A307	60.95	157.13	20.1	GLN
A308	60.16	153.96	18.26	LEU
A309	58.8	155.57	15.07	ARG
A310	55.0	156.12	14.72	PRO
A311	54.15	153.33	12.26	TYR
A312	56.14	150.71	14.15	GLN
A313	54.58	152.2	17.34	MET
A314	50.93	151.57	16.28	GLU
A315	51.35	147.82	15.94	VAL
A316	53.52	147.37	19.16	ALA
A317	51.3	149.16	21.71	GLN
A318	49.37	146.08	22.95	PRO
A319	52.65	144.27	23.67	ALA
A320	54.02	147.27	25.5	LEU
A321	50.97	146.83	27.83	GLU
A322	51.7	143.1	28.04	GLY
A323	49.16	141.36	25.7	LYS
A324	50.29	138.64	23.25	ASN
A325	50.11	139.89	19.66	ILE
A326	50.85	139.19	15.99	ILE
A327	52.77	142.02	14.33	ILE
A328	51.74	142.37	10.67	CYS
A329	53.91	144.4	8.32	LEU
A330	55.26	144.31	4.68	PRO
A331	58.44	142.51	3.6	THR
A332	61.67	144.48	4.0	GLY
A333	60.22	146.47	6.96	SER
A334	61.81	147.16	10.37	GLY
A335	60.81	143.76	11.88	LYS
A336	63.93	143.29	14.09	THR
A337	63.88	146.92	15.3	ARG
A338	60.32	146.17	16.51	VAL
A339	61.64	143.15	18.38	ALA
A340	64.66	144.75	20.08	VAL
A341	62.62	147.84	21.13	TYR
A342	60.0	145.63	22.83	ILE
A343	62.55	143.16	24.33	ALA
A344	64.4	146.08	25.85	LYS
A345	61.14	147.37	27.49	ASP
A346	60.5	143.76	28.65	HIS
A347	63.89	143.2	30.25	LEU
A348	63.86	146.57	31.97	ASP
A349	60.41	145.92	33.44	LYS
A350	61.85	142.96	35.45	LYS
A351	64.93	145.03	36.34	LYS
A352	62.92	147.95	37.63	LYS
A353	61.02	145.33	39.63	ALA
A354	64.15	143.61	41.05	SER
A355	63.05	140.34	39.28	GLU
A356	64.85	138.18	36.67	PRO
A357	64.18	138.41	32.86	GLY
A358	65.0	136.24	29.83	LYS
A359	64.21	136.4	26.12	VAL
A360	64.4	133.57	23.6	ILE
A361	63.94	134.04	19.83	VAL
A362	62.96	131.58	17.03	LEU
A363	63.65	131.45	13.28	VAL
A364	62.89	128.5	10.9	ASN
A365	66.49	128.26	9.55	LYS
A366	69.89	128.33	11.37	VAL
A367	71.42	130.8	8.92	LEU
A368	68.9	133.39	10.23	LEU
A369	70.25	133.0	13.77	VAL
A370	73.54	134.97	13.35	GLU
A371	71.74	137.4	10.88	GLN
A372	69.49	138.51	13.73	LEU
A373	72.08	138.22	16.49	PHE
A374	74.89	140.43	15.08	ARG
A375	73.05	142.91	12.75	LYS
A376	70.49	144.16	15.31	GLU
A377	69.78	141.88	18.33	PHE
A378	73.27	142.64	19.9	GLN
A379	74.15	146.27	18.81	PRO
A380	70.75	147.54	20.09	PHE
A381	71.22	145.75	23.43	LEU
A382	74.9	145.16	24.26	LYS
A383	75.26	148.14	26.62	LYS
A384	72.87	146.5	29.08	TRP
A385	72.03	142.81	28.34	TYR
A386	73.68	139.59	27.28	ARG
A387	73.01	138.33	23.73	VAL
A388	73.98	135.04	22.05	ILE
A389	72.86	133.64	18.71	GLY
A390	73.2	129.81	18.84	LEU
A391	75.91	128.18	16.64	SER
A392	78.1	124.98	16.42	GLY
A393	77.8	121.57	18.12	ASP
A394	78.54	122.88	21.59	THR
A395	75.34	124.99	21.37	GLN
A396	73.19	123.1	18.77	LEU
A397	73.46	119.39	20.0	LYS
A398	75.16	119.39	23.45	ILE
A399	73.46	120.49	26.71	SER
A400	70.65	122.75	25.52	PHE
A401	69.29	122.97	29.1	PRO
A402	72.79	124.4	30.05	GLU
A403	72.91	126.76	27.06	VAL
A404	69.66	128.59	27.88	VAL
A405	71.02	129.54	31.36	LYS
A406	73.42	131.9	29.54	SER
A407	72.42	135.35	28.43	CYS
A408	69.37	137.65	28.94	ASP
A409	68.51	137.25	25.23	ILE
A410	68.97	134.12	23.05	ILE
A411	68.55	133.48	19.28	ILE
A412	67.79	129.91	18.06	SER
A413	66.43	127.94	15.21	THR
A414	63.05	126.29	15.92	ALA
A415	63.96	122.65	15.23	GLN
A416	66.14	122.3	18.45	ILE
A417	63.13	123.02	20.68	LEU
A418	60.76	120.16	19.65	GLU
A419	61.82	117.73	22.51	ASN
A420	63.75	120.15	24.79	SER
A421	60.98	122.82	25.18	LEU
A422	58.22	120.27	24.21	LEU
A423	57.39	116.92	25.7	ASN
A424	53.93	115.42	26.21	LEU
A425	54.26	112.01	24.44	GLU
A426	57.69	110.82	25.89	ASN
A427	56.69	112.52	29.1	GLY
A428	54.35	115.18	30.52	GLU
A429	56.68	118.21	30.83	ASP
A430	59.66	119.63	28.93	ALA
A431	63.31	119.62	29.91	GLY
A432	63.56	123.44	29.59	VAL
A433	61.51	125.65	31.91	GLN
A434	58.97	127.6	29.82	LEU
A435	57.98	129.61	32.88	SER
A436	61.49	131.02	33.42	ASP
A437	61.51	133.11	30.22	PHE
A438	59.57	136.34	30.04	SER
A439	59.28	136.94	26.26	LEU
A440	59.29	134.65	23.27	ILE
A441	59.57	136.03	19.77	ILE
A442	58.68	133.92	16.72	ILE
A443	59.99	135.31	13.43	ASP
A444	58.16	134.35	10.3	GLU
A445	55.58	132.61	12.49	CYS
A446	53.15	131.94	9.58	HIS
A447	55.61	129.46	7.82	HIS
A448	53.67	126.39	8.9	THR
A449	54.15	122.78	7.63	ASN
A450	52.67	119.2	8.0	LYS
A451	55.16	117.7	10.45	GLU
A452	57.77	120.48	10.35	ALA
A453	58.2	123.92	11.86	VAL
A454	55.95	125.89	12.41	TYR
A455	54.91	124.79	15.01	ASN
A456	56.62	122.3	17.42	ASN
A457	56.79	124.33	20.66	ILE
A458	53.57	126.17	21.15	MET
A459	51.59	123.03	21.95	ARG
A460	53.38	122.88	25.27	HIS
A461	52.38	126.51	25.74	TYR
A462	48.71	126.01	24.98	LEU
A463	48.58	122.84	27.02	MET
A464	50.25	124.71	29.93	GLN
A465	47.61	127.48	29.78	LYS
A466	44.89	124.69	30.09	LEU
A467	46.65	123.28	33.13	LYS
A468	46.76	126.87	34.5	ASN
A469	42.92	127.41	34.14	ASN
A470	42.31	124.0	35.78	ARG
A471	44.64	124.8	38.72	LEU
A472	43.19	128.35	38.89	LYS
A473	39.64	126.89	39.16	LYS
A474	41.05	124.8	41.98	GLU
A475	42.08	128.15	43.49	ASN
A476	45.76	127.1	43.66	LYS
A477	48.76	129.22	42.82	PRO
A478	49.82	128.95	39.16	VAL
A479	53.2	129.11	37.29	ILE
A480	53.63	132.03	34.93	PRO
A481	53.81	131.9	31.13	LEU
A482	55.72	134.14	28.73	PRO
A483	54.66	136.98	26.56	GLN
A484	54.38	135.98	22.9	ILE
A485	55.34	138.32	19.99	LEU
A486	54.52	136.84	16.63	GLY
A487	56.53	138.54	13.84	LEU
A488	54.9	138.39	10.39	THR
A489	55.83	140.09	7.17	ALA
A490	53.4	138.82	5.7	SER
A491	51.29	135.75	6.62	PRO
A492	49.58	135.02	3.28	GLY
A493	46.5	133.07	2.45	VAL
A494	48.36	130.17	0.73	GLY
A495	45.99	127.33	-0.06	GLY
A496	42.89	129.45	0.88	ALA
A497	41.09	130.49	-2.33	THR
A498	38.38	132.34	-0.44	LYS
A499	38.27	135.01	2.24	GLN
A500	36.52	132.76	4.81	ALA
A501	39.52	130.4	4.67	LYS
A502	41.92	133.35	4.83	ALA
A503	39.97	134.53	7.98	GLU
A504	40.44	131.0	9.25	GLU
A505	44.15	131.14	8.45	HIS
A506	44.57	134.42	10.36	ILE
A507	42.64	132.88	13.33	LEU
A508	44.55	129.51	13.51	LYS
A509	47.71	131.69	13.66	LEU
A510	46.35	133.95	16.4	CYS
A511	45.27	130.73	18.23	ALA
A512	48.75	129.07	18.17	ASN
A513	50.46	132.23	19.46	LEU
A514	47.68	132.93	22.11	ASP
A515	47.43	136.44	20.53	ALA
A516	44.76	138.82	21.96	PHE
A517	44.66	140.16	18.37	THR
A518	46.49	140.59	15.04	ILE
A519	47.74	144.17	14.64	LYS
A520	48.02	146.2	11.44	THR
A521	49.09	149.76	10.61	VAL
A522	45.96	151.91	10.03	LYS
A523	46.37	155.53	11.34	GLU
A524	50.09	155.94	10.39	ASN
A525	49.54	154.45	6.93	LEU
A526	51.02	157.37	4.98	ASP
A527	54.18	157.05	7.15	GLN
A528	54.54	153.37	6.42	LEU
A529	54.0	154.27	2.71	LYS
A530	56.57	157.13	2.91	ASN
A531	59.19	155.33	5.07	GLN
A532	58.85	151.9	3.33	ILE
A533	58.48	153.15	-0.23	GLN
A534	57.61	151.07	-3.31	GLU
A535	59.59	149.97	-6.39	PRO
A536	58.21	150.59	-9.87	CYS
A537	56.8	147.37	-11.36	LYS
A538	57.61	146.46	-15.0	LYS
A539	57.16	143.4	-17.25	PHE
A540	59.11	141.89	-20.14	ALA
A541	59.13	138.86	-22.48	ILE
A542	62.2	136.63	-23.23	ALA
A543	64.15	137.43	-26.38	ASP
A544	63.23	134.42	-28.51	ALA
A545	63.66	134.44	-32.25	THR
A546	62.92	132.7	-35.53	ARG
A547	64.52	129.61	-37.09	GLU
A548	68.22	129.99	-38.01	ASP
A549	71.2	127.91	-39.38	PRO
A550	72.45	126.76	-35.94	PHE
A551	68.93	125.52	-35.01	LYS
A552	68.42	124.06	-38.49	GLU
A553	71.66	122.11	-38.05	LYS
A554	70.52	120.82	-34.64	LEU
A555	67.43	119.55	-36.51	LEU
A556	69.65	117.84	-39.08	GLU
A557	71.4	115.93	-36.31	ILE
A558	68.3	115.04	-34.32	MET
A559	66.51	113.76	-37.47	THR
A560	69.63	111.71	-38.51	ARG
A561	69.56	110.07	-35.06	ILE
A562	65.76	109.58	-35.25	GLN
A563	65.75	108.08	-38.78	THR
A564	68.31	105.41	-37.88	TYR
A565	66.15	104.15	-35.01	CYS
A566	62.93	105.09	-36.9	GLN
A567	61.92	107.2	-33.84	MET
A568	58.65	109.08	-33.72	SER
A569	58.3	111.59	-30.87	PRO
A570	54.71	112.62	-31.81	MET
A571	55.91	116.0	-30.78	SER
A572	57.92	118.98	-32.09	ASP
A573	61.66	119.3	-31.35	PHE
A574	62.81	121.38	-28.35	GLY
A575	59.49	120.9	-26.49	THR
A576	58.02	119.29	-23.33	GLN
A577	56.18	116.67	-25.41	PRO
A578	59.5	115.65	-26.94	TYR
A579	61.21	115.74	-23.53	GLU
A580	58.56	113.47	-22.07	GLN
A581	59.09	111.19	-25.12	TRP
A582	62.86	111.25	-24.73	ALA
A583	63.0	110.35	-21.09	ILE
A584	60.26	107.77	-21.43	GLN
A585	61.83	106.19	-24.48	MET
A586	65.06	105.86	-22.48	GLU
A587	63.26	103.98	-19.64	LYS
A588	61.34	101.81	-22.11	LYS
A589	64.42	100.65	-23.94	ALA
A590	66.7	100.17	-20.91	ALA
A591	64.03	97.6	-19.69	LYS
A592	63.78	96.07	-23.22	GLU
A593	67.59	95.41	-23.53	GLY
A594	67.85	97.79	-26.47	ASN
A595	70.99	99.88	-26.2	ARG
A596	70.71	101.14	-29.81	LYS
A597	67.52	103.05	-29.06	GLU
A598	68.27	103.67	-25.31	ARG
A599	71.55	105.54	-25.97	VAL
A600	70.01	107.56	-28.86	CYS
A601	67.13	108.52	-26.42	ALA
A602	69.66	109.83	-23.85	GLU
A603	71.59	111.75	-26.53	HIS
A604	68.22	113.04	-27.89	LEU
A605	67.27	114.43	-24.45	ARG
A606	70.33	116.68	-24.7	LYS
A607	69.77	118.0	-28.16	TYR
A608	66.12	118.64	-27.07	ASN
A609	67.55	120.32	-23.94	GLU
A610	69.55	122.86	-26.09	ALA
A611	66.38	123.79	-27.98	LEU
A612	64.09	123.82	-24.92	GLN
A613	66.48	126.53	-23.54	ILE
A614	66.75	128.38	-26.86	ASN
A615	65.05	131.54	-25.42	ASP
A616	67.0	131.64	-22.14	THR
A617	70.48	130.65	-23.22	ILE
A618	72.59	132.08	-26.08	ARG
A619	74.02	129.82	-28.74	MET
A620	77.66	129.65	-27.61	ILE
A621	76.76	128.56	-24.05	ASP
A622	74.02	126.25	-25.53	ALA
A623	76.77	124.79	-27.77	TYR
A624	79.08	124.42	-24.76	THR
A625	76.3	122.39	-23.09	HIS
A626	76.54	119.73	-25.88	LEU
A627	80.37	120.24	-26.06	GLU
A628	81.03	119.34	-22.39	THR
A629	78.57	116.44	-22.76	PHE
A630	80.46	115.03	-25.73	TYR
A631	83.69	115.65	-23.81	ASN
A632	82.21	113.48	-20.98	GLU
A633	81.27	110.78	-23.52	GLU
A634	84.91	110.85	-24.82	LYS
A635	86.67	110.99	-21.36	ASP
A636	84.53	108.2	-19.94	LYS
A637	85.54	105.89	-22.9	LYS
A638	89.12	106.64	-23.92	PHE
A639	92.75	107.26	-23.01	ALA
A640	94.13	110.75	-23.93	VAL
A641	97.37	112.28	-25.17	ILE
A642	98.22	115.69	-23.76	GLU
A643	100.31	118.41	-25.53	ASP
A644	101.73	121.67	-24.1	ASP
A645	102.37	125.17	-25.35	SER
A646	103.81	128.22	-23.67	ASP
A647	100.22	129.32	-22.71	GLU
A648	98.35	125.98	-22.14	GLY
A649	97.9	123.19	-24.7	GLY
A650	95.81	120.53	-26.5	ASP
A651	94.1	117.16	-25.89	ASP
A652	93.34	114.14	-28.08	GLU
A653	91.19	111.18	-26.96	TYR
A654	92.26	107.76	-28.3	CYS
A655	88.9	106.74	-29.84	ASP
A656	90.55	105.15	-32.93	GLY
A657	92.9	102.26	-32.22	ASP
A658	94.51	100.5	-29.22	GLU
A659	97.29	99.48	-31.56	ASP
A660	100.67	100.27	-33.19	GLU
A661	102.48	96.87	-33.38	ASP
A662	101.47	94.74	-36.43	ASP
A663	98.58	92.99	-34.67	LEU
A664	95.26	94.78	-33.85	LYS
A665	92.81	94.28	-31.04	LYS
A666	89.0	93.87	-31.34	PRO
A667	86.53	96.76	-31.1	LEU
A668	84.88	97.31	-27.73	LYS
A669	83.23	100.58	-28.97	LEU
A670	79.58	100.32	-30.14	ASP
A671	78.78	101.53	-33.72	GLU
A672	75.9	103.64	-32.51	THR
A673	78.3	105.49	-30.19	ASP
A674	80.65	105.97	-33.14	ARG
A675	77.69	107.41	-35.14	PHE
A676	76.54	109.63	-32.25	LEU
A677	80.23	110.76	-32.03	MET
A678	80.47	111.37	-35.76	THR
A679	77.25	113.52	-35.74	LEU
A680	78.94	115.83	-33.27	PHE
A681	82.61	115.84	-34.46	PHE
A682	81.59	116.27	-38.13	GLU
A683	79.39	119.31	-37.33	ASN
A684	80.85	120.93	-34.12	ASN
A685	83.2	123.45	-35.78	LYS
A686	80.33	124.68	-37.93	MET
A687	78.05	124.97	-34.87	LEU
A688	80.92	126.6	-32.95	LYS
A689	81.34	129.06	-35.85	ARG
A690	77.67	130.03	-36.12	LEU
A691	77.36	130.3	-32.31	ALA
A692	79.33	133.58	-32.4	GLU
A693	77.74	134.93	-35.71	ASN
A694	74.14	136.13	-36.32	PRO
A695	72.56	135.28	-39.65	GLU
A696	69.83	137.79	-39.03	TYR
A697	69.8	141.49	-38.1	GLU
A698	68.06	140.49	-34.82	ASN
A699	69.08	137.54	-32.62	GLU
A700	68.69	135.91	-29.13	LYS
A701	71.59	138.0	-27.67	LEU
A702	69.28	140.78	-26.51	THR
A703	69.26	139.43	-22.99	LYS
A704	68.0	142.11	-20.64	LEU
A705	70.92	144.58	-21.02	ARG
A706	68.68	147.65	-21.54	ASN
A707	66.3	146.46	-18.75	THR
A708	69.28	146.63	-16.32	ILE
A709	71.56	149.41	-17.7	MET
A710	68.83	152.07	-17.22	GLU
A711	69.08	151.95	-13.36	GLN
A712	72.9	151.94	-13.52	TYR
A713	73.1	154.97	-15.77	THR
A714	70.87	157.12	-13.5	ARG
A715	73.47	156.31	-10.77	THR
A716	76.88	158.08	-10.42	GLU
A717	78.87	155.99	-7.93	GLU
A718	77.49	152.38	-7.72	SER
A719	74.07	150.68	-7.9	ALA
A720	72.85	147.32	-6.56	ARG
A721	71.12	144.47	-8.44	GLY
A722	69.76	141.06	-7.78	ILE
A723	68.63	138.67	-10.53	ILE
A724	66.3	135.91	-9.33	PHE
A725	66.28	133.27	-12.08	THR
A726	64.75	129.83	-12.27	LYS
A727	67.92	127.97	-13.26	THR
A728	71.56	127.37	-12.33	ARG
A729	72.31	127.46	-16.03	GLN
A730	70.71	130.9	-16.45	SER
A731	72.6	132.02	-13.36	ALA
A732	76.14	131.19	-14.51	TYR
A733	75.45	132.17	-18.18	ALA
A734	74.13	135.65	-17.1	LEU
A735	77.37	135.93	-15.03	SER
A736	79.2	135.12	-18.26	GLN
A737	77.01	137.69	-20.07	TRP
A738	78.23	140.48	-17.76	ILE
A739	81.83	139.42	-18.44	THR
A740	81.59	138.72	-22.17	GLU
A741	80.65	140.84	-25.22	ASN
A742	81.77	144.14	-23.83	GLU
A743	80.57	146.76	-22.68	LYS
A744	77.45	145.82	-20.63	PHE
A745	78.03	148.55	-19.39	ALA
A746	78.91	150.35	-16.13	GLU
A747	77.94	147.4	-13.89	VAL
A748	81.48	146.01	-13.55	GLY
A749	82.77	143.0	-15.39	VAL
A750	82.25	140.25	-12.75	LYS
A751	79.1	138.58	-11.3	ALA
A752	78.35	135.59	-9.04	HIS
A753	75.62	132.99	-8.56	HIS
A754	74.18	132.36	-5.11	LEU
A755	73.23	128.74	-4.93	ILE
A756	72.19	126.09	-2.38	GLY
A757	74.35	123.21	-1.22	ALA
A758	72.38	120.71	-3.42	GLY
A759	73.77	119.17	-6.59	HIS
A760	70.97	120.65	-8.63	SER
A761	71.3	120.35	-12.34	SER
A762	74.6	118.62	-11.5	GLU
A763	76.46	121.8	-10.62	PHE
A764	79.18	122.15	-7.97	LYS
A765	77.3	123.24	-4.83	PRO
A766	78.0	126.22	-2.52	MET
A767	78.05	125.94	1.36	THR
A768	76.75	128.43	3.94	GLN
A769	80.1	129.95	4.89	ASN
A770	80.7	130.69	1.16	GLU
A771	77.07	131.76	0.75	GLN
A772	77.88	134.55	3.39	LYS
A773	81.02	135.72	1.56	GLU
A774	79.03	136.81	-1.47	VAL
A775	76.94	139.06	0.77	ILE
A776	80.09	140.58	2.31	SER
A777	81.35	141.19	-1.21	LYS
A778	78.13	142.91	-2.19	PHE
A779	77.59	145.02	0.93	ARG
A780	80.96	145.41	2.76	THR
A781	83.7	147.75	1.62	GLY
A782	85.73	147.44	-0.61	LYS
A783	82.94	145.96	-2.84	ILE
A784	83.54	143.19	-5.48	ASN
A785	80.0	142.73	-6.75	LEU
A786	77.6	145.39	-7.99	LEU
A787	75.23	142.72	-9.34	ILE
A788	74.52	139.1	-8.4	ALA
A789	72.37	136.22	-9.66	THR
A790	70.67	133.62	-7.47	THR
A791	68.44	130.51	-7.3	VAL
A792	68.29	130.96	-3.48	ALA
A793	65.79	133.2	-1.84	GLU
A794	64.96	132.1	1.72	GLU
A795	68.05	133.29	3.58	GLY
A796	69.38	135.74	0.9	LEU
A797	70.66	138.93	2.42	ASP
A798	70.89	140.8	-0.94	ILE
A799	68.58	143.8	-0.65	LYS
A800	68.23	147.51	-1.33	GLU
A801	68.51	146.71	-5.07	CYS
A802	68.01	149.53	-7.62	ASN
A803	67.21	146.83	-10.29	ILE
A804	65.47	143.52	-9.42	VAL
A805	64.43	140.99	-12.05	ILE
A806	62.57	137.62	-11.59	ARG
A807	63.34	135.65	-14.77	TYR
A808	60.84	132.75	-15.04	GLY
A809	59.51	133.07	-11.46	LEU
A810	55.95	134.4	-10.71	VAL
A811	54.24	131.31	-9.19	THR
A812	55.59	131.31	-5.64	ASN
A813	53.82	134.13	-3.83	GLU
A814	56.21	134.63	-0.87	ILE
A815	59.21	134.52	-3.31	ALA
A816	57.78	137.44	-5.21	MET
A817	56.82	139.6	-2.18	VAL
A818	60.24	138.99	-0.59	GLN
A819	61.7	140.13	-3.91	ALA
A820	59.58	143.23	-3.7	ARG
A821	60.97	143.72	-0.17	GLY
A822	64.55	143.43	-1.6	ARG
A823	63.62	146.16	-4.11	ALA
A824	62.46	148.68	-1.49	ARG
A825	63.05	151.66	-1.78	ALA
A826	62.46	154.17	-3.53	ASP
A827	63.53	154.93	-7.09	GLU
A828	64.06	151.18	-7.61	SER
A829	62.6	149.11	-10.43	THR
A830	61.23	145.65	-10.08	TYR
A831	60.71	143.37	-13.08	VAL
A832	58.99	140.06	-14.05	LEU
A833	59.96	138.04	-17.11	VAL
A834	57.73	135.71	-19.03	ALA
A835	59.1	133.49	-21.69	HIS
A836	56.41	134.33	-24.36	SER
A837	53.71	136.82	-25.35	GLY
A838	51.64	138.48	-24.06	SER
A839	53.62	137.94	-20.85	GLY
A840	52.89	137.04	-17.16	VAL
A841	51.04	140.33	-16.65	ILE
A842	47.61	138.98	-15.47	GLU
A843	49.06	135.98	-13.65	HIS
A844	50.75	138.56	-11.37	GLU
A845	47.4	140.32	-10.83	THR
A846	45.82	137.31	-9.05	VAL
A847	48.62	137.53	-6.44	ASN
A848	47.95	141.36	-6.02	ASP
A849	44.28	140.52	-5.53	PHE
A850	45.18	137.84	-2.98	ARG
A851	47.54	140.35	-1.21	GLU
A852	44.51	142.64	-0.76	LYS
A853	42.46	139.6	0.35	MET
A854	45.09	138.88	3.06	MET
A855	44.2	142.34	4.4	TYR
A856	40.48	141.79	3.84	LYS
A857	40.75	138.62	5.98	ALA
A858	42.72	140.39	8.67	ILE
A859	40.13	143.22	8.7	HIS
A860	37.19	140.76	9.26	CYS
A861	38.93	138.77	11.96	VAL
A862	39.99	142.07	13.58	GLN
A863	36.3	143.26	13.3	ASN
A864	35.13	140.01	15.0	MET
A865	33.1	140.5	18.16	LYS
A866	34.57	139.5	21.56	PRO
A867	32.42	136.44	22.28	GLU
A868	32.92	135.15	18.67	GLU
A869	36.64	135.96	18.54	TYR
A870	37.31	134.15	21.86	ALA
A871	35.11	131.12	21.06	HIS
A872	36.87	130.61	17.69	LYS
A873	40.39	131.04	19.2	ILE
A874	39.72	128.85	22.27	LEU
A875	38.47	125.94	20.07	GLU
A876	41.09	126.58	17.35	LEU
A877	43.57	126.35	20.29	GLN
A878	42.08	122.99	21.35	MET
A879	42.56	121.73	17.78	GLN
A880	46.15	123.0	17.93	SER
A881	46.44	120.99	21.18	ILE
A882	44.56	117.83	20.12	MET
A883	44.7	117.17	16.4	GLU
A884	48.43	116.37	15.86	LYS
A885	51.47	114.79	17.56	LYS
A886	54.07	114.3	14.73	MET
A887	57.42	116.25	14.58	LYS
A888	60.26	117.27	12.2	THR
A889	62.53	114.41	13.27	LYS
A890	61.26	110.87	13.8	ARG
A891	61.87	107.33	15.25	ASN
A892	61.52	105.1	12.17	ILE
A893	65.08	104.49	10.72	ALA
A894	63.94	102.0	8.07	LYS
A895	60.68	100.64	6.65	HIS
A896	59.47	97.09	6.13	TYR
A897	60.74	95.51	2.85	LYS
A898	61.2	92.1	1.07	ASN
A899	64.11	89.68	0.94	ASN
A900	66.84	90.24	-1.78	PRO
A901	66.17	86.74	-3.27	SER
A902	63.64	88.43	-5.52	LEU
A903	65.96	90.7	-7.59	ILE
A904	68.96	90.89	-9.91	THR
A905	70.88	93.84	-11.54	PHE
A906	72.4	94.91	-14.83	LEU
A907	73.5	98.19	-16.4	CYS
A908	71.11	100.2	-18.59	LYS
A909	73.22	99.19	-21.64	ASN
A910	74.0	95.57	-20.75	CYS
A911	72.79	92.15	-21.79	SER
A912	73.94	90.07	-18.71	VAL
A913	72.99	89.99	-15.04	LEU
A914	76.1	91.16	-13.29	ALA
A915	74.92	90.7	-9.71	CYS
A916	72.1	89.41	-7.53	SER
A917	70.36	91.31	-4.82	GLY
A918	71.94	88.8	-2.44	GLU
A919	75.45	89.82	-3.49	ASP
A920	75.07	93.33	-2.01	ILE
A921	75.47	94.43	1.64	HIS
A922	75.14	97.96	3.13	VAL
A923	77.89	99.48	5.26	ILE
A924	77.35	102.47	7.62	GLU
A925	73.8	102.79	6.19	LYS
A926	75.08	104.76	3.19	MET
A927	77.23	102.71	0.79	HIS
A928	76.13	99.55	-1.11	HIS
A929	79.03	97.2	-1.71	VAL
A930	79.25	93.86	-3.48	ASN
A931	80.43	90.86	-1.46	MET
A932	80.25	87.9	-3.84	THR
A933	83.51	86.62	-5.45	PRO
A934	83.11	85.98	-9.2	GLU
A935	81.93	89.62	-9.61	PHE
A936	85.57	90.81	-9.3	LYS
A937	86.32	89.1	-12.67	GLU
A938	83.1	90.47	-14.28	LEU
A939	83.69	94.2	-13.58	TYR
A940	85.97	96.69	-15.29	ILE
A941	87.86	99.57	-13.69	VAL
A942	89.43	102.87	-14.83	ARG
A943	92.08	104.4	-12.55	GLU
A944	91.98	107.84	-10.77	ASN
A945	94.26	110.82	-11.71	LYS
A946	93.13	113.31	-9.06	ALA
A947	95.61	113.7	-6.16	LEU
A948	94.5	111.53	-3.18	GLN
A949	93.0	112.64	0.2	LYS
A950	95.11	113.72	3.18	LYS
A951	93.21	111.45	5.62	CYS
A952	92.82	107.62	5.42	ALA
A953	89.08	107.05	4.9	ASP
A954	87.48	105.66	1.75	TYR
A955	90.19	106.7	-0.7	GLN
A956	89.18	106.49	-4.4	ILE
A957	91.29	104.23	-6.53	ASN
A958	89.11	104.58	-9.62	GLY
A959	85.62	104.29	-11.15	GLU
A960	83.97	100.95	-11.99	ILE
A961	82.63	101.23	-15.56	ILE
A962	80.96	99.2	-18.34	CYS
A963	82.16	98.62	-21.86	LYS
A964	80.12	101.79	-22.7	CYS
A965	82.43	103.75	-20.4	GLY
A966	79.37	104.26	-18.26	GLN
A967	79.76	104.18	-14.47	ALA
A968	78.7	101.37	-12.14	TRP
A969	79.99	103.27	-9.11	GLY
A970	83.41	103.97	-7.57	THR
A971	86.19	101.58	-6.56	MET
A972	87.33	102.49	-2.99	MET
A973	90.07	101.45	-0.53	VAL
A974	89.42	101.4	3.17	HIS
A975	90.99	99.86	6.34	LYS
A976	93.31	97.71	4.26	GLY
A977	90.4	96.21	2.29	LEU
A978	89.17	97.09	-1.23	ASP
A979	85.41	97.81	-1.6	LEU
A980	83.26	97.75	-4.83	PRO
A981	80.68	100.49	-4.25	CYS
A982	77.53	100.63	-6.45	LEU
A983	74.89	103.32	-7.12	LYS
A984	71.4	102.13	-8.06	ILE
A985	70.99	105.06	-10.44	ARG
A986	73.38	103.22	-12.82	ASN
A987	71.1	100.15	-13.11	PHE
A988	68.04	98.35	-14.33	VAL
A989	66.54	96.07	-11.65	VAL
A990	65.12	92.72	-12.9	VAL
A991	62.78	90.65	-10.79	PHE
A992	63.63	87.02	-10.49	LYS
A993	60.38	85.12	-10.02	ASN
A994	58.27	87.58	-12.06	ASN
A995	60.2	88.57	-15.3	SER
A996	59.55	92.24	-14.75	THR
A997	61.89	95.24	-14.75	LYS
A998	62.22	98.74	-13.26	LYS
A999	64.79	101.55	-12.85	GLN
A1000	65.35	103.8	-9.79	TYR
A1001	67.22	106.84	-8.55	LYS
A1002	67.36	106.01	-4.81	LYS
A1003	67.37	102.75	-2.82	TRP
A1004	64.08	103.45	-0.91	VAL
A1005	61.94	103.39	-4.03	GLU
A1006	62.94	99.68	-4.27	LEU
A1007	60.81	97.16	-2.27	PRO
A1008	63.97	95.38	-1.04	ILE
A1009	66.08	95.37	2.18	THR
A1010	69.73	94.43	2.39	PHE
A1011	72.16	93.04	5.04	PRO
A1012	74.59	95.12	7.05	ASN
A1013	78.31	94.19	7.17	LEU