LISTADO DE SECUENCIAS <110> Molecular Partners AG <120> Prote’nas de uni—n recombinantes <130> P015 <160> 33 <170> BiSSAP 1.3 <210> 1 <211> 10 <212> PRT <213> Secuencia Artificial <220> <223> Marcador His <400> 1 Met Arg Gly Ser His His His His His His 1 5 10 <210> 2 <211> 5 <212> PRT <213> Secuencia Artificial <220> <223> Enlazador GlySer <400> 2 Gly Gly Gly Gly Ser 1 5 <210> 3 <211> 7 <212> PRT <213> Secuencia Artificial <220> <223> Enlazador GlySer <400> 3 Gly Gly Gly Gly Ser Gly Ser 1 5 <210> 4 <211> 10 <212> PRT <213> Secuencia Artificial <220> <223> Enlazador GlySer <400> 4 Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser 1 5 10 <210> 5 <211> 15 <212> PRT <213> Secuencia Artificial <220> <223> Enlazador GlySer <400> 5 Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser 1 5 10 15 <210> 6 <211> 20 <212> PRT <213> Secuencia Artificial <220> <223> Enlazador GlySer <400> 6 Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly 1 5 10 15 Gly Gly Gly Ser 20 <210> 7 <211> 8 <212> PRT <213> Secuencia Artificial <220> <223> Enlazador ProThr <400> 7 Gly Ser Pro Thr Pro Thr Pro Thr 1 5 <210> 8 <211> 15 <212> PRT <213> Secuencia Artificial <220> <223> Enlazador ProThr <400> 8 Gly Ser Pro Thr Pro Thr Pro Thr Thr Pro Thr Pro Thr Pro Thr 1 5 10 15 <210> 9 <211> 22 <212> PRT <213> Secuencia Artificial <220> <223> Enlazador ProThr <400> 9 Gly Ser Pro Thr Pro Thr Pro Thr Thr Pro Thr Pro Thr Pro Thr Thr 1 5 10 15 Pro Thr Pro Thr Pro Thr 20 <210> 10 <211> 159 <212> PRT <213> Secuencia Artificial <220> <223> Dominio dise–ado con repeticiones de anquirina <400> 10 Gly Ser Asp Leu Gly Lys Lys Leu Leu Glu Ala Ala Arg Ala Gly Gln 1 5 10 15 Asp Asp Glu Val Arg Ile Leu Met Ala Asn Gly Ala Asp Val Asn Ala 20 25 30 Thr Asp Asn Asp Gly Tyr Thr Pro Leu His Leu Ala Ala Ser Asn Gly 35 40 45 His Leu Glu Ile Val Glu Val Leu Leu Lys Asn Gly Ala Asp Val Asn 50 55 60 Ala Ser Asp Leu Thr Gly Ile Thr Pro Leu His Leu Ala Ala Ala Thr 65 70 75 80 Gly His Leu Glu Ile Val Glu Val Leu Leu Lys His Gly Ala Asp Val 85 90 95 Asn Ala Tyr Asp Asn Asp Gly His Thr Pro Leu His Leu Ala Ala Lys 100 105 110 Tyr Gly His Leu Glu Ile Val Glu Val Leu Leu Lys His Gly Ala Asp 115 120 125 Val Asn Ala Gln Asp Lys Phe Gly Lys Thr Ala Phe Asp Ile Ser Ile 130 135 140 Asp Asn Gly Asn Glu Asp Leu Ala Glu Ile Leu Gln Lys Ala Ala 145 150 155 <210> 11 <211> 126 <212> PRT <213> Secuencia Artificial <220> <223> Dominio dise–ado con repeticiones de anquirina <400> 11 Gly Ser Asp Leu Gly Lys Lys Leu Leu Glu Ala Ala Arg Ala Gly Gln 1 5 10 15 Asp Asp Glu Val Arg Ile Leu Met Ala Asn Gly Ala Asp Val Asn Ala 20 25 30 Lys Asp Lys Asp Gly Tyr Thr Pro Leu His Leu Ala Ala Arg Glu Gly 35 40 45 His Leu Glu Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn 50 55 60 Ala Lys Asp Lys Asp Gly Tyr Thr Pro Leu His Leu Ala Ala Arg Glu 65 70 75 80 Gly His Leu Glu Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val 85 90 95 Asn Ala Gln Asp Lys Phe Gly Lys Thr Ala Phe Asp Ile Ser Ile Asp 100 105 110 Asn Gly Asn Glu Asp Leu Ala Glu Ile Leu Gln Lys Ala Ala 115 120 125 <210> 12 <211> 126 <212> PRT <213> Secuencia Artificial <220> <223> Dominio dise–ado con repeticiones de anquirina <400> 12 Gly Ser Asp Leu Gly Lys Lys Leu Leu Glu Ala Ala Arg Ala Gly Gln 1 5 10 15 Asp Asp Glu Val Arg Ile Leu Leu Lys Ala Gly Ala Asp Val Asn Ala 20 25 30 Lys Asp Tyr Phe Ser His Thr Pro Leu His Leu Ala Ala Arg Asn Gly 35 40 45 His Leu Lys Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn 50 55 60 Ala Lys Asp Phe Ala Gly Lys Thr Pro Leu His Leu Ala Ala Asn Asp 65 70 75 80 Gly His Leu Glu Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val 85 90 95 Asn Ala Gln Asp Ile Phe Gly Lys Thr Pro Ala Asp Ile Ala Ala Asp 100 105 110 Ala Gly His Glu Asp Ile Ala Glu Val Leu Gln Lys Ala Ala 115 120 125 <210> 13 <211> 126 <212> PRT <213> Secuencia Artificial <220> <223> Dominio dise–ado con repeticiones de anquirina <400> 13 Gly Ser Asp Leu Gly Lys Lys Leu Leu Glu Ala Ala Arg Ala Gly Gln 1 5 10 15 Asp Asp Glu Val Arg Glu Leu Leu Lys Ala Gly Ala Asp Val Asn Ala 20 25 30 Lys Asp Tyr Phe Ser His Thr Pro Leu His Leu Ala Ala Arg Asn Gly 35 40 45 His Leu Lys Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn 50 55 60 Ala Lys Asp Phe Ala Gly Lys Thr Pro Leu His Leu Ala Ala Asn Asp 65 70 75 80 Gly His Leu Glu Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val 85 90 95 Asn Ala Gln Asp Ile Phe Gly Lys Thr Pro Ala Asp Ile Ala Ala Asp 100 105 110 Ala Gly His Glu Asp Ile Ala Glu Val Leu Gln Lys Ala Ala 115 120 125 <210> 14 <211> 126 <212> PRT <213> Secuencia Artificial <220> <223> Dominio dise–ado con repeticiones de anquirina <400> 14 Gly Ser Asp Leu Gly Lys Lys Leu Leu Glu Ala Ala Arg Ala Gly Gln 1 5 10 15 Asp Asp Glu Val Arg Glu Leu Leu Lys Ala Gly Ala Asp Val Asn Ala 20 25 30 Lys Asp Tyr Phe Ser His Thr Pro Leu His Leu Ala Ala Arg Asn Gly 35 40 45 His Leu Lys Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn 50 55 60 Ala Lys Asp Phe Ala Gly Lys Thr Pro Leu His Leu Ala Ala Asn Glu 65 70 75 80 Gly His Leu Glu Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val 85 90 95 Asn Ala Gln Asp Ile Phe Gly Lys Thr Pro Ala Asp Ile Ala Ala Asp 100 105 110 Ala Gly His Glu Asp Ile Ala Glu Val Leu Gln Lys Ala Ala 115 120 125 <210> 15 <211> 126 <212> PRT <213> Secuencia Artificial <220> <223> Dominio dise–ado con repeticiones de anquirina <400> 15 Gly Ser Asp Leu Gly Lys Lys Leu Leu Glu Ala Ala Arg Ala Gly Gln 1 5 10 15 Asp Asp Glu Val Arg Ile Leu Met Ala Asn Gly Ala Asp Val Asn Ala 20 25 30 Lys Asp Tyr Phe Ser His Thr Pro Leu His Leu Ala Ala Arg Asn Gly 35 40 45 His Leu Lys Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn 50 55 60 Ala Lys Asp Phe Ala Gly Lys Thr Pro Leu His Leu Ala Ala Asn Asp 65 70 75 80 Gly His Leu Glu Ile Val Glu Val Leu Leu Lys His Gly Ala Asp Val 85 90 95 Asn Ala Gln Asp Ile Phe Gly Lys Thr Pro Ala Asp Ile Ala Ala Asp 100 105 110 Ala Gly His Glu Asp Ile Ala Glu Val Leu Gln Lys Ala Ala 115 120 125 <210> 16 <211> 126 <212> PRT <213> Secuencia Artificial <220> <223> Dominio dise–ado con repeticiones de anquirina <400> 16 Gly Ser Asp Leu Gly Ile Lys Leu Leu Phe Ala Ala Ala Lys Gly Gln 1 5 10 15 Asp Asp Glu Val Arg Glu Leu Leu Lys Ala Gly Ala Asp Val Asn Ala 20 25 30 Lys Asp Phe Gln Gly Val Thr Pro Leu His Ile Ala Ala Gln Ser Gly 35 40 45 His Leu Glu Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn 50 55 60 Ala Lys Asp Val Thr Gly Asp Thr Pro Leu His Leu Ala Ala Gln His 65 70 75 80 Gly His Leu Glu Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val 85 90 95 Asn Ala Gln Asp Glu Arg Gly Trp Thr Pro Ala Asp Leu Ala Ala Asp 100 105 110 Trp Gly His Glu Asp Ile Ala Glu Val Leu Gln Lys Ala Ala 115 120 125 <210> 17 <211> 126 <212> PRT <213> Secuencia Artificial <220> <223> Dominio dise–ado con repeticiones de anquirina <400> 17 Gly Ser Asp Leu Gly Lys Lys Leu Leu Glu Ala Ala Arg Ala Gly Gln 1 5 10 15 Asp Asp Glu Val Arg Glu Leu Leu Lys Ala Gly Ala Asp Val Asn Ala 20 25 30 Lys Asp Glu Tyr Gly Leu Thr Pro Leu Tyr Leu Ala Thr Ala His Gly 35 40 45 His Leu Glu Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn 50 55 60 Ala Val Asp Ala Ile Gly Phe Thr Pro Leu His Leu Ala Ala Phe Ile 65 70 75 80 Gly His Leu Glu Ile Ala Glu Val Leu Leu Lys Ala Gly Ala Asp Val 85 90 95 Asn Ala Gln Asp Lys Phe Gly Lys Thr Pro Ala Asp Ile Ala Ala Gly 100 105 110 Ala Gly Asn Glu Asp Ile Ala Glu Val Leu Gln Lys Ala Ala 115 120 125 <210> 18 <211> 126 <212> PRT <213> Secuencia Artificial <220> <223> Dominio dise–ado con repeticiones de anquirina <400> 18 Gly Ser Asp Leu Gly Val Lys Leu Leu Trp Ala Ala Ala Arg Gly Gln 1 5 10 15 Asp Asp Glu Val Arg Glu Leu Leu Lys Ala Gly Ala Asp Val Asn Ala 20 25 30 Lys Asp Phe Gln Gly Ile Thr Pro Leu His Ile Ala Ala Thr Asn Gly 35 40 45 His Leu Glu Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn 50 55 60 Ala Lys Asp Ile Thr Gly Glu Thr Pro Leu His His Ala Ala Asp Ser 65 70 75 80 Gly His Leu Glu Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val 85 90 95 Asn Ala Gln Asp Lys Ala Gly Val Thr Pro Ala Asp Leu Ala Ala Ala 100 105 110 Trp Gly His Glu Asp Ile Ala Glu Val Leu Gln Lys Ala Ala 115 120 125 <210> 19 <211> 126 <212> PRT <213> Secuencia Artificial <220> <223> Dominio dise–ado con repeticiones de anquirina <400> 19 Gly Ser Asp Leu Gly Val Lys Leu Leu Trp Ala Ala Ala Arg Gly Gln 1 5 10 15 Asp Asp Glu Val Arg Ile Leu Leu Ala Ala Gly Ala Asp Val Asn Ala 20 25 30 Lys Asp Phe Gln Gly Ile Thr Pro Leu His Ile Ala Ala Gln Ser Gly 35 40 45 His Leu Glu Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn 50 55 60 Ala Lys Asp Val Thr Gly Asp Thr Pro Leu His Leu Ala Ala Gln His 65 70 75 80 Gly His Leu Val Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val 85 90 95 Asn Ala Gln Asp Glu Arg Gly Trp Thr Pro Ala Asp Leu Ala Ala Asp 100 105 110 Trp Gly His Glu Asp Ile Ala Glu Val Leu Gln Lys Ala Ala 115 120 125 <210> 20 <211> 126 <212> PRT <213> Secuencia Artificial <220> <223> Dominio dise–ado con repeticiones de anquirina <400> 20 Gly Ser Asp Leu Gly Lys Lys Leu Leu Glu Ala Ala Arg Ala Gly Gln 1 5 10 15 Asp Asp Glu Val Arg Ile Leu Met Ala Asn Gly Ala Asp Val Asn Ala 20 25 30 Lys Asp Glu Tyr Gly Leu Thr Pro Leu Tyr Leu Ala Thr Ala His Gly 35 40 45 His Leu Glu Ile Val Glu Val Leu Leu Lys Asn Gly Ala Asp Val Asn 50 55 60 Ala Val Asp Ala Ile Gly Phe Thr Pro Leu His Leu Ala Ala Phe Ile 65 70 75 80 Gly His Leu Glu Ile Ala Glu Val Leu Leu Lys His Gly Ala Asp Val 85 90 95 Asn Ala Gln Asp Lys Phe Gly Lys Thr Ala Phe Asp Ile Ser Ile Gly 100 105 110 Asn Gly Asn Glu Asp Leu Ala Glu Ile Leu Gln Lys Ala Ala 115 120 125 <210> 21 <211> 570 <212> PRT <213> Secuencia Artificial <220> <223> Prote’na que comprende cuatro dominios dise–ados con repeticiones de anquirina <400> 21 Gly Ser Asp Leu Gly Lys Lys Leu Leu Glu Ala Ala Arg Ala Gly Gln 1 5 10 15 Asp Asp Glu Val Arg Glu Leu Leu Lys Ala Gly Ala Asp Val Asn Ala 20 25 30 Lys Asp Tyr Phe Ser His Thr Pro Leu His Leu Ala Ala Arg Asn Gly 35 40 45 His Leu Lys Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn 50 55 60 Ala Lys Asp Phe Ala Gly Lys Thr Pro Leu His Leu Ala Ala Asn Glu 65 70 75 80 Gly His Leu Glu Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val 85 90 95 Asn Ala Gln Asp Ile Phe Gly Lys Thr Pro Ala Asp Ile Ala Ala Asp 100 105 110 Ala Gly His Glu Asp Ile Ala Glu Val Leu Gln Lys Ala Ala Gly Ser 115 120 125 Pro Thr Pro Thr Pro Thr Thr Pro Thr Pro Thr Pro Thr Thr Pro Thr 130 135 140 Pro Thr Pro Thr Gly Ser Asp Leu Gly Ile Lys Leu Leu Phe Ala Ala 145 150 155 160 Ala Lys Gly Gln Asp Asp Glu Val Arg Glu Leu Leu Lys Ala Gly Ala 165 170 175 Asp Val Asn Ala Lys Asp Phe Gln Gly Val Thr Pro Leu His Ile Ala 180 185 190 Ala Gln Ser Gly His Leu Glu Ile Val Glu Val Leu Leu Lys Ala Gly 195 200 205 Ala Asp Val Asn Ala Lys Asp Val Thr Gly Asp Thr Pro Leu His Leu 210 215 220 Ala Ala Gln His Gly His Leu Glu Ile Val Glu Val Leu Leu Lys Ala 225 230 235 240 Gly Ala Asp Val Asn Ala Gln Asp Glu Arg Gly Trp Thr Pro Ala Asp 245 250 255 Leu Ala Ala Asp Trp Gly His Glu Asp Ile Ala Glu Val Leu Gln Lys 260 265 270 Ala Ala Gly Ser Pro Thr Pro Thr Pro Thr Thr Pro Thr Pro Thr Pro 275 280 285 Thr Thr Pro Thr Pro Thr Pro Thr Gly Ser Asp Leu Gly Lys Lys Leu 290 295 300 Leu Glu Ala Ala Arg Ala Gly Gln Asp Asp Glu Val Arg Glu Leu Leu 305 310 315 320 Lys Ala Gly Ala Asp Val Asn Ala Lys Asp Glu Tyr Gly Leu Thr Pro 325 330 335 Leu Tyr Leu Ala Thr Ala His Gly His Leu Glu Ile Val Glu Val Leu 340 345 350 Leu Lys Ala Gly Ala Asp Val Asn Ala Val Asp Ala Ile Gly Phe Thr 355 360 365 Pro Leu His Leu Ala Ala Phe Ile Gly His Leu Glu Ile Ala Glu Val 370 375 380 Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Gln Asp Lys Phe Gly Lys 385 390 395 400 Thr Pro Ala Asp Ile Ala Ala Gly Ala Gly Asn Glu Asp Ile Ala Glu 405 410 415 Val Leu Gln Lys Ala Ala Gly Ser Pro Thr Pro Thr Pro Thr Thr Pro 420 425 430 Thr Pro Thr Pro Thr Thr Pro Thr Pro Thr Pro Thr Gly Ser Asp Leu 435 440 445 Gly Lys Lys Leu Leu Glu Ala Ala Arg Ala Gly Gln Asp Asp Glu Val 450 455 460 Arg Glu Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Lys Asp Tyr Phe 465 470 475 480 Ser His Thr Pro Leu His Leu Ala Ala Arg Asn Gly His Leu Lys Ile 485 490 495 Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Lys Asp Phe 500 505 510 Ala Gly Lys Thr Pro Leu His Leu Ala Ala Asn Glu Gly His Leu Glu 515 520 525 Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Gln Asp 530 535 540 Ile Phe Gly Lys Thr Pro Ala Asp Ile Ala Ala Asp Ala Gly His Glu 545 550 555 560 Asp Ile Ala Glu Val Leu Gln Lys Ala Ala 565 570 <210> 22 <211> 570 <212> PRT <213> Secuencia Artificial <220> <223> Prote’na que comprende cuatro dominios dise–ados con repeticiones de anquirina <400> 22 Gly Ser Asp Leu Gly Lys Lys Leu Leu Glu Ala Ala Arg Ala Gly Gln 1 5 10 15 Asp Asp Glu Val Arg Glu Leu Leu Lys Ala Gly Ala Asp Val Asn Ala 20 25 30 Lys Asp Tyr Phe Ser His Thr Pro Leu His Leu Ala Ala Arg Asn Gly 35 40 45 His Leu Lys Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn 50 55 60 Ala Lys Asp Phe Ala Gly Lys Thr Pro Leu His Leu Ala Ala Asn Asp 65 70 75 80 Gly His Leu Glu Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val 85 90 95 Asn Ala Gln Asp Ile Phe Gly Lys Thr Pro Ala Asp Ile Ala Ala Asp 100 105 110 Ala Gly His Glu Asp Ile Ala Glu Val Leu Gln Lys Ala Ala Gly Ser 115 120 125 Pro Thr Pro Thr Pro Thr Thr Pro Thr Pro Thr Pro Thr Thr Pro Thr 130 135 140 Pro Thr Pro Thr Gly Ser Asp Leu Gly Ile Lys Leu Leu Phe Ala Ala 145 150 155 160 Ala Lys Gly Gln Asp Asp Glu Val Arg Glu Leu Leu Lys Ala Gly Ala 165 170 175 Asp Val Asn Ala Lys Asp Phe Gln Gly Val Thr Pro Leu His Ile Ala 180 185 190 Ala Gln Ser Gly His Leu Glu Ile Val Glu Val Leu Leu Lys Ala Gly 195 200 205 Ala Asp Val Asn Ala Lys Asp Val Thr Gly Asp Thr Pro Leu His Leu 210 215 220 Ala Ala Gln His Gly His Leu Glu Ile Val Glu Val Leu Leu Lys Ala 225 230 235 240 Gly Ala Asp Val Asn Ala Gln Asp Glu Arg Gly Trp Thr Pro Ala Asp 245 250 255 Leu Ala Ala Asp Trp Gly His Glu Asp Ile Ala Glu Val Leu Gln Lys 260 265 270 Ala Ala Gly Ser Pro Thr Pro Thr Pro Thr Thr Pro Thr Pro Thr Pro 275 280 285 Thr Thr Pro Thr Pro Thr Pro Thr Gly Ser Asp Leu Gly Lys Lys Leu 290 295 300 Leu Glu Ala Ala Arg Ala Gly Gln Asp Asp Glu Val Arg Glu Leu Leu 305 310 315 320 Lys Ala Gly Ala Asp Val Asn Ala Lys Asp Glu Tyr Gly Leu Thr Pro 325 330 335 Leu Tyr Leu Ala Thr Ala His Gly His Leu Glu Ile Val Glu Val Leu 340 345 350 Leu Lys Ala Gly Ala Asp Val Asn Ala Val Asp Ala Ile Gly Phe Thr 355 360 365 Pro Leu His Leu Ala Ala Phe Ile Gly His Leu Glu Ile Ala Glu Val 370 375 380 Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Gln Asp Lys Phe Gly Lys 385 390 395 400 Thr Pro Ala Asp Ile Ala Ala Gly Ala Gly Asn Glu Asp Ile Ala Glu 405 410 415 Val Leu Gln Lys Ala Ala Gly Ser Pro Thr Pro Thr Pro Thr Thr Pro 420 425 430 Thr Pro Thr Pro Thr Thr Pro Thr Pro Thr Pro Thr Gly Ser Asp Leu 435 440 445 Gly Lys Lys Leu Leu Glu Ala Ala Arg Ala Gly Gln Asp Asp Glu Val 450 455 460 Arg Glu Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Lys Asp Tyr Phe 465 470 475 480 Ser His Thr Pro Leu His Leu Ala Ala Arg Asn Gly His Leu Lys Ile 485 490 495 Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Lys Asp Phe 500 505 510 Ala Gly Lys Thr Pro Leu His Leu Ala Ala Asn Asp Gly His Leu Glu 515 520 525 Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Gln Asp 530 535 540 Ile Phe Gly Lys Thr Pro Ala Asp Ile Ala Ala Asp Ala Gly His Glu 545 550 555 560 Asp Ile Ala Glu Val Leu Gln Lys Ala Ala 565 570 <210> 23 <211> 570 <212> PRT <213> Secuencia Artificial <220> <223> Prote’na que comprende cuatro dominios dise–ados con repeticiones de anquirina <400> 23 Gly Ser Asp Leu Gly Lys Lys Leu Leu Glu Ala Ala Arg Ala Gly Gln 1 5 10 15 Asp Asp Glu Val Arg Glu Leu Leu Lys Ala Gly Ala Asp Val Asn Ala 20 25 30 Lys Asp Tyr Phe Ser His Thr Pro Leu His Leu Ala Ala Arg Asn Gly 35 40 45 His Leu Lys Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn 50 55 60 Ala Lys Asp Phe Ala Gly Lys Thr Pro Leu His Leu Ala Ala Asn Glu 65 70 75 80 Gly His Leu Glu Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val 85 90 95 Asn Ala Gln Asp Ile Phe Gly Lys Thr Pro Ala Asp Ile Ala Ala Asp 100 105 110 Ala Gly His Glu Asp Ile Ala Glu Val Leu Gln Lys Ala Ala Gly Ser 115 120 125 Pro Thr Pro Thr Pro Thr Thr Pro Thr Pro Thr Pro Thr Thr Pro Thr 130 135 140 Pro Thr Pro Thr Gly Ser Asp Leu Gly Val Lys Leu Leu Trp Ala Ala 145 150 155 160 Ala Arg Gly Gln Asp Asp Glu Val Arg Glu Leu Leu Lys Ala Gly Ala 165 170 175 Asp Val Asn Ala Lys Asp Phe Gln Gly Ile Thr Pro Leu His Ile Ala 180 185 190 Ala Thr Asn Gly His Leu Glu Ile Val Glu Val Leu Leu Lys Ala Gly 195 200 205 Ala Asp Val Asn Ala Lys Asp Ile Thr Gly Glu Thr Pro Leu His His 210 215 220 Ala Ala Asp Ser Gly His Leu Glu Ile Val Glu Val Leu Leu Lys Ala 225 230 235 240 Gly Ala Asp Val Asn Ala Gln Asp Lys Ala Gly Val Thr Pro Ala Asp 245 250 255 Leu Ala Ala Ala Trp Gly His Glu Asp Ile Ala Glu Val Leu Gln Lys 260 265 270 Ala Ala Gly Ser Pro Thr Pro Thr Pro Thr Thr Pro Thr Pro Thr Pro 275 280 285 Thr Thr Pro Thr Pro Thr Pro Thr Gly Ser Asp Leu Gly Lys Lys Leu 290 295 300 Leu Glu Ala Ala Arg Ala Gly Gln Asp Asp Glu Val Arg Glu Leu Leu 305 310 315 320 Lys Ala Gly Ala Asp Val Asn Ala Lys Asp Glu Tyr Gly Leu Thr Pro 325 330 335 Leu Tyr Leu Ala Thr Ala His Gly His Leu Glu Ile Val Glu Val Leu 340 345 350 Leu Lys Ala Gly Ala Asp Val Asn Ala Val Asp Ala Ile Gly Phe Thr 355 360 365 Pro Leu His Leu Ala Ala Phe Ile Gly His Leu Glu Ile Ala Glu Val 370 375 380 Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Gln Asp Lys Phe Gly Lys 385 390 395 400 Thr Pro Ala Asp Ile Ala Ala Gly Ala Gly Asn Glu Asp Ile Ala Glu 405 410 415 Val Leu Gln Lys Ala Ala Gly Ser Pro Thr Pro Thr Pro Thr Thr Pro 420 425 430 Thr Pro Thr Pro Thr Thr Pro Thr Pro Thr Pro Thr Gly Ser Asp Leu 435 440 445 Gly Lys Lys Leu Leu Glu Ala Ala Arg Ala Gly Gln Asp Asp Glu Val 450 455 460 Arg Glu Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Lys Asp Tyr Phe 465 470 475 480 Ser His Thr Pro Leu His Leu Ala Ala Arg Asn Gly His Leu Lys Ile 485 490 495 Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Lys Asp Phe 500 505 510 Ala Gly Lys Thr Pro Leu His Leu Ala Ala Asn Glu Gly His Leu Glu 515 520 525 Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Gln Asp 530 535 540 Ile Phe Gly Lys Thr Pro Ala Asp Ile Ala Ala Asp Ala Gly His Glu 545 550 555 560 Asp Ile Ala Glu Val Leu Gln Lys Ala Ala 565 570 <210> 24 <211> 570 <212> PRT <213> Secuencia Artificial <220> <223> Prote’na que comprende cuatro dominios dise–ados con repeticiones de anquirina <400> 24 Gly Ser Asp Leu Gly Lys Lys Leu Leu Glu Ala Ala Arg Ala Gly Gln 1 5 10 15 Asp Asp Glu Val Arg Glu Leu Leu Lys Ala Gly Ala Asp Val Asn Ala 20 25 30 Lys Asp Tyr Phe Ser His Thr Pro Leu His Leu Ala Ala Arg Asn Gly 35 40 45 His Leu Lys Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn 50 55 60 Ala Lys Asp Phe Ala Gly Lys Thr Pro Leu His Leu Ala Ala Asn Glu 65 70 75 80 Gly His Leu Glu Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val 85 90 95 Asn Ala Gln Asp Ile Phe Gly Lys Thr Pro Ala Asp Ile Ala Ala Asp 100 105 110 Ala Gly His Glu Asp Ile Ala Glu Val Leu Gln Lys Ala Ala Gly Ser 115 120 125 Pro Thr Pro Thr Pro Thr Thr Pro Thr Pro Thr Pro Thr Thr Pro Thr 130 135 140 Pro Thr Pro Thr Gly Ser Asp Leu Gly Lys Lys Leu Leu Glu Ala Ala 145 150 155 160 Arg Ala Gly Gln Asp Asp Glu Val Arg Glu Leu Leu Lys Ala Gly Ala 165 170 175 Asp Val Asn Ala Lys Asp Tyr Phe Ser His Thr Pro Leu His Leu Ala 180 185 190 Ala Arg Asn Gly His Leu Lys Ile Val Glu Val Leu Leu Lys Ala Gly 195 200 205 Ala Asp Val Asn Ala Lys Asp Phe Ala Gly Lys Thr Pro Leu His Leu 210 215 220 Ala Ala Asn Glu Gly His Leu Glu Ile Val Glu Val Leu Leu Lys Ala 225 230 235 240 Gly Ala Asp Val Asn Ala Gln Asp Ile Phe Gly Lys Thr Pro Ala Asp 245 250 255 Ile Ala Ala Asp Ala Gly His Glu Asp Ile Ala Glu Val Leu Gln Lys 260 265 270 Ala Ala Gly Ser Pro Thr Pro Thr Pro Thr Thr Pro Thr Pro Thr Pro 275 280 285 Thr Thr Pro Thr Pro Thr Pro Thr Gly Ser Asp Leu Gly Ile Lys Leu 290 295 300 Leu Phe Ala Ala Ala Lys Gly Gln Asp Asp Glu Val Arg Glu Leu Leu 305 310 315 320 Lys Ala Gly Ala Asp Val Asn Ala Lys Asp Phe Gln Gly Val Thr Pro 325 330 335 Leu His Ile Ala Ala Gln Ser Gly His Leu Glu Ile Val Glu Val Leu 340 345 350 Leu Lys Ala Gly Ala Asp Val Asn Ala Lys Asp Val Thr Gly Asp Thr 355 360 365 Pro Leu His Leu Ala Ala Gln His Gly His Leu Glu Ile Val Glu Val 370 375 380 Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Gln Asp Glu Arg Gly Trp 385 390 395 400 Thr Pro Ala Asp Leu Ala Ala Asp Trp Gly His Glu Asp Ile Ala Glu 405 410 415 Val Leu Gln Lys Ala Ala Gly Ser Pro Thr Pro Thr Pro Thr Thr Pro 420 425 430 Thr Pro Thr Pro Thr Thr Pro Thr Pro Thr Pro Thr Gly Ser Asp Leu 435 440 445 Gly Lys Lys Leu Leu Glu Ala Ala Arg Ala Gly Gln Asp Asp Glu Val 450 455 460 Arg Glu Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Lys Asp Glu Tyr 465 470 475 480 Gly Leu Thr Pro Leu Tyr Leu Ala Thr Ala His Gly His Leu Glu Ile 485 490 495 Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Val Asp Ala 500 505 510 Ile Gly Phe Thr Pro Leu His Leu Ala Ala Phe Ile Gly His Leu Glu 515 520 525 Ile Ala Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Gln Asp 530 535 540 Lys Phe Gly Lys Thr Pro Ala Asp Ile Ala Ala Gly Ala Gly Asn Glu 545 550 555 560 Asp Ile Ala Glu Val Leu Gln Lys Ala Ala 565 570 <210> 25 <211> 570 <212> PRT <213> Secuencia Artificial <220> <223> Prote’na que comprende cuatro dominios dise–ados con repeticiones de anquirina <400> 25 Gly Ser Asp Leu Gly Lys Lys Leu Leu Glu Ala Ala Arg Ala Gly Gln 1 5 10 15 Asp Asp Glu Val Arg Glu Leu Leu Lys Ala Gly Ala Asp Val Asn Ala 20 25 30 Lys Asp Tyr Phe Ser His Thr Pro Leu His Leu Ala Ala Arg Asn Gly 35 40 45 His Leu Lys Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn 50 55 60 Ala Lys Asp Phe Ala Gly Lys Thr Pro Leu His Leu Ala Ala Asn Glu 65 70 75 80 Gly His Leu Glu Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val 85 90 95 Asn Ala Gln Asp Ile Phe Gly Lys Thr Pro Ala Asp Ile Ala Ala Asp 100 105 110 Ala Gly His Glu Asp Ile Ala Glu Val Leu Gln Lys Ala Ala Gly Ser 115 120 125 Pro Thr Pro Thr Pro Thr Thr Pro Thr Pro Thr Pro Thr Thr Pro Thr 130 135 140 Pro Thr Pro Thr Gly Ser Asp Leu Gly Lys Lys Leu Leu Glu Ala Ala 145 150 155 160 Arg Ala Gly Gln Asp Asp Glu Val Arg Glu Leu Leu Lys Ala Gly Ala 165 170 175 Asp Val Asn Ala Lys Asp Tyr Phe Ser His Thr Pro Leu His Leu Ala 180 185 190 Ala Arg Asn Gly His Leu Lys Ile Val Glu Val Leu Leu Lys Ala Gly 195 200 205 Ala Asp Val Asn Ala Lys Asp Phe Ala Gly Lys Thr Pro Leu His Leu 210 215 220 Ala Ala Asn Glu Gly His Leu Glu Ile Val Glu Val Leu Leu Lys Ala 225 230 235 240 Gly Ala Asp Val Asn Ala Gln Asp Ile Phe Gly Lys Thr Pro Ala Asp 245 250 255 Ile Ala Ala Asp Ala Gly His Glu Asp Ile Ala Glu Val Leu Gln Lys 260 265 270 Ala Ala Gly Ser Pro Thr Pro Thr Pro Thr Thr Pro Thr Pro Thr Pro 275 280 285 Thr Thr Pro Thr Pro Thr Pro Thr Gly Ser Asp Leu Gly Val Lys Leu 290 295 300 Leu Trp Ala Ala Ala Arg Gly Gln Asp Asp Glu Val Arg Glu Leu Leu 305 310 315 320 Lys Ala Gly Ala Asp Val Asn Ala Lys Asp Phe Gln Gly Ile Thr Pro 325 330 335 Leu His Ile Ala Ala Thr Asn Gly His Leu Glu Ile Val Glu Val Leu 340 345 350 Leu Lys Ala Gly Ala Asp Val Asn Ala Lys Asp Ile Thr Gly Glu Thr 355 360 365 Pro Leu His His Ala Ala Asp Ser Gly His Leu Glu Ile Val Glu Val 370 375 380 Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Gln Asp Lys Ala Gly Val 385 390 395 400 Thr Pro Ala Asp Leu Ala Ala Ala Trp Gly His Glu Asp Ile Ala Glu 405 410 415 Val Leu Gln Lys Ala Ala Gly Ser Pro Thr Pro Thr Pro Thr Thr Pro 420 425 430 Thr Pro Thr Pro Thr Thr Pro Thr Pro Thr Pro Thr Gly Ser Asp Leu 435 440 445 Gly Lys Lys Leu Leu Glu Ala Ala Arg Ala Gly Gln Asp Asp Glu Val 450 455 460 Arg Glu Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Lys Asp Glu Tyr 465 470 475 480 Gly Leu Thr Pro Leu Tyr Leu Ala Thr Ala His Gly His Leu Glu Ile 485 490 495 Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Val Asp Ala 500 505 510 Ile Gly Phe Thr Pro Leu His Leu Ala Ala Phe Ile Gly His Leu Glu 515 520 525 Ile Ala Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Gln Asp 530 535 540 Lys Phe Gly Lys Thr Pro Ala Asp Ile Ala Ala Gly Ala Gly Asn Glu 545 550 555 560 Asp Ile Ala Glu Val Leu Gln Lys Ala Ala 565 570 <210> 26 <211> 562 <212> PRT <213> Secuencia Artificial <220> <223> Prote’na que comprende cuatro dominios dise–ados con repeticiones de anquirina <400> 26 Gly Ser Asp Leu Gly Lys Lys Leu Leu Glu Ala Ala Arg Ala Gly Gln 1 5 10 15 Asp Asp Glu Val Arg Ile Leu Met Ala Asn Gly Ala Asp Val Asn Ala 20 25 30 Lys Asp Tyr Phe Ser His Thr Pro Leu His Leu Ala Ala Arg Asn Gly 35 40 45 His Leu Lys Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn 50 55 60 Ala Lys Asp Phe Ala Gly Lys Thr Pro Leu His Leu Ala Ala Asn Asp 65 70 75 80 Gly His Leu Glu Ile Val Glu Val Leu Leu Lys His Gly Ala Asp Val 85 90 95 Asn Ala Gln Asp Ile Phe Gly Lys Thr Pro Ala Asp Ile Ala Ala Asp 100 105 110 Ala Gly His Glu Asp Ile Ala Glu Val Leu Gln Lys Ala Ala Gly Gly 115 120 125 Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly 130 135 140 Gly Ser Gly Ser Asp Leu Gly Ala Lys Leu Leu Ser Asp Leu Gly Val 145 150 155 160 Lys Leu Leu Trp Ala Ala Ala Arg Gly Gln Asp Asp Glu Val Arg Ile 165 170 175 Leu Leu Ala Ala Gly Ala Asp Val Asn Ala Lys Asp Phe Gln Gly Ile 180 185 190 Thr Pro Leu His Ile Ala Ala Gln Ser Gly His Leu Glu Ile Val Glu 195 200 205 Val Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Lys Asp Val Thr Gly 210 215 220 Asp Thr Pro Leu His Leu Ala Ala Gln His Gly His Leu Val Ile Val 225 230 235 240 Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Gln Asp Glu Arg 245 250 255 Gly Trp Thr Pro Ala Asp Leu Ala Ala Asp Trp Gly His Glu Asp Ile 260 265 270 Ala Glu Val Leu Gln Lys Ala Ala Gly Gly Gly Gly Ser Gly Gly Gly 275 280 285 Gly Ser Gly Ser Asp Leu Gly Lys Lys Leu Leu Glu Ala Ala Arg Ala 290 295 300 Gly Gln Asp Asp Glu Val Arg Ile Leu Met Ala Asn Gly Ala Asp Val 305 310 315 320 Asn Ala Lys Asp Glu Tyr Gly Leu Thr Pro Leu Tyr Leu Ala Thr Ala 325 330 335 His Gly His Leu Glu Ile Val Glu Val Leu Leu Lys Asn Gly Ala Asp 340 345 350 Val Asn Ala Val Asp Ala Ile Gly Phe Thr Pro Leu His Leu Ala Ala 355 360 365 Phe Ile Gly His Leu Glu Ile Ala Glu Val Leu Leu Lys His Gly Ala 370 375 380 Asp Val Asn Ala Gln Asp Lys Phe Gly Lys Thr Ala Phe Asp Ile Ser 385 390 395 400 Ile Gly Asn Gly Asn Glu Asp Leu Ala Glu Ile Leu Gln Lys Ala Ala 405 410 415 Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly 420 425 430 Gly Gly Gly Ser Gly Ser Asp Leu Gly Lys Lys Leu Leu Glu Ala Ala 435 440 445 Arg Ala Gly Gln Asp Asp Glu Val Arg Ile Leu Met Ala Asn Gly Ala 450 455 460 Asp Val Asn Ala Lys Asp Tyr Phe Ser His Thr Pro Leu His Leu Ala 465 470 475 480 Ala Arg Asn Gly His Leu Lys Ile Val Glu Val Leu Leu Lys Ala Gly 485 490 495 Ala Asp Val Asn Ala Lys Asp Phe Ala Gly Lys Thr Pro Leu His Leu 500 505 510 Ala Ala Asn Asp Gly His Leu Glu Ile Val Glu Val Leu Leu Lys His 515 520 525 Gly Ala Asp Val Asn Ala Gln Asp Ile Phe Gly Lys Thr Pro Ala Asp 530 535 540 Ile Ala Ala Asp Ala Gly His Glu Asp Ile Ala Glu Val Leu Gln Lys 545 550 555 560 Ala Ala <210> 27 <211> 578 <212> PRT <213> Secuencia Artificial <220> <223> Prote’na que comprende cuatro dominios dise–ados con repeticiones de anquirina <400> 27 Gly Ser Asp Leu Gly Lys Lys Leu Leu Glu Ala Ala Arg Ala Gly Gln 1 5 10 15 Asp Asp Glu Val Arg Ile Leu Met Ala Asn Gly Ala Asp Val Asn Ala 20 25 30 Lys Asp Tyr Phe Ser His Thr Pro Leu His Leu Ala Ala Arg Asn Gly 35 40 45 His Leu Lys Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn 50 55 60 Ala Lys Asp Phe Ala Gly Lys Thr Pro Leu His Leu Ala Ala Asn Asp 65 70 75 80 Gly His Leu Glu Ile Val Glu Val Leu Leu Lys His Gly Ala Asp Val 85 90 95 Asn Ala Gln Asp Ile Phe Gly Lys Thr Pro Ala Asp Ile Ala Ala Asp 100 105 110 Ala Gly His Glu Asp Ile Ala Glu Val Leu Gln Lys Ala Ala Gly Ser 115 120 125 Pro Thr Pro Thr Pro Thr Thr Pro Thr Pro Thr Pro Thr Thr Pro Thr 130 135 140 Pro Thr Pro Thr Gly Ser Asp Leu Gly Ala Lys Leu Leu Ser Asp Leu 145 150 155 160 Gly Val Lys Leu Leu Trp Ala Ala Ala Arg Gly Gln Asp Asp Glu Val 165 170 175 Arg Ile Leu Leu Ala Ala Gly Ala Asp Val Asn Ala Lys Asp Phe Gln 180 185 190 Gly Ile Thr Pro Leu His Ile Ala Ala Gln Ser Gly His Leu Glu Ile 195 200 205 Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Lys Asp Val 210 215 220 Thr Gly Asp Thr Pro Leu His Leu Ala Ala Gln His Gly His Leu Val 225 230 235 240 Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Gln Asp 245 250 255 Glu Arg Gly Trp Thr Pro Ala Asp Leu Ala Ala Asp Trp Gly His Glu 260 265 270 Asp Ile Ala Glu Val Leu Gln Lys Ala Ala Gly Ser Pro Thr Pro Thr 275 280 285 Pro Thr Thr Pro Thr Pro Thr Pro Thr Thr Pro Thr Pro Thr Pro Thr 290 295 300 Gly Ser Asp Leu Gly Lys Lys Leu Leu Glu Ala Ala Arg Ala Gly Gln 305 310 315 320 Asp Asp Glu Val Arg Ile Leu Met Ala Asn Gly Ala Asp Val Asn Ala 325 330 335 Lys Asp Glu Tyr Gly Leu Thr Pro Leu Tyr Leu Ala Thr Ala His Gly 340 345 350 His Leu Glu Ile Val Glu Val Leu Leu Lys Asn Gly Ala Asp Val Asn 355 360 365 Ala Val Asp Ala Ile Gly Phe Thr Pro Leu His Leu Ala Ala Phe Ile 370 375 380 Gly His Leu Glu Ile Ala Glu Val Leu Leu Lys His Gly Ala Asp Val 385 390 395 400 Asn Ala Gln Asp Lys Phe Gly Lys Thr Ala Phe Asp Ile Ser Ile Gly 405 410 415 Asn Gly Asn Glu Asp Leu Ala Glu Ile Leu Gln Lys Ala Ala Gly Ser 420 425 430 Pro Thr Pro Thr Pro Thr Thr Pro Thr Pro Thr Pro Thr Thr Pro Thr 435 440 445 Pro Thr Pro Thr Gly Ser Asp Leu Gly Lys Lys Leu Leu Glu Ala Ala 450 455 460 Arg Ala Gly Gln Asp Asp Glu Val Arg Ile Leu Met Ala Asn Gly Ala 465 470 475 480 Asp Val Asn Ala Lys Asp Tyr Phe Ser His Thr Pro Leu His Leu Ala 485 490 495 Ala Arg Asn Gly His Leu Lys Ile Val Glu Val Leu Leu Lys Ala Gly 500 505 510 Ala Asp Val Asn Ala Lys Asp Phe Ala Gly Lys Thr Pro Leu His Leu 515 520 525 Ala Ala Asn Asp Gly His Leu Glu Ile Val Glu Val Leu Leu Lys His 530 535 540 Gly Ala Asp Val Asn Ala Gln Asp Ile Phe Gly Lys Thr Pro Ala Asp 545 550 555 560 Ile Ala Ala Asp Ala Gly His Glu Asp Ile Ala Glu Val Leu Gln Lys 565 570 575 Ala Ala <210> 28 <211> 283 <212> PRT <213> Secuencia Artificial <220> <223> Prote’na que comprende dos dominios dise–ados con repeticiones de anquirina <400> 28 Gly Ser Asp Leu Gly Ile Lys Leu Leu Phe Ala Ala Ala Lys Gly Gln 1 5 10 15 Asp Asp Glu Val Arg Glu Leu Leu Lys Ala Gly Ala Asp Val Asn Ala 20 25 30 Lys Asp Phe Gln Gly Val Thr Pro Leu His Ile Ala Ala Gln Ser Gly 35 40 45 His Leu Glu Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn 50 55 60 Ala Lys Asp Val Thr Gly Asp Thr Pro Leu His Leu Ala Ala Gln His 65 70 75 80 Gly His Leu Glu Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val 85 90 95 Asn Ala Gln Asp Glu Arg Gly Trp Thr Pro Ala Asp Leu Ala Ala Asp 100 105 110 Trp Gly His Glu Asp Ile Ala Glu Val Leu Gln Lys Ala Ala Gly Ser 115 120 125 Pro Thr Pro Thr Pro Thr Thr Pro Thr Pro Thr Pro Thr Thr Pro Thr 130 135 140 Pro Thr Pro Thr Gly Ser Asp Leu Gly Lys Lys Leu Leu Glu Ala Ala 145 150 155 160 Arg Ala Gly Gln Asp Asp Glu Val Arg Glu Leu Leu Lys Ala Gly Ala 165 170 175 Asp Val Asn Ala Lys Asp Glu Tyr Gly Leu Thr Pro Leu Tyr Leu Ala 180 185 190 Thr Ala His Gly His Leu Glu Ile Val Glu Val Leu Leu Lys Ala Gly 195 200 205 Ala Asp Val Asn Ala Val Asp Ala Ile Gly Phe Thr Pro Leu His Leu 210 215 220 Ala Ala Phe Ile Gly His Leu Glu Ile Ala Glu Val Leu Leu Lys Ala 225 230 235 240 Gly Ala Asp Val Asn Ala Gln Asp Lys Phe Gly Lys Thr Pro Ala Asp 245 250 255 Ile Ala Ala Gly Ala Gly Asn Glu Asp Ile Ala Glu Val Leu Gln Lys 260 265 270 Ala Ala Gly Gly Gly Ser Gly Gly Gly Ser Cys 275 280 <210> 29 <211> 414 <212> PRT <213> Secuencia Artificial <220> <223> Prote’na que comprende tres dominios dise–ados con repeticiones de anquirina <400> 29 Gly Ser Asp Leu Gly Lys Lys Leu Leu Glu Ala Ala Arg Ala Gly Gln 1 5 10 15 Asp Asp Glu Val Arg Ile Leu Met Ala Asn Gly Ala Asp Val Asn Ala 20 25 30 Lys Asp Tyr Phe Ser His Thr Pro Leu His Leu Ala Ala Arg Asn Gly 35 40 45 His Leu Lys Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn 50 55 60 Ala Lys Asp Phe Ala Gly Lys Thr Pro Leu His Leu Ala Ala Asn Asp 65 70 75 80 Gly His Leu Glu Ile Val Glu Val Leu Leu Lys His Gly Ala Asp Val 85 90 95 Asn Ala Gln Asp Ile Phe Gly Lys Thr Pro Ala Asp Ile Ala Ala Asp 100 105 110 Ala Gly His Glu Asp Ile Ala Glu Val Leu Gln Lys Leu Gly Gly Gly 115 120 125 Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly 130 135 140 Ser Arg Ser Asp Leu Gly Ala Lys Leu Leu Ser Asp Leu Gly Val Lys 145 150 155 160 Leu Leu Trp Ala Ala Ala Arg Gly Gln Asp Asp Glu Val Arg Ile Leu 165 170 175 Leu Ala Ala Gly Ala Asp Val Asn Ala Lys Asp Phe Gln Gly Ile Thr 180 185 190 Pro Leu His Ile Ala Ala Gln Ser Gly His Leu Glu Ile Val Glu Val 195 200 205 Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Lys Asp Val Thr Gly Asp 210 215 220 Thr Pro Leu His Leu Ala Ala Gln His Gly His Leu Val Ile Val Glu 225 230 235 240 Val Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Gln Asp Glu Arg Gly 245 250 255 Trp Thr Pro Ala Asp Leu Ala Ala Asp Trp Gly His Glu Asp Ile Ala 260 265 270 Glu Val Leu Gln Lys Leu Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser 275 280 285 Arg Ser Asp Leu Gly Lys Lys Leu Leu Glu Ala Ala Arg Ala Gly Gln 290 295 300 Asp Asp Glu Val Arg Ile Leu Met Ala Asn Gly Ala Asp Val Asn Ala 305 310 315 320 Lys Asp Glu Tyr Gly Leu Thr Pro Leu Tyr Leu Ala Thr Ala His Gly 325 330 335 His Leu Glu Ile Val Glu Val Leu Leu Lys Asn Gly Ala Asp Val Asn 340 345 350 Ala Val Asp Ala Ile Gly Phe Thr Pro Leu His Leu Ala Ala Phe Ile 355 360 365 Gly His Leu Glu Ile Ala Glu Val Leu Leu Lys His Gly Ala Asp Val 370 375 380 Asn Ala Gln Asp Lys Phe Gly Lys Thr Ala Phe Asp Ile Ser Ile Gly 385 390 395 400 Asn Gly Asn Glu Asp Leu Ala Glu Ile Leu Gln Lys Leu Asn 405 410 <210> 30 <211> 562 <212> PRT <213> Secuencia Artificial <220> <223> Prote’na que comprende cuatro dominios dise–ados con repeticiones de anquirina <400> 30 Gly Ser Asp Leu Gly Lys Lys Leu Leu Glu Ala Ala Arg Ala Gly Gln 1 5 10 15 Asp Asp Glu Val Arg Ile Leu Met Ala Asn Gly Ala Asp Val Asn Ala 20 25 30 Lys Asp Tyr Phe Ser His Thr Pro Leu His Leu Ala Ala Arg Asn Gly 35 40 45 His Leu Lys Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn 50 55 60 Ala Lys Asp Phe Ala Gly Lys Thr Pro Leu His Leu Ala Ala Asn Asp 65 70 75 80 Gly His Leu Glu Ile Val Glu Val Leu Leu Lys His Gly Ala Asp Val 85 90 95 Asn Ala Gln Asp Ile Phe Gly Lys Thr Pro Ala Asp Ile Ala Ala Asp 100 105 110 Ala Gly His Glu Asp Ile Ala Glu Val Leu Gln Lys Ala Ala Gly Gly 115 120 125 Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly 130 135 140 Gly Ser Gly Ser Asp Leu Gly Lys Lys Leu Leu Glu Ala Ala Arg Ala 145 150 155 160 Gly Gln Asp Asp Glu Val Arg Ile Leu Met Ala Asn Gly Ala Asp Val 165 170 175 Asn Ala Lys Asp Tyr Phe Ser His Thr Pro Leu His Leu Ala Ala Arg 180 185 190 Asn Gly His Leu Lys Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp 195 200 205 Val Asn Ala Lys Asp Phe Ala Gly Lys Thr Pro Leu His Leu Ala Ala 210 215 220 Asn Asp Gly His Leu Glu Ile Val Glu Val Leu Leu Lys His Gly Ala 225 230 235 240 Asp Val Asn Ala Gln Asp Ile Phe Gly Lys Thr Pro Ala Asp Ile Ala 245 250 255 Ala Asp Ala Gly His Glu Asp Ile Ala Glu Val Leu Gln Lys Ala Ala 260 265 270 Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly 275 280 285 Gly Gly Gly Ser Gly Ser Asp Leu Gly Ala Lys Leu Leu Ser Asp Leu 290 295 300 Gly Val Lys Leu Leu Trp Ala Ala Ala Arg Gly Gln Asp Asp Glu Val 305 310 315 320 Arg Ile Leu Leu Ala Ala Gly Ala Asp Val Asn Ala Lys Asp Phe Gln 325 330 335 Gly Ile Thr Pro Leu His Ile Ala Ala Gln Ser Gly His Leu Glu Ile 340 345 350 Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Lys Asp Val 355 360 365 Thr Gly Asp Thr Pro Leu His Leu Ala Ala Gln His Gly His Leu Val 370 375 380 Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Gln Asp 385 390 395 400 Glu Arg Gly Trp Thr Pro Ala Asp Leu Ala Ala Asp Trp Gly His Glu 405 410 415 Asp Ile Ala Glu Val Leu Gln Lys Ala Ala Gly Gly Gly Gly Ser Gly 420 425 430 Gly Gly Gly Ser Gly Ser Asp Leu Gly Lys Lys Leu Leu Glu Ala Ala 435 440 445 Arg Ala Gly Gln Asp Asp Glu Val Arg Ile Leu Met Ala Asn Gly Ala 450 455 460 Asp Val Asn Ala Lys Asp Glu Tyr Gly Leu Thr Pro Leu Tyr Leu Ala 465 470 475 480 Thr Ala His Gly His Leu Glu Ile Val Glu Val Leu Leu Lys Asn Gly 485 490 495 Ala Asp Val Asn Ala Val Asp Ala Ile Gly Phe Thr Pro Leu His Leu 500 505 510 Ala Ala Phe Ile Gly His Leu Glu Ile Ala Glu Val Leu Leu Lys His 515 520 525 Gly Ala Asp Val Asn Ala Gln Asp Lys Phe Gly Lys Thr Ala Phe Asp 530 535 540 Ile Ser Ile Gly Asn Gly Asn Glu Asp Leu Ala Glu Ile Leu Gln Lys 545 550 555 560 Ala Ala <210> 31 <211> 580 <212> PRT <213> Secuencia Artificial <220> <223> Prote’na que comprende cuatro dominios dise–ados con repeticiones de anquirina <400> 31 Met Arg Gly Ser His His His His His His Gly Ser Asp Leu Gly Lys 1 5 10 15 Lys Leu Leu Glu Ala Ala Arg Ala Gly Gln Asp Asp Glu Val Arg Glu 20 25 30 Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Lys Asp Tyr Phe Ser His 35 40 45 Thr Pro Leu His Leu Ala Ala Arg Asn Gly His Leu Lys Ile Val Glu 50 55 60 Val Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Lys Asp Phe Ala Gly 65 70 75 80 Lys Thr Pro Leu His Leu Ala Ala Asn Glu Gly His Leu Glu Ile Val 85 90 95 Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Gln Asp Ile Phe 100 105 110 Gly Lys Thr Pro Ala Asp Ile Ala Ala Asp Ala Gly His Glu Asp Ile 115 120 125 Ala Glu Val Leu Gln Lys Ala Ala Gly Ser Pro Thr Pro Thr Pro Thr 130 135 140 Thr Pro Thr Pro Thr Pro Thr Thr Pro Thr Pro Thr Pro Thr Gly Ser 145 150 155 160 Asp Leu Gly Ile Lys Leu Leu Phe Ala Ala Ala Lys Gly Gln Asp Asp 165 170 175 Glu Val Arg Glu Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Lys Asp 180 185 190 Phe Gln Gly Val Thr Pro Leu His Ile Ala Ala Gln Ser Gly His Leu 195 200 205 Glu Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Lys 210 215 220 Asp Val Thr Gly Asp Thr Pro Leu His Leu Ala Ala Gln His Gly His 225 230 235 240 Leu Glu Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn Ala 245 250 255 Gln Asp Glu Arg Gly Trp Thr Pro Ala Asp Leu Ala Ala Asp Trp Gly 260 265 270 His Glu Asp Ile Ala Glu Val Leu Gln Lys Ala Ala Gly Ser Pro Thr 275 280 285 Pro Thr Pro Thr Thr Pro Thr Pro Thr Pro Thr Thr Pro Thr Pro Thr 290 295 300 Pro Thr Gly Ser Asp Leu Gly Lys Lys Leu Leu Glu Ala Ala Arg Ala 305 310 315 320 Gly Gln Asp Asp Glu Val Arg Glu Leu Leu Lys Ala Gly Ala Asp Val 325 330 335 Asn Ala Lys Asp Glu Tyr Gly Leu Thr Pro Leu Tyr Leu Ala Thr Ala 340 345 350 His Gly His Leu Glu Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp 355 360 365 Val Asn Ala Val Asp Ala Ile Gly Phe Thr Pro Leu His Leu Ala Ala 370 375 380 Phe Ile Gly His Leu Glu Ile Ala Glu Val Leu Leu Lys Ala Gly Ala 385 390 395 400 Asp Val Asn Ala Gln Asp Lys Phe Gly Lys Thr Pro Ala Asp Ile Ala 405 410 415 Ala Gly Ala Gly Asn Glu Asp Ile Ala Glu Val Leu Gln Lys Ala Ala 420 425 430 Gly Ser Pro Thr Pro Thr Pro Thr Thr Pro Thr Pro Thr Pro Thr Thr 435 440 445 Pro Thr Pro Thr Pro Thr Gly Ser Asp Leu Gly Lys Lys Leu Leu Glu 450 455 460 Ala Ala Arg Ala Gly Gln Asp Asp Glu Val Arg Glu Leu Leu Lys Ala 465 470 475 480 Gly Ala Asp Val Asn Ala Lys Asp Tyr Phe Ser His Thr Pro Leu His 485 490 495 Leu Ala Ala Arg Asn Gly His Leu Lys Ile Val Glu Val Leu Leu Lys 500 505 510 Ala Gly Ala Asp Val Asn Ala Lys Asp Phe Ala Gly Lys Thr Pro Leu 515 520 525 His Leu Ala Ala Asn Glu Gly His Leu Glu Ile Val Glu Val Leu Leu 530 535 540 Lys Ala Gly Ala Asp Val Asn Ala Gln Asp Ile Phe Gly Lys Thr Pro 545 550 555 560 Ala Asp Ile Ala Ala Asp Ala Gly His Glu Asp Ile Ala Glu Val Leu 565 570 575 Gln Lys Ala Ala 580 <210> 32 <211> 274 <212> PRT <213> Secuencia Artificial <220> <223> Prote’na que comprende dos dominios dise–ados con repeticiones de anquirina <400> 32 Gly Ser Asp Leu Gly Ile Lys Leu Leu Phe Ala Ala Ala Lys Gly Gln 1 5 10 15 Asp Asp Glu Val Arg Glu Leu Leu Lys Ala Gly Ala Asp Val Asn Ala 20 25 30 Lys Asp Phe Gln Gly Val Thr Pro Leu His Ile Ala Ala Gln Ser Gly 35 40 45 His Leu Glu Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn 50 55 60 Ala Lys Asp Val Thr Gly Asp Thr Pro Leu His Leu Ala Ala Gln His 65 70 75 80 Gly His Leu Glu Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val 85 90 95 Asn Ala Gln Asp Glu Arg Gly Trp Thr Pro Ala Asp Leu Ala Ala Asp 100 105 110 Trp Gly His Glu Asp Ile Ala Glu Val Leu Gln Lys Ala Ala Gly Ser 115 120 125 Pro Thr Pro Thr Pro Thr Thr Pro Thr Pro Thr Pro Thr Thr Pro Thr 130 135 140 Pro Thr Pro Thr Gly Ser Asp Leu Gly Lys Lys Leu Leu Glu Ala Ala 145 150 155 160 Arg Ala Gly Gln Asp Asp Glu Val Arg Glu Leu Leu Lys Ala Gly Ala 165 170 175 Asp Val Asn Ala Lys Asp Glu Tyr Gly Leu Thr Pro Leu Tyr Leu Ala 180 185 190 Thr Ala His Gly His Leu Glu Ile Val Glu Val Leu Leu Lys Ala Gly 195 200 205 Ala Asp Val Asn Ala Val Asp Ala Ile Gly Phe Thr Pro Leu His Leu 210 215 220 Ala Ala Phe Ile Gly His Leu Glu Ile Ala Glu Val Leu Leu Lys Ala 225 230 235 240 Gly Ala Asp Val Asn Ala Gln Asp Lys Phe Gly Lys Thr Pro Ala Asp 245 250 255 Ile Ala Ala Gly Ala Gly Asn Glu Asp Ile Ala Glu Val Leu Gln Lys 260 265 270 Ala Ala <210> 33 <211> 422 <212> PRT <213> Secuencia Artificial <220> <223> Prote’na que comprende tres dominios dise–ados con repeticiones de anquirina <400> 33 Gly Ser Asp Leu Gly Lys Lys Leu Leu Glu Ala Ala Arg Ala Gly Gln 1 5 10 15 Asp Asp Glu Val Arg Glu Leu Leu Lys Ala Gly Ala Asp Val Asn Ala 20 25 30 Lys Asp Tyr Phe Ser His Thr Pro Leu His Leu Ala Ala Arg Asn Gly 35 40 45 His Leu Lys Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val Asn 50 55 60 Ala Lys Asp Phe Ala Gly Lys Thr Pro Leu His Leu Ala Ala Asn Glu 65 70 75 80 Gly His Leu Glu Ile Val Glu Val Leu Leu Lys Ala Gly Ala Asp Val 85 90 95 Asn Ala Gln Asp Ile Phe Gly Lys Thr Pro Ala Asp Ile Ala Ala Asp 100 105 110 Ala Gly His Glu Asp Ile Ala Glu Val Leu Gln Lys Ala Ala Gly Ser 115 120 125 Pro Thr Pro Thr Pro Thr Thr Pro Thr Pro Thr Pro Thr Thr Pro Thr 130 135 140 Pro Thr Pro Thr Gly Ser Asp Leu Gly Ile Lys Leu Leu Phe Ala Ala 145 150 155 160 Ala Lys Gly Gln Asp Asp Glu Val Arg Glu Leu Leu Lys Ala Gly Ala 165 170 175 Asp Val Asn Ala Lys Asp Phe Gln Gly Val Thr Pro Leu His Ile Ala 180 185 190 Ala Gln Ser Gly His Leu Glu Ile Val Glu Val Leu Leu Lys Ala Gly 195 200 205 Ala Asp Val Asn Ala Lys Asp Val Thr Gly Asp Thr Pro Leu His Leu 210 215 220 Ala Ala Gln His Gly His Leu Glu Ile Val Glu Val Leu Leu Lys Ala 225 230 235 240 Gly Ala Asp Val Asn Ala Gln Asp Glu Arg Gly Trp Thr Pro Ala Asp 245 250 255 Leu Ala Ala Asp Trp Gly His Glu Asp Ile Ala Glu Val Leu Gln Lys 260 265 270 Ala Ala Gly Ser Pro Thr Pro Thr Pro Thr Thr Pro Thr Pro Thr Pro 275 280 285 Thr Thr Pro Thr Pro Thr Pro Thr Gly Ser Asp Leu Gly Lys Lys Leu 290 295 300 Leu Glu Ala Ala Arg Ala Gly Gln Asp Asp Glu Val Arg Glu Leu Leu 305 310 315 320 Lys Ala Gly Ala Asp Val Asn Ala Lys Asp Glu Tyr Gly Leu Thr Pro 325 330 335 Leu Tyr Leu Ala Thr Ala His Gly His Leu Glu Ile Val Glu Val Leu 340 345 350 Leu Lys Ala Gly Ala Asp Val Asn Ala Val Asp Ala Ile Gly Phe Thr 355 360 365 Pro Leu His Leu Ala Ala Phe Ile Gly His Leu Glu Ile Ala Glu Val 370 375 380 Leu Leu Lys Ala Gly Ala Asp Val Asn Ala Gln Asp Lys Phe Gly Lys 385 390 395 400 Thr Pro Ala Asp Ile Ala Ala Gly Ala Gly Asn Glu Asp Ile Ala Glu 405 410 415 Val Leu Gln Lys Ala Ala 420