64.19	61.6	74.58	THR
A57	66.24	63.33	71.81	LYS
A58	69.6	63.46	69.92	CYS
A59	72.88	65.16	71.02	ARG
A60	75.11	65.7	67.89	ASP
A67	77.05	63.08	65.9	GLY
A68	77.73	59.41	65.35	CYS
A69	80.54	57.65	67.28	ARG
A70	82.28	54.31	66.43	GLY
A71	81.23	53.73	62.84	ILE
A72	83.44	52.32	60.04	ASP
A73	84.16	55.68	58.13	SER
A74	85.93	54.13	55.14	LYS
A75	82.83	52.2	53.95	HIS
A76	80.08	54.49	55.35	TRP
A77	78.64	57.88	55.88	ASN
A78	76.4	58.33	58.83	SER
A79	74.32	60.82	60.87	TYR
A80	72.35	60.56	64.16	CYS
A81	68.54	61.26	64.14	THR
A82	65.76	61.37	66.65	THR
A83	63.23	58.65	66.29	THR
A84	59.57	58.86	67.41	HIS
A85	57.04	56.88	69.42	THR
A86	53.07	57.13	69.58	PHE
A87	52.05	57.83	73.24	VAL
A88	48.34	58.22	73.88	LYS
A89	46.87	61.64	74.82	ALA
A90	43.93	63.9	75.46	LEU
A91	43.64	65.59	72.04	THR
A92	41.21	68.0	70.41	MET
A93	40.56	66.81	66.86	ASP
A94	39.8	70.21	65.19	GLY
A95	36.19	69.62	66.22	LYS
A96	36.11	68.04	69.71	GLN
A97	38.09	66.19	72.45	ALA
A98	39.12	62.54	72.22	ALA
A99	41.6	60.08	73.55	TRP
A100	44.02	59.54	70.53	ARG
A101	47.82	58.79	69.91	PHE
A102	50.5	61.55	69.28	ILE
A103	54.07	61.34	67.77	ARG
A104	56.77	62.36	70.32	ILE
A105	60.73	61.96	70.44	ASP
A106	61.73	58.51	72.01	THR
A107	65.36	57.69	71.21	ALA
A108	68.34	58.88	69.1	CYS
A109	69.6	56.38	66.37	VAL
A110	72.62	56.4	63.87	CYS
A111	71.76	56.24	60.13	VAL
A112	74.14	54.45	57.66	LEU
A113	74.64	55.19	53.97	SER
A114	77.44	53.8	51.76	ARG
A115	80.62	55.59	50.39	LYS
B282	63.93	62.13	21.03	VAL
B283	60.65	62.19	22.9	SER
B284	58.84	59.07	24.09	PHE
B285	55.83	57.98	26.28	PRO
B286	56.07	57.69	30.05	ALA
B287	56.41	54.29	31.94	SER
B288	56.61	53.47	35.56	VAL
B289	56.78	50.6	37.96	GLN
B290	56.66	50.01	41.61	LEU
B291	58.37	47.43	43.73	HIS
B292	57.63	45.73	47.08	THR
B293	57.81	47.96	50.14	ALA
B294	61.07	47.79	52.1	VAL
B295	62.07	49.05	55.67	GLU
B296	65.53	50.77	55.98	MET
B297	65.99	53.84	58.25	HIS
B298	62.66	54.78	56.83	HIS
B299	60.1	52.6	55.17	TRP
B300	60.39	52.99	51.31	CYS
B301	58.09	51.96	48.46	ILE
B302	60.57	51.98	45.58	PRO
B303	59.91	53.44	42.06	PHE
B304	61.46	53.36	38.61	SER
B305	60.17	55.96	36.12	VAL
B306	61.07	56.81	32.45	ASP
B307	59.81	59.25	29.74	GLY
B308	60.81	62.29	27.55	GLN
B309	59.45	65.09	28.32	PRO
B310	60.39	64.13	31.98	ALA
B311	57.05	63.09	33.7	PRO
B312	55.39	64.83	36.49	SER
B313	54.65	62.49	39.46	LEU
B314	51.58	62.21	41.74	ARG
B315	51.13	59.58	44.37	TRP
B316	47.7	58.23	45.33	LEU
B317	46.55	56.2	48.42	PHE
B318	43.43	53.88	47.95	ASN
B319	42.69	55.85	44.72	GLY
B320	42.81	59.26	46.49	SER
B321	45.48	62.01	46.17	VAL
B322	48.49	61.56	48.57	LEU
B323	49.52	64.89	50.12	ASN
B324	53.26	64.9	50.83	GLU
B325	54.28	65.89	54.38	THR
B326	57.51	65.91	56.34	SER
B327	56.72	62.23	57.33	PHE
B328	55.53	60.99	53.94	ILE
B329	57.62	62.25	51.0	PHE
B330	59.0	61.48	47.57	THR
B331	62.74	61.11	47.34	GLU
B332	64.55	60.57	44.08	PHE
B333	67.93	58.73	44.07	LEU
B334	70.69	60.66	42.31	GLU
B335	70.62	59.86	38.48	PRO
B336	73.12	57.72	36.58	ALA
B337	75.21	59.04	33.59	ALA
B338	73.19	59.19	30.27	ASN
B339	70.07	57.37	31.24	GLU
B340	66.71	59.09	31.47	THR
B341	65.2	56.57	33.99	VAL
B342	64.78	58.0	37.46	ARG
B343	64.78	55.88	40.59	HIS
B344	63.7	56.53	44.06	GLY
B345	61.17	56.21	46.95	CYS
B346	58.02	57.15	48.56	LEU
B347	59.45	57.44	51.98	ARG
B348	57.39	56.77	55.09	LEU
B349	58.95	57.83	58.43	ASN
B350	57.58	55.3	61.03	GLN
B351	54.14	54.42	59.39	PRO
B352	51.31	52.6	61.28	THR
B353	48.31	50.37	60.35	HIS
B354	46.41	53.55	59.33	VAL
B355	48.98	53.75	56.47	ASN
B356	48.24	50.21	55.22	ASN
B357	46.59	50.39	51.81	GLY
B358	47.08	50.52	48.01	ASN
B359	49.74	52.83	46.78	TYR
B360	49.66	54.05	43.18	THR
B361	52.17	56.27	41.24	LEU
B362	50.64	58.25	38.36	LEU
B363	53.24	59.49	35.94	ALA
B364	52.37	62.01	33.22	ALA
B365	53.89	63.66	30.17	ASN
B366	52.51	64.89	26.7	PRO
B367	51.6	61.27	25.28	PHE
B368	49.39	60.26	28.19	GLY
B369	49.69	58.87	31.67	GLN
B370	51.58	55.87	32.98	ALA
B371	50.47	54.14	36.24	SER
B372	50.93	51.04	38.35	ALA
B373	49.8	49.93	41.89	SER
B374	50.97	47.93	44.9	ILE
B375	49.57	47.16	48.29	MET
B376	51.71	47.99	51.42	ALA
B377	51.11	46.74	54.94	ALA
B378	53.39	48.47	57.65	PHE
B379	51.81	47.34	60.87	MET
B380	49.02	44.93	62.13	ASP
B381	45.51	46.2	63.23	ASN
B382	44.07	46.12	66.86	PRO