A307	124.76	38.7	11.59	GLN
A308	122.89	41.53	9.84	LEU
A309	119.05	41.38	10.08	ARG
A310	117.4	40.71	6.68	PRO
A311	116.55	44.43	6.39	TYR
A312	120.13	45.33	7.26	GLN
A313	121.56	42.67	4.97	MET
A314	119.66	43.65	1.82	GLU
A315	121.45	47.01	2.25	VAL
A316	124.98	45.9	3.28	ALA
A317	124.92	43.51	0.33	GLN
A318	126.01	45.73	-2.6	PRO
A319	128.68	47.21	-0.26	ALA
A320	129.91	43.79	0.8	LEU
A321	129.87	43.28	-3.01	GLU
A322	132.26	46.1	-3.73	GLY
A323	129.7	48.64	-4.87	LYS
A324	129.34	52.38	-4.09	ASN
A325	126.03	53.0	-2.29	ILE
A326	124.17	55.52	-0.16	ILE
A327	122.36	53.5	2.53	ILE
A328	119.02	55.02	3.61	CYS
A329	118.49	53.69	7.14	LEU
A330	117.35	55.95	10.02	PRO
A331	119.29	56.91	13.16	THR
A332	117.97	54.22	15.51	GLY
A333	117.26	51.22	13.16	SER
A334	120.53	49.55	12.25	GLY
A335	122.26	52.66	10.98	LYS
A336	125.81	51.92	12.32	THR
A337	125.89	48.07	12.33	ARG
A338	126.18	48.19	8.46	VAL
A339	129.35	50.24	8.47	ALA
A340	131.21	48.08	11.01	VAL
A341	130.22	44.94	9.12	TYR
A342	131.38	46.43	5.75	ILE
A343	134.48	47.83	7.34	ALA
A344	135.53	44.33	8.48	LYS
A345	134.75	42.76	5.07	ASP
A346	137.28	45.12	3.47	HIS
A347	140.02	44.18	5.99	LEU
A348	139.43	40.4	5.82	ASP
A349	139.77	40.66	1.95	LYS
A350	142.89	42.83	2.18	LYS
A351	144.3	40.16	4.65	LYS
A352	143.22	37.15	2.55	LYS
A353	144.94	38.67	-0.57	ALA
A354	148.13	39.5	1.44	SER
A355	148.2	43.25	0.94	GLU
A356	147.87	46.3	3.26	PRO
A357	144.22	47.46	3.94	GLY
A358	142.59	50.54	5.49	LYS
A359	139.23	51.9	6.43	VAL
A360	138.66	55.67	6.85	ILE
A361	135.47	57.1	8.52	VAL
A362	134.6	60.67	7.74	LEU
A363	132.48	63.04	9.84	VAL
A364	131.02	66.54	9.71	ASN
A365	132.37	68.21	12.91	LYS
A366	135.04	67.13	15.35	VAL
A367	132.79	66.4	18.34	LEU
A368	131.14	63.59	16.32	LEU
A369	134.35	61.58	16.04	VAL
A370	134.63	60.34	19.6	GLU
A371	131.57	58.11	20.37	GLN
A372	131.49	56.97	16.69	LEU
A373	134.96	55.54	17.42	PHE
A374	134.79	54.34	21.01	ARG
A375	131.11	53.13	21.23	LYS
A376	129.79	52.59	17.63	GLU
A377	132.99	51.02	16.24	PHE
A378	135.45	49.9	19.01	GLN
A379	133.15	47.36	20.76	PRO
A380	132.44	45.6	17.39	PHE
A381	135.9	45.54	15.86	LEU
A382	138.74	45.65	18.38	LYS
A383	139.16	41.87	18.58	LYS
A384	140.16	41.61	14.89	TRP
A385	141.69	45.0	13.9	TYR
A386	143.2	48.22	15.27	ARG
A387	140.72	51.09	15.64	VAL
A388	141.47	54.74	16.45	ILE
A389	139.31	57.85	16.54	GLY
A390	141.29	61.15	16.22	LEU
A391	139.87	62.57	19.4	SER
A392	142.21	61.79	22.4	GLY
A393	143.52	64.62	24.56	ASP
A394	147.31	64.14	24.06	THR
A395	146.61	63.2	20.42	GLN
A396	147.28	66.82	19.4	LEU
A397	150.97	65.7	19.27	LYS
A398	150.55	63.65	16.02	ILE
A399	148.76	63.9	12.64	SER
A400	146.1	62.17	10.49	PHE
A401	148.81	60.23	8.57	PRO
A402	150.4	59.16	11.94	GLU
A403	147.1	57.47	13.03	VAL
A404	146.72	56.01	9.48	VAL
A405	150.25	54.52	10.11	LYS
A406	149.29	53.03	13.49	SER
A407	145.72	51.68	12.8	CYS
A408	143.57	49.76	10.3	ASP
A409	140.33	51.73	11.02	ILE
A410	140.49	55.54	11.58	ILE
A411	137.67	58.01	12.37	ILE
A412	138.27	61.72	11.5	SER
A413	136.59	64.86	10.12	THR
A414	136.06	65.34	6.39	ALA
A415	138.15	68.52	6.44	GLN
A416	141.15	66.65	7.89	ILE
A417	141.44	64.18	5.05	LEU
A418	141.06	67.1	2.63	GLU
A419	144.01	68.99	4.24	ASN
A420	145.83	65.71	4.03	SER
A421	145.16	65.1	0.35	LEU
A422	146.04	68.74	-0.38	LEU
A423	149.26	67.54	1.31	ASN
A424	149.0	70.34	3.89	LEU
A425	149.77	67.61	6.45	GLU
A426	152.27	64.82	5.7	ASN
A427	153.12	63.71	9.31	GLY
A428	156.5	62.09	9.85	GLU
A429	156.91	61.02	6.21	ASP
A430	155.27	61.49	2.78	ALA
A431	151.6	61.66	3.93	GLY
A432	148.66	59.9	2.22	VAL
A433	147.16	59.11	-1.2	GLN
A434	143.98	57.58	-2.69	LEU
A435	145.65	54.13	-3.0	SER
A436	146.33	53.96	0.82	ASP
A437	142.7	53.1	1.78	PHE
A438	140.08	50.69	0.39	SER
A439	136.93	52.25	1.98	LEU
A440	135.71	55.74	2.73	ILE
A441	132.64	55.71	5.05	ILE
A442	130.65	58.91	5.48	ILE
A443	128.09	59.76	8.21	ASP
A444	125.09	62.12	8.14	GLU
A445	125.4	63.1	4.47	CYS
A446	122.29	65.05	3.6	HIS
A447	123.43	68.03	1.43	HIS
A448	126.28	68.87	-0.89	THR
A449	128.84	71.73	-1.35	ASN
A450	131.53	73.02	-3.74	LYS
A451	134.32	73.34	-1.17	GLU
A452	133.14	71.87	2.16	THR
A453	130.91	69.07	3.6	VAL
A454	130.16	67.03	1.32	TYR
A455	132.19	65.87	-0.5	ASN
A456	135.64	67.54	-0.14	ASN
A457	137.45	64.55	-1.59	ILE
A458	135.62	64.65	-4.97	MET
A459	138.21	67.01	-6.47	ARG
A460	140.71	64.21	-5.89	HIS
A461	138.56	61.21	-6.58	TYR
A462	136.97	62.18	-9.88	LEU
A463	140.19	63.52	-11.3	MET
A464	141.97	60.18	-10.53	GLN
A465	138.99	58.33	-12.18	LYS
A466	139.06	60.42	-15.39	LEU
A467	142.83	59.75	-15.46	LYS
A468	141.95	56.05	-15.1	ASN
A469	139.46	56.36	-17.96	ASN
A470	142.0	58.1	-20.25	ARG
A471	144.7	55.46	-19.24	LEU
A472	142.27	52.58	-19.78	LYS
A473	141.25	53.5	-23.37	LYS
A474	145.0	53.31	-24.06	GLU
A475	145.02	49.83	-22.56	ASN
A476	147.28	50.84	-19.6	LYS
A477	146.62	49.61	-16.04	PRO
A478	145.57	52.19	-13.38	VAL
A479	145.82	53.14	-9.67	ILE
A480	142.83	51.65	-7.81	PRO
A481	140.42	53.88	-5.97	LEU
A482	138.58	53.82	-2.68	PRO
A483	135.06	52.42	-2.4	GLN
A484	132.54	54.95	-1.15	ILE
A485	129.91	54.23	1.54	LEU
A486	127.38	57.03	2.53	GLY
A487	125.0	56.64	5.56	LEU
A488	122.05	59.01	5.21	THR
A489	119.09	59.67	7.54	ALA
A490	117.85	61.65	5.49	SER
A491	118.54	64.08	2.53	PRO
A492	115.26	66.08	2.41	GLY
A493	114.24	67.93	-0.85	VAL
A494	117.05	70.51	-1.12	GLY
A495	116.34	74.21	-0.6	GLY
A496	113.51	74.44	-3.23	ALA
A497	110.47	72.14	-2.82	THR
A498	109.65	70.59	-6.17	LYS
A499	109.84	66.88	-7.18	GLN
A500	112.29	67.35	-10.08	ALA
A501	114.6	69.42	-7.82	LYS
A502	114.44	66.91	-4.97	ALA
A503	115.4	64.36	-7.67	GLU
A504	118.34	66.62	-8.64	GLU
A505	119.26	66.89	-4.91	HIS
A506	119.43	63.09	-4.67	ILE
A507	121.46	63.07	-7.94	LEU
A508	123.9	65.64	-6.52	LYS
A509	124.32	63.45	-3.34	LEU
A510	124.91	60.33	-5.5	CYS
A511	127.47	62.17	-7.79	ALA
A512	129.38	63.4	-4.67	ASN
A513	129.61	59.78	-3.46	LEU
A514	130.24	58.21	-6.91	ASP
A515	127.27	55.96	-6.24	ALA
A516	125.94	53.11	-8.31	PHE
A517	122.63	53.8	-6.49	THR
A518	120.83	54.92	-3.39	ILE
A519	119.68	51.95	-1.43	LYS
A520	116.44	51.32	0.58	THR
A521	114.84	48.35	2.33	VAL
A522	112.58	46.71	-0.34	LYS
A523	112.34	43.11	0.72	GLU
A524	111.95	43.13	4.57	ASN
A525	110.02	46.43	4.97	LEU
A526	107.95	45.41	8.03	ASP
A527	111.2	44.63	9.87	GLN
A528	112.42	48.24	9.34	LEU
A529	108.93	49.38	10.48	LYS
A530	109.18	47.35	13.67	ASN
A531	111.43	50.02	15.2	GLN
A532	110.47	53.65	15.92	ILE
A533	112.69	56.78	16.62	GLN
A534	110.52	59.89	16.02	GLU
A535	109.08	62.17	18.75	PRO
A536	105.45	62.75	19.44	CYS
A537	105.0	66.25	17.95	LYS
A538	103.1	68.89	20.05	LYS
A539	101.77	72.3	18.89	PHE
A540	101.46	75.02	21.58	ALA
A541	100.96	78.76	22.12	ILE
A542	103.42	80.96	24.09	ALA
A543	102.42	82.83	27.25	ASP
A544	101.72	86.56	27.09	ALA
A545	100.24	89.44	29.15	THR
A546	97.23	91.43	27.85	ARG
A547	98.62	94.97	27.62	GLU
A548	102.12	96.3	28.06	ASP
A549	102.41	99.92	29.28	PRO
A550	106.2	100.06	28.81	PHE
A551	106.04	98.87	25.11	LYS
A552	103.15	101.26	24.69	GLU
A553	105.43	104.1	25.85	LYS
A554	108.2	103.24	23.38	LEU
A555	105.5	103.17	20.71	LEU
A556	104.36	106.63	21.8	GLU
A557	108.04	107.83	21.61	ILE
A558	108.35	106.41	18.05	MET
A559	105.07	107.99	17.08	THR
A560	106.14	111.48	18.32	ARG
A561	109.27	111.22	16.12	ILE
A562	107.65	109.77	13.06	GLN
A563	104.84	112.32	13.14	THR
A564	107.36	115.18	13.56	TYR
A565	109.08	114.17	10.28	CYS
A566	105.69	112.93	8.97	GLN
A567	106.93	109.63	7.5	MET
A568	104.89	106.76	6.18	SER
A569	106.17	103.17	6.93	PRO
A570	102.67	101.5	6.49	MET
A571	104.21	98.96	8.95	SER
A572	104.17	97.62	12.45	ASP
A573	106.9	98.06	15.04	PHE
A574	109.22	95.57	16.74	GLY
A575	109.87	93.8	13.46	THR
A576	112.82	93.06	11.12	GLN
A577	110.67	94.29	8.28	PRO
A578	110.43	97.64	10.15	TYR
A579	114.18	97.51	10.78	GLU
A580	114.32	97.11	6.95	GLN
A581	112.14	100.14	6.05	TRP
A582	114.07	102.36	8.48	ALA
A583	117.34	101.25	6.84	ILE
A584	116.0	102.15	3.34	GLN
A585	114.5	105.48	4.48	MET
A586	117.75	106.56	6.12	GLU
A587	119.57	105.47	2.97	LYS
A588	117.45	107.17	0.34	LYS
A589	117.72	110.33	2.43	ALA
A590	121.53	110.1	2.82	ALA
A591	121.56	109.51	-1.0	LYS
A592	119.12	112.48	-1.59	GLU
A593	121.03	114.97	0.67	GLY
A594	118.5	115.13	3.55	ASN
A595	120.07	115.33	7.0	ARG
A596	116.66	115.83	8.79	LYS
A597	114.98	112.73	7.26	GLU
A598	118.06	110.5	7.54	ARG
A599	118.63	111.23	11.24	VAL
A600	114.97	110.69	12.19	CYS
A601	114.8	107.26	10.58	ALA
A602	118.01	106.13	12.19	GLU
A603	116.83	107.15	15.68	HIS
A604	113.53	105.35	15.02	LEU
A605	115.51	102.32	13.92	ARG
A606	117.24	102.51	17.37	LYS
A607	113.96	102.31	19.43	TYR
A608	112.76	99.52	17.13	ASN
A609	115.65	97.41	18.37	GLU
A610	114.24	97.6	21.91	ALA
A611	110.83	96.52	20.53	LEU
A612	112.28	93.57	18.58	GLN
A613	113.47	92.0	21.91	ILE
A614	110.24	92.77	23.78	ASN
A615	108.79	89.19	24.02	ASP
A616	111.9	87.39	25.34	THR
A617	114.43	89.85	26.94	ILE
A618	113.9	91.97	30.1	ARG
A619	112.38	95.5	30.03	MET
A620	115.58	96.69	31.75	ILE
A621	117.83	95.46	28.89	ASP
A622	115.67	97.24	26.34	ALA
A623	116.12	100.3	28.51	TYR
A624	119.86	99.74	28.66	THR
A625	119.78	99.27	24.81	HIS
A626	118.57	102.88	24.65	LEU
A627	120.16	104.26	27.84	GLU
A628	123.63	103.5	26.53	THR
A629	123.05	105.18	23.19	PHE
A630	122.01	108.59	24.53	TYR
A631	124.86	108.65	27.1	ASN
A632	127.5	109.18	24.38	GLU
A633	125.18	111.51	22.57	GLU
A634	125.23	113.26	25.94	LYS
A635	129.03	113.27	26.26	ASP
A636	129.49	114.55	22.73	LYS
A637	127.34	117.59	23.7	LYS
A638	129.22	118.43	26.96	PHE
A639	130.31	121.95	25.85	ALA
A640	126.77	122.58	24.57	VAL
A641	124.41	121.64	27.45	ILE
A642	124.52	120.91	31.18	GLU
A643	121.51	118.51	31.35	ASP
A644	119.89	117.87	27.91	ASP
A645	118.55	120.97	26.19	SER
A646	120.22	124.33	25.55	ASP
A647	119.99	127.31	27.92	GLU
A648	121.07	130.98	27.61	GLY
A649	123.76	133.09	29.1	GLY
A650	124.82	135.72	26.56	ASP
A651	123.79	138.64	28.76	ASP
A652	127.23	138.1	30.41	GLU
A653	129.09	137.66	27.08	TYR
A654	128.01	140.63	24.97	CYS
A655	129.44	144.19	25.09	ASP
A656	129.8	147.2	22.68	GLY
A657	127.63	149.15	20.23	ASP
A658	128.46	147.27	17.07	GLU
A659	131.3	144.95	18.23	ASP
A660	130.01	141.41	17.6	GLU
A661	130.58	138.6	20.15	ASP
A662	129.24	135.67	18.12	ASP
A663	132.27	133.42	18.86	LEU
A664	132.56	134.66	22.51	LYS
A665	128.93	133.85	23.39	LYS
A666	127.75	130.47	24.79	PRO
A667	126.52	127.76	22.41	LEU
A668	123.1	126.55	21.38	LYS
A669	121.27	123.69	19.65	LEU
A670	119.21	123.31	16.44	ASP
A671	115.63	121.88	16.11	GLU
A672	116.41	118.16	15.56	THR
A673	119.88	118.05	17.17	ASP
A674	117.87	119.08	20.26	ARG
A675	114.58	117.18	20.03	PHE
A676	116.11	113.68	19.4	LEU
A677	118.03	113.77	22.7	MET
A678	115.44	115.89	24.54	THR
A679	112.58	113.39	23.89	LEU
A680	114.74	110.65	25.53	PHE
A681	115.45	112.87	28.55	PHE
A682	111.77	113.86	28.77	GLU
A683	110.85	110.28	29.42	ASN
A684	113.88	108.54	31.03	ASN
A685	112.66	108.95	34.64	LYS
A686	109.34	107.47	33.53	MET
A687	110.89	104.66	31.52	LEU
A688	113.18	103.58	34.38	LYS
A689	110.11	103.42	36.67	ARG
A690	108.15	101.4	34.0	LEU
A691	111.01	98.85	33.83	ALA
A692	112.12	98.37	37.45	GLU
A693	108.81	98.76	39.32	ASN
A694	105.54	96.74	39.54	PRO
A695	103.69	99.32	37.36	GLU
A696	101.41	96.83	35.57	TYR
A697	98.9	94.18	36.71	GLU
A698	101.25	91.24	36.02	ASN
A699	104.9	90.26	35.39	GLU
A700	106.32	90.46	31.88	LYS
A701	108.2	87.16	31.68	LEU
A702	105.73	84.22	31.72	THR
A703	106.85	81.59	29.17	LYS
A704	108.53	78.13	28.94	LEU
A705	108.5	77.21	32.64	ARG
A706	105.41	74.98	32.4	ASN
A707	106.37	73.66	28.97	THR
A708	109.17	71.5	30.49	ILE
A709	107.26	70.9	33.68	MET
A710	104.58	69.11	31.56	GLU
A711	107.15	66.86	29.89	GLN
A712	108.8	66.21	33.27	TYR
A713	105.27	65.25	34.59	THR
A714	104.84	62.75	31.65	ARG
A715	108.31	61.28	32.21	THR
A716	109.21	58.88	35.0	GLU
A717	113.02	59.4	35.08	GLU
A718	115.51	62.29	35.21	SER
A719	115.18	62.78	31.46	ALA
A720	117.05	65.2	29.17	ARG
A721	116.22	67.8	26.55	GLY
A722	116.76	71.24	24.98	ILE
A723	115.06	74.65	24.47	ILE
A724	116.03	76.03	20.95	PHE
A725	115.46	79.76	20.16	THR
A726	116.22	82.44	17.49	LYS
A727	118.95	84.32	19.35	THR
A728	121.95	84.03	21.69	ARG
A729	120.38	86.72	23.93	GLN
A730	117.17	84.62	24.16	SER
A731	119.2	81.45	24.76	ALA
A732	120.95	82.96	27.76	TYR
A733	117.83	84.88	28.91	ALA
A734	115.71	81.75	29.2	LEU
A735	118.44	79.96	31.17	SER
A736	118.33	82.79	33.7	GLN
A737	114.51	82.73	33.82	TRP
A738	114.15	78.94	34.33	ILE
A739	116.86	78.91	37.04	THR
A740	114.78	81.38	39.18	GLU
A741	111.62	80.15	40.97	ASN
A742	110.66	76.47	41.53	GLU
A743	110.05	73.84	39.95	LYS
A744	110.21	72.5	36.35	PHE
A745	111.05	69.81	37.59	ALA
A746	114.61	69.74	38.97	GLU
A747	116.39	72.25	36.66	VAL
A748	117.07	75.09	39.11	GLY
A749	120.83	74.54	39.41	VAL
A750	120.81	72.0	36.55	LYS
A751	120.04	74.25	33.52	ALA
A752	122.77	75.98	31.47	HIS
A753	123.12	77.5	28.01	HIS
A754	124.97	76.52	24.84	LEU
A755	126.11	78.63	21.87	ILE
A756	128.85	78.57	19.13	GLY
A757	132.32	80.07	19.04	ALA
A758	132.04	82.96	16.66	GLY
A759	131.02	86.53	16.18	HIS
A760	127.17	86.37	16.1	SER
A761	125.33	89.5	17.31	SER
A762	128.65	90.34	19.12	GLU
A763	127.06	88.19	21.97	PHE
A764	129.34	86.26	24.31	LYS
A765	130.3	82.97	22.58	PRO
A766	131.92	79.94	24.1	MET
A767	135.05	78.07	22.95	THR
A768	135.29	74.41	21.89	GLN
A769	136.35	72.99	25.33	ASN
A770	133.64	75.11	27.07	GLU
A771	131.07	73.61	24.54	GLN
A772	132.5	70.06	25.32	LYS
A773	132.38	70.72	29.1	GLU
A774	128.66	71.43	29.01	VAL
A775	128.28	68.26	26.87	ILE
A776	130.18	66.08	29.35	SER
A777	127.97	67.54	32.09	LYS
A778	124.86	66.52	29.93	PHE
A779	125.93	62.93	29.51	ARG
A780	128.57	61.54	31.95	THR
A781	127.96	59.88	35.31	GLY
A782	125.93	61.24	37.23	LYS
A783	124.34	63.9	34.95	ILE
A784	124.86	67.5	36.1	ASN
A785	122.6	69.31	33.58	LEU
A786	119.21	68.29	32.13	LEU
A787	118.12	71.28	30.03	ILE
A788	120.26	73.08	27.51	ALA
A789	119.14	76.44	25.98	THR
A790	120.32	76.11	22.4	THR
A791	120.82	77.82	19.09	VAL
A792	122.12	74.85	16.97	ALA
A793	121.79	71.0	16.81	GLU
A794	124.0	69.57	13.98	GLU
A795	127.63	68.58	14.55	GLY
A796	127.15	68.86	18.28	LEU
A797	127.14	65.4	19.85	ASP
A798	123.96	66.0	21.9	ILE
A799	121.89	62.82	22.37	LYS
A800	119.06	61.17	24.26	GLU
A801	116.96	64.35	23.98	CYS
A802	113.44	63.3	24.99	ASN
A803	112.47	67.02	25.22	ILE
A804	113.02	69.45	22.29	VAL
A805	111.26	72.76	22.24	ILE
A806	111.3	75.44	19.58	ARG
A807	109.94	78.95	20.25	TYR
A808	109.59	81.55	17.5	GLY
A809	111.06	79.42	14.63	LEU
A810	110.18	76.13	12.84	VAL
A811	112.03	73.0	11.89	THR
A812	113.22	72.47	8.35	ASN
A813	113.27	69.0	6.77	GLU
A814	116.78	67.73	7.6	ILE
A815	116.79	68.86	11.25	ALA
A816	113.42	66.99	11.72	MET
A817	114.92	63.66	10.77	VAL
A818	118.18	64.42	12.6	GLN
A819	116.37	65.43	15.78	ALA
A820	115.07	61.83	15.84	ARG
A821	118.6	60.43	16.09	GLY
A822	119.27	63.01	18.85	ARG
A823	116.13	61.93	20.84	ALA
A824	115.85	58.18	20.56	ARG
A825	114.83	56.41	22.79	ALA
A826	112.09	56.01	24.16	ASP
A827	108.82	58.02	24.06	GLU
A828	110.18	61.42	22.96	SER
A829	108.52	64.77	22.36	THR
A830	109.07	67.72	20.12	TYR
A831	107.17	70.93	20.79	VAL
A832	106.68	73.95	18.56	LEU
A833	105.7	77.09	20.49	VAL
A834	103.9	79.73	18.33	ALA
A835	103.7	83.37	19.55	HIS
A836	99.93	83.6	19.24	SER
A837	99.26	80.85	16.66	GLY
A838	98.43	79.26	14.19	SER
A839	100.07	80.3	10.94	GLY
A840	103.43	78.79	11.82	VAL
A841	102.06	75.38	12.9	ILE
A842	100.95	74.97	9.29	GLU
A843	104.52	75.74	8.04	HIS
A844	105.99	73.17	10.37	GLU
A845	103.43	70.85	8.77	THR
A846	105.27	71.21	5.42	VAL
A847	108.14	68.91	6.46	ASN
A848	105.84	65.85	5.94	ASP
A849	105.14	66.87	2.28	PHE
A850	108.96	67.25	2.02	ARG
A851	109.64	63.78	3.55	GLU
A852	106.95	62.27	1.17	LYS
A853	108.7	64.08	-1.88	MET
A854	112.0	62.77	-0.53	MET
A855	111.21	59.05	-0.87	TYR
A856	109.44	59.73	-4.17	LYS
A857	112.63	61.43	-5.42	ALA
A858	114.92	58.65	-4.27	ILE
A859	112.52	56.11	-5.83	HIS
A860	112.72	57.67	-9.29	CYS
A861	116.57	57.59	-9.12	VAL
A862	116.2	53.86	-8.12	GLN
A863	114.24	53.28	-11.35	ASN
A864	116.39	55.43	-13.69	MET
A865	117.73	54.15	-17.01	LYS
A866	121.37	52.84	-16.72	PRO
A867	122.48	54.97	-19.63	GLU
A868	120.51	58.08	-18.51	GLU
A869	121.76	57.81	-14.88	TYR
A870	125.24	57.75	-16.33	ALA
A871	124.63	60.71	-18.67	HIS
A872	122.97	62.88	-15.94	LYS
A873	125.59	61.86	-13.31	ILE
A874	128.4	62.55	-15.8	LEU
A875	127.18	66.23	-15.82	GLU
A876	126.9	66.37	-11.96	LEU
A877	130.37	64.95	-11.57	GLN
A878	132.77	66.07	-14.29	MET
A879	130.85	69.27	-15.19	GLN
A880	129.8	70.31	-11.63	SER
A881	132.16	69.3	-8.85	ILE
A882	135.58	68.23	-10.32	MET
A883	137.2	71.72	-10.41	GLU
A884	137.9	73.72	-7.19	LYS
A885	136.15	76.91	-6.04	LYS
A886	137.28	79.88	-8.13	MET
A887	138.82	83.1	-6.62	LYS
A888	136.57	86.13	-7.15	THR
A889	138.2	88.03	-4.32	LYS
A890	141.99	88.62	-4.49	ARG
A891	144.08	90.36	-1.77	ASN
A892	146.26	93.22	-2.95	ILE
A893	150.04	93.4	-2.35	ALA
A894	152.69	95.82	-3.63	LYS
A895	150.32	98.23	-5.45	HIS
A896	151.69	101.81	-5.02	TYR
A897	149.65	104.01	-7.42	LYS
A898	146.75	105.99	-5.9	ASN
A899	143.23	106.29	-7.27	ASN
A900	141.91	109.47	-9.07	PRO
A901	140.28	112.29	-6.98	SER
A902	137.22	111.73	-9.16	LEU
A903	135.86	109.85	-6.12	ILE
A904	134.86	111.86	-2.97	THR
A905	133.41	110.94	0.44	PHE
A906	131.07	112.92	2.74	LEU
A907	129.27	112.18	5.95	CYS
A908	125.59	111.22	5.34	LYS
A909	124.67	113.74	8.11	ASN
A910	126.64	116.55	6.5	CYS
A911	126.9	118.75	3.38	SER
A912	130.68	119.27	3.11	VAL
A913	133.16	116.82	1.39	LEU
A914	135.8	115.02	3.55	ALA
A915	138.42	113.11	1.58	CYS
A916	138.93	111.67	-1.88	SER
A917	139.61	108.2	-3.39	GLY
A918	143.27	109.06	-3.8	GLU
A919	143.47	109.33	0.03	ASP
A920	142.47	105.63	0.61	ILE
A921	145.14	102.89	1.39	HIS
A922	145.36	99.42	2.94	VAL
A923	147.42	98.15	5.88	ILE
A924	148.0	94.36	6.31	GLU
A925	146.75	93.91	2.68	LYS
A926	143.19	93.79	4.0	MET
A927	142.41	96.78	6.22	HIS
A928	141.42	100.28	5.13	HIS
A929	142.94	103.61	6.2	VAL
A930	143.15	107.14	5.33	ASN
A931	146.66	108.61	5.17	MET
A932	146.37	112.34	4.24	THR
A933	147.25	114.94	6.88	PRO
A934	144.37	117.28	6.08	GLU
A935	141.98	114.39	7.04	PHE
A936	143.9	113.46	10.19	LYS
A937	142.68	116.85	11.49	GLU
A938	139.3	116.95	9.75	LEU
A939	137.61	114.77	12.37	TYR
A940	137.29	114.72	16.09	ILE
A941	138.65	111.69	18.06	VAL
A942	137.16	110.59	21.43	ARG
A943	136.71	108.2	24.3	GLU
A944	133.66	105.94	24.1	ASN
A945	132.29	104.41	27.32	LYS
A946	128.78	103.06	26.68	ALA
A947	129.07	101.42	23.26	LEU
A948	132.62	100.01	22.92	GLN
A949	133.8	96.97	24.89	LYS
A950	137.06	96.31	26.73	LYS
A951	139.52	93.36	27.07	CYS
A952	142.3	92.96	29.58	ALA
A953	145.03	95.31	28.36	ASP
A954	143.7	95.55	24.75	TYR
A955	141.65	98.73	23.95	GLN
A956	141.31	101.09	20.9	ILE
A957	143.26	104.33	20.72	ASN
A958	140.01	106.13	20.23	GLY
A959	136.76	106.65	18.33	GLU
A960	136.29	108.86	15.3	ILE
A961	133.25	111.16	14.9	ILE
A962	131.79	113.78	12.58	CYS
A963	130.63	117.25	13.62	LYS
A964	127.06	116.22	14.59	CYS
A965	128.38	113.26	16.61	GLY
A966	127.99	110.1	14.49	GLN
A967	130.86	107.71	14.13	ALA
A968	133.24	107.14	11.2	TRP
A969	135.74	104.51	12.55	GLY
A970	138.42	103.9	15.2	THR
A971	141.67	105.73	15.75	MET
A972	144.2	102.89	16.31	MET
A973	148.02	102.53	16.2	VAL
A974	149.58	99.92	13.97	HIS
A975	153.3	99.18	13.53	LYS
A976	154.82	102.59	14.1	GLY
A977	151.98	104.52	12.51	LEU
A978	149.01	106.2	14.03	ASP
A979	146.04	105.76	11.82	LEU
A980	142.38	106.69	11.42	PRO
A981	140.51	103.52	10.32	CYS
A982	137.16	104.62	8.67	LEU
A983	134.25	102.3	8.02	LYS
A984	132.6	102.76	4.63	ILE
A985	128.84	102.55	5.59	ARG
A986	129.11	105.9	7.41	ASN
A987	129.67	107.89	4.19	PHE
A988	127.97	108.84	0.9	VAL
A989	130.33	108.4	-2.05	VAL
A990	130.32	110.86	-4.98	VAL
A991	131.49	110.51	-8.57	PHE
A992	132.55	113.91	-9.99	LYS
A993	132.51	112.54	-13.55	ASN
A994	128.87	111.33	-13.32	ASN
A995	127.47	113.9	-10.81	SER
A996	126.01	110.92	-8.89	THR
A997	125.9	109.63	-5.3	LYS
A998	126.34	106.05	-3.94	LYS
A999	126.47	104.05	-0.68	GLN
A1000	128.52	100.99	0.06	TYR
A1001	128.72	98.36	2.83	LYS
A1002	132.11	96.66	1.98	LYS
A1003	135.17	98.21	0.24	TRP
A1004	135.04	95.39	-2.38	VAL
A1005	132.02	97.2	-3.93	GLU
A1006	134.04	100.23	-5.07	LEU
A1007	135.44	100.6	-8.6	PRO
A1008	138.9	101.69	-7.36	ILE
A1009	142.12	99.81	-6.41	THR
A1010	143.8	100.94	-3.18	PHE
A1011	147.57	100.99	-2.84	PRO
A1012	149.37	99.38	0.16	ASN
A1013	151.49	101.25	2.76	LEU