A1	100.16	67.28	-61.401	PRO
A2	99.88	70.41	-59.091	ILE
A3	102.56	71.25	-56.341	SER
A4	101.9	70.98	-52.551	PRO
A5	101.51	73.62	-49.741	ILE
A6	101.8	73.4	-45.921	GLU
A7	98.94	74.06	-43.471	THR
A8	98.88	77.03	-41.021	VAL
A9	97.85	75.98	-37.381	PRO
A10	94.75	77.88	-35.871	VAL
A11	92.46	77.56	-32.761	LYS
A12	88.94	78.23	-31.321	LEU
A13	88.17	80.82	-28.571	LYS
A14	88.79	79.51	-25.001	PRO
A15	85.65	78.16	-23.361	GLY
A16	83.93	77.4	-26.691	MET
A17	83.45	74.33	-28.891	ASP
A18	82.64	73.97	-32.631	GLY
A19	79.03	74.68	-34.011	PRO
A20	76.22	72.11	-33.791	LYS
A21	73.5	73.98	-35.711	VAL
A22	70.71	71.93	-37.401	LYS
A23	70.23	71.91	-41.241	GLN
A24	67.15	73.69	-42.811	TRP
A25	65.06	72.42	-45.911	PRO
A26	66.05	73.08	-49.591	LEU
A27	63.88	72.57	-52.811	THR
A28	64.44	69.28	-54.891	GLU
A29	66.49	71.07	-57.651	GLU
A30	68.65	72.99	-55.101	LYS
A31	69.37	69.53	-53.401	ILE
A32	70.14	68.0	-56.981	LYS
A33	72.41	70.82	-57.971	ALA
A34	74.16	70.72	-54.541	LEU
A35	75.12	66.95	-54.901	VAL
A36	76.55	67.73	-58.411	GLU
A37	78.52	70.78	-56.701	ILE
A38	79.52	68.28	-53.841	CYS
A39	80.98	65.87	-56.591	THR
A40	83.27	68.64	-58.051	GLU
A41	84.15	69.57	-54.481	MET
A42	84.83	65.93	-53.491	GLU
A43	86.76	64.78	-56.641	LYS
A44	88.73	68.16	-56.511	GLU
A45	90.06	67.77	-52.871	GLY
A46	87.75	70.7	-51.401	LYS
A47	85.56	68.5	-49.061	ILE
A48	85.68	65.05	-47.491	SER
A49	83.33	62.71	-45.711	LYS
A50	83.15	62.26	-41.961	ILE
A51	81.84	59.49	-39.551	GLY
A52	79.27	59.43	-36.621	PRO
A53	81.88	60.53	-33.841	GLU
A54	82.38	64.0	-35.511	ASN
A55	79.84	66.12	-33.441	PRO
A56	79.72	69.42	-35.441	TYR
A57	77.47	71.14	-38.091	ASN
A58	76.89	74.58	-39.871	THR
A59	73.85	75.02	-42.221	PRO
A60	74.19	75.23	-46.111	VAL
A61	72.19	76.96	-48.751	PHE
A62	72.16	77.8	-52.511	ALA
A63	71.46	80.62	-54.981	ILE
A64	71.79	81.52	-58.671	LYS
A65	75.03	82.69	-60.461	LYS
A66	74.82	86.17	-61.981	LYS
A67	73.4	86.15	-65.561	ASP
A68	73.45	82.26	-65.531	SER
A69	70.86	79.36	-65.121	THR
A70	73.22	77.61	-62.781	LYS
A71	73.4	77.5	-58.861	TRP
A72	76.11	78.4	-56.401	ARG
A73	76.46	77.29	-52.661	LYS
A74	76.64	79.46	-49.451	LEU
A75	77.49	78.31	-45.861	VAL
A76	76.19	80.3	-42.791	ASP
A77	79.38	80.11	-40.571	PHE
A78	78.0	82.86	-38.231	ARG
A79	78.78	80.7	-35.171	GLU
A80	82.15	79.28	-36.341	LEU
A81	83.03	82.95	-37.081	ASN
A82	81.89	83.86	-33.531	LYS
A83	83.99	80.86	-32.211	ARG
A84	87.39	81.19	-34.041	THR
A85	90.17	82.6	-31.741	GLN
A86	91.31	86.26	-32.311	ASP
A87	94.27	86.68	-34.781	PHE
A88	97.13	89.27	-34.711	TRP
A89	96.93	91.28	-38.061	GLU
A90	100.08	91.52	-40.051	VAL
A91	98.92	90.68	-43.581	GLN
A92	95.43	92.26	-44.281	LEU
A93	96.38	96.0	-44.571	GLY
A94	96.56	98.36	-47.671	ILE
A95	99.6	100.67	-48.421	PRO
A96	99.61	104.44	-48.711	HIS
A97	100.64	105.43	-52.311	PRO
A98	102.6	108.32	-50.841	ALA
A99	104.89	105.71	-49.371	GLY
A100	105.27	103.7	-52.651	LEU
A101	108.16	104.65	-55.201	LYS
A102	107.85	105.48	-58.981	LYS
A103	108.13	102.6	-61.621	LYS
A104	108.17	102.56	-65.451	LYS
A105	105.71	99.63	-65.551	SER
A106	103.03	98.38	-63.001	VAL
A107	100.27	95.66	-63.321	THR
A108	98.1	93.0	-61.611	VAL
A109	97.03	89.33	-61.691	LEU
A110	93.57	88.17	-60.391	ASP
A111	93.52	85.57	-57.421	VAL
A112	89.96	86.43	-56.011	GLY
A113	88.92	82.69	-55.281	ASP
A114	92.47	81.06	-54.831	ALA
A115	91.96	80.49	-51.031	TYR
A116	89.77	77.7	-52.181	PHE
A117	92.98	75.94	-53.611	SER
A118	95.08	76.2	-50.321	VAL
A119	94.77	73.49	-47.621	PRO
A120	93.01	73.85	-44.291	LEU
A121	94.68	72.78	-41.031	ASP
A122	93.78	69.03	-40.421	GLU
A123	93.14	69.77	-36.581	ASP
A124	90.33	72.44	-37.481	PHE
A125	88.57	70.59	-40.521	ARG
A126	86.25	68.89	-37.931	LYS
A127	84.71	72.36	-36.981	TYR
A128	83.85	73.15	-40.771	THR
A129	81.28	70.47	-40.851	ALA
A130	78.06	70.64	-43.061	PHE
A131	75.14	68.39	-44.191	THR
A132	72.99	67.91	-47.401	ILE
A133	69.33	67.69	-46.111	PRO
A134	67.53	64.44	-45.381	SER
A135	64.73	65.43	-47.831	ILE
A136	61.1	64.26	-48.301	ASN
A137	61.42	62.44	-44.851	ASN
A138	62.83	59.28	-46.611	GLU
A139	65.97	60.47	-48.511	THR
A140	69.33	60.22	-46.601	PRO
A141	71.51	63.32	-45.831	GLY
A142	75.28	63.37	-46.581	ILE
A143	77.78	64.98	-44.041	ARG
A144	81.1	66.63	-45.001	TYR
A145	83.89	68.76	-43.741	GLN
A146	86.23	71.01	-45.811	TYR
A147	89.88	70.26	-47.051	ASN
A148	90.83	73.8	-48.431	VAL
A149	90.09	77.16	-46.891	LEU
A150	86.25	77.44	-46.821	PRO
A151	83.98	80.15	-48.331	GLN
A152	82.8	82.76	-45.771	GLY
A153	84.87	81.57	-42.811	TRP
A154	86.64	84.65	-41.211	LYS
A155	90.08	83.0	-41.301	GLY
A156	90.29	82.49	-45.091	SER
A157	91.87	85.92	-45.671	PRO
A158	94.72	85.7	-42.991	ALA
A159	95.54	82.1	-44.251	ILE
A160	95.56	82.64	-47.961	PHE
A161	97.88	85.63	-47.211	GLN
A162	100.12	83.38	-44.931	SER
A163	100.5	80.75	-47.691	SER
A164	100.92	83.2	-50.711	MET
A165	104.13	84.59	-48.921	THR
A166	105.53	81.0	-49.261	LYS
A167	104.58	80.48	-53.061	ILE
A168	106.16	84.01	-53.671	LEU
A169	109.26	83.41	-51.611	GLU
A170	110.81	81.16	-54.381	PRO
A171	109.52	83.48	-57.091	PHE
A172	111.34	86.47	-55.361	ALA
A173	114.58	84.55	-54.711	ALA
A174	114.58	84.01	-58.571	GLN
A175	113.39	87.67	-59.601	ASN
A176	115.09	90.35	-57.281	PRO
A177	114.45	93.48	-59.381	ASP
A178	110.7	93.35	-59.781	ILE
A179	108.76	94.95	-56.911	VAL
A180	105.67	93.18	-55.411	ILE
A181	102.54	93.7	-53.281	TYR
A182	100.1	90.91	-52.251	GLN
A183	96.49	91.45	-51.431	TYR
A184	93.45	89.36	-50.511	MET
A185	92.14	89.24	-54.201	ASP
A186	94.98	90.47	-56.331	ASP
A187	98.73	90.44	-56.991	LEU
A188	100.34	93.82	-57.841	TYR
A189	103.79	93.92	-59.671	VAL
A190	106.07	96.68	-60.951	GLY
A191	109.51	97.39	-62.521	SER
A192	112.05	99.9	-63.891	ASP
A193	111.12	98.56	-67.491	LEU
A194	108.52	99.47	-70.141	GLU
A195	105.64	96.9	-69.681	ILE
A196	106.53	95.37	-73.121	GLY
A197	109.86	94.02	-71.641	GLN
A198	108.21	93.14	-68.151	HIS
A199	105.23	91.11	-69.661	ARG
A200	107.26	87.83	-70.331	THR
A201	107.99	88.0	-66.521	LYS
A202	104.24	88.44	-65.731	ILE
A203	103.41	85.48	-67.921	GLU
A204	106.14	83.53	-65.961	GLU
A205	104.53	84.57	-62.601	LEU
A206	101.3	83.04	-63.951	ARG
A207	103.12	79.84	-65.011	GLN
A208	104.61	79.75	-61.561	HIS
A209	101.13	80.23	-59.901	LEU
A210	99.78	77.41	-62.211	LEU
A211	102.43	74.81	-61.251	ARG
A212	101.17	75.62	-57.651	TRP
A213	97.69	74.88	-58.961	GLY
A214	95.92	78.18	-57.941	LEU
A215	92.84	79.72	-59.831	THR
A216	93.91	82.82	-61.891	THR
A217	91.53	83.92	-64.761	PRO
A218	92.34	85.85	-68.061	ASP
A219	92.08	89.6	-67.041	LYS
A220	95.28	90.67	-69.091	LYS
A221	98.93	91.11	-68.031	HIS
A222	98.37	94.94	-67.861	GLN
A223	95.94	97.84	-67.151	LYS
A224	95.9	101.27	-68.791	GLU
A225	96.44	104.3	-66.461	PRO
A226	95.15	106.09	-64.391	PRO
A227	94.55	103.09	-62.021	PHE
A228	91.29	103.35	-60.061	LEU
A229	91.83	101.72	-56.611	TRP
A230	90.33	102.02	-53.101	MET
A231	88.98	105.66	-53.601	GLY
A232	92.6	106.59	-54.841	TYR
A233	93.48	107.56	-58.411	GLU
A234	97.02	106.53	-59.401	LEU
A235	99.09	107.77	-62.341	HIS
A236	102.63	106.94	-63.741	PRO
A237	104.04	110.24	-62.381	ASP
A238	101.81	111.36	-59.411	LYS
A239	99.03	110.09	-56.901	TRP
A240	95.54	111.68	-56.081	THR
A241	92.03	110.73	-54.691	VAL
A242	88.66	110.19	-56.521	GLN
A243	86.56	113.37	-56.731	PRO
A244	84.7	114.02	-53.371	ILE
A245	81.19	115.59	-53.741	VAL
A246	80.12	118.01	-50.921	LEU
A247	76.27	118.55	-51.431	PRO
A248	74.22	121.81	-50.931	GLU
A249	70.91	120.76	-49.341	LYS
A250	69.22	122.43	-46.421	ASP
A251	68.52	119.05	-44.671	SER
A252	70.51	115.94	-43.551	TRP
A253	70.57	112.86	-41.261	THR
A254	73.26	111.89	-38.751	VAL
A255	74.05	108.87	-40.991	ASN
A256	74.62	111.4	-43.741	ASP
A257	76.76	113.69	-41.471	ILE
A258	78.83	110.73	-40.351	GLN
A259	79.43	109.95	-44.101	LYS
A260	80.04	113.78	-44.871	LEU
A261	82.84	113.87	-42.131	VAL
A262	84.09	110.52	-43.521	GLY
A263	84.21	112.19	-47.021	LYS
A264	86.09	115.26	-45.631	LEU
A265	88.71	113.0	-43.931	ASN
A266	89.21	111.17	-47.321	TRP
A267	89.78	114.68	-48.831	ALA
A268	92.09	116.09	-45.961	SER
A269	95.01	113.73	-46.841	GLN
A270	95.67	115.86	-49.991	ILE
A271	93.87	119.28	-49.621	TYR
A272	95.35	122.09	-47.341	PRO
A273	93.11	124.16	-45.171	GLY
A274	90.11	121.8	-44.581	ILE
A275	87.85	122.19	-41.391	LYS
A276	85.24	120.02	-39.721	VAL
A277	84.33	121.69	-36.291	ARG
A278	81.05	123.38	-37.371	GLN
A279	79.8	120.18	-39.151	LEU
A280	80.85	117.57	-36.411	SER
A281	78.35	119.43	-33.881	LYS
A282	75.4	117.66	-35.641	LEU
A283	76.52	114.22	-34.371	LEU
A284	74.4	115.2	-31.191	ARG
A285	70.64	116.15	-31.511	GLY
A286	68.52	112.99	-31.991	THR
A287	67.36	109.58	-30.481	LYS
A288	68.55	107.58	-33.581	ALA
A289	71.03	108.34	-36.481	LEU
A290	68.41	108.55	-39.401	THR
A291	66.27	111.32	-37.751	GLU
A292	66.14	114.41	-39.921	VAL
A293	68.21	117.67	-39.071	ILE
A294	68.75	121.19	-40.511	PRO
A295	72.11	122.36	-41.891	LEU
A296	73.33	124.97	-39.341	THR
A297	74.48	128.29	-40.931	GLU
A298	78.07	128.18	-39.311	GLU
A299	78.47	124.71	-40.961	ALA
A300	76.87	125.83	-44.341	GLU
A301	79.91	128.17	-44.491	LEU
A302	82.38	125.54	-43.331	GLU
A303	80.79	122.98	-45.911	LEU
A304	80.64	125.79	-48.631	ALA
A305	84.38	126.74	-47.881	GLU
A306	85.35	123.02	-48.191	ASN
A307	83.37	122.77	-51.621	ARG
A308	85.23	125.89	-52.761	GLU
A309	88.78	124.51	-51.671	ILE
A310	87.69	121.34	-53.611	LEU
A311	86.91	123.49	-56.801	LYS
A312	90.11	122.23	-58.611	GLU
A313	92.16	119.05	-59.481	PRO
A314	95.18	118.32	-57.151	VAL
A315	97.87	115.55	-57.021	HIS
A316	100.96	114.73	-54.961	GLY
A317	104.05	112.61	-55.631	VAL
A318	105.68	109.19	-55.101	TYR
A319	108.44	109.01	-52.391	TYR
A320	112.3	109.01	-53.151	ASP
A321	114.77	107.78	-50.511	PRO
A322	117.48	109.85	-52.511	SER
A323	115.82	113.14	-51.661	LYS
A324	115.12	114.99	-48.341	ASP
A325	111.87	115.1	-46.161	LEU
A326	110.25	118.27	-44.781	ILE
A327	106.93	119.19	-42.901	ALA
A328	105.22	122.7	-42.731	GLU
A329	102.43	123.56	-40.321	ILE
A330	99.75	126.4	-40.071	GLN
A331	96.99	127.59	-37.591	LYS
A332	93.26	127.51	-38.431	GLN
A333	89.95	128.68	-36.781	GLY
A334	88.11	126.94	-33.951	GLN
A335	91.31	125.21	-32.491	GLY
A336	92.3	123.41	-35.811	GLN
A337	95.58	123.14	-37.731	TRP
A338	96.68	122.12	-41.301	THR
A339	100.16	120.55	-42.501	TYR
A340	101.96	119.71	-45.721	GLN
A341	104.89	117.31	-46.161	ILE
A342	107.26	117.35	-49.121	TYR
A343	110.74	116.43	-50.501	GLN
A344	111.04	119.33	-53.031	GLU
A345	109.64	122.99	-53.571	PRO
A346	106.33	123.37	-55.521	PHE
A347	105.42	119.59	-54.761	LYS
A348	103.35	117.69	-52.171	ASN
A349	104.22	114.22	-50.711	LEU
A350	101.19	114.15	-48.321	LYS
A351	98.91	116.63	-46.601	THR
A352	97.07	116.48	-43.241	GLY
A353	95.2	118.12	-40.271	LYS
A354	95.1	118.23	-36.441	TYR
A355	92.49	119.58	-33.931	ALA
A356	92.67	120.11	-30.081	ARG
A357	90.1	118.61	-27.571	MET
A358	87.29	120.55	-25.681	ARG
A359	88.17	121.53	-22.071	GLY
A360	88.55	124.71	-19.821	ALA
A361	91.73	126.58	-21.261	HIS
A362	94.83	126.13	-23.581	THR
A363	97.55	127.96	-25.761	ASN
A364	98.68	127.49	-29.391	ASP
A365	102.24	126.14	-28.551	VAL
A366	100.83	123.22	-26.541	LYS
A367	98.76	122.33	-29.631	GLN
A368	101.59	122.98	-32.141	LEU
A369	103.9	120.74	-29.931	THR
A370	101.5	117.69	-30.221	GLU
A371	100.87	118.38	-34.011	ALA
A372	104.61	117.78	-34.721	VAL
A373	104.4	114.42	-32.861	GLN
A374	101.26	113.47	-34.941	LYS
A375	103.25	114.24	-38.111	ILE
A376	106.14	112.09	-36.741	THR
A377	103.85	109.09	-35.831	THR
A378	102.4	109.24	-39.311	GLU
A379	105.75	110.06	-41.031	SER
A380	107.58	107.02	-39.721	ILE
A381	104.63	104.63	-40.701	VAL
A382	104.35	105.86	-44.371	ILE
A383	108.15	106.44	-44.921	TRP
A384	110.09	105.12	-41.881	GLY
A385	111.62	108.69	-41.441	LYS
A386	110.96	111.91	-39.431	THR
A387	110.9	115.23	-41.361	PRO
A388	112.68	118.54	-40.561	LYS
A389	109.95	120.81	-39.221	PHE
A390	109.07	124.23	-40.571	LYS
A391	107.35	125.51	-37.381	LEU
A392	104.76	128.46	-37.371	PRO
A393	106.33	129.6	-34.001	ILE
A394	107.95	132.88	-32.831	GLN
A395	111.68	132.92	-31.841	LYS
A396	111.28	134.39	-28.221	GLU
A397	108.3	132.24	-27.371	THR
A398	110.28	129.2	-28.581	TRP
A399	113.36	130.38	-26.471	GLU
A400	111.08	130.95	-23.461	THR
A401	109.33	127.58	-23.781	TRP
A402	112.46	125.5	-23.601	TRP
A403	114.44	127.62	-20.961	THR
A404	111.8	128.58	-18.391	GLU
A405	108.3	127.22	-19.241	TYR
A406	107.52	124.1	-17.121	TRP
A407	106.19	121.66	-19.801	GLN
A408	108.65	119.05	-21.031	ALA
A409	108.98	118.99	-24.811	THR
A410	111.35	117.48	-27.541	TRP
A411	111.65	117.34	-31.371	ILE
A412	114.83	116.55	-33.341	PRO
A413	115.62	119.28	-36.081	GLU
A414	113.5	122.28	-37.171	TRP
A415	113.43	125.79	-38.621	GLU
A416	110.86	128.69	-38.551	PHE
A417	108.2	129.13	-41.431	VAL
A418	108.89	131.82	-44.041	ASN
A419	105.56	133.53	-44.001	THR
A420	104.49	135.7	-40.881	PRO
A421	102.62	136.27	-38.451	PRO
A422	104.01	133.65	-35.891	LEU
A423	102.44	131.52	-33.081	VAL
A424	103.42	133.18	-29.611	LYS
A425	102.79	133.12	-25.751	LEU
A426	100.63	136.31	-25.511	TRP
A427	101.46	137.52	-21.971	TYR
A428	104.15	136.92	-19.311	GLN
A429	104.06	137.45	-15.551	LEU
A430	106.48	139.38	-13.251	GLU
A431	109.42	137.77	-11.281	LYS
A432	109.46	140.241	-8.461	GLU
A433	106.43	141.991	-6.751	PRO
A434	105.91	145.391	-8.211	ILE
A435	107.49	148.641	-6.991	VAL
A436	105.16	151.551	-7.641	GLY
A437	101.93	149.481	-7.791	ALA
A438	98.8	148.471	-5.891	GLU
A439	98.43	145.171	-4.091	THR
A440	95.1	143.441	-4.031	PHE
A441	94.44	140.611	-1.371	TYR
A442	91.44	138.42	-2.651	VAL
A443	88.91	135.93	-1.341	ASP
A444	85.56	134.24	-2.431	GLY
A445	83.09	131.94	-0.711	ALA
A446	80.09	129.76	-1.701	ALA
A447	77.21	127.52	-0.581	ASN
A448	77.51	123.71	-1.471	ARG
A449	73.99	122.99	-2.481	GLU
A450	72.3	126.35	-3.361	THR
A451	75.4	127.7	-5.211	LYS
A452	75.17	131.29	-3.751	LEU
A453	78.43	133.04	-2.911	GLY
A454	80.6	136.13	-2.721	LYS
A455	83.85	137.5	-4.171	ALA
A456	85.88	140.391	-2.811	GLY
A457	89.23	142.251	-2.081	TYR
A458	91.22	144.691	0.06	VAL
A459	93.93	146.991	-1.261	THR
A460	97.02	148.481	0.38	ASN
A461	95.47	151.901	-0.581	LYS
A462	92.73	151.511	2.12	GLY
A463	90.07	150.691	-0.511	ARG
A464	87.9	147.441	-0.011	GLN
A465	84.94	145.721	-1.901	LYS
A466	82.73	142.481	-2.071	VAL
A467	79.9	141.241	-4.461	VAL
A468	77.05	138.67	-3.901	PRO
A469	76.97	135.79	-6.601	LEU
A470	74.87	132.7	-7.771	THR
A471	75.59	129.43	-9.691	ASN
A472	79.1	129.05	-8.241	THR
A473	81.62	127.22	-6.111	THR
A474	84.32	127.97	-3.541	ASN
A475	86.89	127.3	-6.361	GLN
A476	85.12	129.54	-9.051	LYS
A477	84.47	132.4	-6.471	THR
A478	88.23	132.55	-5.771	GLU
A479	88.79	133.3	-9.571	LEU
A480	85.9	135.9	-9.731	GLN
A481	87.68	137.83	-6.861	ALA
A482	90.93	137.75	-9.121	ILE
A483	88.79	138.83	-12.201	TYR
A484	87.55	141.701	-9.821	LEU
A485	91.14	142.511	-8.991	ALA
A486	92.2	142.401	-12.671	LEU
A487	89.15	144.771	-13.481	GLN
A488	89.16	147.531	-10.781	ASP
A489	92.97	148.151	-11.331	SER
A490	95.37	150.311	-13.391	GLY
A491	98.01	149.081	-15.951	LEU
A492	100.09	147.401	-13.061	GLU
A493	98.86	144.931	-10.341	VAL
A494	100.07	142.761	-7.431	ASN
A495	97.55	140.131	-6.261	ILE
A496	97.62	137.75	-3.111	VAL
A497	95.37	134.56	-3.021	THR
A498	95.3	131.35	-0.881	ASP
A499	93.73	129.2	-3.731	SER
A500	96.23	126.98	-5.551	GLN
A501	93.24	126.01	-8.071	TYR
A502	92.75	129.58	-9.201	ALA
A503	96.48	130.47	-9.401	LEU
A504	97.17	127.32	-11.401	GLY
A505	95.03	128.64	-14.331	ILE
A506	97.01	131.87	-14.801	ILE
A507	100.45	130.12	-14.301	GLN
A508	99.68	127.94	-17.371	ALA
A509	99.41	131.02	-19.561	GLN
A510	96.35	130.09	-21.761	PRO
A511	94.9	132.5	-24.431	ASP
A512	91.7	130.53	-25.151	LYS
A513	89.21	129.48	-22.461	SER
A514	85.56	127.97	-22.791	GLU
A515	84.0	130.23	-20.001	SER
A516	83.31	134.08	-20.261	GLU
A517	84.76	134.75	-16.821	LEU
A518	88.07	133.5	-18.111	VAL
A519	88.21	135.09	-21.641	ASN
A520	87.68	138.39	-19.681	GLN
A521	90.54	137.51	-17.261	ILE
A522	92.78	136.89	-20.371	ILE
A523	91.78	140.261	-21.851	GLU
A524	93.21	141.951	-18.721	GLN
A525	96.31	139.55	-18.481	LEU
A526	97.19	140.971	-22.091	ILE
A527	96.2	144.591	-21.301	LYS
A528	98.32	145.261	-18.121	LYS
A529	102.16	145.961	-18.311	GLU
A530	103.11	144.371	-14.891	LYS
A531	101.16	141.411	-13.291	VAL
A532	102.23	139.58	-10.101	TYR
A533	100.57	136.73	-8.161	LEU
A534	101.57	135.71	-4.641	ALA
A535	100.42	132.69	-2.611	TRP
A536	99.96	132.08	1.19	VAL
A537	98.85	129.13	3.35	PRO
A538	95.1	129.43	4.29	ALA
A539	93.65	130.38	7.77	HIS
A540	97.01	131.23	9.31	LYS
A541	96.5	134.9	10.32	GLY
A542	98.37	136.4	7.19	ILE
A543	98.11	140.161	6.67	GLY
A544	95.58	141.161	4.08	GLY
A545	94.5	137.36	3.68	ASN
A546	92.8	137.48	7.09	GLU
A547	91.12	140.991	6.16	GLN
A548	89.6	139.971	2.81	VAL
A549	88.22	136.7	4.37	ASP
A550	86.69	138.94	7.18	LYS
A551	85.04	141.071	4.5	LEU
A552	83.75	138.02	2.58	VAL
A553	82.46	136.74	5.92	SER
A554	80.35	139.991	6.37	ALA
B5	112.42	69.31	-23.221	ILE
B6	112.29	69.03	-19.351	GLU
B7	111.89	72.36	-17.511	THR
B8	110.73	74.45	-14.461	VAL
B9	106.94	74.77	-15.121	PRO
B10	105.74	78.54	-14.861	VAL
B11	102.19	79.86	-14.041	LYS
B12	100.18	83.01	-14.571	LEU
B13	98.14	84.66	-11.811	LYS
B14	95.01	83.05	-10.251	PRO
B15	92.43	82.5	-13.111	GLY
B16	94.25	85.02	-15.341	MET
B17	95.15	84.84	-19.041	ASP
B18	98.0	85.92	-21.491	GLY
B19	99.02	89.53	-22.481	PRO
B20	97.78	91.43	-25.731	LYS
B21	100.0	94.53	-25.721	VAL
B22	99.88	96.39	-29.071	LYS
B23	103.01	97.11	-31.261	GLN
B24	104.19	100.68	-31.871	TRP
B25	105.51	102.05	-35.191	PRO
B26	109.17	102.95	-35.551	LEU
B27	111.83	104.44	-38.011	THR
B28	113.18	102.35	-40.931	GLU
B29	116.77	101.67	-39.591	GLU
B30	115.25	100.66	-36.231	LYS
B31	112.71	98.25	-37.771	ILE
B32	115.78	96.71	-39.691	LYS
B33	117.66	96.44	-36.271	ALA
B34	114.52	94.56	-34.851	LEU
B35	114.59	91.98	-37.681	VAL
B36	118.49	91.78	-37.931	GLU
B37	119.03	90.98	-34.181	ILE
B38	116.06	88.52	-34.361	CYS
B39	117.71	86.84	-37.441	THR
B40	121.02	86.19	-35.631	GLU
B41	119.21	85.04	-32.421	MET
B42	117.0	82.58	-34.451	GLU
B43	120.21	81.21	-36.131	LYS
B44	121.4	80.27	-32.621	GLU
B45	117.86	79.21	-31.901	GLY
B46	116.96	81.41	-28.821	LYS
B47	113.66	82.6	-30.431	ILE
B48	111.25	80.71	-32.871	SER
B49	108.43	81.52	-35.291	LYS
B50	104.71	81.1	-34.301	ILE
B51	101.29	80.5	-36.071	GLY
B52	97.9	82.27	-35.601	PRO
B53	96.96	79.52	-32.961	GLU
B54	98.72	81.96	-30.611	ASN
B55	96.75	85.23	-29.761	PRO
B56	99.33	87.1	-27.591	TYR
B57	101.75	89.97	-27.861	ASN
B58	104.3	92.01	-25.891	THR
B59	105.99	95.01	-27.771	PRO
B60	109.65	95.4	-29.061	VAL
B61	111.92	98.25	-29.951	PHE
B62	115.7	98.82	-30.351	ALA
B63	118.14	101.68	-29.291	ILE
B64	121.77	102.6	-30.121	LYS
B65	124.41	101.89	-27.381	LYS
B66	126.64	104.69	-25.851	LYS
B67	130.24	103.52	-26.661	ASP
B68	129.5	101.51	-29.891	SER
B69	126.44	102.94	-31.811	THR
B70	125.46	99.2	-32.411	LYS
B71	121.81	98.23	-31.711	TRP
B72	120.28	96.27	-28.871	ARG
B73	116.6	94.99	-28.591	LYS
B74	114.41	96.21	-25.621	LEU
B75	110.92	95.0	-24.721	VAL
B76	107.9	96.08	-22.641	ASP
B77	107.1	93.12	-20.391	PHE
B78	104.81	95.07	-17.811	ARG
B79	101.68	93.08	-18.731	GLU
B80	103.61	89.75	-18.891	LEU
B81	105.08	90.59	-15.541	ASN
B82	101.96	91.67	-13.681	LYS
B83	100.15	88.61	-15.201	ARG
B84	102.72	86.23	-13.721	THR
B85	102.2	84.87	-10.221	GLN
B86	104.05	86.22	-7.111	ASP
B87	104.12	82.71	-5.261	PHE
B88	107.06	80.3	-6.421	TRP
B89	108.59	76.91	-5.141	GLU
B90	111.61	76.86	-7.561	VAL
B91	112.49	80.16	-5.541	GLN
B92	114.96	79.34	-2.821	LEU
B93	113.66	82.52	-1.151	GLY
B94	113.11	86.19	-1.641	ILE
B95	115.7	88.89	-2.541	PRO
B96	116.23	91.84	-0.031	HIS
B97	118.51	94.93	-0.611	PRO
B98	120.08	94.53	2.95	ALA
B99	123.73	95.3	3.29	GLY
B100	124.53	97.15	0.06	LEU
B101	124.56	100.81	1.38	LYS
B102	127.42	100.05	3.99	LYS
B103	129.69	98.94	1.03	LYS
B104	132.49	101.05	-0.681	LYS
B105	130.86	100.35	-4.111	SER
B106	128.21	98.06	-5.741	VAL
B107	128.67	96.39	-9.131	THR
B108	125.57	96.03	-11.221	VAL
B109	126.43	92.6	-12.671	LEU
B110	124.48	91.47	-15.891	ASP
B111	122.87	87.87	-16.181	VAL
B112	120.7	88.42	-19.261	GLY
B113	122.81	86.06	-21.511	ASP
B114	122.67	83.25	-18.901	ALA
B115	118.92	83.75	-18.811	TYR
B116	119.16	83.7	-22.691	PHE
B117	120.59	80.08	-22.611	SER
B118	118.3	78.19	-19.861	VAL
B119	115.3	76.77	-21.761	PRO
B120	111.86	78.2	-20.891	LEU
B121	108.78	76.11	-20.091	ASP
B122	107.53	74.71	-23.491	GLU
B123	103.99	75.71	-22.191	ASP
B124	104.58	79.28	-21.051	PHE
B125	106.53	80.59	-24.171	ARG
B126	103.16	81.48	-26.021	LYS
B127	102.93	84.33	-23.401	TYR
B128	106.17	85.95	-24.461	THR
B129	105.18	86.42	-28.181	ALA
B130	106.19	89.53	-30.331	PHE
B131	105.54	90.83	-33.871	THR
B132	107.94	92.61	-36.251	ILE
B133	105.94	95.02	-38.481	PRO
B134	106.4	96.68	-41.981	SER
B135	106.98	100.13	-43.451	ILE
B136	103.72	101.35	-45.131	ASN
B137	101.9	97.85	-45.381	ASN
B138	104.04	97.11	-48.531	GLU
B139	105.1	93.68	-47.021	THR
B140	103.32	91.49	-44.261	PRO
B141	104.98	91.34	-40.811	GLY
B142	106.46	88.19	-38.961	ILE
B143	105.74	86.71	-35.331	ARG
B144	108.22	85.13	-32.791	TYR
B145	108.19	83.76	-29.321	GLN
B146	111.08	83.27	-26.751	TYR
B147	112.8	79.78	-26.381	ASN
B148	114.7	80.83	-23.231	VAL
B149	113.97	83.09	-20.221	LEU
B150	113.31	86.88	-20.971	PRO
B151	114.99	89.99	-19.541	GLN
B152	112.98	92.65	-17.451	GLY
B153	110.74	90.03	-15.911	TRP
B154	110.55	88.8	-12.281	LYS
B155	110.46	85.05	-13.361	GLY
B156	114.05	84.84	-14.601	SER
B157	115.92	85.57	-11.251	PRO
B158	113.51	83.06	-9.521	ALA
B159	114.01	80.12	-11.961	ILE
B160	117.69	80.99	-12.241	PHE
B161	118.16	81.17	-8.311	GLN
B162	119.32	77.49	-8.021	SER
B163	121.71	78.0	-11.061	SER
B164	123.42	80.75	-8.911	MET
B165	123.25	79.87	-5.141	THR
B166	125.52	76.89	-6.011	LYS
B167	128.37	79.33	-6.881	ILE
B168	127.3	82.35	-4.561	LEU
B169	127.63	80.43	-1.321	GLU
B170	131.14	78.86	-2.181	PRO
B171	132.31	82.34	-2.921	PHE
B172	130.86	83.96	0.41	LYS
B173	132.74	81.17	2.4	LYS
B174	135.99	82.55	0.96	GLN
B175	134.96	86.21	0.78	ASN
B176	132.78	87.04	3.95	PRO
B177	133.48	90.72	2.77	ASP
B178	130.98	90.44	-0.261	ILE
B179	127.28	91.32	-0.141	VAL
B180	124.88	89.86	-3.011	ILE
B181	121.35	91.03	-4.221	TYR
B182	119.2	89.97	-7.271	GLN
B183	116.58	91.92	-9.231	TYR
B184	115.18	91.37	-12.731	MET
B185	118.3	90.72	-14.901	ASP
B186	120.95	92.08	-12.571	ASP
B187	122.94	91.09	-9.541	LEU
B188	124.06	94.01	-7.281	TYR
B189	127.41	93.0	-5.561	VAL
B190	128.55	95.02	-2.531	GLY
B191	132.43	95.11	-2.291	SER
B192	135.2	96.94	-0.301	ASP
B193	138.16	96.28	-2.681	LEU
B194	141.181	97.69	-4.601	GLU
B195	140.961	98.01	-8.551	ILE
B196	143.071	94.88	-9.051	GLY
B197	140.801	92.85	-6.841	GLN
B198	137.55	94.66	-8.141	HIS
B199	138.35	93.2	-11.591	ARG
B200	139.72	89.76	-10.521	THR
B201	136.97	88.89	-8.011	LYS
B202	134.09	89.84	-10.321	ILE
B203	135.9	87.96	-13.261	GLU
B204	136.01	84.87	-10.881	GLU
B205	132.26	85.18	-10.191	LEU
B206	131.4	85.52	-13.921	ARG
B207	133.6	82.6	-14.751	GLN
B208	132.1	80.51	-11.871	HIS
B209	128.52	81.24	-13.271	LEU
B210	129.85	80.1	-16.691	LEU
B211	131.72	76.91	-15.631	ARG
B212	129.53	75.87	-12.661	TRP
B213	126.32	78.02	-12.851	GLY
B214	125.27	76.96	-16.321	LEU
B215	124.63	73.23	-17.371	THR
B216	123.92	73.19	-21.151	THR
B217	126.04	71.35	-23.701	PRO
B218	126.48	74.34	-26.101	ASP
B219	129.92	75.97	-26.301	LYS
B220	130.76	79.32	-24.661	LYS
B221	133.65	81.96	-24.371	HIS
B222	134.79	82.52	-20.811	GLN
B223	137.71	85.07	-21.001	LYS
B224	134.98	87.62	-22.181	GLU
B225	135.74	91.34	-22.201	PRO
B226	134.04	93.24	-19.311	PRO
B227	132.22	95.61	-21.711	PHE
B228	129.47	92.94	-22.401	LEU
B229	128.69	91.48	-18.781	TRP
B230	130.37	93.73	-16.231	MET
B231	127.39	96.13	-16.211	GLY
B232	128.13	99.36	-14.231	TYR
B233	128.95	100.51	-10.641	GLU
B234	126.92	102.43	-7.891	LEU
B235	128.71	104.21	-4.951	HIS
B236	126.5	104.41	-1.751	PRO
B237	128.61	107.23	-0.141	ASP
B238	126.88	109.41	-2.921	LYS
B239	123.31	107.93	-2.261	TRP
B240	122.88	110.63	0.5	THR
B241	119.56	112.6	0.79	VAL
B242	119.89	116.29	-0.151	GLN
B243	119.24	118.3	3.05	PRO
B244	117.16	121.54	2.64	ILE
B245	118.23	125.12	3.35	VAL
B246	116.74	128.71	3.78	LEU
B247	117.74	132.11	2.25	PRO
B248	119.43	134.92	4.21	GLU
B249	118.58	138.57	3.95	LYS
B250	120.04	141.751	5.6	ASP
B251	116.53	143.221	5.35	SER
B252	113.23	141.411	4.75	TRP
B253	110.14	142.441	2.66	THR
B254	106.52	141.341	2.96	VAL
B255	107.18	138.96	0.03	ASN
B256	110.43	137.46	1.48	ASP
B257	108.34	136.54	4.65	ILE
B258	105.3	135.12	2.61	GLN
B259	107.67	132.97	0.42	LYS
B260	109.48	131.6	3.54	LEU
B261	106.17	130.75	5.4	VAL
B262	104.9	129.06	2.11	GLY
B263	108.08	126.98	1.73	LYS
B264	108.06	125.99	5.46	LEU
B265	104.31	125.0	5.05	ASN
B266	105.54	122.84	2.15	TRP
B267	108.7	121.56	4.06	ALA
B268	106.51	120.37	7.11	SER
B269	105.43	117.26	5.06	GLN
B270	109.1	116.35	4.59	ILE
B271	110.84	117.39	7.96	TYR
B272	109.09	117.18	11.4	PRO
B273	108.98	120.22	13.91	GLY
B274	108.83	122.79	11.08	ILE
B275	107.09	125.8	12.72	LYS
B276	105.45	128.97	11.34	VAL
B277	104.22	130.4	14.72	ARG
B278	106.06	133.76	14.87	GLN
B279	106.95	134.22	11.07	LEU
B280	103.05	134.34	10.7	SER
B281	102.83	137.29	13.25	LYS
B282	105.04	139.49	11.14	LEU
B283	102.52	139.37	8.21	LEU
B284	99.99	141.791	9.58	ARG
B285	97.7	144.311	7.91	GLY
B286	97.06	145.041	4.14	THR
B287	100.82	146.081	3.7	LYS
B288	102.39	146.081	0.21	ALA
B289	104.45	143.331	-1.281	LEU
B290	107.64	145.471	-1.451	THR
B291	107.41	147.201	2.04	GLU
B292	110.19	146.701	4.6	VAL
B293	108.7	145.271	7.9	ILE
B294	110.36	145.111	11.43	PRO
B295	111.37	141.721	12.56	LEU
B296	111.11	140.331	16.18	THR
B297	113.6	138.47	18.4	GLU
B298	111.06	135.57	18.68	GLU
B299	110.51	135.54	14.75	ALA
B300	114.24	135.91	14.0	GLU
B301	114.72	132.98	16.46	LEU
B302	112.05	130.88	14.59	GLU
B303	114.12	131.54	11.4	LEU
B304	117.19	130.09	13.24	ALA
B305	115.19	127.09	14.58	GLU
B306	113.65	125.97	11.33	ASN
B307	117.11	126.24	9.64	ARG
B308	118.36	123.75	12.36	GLU
B309	115.68	121.14	11.07	ILE
B310	116.19	121.43	7.23	LEU
B311	119.92	120.76	7.38	LYS
B312	119.95	116.99	8.35	GLU
B313	120.45	114.38	5.59	PRO
B314	117.32	112.24	6.53	VAL
B315	114.29	110.51	4.8	HIS
B316	110.67	111.51	5.75	GLY
B317	108.09	109.11	7.32	VAL
B318	108.53	105.33	7.39	TYR
B319	108.51	103.02	4.29	TYR
B320	105.75	100.34	4.57	ASP
B321	106.78	97.22	2.45	PRO
B322	103.02	96.5	1.87	SER
B323	102.5	99.84	0.2	LYS
B324	103.73	100.78	-3.261	ASP
B325	106.03	103.72	-4.441	LEU
B326	105.01	106.75	-6.251	ILE
B327	107.17	109.68	-7.611	ALA
B328	106.58	113.2	-9.111	GLU
B329	109.15	115.25	-11.261	ILE
B330	109.04	118.94	-12.341	GLN
B331	111.32	120.62	-14.931	LYS
B332	113.22	123.86	-14.031	GLN
B333	115.18	126.18	-16.311	GLY
B334	116.53	124.42	-19.391	GLN
B335	117.36	120.96	-17.921	GLY
B336	117.05	120.81	-14.031	GLN
B337	114.61	118.53	-12.371	TRP
B338	112.95	118.96	-8.921	THR
B339	111.1	115.8	-7.551	TYR
B340	109.63	113.68	-4.761	GLN
B341	109.17	109.99	-3.801	ILE
B342	106.23	108.82	-1.581	TYR
B343	103.71	106.0	-0.781	GLN
B344	100.78	108.28	0.52	GLU
B345	99.46	111.89	-0.321	PRO
B346	101.25	114.84	1.39	PHE
B347	103.7	112.48	3.53	LYS
B348	107.15	112.3	1.85	ASN
B349	109.86	109.52	1.8	LEU
B350	112.35	111.52	-0.381	LYS
B351	112.58	115.06	-1.991	THR
B352	115.2	116.38	-4.451	GLY
B353	116.65	118.19	-7.661	LYS
B354	118.87	116.9	-10.541	TYR
B355	120.95	118.83	-13.161	ALA
B356	123.15	118.02	-16.301	ARG
B357	122.53	114.27	-15.901	MET
B358	125.46	112.23	-17.471	ARG
B359	126.03	115.46	-19.471	GLY
B360	122.4	115.72	-20.761	ALA
B361	120.8	119.24	-20.331	HIS
B362	119.41	120.02	-23.791	THR
B363	116.77	117.22	-24.631	ASN
B364	113.84	116.94	-22.281	ASP
B365	113.02	113.23	-23.171	VAL
B366	116.57	111.93	-22.891	LYS
B367	116.67	113.69	-19.431	GLN
B368	113.1	112.76	-18.261	LEU
B369	113.6	109.06	-18.971	THR
B370	117.05	109.4	-17.211	GLU
B371	115.66	110.96	-13.971	ALA
B372	113.05	108.08	-13.831	VAL
B373	115.87	105.45	-14.301	GLN
B374	118.08	107.09	-11.471	LYS
B375	115.07	107.1	-9.021	ILE
B376	114.06	103.49	-9.891	THR
B377	117.66	102.3	-9.411	THR
B378	117.78	103.97	-5.921	GLU
B379	114.24	102.45	-5.311	SER
B380	115.58	99.0	-6.171	ILE
B381	118.86	99.18	-3.911	VAL
B382	116.99	100.92	-0.991	ILE
B383	113.43	99.62	-0.831	TRP
B384	113.28	96.81	-3.491	GLY
B385	110.19	98.28	-5.401	LYS
B386	109.66	99.94	-8.841	THR
B387	107.6	103.21	-8.461	PRO
B388	104.6	105.09	-10.291	LYS
B389	105.95	108.36	-11.871	PHE
B390	103.68	111.47	-12.341	LYS
B391	104.83	113.39	-15.481	LEU
B392	104.74	117.0	-16.751	PRO
B393	104.21	115.88	-20.381	ILE
B394	101.92	115.23	-23.321	GLN
B395	101.36	111.45	-24.021	LYS
B396	102.23	112.16	-27.701	GLU
B397	105.66	113.62	-26.841	THR
B398	106.36	110.55	-24.531	TRP
B399	105.07	107.62	-26.681	GLU
B400	107.07	108.88	-29.851	THR
B401	110.36	109.18	-27.771	TRP
B402	110.68	106.86	-24.631	TRP
B403	111.47	104.01	-27.141	THR
B404	114.51	106.08	-28.161	GLU
B405	115.99	107.05	-24.701	TYR
B406	114.88	104.21	-22.281	TRP
B407	117.85	101.87	-21.391	GLN
B408	116.39	99.72	-18.521	ALA
B409	115.03	96.2	-19.041	THR
B410	112.61	97.01	-16.071	TRP
B411	109.9	99.73	-16.781	ILE
B412	107.72	101.54	-14.031	PRO
B413	104.15	102.78	-14.471	GLU
B414	103.12	106.5	-14.881	TRP
B415	100.56	109.22	-15.151	GLU
B416	100.27	112.38	-17.371	PHE
B417	99.74	115.53	-15.171	VAL
B418	100.3	118.9	-16.911	ASN
B419	99.86	121.49	-13.921	THR
B420	102.32	124.28	-12.931	PRO
B421	104.9	123.02	-10.191	PRO
B422	103.93	123.69	-6.561	LEU
B423	107.58	124.9	-5.921	VAL
B424	106.33	127.94	-8.001	LYS
B425	104.27	128.93	-4.931	LEU
B426	107.45	130.26	-3.021	TRP
B427	110.34	130.3	-5.731	TYR
B428	112.98	129.76	-2.801	GLN