A2	88.75	62.22	87.89	SER
A3	92.29	59.47	84.37	SER
A4	87.49	56.65	86.32	HIS
A5	89.31	51.81	84.32	PRO
A6	84.22	53.86	83.97	ILE
A7	86.79	57.48	80.48	PHE
A8	89.07	53.3	78.12	HIS
A9	87.24	49.44	80.39	ARG
A10	82.73	51.16	79.61	GLY
A11	78.58	50.05	77.32	GLU
A12	80.18	54.77	74.64	PHE
A13	74.99	55.45	73.08	SER
A14	76.1	54.39	67.62	VAL
A15	73.47	58.8	68.49	CYS
A16	75.6	61.74	72.75	ASP
A17	70.15	60.6	73.52	SER
A18	69.61	65.34	76.23	VAL
A19	65.68	61.6	78.9	SER
A20	63.3	66.69	78.55	VAL
A21	59.49	65.72	82.53	TRP
A22	57.65	67.54	77.0	VAL
A23	54.66	69.71	80.26	GLY
A24	55.09	73.82	78.08	ASP
A25	53.08	69.25	74.66	LYS
A26	50.17	74.04	72.64	THR
A27	50.63	71.96	67.9	THR
A28	51.4	66.48	69.19	ALA
A29	51.96	65.29	63.9	THR
A30	47.36	62.68	65.53	ASP
A31	47.68	57.85	64.86	ILE
A32	45.55	60.63	60.74	LYS
A33	49.61	62.87	60.35	GLY
A34	45.55	65.56	61.42	LYS
A35	48.65	69.98	63.3	GLU
A36	46.12	66.86	67.26	VAL
A37	44.62	71.47	70.01	MET
A38	48.49	68.36	73.13	VAL
A39	43.57	68.86	76.63	LEU
A40	47.0	70.81	79.35	GLY
A41	44.39	69.56	83.13	GLU
A42	44.25	64.28	81.43	VAL
A43	40.05	64.7	85.21	ASN
A44	41.05	59.12	86.05	ILE
A45	36.12	59.15	87.97	ASN
A46	38.79	62.02	91.07	ASN
A47	41.64	65.87	91.49	SER
A48	43.07	68.2	86.67	VAL
A49	47.1	64.12	85.78	PHE
A50	49.84	68.91	84.93	LYS
A51	48.63	66.32	79.74	GLN
A52	53.95	65.12	82.0	TYR
A53	54.91	63.87	76.69	PHE
A54	58.79	60.47	79.2	PHE
A55	60.33	64.01	75.05	GLU
A56	64.43	60.1	74.84	THR
A57	65.57	64.71	71.36	LYS
A58	69.58	63.62	68.4	CYS
A59	73.19	64.88	72.51	ARG
A60	75.81	66.98	68.42	ASP
A67	77.05	63.08	65.9	GLY
A68	77.4	58.52	64.07	CYS
A69	80.52	57.89	68.84	ARG
A70	82.28	54.31	66.43	GLY
A71	80.24	54.7	62.09	ILE
A72	83.4	50.89	59.47	ASP
A73	85.25	56.64	58.67	SER
A74	87.01	53.13	55.35	LYS
A75	82.62	50.88	54.51	HIS
A76	79.24	53.79	56.53	TRP
A77	77.92	58.6	54.65	ASN
A78	76.88	57.39	60.02	SER
A79	73.59	61.79	59.91	TYR
A80	72.72	60.95	65.6	CYS
A81	68.01	61.14	62.73	THR
A82	65.28	62.65	67.26	THR
A83	63.62	57.14	66.29	THR
A84	58.76	59.81	66.53	HIS
A85	57.36	56.4	70.73	THR
A86	52.16	56.35	68.6	PHE
A87	53.06	58.49	74.29	VAL
A88	47.37	57.03	74.08	LYS
A89	47.85	62.66	74.08	ALA
A90	43.32	64.46	76.77	LEU
A91	44.43	64.75	70.97	THR
A92	40.94	69.4	71.09	MET
A93	39.73	65.53	66.49	ASP
A94	39.8	70.21	65.19	GLY
A95	35.31	68.75	65.37	LYS
A96	34.74	67.19	69.55	GLN
A97	37.87	66.56	73.99	ALA
A98	39.17	62.18	70.74	ALA
A99	41.24	59.03	74.65	TRP
A100	43.55	60.36	69.23	ARG
A101	48.36	57.49	69.21	PHE
A102	50.21	62.95	69.94	ILE
A103	54.25	61.63	66.36	ARG
A104	56.23	62.35	71.78	ILE
A105	61.62	63.14	70.85	ASP
A106	60.75	57.42	71.6	THR
A107	65.51	56.18	70.95	ALA
A108	69.43	59.79	69.73	CYS
A109	68.59	55.44	65.74	VAL
A110	74.12	55.8	64.22	CYS
A111	70.83	57.29	59.57	VAL
A112	74.35	52.97	57.93	LEU
A113	74.21	56.56	53.43	SER
A114	77.22	52.67	50.71	ARG
A115	82.04	55.46	50.97	LYS
B282	64.37	60.68	20.6	VAL
B283	59.62	63.3	22.56	SER
B284	59.88	57.84	23.99	PHE
B285	54.92	56.82	25.74	PRO
B286	55.5	58.63	31.18	ALA
B287	57.21	53.29	31.14	SER
B288	55.63	54.48	36.17	VAL
B289	57.64	49.39	37.46	GLN
B290	55.27	50.28	42.32	LEU
B291	59.9	47.57	43.85	HIS
B292	57.89	44.27	47.3	THR
B293	56.57	48.31	50.97	ALA
B294	62.25	47.61	51.12	VAL
B295	61.48	48.28	56.85	GLU
B296	66.12	51.38	54.67	MET
B297	66.77	55.16	58.12	HIS
B298	62.1	56.02	56.11	HIS
B299	58.67	52.24	55.59	TRP
B300	61.87	52.99	50.61	CYS
B301	56.6	52.23	48.27	ILE
B302	61.49	50.84	45.31	PRO
B303	59.11	54.75	41.88	PHE
B304	62.06	52.0	38.15	SER
B305	59.33	57.04	36.78	VAL
B306	61.75	55.7	31.64	ASP
B307	59.81	59.25	29.74	GLY
B308	61.96	61.87	26.51	GLN
B309	58.51	66.34	28.23	PRO
B310	61.36	64.95	32.8	ALA
B311	56.55	61.64	33.66	PRO
B312	54.48	65.99	36.48	SER
B313	55.98	61.97	40.16	LEU
B314	50.37	62.96	41.15	ARG
B315	51.97	59.43	45.64	TRP
B316	46.68	57.71	44.27	LEU
B317	46.8	56.94	49.78	PHE
B318	42.62	53.78	49.26	ASN
B319	42.69	55.85	44.72	GLY
B320	42.12	59.51	47.91	SER
B321	45.39	63.4	45.7	VAL
B322	49.43	60.26	48.47	LEU
B323	48.72	65.76	51.04	ASN
B324	54.34	65.08	49.78	GLU
B325	53.44	65.18	55.46	THR
B326	57.95	66.78	57.54	SER
B327	55.9	61.89	58.56	PHE
B328	54.02	60.57	53.83	ILE
B329	58.52	63.33	51.71	PHE
B330	58.56	61.98	46.18	THR
B331	63.42	60.7	48.69	GLU
B332	64.86	61.57	42.99	PHE
B333	68.2	57.31	43.65	LEU
B334	72.03	61.14	42.94	GLU
B335	70.18	60.94	37.42	PRO
B336	73.08	56.17	36.51	ALA
B337	76.77	58.71	33.51	ALA
B338	74.29	59.04	29.17	ASN
B339	70.16	56.02	31.94	GLU
B340	65.82	59.45	30.22	THR
B341	65.25	55.04	33.98	VAL
B342	64.15	59.35	37.47	ARG
B343	65.98	54.95	40.73	HIS
B344	63.7	56.53	44.06	GLY
B345	61.85	56.05	48.32	CYS
B346	56.56	56.72	48.4	LEU
B347	60.72	58.19	52.38	ARG
B348	56.42	55.62	55.08	LEU
B349	59.15	59.31	58.82	ASN
B350	58.09	55.79	62.44	GLN
B351	54.05	53.82	57.95	PRO
B352	50.63	53.23	62.4	THR
B353	47.55	49.47	61.41	HIS
B354	46.15	54.9	60.01	VAL
B355	50.48	54.26	56.74	ASN
B356	47.55	49.14	56.05	ASN
B357	46.59	50.39	51.81	GLY
B358	45.89	50.4	47.02	ASN
B359	51.16	52.77	47.46	TYR
B360	48.28	54.23	42.47	THR
B361	53.72	56.0	41.41	LEU
B362	49.3	59.05	38.57	LEU
B363	54.2	58.43	35.58	ALA
B364	51.12	62.75	33.62	ALA
B365	55.27	62.97	29.87	ASN
B366	53.33	65.8	25.84	PRO
B367	52.77	60.36	24.88	PHE
B368	49.39	60.26	28.19	GLY
B369	48.48	59.19	32.64	GLN
B370	53.1	55.74	32.63	ALA
B371	49.0	54.58	36.62	SER
B372	52.26	50.33	37.96	ALA
B373	48.3	49.56	41.87	SER
B374	52.53	47.91	44.93	ILE
B375	48.77	45.9	48.63	MET
B376	52.61	49.26	51.26	ALA
B377	50.78	45.26	55.16	ALA
B378	53.34	50.06	57.56	PHE
B379	51.68	48.54	61.78	MET
B380	49.25	43.59	62.92	ASP
B381	44.37	46.01	62.2	ASN
B382	43.78	47.44	67.49	PRO