US20040171115A1 - Multi-functional hematopoietic fusion proteins between sequence rearranged G-CSF receptor agonists and other hematopoietic factors - Google Patents

Multi-functional hematopoietic fusion proteins between sequence rearranged G-CSF receptor agonists and other hematopoietic factors Download PDF

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US20040171115A1
US20040171115A1 US10/695,584 US69558403A US2004171115A1 US 20040171115 A1 US20040171115 A1 US 20040171115A1 US 69558403 A US69558403 A US 69558403A US 2004171115 A1 US2004171115 A1 US 2004171115A1
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xaa
ala
ser
pro
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Yiqing Feng
Nicholas Staten
Charles Baum
Neena Summers
Maire Caparon
S. Bauer
Linda Zurfluh
John McKearn
Barbara Klein
Stephen Lee
Charles McWherter
Judith Giri
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Priority claimed from PCT/US1996/015774 external-priority patent/WO1997012985A2/en
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    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/52—Cytokines; Lymphokines; Interferons
    • C07K14/54—Interleukins [IL]
    • C07K14/5403—IL-3
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/52—Cytokines; Lymphokines; Interferons
    • C07K14/524—Thrombopoietin, i.e. C-MPL ligand
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/52—Cytokines; Lymphokines; Interferons
    • C07K14/53—Colony-stimulating factor [CSF]
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
    • C12N15/09—Recombinant DNA-technology
    • C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
    • C12N15/62—DNA sequences coding for fusion proteins
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K35/00—Medicinal preparations containing materials or reaction products thereof with undetermined constitution
    • A61K35/12—Materials from mammals; Compositions comprising non-specified tissues or cells; Compositions comprising non-embryonic stem cells; Genetically modified cells
    • A61K2035/124—Materials from mammals; Compositions comprising non-specified tissues or cells; Compositions comprising non-embryonic stem cells; Genetically modified cells the cells being hematopoietic, bone marrow derived or blood cells
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K39/00—Medicinal preparations containing antigens or antibodies
    • A61K2039/51—Medicinal preparations containing antigens or antibodies comprising whole cells, viruses or DNA/RNA
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K48/00—Medicinal preparations containing genetic material which is inserted into cells of the living body to treat genetic diseases; Gene therapy
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2319/00—Fusion polypeptide
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2319/00—Fusion polypeptide
    • C07K2319/70—Fusion polypeptide containing domain for protein-protein interaction
    • C07K2319/74—Fusion polypeptide containing domain for protein-protein interaction containing a fusion for binding to a cell surface receptor
    • C07K2319/75—Fusion polypeptide containing domain for protein-protein interaction containing a fusion for binding to a cell surface receptor containing a fusion for activation of a cell surface receptor, e.g. thrombopoeitin, NPY and other peptide hormones

Definitions

  • the diskette is labeled as follows:
  • the diskette contains the following file in ASCII file format: File Name File size Creation Date Sequence.txt 574 kb Oct. 23, 2003
  • the present invention relates to multi-functional hematopoietic receptor agonists.
  • Colony stimulating factors which stimulate the differentiation and/or proliferation of bone marrow cells have generated much interest because of their therapeutic potential for restoring depressed levels of hematopoietic stem cell-derived cells.
  • CSFs in both human and murine systems have been identified and distinguished according to their activities.
  • granulocyte-CSF G-CSF
  • macrophage-CSF M-CSF
  • GM-CSF and interleukin-3 IL-3
  • IL-3 also stimulates the formation of mast, megakaryocyte and pure and mixed erythroid colonies.
  • U.S. Pat. No. 4,877,729 and U.S. Pat. No. 4,959,455 disclose human IL-3 and gibbon IL-3 cDNAs and the protein sequences for which they code.
  • the hIL-3 disclosed has serine rather than proline at position 8 in the protein sequence.
  • PCT International Patent Application
  • Wo 88/00598 discloses gibbon- and human-like IL-3.
  • the hIL-3 contains a Ser 8 ->Pro 8 replacement. Suggestions are made to replace Cys by Ser, thereby breaking the disulfide bridge, and to replace one or more amino acids at the glycosylation sites.
  • U.S. Pat. No. 4,810,643 discloses the DNA sequence encoding human G-CSF.
  • WO 91/02754 discloses a fusion protein comprised of GM-CSF and IL-3 which has increased biological activity compared to GM-CSF or IL-3 alone. Also disclosed are nonglycosylated IL-3 and GM-CSF analog proteins as components of the multi-functional hematopoietic receptor agonist.
  • WO 92/04455 discloses fusion proteins composed of IL-3 fused to a lymphokine selected from the group consisting of IL-3, IL-6, IL-7, IL-9, IL-11, EPO and G-CSF.
  • WO 95/21197 and WO 95/21254 disclose fusion proteins capable of broad multi-functional hematopoietic properties.
  • GB 2,285,446 relates to the c-mpl ligand (thrombopoietin) and various forms of thrombopoietin which are shown to influence the replication, differentiation and maturation of megakaryocytes and megakaryocytes progenitors which may be used for the treatment of thrombocytopenia.
  • EP 675,201 A1 relates to the c-mpl ligand (Megakaryocyte growth and development factor (MGDF), allelic variations of c-mpl ligand and c-mpl ligand attached to water soluble polymers such as polyethylene glycol.
  • MGDF Megakaryocyte growth and development factor
  • WO 95/21920 provides the murine and human c-mpl ligand and polypeptide fragments thereof.
  • the proteins are useful for in vivo and ex vivo therapy for stimulating platelet production.
  • the new sequence is joined, either directly or through an additional portion of sequence (linker), to an amino acid that is at or near the original N-terminus, and the new sequence continues with the same sequence as the original until it reaches a point that is at or near the amino acid that was N-terminal to the breakpoint site of the original sequence, this residue forming the new C-terminus of the chain.
  • linker an additional portion of sequence
  • yeast Ritco-Vonsovici et al. Biochemistry phosphoglycerate 34: 16543-16551, 1995). dehydrogenase Enzyme Inhibitor basic pancreatic Goldenberg & Creighton, J. Mol. trypsin inhibitor Biol. 165: 407-413, 1983). Cytokines interleukin-1b Horlick et al., Protein Eng. 5: 427-431, 1992). interleukin-4 Kreitman et al., Cytokine 7: 311-318, 1995). Tyrosine Kinase Recognition Domain a-spectrin SH3 Viguera, et al., J. Mol. Biol. domain 247: 670-681, 1995).
  • sequence rearranged protein appeared to have many nearly identical properties as its natural counterpart (basic pancreatic trypsin inhibitor, T4 lysozyme, ribonuclease Tl, Bacillus b-glucanase, interleukin-1b, a-spectrin SH3 domain, pepsinogen, interleukin-4).
  • Novel hematopoietic proteins of this invention are represented by the formulas:
  • R 1 and R 2 are independently selected from the group consisting of;
  • a polypeptide comprising; a modified human G-CSF amino acid sequence of the formula: 1 Xaa Xaa Xaa Gly Pro Ala Ser Ser Leu (SEQ ID NO: 1) 10 Pro Gln Ser Xaa Leu Leu Xaa Xaa Xaa 20 Glu Gln Val Xaa Lys Xaa Gln Gly Xaa 30 Gly Ala Xaa Leu Gln Glu Xaa Leu Xaa 40 Ala Thr Tyr Lys Leu Xaa Xaa Xaa Glu 50 Xaa Xaa Val Xaa Xaa Gly His Ser Xaa 60 Gly Ile Pro Trp Ala Pro Leu Ser Ser 70 Xaa Pro Ser Xaa Ala Leu Xaa Leu Ala 80 Gly Xaa Leu Ser Gln Leu His Ser Gly 90 Leu Phe Leu Tyr Gln G
  • Xaa at position 1 is Thr, Ser, Arg, Tyr or Gly;
  • Xaa at position 2 is Pro or Leu
  • Xaa at position 3 is Leu, Arg, Tyr or Ser;
  • Xaa at position 13 is Phe, Ser, His, Thr or Pro;
  • Xaa at position 16 is Lys, Pro, Ser, Thr or His;
  • Xaa at position 17 is Cys, Ser, Gly, Ala, Ile, Tyr or Arg;
  • Xaa at position 18 is Leu, Thr, Pro, His, Ile or Cys
  • Xaa at position 22 is Arg, Tyr, Ser, Thr or Ala;
  • Xaa at position 24 is Ile, Pro, Tyr or Leu;
  • Xaa at position 27 is Asp, or Gly;
  • Xaa at position 30 is Ala, Ile, Leu or Gly;
  • Xaa at position 34 is Lys or Ser
  • Xaa at position 36 is Cys or Ser
  • Xaa at position 42 is Cys or Ser
  • Xaa at position 43 is His, Thr, Gly, Val, Lys, Trp, Ala, Arg, Cys, or Leu;
  • Xaa at position 44 is Pro, Gly, Arg, Asp, Val, Ala, His, Trp, Gln, or Thr;
  • Xaa at position 46 is Glu, Arg, Phe, Arg, Ile or Ala;
  • Xaa at position 47 is Leu or Thr
  • Xaa at position 49 is Leu, Phe, Arg or Ser;
  • Xaa at position 50 is Leu, Ile, His, Pro or Tyr;
  • Xaa at position 54 is Leu or His
  • Xaa at position 64 is Cys or Ser
  • Xaa at position 67 is Gln, Lys, Leu or Cys;
  • Xaa at position 70 is Gln, Pro, Leu, Arg or Ser;
  • Xaa at position 74 is Cys or Ser
  • Xaa at position 104 is Asp, Gly or Val;
  • Xaa at position 108 is Leu, Ala, Val, Arg, Trp, Gln or Gly;
  • Xaa at position 115 is Thr, His, Leu or Ala
  • Xaa at position 120 is Gln, Gly, Arg, Lys or His
  • Xaa at position 123 is Glu, Arg, Phe or Thr
  • Xaa at position 144 is Phe, His, Arg, Pro, Leu, Gln or Glu;
  • Xaa at position 146 is Arg or Gln;
  • Xaa at position 147 is Arg or Gln;
  • Xaa at position 156 is His, Gly or Ser;
  • Xaa at position 159 is Ser, Arg, Thr, Tyr, Val or Gly;
  • Xaa at position 162 is Glu, Leu, Gly or Trp;
  • Xaa at position 163 is Val, Gly, Arg or Ala;
  • Xaa at position 169 is Arg, Ser, Leu, Arg or Cys;
  • Xaa at position 170 is His, Arg or Ser;
  • N-terminus is joined to the C-terminus directly or through a linker capable of joining the N-terminus to the C-terminus and having new C- and N-termini at amino acids; 38-39 39-40 40-41 41-42 42-43 43-44 45-46 48-49 49-50 52-53 53-54 54-55 55-56 56-57 57-58 58-59 59-60 60-61 61-62 62-63 63-64 64-65 65-66 66-67 67-68 68-69 69-70 70-71 71-72 91-92 92-93 93-94 94-95 95-96 96-97 97-98 98-99 99-100 123-124 124-125 125-126 126-127 128-129 128-129 129-130 130-131 131-132 132-133 133-134 134-135 135-136 136-137 137-138 138-139 139-140 140-141 141
  • a polypeptide comprising; a modified hIL-3 amino acid sequence of the formula: Ala Pro Met Thr Gln Thr Thr Ser Leu (SEQ ID NO: 2) 1 5 Lys Thr Ser Trp Val Asn Cys Xaa Xaa 10 15 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa 20 25 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa 30 35 Xaa Xaa Asn Xaa Xaa Xaa Xaa Xaa Xaa Xaa 40 45 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa 50 Xaa Xaa Xaa Xaa Xaa
  • Xaa at position 17 is Ser, Lys, Gly, Asp, Met, Gln, or Arg;
  • Xaa at position 18 is Asn, His, Leu, Ile, Phe, Arg, or Gln;
  • Xaa at position 19 is Met, Phe, Ile, Arg, Gly, Ala, or Cys;
  • Xaa at position 20 is Ile, Cys, Gln, Glu, Arg, Pro, or Ala;
  • Xaa at position 21 is Asp, Phe, Lys, Arg, Ala, Gly, Glu, Gln, Asn, Thr, Ser or Val;
  • Xaa at position 22 is Glu, Trp, Pro, Ser, Ala, His, Asp, Asn, Gln, Leu, Val or Gly;
  • Xaa at position 23 is Ile, Val, Ala, Gly, Trp, Lys, Phe, Leu, Ser, or Arg;
  • Xaa at position 24 is Ile, Gly, Val, Arg, Ser, Phe, or Leu;
  • Xaa at position 25 is Thr, His, Gly, Gln, Arg, Pro, or Ala;
  • Xaa at position 26 is His, Thr, Phe, Gly, Arg, Ala, or Trp;
  • Xaa at position 27 is Leu, Gly, Arg, Thr, Ser, or Ala;
  • Xaa at position 28 is Lys, Arg, Leu, Gln, Gly, Pro, Val or Trp;
  • Xaa at position 29 is Gln, Asn, Leu, Pro, Arg, or Val;
  • Xaa at position 30 is Pro, His, Thr, Gly, Asp, Gln, Ser, Leu, or Lys;
  • Xaa at position 31 is Pro, Asp, Gly, Ala, Arg, Leu, or Gln;
  • Xaa at position 32 is Leu, Val, Arg, Gln, Asn, Gly, Ala, or Glu;
  • Xaa at position 33 is Pro, Leu, Gln, Ala, Thr, or Glu;
  • Xaa at position 34 is Leu, Val, Gly, Ser, Lys, Glu, Gln, Thr, Arg, Ala, Phe, Ile or Met;
  • Xaa at position 35 is Leu, Ala, Gly, Asn, Pro, Gln, or Val;
  • Xaa at position 36 is Asp, Leu, or Val
  • Xaa at position 37 is Phe, Ser, Pro, Trp, or Ile;
  • Xaa at position 38 is Asn, or Ala;
  • Xaa at position 40 is Leu, Trp, or Arg;
  • Xaa at position 41 is Asn, Cys, Arg, Leu, His, Met, or Pro;
  • Xaa at position 42 is Gly, Asp, Ser, Cys, Asn, Lys, Thr, Leu, Val, Glu, Phe, Tyr, Ile, Met or Ala;
  • Xaa at position 43 is Glu, Asn, Tyr, Leu, Phe, Asp, Ala, Cys, Gln, Arg, Thr, Gly or Ser;
  • Xaa at position 44 is Asp, Ser, Leu, Arg, Lys, Thr, Met, Trp, Glu, Asn, Gln, Ala or Pro;
  • Xaa at position 45 is Gln, Pro, Phe, Val, Met, Leu, Thr, Lys, Trp, Asp, Asn, Arg, Ser, Ala, Ile, Glu or His;
  • Xaa at position 46 is Asp, Phe, Ser, Thr, Cys, Glu, Asn, Gln, Lys, His, Ala, Tyr, Ile, Val or Gly;
  • Xaa at position 47 is Ile, Gly, Val, Ser, Arg, Pro, or His;
  • Xaa at position 48 is Leu, Ser, Cys, Arg, Ile, His, Phe, Glu, Lys, Thr, Ala, Met, Val or Asn;
  • Xaa at position 49 is Met, Arg, Ala, Gly, Pro, Asn, His, or Asp;
  • Xaa at position 50 is Glu, Leu, Thr, Asp, Tyr, Lys, Asn, Ser, Ala, Ile, Val, His, Phe, Met or Gln;
  • Xaa at position 51 is Asn, Arg, Met, Pro, Ser, Thr, or His;
  • Xaa at position 52 is Asn, His, Arg, Leu, Gly, Ser, or Thr;
  • Xaa at position 53 is Leu, Thr, Ala, Gly, Glu, Pro, Lys, Ser, or Met;
  • Xaa at position 54 is Arg, Asp, Ile, Ser, Val, Thr, Gln, Asn, Lys, His, Ala or Leu;
  • Xaa at position 55 is Arg, Thr, Val, Ser, Leu, or Gly;
  • Xaa at position 56 is Pro, Gly, Cys, Ser, Gln, Glu, Arg, His, Thr, Ala, Tyr, Phe, Leu, Val or Lys;
  • Xaa at position 57 is Asn or Gly;
  • Xaa at position 58 is Leu, Ser, Asp, Arg, Gln, Val, or Cys;
  • Xaa at position 59 is Glu Tyr, His, Leu, Pro, or Arg;
  • Xaa at position 60 is Ala, Ser, Pro, Tyr, Asn, or Thr;
  • Xaa at position 61 is Phe, Asn, Glu, Pro, Lys, Arg, or Ser;
  • Xaa at position 62 is Asn, His, Val, Arg, Pro, Thr, Asp, or Ile;
  • Xaa at position 63 is Arg, Tyr, Trp, Lys, Ser, His, Pro, or Val;
  • Xaa at position 64 is Ala, Asn, Pro, Ser, or Lys;
  • Xaa at position 65 is Val, Thr, Pro, His, Leu, Phe, or Ser;
  • Xaa at position 66 is Lys, Ile, Arg, Val, Asn, Glu, or Ser;
  • Xaa at position 67 is Ser, Ala, Phe, Val, Gly, Asn, Ile, Pro, or His;
  • Xaa at position 68 is Leu, Val, Trp, Ser, Ile, Phe, Thr, or His;
  • Xaa at position 69 is Gln, Ala, Pro, Thr, Glu, Arg, Trp, Gly, or Leu;
  • Xaa at position 70 is Asn, Leu, Val, Trp, Pro, or Ala;
  • Xaa at position 71 is Ala, Met, Leu, Pro, Arg, Glu, Thr, Gln, Trp, or Asn;
  • Xaa at position 72 is Ser, Glu, Met, Ala, His, Asn, Arg, or Asp;
  • Xaa at position 73 is Ala, Glu, Asp, Leu, Ser, Gly, Thr, or Arg;
  • Xaa at position 74 is Ile, Met, Thr, Pro, Arg, Gly, Ala;
  • Xaa at position 75 is Glu, Lys, Gly, Asp, Pro, Trp, Arg, Ser, Gln, or Leu;
  • Xaa at position 76 is Ser, Val, Ala, Asn, Trp, Glu, Pro, Gly, or Asp;
  • Xaa at position 77 is Ile, Ser, Arg, Thr, or Leu;
  • Xaa at position 78 is Leu, Ala, Ser, Glu, Phe, Gly, or Arg;
  • Xaa at position 79 is Lys, Thr, Asn, Met, Arg, Ile, Gly, or Asp;
  • Xaa at position 80 is Asn, Trp, Val, Gly, Thr, Leu, Glu, or Arg;
  • Xaa at position 81 is Leu, Gln, Gly, Ala, Trp, Arg, Val, or Lys;
  • Xaa at position 82 is Leu, Gln, Lys, Trp, Arg, Asp, Glu, Asn, His, Thr, Ser, Ala, Tyr, Phe, Ile, Met or Val;
  • Xaa at position 83 is Pro, Ala, Thr, Trp, Arg, or Met;
  • Xaa at position 84 is Cys, Glu, Gly, Arg, Met, or Val;
  • Xaa at position 85 is Leu, Asn, Val, or Gln;
  • Xaa at position 86 is Pro, Cys, Arg, Ala, or Lys;
  • Xaa at position 87 is Leu, Ser, Trp, or Gly;
  • Xaa at position 88 is Ala, Lys, Arg, Val, or Trp;
  • Xaa at position 89 is Thr, Asp, Cys, Leu, Val, Glu, His, Asn, or Ser;
  • Xaa at position 90 is Ala, Pro, Ser, Thr, Gly, Asp, Ile, or Met;
  • Xaa at position 91 is Ala, Pro, Ser, Thr, Phe, Leu, Asp, or His;
  • Xaa at position 92 is Pro, Phe, Arg, Ser, Lys, His, Ala, Gly, Ile or Leu;
  • Xaa at position 93 is Thr, Asp, Ser, Asn, Pro, Ala, Leu, or Arg;
  • Xaa at position 94 is Arg, Ile, Ser, Glu, Leu, Val, Gln, Lys, His, Ala, or Pro;
  • Xaa at position 95 is His, Gln, Pro, Arg, Val, Leu, Gly, Thr, Asn, Lys, Ser, Ala, Trp, Phe, Ile, or Tyr;
  • Xaa at position 96 is Pro, Lys, Tyr, Gly, Ile, or Thr;
  • Xaa at position 97 is Ile, Val, Lys, Ala, or Asn;
  • Xaa at position 98 is His, Ile, Asn, Leu, Asp, Ala, Thr, Glu, Gln, Ser, Phe, Met, Val, Lys, Arg, Tyr or Pro;
  • Xaa at position 99 is Ile, Leu, Arg, Asp, Val, Pro, Gln, Gly, Ser, Phe, or His;
  • Xaa at position 100 is Lys, Tyr, Leu, His, Arg, Ile, Ser, Gln, or Pro;
  • Xaa at position 101 is Asp, Pro, Met, Lys, His, Thr, Val, Tyr, Glu, Asn, Ser, Ala, Gly, Ile, Leu, or Gln;
  • Xaa at position 102 is Gly, Leu, Glu, Lys, Ser, Tyr, or Pro;
  • Xaa at position 103 is Asp, or Ser;
  • Xaa at position 104 is Trp, Val, Cys, Tyr, Thr, Met, Pro, Leu, Gln, Lys, Ala, Phe, or Gly;
  • Xaa at position 105 is Asn, Pro, Ala, Phe, Ser, Trp, Gln, Tyr, Leu, Lys, Ile, Asp, or His;
  • Xaa at position 106 is Glu, Ser, Ala, Lys, Thr, Ile, Gly, or Pro;
  • Xaa at position 108 is Arg, Lys, Asp, Leu, Thr, Ile, Gln, His, Ser, Ala or Pro;
  • Xaa at position 109 is Arg, Thr, Pro, Glu, Tyr, Leu, Ser, or Gly;
  • Xaa at position 110 is Lys, Ala, Asn, Thr, Leu, Arg, Gln, His, Glu, Ser, or Trp;
  • Xaa at position 111 is Leu, Ile, Arg, Asp, or Met;
  • Xaa at position 112 is Thr, Val, Gln, Tyr, Glu, His, Ser, or Phe;
  • Xaa at position 113 is Phe, Ser, Cys, His, Gly, Trp, Tyr, Asp, Lys, Leu, Ile, Val or Asn;
  • Xaa at position 114 is Tyr, Cys, His, Ser, Trp, Arg, or Leu;
  • Xaa at position 115 is Leu, Asn, Val, Pro, Arg, Ala, His, Thr, Trp, or Met;
  • Xaa at position 116 is Lys, Leu, Pro, Thr, Met, Asp, Val, Glu, Arg, Trp, Ser, Asn, His, Ala, Tyr, Phe, Gln, or Ile;
  • Xaa at position 117 is Thr, Ser, Asn, Ile, Trp, Lys, or Pro;
  • Xaa at position 118 is Leu, Ser, Pro, Ala, Glu, Cys, Asp, or Tyr;
  • Xaa at position 119 is Glu, Ser, Lys, Pro, Leu, Thr, Tyr, or Arg;
  • Xaa at position 120 is Asn, Ala, Pro, Leu, His, Val, or Gln;
  • Xaa at position 121 is Ala, Ser, Ile, Asn, Pro, Lys, Asp, or Gly;
  • Xaa at position 122 is Gln, Ser, Met, Trp, Arg, Phe, Pro, His, Ile, Tyr, or Cys;
  • Xaa at position 123 is Ala, Met, Glu, His, Ser, Pro, Tyr, or Leu;
  • N-terminus is joined to the C-terminus directly or through a linker (L 2 ) capable of joining the N-terminus to the C-terminus and having new C- and N-termini at amino acids; 26-27 27-28 28-29 29-30 30-31 31-32 32-33 33-34 34-35 35-36 36-37 37-38 38-39 39-40 40-41 41-42 49-50 50-51 51-52 52-53 53-54 54-55 64-65 65-66 66-67 67-68 68-69 69-70 70-71 71-72 72-73 82-83 83-84 84-85 85-86 86-87 87-88 88-89 89-90 90-91 91-92 92-93 97-98 98-99 99-100 100-101 101-102 102-103 or 103-104;
  • a polypeptide comprising; a modified human c-mpl ligand amino acid sequence of the formula: SerProAlaProProAlaCysAspLeuArgValLeu (SEQ ID NO: 3) 1 5 10 SerLysLeuLeuArgAspSerHisValLeuHisSer 15 20 ArgLeuSerGlnCysProGluValHisProLeuPro 25 30 35 ThrProValLeuLeuProAlaValAspPheSerLeu 40 45 GlyGluTrpLysThrGlnMetGluGluThrLysAla 50 55 60 GlnAspIleLeuGlyAlaValThrLeuLeuLeuGlu 65 70 GlyValMetAlaAlaArgGlyGlnLeuGlyProThr 75 80 CysLeuSerSerLeuLeuGlyGlnLeuSerGlyGln 85 90 95 ValArgLeuLeuGlyAlaLeuGlnS
  • Xaa at position 112 is deleted or Leu, Ala, Val, Ile, Pro, Phe, Trp, or Met;
  • Xaa at position 113 is deleted or Pro, Phe, Ala, Val, Leu, Ile, Trp, or Met;
  • Xaa at position 114 is deleted or Pro, Phe, Ala, Val, Leu, Ile, Trp, or Met;
  • Xaa at position 115 is deleted or Gln, Gly, Ser, Thr, Tyr, or Asn;
  • N-terminus is joined to the C-terminus directly or through a linker (L 2 ) capable of joining the N-terminus to the C-terminus and having new C- and N-termini at amino acids; 26-27 27-28 28-29 29-30 30-31 32-33 33-34 34-35 36-37 37-38 38-39 40-41 41-42 42-43 43-44 44-45 46-47 47-48 48-49 50-51 51-52 52-53 53-54 54-55 55-56 56-57 57-58 58-59 59-60 78-79 79-80 80-81 81-82 82-83 83-84 84-85 85-86 86-87 87-88 88-89 108-109 109-110 110-111 111-112 112-113 113-114 114-115 115-116 116-117 117-118 118-119 119-120 120-121 121-122 122-123 123-124 124-125 125-
  • Xaa at position 17 is Ser, Lys, Gly, Asp, Met, Gln, or Arg;
  • Xaa at position 18 is Asn, His, Leu, Ile, Phe, Arg, or Gln;
  • Xaa at position 19 is Met, Phe, Ile, Arg, Gly, Ala, or Cys;
  • Xaa at position 20 is Ile, Cys, Gln, Glu, Arg, Pro, or Ala;
  • Xaa at position 21 is Asp, Phe, Lys, Arg, Ala, Gly, Glu, Gln, Asn, Thr, Ser or Val;
  • Xaa at position 22 is Glu, Trp, Pro, Ser, Ala, His, Asp, Asn, Gln, Leu, Val or Gly;
  • Xaa at position 23 is Ile, Val, Ala, Gly, Trp, Lys, Phe, Leu, Ser, or Arg;
  • Xaa at position 24 is Ile, Gly, Val, Arg, Ser, Phe, or Leu;
  • Xaa at position 25 is Thr, His, Gly, Gln, Arg, Pro, or Ala;
  • Xaa at position 26 is His, Thr, Phe, Gly, Arg, Ala, or Trp;
  • Xaa at position 27 is Leu, Gly, Arg, Thr, Ser, or Ala;
  • Xaa at position 28 is Lys, Arg, Leu, Gln, Gly, Pro, Val or Trp;
  • Xaa at position 29 is Gln, Asn, Leu, Pro, Arg, or Val;
  • Xaa at position 30 is Pro, His, Thr, Gly, Asp, Gln, Ser, Leu, or Lys;
  • Xaa at position 31 is Pro, Asp, Gly, Ala, Arg, Leu, or Gln;
  • Xaa at position 32 is Leu, Val, Arg, Gln, Asn, Gly, Ala, or Glu;
  • Xaa at position 33 is Pro, Leu, Gln, Ala, Thr, or Glu;
  • Xaa at position 34 is Leu, Val, Gly, Ser, Lys, Glu, Gln, Thr, Arg, Ala, Phe, Ile or Met;
  • Xaa at position 35 is Leu, Ala, Gly, Asn, Pro, Gln, or Val;
  • Xaa at position 36 is Asp, Leu, or Val
  • Xaa at position 37 is Phe, Ser, Pro, Trp, or Ile;
  • Xaa at position 38 is Asn, or Ala
  • Xaa at position 40 is Leu, Trp, or Arg;
  • Xaa at position 41 is Asn, Cys, Arg, Leu, His, Met, or Pro;
  • Xaa at position 42 is Gly, Asp, Ser, Cys, Asn, Lys, Thr, Leu, Val, Glu, Phe, Tyr, Ile, Met or Ala;
  • Xaa at position 43 is Glu, Asn, Tyr, Leu, Phe, Asp, Ala, Cys, Gln, Arg, Thr, Gly or Ser;
  • Xaa at position 44 is Asp, Ser, Leu, Arg, Lys, Thr, Met, Trp, Glu, Asn, Gln, Ala or Pro;
  • Xaa at position 45 is Gln, Pro, Phe, Val, Met, Leu, Thr, Lys, Trp, Asp, Asn, Arg, Ser, Ala, Ile, Glu or His;
  • Xaa at position 46 is Asp, Phe, Ser, Thr, Cys, Glu, Asn, Gln, Lys, His, Ala, Tyr, Ile, Val or Gly;
  • Xaa at position 47 is Ile, Gly, Val, Ser, Arg, Pro, or His;
  • Xaa at position 48 is Leu, Ser, Cys, Arg, Ile, His, Phe, Glu, Lys, Thr, Ala, Met, Val or Asn;
  • Xaa at position 49 is Met, Arg, Ala, Gly, Pro, Asn, His, or Asp;
  • Xaa at position 50 is Glu, Leu, Thr, Asp, Tyr, Lys, Asn, Ser, Ala, Ile, Val, His, Phe, Met or Gln;
  • Xaa at position 51 is Asn, Arg, Met, Pro, Ser, Thr, or His;
  • Xaa at position 52 is Asn, His, Arg, Leu, Gly, Ser, or Thr;
  • Xaa at position 53 is Leu, Thr, Ala, Gly, Glu, Pro, Lys, Ser, or Met;
  • Xaa at position 54 is Arg, Asp, Ile, Ser, Val, Thr, Gln, Asn, Lys, His, Ala or Leu;
  • Xaa at position 55 is Arg, Thr, Val, Ser, Leu, or Gly;
  • Xaa at position 56 is Pro, Gly, Cys, Ser, Gln, Glu, Arg, His, Thr, Ala, Tyr, Phe, Leu, Val or Lys;
  • Xaa at position 57 is Asn or Gly;
  • Xaa at position 58 is Leu, Ser, Asp, Arg, Gln, Val, or Cys;
  • Xaa at position 59 is Glu Tyr, His, Leu, Pro, or Arg;
  • Xaa at position 60 is Ala, Ser, Pro, Tyr, Asn, or Thr;
  • Xaa at position 61 is Phe, Asn, Glu, Pro, Lys, Arg, or Ser;
  • Xaa at position 62 is Asn, His, Val, Arg, Pro, Thr, Asp, or Ile;
  • Xaa at position 63 is Arg, Tyr, Trp, Lys, Ser, His, Pro, or Val;
  • Xaa at position 64 is Ala, Asn, Pro, Ser, or Lys;
  • Xaa at position 65 is Val, Thr, Pro, His, Leu, Phe, or Ser;
  • Xaa at position 66 is Lys, Ile, Arg, Val, Asn, Glu, or Ser;
  • Xaa at position 67 is Ser, Ala, Phe, Val, Gly, Asn, Ile, Pro, or His;
  • Xaa at position 68 is Leu, Val, Trp, Ser, Ile, Phe, Thr, or His;
  • Xaa at position 69 is Gln, Ala, Pro, Thr, Glu, Arg, Trp, Gly, or Leu;
  • Xaa at position 70 is Asn, Leu, Val, Trp, Pro, or Ala;
  • Xaa at position 71 is Ala, Met, Leu, Pro, Arg, Glu, Thr, Gln, Trp, or Asn;
  • Xaa at position 72 is Ser, Glu, Met, Ala, His, Asn, Arg, or Asp;
  • Xaa at position 73 is Ala, Glu, Asp, Leu, Ser, Gly, Thr, or Arg;
  • Xaa at position 74 is Ile, Met, Thr, Pro, Arg, Gly, Ala;
  • Xaa at position 75 is Glu, Lys, Gly, Asp, Pro, Trp, Arg, Ser, Gln, or Leu;
  • Xaa at position 76 is Ser, Val, Ala, Asn, Trp, Glu, Pro, Gly, or Asp;
  • Xaa at position 77 is Ile, Ser, Arg, Thr, or Leu;
  • Xaa at position 78 is Leu, Ala, Ser, Glu, Phe, Gly, or Arg;
  • Xaa at position 79 is Lys, Thr, Asn, Met, Arg, Ile, Gly, or Asp;
  • Xaa at position 80 is Asn, Trp, Val, Gly, Thr, Leu, Glu, or Arg;
  • Xaa at position 81 is Leu, Gln, Gly, Ala, Trp, Arg, Val, or Lys;
  • Xaa at position 82 is Leu, Gln, Lys, Trp, Arg, Asp, Glu, Asn, His, Thr, Ser, Ala, Tyr, Phe, Ile, Met or Val;
  • Xaa at position 83 is Pro, Ala, Thr, Trp, Arg, or Met;
  • Xaa at position 84 is Cys, Glu, Gly, Arg, Met, or Val;
  • Xaa at position 85 is Leu, Asn, Val, or Gln;
  • Xaa at position 86 is Pro, Cys, Arg, Ala, or Lys;
  • Xaa at position 87 is Leu, Ser, Trp, or Gly;
  • Xaa at position 88 is Ala, Lys, Arg, Val, or Trp;
  • Xaa at position 89 is Thr, Asp, Cys, Leu, Val, Glu, His, Asn, or Ser;
  • Xaa at position 90 is Ala, Pro, Ser, Thr, Gly, Asp, Ile, or Met;
  • Xaa at position 91 is Ala, Pro, Ser, Thr, Phe, Leu, Asp, or His;
  • Xaa at position 92 is Pro, Phe, Arg, Ser, Lys, His, Ala, Gly, Ile or Leu;
  • Xaa at position 93 is Thr, Asp, Ser, Asn, Pro, Ala, Leu, or Arg;
  • Xaa at position 94 is Arg, Ile, Ser, Glu, Leu, Val, Gln, Lys, His, Ala, or Pro;
  • Xaa at position 95 is His, Gln, Pro, Arg, Val, Leu, Gly, Thr, Asn, Lys, Ser, Ala, Trp, Phe, Ile, or Tyr;
  • Xaa at position 96 is Pro, Lys, Tyr, Gly, Ile, or Thr;
  • Xaa at position 97 is Ile, Val, Lys, Ala, or Asn;
  • Xaa at position 98 is His, Ile, Asn, Leu, Asp, Ala, Thr, Glu, Gln, Ser, Phe, Met, Val, Lys, Arg, Tyr or Pro;
  • Xaa at position 99 is Ile, Leu, Arg, Asp, Val, Pro, Gln, Gly, Ser, Phe, or His;
  • Xaa at position 100 is Lys, Tyr, Leu, His, Arg, Ile, Ser, Gln, or Pro;
  • Xaa at position 101 is Asp, Pro, Met, Lys, His, Thr, Val, Tyr, Glu, Asn, Ser, Ala, Gly, Ile, Leu, or Gln;
  • Xaa at position 102 is Gly, Leu, Glu, Lys, Ser, Tyr, or Pro;
  • Xaa at position 103 is Asp, or Ser;
  • Xaa at position 104 is Trp, Val, Cys, Tyr, Thr, Met, Pro, Leu, Gln, Lys, Ala, Phe, or Gly;
  • Xaa at position 105 is Asn, Pro, Ala, Phe, Ser, Trp, Gln, Tyr, Leu, Lys, Ile, Asp, or His;
  • Xaa at position 106 is Glu, Ser, Ala, Lys, Thr, Ile, Gly, or Pro;
  • Xaa at position 108 is Arg, Lys, Asp, Leu, Thr, Ile, Gln, His, Ser, Ala or Pro;
  • Xaa at position 109 is Arg, Thr, Pro, Glu, Tyr, Leu, Ser, or Gly;
  • Xaa at position 110 is Lys, Ala, Asn, Thr, Leu, Arg, Gln, His, Glu, Ser, or Trp;
  • Xaa at position 111 is Leu, Ile, Arg, Asp, or Met;
  • Xaa at position 112 is Thr, Val, Gln, Tyr, Glu, His, Ser, or Phe;
  • Xaa at position 113 is Phe, Ser, Cys, His, Gly, Trp, Tyr, Asp, Lys, Leu, Ile, Val or Asn;
  • Xaa at position 114 is Tyr, Cys, His, Ser, Trp, Arg, or Leu;
  • Xaa at position 115 is Leu, Asn, Val, Pro, Arg, Ala, His, Thr, Trp, or Met;
  • Xaa at position 116 is Lys, Leu, Pro, Thr, Met, Asp, Val, Glu, Arg, Trp, Ser, Asn, His, Ala, Tyr, Phe, Gln, or Ile;
  • Xaa at position 117 is Thr, Ser, Asn, Ile, Trp, Lys, or Pro;
  • Xaa at position 118 is Leu, Ser, Pro, Ala, Glu, Cys, Asp, or Tyr;
  • Xaa at position 119 is Glu, Ser, Lys, Pro, Leu, Thr, Tyr, or Arg;
  • Xaa at position 120 is Asn, Ala, Pro, Leu, His, Val, or Gln;
  • Xaa at position 121 is Ala, Ser, Ile, Asn, Pro, Lys, Asp, or Gly;
  • Xaa at position 122 is Gln, Ser, Met, Trp, Arg, Phe, Pro, His, Ile, Tyr, or Cys;
  • Xaa at position 123 is Ala, Met, Glu, His, Ser, Pro, Tyr, or Leu;
  • (V) a colony stimulating factor; and wherein L 1 is a linker capable of linking R 1 to R 2 ;
  • R 1 or R 2 is selected from the polypeptide of formula (I), (II), or (III);
  • said hematopoietic protein can optionally be immediately preceded by (methionine ⁇ 1 ), (alanine ⁇ 1 ) or (methionine ⁇ 2 , alanine ⁇ 1 ).
  • the more preferred breakpoints at which new C-terminus and N-terminus can be made in the polypeptide (I) above are; 38-39, 39-40, 40-41, 41-42, 48-49, 53-54, 54-55, 55-56, 56-57, 57-58, 58-59, 59-60, 60-61, 61-62, 62-63, 64-65, 65-66, 66-67, 67-68, 68-69, 69-70, 96-97, 125-126, 126-127, 127-128, 128-129, 129-130, 130-131, 131-132, 132-133, 133-134, 134-135, 135-136, 136-137, 137-138, 138-139, 139-140, 140-141 and 141-142.
  • breakpoints at which new C-terminus and N-terminus can be made in the polypeptide (I) above are; 38-39, 48-49, 96-97, 125-126, 132-133 and 141-142.
  • the more preferred breakpoints at which new C-terminus and N-terminus can be made in the polypeptide (II) above are; 28-29, 29-30, 30-31, 31-32, 32-33, 33-34, 34-35, 35-36, 36-37, 37-38, 38-39, 39-40, 66-67, 67-68, 68-69, 69-70, 70-71, 84-85, 85-86, 86-87, 87-88, 88-89, 89-90, 90-91, 98-99, 99-100, 100-101 and 101-102.
  • the more preferred breakpoints at which new C-terminus and N-terminus can be made in the polypeptide (III) above or the amino acid sequence of (SEQ ID NO:256) are; 80-81, 81-82, 82-83, 83-84, 84-85, 85-86, 86-87, 108-109, 109-110, 110-111, 111-112, 112-113, 113-114, 114-115, 115-116, 116-117, 117-118, 118-119, 119-120, 120-121, 121-122, 122-123, 123-124, 124-125, 125-126 and 126-127.
  • breakpoints at which new C-terminus and N-terminus can be made in the polypeptide (III) above or the amino acid sequence of (SEQ ID NO:256) are; 81-82, 108-109, 115-116, 119-120, 122-123 and 125-126.
  • the invention is also intended to include multifunctional receptor agoinist which comprises a sequence rearranged c-mpl receptor agonist in which the cysteine at position 7 and/or 151 are substituted with another amino acid.
  • the substitution at position 7 and 151 is Ser, Ala, Gly, His, Asn, Asp, Thr, Phe or Thr. More preferably, the substitution at position 7 and 151 is Ser, Ala, Gly, His or Asn.
  • the multifunctional receptor agonist of the present invention can also be represented by the following formula:
  • X 1 is a peptide comprising an amino acid sequence corresponding to the sequence of residues n+1 through J of the original protein having amino acids residues numbered sequentially 1 through J with an amino terminus at residue 1;
  • L is an optional linker
  • X 2 is a peptide comprising an amino acid sequence of residues 1 through n of the original protein
  • Y 2 is a peptide comprising an amino acid sequence of residues 1 through n of the original protein
  • L 1 and L 2 are optional peptide spacers:
  • n is an integer ranging from 1 to J-1;
  • b, c, and d are each independently 0 or 1;
  • a and e are either 0 or 1, provided that both a and e cannot both be 0;
  • T 1 and T 2 are proteins.
  • the present invention relates to recombinant expression vectors comprising nucleotide sequences encoding the multi-functional hematopoietic receptor agonists, related microbial expression systems, and processes for making the multi-functional hematopoietic receptor agonists.
  • the invention also relates to pharmaceutical compositions containing the multi-functional hematopoietic receptor agonists, and methods for using the multi-functional hematopoietic receptor agonists.
  • FIG. 1 schematically illustrates the sequence rearrangement of a protein.
  • the N-terminus (N) and the C-terminus (C) of the native protein are joined through a linker, or joined directly.
  • the protein is opened at a breakpoint creating a new N-terminus (new N) and a new C-terminus (new-C) resulting in a protein with a new linear amino acid sequence.
  • a rearranged molecule may be synthesized de novo as linear molecule and not go through the steps of joining the original N-terminus and the C-terminus and opening of the protein at the breakpoint.
  • FIG. 2 shows a schematic of Method I, for creating new proteins in which the original N-terminus and C-terminus of the native protein are joined with a linker and different N-terminus and C-terminus of the protein are created.
  • the sequence rearrangement results in a new gene encoding a protein with a new N-terminus created at amino acid 97 of the original protein, the original C-terminus (a.a. 174) joined to the amino acid 11 (a.a. 1-10 are deleted) through a linker region and a new C-terminus created at amino acid 96 of the original sequence.
  • FIG. 3 shows a schematic of Method II, for creating new proteins in which the original N-terminus and C-terminus of the native protein are joined without a linker and different N-terminus and C-terminus of the protein are created.
  • the sequence rearrangement results in a new gene encoding a protein with a new N-terminus created at amino acid 97 of the original protein, the original C-terminus (a.a. 174) joined to the original N-terminus and a new C-terminus created at amino acid 96 of the original sequence.
  • FIG. 4 shows a schematic of Method III, for creating new proteins in which the original N-terminus and C-terminus of the native protein are joined with a linker and different N-terminus and C-terminus of the protein are created.
  • the sequence rearrangement results in a new gene encoding a protein with a new N-terminus created at amino acid 97 of the original protein, the original C-terminus (a.a. 174) joined to amino acid 1 through a linker region and a new C-terminus created at amino acid 96 of the original sequence.
  • the present invention encompasses multi-functional hematopoietic receptor agonists formed from covalently linked polypeptides, each of which may act through a different and specific cell receptor to initiate complementary biological activities.
  • Hematopoiesis requires a complex series of cellular events in which stem cells generate continuously into large populations of maturing cells in all major lineages.
  • regulators with hematopoietic proliferative activity There are currently at least 20 known regulators with hematopoietic proliferative activity. Most of these proliferative regulators can only stimulate one or another type of colony formation in vitro, the precise pattern of colony formation stimulated by each regulator is quite distinctive.
  • No two regulators stimulate exactly the same pattern of colony formation, as evaluated by colony numbers or, more importantly, by the lineage and maturation pattern of the cells making up the developing colonies.
  • Proliferative responses can most readily be analyzed in simplified in vitro culture systems. Three quite different parameters can be distinguished: alteration in colony size, alteration in colony numbers and cell lineage. Two or more factors may act on the progenitor cell, inducing the formation of larger number of progeny thereby increasing the colony size. Two or more factors may allow increased number of progenitor cells to proliferate either because distinct subsets of progenitors cells exist that respond exclusively to one factor or because some progenitors require stimulation by two or more factors before being able to respond.
  • Activation of additional receptors on a cell by the use of two or more factors is likely to enhance the mitotic signal because of coalescence of initially differing signal pathways into a common final pathway reaching the nucleus (Metcalf, Nature 339:27, 1989).
  • Other mechanisms could explain synergy. For example, if one signaling pathway is limited by an intermediate activation of an additional signaling pathway which is caused by a second factor, then this may result in a super additive response.
  • activation of one receptor type can induce an enhanced expression of other receptors (Metcalf, Blood 82:3515-3523, 1993).
  • Two or more factors may result in a different pattern of cell lineages than from a single factor.
  • the use of multi-functional hematopoietic receptor agonists may have a potential clinical advantage resulting from a proliferative response that is not possible by any single factor.
  • tyrosine kinase receptors including those for epidermal growth factor, M-CSF (Sherr, Blood 75:1, 1990) and SCF (Yarden et al., EMBO J. 6:3341, 1987): and (2) hematopoietic receptors, not containing a tyrosine kinase domain, but exhibiting obvious homology in their extracellular domain (Bazan, PNAS USA 87:6934-6938, 1990).
  • EPO erythropoietin
  • GM-CSF Gearing et al., EMBO J. 8:3667, 1989
  • IL-3 Kitamura et al., Cell 66:1165, 1991
  • G-CSF Fukunaga et al., J. Bio. Chem. 265:14008-15, 1990
  • IL-4 Harada et al., PNAS USA 87:857, 1990
  • IL-5 Takaki et al., EMBO J.
  • GM-CSF, IL-3 and IL-5 share the same b-chain (Kitamura et al., Cell 66:1165, 1991), Takaki et al., EMBO J. 10:2833-8, 1991) and receptor complexes for IL-6, LIF and IL-11 share a common b-chain (gp130) (Taga et al., Cell 58:573-81, 1989; Gearing et al., Science 255:1434-7, 1992).
  • the receptor complexes of IL-2, IL-4, IL-7, IL-9 and IL-15 share a common g-chain (Kondo et al., Science 262:1874, 1993; Russell et al., Science 266: 1042-1045, 1993; Noguchi et al., Science 262:1877, 1993; Giri et al., EMBO J. 13:2822-2830, 1994).
  • the use of a multiply acting hematopoietic factor may also have a potential advantage by reducing the demands placed on factor-producing cells and their induction systems. If there are limitations in the ability of a cell to produce a factor, then by lowering the required concentrations of each of the factors, and using them in combination may usefully reduce demands on the factor-producing cells.
  • the use of a multiply acting hematopoietic factor may lower the amount of the factors that would be needed, probably reducing the likelihood of adverse side-effects.
  • Novel compounds of this invention are represented by a formula selected from the group consisting of:
  • R 1 and R 2 are as defined above.
  • R 2 is preferably a colony stimulating factor with a different but complementary activity than R 1 .
  • complementary activity is meant activity which enhances or changes the response to another cell modulator.
  • the R 1 polypeptide is joined either directly or through a linker segment to the R 2 polypeptide.
  • the term “directly” defines multi-functional hematopoietic receptor agonists in which the polypeptides are joined without a peptide linker.
  • L 1 represents a chemical bond or polypeptide segment to which both R 1 and R 2 are joined in frame
  • L 1 is a linear peptide to which R 1 and R 2 are joined by amide bonds linking the carboxy terminus of R 1 to the amino terminus of L 1 and carboxy terminus of L 1 to the amino terminus of R 2 .
  • joined in frame is meant that there is no translation termination or disruption between the reading frames of the DNA encoding R 1 and R 2 .
  • CSFs colony stimulating factors
  • cytokines are cytokines, lymphokines, interleukins, or hematopoietic growth factors which can be joined to (I), (II) or (III) include GM-CSF, G-CSF, c-mpl ligand (also known as TPO or MGDF), M-CSF, erythropoietin (EPO), IL-1, IL-4, IL-2, IL-3, IL-5, IL 6, IL-7, IL-8, IL-9, IL-10, IL-11, IL-12, IL-13, IL-15, LIF, flt3 ligand, human growth hormone, and stem cell factor (SCF) also known as steel factor or c-kit ligand.
  • SCF stem cell factor
  • this invention encompasses the use of modified R 1 or R 2 molecules or mutated or modified DNA sequences encoding these R 1 or R 2 molecules.
  • the present invention also includes multi-functional hematopoietic receptor agonists in which R 1 or R 2 is an hIL-3 variant, c-mpl ligand variant, or G-CSF variant.
  • a “hIL-3 variant” is defined as a hIL-3 molecule which has amino acid substitutions and/or portions of hIL-3 deleted as disclosed in WO 94/12638, WO 94/12639 and WO 95/00646, as well as other variants known in the art.
  • a “c-mpl ligand variant” is defined an c-mpl ligand molecule which has amino acid substitutions and/or portions of c-mpl ligand deleted, disclosed in U.S. application Ser. No. 08/383,035 as well as other variants known in the art.
  • a “G-CSF variant” is defined an G-CSF molecule which has amino acid substitutions and/or portions of G-CSF deleted, as disclosed herein, as well as other variants known in the art.
  • the linking group (L 1 ) is generally a polypeptide of between 1 and 500 amino acids in length.
  • the linkers joining the two molecules are preferably designed to (1) allow the two molecules to fold and act independently of each other, (2) not have a propensity for developing an ordered secondary structure which could interfere with the functional domains of the two proteins, (3) have minimal hydrophobic characteristics which could interact with the functional protein domains and (4) provide steric separation of R 1 and R 2 such that R 1 and R 2 could interact simultaneously with their corresponding receptors on a single cell.
  • surface amino acids in flexible protein regions include Gly, Asn and Ser. Virtually any permutation of amino acid sequences containing Gly, Asn and Ser would be expected to satisfy the above criteria for a linker sequence.
  • Thr and Ala may also be used in the linker sequence. Additional amino acids may also be included in the linkers due to the addition of unique restriction sites in the linker sequence to facilitate construction of the multi-functional hematopoietic receptor agonists.
  • Preferred L 1 linkers of the present invention include sequences selected from the group of formulas: (Gly 3 Ser) n , (SEQ ID NO: 4), (Gly 4 Ser) n , (SEQ ID NO: 5) (Gly 5 Ser) n , (SEQ ID NO: 6) (Gly n Ser) n or (SEQ ID NO: 7) (AlaGlySer) n . (SEQ ID NO: 8)
  • a highly-flexible linker is the glycine and serine-rich spacer region present within the pIII protein of the filamentous bacteriophages, e.g. bacteriophages M13 or fd (Schaller et al., PNAS USA 72: 737-741, 1975). This region provides a long, flexible spacer region between two domains of the pIII surface protein.
  • the spacer region consists of the amino acid sequence: GlyGlyGlySerGlyGlyGlySerGlyGlyGlyGlyGlyGlyGlyGly (SEQ ID NO: 9) SerGluGlyGlyGlySerGluGlyGlyGlySer GluGlyGlyGlySerGluGlyGlyGlySerGly GlyGlySer.
  • the present invention also includes linkers in which an endopeptidase recognition sequence is included.
  • a cleavage site may be valuable to separate the individual components of the multi-functional hematopoietic receptor agonist to determine if they are properly folded and active in vitro.
  • endopeptidases include, but are not limited to, plasmin, enterokinase, kallikrein, urokinase, tissue plasminogen activator, clostripain, chymosin, collagenase, Russell's viper venom protease, postproline cleavage enzyme, V8 protease, Thrombin and factor Xa.
  • Peptide linker segments from the hinge region of heavy chain immunoglobulins IgG, IgA, IgM, IgD or IgE provide an angular relationship between the attached polypeptides. Especially useful are those hinge regions where the cysteines are replaced with serines.
  • Preferred linkers of the present invention include sequences derived from murine IgG gamma 2b hinge region in which the cysteines have been changed to serines. These linkers may also include an endopeptidase cleavage site.
  • linkers include the following sequences: IleSerGluProSerGlyProIleSerThrIle (SEQ ID NO: 10) AsnProSerProProSerLysGluSerHisLys SerPro and IleGluGlyArgIleSerGluProSerGlyPro (SEQ ID NO: 11) IleSerThrIleAsnProSerProProSerLys GluSerHisLysSerPro.
  • the present invention is, however, not limited by the form, size or number of linker sequences employed and the only requirement of the linker is that functionally it does not interfere with the folding and function of the individual molecules of the multi-functional hematopoietic receptor agonist.
  • One aspect of the invention includes multi-functional hematopoietic receptor agonists which comprise a sequence rearranged c-mpl receptor agonist in which the cysteine(s) at position 7 and 151 of c-mpl ligand, have been substituted with another amino acid.
  • Kaushansky et al. ( Blood 86:255a Abstract 1008, 1995) teaches that all four of the cysteines at positions 7, 29, 85, and 151 are required for bioactivity.
  • the presence of cysteines in a protein can cause problems in processing when the protein is being produced recombinantly in a bacterial host. Microbially produced cysteine-containing proteins may tend to form multimers which greatly complicate purification of the protein product.
  • a molecule in which a pair of cysteines at positions 7 and 151 are substituted with another amino acid may have one or more advantages including, but not limited to: 1) increased folding efficiency of the heterologously expressed protein; 2) elimination of mispaired disulfides, 3) use of milder refold conditions (ie. Guanidine vs. Urea); 4) increased purification yields, 5) increased protein solubility; and 6) increased protein stability.
  • the length of the amino acid sequence of the linker L 2 to be used in R 1 and/or R 2 can be selected empirically or with guidance from structural information, or by using a combination of the two approaches.
  • a small series of linkers can be prepared for testing using a design whose length is varied in order to span a range from 0 to 50 ⁇ and whose sequence is chosen in order to be consistent with surface exposure (hydrophilicity, Hopp & Woods, Mol. Immunol. 20: 483-489, 1983), Kyte & Doolittle, J. Mol. Biol. 157:105-132; solvent exposed surface area, Lee & Richards, J. Mol. Biol. 55:379-400, 1971) and the ability to adopt the necessary conformation with out deranging the conformation of R 1 or R 2 (conformationally flexible; Karplus & Schulz, Naturwissenschaften 72:212-213, 1985).
  • linkers may be composed of the original sequence, shortened or lengthened as necessary, and when lengthened the additional residues may be chosen to be flexible and hydrophilic as described above; or optionally the original sequence may be substituted for using a series of linkers, one example being the Gly-Gly-Gly-Ser (SEQ ID NO:12) cassette approach mentioned above; or optionally a combination of the original sequence and new sequence having the appropriate total length may be used.
  • Sequences of R 1 and R 2 capable of folding to biologically active states can be prepared by appropriate selection of the beginning (amino terminus) and ending (carboxyl terminus) positions from within the original polypeptide chain while using the linker sequence L 2 as described above.
  • Amino and carboxyl termini are selected from within a common stretch of sequence, referred to as a breakpoint region, using the guidelines described below.
  • a novel amino acid sequence is thus generated by selecting amino and carboxyl termini from within the same breakpoint region. In many cases the selection of the new termini will be such that the original position of the carboxyl terminus immediately preceded that of the amino terminus.
  • those skilled in the art will recognize that selections of termini anywhere within the region may function, and that these will effectively lead to either deletions or additions to the amino or carboxyl portions of the new sequence.
  • Examples of structural information that are relevant to the identification of breakpoint regions include the location and type of protein secondary structure (alpha and 3-10 helices, parallel and anti-parallel beta sheets, chain reversals and turns, and loops; Kabsch & Sander, Biopolymers 22: 2577-2637, 1983), the degree of solvent exposure of amino acid residues, the extent and type of interactions of residues with one another (Chothia, Ann. Rev. Biochem. 53:537-572, 1984) and the static and dynamic distribution of conformations along the polypeptide chain (Alber & Mathews, Methods Enzymol. 154: 511-533, 1987).
  • the parental amino acid sequence is inspected to classify regions according to whether or not they are integral to the maintenance of secondary and tertiary structure.
  • the occurrence of sequences within regions that are known to be involved in periodic secondary structure are regions that should be avoided.
  • regions of amino acid sequence that are observed or predicted to have a low degree of solvent exposure are more likely to be part of the so-called hydrophobic core of the protein and should also be avoided for selection of amino and carboxyl termini.
  • those regions that are known or predicted to be in surface turns or loops, and especially those regions that are known not to be required for biological activity, are the preferred sites for location of the extremes of the polypeptide chain. Continuous stretches of amino acid sequence that are preferred based on the above criteria are referred to as a breakpoint region.
  • R 1 -C 1 +R 2 -C 2 or C 1 -R 1 +C 2 -R 2 ; C 1 -R 1 +R 2 -C 2 ; or C 1 -R 1 +R 2 -C 2 .
  • R 1 and R 2 are as is defined above. Domains C 1 and C 2 are either identical or non-identical chemical structures, typically proteinaceous, which can form a non-covalent, specific association. Complexes between C 1 and C 2 result in a one-to-one stoichiometric relationship between R 1 and R 2 for each complex. Examples of domains which associate are “leucine zipper” domains of transcription factors, dimerization domains of bacterial transcription repressors and immunoglobulin constant domains. Covalent bonds link R 1 and C1, and R 2 and C 2 , respectively.
  • the domains C1 and C 2 can be present either at the N-terminus or C-terminus of their corresponding hematopoietic growth factor (R).
  • These multimerization domains (C 1 and C 2 ) include those derived from the bZIP family of proteins (Abel et al., Nature 341:24-25, 1989; Landshulz et al., Science 240:1759-1764, 1988; Pu et al., Nuc. Acid Res.
  • Preferred multi-functional hematopoietic receptor agonists of the present invention include colony stimulating factors dimerized by virtue of their incorporation as translational multi-functional hematopoietic receptor agonists with the leucine zipper dimerization domains of the bZIP family proteins Fos and Jun.
  • the leucine zipper domain of Jun is capable of interacting with identical domains.
  • the leucine zipper domain of Fos interacts with the Jun leucine zipper domain, but does not interact with other Fos leucine zipper domains. Mixtures of Fos and Jun predominantly result in formation of Fos-Jun heterodimers. Consequently, when joined to colony stimulating factors, the Jun domain can be used to direct the formation of either homo- or heterodimers. Preferential formation of heterodimers can be achieved if one of the colony stimulating factor partners is engineered to possess the Jun leucine zipper domain while the other is engineered to possess the Fos zipper.
  • Additional peptide sequences may also be added to facilitate purification or identification of multi-functional hematopoietic receptor agonist proteins (e.g., poly-His).
  • a highly antigenic peptide may also be added that would enable rapid assay and facile purification of the multi-functional hematopoietic receptor agonist protein by a specific monoclonal antibody.
  • mutant amino acid sequence refers to a polypeptide having an amino acid sequence which varies from a native sequence due to amino acid deletions, substitutions, or both, or is encoded by a nucleotide sequence intentionally made variant from a native sequence.
  • Native sequence refers to an amino acid or nucleic acid sequence which is identical to a wild-type or native form of a gene or protein.
  • Hematopoietic growth factors can be characterized by their ability to stimulate colony formation by human hematopoietic progenitor cells.
  • the colonies formed include erythroid, granulocyte, megakaryocyte, granulocytic macrophages and mixtures thereof.
  • Many of the hematopoietic growth factors have demonstrated the ability to restore bone marrow function and peripheral blood cell populations to therapeutically beneficial levels in studies performed initially in primates and subsequently in humans. Many or all of these biological activities of hematopoietic growth factors involve signal transduction and high affinity receptor binding.
  • Multi-functional hematopoietic receptor agonists of the present invention may exhibit useful properties such as having similar or greater biological activity when compared to a single factor or by having improved half-life or decreased adverse side effects, or a combination of these properties.
  • Multi-functional hematopoietic receptor agonists which have little or no agonist activity maybe useful as antagonists, as antigens for the production of antibodies for use in immunology or immunotherapy, as genetic probes or as intermediates used to construct other useful hIL-3 muteins.
  • Biological activity of the multi-functional hematopoietic receptor agonist proteins of the present invention can be determined by DNA synthesis in factor-dependent cell lines or by counting the colony forming units in an in vitro bone marrow assay.
  • the multi-functional hematopoietic receptor agonists of the present invention may have an improved therapeutic profile as compared to single acting hematopoietic agonists.
  • some multi-functional hematopoietic receptor agonists of the present invention may have a similar or more potent growth factor activity relative to other hematopoietic agonists without having a similar or corresponding increase in side-effects.
  • the present invention also includes the DNA sequences which code for the multi-functional hematopoietic receptor agonist proteins, DNA sequences which are substantially similar and perform substantially the same function, and DNA sequences which differ from the DNAs encoding the multi-functional hematopoietic receptor agonists of the invention only due to the degeneracy of the genetic code. Also included in the present invention are the oligonucleotide intermediates used to construct the mutant DNAs and the polypeptides coded for by these oligonucleotides.
  • Pairs of complementary synthetic oligonucleotides encoding the desired gene can be made and annealed to each other.
  • the DNA sequence of the oligonucleotide would encode sequence for amino acids of desired gene with the exception of those substituted and/or deleted from the sequence.
  • Plasmid DNA can be treated with the chosen restriction endonucleases then ligated to the annealed oligonucleotides.
  • the ligated mixtures can be used to transform competent JM101 cells to resistance to an appropriate antibiotic.
  • Single colonies can be picked and the plasmid DNA examined by restriction analysis and/or DNA sequencing to identify plasmids with the desired genes.
  • Cloning of the DNA sequences of the novel multifunctional hematopoietic agonists wherein at least one of the with the DNA sequence of the other colony stimulating factor may be accomplished by the use of intermediate vectors.
  • one gene can be cloned directly into a vector containing the other gene.
  • Linkers and adapters can be used for joining the DNA sequences, as well as replacing lost sequences, where a restriction site was internal to the region of interest.
  • genetic material (DNA) encoding one polypeptide, peptide linker, and the other polypeptide is inserted into a suitable expression vector which is used to transform bacteria, yeast, insect cells or mammalian cells. The transformed organism is grown and the protein isolated by standard techniques. The resulting product is therefore a new protein which has a colony stimulating factor joined by a linker region to a second colony stimulating factor.
  • Another aspect of the present invention provides plasmid DNA vectors for use in the expression of these novel multi-functional hematopoietic receptor agonists.
  • These vectors contain the novel DNA sequences described above which code for the novel polypeptides of the invention.
  • Appropriate vectors which can transform microorganisms capable of expressing the multi-functional hematopoietic receptor agonists include expression vectors comprising nucleotide sequences coding for the multi-functional hematopoietic receptor agonists joined to transcriptional and translational regulatory sequences which are selected according to the host cells used.
  • Vectors incorporating modified sequences as described above are included in the present invention and are useful in the production of the multi-functional hematopoietic receptor agonist polypeptides.
  • the vector employed in the method also contains selected regulatory sequences in operative association with the DNA coding sequences of the invention and which are capable of directing the replication and expression thereof in selected host cells.
  • a method for producing the novel multi-functional hematopoietic receptor agonists involves culturing suitable cells or cell line, which has been transformed with a vector containing a DNA sequence coding for expression of a novel multi-functional hematopoietic receptor agonist.
  • suitable cells or cell lines may be bacterial cells.
  • E. coli the various strains of E. coli are well-known as host cells in the field of biotechnology. Examples of such strains include E. coli strains JM101 (Yanish-Perron et al.
  • the gene encoding the multi-functional hematopoietic receptor agonists of the present invention may also be constructed such that at the 5′ end of the gene codons are added to encode Met ⁇ 2 -Ala ⁇ 1 - or Met ⁇ 1 at the N-terminus of the protein.
  • the N termini of proteins made in the cytoplasm of E. coli are affected by post-translational processing by methionine aminopeptidase (Ben Bassat et al., J. Bac. 169:751-757, 1987) and possibly by other peptidases so that upon expression the methionine is cleaved off the N-terminus.
  • the multi-functional hematopoietic receptor agonists of the present invention may include multi-functional hematopoietic receptor agonist polypeptides having Met ⁇ 1 , Ala ⁇ 1 or Met ⁇ 2 -Ala ⁇ 1 at the N-terminus. These mutant multi-functional hematopoietic receptor agonists may also be expressed in E. coli by fusing a secretion signal peptide to the N-terminus. This signal peptide is cleaved from the polypeptide as part of the secretion process.
  • mammalian cells such as Chinese hamster ovary cells (CHO).
  • CHO Chinese hamster ovary cells
  • An expression vector is constructed in which a strong promoter capable of functioning in mammalian cells drives transcription of a eukaryotic secretion signal peptide coding region, which is translationally joined to the coding region for the multi-functional hematopoietic receptor agonist.
  • plasmids such as pcDNA I/Neo, pRc/RSV, and pRc/CMV (obtained from Invitrogen Corp., San Diego, Calif.) can be used.
  • the eukaryotic secretion signal peptide coding region can be from the gene itself or it can be from another secreted mammalian protein (Bayne, M. L. et al., Proc. Natl. Acad. Sci. USA 84: 2638-2642, 1987).
  • the vector DNA is transfected into mammalian cells.
  • Such cells can be, for example, the COS7, HeLa, BHK, CHO, or mouse L lines.
  • the cells can be cultured, for example, in DMEM media (JRH Scientific).
  • the polypeptide secreted into the media can be recovered by standard biochemical approaches following transient expression for 24-72 hours after transfection of the cells or after establishment of stable cell lines following selection for antibiotic resistance.
  • suitable mammalian host cells and methods for transformation, culture, amplification, screening and product production and purification are known in the art. See, e.g., Gething and Sambrook, Nature, 293:620-625, 1981), or alternatively, Kaufman et al, Mol. Cell. Biol., 5(7):1750-1759, 1985) or Howley et al., U.S. Pat. No. 4,419,446.
  • Another suitable mammalian cell line is the monkey COS-1 cell line.
  • a similarly useful mammalian cell line is the CV-1 cell line.
  • insect cells may be utilized as host cells in the method of the present invention. See, e.g., Miller et al., Genetic Engineering, 8:277-298 (Plenum Press 1986) and references cited therein.
  • general methods for expression of foreign genes in insect cells using Baculovirus vectors are described in: Summers, M. D. and Smith, G. E., 1987)—A manual of methods for Baculovirus vectors and insect cell culture procedures, Texas Agricultural Experiment Station Bulletin No. 1555.
  • An expression vector is constructed comprising a Baculovirus transfer vector, in which a strong Baculovirus promoter (such as the polyhedron promoter) drives transcription of a eukaryotic secretion signal peptide coding region, which is translationally joined to the coding region for the multi-functional hematopoietic receptor agonist polypeptide.
  • a strong Baculovirus promoter such as the polyhedron promoter
  • the plasmid pVL1392 obtained from Invitrogen Corp., San Diego, Calif.
  • the multi-functional hematopoietic receptor agonists of the present invention may be useful in the treatment of diseases characterized by decreased levels of either myeloid, erythroid, lymphoid, or megakaryocyte cells of the hematopoietic system or combinations thereof. In addition, they may be used to activate mature myeloid and/or lymphoid cells.
  • diseases susceptible to treatment with the polypeptides of the present invention is leukopenia, a reduction in the number of circulating leukocytes (white cells) in the peripheral blood. Leukopenia may be induced by exposure to certain viruses or to radiation.
  • the multi-functional hematopoietic receptor agonists of the present invention may be useful in the treatment of neutropenia and, for example, in the treatment of such conditions as aplastic anemia, cyclic neutropenia, idiopathic neutropenia, Chediak-Higashi syndrome, systemic lupus erythematosus (SLE), leukemia, myelodysplastic syndrome and myelofibrosis.
  • the multi-functional hematopoietic receptor agonist of the present invention may be useful in the treatment or prevention of thrombocytopenia.
  • thrombocytopenia Currently the only therapy for thrombocytopenia is platelet transfusion which are costly and carry the significant risks of infection (HIV, HBV) and alloimmunization.
  • the multi-functional hematopoietic receptor agonist may alleviate or diminish the need for platelet transfusion. Severe thrombocytopenia may result from genetic defects such as Fanconi's Anemia, Wiscott-Aldrich, or May Hegglin syndromes.
  • thrombocytopenia may result from auto- or allo-antibodies as in Immune Thrombocytopenia Purpura, Systemic Lupus Erythromatosis, hemolytic anemia, or fetal maternal incompatibility.
  • splenomegaly, disseminated intravascular coagulation, thrombotic thrombocytopenic purpura, infection or prosthetic heart valves may result in thrombocytopenia.
  • Severe thrombocytopenia may also result from chemotherapy and/or radiation therapy or cancer.
  • Thrombocytopenia may also result from marrow invasion by carcinoma, lymphoma, leukemia or fibrosis.
  • the multi-functional hematopoietic receptor agonists of the present invention may be useful in the mobilization of hematopoietic progenitors and stem cells in peripheral blood.
  • Peripheral blood derived progenitors have been shown to be effective in reconstituting patients in the setting of autologous marrow transplantation.
  • Hematopoietic growth factors including G-CSF and GM-CSF have been shown to enhance the number of circulating progenitors and stem cells in the peripheral blood. This has simplified the procedure for peripheral stem cell collection and dramatically decreased the cost of the procedure by decreasing the number of pheresis required.
  • the multi-functional hematopoietic receptor agonist may be useful in mobilization of stem cells and further enhance the efficacy of peripheral stem cell transplantation.
  • the multi-functional hematopoietic receptor agonists of the present invention may also be useful in the ex vivo expansion of hematopoietic progenitors and stem cells.
  • Colony stimulating factors such as hIL-3
  • hIL-3 have been administered alone, co-administered with other CSFs, or in combination with bone marrow transplants subsequent to high dose chemotherapy to treat the neutropenia and thrombocytopenia which are often the result of such treatment.
  • CSFs colony stimulating factors
  • hIL-3 have been administered alone, co-administered with other CSFs, or in combination with bone marrow transplants subsequent to high dose chemotherapy to treat the neutropenia and thrombocytopenia which are often the result of such treatment.
  • the period of severe neutropenia and thrombocytopenia may not be totally eliminated.
  • the myeloid lineage which is comprised of monocytes (macrophages), granulocytes (including neutrophils) and megakaryocytes, is critical in preventing infections and bleeding which can be life-threatening.
  • Neutropenia and thrombocytopenia may also be the result of disease, genetic disorders, drugs, toxins, radiation and many therapeutic treatments such as conventional oncology therapy.
  • Bone marrow transplants have been used to treat this patient population.
  • several problems are associated with the use of bone marrow to reconstitute a compromised hematopoietic system including: 1) the number of stem cells in bone marrow, spleen, or peripheral blood is limited, 2) Graft Versus Host Disease, 3) graft rejection and 4) possible contamination with tumor cells.
  • Stem cells make up a very small percentage of the nucleated cells in the bone marrow, spleen and peripheral blood. It is clear that a dose response exists such that a greater number of stem cells will enhance hematopoietic recovery. Therefore, the in vitro expansion of stem cells should enhance hematopoietic recovery and patient survival.
  • Bone marrow from an allogeneic donor has been used to provide bone marrow for transplant.
  • Graft Versus Host Disease and graft rejection limit bone marrow transplantation even in recipients with HLA-matched sibling donors.
  • An alternative to allogeneic bone marrow transplants is autologous bone marrow transplants.
  • autologous bone marrow transplants some of the patient's own marrow is harvested prior to myeloablative therapy, e.g. high dose chemotherapy, and is transplanted back into the patient afterwards.
  • Autologous transplants eliminate the risk of Graft Versus Host Disease and graft rejection.
  • stem cells can be specifically isolated, based on the presence of specific surface antigens such as CD34+ in order to decrease tumor cell contamination of the marrow graft.
  • U.S. Pat. No. 5,061,620 relates to compositions comprising human hematopoietic stem cells provided by separating the stem cells from dedicated cells.
  • U.S. Pat. No. 5,199,942 describes a method for autologous hematopoietic cell transplantation comprising: (1) obtaining hematopoietic progenitor cells from a patient; (2) ex-vivo expansion of cells with a growth factor selected from the group consisting of IL-3, flt3 ligand, c-kit ligand, GM-CSF, IL-1, GM-CSF/IL-3 fusion protein and combinations thereof; (3) administering cellular preparation to a patient.
  • a growth factor selected from the group consisting of IL-3, flt3 ligand, c-kit ligand, GM-CSF, IL-1, GM-CSF/IL-3 fusion protein and combinations thereof.
  • U.S. Pat. No. 5,240,856 relates to a cell separator that includes an apparatus for automatically controlling the cell separation process.
  • WO 91/16116 describes devices and methods for selectively isolating and separating target cells from a mixture of cells.
  • WO 91/18972 describes methods for in vitro culturing of bone marrow, by incubating suspension of bone marrow cells, using a hollow fiber bioreactor.
  • WO 92/18615 relates to a process for maintaining and expanding bone marrow cells, in a culture medium containing specific mixtures of cytokines, for use in transplants.
  • WO 93/08268 describes a method for selectively expanding stem cells, comprising the steps of (a) separating CD34+ stem cells from other cells and (b) incubating the separated cells in a selective medium, such that the stem cells are selectively expanded.
  • WO 93/18136 describes a process for in vitro support of mammalian cells derived from peripheral blood.
  • WO 93/18648 relates to a composition comprising human neutrophil precursor cells with a high content of myeloblasts and promyelocytes for treating genetic or acquired neutropenia.
  • WO 94/08039 describes a method of enrichment for human hematopoietic stem cells by selection for cells which express c-kit protein.
  • WO 94/11493 describes a stem cell population that are CD34+ and small in size, which are isolated using a counterflow elutriation method.
  • WO 94/27698 relates to a method combining immunoaffinity separation and continuous flow centrifugal separation for the selective separation of a nucleated heterogeneous cell population from a heterogeneous cell mixture.
  • WO 94/25848 describes a cell separation apparatus for collection and manipulation of target cells.
  • stem cell refers to the totipotent hematopoietic stem cells as well as early precursors and progenitor cells which can be isolated from bone marrow, spleen or peripheral blood.
  • expansion refers to the differentiation and proliferation of the cells.
  • the present invention provides a method for selective ex-vivo expansion of stem cells, comprising the steps of: (a) separating stem cells from other cells, (b) culturing said separated stem cells with a selective media which contains multi-functional hematopoietic receptor agonist protein(s) and (c) harvesting said stems cells.
  • Stem cells as well as committed progenitor cells destined to become neutrophils, erythrocytes, platelets, etc. may be distinguished from most other cells by the presence or absence of particular progenitor marker antigens, such as CD34, that are present on the surface of these cells and/or by morphological characteristics.
  • progenitor marker antigens such as CD34
  • the phenotype for a highly enriched human stem cell fraction is reported as CD34+, Thy-1+ and lin-, but it is to be understood that the present invention is not limited to the expansion of this stem cell population.
  • the CD34+ enriched human stem cell fraction can be separated by a number of reported methods, including affinity columns or beads, magnetic beads or flow cytometry using antibodies directed to surface antigens such as the CD34+.
  • CD34+ progenitors are heterogeneous, and may be divided into several sub-populations characterized by the presence or absence of co-expression of different lineage associated cell surface associated molecules.
  • the most immature progenitor cells do not express any known lineage associated markers, such as HLA-DR or CD38, but they may express CD90(thy-1).
  • Other surface antigens such as CD33, CD38, CD41, CD71, HLA-DR or c-kit can also be used to selectively isolate hematopoietic progenitors.
  • the separated cells can be incubated in selected medium in a culture flask, sterile bag or in hollow fibers.
  • Various colony stimulating factors may be utilized in order to selectively expand cells.
  • Representative factors that have been utilized for ex-vivo expansion of bone marrow include, c-kit ligand, IL-3, G-CSF, GM-CSF, IL-1, IL-6, IL-11, flt-3 ligand or combinations thereof.
  • the proliferation of the stem cells can be monitored by enumerating the number of stem cells and other cells, by standard techniques (e.g. hemacytometer, CFU, LTCIC) or by flow cytometry prior and subsequent to incubation.
  • hIL-3 has been shown to be one of the most potent in expanding peripheral blood CD34+ cells (Sato et al., Blood 82:3600-3609 [1993], Kobayashi et al., Blood 73:1836-1841 [1989]).
  • no single factor has been shown to be as effective as the combination of multiple factors.
  • the present invention provides methods for ex vivo expansion that utilize multi-functional hematopoietic receptor agonists that are more effective than a single factor alone.
  • Another aspect of the invention provides methods of sustaining and/or expanding hematopoietic precursor cells which includes inoculating the cells into a culture vessel which contains a culture medium that has been conditioned by exposure to a stromal cell line such as HS-5 (WO 96/02662, Roecklein and Torok-Strob, Blood 85:997-1105, 1995) that has been supplemented with a multi-functional hematopoietic receptor agonist of the present invention.
  • a stromal cell line such as HS-5 (WO 96/02662, Roecklein and Torok-Strob, Blood 85:997-1105, 1995) that has been supplemented with a multi-functional hematopoietic receptor agonist of the present invention.
  • Gene therapy Potential applications include; 1) the treatment of many congenital metabolic disorders and immunodeficiencies (Kay and Woo, Trends Genet. 10:253-257 [1994]), 2) neurological disorders (Friedmann, Trends Genet. 10:210-214 [1994]), 3) cancer (Culver and Blaese, Trends Genet. 10:174-178 [1994]) and 4) infectious diseases (Gilboa and Smith, Trends Genet. 10:139-144 [1994]).
  • Viral based vectors include; 1) replication deficient recombinant retrovirus (Boris-Lawrie and Temin, Curr. Opin. Genet. Dev. 3:102-109 [1993], Boris-Lawrie and Temin, Annal. New York Acad. Sci. 716:59-71 [1994], Miller, Current Top. Microbiol. Immunol.
  • Non-viral based vectors include protein/DNA complexes (Cristiano et al., PNAS USA. 90:2122-2126 [1993], Curiel et al., PNAS USA 88:8850-8854 [1991], Curiel, Annal. New York Acad. Sci. 716:36-58 [1994]), electroporation and liposome mediated delivery such as cationic liposomes (Farhood et al., Annal. New York Acad. Sci. 716:23-35 [1994]).
  • the present invention provides an improvement to the existing methods of expanding hematopoietic cells, which new genetic material has been introduced, in that it provides methods utilizing multi-functional hematopoietic receptor agonist proteins that have improved biological activity, including an activity not seen by any single colony stimulation factor.
  • drugs may cause bone marrow suppression or hematopoietic deficiencies.
  • examples of such drugs are AZT, DDI, alkylating agents and anti-metabolites used in chemotherapy, antibiotics such as chloramphenicol, penicillin, gancyclovir, daunomycin and sulfa drugs, phenothiazones, tranquilizers such as meprobamate, analgesics such as aminopyrine and dipyrone, anti-convulsants such as phenyloin or carbamazepine, antithyroids such as propylthiouracil and methimazole and diuretics.
  • the multi-functional hematopoietic receptor agonists of the present invention may be useful in preventing or treating the bone marrow suppression or hematopoietic deficiencies which often occur in patients treated with these drugs.
  • Hematopoietic deficiencies may also occur as a result of viral, microbial or parasitic infections and as a result of treatment for renal disease or renal failure, e.g., dialysis.
  • the multi-functional hematopoietic receptor agonists of the present invention may be useful in treating such hematopoietic deficiencies.
  • the treatment of hematopoietic deficiency may include administration of a pharmaceutical composition containing the multi-functional hematopoietic receptor agonists to a patient.
  • the multi-functional hematopoietic receptor agonists of the present invention may also be useful for the activation and amplification of hematopoietic precursor cells by treating these cells in vitro with the multi-functional hematopoietic receptor agonist proteins of the present invention prior to injecting the cells into a patient.
  • Various immunodeficiencies e.g., in T and/or B lymphocytes, or immune disorders, e.g., rheumatoid arthritis, may also be beneficially affected by treatment with the multi-functional hematopoietic receptor agonists of the present invention.
  • Immunodeficiencies may be the result of viral infections, e.g., HTLVI, HTLVII, HTLVIII, severe exposure to radiation, cancer therapy or the result of other medical treatment.
  • the multi-functional hematopoietic receptor agonists of the present invention may also be employed, alone or in combination with other colony stimulating factors, in the treatment of other blood cell deficiencies, including thrombocytopenia (platelet deficiency), or anemia.
  • Other uses for these novel polypeptides are the in vivo and ex vivo treatment of patients recovering from bone marrow transplants, and in the development of monoclonal and polyclonal antibodies generated by standard methods for diagnostic or therapeutic use.
  • compositions for treating the conditions referred to above.
  • Such compositions comprise a therapeutically effective amount of one or more of the multi-functional hematopoietic receptor agonists of the present invention in a mixture with a pharmaceutically acceptable carrier.
  • This composition can be administered either parenterally, intravenously or subcutaneously.
  • the therapeutic composition for use in this invention is preferably in the form of a pyrogen-free, parenterally acceptable aqueous solution.
  • the preparation of such a parenterally acceptable protein solution having due regard to pH, isotonicity, stability and the like, is within the skill of the art.
  • the dosage regimen involved in a method for treating the above-described conditions will be determined by the attending physician considering various factors which modify the action of drugs, e.g., the condition, body weight, sex and diet of the patient, the severity of any infection, time of administration and other clinical factors.
  • a daily regimen may be in the range of 0.2-150 ⁇ g/kg of multi-functional hematopoietic receptor agonist protein per kilogram of body weight. Dosages would be adjusted relative to the activity of a given multi-functional hematopoietic receptor agonist protein and it would not be unreasonable to note that dosage regimens may include doses as low as 0.1 microgram and as high as 1 milligram per kilogram of body weight per day.
  • multi-functional hematopoietic receptor agonist would be adjusted higher or lower than the range of 0.2-150 micrograms per kilogram of body weight.
  • these include co-administration with other colony stimulating factors or IL-3 variants or growth factors; co-administration with chemotherapeutic drugs and/or radiation; the use of glycosylated multi-functional hematopoietic receptor agonist protein; and various patient-related issues mentioned earlier in this section.
  • the therapeutic method and compositions may also include co-administration with other human factors.
  • CSFs colony stimulating factors
  • cytokines cytokines
  • lymphokines hematopoietic growth factors and interleukins
  • GM-CSF colony stimulating factor
  • G-CSF G-CSF
  • c-mpl ligand also known as TPO or MGDF
  • M-CSF erythropoietin
  • EPO erythropoietin
  • IL-1 IL-4, IL-2, IL-3, IL-5, IL-6, IL-7, IL-8, IL-9, IL-10, IL-11, IL-12, IL-13, IL-15, IL-16, LIF, flt3 ligand, and stem cell factor (SCF) also known as steel factor or c-kit ligand, or combinations thereof.
  • SCF stem cell factor
  • the dosage recited above would be adjusted to compensate for such additional components in the therapeutic composition. Progress of the treated patient can be monitored by periodic assessment of the hematological profile, e.
  • E. coli strains such as DH5áTM (Life Technologies, Gaithersburg, Md.) and TG1 (Amersham Corp., Arlington Heights, Ill.) are used for transformation of ligation reactions and are the source of plasmid DNA for transfecting mammalian cells.
  • E. coli strains such as JM101 (Yanisch-Perron, et al., Gene, 33: 103-119, 1985) and MON 1 O 5 (Obukowicz, et al., Appl. and Envir. Micr., 58: 1511-1523, 1992) can be used for expressing the multi-functional hematopoietic receptor agonist of the present invention in the cytoplasm or periplasmic space.
  • MON105 ATCC#55204 F—, lambda-,IN(rrnD, rrE)1, rpoD+, rpoH358
  • DH5áTM F—, phi80dlacZdeltaM15, delta(lacZYA-argF)U169, deoR, recA1, endA1, hsdR17(rk ⁇ , mk+), phoA, supE44lamda-, thi-1, gyrA96, relA1
  • TG1 delta(lac-pro), supE, thi-1, hsdD5/F′(traD36, proA+B+, lacIq, lacZdeltaM15)
  • JM101 ATCC#33876 delta (pro lac), supE, thi, F′(traD36, proA+B+, lacIq, lacZdeltaM15)
  • DH5áTM Subcloning efficiency cells are purchased as competent cells and are ready for transformation using the manufacturer's protocol, while both E. coli strains TG1 and MON 1 O 5 are rendered competent to take up DNA using a CaCl 2 method.
  • 20 to 50 mL of cells are grown in LB medium (1% bacto-tryptone, 0.5% bacto-yeast extract, 150 mM NaCl) to a density of approximately 1.0 optical density unit at 600 nanometers (OD600) as measured by a Baush & Lomb Spectronic spectrophotometer (Rochester, N.Y.).
  • the cells are collected by centrifugation and resuspended in one-fifth culture volume of CaCl 2 solution (50 mM CaCl 2 , 10 mM Tris-Cl, pH7.4) and are held at 4° C. for 30 minutes.
  • the cells are again collected by centrifugation and resuspended in one-tenth culture volume of CaCl 2 solution.
  • Ligated DNA is added to 0.2 mL of these cells, and the samples are held at 4° C. for 30-60 minutes.
  • the samples are shifted to 42° C. for two minutes and 1.0 mL of LB is added prior to shaking the samples at 37° C. for one hour.
  • Cells from these samples are spread on plates (LB medium plus 1.5% bacto-agar) containing either ampicillin (100 micrograms/mL, ug/mL) when selecting for ampicillin-resistant transformants, or spectinomycin (75 ug/mL) when selecting for spectinomycin-resistant transformants.
  • ampicillin 100 micrograms/mL, ug/mL
  • spectinomycin 75 ug/mL
  • the first primer set (“new start” and “linker start”) is used to create and amplify, from the original gene sequence, the DNA fragment (“Fragment Start”) that contains the sequence encoding the new N-terminal portion of the new protein followed by the linker (L 2 ) that connects the C-terminal and N-terminal ends of the original protein.
  • the second primer set (“new stop” and “linker stop”) is used to create and amplify, from the original gene sequence, the DNA fragment (“Fragment Stop”) that encodes the same linker as used above, followed by the new C-terminal portion of the new protein.
  • the “new start” and “new stop” primers are designed to include the appropriate restriction sites which allow cloning of the new gene into expression plasmids.
  • Typical PCR conditions are one cycle 95° C. melting for two minutes; 25 cycles 94° C. denaturation for one minute, 50° C. annealing for one minute and 72° C. extension for one minute; plus one cycle 72° C. extension for seven minutes.
  • a Perkin Elmer GeneAmp PCR Core Reagents kit is used.
  • a 100 ul reaction contains 100 pmole of each primer and one ug of template DNA; and 1 ⁇ PCR buffer, 200 uM dGTP, 200 uM dATP, 200 uM dTTP, 200 uM dCTP, 2.5 units AmpliTaq DNA polymerase and 2 mM MgCl2.
  • PCR reactions are performed in a Model 480 DNA thermal cycler (Perkin Elmer Corporation, Norwalk, Conn.).
  • the DNA fragments “Fragment Start” and “Fragment Stop” are resolved on a 1% TAE gel, stained with ethidium bromide and isolated using a Qiaex Gel Extraction kit (Qiagen). These fragments are combined in equimolar quantities, heated at 70° C. for ten minutes and slow cooled to allow annealing through their shared sequence in “linker start” and “linker stop”.
  • primers “new start” and “new stop” are added to the annealed fragments to create and amplify the full-length new N-terminus/C-terminus gene.
  • Typical PCR conditions are one cycle 95° C. melting for two minutes; 25 cycles 94° C. denaturation for one minute, 60° C. annealing for one minute and 72° C. extension for one minute; plus one cycle 72° C. extension for seven minutes.
  • a Perkin Elmer GeneAmp PCR Core Reagents kit is used.
  • a 100 ul reaction contains 100 pmole of each primer and approximately 0.5 ug of DNA; and 1 ⁇ PCR buffer, 200 uM dGTP, 200 uM dATP, 200 uM dTTP, 200 uM dCTP, 2.5 units AmpliTaq DNA polymerase and 2 mM MgCl2.
  • PCR reactions are purified using a Wizard PCR Preps kit (Promega).
  • New N-terminus/C-terminus genes without a linker joining the original N-terminus and C-terminus can be made using two steps of PCR amplification and a blunt end ligation. The steps are illustrated in FIG. 3.
  • the primer set (“new start” and “P-bl start”) is used to create and amplify, from the original gene sequence, the DNA fragment (“Fragment Start”) that contains the sequence encoding the new N-terminal portion of the new protein.
  • the primer set (“new stop” and “P-bl stop”) is used to create and amplify, from gene sequence, the DNA fragment (“Fragment Stop”) that contains the sequence encoding the new C-terminal portion of the new protein.
  • the “new start” and “new stop” primers are designed to include appropriate restriction sites which allow cloning of the new gene into expression vectors. Typical PCR conditions are one cycle 95° C. melting for two minutes; 25 cycles 94° C. denaturation for one minute, 50° C. annealing for 45 seconds and 72° C. extension for 45 seconds. Deep Vent polymerase (New England Biolabs) is used to reduce the occurrence of overhangs in conditions recommended by the manufacturer.
  • the “P-bl start” and “P-bl stop” primers are phosphorylated at the 5′ end to aid in the subsequent blunt end ligation of “Fragment Start” and “Fragment Stop” to each other.
  • a 100 ul reaction contained 150 pmole of each primer and one ug of template DNA; and 1 ⁇ Vent buffer (New England Biolabs), 300 uM dGTP, 300 uM dATP, 300 uM dTTP, 300 uM dCTP, and 1 unit Deep Vent polymerase.
  • PCR reactions are performed in a Model 480 DNA thermal cycler (Perkin Elmer Corporation, Norwalk, Conn.). PCR reaction products are purified using a Wizard PCR Preps kit (Promega).
  • the primers are designed to include appropriate restriction sites which allow for the cloning of the new gene into expression vectors.
  • “Fragment Start” is designed to create NcoI restriction site
  • “Fragment Stop” is designed to create a HindIII restriction site.
  • Restriction digest reactions are purified using a Magic DNA Clean-up System kit (Promega). Fragments Start and Stop are resolved on a 1% TAE gel, stained with ethidium bromide and isolated using a Qiaex Gel Extraction kit (Qiagen). These fragments are combined with and annealed to the ends of the ⁇ 3800 base pair NcoI/HindIII vector fragment of pMON3934 by heating at 50° C. for ten minutes and allowed to slow cool.
  • the three fragments are ligated together using T4 DNA ligase (Boehringer Mannheim).
  • T4 DNA ligase Boehringer Mannheim
  • the result is a plasmid containing the full-length new N-terminus/C-terminus gene.
  • a portion of the ligation reaction is used to transform E. coli strain DH5á cells (Life Technologies, Gaithersburg, Md.). Plasmid DNA is purified and sequence confirmed as below.
  • New N-terminus/C-terminus genes can be made based on the method described in R. A. Horlick, et al Protein Eng. 5:427-431, 1992). Polymerase chain reaction (PCR) amplification of the new N-terminus/C-terminus genes is performed using a tandemly duplicated template DNA. The steps are illustrated in FIG. 3.
  • the tandemly-duplicated template DNA is created by cloning and contains two copies of the gene separated by DNA sequence encoding a linker connecting the original C- and N-terminal ends of the two copies of the gene.
  • Specific primer sets are used to create and amplify a full-length new N terminus/C-terminus gene from the tandemly-duplicated template DNA. These primers are designed to include appropriate restriction sites which allow for the cloning of the new gene into expression vectors.
  • Typical PCR conditions are one cycle 95° C. melting for two minutes; 25 cycles 94° C. denaturation for one minute, 50° C. annealing for one minute and 72° C. extension for one minute; plus one cycle 72° C. extension for seven minutes.
  • a Perkin Elmer GeneAmp PCR Core Reagents kit (Perkin Elmer Corporation, Norwalk, Conn.) is used.
  • a 100 ul reaction contains 100 pmole of each primer and one ug of template DNA; and 1 ⁇ PCR buffer, 200 uM dGTP, 200 uM dATP, 200 uM dTTP, 200 uM dCTP, 2.5 units AmpliTaq DNA polymerase and 2 mM MgCl 2 .
  • PCR reactions are performed in a Model 480 DNA thermal cycler (Perkin Elmer Corporation, Norwalk, Conn.). PCR reactions are purified using a Wizard PCR Preps kit (Promega).
  • the new N-terminus/C-terminus gene is digested with restriction endonucleases to create ends that are compatible to insertion into an expression vector containing another colony stimulating factor gene.
  • This expression vector is likewise digested with restriction endonucleases to form compatible ends.
  • the gene and the vector DNAs are combined and ligated using T4 DNA ligase. A portion of the ligation reaction is used to transform E. coli . Plasmid DNA is purified and sequenced to confirm the correct insert. The correct clones are grown for protein expression.
  • Plasmid DNA can be isolated by a number of different methods and using commercially available kits known to those skilled in the art. A few such methods are shown herein. Plasmid DNA is isolated using the Promega WizardTM Miniprep kit (Madison, Wis.), the Qiagen QIAwell Plasmid isolation kits (Chatsworth, Calif.) or Qiagen Plasmid Midi kit. These kits follow the same general procedure for plasmid DNA isolation. Briefly, cells are pelleted by centrifugation (5000 ⁇ g), plasmid DNA released with sequential NaOH/acid treatment, and cellular debris is removed by centrifugation (10000 ⁇ g).
  • the supernatant (containing the plasmid DNA) is loaded onto a column containing a DNA-binding resin, the column is washed, and plasmid DNA eluted with TE. After screening for the colonies with the plasmid of interest, the E. coli cells are inoculated into 50-100 mls of LB plus appropriate antibiotic for overnight growth at 37° C. in an air incubator while shaking.
  • the purified plasmid DNA is used for DNA sequencing, further restriction enzyme digestion, additional subcloning of DNA fragments and transfection into mammalian, E. coli or other cells.
  • Samples are purified to remove excess dye terminators with Centri-SepTM spin columns (Princeton Separations, Adelphia, N.J.) and lyophilized. Fluorescent dye labeled sequencing reactions are resuspended in deionized formamide, and sequenced on denaturing 4.75% polyacrylamide-8M urea gels using an ABI Model 373A automated DNA sequencer. Overlapping DNA sequence fragments are analyzed and assembled into master DNA contigs using Sequencher v2.1 DNA analysis software (Gene Codes Corporation, Ann Arbor, Mich.).
  • the BHK-21 cell line can be obtained from the ATCC (Rockville, Md.). The cells are cultured in Dulbecco's modified Eagle media (DMEM/high-glucose), supplemented to 2 mM (mM) L-glutamine and 10% fetal bovine serum (FBS). This formulation is designated BHK growth media. Selective media is BHK growth media supplemented with 453 units/mL hygromycin B (Calbiochem, San Diego, Calif.).
  • DMEM/high-glucose Dulbecco's modified Eagle media
  • FBS fetal bovine serum
  • the BHK-21 cell line was previously stably transfected with the HSV transactivating protein VP16, which transactivates the IE110 promoter found on the plasmid pMON3359 (See Hippenmeyer et al., Bio/Technology , pp.1037-1041, 1993).
  • the VP16 protein drives expression of genes inserted behind the IE110 promoter.
  • BHK-21 cells expressing the transactivating protein VP16 are designated BHK-VP16.
  • the plasmid pMON1118 See Highkin et al., Poultry Sci., 70: 970-981, 1991 expresses the hygromycin resistance gene from the SV40 promoter.
  • a similar plasmid is available from ATCC, pSV2-hph.
  • BHK-VP16 cells are seeded into a 60 millimeter (mm) tissue culture dish at 3 ⁇ 10 5 cells per dish 24 hours prior to transfection.
  • Cells are transfected for 16 hours in 3 mL of “OPTIMEM”TM (Gibco-BRL, Gaithersburg, Md.) containing 10 ug of plasmid DNA containing the gene of interest, 3 ug hygromycin resistance plasmid, pMON1118, and 80 ug of Gibco-BRL “LIPOFECTAMINE”TM per dish.
  • the media is subsequently aspirated and replaced with 3 mL of growth media.
  • media from each dish is collected and assayed for activity (transient conditioned media).
  • the cells are removed from the dish by trypsin-EDTA, diluted 1:10 and transferred to 100 mm tissue culture dishes containing 10 mL of selective media. After approximately 7 days in selective media, resistant cells grow into colonies several millimeters in diameter. The colonies are removed from the dish with filter paper (cut to approximately the same size as the colonies and soaked in trypsin/EDTA) and transferred to individual wells of a 24 well plate containing 1 mL of selective media. After the clones are grown to confluence, the conditioned media is re-assayed, and positive clones are expanded into growth media.
  • E. coli strain MON 1 O 5 or JM101 harboring the plasmid of interest are grown at 37° C. in M9 plus casamino acids medium with shaking in a air incubator Model G25 from New Brunswick Scientific (Edison, N.J.). Growth is monitored at OD600 until it reaches a value of 1.0 at which time Nalidixic acid (10 milligrams/mL) in 0.1 N NaOH is added to a final concentration of 50 ⁇ g/mL. The cultures are then shaken at 37° C. for three to four additional hours. A high degree of aeration is maintained throughout culture period in order to achieve maximal production of the desired gene product. The cells are examined under a light microscope for the presence of inclusion bodies (IB).
  • IB inclusion bodies
  • One mL aliquots of the culture are removed for analysis of protein content by boiling the pelleted cells, treating them with reducing buffer and electrophoresis via SDS-PAGE (see Maniatis et al. Molecular Cloning: A Laboratory Manual, 1982).
  • the culture is centrifuged (5000 ⁇ g) to pellet the cells.
  • the cell pellet from a 330 mL E. coli culture is resuspended in 15 mL of sonication buffer (10 mM 2-amino-2-(hydroxymethyl) 1,3-propanediol hydrochloride (Tris-HCl), pH 8.0+1 mM ethylenediaminetetraacetic acid (EDTA).
  • sonication buffer 10 mM 2-amino-2-(hydroxymethyl) 1,3-propanediol hydrochloride (Tris-HCl), pH 8.0+1 mM ethylenediaminetetraacetic acid (EDTA).
  • Tris-HCl 2-amino-2-(hydroxymethyl) 1,3-propanediol hydrochloride
  • EDTA ethylenediaminetetraacetic acid
  • the IB pellet is resuspended in 10 mL of 50 mM Tris-HCl, pH 9.5, 8 M urea and 5 mM dithiothreitol (DTT) and stirred at room temperature for approximately 45 minutes to allow for denaturation of the expressed protein.
  • DTT dithiothreitol
  • the extraction solution is transferred to a beaker containing 70 mL of 5 mM Tris-HCl, pH 9.5 and 2.3 M urea and gently stirred while exposed to air at 4° C. for 18 to 48 hours to allow the proteins to refold.
  • Refolding is monitored by analysis on a Vydac (Hesperia, Ca.) C18 reversed phase high pressure liquid chromatography (RP-HPLC) column (0.46 ⁇ 25 cm).
  • RP-HPLC reversed phase high pressure liquid chromatography
  • a linear gradient of 40% to 65% acetonitrile, containing 0.1% trifluoroacetic acid (TFA) is employed to monitor the refold. This gradient is developed over 30 minutes at a flow rate of 1.5 mL per minute.
  • Denatured proteins generally elute later in the gradient than the refolded proteins.
  • contaminating E. coli proteins are removed by acid precipitation.
  • the pH of the refold solution is titrated to between pH 5.0 and pH 5.2 using 15% (v/v) acetic acid (HOAc). This solution is stirred at 4° C. for 2 hours and then centrifuged for 20 minutes at 12,000 ⁇ g to pellet any insoluble protein.
  • HOAc acetic acid
  • the supernatant from the acid precipitation step is dialyzed using a Spectra/Por 3 membrane with a molecular weight cut off (MWCO) of 3,500 daltons.
  • the dialysis is against 2 changes of 4 liters (a 50-fold excess) of 10 mM Tris-HCl, pH 8.0 for a total of 18 hours. Dialysis lowers the sample conductivity and removes urea prior to DEAE chromatography.
  • the sample is then centrifuged (20 minutes at 12,000 ⁇ g) to pellet any insoluble protein following dialysis.
  • a Bio-Rad Bio-Scale DEAE2 column (7 ⁇ 52 mm) is used for ion exchange chromatography.
  • the column is equilibrated in a buffer containing 10 mM Tris-HCl, pH 8.0, and a 0-to-500 mM sodium chloride (NaCl) gradient, in equilibration buffer, over 45 column volumes is used to elute the protein.
  • a flow rate of 1.0 mL per minute is used throughout the run.
  • Column fractions (2.0 mL per fraction) are collected across the gradient and analyzed by RP HPLC on a Vydac (Hesperia, Ca.) C18 column (0.46 ⁇ 25 cm).
  • TFA trifluoroacetic acid
  • the folded proteins can be affinity purified using affinity reagents such as mabs or receptor subunits attached to a suitable matrix.
  • affinity reagents such as mabs or receptor subunits attached to a suitable matrix.
  • purification can be accomplished using any of a variety of chromatographic methods such as: ion exchange, gel filtration or hydrophobic chromatography or reversed phase HPLC.
  • the purified protein is analyzed by RP-HPLC, electrospray mass spectrometry, and SDS-PAGE.
  • the protein quantitation is done by amino acid composition, RP-HPLC, and Bradford protein determination.
  • tryptic peptide mapping is performed in conjunction with electrospray mass spectrometry to confirm the identity of the protein.
  • the factor-dependent cell line AML 193 was obtained from the American Type Culture Collection (ATCC, Rockville, Md.). This cell line, established from a patient with acute myelogenous leukemia, is a growth factor dependent cell line which displayed enhanced growth in GM-CSF supplemented medium (Lange, B., et al., Blood 70: 192, 1987; Valtieri, M., et al., J. Immunol. 138:4042, 1987). The ability of AML 193 cells to proliferate in the presence of human IL-3 has also been documented. (Santoli, D., et al., J. Immunol. 139: 348, 1987).
  • a cell line variant was used, AML 193 1.3, which was adapted for long term growth in IL-3 by washing out the growth factors and starving the cytokine dependent AML 193 cells for growth factors for 24 hours. The cells are then replated at 1 ⁇ 10 5 cells/well in a 24 well plate in media containing 100 U/mL IL-3. It took approximately 2 months for the cells to grow rapidly in IL-3. These cells are maintained as AML 193 1.3 thereafter by supplementing tissue culture medium (see below) with human IL-3.
  • AML 193 1.3 cells are washed 6 times in cold Hanks balanced salt solution (HBSS, Gibco, Grand Island, N.Y.) by centrifuging cell suspensions at 250 ⁇ g for 10 minutes followed by decantation of the supernatant. Pelleted cells are resuspended in HBSS and the procedure is repeated until six wash cycles are completed. Cells washed six times by this procedure are resuspended in tissue culture medium at a density ranging from 2 ⁇ 10 5 to 5 ⁇ 10 5 viable cells/mL.
  • HBSS cold Hanks balanced salt solution
  • This medium is prepared by supplementing Iscove's modified Dulbecco's Medium (IMDM, Hazelton, Lenexa, Kans.) with albumin, transferrin, lipids and 2-mercaptoethanol.
  • IMDM Iscove's modified Dulbecco's Medium
  • Bovine albumin Bovine albumin (Boehringer-Mannheim, Indianapolis, Ind.) is added at 500 ⁇ g/mL; human transferrin (Boehringer-Mannheim, Indianapolis, Ind.) is added at 100 ⁇ g/mL; soybean lipid (Boehringer-Mannheim, Indianapolis, Ind.) is added at 50 ⁇ g/mL; and 2-mercaptoethanol (Sigma, St. Louis, Mo.) is added at 5 ⁇ 10 ⁇ 5 M.
  • 0.5 ⁇ Ci 3 H-thymidine (2 Ci/mM, New England Nuclear, Boston, Mass.) is added in 50 ⁇ l of tissue culture medium. Cultures are incubated at 37° C. with 5% CO 2 in humidified air for 18-24 hours. Cellular DNA is harvested onto glass filter mats (Pharmacia LKB, Gaithersburg, Md.) using a TOMTEC cell harvester (TOMTEC, Orange, Conn.) which utilized a water wash cycle followed by a 70% ethanol wash cycle. Filter mats are allowed to air dry and then placed into sample bags to which scintillation fluid (Scintiverse II, Fisher Scientific, St. Louis, Mo.
  • TOMTEC TOMTEC, Orange, Conn.
  • BetaPlate Scintillation Fluid Pharmacia LKB, Gaithersburg, Md.
  • Beta emissions of samples from individual tissue culture wells are counted in a LKB BetaPlate model 1205 scintillation counter (Pharmacia LKB, Gaithersburg, Md.) and data is expressed as counts per minute of 3 H-thymidine incorporated into cells from each tissue culture well.
  • Activity of each human interleukin-3 preparation or multi-functional hematopoietic receptor agonist protein preparation is quantitated by measuring cell proliferation ( 3 H-thymidine incorporation) induced by graded concentrations of interleukin-3 or multi-functional hematopoietic receptor agonist.
  • concentration ranges from 0.05 pM-10 5 pM are quantitated in these assays.
  • the multi-functional hematopoietic receptor agonist proteins were tested in a concentration range of 2000 pM to 0.06 pM titrated in serial 2 fold dilutions.
  • the proliferation assay was performed with the multi-functional hematopoietic receptor agonist plus and minus neutralizing monoclonal antibodies to the hIL-3 receptor agonist portion.
  • a fusion molecule with the factor Xa cleavage site was cleaved then purified and the halves of the molecule were assayed for proliferative activity.
  • c-mpl ligand proliferative activity can be assayed using a subclone of the pluripotential human cell line TF1 (Kitamura et al., J. Cell Physiol 140:323-334. [1989]). TF1 cells are maintained in h-IL3 (100 U/mL). To establish a sub-clone responsive to c-mpl ligand, cells are maintained in passage media containing 10% supernatant from BHK cells transfected with the gene expressing the 1-153 form of c-mpl ligand (pMON26448). Most of the cells die, but a subset of cells survive.
  • a c-mpl ligand responsive clone is selected, and these cells are split into passage media to a density of 0.3 ⁇ 10 6 cells/mL the day prior to assay set-up.
  • Passage media for these cells is the following: RPMI 1640 (Gibco), 10% FBS (Harlan, Lot #91206), 10% c-mpl ligand supernatant from transfected BHK cells, 1 mM sodium pyruvate (Gibco), 2 mM glutamine (Gibco), and 100 ug/mL penicillin-streptomycin (Gibco).
  • ATL medium consists of the following:IMDM (Gibco), 500 ug/mL of bovine serum albumin, 100 ug/mL of human transferrin, 50 ug/mL soybean lipids, 4 ⁇ 10-8M beta-mercaptoethanol and 2 mL of A9909 (Sigma, antibiotic solution) per 1000 mL of ATL.
  • Cells are diluted in assay media to a final density of 0.25 ⁇ 10 6 cells/mL in a 96-well low evaporation plate (Costar) to a final volume of 50 ul.
  • Transient supernatants (conditioned media) from transfected clones are added at a volume of 50 ul as duplicate samples at a final concentration of 50% and diluted three-fold to a final dilution of 1.8%.
  • Triplicate samples of a dose curve of IL-3 variant pMON13288 starting at 1 ng/mL and diluted using three-fold dilutions to 0.0014 ng/mL is included as a positive control. Plates are incubated at 5% CO 2 and 37° C. At day six of culture, the plate is pulsed with 0.5 Ci of 3H/well (NEN) in a volume of 20 ul/well and allowed to incubate at 5% CO 2 and 37° C. for four hours. The plate is harvested and counted on a Betaplate counter.
  • TF1 proliferation assay TF1 is a pluripotential human cell line (Kitamura et al., J. Cell Physiol 140:323-334. [1989]) that responds to hIL-3.
  • 32D proliferation assay 32D is a murine IL-3 dependent cell line which does not respond to human IL-3 but does respond to human G-CSF which is not species restricted.
  • Baf/3 proliferation assay Baf/3 is a murine IL-3 dependent cell line which does not respond to human IL-3 or human c-mpl ligand but does respond to human G-CSF which is not species restricted.
  • T1165 proliferation assay T1165 cells are a IL-6 dependent murine cell line (Nordan et al., 1986) which respond to IL-6 and IL-11.
  • Human Plasma Clot meg-CSF Assay Used to assay megakaryocyte colony formation activity (Mazur et al., 1981).
  • Cell lines such as the murine Baf/3 cell line can be transfected with a colony stimulating factor receptor, such as the human G-CSF receptor or human c-mpl receptor, which the cell line does not have. These transfected cell lines can be used to determine the activity of the ligand for which the receptor has been transfected into the cell line.
  • a colony stimulating factor receptor such as the human G-CSF receptor or human c-mpl receptor
  • One such transfected Baf/3 cell line was made by cloning the cDNA encoding c-mpl from a library made from a c-mpl responsive cell line and cloned into the multiple cloning site of the plasmid pcDNA3 (Invitrogen, San Diego Calif.). Baf/3 cells were transfected with the plasmid via electroporation. The cells were grown under G418 selection in the presence of mouse IL-3 in Wehi conditioned media. Clones were established through limited dilution.
  • the human G-CSF receptor can be transfected into the Baf/3 cell line and used to determine the bioactivity of the multi-functional hematopoietic receptor agoinsts.
  • Bone marrow aspirates (15-20 mL) were obtained from normal allogeneic marrow donors after informed consent. Cells were diluted 1:3 in phosphate buffered saline (PBS, Gibco-BRL), 30 mL were layered over 15 mL Histopaque-1077 (Sigma) and centrifuged for 30 minutes at 300 RCF. The mononuclear interface layer was collected and washed in PBS. CD34+ cells were enriched from the mononuclear cell preparation using an affinity column per manufacturers instructions (CellPro, Inc, Bothell Wash.).
  • PBS phosphate buffered saline
  • CD34+ cells After enrichment, the purity of CD34+ cells was 70% on average as determined by using flow cytometric analysis using anti-CD34 monoclonal antibody conjugated to fluorescein and anti-CD38 conjugated to phycoerythrin (Becton Dickinson, San Jose Calif.).
  • CD41a-FITC Green fluorescence
  • PI red fluorescence
  • CD34+ enriched population were isolated as described above. Cells were suspended at 25,000 cells/mL with or without cytokine(s) in a media consisting of a base Iscoves IMDM media supplemented with 0.3% BSA, 0.4 mg/mL apo-transferrin, 6.67 ⁇ M FeCl 2 , 25 ⁇ g/mL CaCl 2 , 25 ⁇ g/mL L-asparagine, 500 ⁇ g/mL e-amino-n-caproic acid and penicillin/streptomycin. Prior to plating into 35 mm plates, thrombin was added (0.25 Units/mL) to initiate clot formation. Cells were incubated at 37° C. for 13 days at 5% CO 2 in a 37° C. humidified incubator.
  • This assay reflects the ability of colony stimulating factors to stimulate normal bone marrow cells to produce different types of hematopoietic colonies in vitro (Bradley et al., Aust. Exp Biol. Sci. 44:287-300, 1966), Pluznik et al., J. Cell Comp. Physio 66:319-324, 1965).
  • CD34+ cells are counted and CD34+ cells are selected using the Ceprate LC (CD34) Kit (CellPro Co., Bothel, Wash.) column. This fractionation is performed since all stem and progenitor cells within the bone marrow display CD34 surface antigen.
  • Cultures are set up in triplicate with a final volume of 1.0 mL in a 35 ⁇ 10 mm petri dish (Nunc#174926).
  • Culture medium is purchased from Terry Fox Labs. (HCC-4230 medium (Terry Fox Labs, Vancouver, B.C., Canada) and erythropoietin (Amgen, Thousand Oaks, Calif.) is added to the culture media.
  • 3,000-10,000 CD34+ cells are added per dish.
  • Recombinant IL-3 purified from mammalian cells or E. coli , and multi-functional hematopoietic receptor agonist proteins, in conditioned media from transfected mammalian cells or purified from conditioned media from transfected mammalian cells or E.
  • coli are added to give final concentrations ranging from 0.001 nM to 10 nM.
  • Recombinant hIL-3, GM-CSF, c-mpl ligand and multi-functional hematopoietic receptor agonist are supplied in house.
  • G-CSF Neurogen
  • Cultures are resuspended using a 3 cc syringe and 1.0 mL is dispensed per dish.
  • Control baseline response cultures received no colony stimulating factors.
  • Positive control cultures received conditioned media (PHA stimulated human cells: Terry Fox Lab. H2400). Cultures are incubated at 37° C., 5% CO 2 in humidified air.
  • Hematopoietic colonies which are defined as greater than 50 cells are counted on the day of peak response (days 10-11) using a Nikon inverted phase microscope with a 40 ⁇ objective combination. Groups of cells containing fewer than 50 cells are referred to as clusters. Alternatively colonies can be identified by spreading the colonies on a slide and stained or they can be picked, resuspended and spun onto cytospin slides for staining.
  • Bone marrow cells are traditionally used for in vitro assays of hematopoietic colony stimulating factor (CSF) activity.
  • CSF colony stimulating factor
  • human bone marrow is not always available, and there is considerable variability between donors.
  • Umbilical cord blood is comparable to bone marrow as a source of hematopoietic stem cells and progenitors (Broxmeyer et al., PNAS USA 89:4109-113, 1992; Mayani et al., Blood 81:3252-3258, 1993). In contrast to bone marrow, cord blood is more readily available on a regular basis.
  • There is also a potential to reduce assay variability by pooling cells obtained fresh from several donors, or to create a bank of cryopreserved cells for this purpose.
  • CFU-GM granulocyte/macrophage colonies
  • HPP-CFC high proliferative potential colony forming cell
  • Mononuclear cells are isolated from cord blood within 24 hr. of collection, using a standard density gradient (1.077 g/mL Histopaque).
  • Cord blood MNC have been further enriched for stem cells and progenitors by several procedures, including immunomagnetic selection for CD14-, CD34+ cells; panning for SBA-, CD34+ fraction using coated flasks from Applied Immune Science (Santa Clara, Calif.); and CD34+ selection using a CellPro (Bothell, Wash.) avidin column. Either freshly isolated or cryopreserved CD34+ cell enriched fractions are used for the assay.
  • Duplicate cultures for each serial dilution of sample are prepared with 1 ⁇ 10 4 cells in 1 ml of 0.9% methycellulose containing medium without additional growth factors (Methocult H4230 from Stem Cell Technologies, Vancouver, BC.).
  • Methocult H4330 containing erythropoietin (EPO) was used instead of Methocult H4230, or Stem Cell Factor (SCF), 50 ng/mL (Biosource International, Camarillo, Calif.) was added. After culturing for 7-9 days, colonies containing>30 cells are counted. In order to rule out subjective bias in scoring, assays are scored blind.

Abstract

Disclosed are novel multi-functional hematopoietic receptor agonist proteins, DNAs which encode the multi-functional hematopoietic receptor agonists proteins, methods of making the multi-functional hematopoietic receptor agonists proteins and methods of using the multi-functional hematopoietic receptor agonists proteins.

Description

    CROSS-REFERENCE TO RELATED APPLICATIONS
  • The present application is a continuation of U.S. patent application Ser. No. 09/510,238, filed Feb. 22, 2002, pending, which is a divisional of U.S. patent application Ser. No. 08/835,162 filed Apr. 4, 1997, now issued as U.S. Pat. No. 6,066,318 on May 23, 2000, which is a continuation-in-part of PCT/US 96/15774 filed Oct. 4, 1996 which claims priority under 35 U.S.C. §119(e) of U.S. Provisional Pat. App. Ser. No. 60/004,834, filed Oct. 5, 1995, now abandoned.[0001]
    • REFERENCE TO A “SEQUENTIAL LISTING,” A TABLE, OR A COMPTUER PROGRAM LISTING APPENDIX SUBMITTED ON A DISKETTE
  • This application includes a computer program listing appendix, pursuant to 37 CFR 1.96, contained on a diskette, which is incorporated fully into this application by this reference. [0002]
  • The diskette is labeled as follows: [0003]
  • Applicant: Feng, et al. [0004]
  • Title: Multi-Functional Hematopoietic Fusion Proteins Between Sequence Rearranged G-CSF Receptor Agonists and Other Hematopoietic Factors [0005]
  • Recorded: Oct. 23, 2003 [0006]
  • Atty No.: 126181-1058 [0007]
  • Serial No.: Unknown [0008]
  • Filing Date: Oct. 27, 2003 [0009]
  • The diskette contains the following file in ASCII file format: [0010]
    File Name File size Creation Date
    Sequence.txt 574 kb Oct. 23, 2003
    • BACKGROUND OF THE INVENTION
  • The present invention relates to multi-functional hematopoietic receptor agonists. [0011]
  • Colony stimulating factors (CSFs) which stimulate the differentiation and/or proliferation of bone marrow cells have generated much interest because of their therapeutic potential for restoring depressed levels of hematopoietic stem cell-derived cells. CSFs in both human and murine systems have been identified and distinguished according to their activities. For example, granulocyte-CSF (G-CSF) and macrophage-CSF (M-CSF) stimulate the in vitro formation of neutrophilic granulocyte and macrophage colonies, respectively, while GM-CSF and interleukin-3 (IL-3) have broader activities and stimulate the formation of both macrophage, neutrophilic and eosinophilic granulocyte colonies. IL-3 also stimulates the formation of mast, megakaryocyte and pure and mixed erythroid colonies. [0012]
    • DESCRIPTION OF RELATED ART
  • U.S. Pat. No. 4,877,729 and U.S. Pat. No. 4,959,455 disclose human IL-3 and gibbon IL-3 cDNAs and the protein sequences for which they code. The hIL-3 disclosed has serine rather than proline at position 8 in the protein sequence. [0013]
  • International Patent Application (PCT) Wo 88/00598 discloses gibbon- and human-like IL-3. The hIL-3 contains a Ser[0014] 8->Pro8 replacement. Suggestions are made to replace Cys by Ser, thereby breaking the disulfide bridge, and to replace one or more amino acids at the glycosylation sites.
  • U.S. Pat. No. 4,810,643 discloses the DNA sequence encoding human G-CSF. [0015]
  • WO 91/02754 discloses a fusion protein comprised of GM-CSF and IL-3 which has increased biological activity compared to GM-CSF or IL-3 alone. Also disclosed are nonglycosylated IL-3 and GM-CSF analog proteins as components of the multi-functional hematopoietic receptor agonist. [0016]
  • WO 92/04455 discloses fusion proteins composed of IL-3 fused to a lymphokine selected from the group consisting of IL-3, IL-6, IL-7, IL-9, IL-11, EPO and G-CSF. [0017]
  • WO 95/21197 and WO 95/21254 disclose fusion proteins capable of broad multi-functional hematopoietic properties. [0018]
  • GB 2,285,446 relates to the c-mpl ligand (thrombopoietin) and various forms of thrombopoietin which are shown to influence the replication, differentiation and maturation of megakaryocytes and megakaryocytes progenitors which may be used for the treatment of thrombocytopenia. [0019]
  • EP 675,201 A1 relates to the c-mpl ligand (Megakaryocyte growth and development factor (MGDF), allelic variations of c-mpl ligand and c-mpl ligand attached to water soluble polymers such as polyethylene glycol. [0020]
  • WO 95/21920 provides the murine and human c-mpl ligand and polypeptide fragments thereof. The proteins are useful for in vivo and ex vivo therapy for stimulating platelet production. [0021]
    • Rearrangement of Protein Sequences
  • In evolution, rearrangements of DNA sequences serve an important role in generating a diversity of protein structure and function. Gene duplication and exon shuffling provide an important mechanism to rapidly generate diversity and thereby provide organisms with a competitive advantage, especially since the basal mutation rate is low (Doolittle, [0022] Protein Science 1:191-200, 1992).
  • The development of recombinant DNA methods has made it possible to study the effects of sequence transposition on protein folding, structure and function. The approach used in creating new sequences resembles that of naturally occurring pairs of proteins that are related by linear reorganization of their amino acid sequences (Cunningham, et al., [0023] Proc. Natl. Acad. Sci. U.S.A. 76:3218-3222, 1979; Teather & Erfle, J. Bacteriol. 172: 3837-3841, 1990; Schimming et al., Eur. J. Biochem. 204: 13-19, 1992; Yamiuchi and Minamikawa, FEBS Lett. 260:127-130, 1991; MacGregor et al., FEBS Lett. 378:263-266). The first in vitro application of this type of rearrangement to proteins was described by Goldenberg and Creighton (J. Mol. Biol. 165:407-413, 1983). A new N-terminus is selected at an internal site (breakpoint) of the original sequence, the new sequence having the same order of amino acids as the original from the breakpoint until it reaches an amino acid that is at or near the original C-terminus. At this point the new sequence is joined, either directly or through an additional portion of sequence (linker), to an amino acid that is at or near the original N-terminus, and the new sequence continues with the same sequence as the original until it reaches a point that is at or near the amino acid that was N-terminal to the breakpoint site of the original sequence, this residue forming the new C-terminus of the chain.
  • This approach has been applied to proteins which range in size from 58 to 462 amino acids (Goldenberg & Creighton, [0024] J. Mol. Biol. 165:407-413, 1983; Li & Coffino, Mol. Cell. Biol. 13:2377-2383, 1993). The proteins examined have represented a broad range of structural classes, including proteins that contain predominantly a-helix (interleukin-4; Kreitman et al., Cytokine 7:311-318, 1995), b-sheet (interleukin-1; Horlick et al., Protein Eng. 5:427-431, 1992), or mixtures of the two (yeast phosphoribosyl anthranilate isomerase; Luger et al., Science 243:206-210, 1989). Broad categories of protein function are represented in these sequence reorganization studies:
    Enzymes
    T4 lysozyme Zhang et al., Biochemistry 32: 12311-12318,
    1993; Zhang et al., Nature Struct. Biol.
    1: 434-438 (1995).
    dihydrofolate Buchwalder et al., Biochemistry reductase
    31: 1621-1630, 1994; Protasova et al.,
    Prot. Eng. 7: 1373-1377, 1995).
    ribonuclease T1 Mullins et al., J. Am. Chem. Soc.
    116: 5529-5533, 1994; Garrett et al.,
    Protein Science 5: 204-211, 1996).
    Bacillus b-glucanse Hahn et al., Proc. Natl. Acad. Sci. U.S.A.
    91: 10417-10421, 1994).
    aspartate Yang & Schachman, Proc. Natl. Acad.
    transcarbamoylase
    Sci. U.S.A. 90: 11980-11984, 1993).
    phosphoribosyl Luger et al., Science 243: 206-210
    anthranilate (1989; Luger et al., Prot. Eng. Isomerase
    3: 249-258, 1990).
    pepsin/pepsinogen Lin et al., Protein Science 4: 159-166,
    1995).
    glyceraldehyde-3- Vignais et al., Protein Science
    phosphate dehydro- 4: 994-1000, 1995).
    genase
    ornithine Li & Coffino, Mol. Cell. Biol.
    decarboxylase 13: 2377-2383, 1993).
    yeast Ritco-Vonsovici et al., Biochemistry
    phosphoglycerate 34: 16543-16551, 1995).
    dehydrogenase
    Enzyme Inhibitor
    basic pancreatic Goldenberg & Creighton, J. Mol.
    trypsin inhibitor Biol. 165: 407-413, 1983).
    Cytokines
    interleukin-1b Horlick et al., Protein Eng. 5: 427-431,
    1992).
    interleukin-4 Kreitman et al., Cytokine 7: 311-318,
    1995).
    Tyrosine Kinase
    Recognition Domain
    a-spectrin SH3 Viguera, et al., J. Mol. Biol.
    domain 247: 670-681, 1995).
    Transmembrane Protein
    omp A Koebnik & Kramer, J. Mol. Biol.
    250: 617-626, 1995).
    Chimeric Protein
    interleukin-4- Kreitman et al., Proc. Natl. Acad.
    Pseudomonas Sci. U.S.A. 91: 6889-6893, 1994).
    exotoxin
  • The results of these studies have been highly variable. In many cases substantially lower activity, solubility or thermodynamic stability were observed ([0025] E. coli dihydrofolate reductase, aspartate transcarbamoylase, phosphoribosyl anthranilate isomerase, glyceraldehyde-3-phosphate dehydrogenase, ornithine decarboxylase, omp A, yeast phosphoglycerate dehydrogenase). In other cases, the sequence rearranged protein appeared to have many nearly identical properties as its natural counterpart (basic pancreatic trypsin inhibitor, T4 lysozyme, ribonuclease Tl, Bacillus b-glucanase, interleukin-1b, a-spectrin SH3 domain, pepsinogen, interleukin-4). In exceptional cases, an unexpected improvement over some properties of the natural sequence was observed, e.g., the solubility and refolding rate for rearranged a-spectrin SH3 domain sequences, and the receptor affinity and anti-tumor activity of transposed interleukin-4-Pseudomonas exotoxin fusion molecule (Kreitman et al., Proc. Natl. Acad. Sci. U.S.A. 91:6889-6893, 1994; Kreitman et al., Cancer Res. 55:3357-3363, 1995).
  • The primary motivation for these types of studies has been to study the role of short-range and long-range interactions in protein folding and stability. Sequence rearrangements of this type convert a subset of interactions that are long-range in the original sequence into short-range interactions in the new sequence, and vice versa. The fact that many of these sequence rearrangements are able to attain a conformation with at least some activity is persuasive evidence that protein folding occurs by multiple folding pathways (Viguera, et al., [0026] J. Mol. Biol. 247:670-681, 1995). In the case of the SH3 domain of a-spectrin, choosing new termini at locations that corresponded to b-hairpin turns resulted in proteins with slightly less stability, but which were nevertheless able to fold.
  • The positions of the internal breakpoints used in the studies cited here are found exclusively on the surface of proteins, and are distributed throughout the linear sequence without any obvious bias towards the ends or the middle (the variation in the relative distance from the original N-terminus to the breakpoint is ca. 10 to 80% of the total sequence length). The linkers connecting the original N- and C-termini in these studies have ranged from 0 to 9 residues. In one case (Yang & Schachman, [0027] Proc. Natl. Acad. Sci. U.S.A. 90:11980-11984, 1993), a portion of sequence has been deleted from the original C-terminal segment, and the connection made from the truncated C-terminus to the original N-terminus. Flexible hydrophilic residues such as Gly and Ser are frequently used in the linkers. Viguera, et al. (J. Mol. Biol. 247:670-681, 1995) compared joining the original N- and C-termini with 3- or 4-residue linkers; the 3-residue linker was less thermodynamically stable. Protasova et al. (Protein Eng. 7:1373-1377, 1994) used 3- or 5-residue linkers in connecting the original N-termini of E. coli dihydrofolate reductase; only the 3-residue linker produced protein in good yield.
    • BRIEF SUMMARY OF THE INVENTION
  • Novel hematopoietic proteins of this invention are represented by the formulas: [0028]
  • R1-L1-R2, R2-L1-R1, R1-R2, or R2-R1
  • wherein R[0029] 1 and R2 are independently selected from the group consisting of;
  • (I) A polypeptide comprising; a modified human G-CSF amino acid sequence of the formula: [0030]
    1
    Xaa Xaa Xaa Gly Pro Ala Ser Ser Leu (SEQ ID NO: 1)
    10
    Pro Gln Ser Xaa Leu Leu Xaa Xaa Xaa
        20
    Glu Gln Val Xaa Lys Xaa Gln Gly Xaa
            30
    Gly Ala Xaa Leu Gln Glu Xaa Leu Xaa
                40
    Ala Thr Tyr Lys Leu Xaa Xaa Xaa Glu
                    50
    Xaa Xaa Val Xaa Xaa Gly His Ser Xaa
                        60
    Gly Ile Pro Trp Ala Pro Leu Ser Ser
                            70
    Xaa Pro Ser Xaa Ala Leu Xaa Leu Ala
                                80
    Gly Xaa Leu Ser Gln Leu His Ser Gly
                                    90
    Leu Phe Leu Tyr Gln Gly Leu Leu Gln
    Ala Leu Glu Gly Ile Ser Pro Glu Leu
    100
    Gly Pro Thr Leu Xaa Thr Leu Gln Xaa
        110
    Asp Val Ala Asp Phe Ala Xaa Thr Ile
            120
    Trp Gln Gln Met Glu Xaa Xaa Gly Met
                130
    Ala Pro Ala Leu Gln Pro Thr Gln Gly
                    140
    Ala Met Pro Ala Phe Ala Ser Ala Xaa
                        150
    Gln Xaa Xaa Ala Gly Gly Val Leu Val
                            160
    Ala Ser Xaa Leu Gln Xaa Phe Leu Xaa
                                170
    Xaa Ser Tyr Arg Val Leu Xaa Xaa Leu
    Ala Gln Pro
  • wherein [0031]
  • Xaa at [0032] position 1 is Thr, Ser, Arg, Tyr or Gly;
  • Xaa at [0033] position 2 is Pro or Leu;
  • Xaa at [0034] position 3 is Leu, Arg, Tyr or Ser;
  • Xaa at position 13 is Phe, Ser, His, Thr or Pro; [0035]
  • Xaa at position 16 is Lys, Pro, Ser, Thr or His; [0036]
  • Xaa at position 17 is Cys, Ser, Gly, Ala, Ile, Tyr or Arg; [0037]
  • Xaa at position 18 is Leu, Thr, Pro, His, Ile or Cys; [0038]
  • Xaa at position 22 is Arg, Tyr, Ser, Thr or Ala; [0039]
  • Xaa at position 24 is Ile, Pro, Tyr or Leu; [0040]
  • Xaa at position 27 is Asp, or Gly; [0041]
  • Xaa at position 30 is Ala, Ile, Leu or Gly; [0042]
  • Xaa at position 34 is Lys or Ser; [0043]
  • Xaa at position 36 is Cys or Ser; [0044]
  • Xaa at position 42 is Cys or Ser; [0045]
  • Xaa at position 43 is His, Thr, Gly, Val, Lys, Trp, Ala, Arg, Cys, or Leu; [0046]
  • Xaa at position 44 is Pro, Gly, Arg, Asp, Val, Ala, His, Trp, Gln, or Thr; [0047]
  • Xaa at position 46 is Glu, Arg, Phe, Arg, Ile or Ala; [0048]
  • Xaa at position 47 is Leu or Thr; [0049]
  • Xaa at position 49 is Leu, Phe, Arg or Ser; [0050]
  • Xaa at position 50 is Leu, Ile, His, Pro or Tyr; [0051]
  • Xaa at position 54 is Leu or His; [0052]
  • Xaa at position 64 is Cys or Ser; [0053]
  • Xaa at position 67 is Gln, Lys, Leu or Cys; [0054]
  • Xaa at position 70 is Gln, Pro, Leu, Arg or Ser; [0055]
  • Xaa at position 74 is Cys or Ser; [0056]
  • Xaa at position 104 is Asp, Gly or Val; [0057]
  • Xaa at position 108 is Leu, Ala, Val, Arg, Trp, Gln or Gly; [0058]
  • Xaa at position 115 is Thr, His, Leu or Ala; [0059]
  • Xaa at position 120 is Gln, Gly, Arg, Lys or His [0060]
  • Xaa at position 123 is Glu, Arg, Phe or Thr [0061]
  • Xaa at position 144 is Phe, His, Arg, Pro, Leu, Gln or Glu; [0062]
  • Xaa at position 146 is Arg or Gln; [0063]
  • Xaa at position 147 is Arg or Gln; [0064]
  • Xaa at position 156 is His, Gly or Ser; [0065]
  • Xaa at position 159 is Ser, Arg, Thr, Tyr, Val or Gly; [0066]
  • Xaa at position 162 is Glu, Leu, Gly or Trp; [0067]
  • Xaa at position 163 is Val, Gly, Arg or Ala; [0068]
  • Xaa at position 169 is Arg, Ser, Leu, Arg or Cys; [0069]
  • Xaa at position 170 is His, Arg or Ser; [0070]
  • wherein optionally 1-11 amino acids from the N-terminus and 1-5 from the C-terminus can be deleted; and [0071]
  • wherein the N-terminus is joined to the C-terminus directly or through a linker capable of joining the N-terminus to the C-terminus and having new C- and N-termini at amino acids; [0072]
    38-39
    39-40
    40-41
    41-42
    42-43
    43-44
    45-46
    48-49
    49-50
    52-53
    53-54
    54-55
    55-56
    56-57
    57-58
    58-59
    59-60
    60-61
    61-62
    62-63
    63-64
    64-65
    65-66
    66-67
    67-68
    68-69
    69-70
    70-71
    71-72
    91-92
    92-93
    93-94
    94-95
    95-96
    96-97
    97-98
    98-99
     99-100
    123-124
    124-125
    125-126
    126-127
    128-129
    128-129
    129-130
    130-131
    131-132
    132-133
    133-134
    134-135
    135-136
    136-137
    137-138
    138-139
    139-140
    140-141
    141-142
    or 142-143;
  • (II) A polypeptide comprising; a modified hIL-3 amino acid sequence of the formula: [0073]
    Ala Pro Met Thr Gln Thr Thr Ser Leu (SEQ ID NO: 2)
    1               5
    Lys Thr Ser Trp Val Asn Cys Xaa Xaa
    10                  15
    Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa
        20                  25
    Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa
            30                  35
    Xaa Xaa Asn Xaa Xaa Xaa Xaa Xaa Xaa
                40                  45
    Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa
                    50
    Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa
    55                  60
    Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa
        65                  70
    Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa
            75                  80
    Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa
                85                  90
    Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa
                    95
    Xaa Xaa Xaa Xaa Xaa Xaa Xaa Phe Xaa
    100                 105
    Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa
        110                 115
    Xaa Xaa Xaa Xaa Xaa Xaa Gln Gln Thr
            120                 125
    Thr Leu Ser Leu Ala Ile Phe;
                130
  • wherein [0074]
  • Xaa at position 17 is Ser, Lys, Gly, Asp, Met, Gln, or Arg; [0075]
  • Xaa at position 18 is Asn, His, Leu, Ile, Phe, Arg, or Gln; [0076]
  • Xaa at position 19 is Met, Phe, Ile, Arg, Gly, Ala, or Cys; [0077]
  • Xaa at position 20 is Ile, Cys, Gln, Glu, Arg, Pro, or Ala; [0078]
  • Xaa at position 21 is Asp, Phe, Lys, Arg, Ala, Gly, Glu, Gln, Asn, Thr, Ser or Val; [0079]
  • Xaa at position 22 is Glu, Trp, Pro, Ser, Ala, His, Asp, Asn, Gln, Leu, Val or Gly; [0080]
  • Xaa at position 23 is Ile, Val, Ala, Gly, Trp, Lys, Phe, Leu, Ser, or Arg; [0081]
  • Xaa at position 24 is Ile, Gly, Val, Arg, Ser, Phe, or Leu; [0082]
  • Xaa at position 25 is Thr, His, Gly, Gln, Arg, Pro, or Ala; [0083]
  • Xaa at position 26 is His, Thr, Phe, Gly, Arg, Ala, or Trp; [0084]
  • Xaa at position 27 is Leu, Gly, Arg, Thr, Ser, or Ala; [0085]
  • Xaa at position 28 is Lys, Arg, Leu, Gln, Gly, Pro, Val or Trp; [0086]
  • Xaa at position 29 is Gln, Asn, Leu, Pro, Arg, or Val; [0087]
  • Xaa at position 30 is Pro, His, Thr, Gly, Asp, Gln, Ser, Leu, or Lys; [0088]
  • Xaa at position 31 is Pro, Asp, Gly, Ala, Arg, Leu, or Gln; [0089]
  • Xaa at position 32 is Leu, Val, Arg, Gln, Asn, Gly, Ala, or Glu; [0090]
  • Xaa at position 33 is Pro, Leu, Gln, Ala, Thr, or Glu; [0091]
  • Xaa at position 34 is Leu, Val, Gly, Ser, Lys, Glu, Gln, Thr, Arg, Ala, Phe, Ile or Met; [0092]
  • Xaa at position 35 is Leu, Ala, Gly, Asn, Pro, Gln, or Val; [0093]
  • Xaa at position 36 is Asp, Leu, or Val; [0094]
  • Xaa at position 37 is Phe, Ser, Pro, Trp, or Ile; [0095]
  • Xaa at position 38 is Asn, or Ala; [0096]
  • Xaa at position 40 is Leu, Trp, or Arg; [0097]
  • Xaa at position 41 is Asn, Cys, Arg, Leu, His, Met, or Pro; [0098]
  • Xaa at position 42 is Gly, Asp, Ser, Cys, Asn, Lys, Thr, Leu, Val, Glu, Phe, Tyr, Ile, Met or Ala; [0099]
  • Xaa at position 43 is Glu, Asn, Tyr, Leu, Phe, Asp, Ala, Cys, Gln, Arg, Thr, Gly or Ser; [0100]
  • Xaa at position 44 is Asp, Ser, Leu, Arg, Lys, Thr, Met, Trp, Glu, Asn, Gln, Ala or Pro; [0101]
  • Xaa at position 45 is Gln, Pro, Phe, Val, Met, Leu, Thr, Lys, Trp, Asp, Asn, Arg, Ser, Ala, Ile, Glu or His; [0102]
  • Xaa at position 46 is Asp, Phe, Ser, Thr, Cys, Glu, Asn, Gln, Lys, His, Ala, Tyr, Ile, Val or Gly; [0103]
  • Xaa at position 47 is Ile, Gly, Val, Ser, Arg, Pro, or His; [0104]
  • Xaa at position 48 is Leu, Ser, Cys, Arg, Ile, His, Phe, Glu, Lys, Thr, Ala, Met, Val or Asn; [0105]
  • Xaa at position 49 is Met, Arg, Ala, Gly, Pro, Asn, His, or Asp; [0106]
  • Xaa at position 50 is Glu, Leu, Thr, Asp, Tyr, Lys, Asn, Ser, Ala, Ile, Val, His, Phe, Met or Gln; [0107]
  • Xaa at position 51 is Asn, Arg, Met, Pro, Ser, Thr, or His; [0108]
  • Xaa at position 52 is Asn, His, Arg, Leu, Gly, Ser, or Thr; [0109]
  • Xaa at position 53 is Leu, Thr, Ala, Gly, Glu, Pro, Lys, Ser, or Met; [0110]
  • Xaa at position 54 is Arg, Asp, Ile, Ser, Val, Thr, Gln, Asn, Lys, His, Ala or Leu; [0111]
  • Xaa at position 55 is Arg, Thr, Val, Ser, Leu, or Gly; [0112]
  • Xaa at position 56 is Pro, Gly, Cys, Ser, Gln, Glu, Arg, His, Thr, Ala, Tyr, Phe, Leu, Val or Lys; [0113]
  • Xaa at position 57 is Asn or Gly; [0114]
  • Xaa at position 58 is Leu, Ser, Asp, Arg, Gln, Val, or Cys; [0115]
  • Xaa at position 59 is Glu Tyr, His, Leu, Pro, or Arg; [0116]
  • Xaa at position 60 is Ala, Ser, Pro, Tyr, Asn, or Thr; [0117]
  • Xaa at position 61 is Phe, Asn, Glu, Pro, Lys, Arg, or Ser; [0118]
  • Xaa at position 62 is Asn, His, Val, Arg, Pro, Thr, Asp, or Ile; [0119]
  • Xaa at position 63 is Arg, Tyr, Trp, Lys, Ser, His, Pro, or Val; [0120]
  • Xaa at position 64 is Ala, Asn, Pro, Ser, or Lys; [0121]
  • Xaa at position 65 is Val, Thr, Pro, His, Leu, Phe, or Ser; [0122]
  • Xaa at position 66 is Lys, Ile, Arg, Val, Asn, Glu, or Ser; [0123]
  • Xaa at position 67 is Ser, Ala, Phe, Val, Gly, Asn, Ile, Pro, or His; [0124]
  • Xaa at position 68 is Leu, Val, Trp, Ser, Ile, Phe, Thr, or His; [0125]
  • Xaa at position 69 is Gln, Ala, Pro, Thr, Glu, Arg, Trp, Gly, or Leu; [0126]
  • Xaa at position 70 is Asn, Leu, Val, Trp, Pro, or Ala; [0127]
  • Xaa at position 71 is Ala, Met, Leu, Pro, Arg, Glu, Thr, Gln, Trp, or Asn; [0128]
  • Xaa at position 72 is Ser, Glu, Met, Ala, His, Asn, Arg, or Asp; [0129]
  • Xaa at position 73 is Ala, Glu, Asp, Leu, Ser, Gly, Thr, or Arg; [0130]
  • Xaa at position 74 is Ile, Met, Thr, Pro, Arg, Gly, Ala; [0131]
  • Xaa at position 75 is Glu, Lys, Gly, Asp, Pro, Trp, Arg, Ser, Gln, or Leu; [0132]
  • Xaa at position 76 is Ser, Val, Ala, Asn, Trp, Glu, Pro, Gly, or Asp; [0133]
  • Xaa at position 77 is Ile, Ser, Arg, Thr, or Leu; [0134]
  • Xaa at position 78 is Leu, Ala, Ser, Glu, Phe, Gly, or Arg; [0135]
  • Xaa at position 79 is Lys, Thr, Asn, Met, Arg, Ile, Gly, or Asp; [0136]
  • Xaa at position 80 is Asn, Trp, Val, Gly, Thr, Leu, Glu, or Arg; [0137]
  • Xaa at position 81 is Leu, Gln, Gly, Ala, Trp, Arg, Val, or Lys; [0138]
  • Xaa at position 82 is Leu, Gln, Lys, Trp, Arg, Asp, Glu, Asn, His, Thr, Ser, Ala, Tyr, Phe, Ile, Met or Val; [0139]
  • Xaa at position 83 is Pro, Ala, Thr, Trp, Arg, or Met; [0140]
  • Xaa at position 84 is Cys, Glu, Gly, Arg, Met, or Val; [0141]
  • Xaa at position 85 is Leu, Asn, Val, or Gln; [0142]
  • Xaa at position 86 is Pro, Cys, Arg, Ala, or Lys; [0143]
  • Xaa at position 87 is Leu, Ser, Trp, or Gly; [0144]
  • Xaa at position 88 is Ala, Lys, Arg, Val, or Trp; [0145]
  • Xaa at position 89 is Thr, Asp, Cys, Leu, Val, Glu, His, Asn, or Ser; [0146]
  • Xaa at position 90 is Ala, Pro, Ser, Thr, Gly, Asp, Ile, or Met; [0147]
  • Xaa at position 91 is Ala, Pro, Ser, Thr, Phe, Leu, Asp, or His; [0148]
  • Xaa at position 92 is Pro, Phe, Arg, Ser, Lys, His, Ala, Gly, Ile or Leu; [0149]
  • Xaa at position 93 is Thr, Asp, Ser, Asn, Pro, Ala, Leu, or Arg; [0150]
  • Xaa at position 94 is Arg, Ile, Ser, Glu, Leu, Val, Gln, Lys, His, Ala, or Pro; [0151]
  • Xaa at position 95 is His, Gln, Pro, Arg, Val, Leu, Gly, Thr, Asn, Lys, Ser, Ala, Trp, Phe, Ile, or Tyr; [0152]
  • Xaa at [0153] position 96 is Pro, Lys, Tyr, Gly, Ile, or Thr;
  • Xaa at [0154] position 97 is Ile, Val, Lys, Ala, or Asn;
  • Xaa at position 98 is His, Ile, Asn, Leu, Asp, Ala, Thr, Glu, Gln, Ser, Phe, Met, Val, Lys, Arg, Tyr or Pro; [0155]
  • Xaa at position 99 is Ile, Leu, Arg, Asp, Val, Pro, Gln, Gly, Ser, Phe, or His; [0156]
  • Xaa at position 100 is Lys, Tyr, Leu, His, Arg, Ile, Ser, Gln, or Pro; [0157]
  • Xaa at position 101 is Asp, Pro, Met, Lys, His, Thr, Val, Tyr, Glu, Asn, Ser, Ala, Gly, Ile, Leu, or Gln; [0158]
  • Xaa at position 102 is Gly, Leu, Glu, Lys, Ser, Tyr, or Pro; [0159]
  • Xaa at position 103 is Asp, or Ser; [0160]
  • Xaa at position 104 is Trp, Val, Cys, Tyr, Thr, Met, Pro, Leu, Gln, Lys, Ala, Phe, or Gly; [0161]
  • Xaa at position 105 is Asn, Pro, Ala, Phe, Ser, Trp, Gln, Tyr, Leu, Lys, Ile, Asp, or His; [0162]
  • Xaa at position 106 is Glu, Ser, Ala, Lys, Thr, Ile, Gly, or Pro; [0163]
  • Xaa at position 108 is Arg, Lys, Asp, Leu, Thr, Ile, Gln, His, Ser, Ala or Pro; [0164]
  • Xaa at position 109 is Arg, Thr, Pro, Glu, Tyr, Leu, Ser, or Gly; [0165]
  • Xaa at position 110 is Lys, Ala, Asn, Thr, Leu, Arg, Gln, His, Glu, Ser, or Trp; [0166]
  • Xaa at position 111 is Leu, Ile, Arg, Asp, or Met; [0167]
  • Xaa at position 112 is Thr, Val, Gln, Tyr, Glu, His, Ser, or Phe; [0168]
  • Xaa at position 113 is Phe, Ser, Cys, His, Gly, Trp, Tyr, Asp, Lys, Leu, Ile, Val or Asn; [0169]
  • Xaa at position 114 is Tyr, Cys, His, Ser, Trp, Arg, or Leu; [0170]
  • Xaa at position 115 is Leu, Asn, Val, Pro, Arg, Ala, His, Thr, Trp, or Met; [0171]
  • Xaa at position 116 is Lys, Leu, Pro, Thr, Met, Asp, Val, Glu, Arg, Trp, Ser, Asn, His, Ala, Tyr, Phe, Gln, or Ile; [0172]
  • Xaa at position 117 is Thr, Ser, Asn, Ile, Trp, Lys, or Pro; [0173]
  • Xaa at position 118 is Leu, Ser, Pro, Ala, Glu, Cys, Asp, or Tyr; [0174]
  • Xaa at position 119 is Glu, Ser, Lys, Pro, Leu, Thr, Tyr, or Arg; [0175]
  • Xaa at position 120 is Asn, Ala, Pro, Leu, His, Val, or Gln; [0176]
  • Xaa at position 121 is Ala, Ser, Ile, Asn, Pro, Lys, Asp, or Gly; [0177]
  • Xaa at position 122 is Gln, Ser, Met, Trp, Arg, Phe, Pro, His, Ile, Tyr, or Cys; [0178]
  • Xaa at position 123 is Ala, Met, Glu, His, Ser, Pro, Tyr, or Leu; [0179]
  • wherein optionally from 1 to 14 amino acids can be deleted from the N-terminus and/or from 1 to 15 amino acids can be deleted from the C-terminus; and wherein from 0 to 44 of the amino acids designated by Xaa are different from the corresponding amino acids of native (1-133) human interleukin-3; and [0180]
  • wherein the N-terminus is joined to the C-terminus directly or through a linker (L[0181] 2) capable of joining the N-terminus to the C-terminus and having new C- and N-termini at amino acids;
    26-27
    27-28
    28-29
    29-30
    30-31
    31-32
    32-33
    33-34
    34-35
    35-36
    36-37
    37-38
    38-39
    39-40
    40-41
    41-42
    49-50
    50-51
    51-52
    52-53
    53-54
    54-55
    64-65
    65-66
    66-67
    67-68
    68-69
    69-70
    70-71
    71-72
    72-73
    82-83
    83-84
    84-85
    85-86
    86-87
    87-88
    88-89
    89-90
    90-91
    91-92
    92-93
    97-98
    98-99
     99-100
    100-101
    101-102
    102-103
    or 103-104;
  • or [0182]
  • (III) A polypeptide comprising; a modified human c-mpl ligand amino acid sequence of the formula: [0183]
    SerProAlaProProAlaCysAspLeuArgValLeu (SEQ ID NO: 3)
    1           5              10
    SerLysLeuLeuArgAspSerHisValLeuHisSer
          15             20
    ArgLeuSerGlnCysProGluValHisProLeuPro
    25             30             35
    ThrProValLeuLeuProAlaValAspPheSerLeu
             40             45
    GlyGluTrpLysThrGlnMetGluGluThrLysAla
       50             55             60
    GlnAspIleLeuGlyAlaValThrLeuLeuLeuGlu
                65             70
    GlyValMetAlaAlaArgGlyGlnLeuGlyProThr
          75             80
    CysLeuSerSerLeuLeuGlyGlnLeuSerGlyGln
    85             90             95
    ValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeu
             100            105
    GlyThrGlnXaaXaaXaaXaaGlyArgThrThrAla
       110            115            120
    HisLysAspProAsnAlaIlePheLeuSerPheGln
                125            130
    HisLeuLeuArgGlyLysValArgPheLeuMetLeu
          135            140
    ValGlyGlySerThrLeuCysValArgArgAlaPro
    145         150               155
    ProThrThrAlaValProSerArgThrSerLeuVal
             160            165
    LeuThrLeuAsnGluLeuProAsnArgThrSerGly
       170            175            180
    LeuLeuGluThrAsnPheThrAlaSerAlaArgThr
                185            190
    ThrGlySerGlyLeuLeuLysTrpGlnGlnGlyPhe
          195            200
    ArgAlaLysIleProGlyLeuLeuAsnGlnThrSer
    205            210            215
    ArgSerLeuAspGlnIleProGlyTyrLeuAsnArg
             220            225
    IleHisGluLeuLeuAsnGlyThrArgGlyLeuPhe
       230            235            240
    ProGlyProSerArgArgThrLeuGlyAlaProAsp
                245            250
    IleSerSerGlyThrSerAspThrGlySerLeuPro
          255            260
    ProAsnLeuGlnProGlyTyrSerProSerProThr
    265            270            275
    HisProProThrGlyGlnTyrThrLeuPheProLeu
             280            285
    ProProThrLeuProThrProValValGlnLeuHis
       290            295            300
    ProLeuLeuProAspProSerAlaProThrProThr
                305            310
    ProThrSerProLeuLeuAsnThrSerTyrThrHis
          315            320
    SerGlnAsnLeuSerGlnGluGly
    325            330   332
    153
  • wherein; [0184]
  • Xaa at position 112 is deleted or Leu, Ala, Val, Ile, Pro, Phe, Trp, or Met; [0185]
  • Xaa at position 113 is deleted or Pro, Phe, Ala, Val, Leu, Ile, Trp, or Met; [0186]
  • Xaa at position 114 is deleted or Pro, Phe, Ala, Val, Leu, Ile, Trp, or Met; [0187]
  • Xaa at position 115 is deleted or Gln, Gly, Ser, Thr, Tyr, or Asn; and [0188]
  • wherein the N-terminus is joined to the C-terminus directly or through a linker (L[0189] 2) capable of joining the N-terminus to the C-terminus and having new C- and N-termini at amino acids;
    26-27
    27-28
    28-29
    29-30
    30-31
    32-33
    33-34
    34-35
    36-37
    37-38
    38-39
    40-41
    41-42
    42-43
    43-44
    44-45
    46-47
    47-48
    48-49
    50-51
    51-52
    52-53
    53-54
    54-55
    55-56
    56-57
    57-58
    58-59
    59-60
    78-79
    79-80
    80-81
    81-82
    82-83
    83-84
    84-85
    85-86
    86-87
    87-88
    88-89
    108-109
    109-110
    110-111
    111-112
    112-113
    113-114
    114-115
    115-116
    116-117
    117-118
    118-119
    119-120
    120-121
    121-122
    122-123
    123-124
    124-125
    125-126
    126-127
    or 127-128;
  • or [0190]
  • (IV) A polypeptide comprising; a modified hIL-3 amino acid sequence of the formula: [0191]
    Ala Pro Met Thr Gln Thr Thr Ser Leu (SEQ ID NO: 2)
    1               5
    Lys Thr Ser Trp Val Asn Cys Xaa Xaa
    10                  15
    Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa
        20                  25
    Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa
            30                  35
    Xaa Xaa Asn Xaa Xaa Xaa Xaa Xaa Xaa
                40                  45
    Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa
                    50
    Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa
    55                  60
    Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa
        65                  70
    Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa
            75                  80
    Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa
                85                  90
    Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa
                    95
    Xaa Xaa Xaa Xaa Xaa Xaa Xaa Phe Xaa
    100                 105
    Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa
        110                 115
    Xaa Xaa Xaa Xaa Xaa Xaa Gln Gln Thr
            120                 125
    Thr Leu Ser Leu Ala Ile Phe
                130
  • wherein [0192]
  • Xaa at position 17 is Ser, Lys, Gly, Asp, Met, Gln, or Arg; [0193]
  • Xaa at position 18 is Asn, His, Leu, Ile, Phe, Arg, or Gln; [0194]
  • Xaa at position 19 is Met, Phe, Ile, Arg, Gly, Ala, or Cys; [0195]
  • Xaa at position 20 is Ile, Cys, Gln, Glu, Arg, Pro, or Ala; [0196]
  • Xaa at position 21 is Asp, Phe, Lys, Arg, Ala, Gly, Glu, Gln, Asn, Thr, Ser or Val; [0197]
  • Xaa at position 22 is Glu, Trp, Pro, Ser, Ala, His, Asp, Asn, Gln, Leu, Val or Gly; [0198]
  • Xaa at position 23 is Ile, Val, Ala, Gly, Trp, Lys, Phe, Leu, Ser, or Arg; [0199]
  • Xaa at position 24 is Ile, Gly, Val, Arg, Ser, Phe, or Leu; [0200]
  • Xaa at position 25 is Thr, His, Gly, Gln, Arg, Pro, or Ala; [0201]
  • Xaa at position 26 is His, Thr, Phe, Gly, Arg, Ala, or Trp; [0202]
  • Xaa at position 27 is Leu, Gly, Arg, Thr, Ser, or Ala; [0203]
  • Xaa at position 28 is Lys, Arg, Leu, Gln, Gly, Pro, Val or Trp; [0204]
  • Xaa at position 29 is Gln, Asn, Leu, Pro, Arg, or Val; [0205]
  • Xaa at position 30 is Pro, His, Thr, Gly, Asp, Gln, Ser, Leu, or Lys; [0206]
  • Xaa at position 31 is Pro, Asp, Gly, Ala, Arg, Leu, or Gln; [0207]
  • Xaa at position 32 is Leu, Val, Arg, Gln, Asn, Gly, Ala, or Glu; [0208]
  • Xaa at position 33 is Pro, Leu, Gln, Ala, Thr, or Glu; [0209]
  • Xaa at position 34 is Leu, Val, Gly, Ser, Lys, Glu, Gln, Thr, Arg, Ala, Phe, Ile or Met; [0210]
  • Xaa at position 35 is Leu, Ala, Gly, Asn, Pro, Gln, or Val; [0211]
  • Xaa at position 36 is Asp, Leu, or Val; [0212]
  • Xaa at position 37 is Phe, Ser, Pro, Trp, or Ile; [0213]
  • Xaa at position 38 is Asn, or Ala; [0214]
  • Xaa at position 40 is Leu, Trp, or Arg; [0215]
  • Xaa at position 41 is Asn, Cys, Arg, Leu, His, Met, or Pro; [0216]
  • Xaa at position 42 is Gly, Asp, Ser, Cys, Asn, Lys, Thr, Leu, Val, Glu, Phe, Tyr, Ile, Met or Ala; [0217]
  • Xaa at position 43 is Glu, Asn, Tyr, Leu, Phe, Asp, Ala, Cys, Gln, Arg, Thr, Gly or Ser; [0218]
  • Xaa at position 44 is Asp, Ser, Leu, Arg, Lys, Thr, Met, Trp, Glu, Asn, Gln, Ala or Pro; [0219]
  • Xaa at position 45 is Gln, Pro, Phe, Val, Met, Leu, Thr, Lys, Trp, Asp, Asn, Arg, Ser, Ala, Ile, Glu or His; [0220]
  • Xaa at position 46 is Asp, Phe, Ser, Thr, Cys, Glu, Asn, Gln, Lys, His, Ala, Tyr, Ile, Val or Gly; [0221]
  • Xaa at position 47 is Ile, Gly, Val, Ser, Arg, Pro, or His; [0222]
  • Xaa at position 48 is Leu, Ser, Cys, Arg, Ile, His, Phe, Glu, Lys, Thr, Ala, Met, Val or Asn; [0223]
  • Xaa at position 49 is Met, Arg, Ala, Gly, Pro, Asn, His, or Asp; [0224]
  • Xaa at position 50 is Glu, Leu, Thr, Asp, Tyr, Lys, Asn, Ser, Ala, Ile, Val, His, Phe, Met or Gln; [0225]
  • Xaa at position 51 is Asn, Arg, Met, Pro, Ser, Thr, or His; [0226]
  • Xaa at position 52 is Asn, His, Arg, Leu, Gly, Ser, or Thr; [0227]
  • Xaa at position 53 is Leu, Thr, Ala, Gly, Glu, Pro, Lys, Ser, or Met; [0228]
  • Xaa at position 54 is Arg, Asp, Ile, Ser, Val, Thr, Gln, Asn, Lys, His, Ala or Leu; [0229]
  • Xaa at position 55 is Arg, Thr, Val, Ser, Leu, or Gly; [0230]
  • Xaa at position 56 is Pro, Gly, Cys, Ser, Gln, Glu, Arg, His, Thr, Ala, Tyr, Phe, Leu, Val or Lys; [0231]
  • Xaa at position 57 is Asn or Gly; [0232]
  • Xaa at position 58 is Leu, Ser, Asp, Arg, Gln, Val, or Cys; [0233]
  • Xaa at position 59 is Glu Tyr, His, Leu, Pro, or Arg; [0234]
  • Xaa at position 60 is Ala, Ser, Pro, Tyr, Asn, or Thr; [0235]
  • Xaa at position 61 is Phe, Asn, Glu, Pro, Lys, Arg, or Ser; [0236]
  • Xaa at position 62 is Asn, His, Val, Arg, Pro, Thr, Asp, or Ile; [0237]
  • Xaa at position 63 is Arg, Tyr, Trp, Lys, Ser, His, Pro, or Val; [0238]
  • Xaa at position 64 is Ala, Asn, Pro, Ser, or Lys; [0239]
  • Xaa at position 65 is Val, Thr, Pro, His, Leu, Phe, or Ser; [0240]
  • Xaa at position 66 is Lys, Ile, Arg, Val, Asn, Glu, or Ser; [0241]
  • Xaa at position 67 is Ser, Ala, Phe, Val, Gly, Asn, Ile, Pro, or His; [0242]
  • Xaa at position 68 is Leu, Val, Trp, Ser, Ile, Phe, Thr, or His; [0243]
  • Xaa at position 69 is Gln, Ala, Pro, Thr, Glu, Arg, Trp, Gly, or Leu; [0244]
  • Xaa at position 70 is Asn, Leu, Val, Trp, Pro, or Ala; [0245]
  • Xaa at position 71 is Ala, Met, Leu, Pro, Arg, Glu, Thr, Gln, Trp, or Asn; [0246]
  • Xaa at position 72 is Ser, Glu, Met, Ala, His, Asn, Arg, or Asp; [0247]
  • Xaa at position 73 is Ala, Glu, Asp, Leu, Ser, Gly, Thr, or Arg; [0248]
  • Xaa at position 74 is Ile, Met, Thr, Pro, Arg, Gly, Ala; [0249]
  • Xaa at position 75 is Glu, Lys, Gly, Asp, Pro, Trp, Arg, Ser, Gln, or Leu; [0250]
  • Xaa at position 76 is Ser, Val, Ala, Asn, Trp, Glu, Pro, Gly, or Asp; [0251]
  • Xaa at position 77 is Ile, Ser, Arg, Thr, or Leu; [0252]
  • Xaa at position 78 is Leu, Ala, Ser, Glu, Phe, Gly, or Arg; [0253]
  • Xaa at position 79 is Lys, Thr, Asn, Met, Arg, Ile, Gly, or Asp; [0254]
  • Xaa at position 80 is Asn, Trp, Val, Gly, Thr, Leu, Glu, or Arg; [0255]
  • Xaa at position 81 is Leu, Gln, Gly, Ala, Trp, Arg, Val, or Lys; [0256]
  • Xaa at position 82 is Leu, Gln, Lys, Trp, Arg, Asp, Glu, Asn, His, Thr, Ser, Ala, Tyr, Phe, Ile, Met or Val; [0257]
  • Xaa at position 83 is Pro, Ala, Thr, Trp, Arg, or Met; [0258]
  • Xaa at position 84 is Cys, Glu, Gly, Arg, Met, or Val; [0259]
  • Xaa at position 85 is Leu, Asn, Val, or Gln; [0260]
  • Xaa at position 86 is Pro, Cys, Arg, Ala, or Lys; [0261]
  • Xaa at position 87 is Leu, Ser, Trp, or Gly; [0262]
  • Xaa at position 88 is Ala, Lys, Arg, Val, or Trp; [0263]
  • Xaa at position 89 is Thr, Asp, Cys, Leu, Val, Glu, His, Asn, or Ser; [0264]
  • Xaa at position 90 is Ala, Pro, Ser, Thr, Gly, Asp, Ile, or Met; [0265]
  • Xaa at position 91 is Ala, Pro, Ser, Thr, Phe, Leu, Asp, or His; [0266]
  • Xaa at position 92 is Pro, Phe, Arg, Ser, Lys, His, Ala, Gly, Ile or Leu; [0267]
  • Xaa at position 93 is Thr, Asp, Ser, Asn, Pro, Ala, Leu, or Arg; [0268]
  • Xaa at position 94 is Arg, Ile, Ser, Glu, Leu, Val, Gln, Lys, His, Ala, or Pro; [0269]
  • Xaa at position 95 is His, Gln, Pro, Arg, Val, Leu, Gly, Thr, Asn, Lys, Ser, Ala, Trp, Phe, Ile, or Tyr; [0270]
  • Xaa at [0271] position 96 is Pro, Lys, Tyr, Gly, Ile, or Thr;
  • Xaa at [0272] position 97 is Ile, Val, Lys, Ala, or Asn;
  • Xaa at position 98 is His, Ile, Asn, Leu, Asp, Ala, Thr, Glu, Gln, Ser, Phe, Met, Val, Lys, Arg, Tyr or Pro; [0273]
  • Xaa at position 99 is Ile, Leu, Arg, Asp, Val, Pro, Gln, Gly, Ser, Phe, or His; [0274]
  • Xaa at position 100 is Lys, Tyr, Leu, His, Arg, Ile, Ser, Gln, or Pro; [0275]
  • Xaa at position 101 is Asp, Pro, Met, Lys, His, Thr, Val, Tyr, Glu, Asn, Ser, Ala, Gly, Ile, Leu, or Gln; [0276]
  • Xaa at position 102 is Gly, Leu, Glu, Lys, Ser, Tyr, or Pro; [0277]
  • Xaa at position 103 is Asp, or Ser; [0278]
  • Xaa at position 104 is Trp, Val, Cys, Tyr, Thr, Met, Pro, Leu, Gln, Lys, Ala, Phe, or Gly; [0279]
  • Xaa at position 105 is Asn, Pro, Ala, Phe, Ser, Trp, Gln, Tyr, Leu, Lys, Ile, Asp, or His; [0280]
  • Xaa at position 106 is Glu, Ser, Ala, Lys, Thr, Ile, Gly, or Pro; [0281]
  • Xaa at position 108 is Arg, Lys, Asp, Leu, Thr, Ile, Gln, His, Ser, Ala or Pro; [0282]
  • Xaa at position 109 is Arg, Thr, Pro, Glu, Tyr, Leu, Ser, or Gly; [0283]
  • Xaa at position 110 is Lys, Ala, Asn, Thr, Leu, Arg, Gln, His, Glu, Ser, or Trp; [0284]
  • Xaa at position 111 is Leu, Ile, Arg, Asp, or Met; [0285]
  • Xaa at position 112 is Thr, Val, Gln, Tyr, Glu, His, Ser, or Phe; [0286]
  • Xaa at position 113 is Phe, Ser, Cys, His, Gly, Trp, Tyr, Asp, Lys, Leu, Ile, Val or Asn; [0287]
  • Xaa at position 114 is Tyr, Cys, His, Ser, Trp, Arg, or Leu; [0288]
  • Xaa at position 115 is Leu, Asn, Val, Pro, Arg, Ala, His, Thr, Trp, or Met; [0289]
  • Xaa at position 116 is Lys, Leu, Pro, Thr, Met, Asp, Val, Glu, Arg, Trp, Ser, Asn, His, Ala, Tyr, Phe, Gln, or Ile; [0290]
  • Xaa at position 117 is Thr, Ser, Asn, Ile, Trp, Lys, or Pro; [0291]
  • Xaa at position 118 is Leu, Ser, Pro, Ala, Glu, Cys, Asp, or Tyr; [0292]
  • Xaa at position 119 is Glu, Ser, Lys, Pro, Leu, Thr, Tyr, or Arg; [0293]
  • Xaa at position 120 is Asn, Ala, Pro, Leu, His, Val, or Gln; [0294]
  • Xaa at position 121 is Ala, Ser, Ile, Asn, Pro, Lys, Asp, or Gly; [0295]
  • Xaa at position 122 is Gln, Ser, Met, Trp, Arg, Phe, Pro, His, Ile, Tyr, or Cys; [0296]
  • Xaa at position 123 is Ala, Met, Glu, His, Ser, Pro, Tyr, or Leu; [0297]
  • wherein optionally from 1 to 14 amino acids can be deleted from the N-terminus and/or from 1 to 15 amino acids can be deleted from the C-terminus; and wherein from 1 to 44 of the amino acids designated by Xaa are different from the corresponding amino acids of native (1-133) human interleukin-3; [0298]
  • or [0299]
  • (V) a colony stimulating factor; and wherein L[0300] 1 is a linker capable of linking R1 to R2;
  • with the proviso that at least R[0301] 1 or R2 is selected from the polypeptide of formula (I), (II), or (III); and
  • said hematopoietic protein can optionally be immediately preceded by (methionine[0302] −1), (alanine−1) or (methionine−2, alanine−1).
  • The more preferred breakpoints at which new C-terminus and N-terminus can be made in the polypeptide (I) above are; 38-39, 39-40, 40-41, 41-42, 48-49, 53-54, 54-55, 55-56, 56-57, 57-58, 58-59, 59-60, 60-61, 61-62, 62-63, 64-65, 65-66, 66-67, 67-68, 68-69, 69-70, 96-97, 125-126, 126-127, 127-128, 128-129, 129-130, 130-131, 131-132, 132-133, 133-134, 134-135, 135-136, 136-137, 137-138, 138-139, 139-140, 140-141 and 141-142. [0303]
  • The most preferred breakpoints at which new C-terminus and N-terminus can be made in the polypeptide (I) above are; 38-39, 48-49, 96-97, 125-126, 132-133 and 141-142. [0304]
  • The more preferred breakpoints at which new C-terminus and N-terminus can be made in the polypeptide (II) above are; 28-29, 29-30, 30-31, 31-32, 32-33, 33-34, 34-35, 35-36, 36-37, 37-38, 38-39, 39-40, 66-67, 67-68, 68-69, 69-70, 70-71, 84-85, 85-86, 86-87, 87-88, 88-89, 89-90, 90-91, 98-99, 99-100, 100-101 and 101-102. [0305]
  • The most preferred breakpoints at which new C-terminus and N-terminus can be made in the polypeptide (II) above are; 34-35, 69-70 and 90-91. [0306]
  • The more preferred breakpoints at which new C-terminus and N-terminus can be made in the polypeptide (III) above or the amino acid sequence of (SEQ ID NO:256) are; 80-81, 81-82, 82-83, 83-84, 84-85, 85-86, 86-87, 108-109, 109-110, 110-111, 111-112, 112-113, 113-114, 114-115, 115-116, 116-117, 117-118, 118-119, 119-120, 120-121, 121-122, 122-123, 123-124, 124-125, 125-126 and 126-127. [0307]
  • The most preferred breakpoints at which new C-terminus and N-terminus can be made in the polypeptide (III) above or the amino acid sequence of (SEQ ID NO:256) are; 81-82, 108-109, 115-116, 119-120, 122-123 and 125-126. [0308]
  • The invention is also intended to include multifunctional receptor agoinist which comprises a sequence rearranged c-mpl receptor agonist in which the cysteine at position 7 and/or 151 are substituted with another amino acid. Preferably, the substitution at position 7 and 151 is Ser, Ala, Gly, His, Asn, Asp, Thr, Phe or Thr. More preferably, the substitution at position 7 and 151 is Ser, Ala, Gly, His or Asn. [0309]
  • The multifunctional receptor agonist of the present invention can also be represented by the following formula: [0310]
  • (T1)a-(L1)b-X1(L)c-X2-(L2)d-(T2)e X1-(L)c-X2-(L)-yl-(L)c-Y2
  • in which: [0311]
  • X[0312] 1 is a peptide comprising an amino acid sequence corresponding to the sequence of residues n+1 through J of the original protein having amino acids residues numbered sequentially 1 through J with an amino terminus at residue 1;
  • L is an optional linker; [0313]
  • X[0314] 2 is a peptide comprising an amino acid sequence of residues 1 through n of the original protein;
  • Y[0315] 1 is a peptide comprising an amino acid sequence corresponding to the sequence of residues n=1 through K of the original protein having amino acids residues numbered sequentially 1 through K with an amino terminus at residue 1;
  • Y[0316] 2 is a peptide comprising an amino acid sequence of residues 1 through n of the original protein;
  • L[0317] 1 and L2 are optional peptide spacers:
  • n is an integer ranging from 1 to J-1; [0318]
  • b, c, and d are each independently 0 or 1; [0319]
  • a and e are either 0 or 1, provided that both a and e cannot both be 0; and [0320]
  • T[0321] 1 and T2 are proteins.
  • Additionally, the present invention relates to recombinant expression vectors comprising nucleotide sequences encoding the multi-functional hematopoietic receptor agonists, related microbial expression systems, and processes for making the multi-functional hematopoietic receptor agonists. The invention also relates to pharmaceutical compositions containing the multi-functional hematopoietic receptor agonists, and methods for using the multi-functional hematopoietic receptor agonists. [0322]
  • In addition to the use of the multi-functional hematopoietic receptor agonists of the present invention in vivo, it is envisioned that in vitro uses would include the ability to stimulate bone marrow and blood cell activation and growth before infusion into patients. [0323]
    • BRIEF DESCRIPTION OF THE FIGURES
  • FIG. 1 schematically illustrates the sequence rearrangement of a protein. The N-terminus (N) and the C-terminus (C) of the native protein are joined through a linker, or joined directly. The protein is opened at a breakpoint creating a new N-terminus (new N) and a new C-terminus (new-C) resulting in a protein with a new linear amino acid sequence. A rearranged molecule may be synthesized de novo as linear molecule and not go through the steps of joining the original N-terminus and the C-terminus and opening of the protein at the breakpoint. [0324]
  • FIG. 2 shows a schematic of Method I, for creating new proteins in which the original N-terminus and C-terminus of the native protein are joined with a linker and different N-terminus and C-terminus of the protein are created. In the example shown the sequence rearrangement results in a new gene encoding a protein with a new N-terminus created at [0325] amino acid 97 of the original protein, the original C-terminus (a.a. 174) joined to the amino acid 11 (a.a. 1-10 are deleted) through a linker region and a new C-terminus created at amino acid 96 of the original sequence.
  • FIG. 3 shows a schematic of Method II, for creating new proteins in which the original N-terminus and C-terminus of the native protein are joined without a linker and different N-terminus and C-terminus of the protein are created. In the example shown the sequence rearrangement results in a new gene encoding a protein with a new N-terminus created at [0326] amino acid 97 of the original protein, the original C-terminus (a.a. 174) joined to the original N-terminus and a new C-terminus created at amino acid 96 of the original sequence.
  • FIG. 4 shows a schematic of Method III, for creating new proteins in which the original N-terminus and C-terminus of the native protein are joined with a linker and different N-terminus and C-terminus of the protein are created. In the example shown the sequence rearrangement results in a new gene encoding a protein with a new N-terminus created at [0327] amino acid 97 of the original protein, the original C-terminus (a.a. 174) joined to amino acid 1 through a linker region and a new C-terminus created at amino acid 96 of the original sequence.
    • DETAILED DESCRIPTION OF THE INVENTION
  • The present invention encompasses multi-functional hematopoietic receptor agonists formed from covalently linked polypeptides, each of which may act through a different and specific cell receptor to initiate complementary biological activities. Hematopoiesis requires a complex series of cellular events in which stem cells generate continuously into large populations of maturing cells in all major lineages. There are currently at least 20 known regulators with hematopoietic proliferative activity. Most of these proliferative regulators can only stimulate one or another type of colony formation in vitro, the precise pattern of colony formation stimulated by each regulator is quite distinctive. No two regulators stimulate exactly the same pattern of colony formation, as evaluated by colony numbers or, more importantly, by the lineage and maturation pattern of the cells making up the developing colonies. Proliferative responses can most readily be analyzed in simplified in vitro culture systems. Three quite different parameters can be distinguished: alteration in colony size, alteration in colony numbers and cell lineage. Two or more factors may act on the progenitor cell, inducing the formation of larger number of progeny thereby increasing the colony size. Two or more factors may allow increased number of progenitor cells to proliferate either because distinct subsets of progenitors cells exist that respond exclusively to one factor or because some progenitors require stimulation by two or more factors before being able to respond. Activation of additional receptors on a cell by the use of two or more factors is likely to enhance the mitotic signal because of coalescence of initially differing signal pathways into a common final pathway reaching the nucleus (Metcalf, [0328] Nature 339:27, 1989). Other mechanisms could explain synergy. For example, if one signaling pathway is limited by an intermediate activation of an additional signaling pathway which is caused by a second factor, then this may result in a super additive response. In some cases, activation of one receptor type can induce an enhanced expression of other receptors (Metcalf, Blood 82:3515-3523, 1993). Two or more factors may result in a different pattern of cell lineages than from a single factor. The use of multi-functional hematopoietic receptor agonists may have a potential clinical advantage resulting from a proliferative response that is not possible by any single factor.
  • The receptors of hematopoietic and other growth factors can be grouped into two distinct families of related proteins: (1) tyrosine kinase receptors, including those for epidermal growth factor, M-CSF (Sherr, [0329] Blood 75:1, 1990) and SCF (Yarden et al., EMBO J. 6:3341, 1987): and (2) hematopoietic receptors, not containing a tyrosine kinase domain, but exhibiting obvious homology in their extracellular domain (Bazan, PNAS USA 87:6934-6938, 1990). Included in this latter group are erythropoietin (EPO) (D'Andrea et al., Cell 57:277, 1989), GM-CSF (Gearing et al., EMBO J. 8:3667, 1989), IL-3 (Kitamura et al., Cell 66:1165, 1991), G-CSF (Fukunaga et al., J. Bio. Chem. 265:14008-15, 1990), IL-4 (Harada et al., PNAS USA 87:857, 1990), IL-5 (Takaki et al., EMBO J. 9:4367, 1990), IL-6 (Yamasaki et al., Science 241:825, 1988), IL-7 (Goodwin et al., Cell 60:941-51, 1990), LIF (Gearing et al., EMBO J. 10:2839, 1991) and IL-2 (Cosman et al., Mol-Immunol. 23: 935-94, 1986). Most of the latter group of receptors exists in a high-affinity form as heterodimers. After ligand binding, the specific a-chains become associated with at least one other receptor chain (b-chain, g-chain). Many of these factors share a common receptor subunit. The a-chains for GM-CSF, IL-3 and IL-5 share the same b-chain (Kitamura et al., Cell 66:1165, 1991), Takaki et al., EMBO J. 10:2833-8, 1991) and receptor complexes for IL-6, LIF and IL-11 share a common b-chain (gp130) (Taga et al., Cell 58:573-81, 1989; Gearing et al., Science 255:1434-7, 1992). The receptor complexes of IL-2, IL-4, IL-7, IL-9 and IL-15 share a common g-chain (Kondo et al., Science 262:1874, 1993; Russell et al., Science 266: 1042-1045, 1993; Noguchi et al., Science 262:1877, 1993; Giri et al., EMBO J. 13:2822-2830, 1994).
  • The use of a multiply acting hematopoietic factor may also have a potential advantage by reducing the demands placed on factor-producing cells and their induction systems. If there are limitations in the ability of a cell to produce a factor, then by lowering the required concentrations of each of the factors, and using them in combination may usefully reduce demands on the factor-producing cells. The use of a multiply acting hematopoietic factor may lower the amount of the factors that would be needed, probably reducing the likelihood of adverse side-effects. [0330]
  • Novel compounds of this invention are represented by a formula selected from the group consisting of: [0331]
  • R1-L1-R2, R2-L1-R1, R1-R2, and R2-R1
  • Where R[0332] 1 and R2 are as defined above.
  • R[0333] 2 is preferably a colony stimulating factor with a different but complementary activity than R1. By complementary activity is meant activity which enhances or changes the response to another cell modulator. The R1 polypeptide is joined either directly or through a linker segment to the R2 polypeptide. The term “directly” defines multi-functional hematopoietic receptor agonists in which the polypeptides are joined without a peptide linker. Thus L1 represents a chemical bond or polypeptide segment to which both R1 and R2 are joined in frame, most commonly L1 is a linear peptide to which R1 and R2 are joined by amide bonds linking the carboxy terminus of R1 to the amino terminus of L1 and carboxy terminus of L1 to the amino terminus of R2. By “joined in frame” is meant that there is no translation termination or disruption between the reading frames of the DNA encoding R1 and R2.
  • A non-exclusive list of other growth factors, i.e. colony stimulating factors (CSFs), are cytokines, lymphokines, interleukins, or hematopoietic growth factors which can be joined to (I), (II) or (III) include GM-CSF, G-CSF, c-mpl ligand (also known as TPO or MGDF), M-CSF, erythropoietin (EPO), IL-1, IL-4, IL-2, IL-3, IL-5, IL 6, IL-7, IL-8, IL-9, IL-10, IL-11, IL-12, IL-13, IL-15, LIF, flt3 ligand, human growth hormone, and stem cell factor (SCF) also known as steel factor or c-kit ligand. Additionally, this invention encompasses the use of modified R[0334] 1 or R2 molecules or mutated or modified DNA sequences encoding these R1 or R2 molecules. The present invention also includes multi-functional hematopoietic receptor agonists in which R1 or R2 is an hIL-3 variant, c-mpl ligand variant, or G-CSF variant. A “hIL-3 variant” is defined as a hIL-3 molecule which has amino acid substitutions and/or portions of hIL-3 deleted as disclosed in WO 94/12638, WO 94/12639 and WO 95/00646, as well as other variants known in the art. A “c-mpl ligand variant” is defined an c-mpl ligand molecule which has amino acid substitutions and/or portions of c-mpl ligand deleted, disclosed in U.S. application Ser. No. 08/383,035 as well as other variants known in the art. A “G-CSF variant” is defined an G-CSF molecule which has amino acid substitutions and/or portions of G-CSF deleted, as disclosed herein, as well as other variants known in the art.
  • The linking group (L[0335] 1) is generally a polypeptide of between 1 and 500 amino acids in length. The linkers joining the two molecules are preferably designed to (1) allow the two molecules to fold and act independently of each other, (2) not have a propensity for developing an ordered secondary structure which could interfere with the functional domains of the two proteins, (3) have minimal hydrophobic characteristics which could interact with the functional protein domains and (4) provide steric separation of R1 and R2 such that R1 and R2 could interact simultaneously with their corresponding receptors on a single cell. Typically surface amino acids in flexible protein regions include Gly, Asn and Ser. Virtually any permutation of amino acid sequences containing Gly, Asn and Ser would be expected to satisfy the above criteria for a linker sequence. Other neutral amino acids, such as Thr and Ala, may also be used in the linker sequence. Additional amino acids may also be included in the linkers due to the addition of unique restriction sites in the linker sequence to facilitate construction of the multi-functional hematopoietic receptor agonists.
  • Preferred L[0336] 1 linkers of the present invention include sequences selected from the group of formulas:
    (Gly3Ser)n, (SEQ ID NO: 4),
    (Gly4Ser)n, (SEQ ID NO: 5)
    (Gly5Ser)n, (SEQ ID NO: 6)
    (GlynSer)n or (SEQ ID NO: 7)
    (AlaGlySer)n. (SEQ ID NO: 8)
  • One example of a highly-flexible linker is the glycine and serine-rich spacer region present within the pIII protein of the filamentous bacteriophages, e.g. bacteriophages M13 or fd (Schaller et al., [0337] PNAS USA 72: 737-741, 1975). This region provides a long, flexible spacer region between two domains of the pIII surface protein. The spacer region consists of the amino acid sequence:
    GlyGlyGlySerGlyGlyGlySerGlyGlyGly (SEQ ID NO: 9)
    SerGluGlyGlyGlySerGluGlyGlyGlySer
    GluGlyGlyGlySerGluGlyGlyGlySerGly
    GlyGlySer.
  • The present invention also includes linkers in which an endopeptidase recognition sequence is included. Such a cleavage site may be valuable to separate the individual components of the multi-functional hematopoietic receptor agonist to determine if they are properly folded and active in vitro. Examples of various endopeptidases include, but are not limited to, plasmin, enterokinase, kallikrein, urokinase, tissue plasminogen activator, clostripain, chymosin, collagenase, Russell's viper venom protease, postproline cleavage enzyme, V8 protease, Thrombin and factor Xa. [0338]
  • Peptide linker segments from the hinge region of heavy chain immunoglobulins IgG, IgA, IgM, IgD or IgE provide an angular relationship between the attached polypeptides. Especially useful are those hinge regions where the cysteines are replaced with serines. Preferred linkers of the present invention include sequences derived from murine IgG gamma 2b hinge region in which the cysteines have been changed to serines. These linkers may also include an endopeptidase cleavage site. Examples of such linkers include the following sequences: [0339]
    IleSerGluProSerGlyProIleSerThrIle (SEQ ID NO: 10)
    AsnProSerProProSerLysGluSerHisLys
    SerPro and
    IleGluGlyArgIleSerGluProSerGlyPro (SEQ ID NO: 11)
    IleSerThrIleAsnProSerProProSerLys
    GluSerHisLysSerPro.
  • The present invention is, however, not limited by the form, size or number of linker sequences employed and the only requirement of the linker is that functionally it does not interfere with the folding and function of the individual molecules of the multi-functional hematopoietic receptor agonist. [0340]
  • One aspect of the invention includes multi-functional hematopoietic receptor agonists which comprise a sequence rearranged c-mpl receptor agonist in which the cysteine(s) at position 7 and 151 of c-mpl ligand, have been substituted with another amino acid. Kaushansky et al. ([0341] Blood 86:255a Abstract 1008, 1995) teaches that all four of the cysteines at positions 7, 29, 85, and 151 are required for bioactivity. The presence of cysteines in a protein can cause problems in processing when the protein is being produced recombinantly in a bacterial host. Microbially produced cysteine-containing proteins may tend to form multimers which greatly complicate purification of the protein product. Several additional purification steps, such as reduction and reoxidation of the recombinant protein may be required to obtain the protein in the proper confirmation. Removal of one of the cysteine residues, with concurrent replacement by a chemically equivalent neutral amino acid, would be desirable, in order to simplify the isolation and purification of the molecule. However, the successful removal of cysteines from biologically active molecules is unpredictable, in that the tertiary structure in the absence of the normally formed disulfide bridges, can be substantially altered. A molecule in which a pair of cysteines at positions 7 and 151 are substituted with another amino acid may have one or more advantages including, but not limited to: 1) increased folding efficiency of the heterologously expressed protein; 2) elimination of mispaired disulfides, 3) use of milder refold conditions (ie. Guanidine vs. Urea); 4) increased purification yields, 5) increased protein solubility; and 6) increased protein stability.
    • Determination of the Linker L2
  • The length of the amino acid sequence of the linker L[0342] 2 to be used in R1 and/or R2 can be selected empirically or with guidance from structural information, or by using a combination of the two approaches.
  • When no structural information is available, a small series of linkers can be prepared for testing using a design whose length is varied in order to span a range from 0 to 50 Å and whose sequence is chosen in order to be consistent with surface exposure (hydrophilicity, Hopp & Woods, [0343] Mol. Immunol. 20: 483-489, 1983), Kyte & Doolittle, J. Mol. Biol. 157:105-132; solvent exposed surface area, Lee & Richards, J. Mol. Biol. 55:379-400, 1971) and the ability to adopt the necessary conformation with out deranging the conformation of R1 or R2 (conformationally flexible; Karplus & Schulz, Naturwissenschaften 72:212-213, 1985). Assuming an average of translation of 2.0 to 3.8 Å per residue, this would mean the length to test would be between 0 to 30 residues, with 0 to 15 residues being the preferred range. Exemplary of such an empirical series would be to construct linkers using a cassette sequence such as Gly-Gly-Gly-Ser (SEQ ID NO:12) repeated n times, where n is 1, 2, 3 or 4. Those skilled in the art will recognize that there are many such sequences that vary in length or composition that can serve as linkers with the primary consideration being that they be neither excessively long nor short (cf., Sandhu, Critical Rev. Biotech. 12: 437-462, 1992); if they are too long, entropy effects will likely destabilize the three-dimensional fold, and may also make folding kinetically impractical, and if they are too short, they will likely destabilize the molecule because of torsional or steric strain.
  • Those skilled in the analysis of protein structural information will recognize that using the distance between the chain ends, defined as the distance between the c-alpha carbons, can be used to define the length of the sequence to be used, or at least to limit the number of possibilities that must be tested in an empirical selection of linkers. They will also recognize that it is sometimes the case that the positions of the ends of the polypeptide chain are ill-defined in structural models derived from x-ray diffraction or nuclear magnetic resonance spectroscopy data, and that when true, this situation will therefore need to be taken into account in order to properly estimate the length of the linker required. From those residues whose positions are well defined are selected two residues that are close in sequence to the chain ends, and the distance between their c-alpha carbons is used to calculate an approximate length for a linker between them. Using the calculated length as a guide, linkers with a range of number of residues (calculated using 2 to 3.8 Å per residue) are then selected. These linkers may be composed of the original sequence, shortened or lengthened as necessary, and when lengthened the additional residues may be chosen to be flexible and hydrophilic as described above; or optionally the original sequence may be substituted for using a series of linkers, one example being the Gly-Gly-Gly-Ser (SEQ ID NO:12) cassette approach mentioned above; or optionally a combination of the original sequence and new sequence having the appropriate total length may be used. [0344]
    • Determination of the Amino and Carboxyl Termini of R1 and R2
  • Sequences of R[0345] 1 and R2 capable of folding to biologically active states can be prepared by appropriate selection of the beginning (amino terminus) and ending (carboxyl terminus) positions from within the original polypeptide chain while using the linker sequence L2 as described above. Amino and carboxyl termini are selected from within a common stretch of sequence, referred to as a breakpoint region, using the guidelines described below. A novel amino acid sequence is thus generated by selecting amino and carboxyl termini from within the same breakpoint region. In many cases the selection of the new termini will be such that the original position of the carboxyl terminus immediately preceded that of the amino terminus. However, those skilled in the art will recognize that selections of termini anywhere within the region may function, and that these will effectively lead to either deletions or additions to the amino or carboxyl portions of the new sequence.
  • It is a central tenet of molecular biology that the primary amino acid sequence of a protein dictates folding to the three-dimensional structure necessary for expression of its biological function. Methods are known to those skilled in the art to obtain and interpret three-dimensional structural information using x-ray diffraction of single protein crystals or nuclear magnetic resonance spectroscopy of protein solutions. Examples of structural information that are relevant to the identification of breakpoint regions include the location and type of protein secondary structure (alpha and 3-10 helices, parallel and anti-parallel beta sheets, chain reversals and turns, and loops; Kabsch & Sander, [0346] Biopolymers 22: 2577-2637, 1983), the degree of solvent exposure of amino acid residues, the extent and type of interactions of residues with one another (Chothia, Ann. Rev. Biochem. 53:537-572, 1984) and the static and dynamic distribution of conformations along the polypeptide chain (Alber & Mathews, Methods Enzymol. 154: 511-533, 1987). In some cases additional information is known about solvent exposure of residues; one example is a site of post-translational attachment of carbohydrate which is necessarily on the surface of the protein. When experimental structural information is not available, or is not feasible to obtain, methods are also available to analyze the primary amino acid sequence in order to make predictions of protein tertiary and secondary structure, solvent accessibility and the occurrence of turns and loops. Biochemical methods are also sometimes applicable for empirically determining surface exposure when direct structural methods are not feasible; for example, using the identification of sites of chain scission following limited proteolysis in order to infer surface exposure (Gentile & Salvatore, Eur. J. Biochem. 218:603-621, 1993)
  • Thus using either the experimentally derived structural information or predictive methods (e.g., Srinivisan & Rose [0347] Proteins: Struct., Funct. & Genetics, 22: 81-99, 1995) the parental amino acid sequence is inspected to classify regions according to whether or not they are integral to the maintenance of secondary and tertiary structure. The occurrence of sequences within regions that are known to be involved in periodic secondary structure (alpha and 3-10 helices, parallel and anti-parallel beta sheets) are regions that should be avoided. Similarly, regions of amino acid sequence that are observed or predicted to have a low degree of solvent exposure are more likely to be part of the so-called hydrophobic core of the protein and should also be avoided for selection of amino and carboxyl termini. In contrast, those regions that are known or predicted to be in surface turns or loops, and especially those regions that are known not to be required for biological activity, are the preferred sites for location of the extremes of the polypeptide chain. Continuous stretches of amino acid sequence that are preferred based on the above criteria are referred to as a breakpoint region.
    • Non-covalent Multifunctional Hematopoietic Growth Factors
  • An alternative method for connecting two hematopoietic growth factors is by means of a non-covalent interaction. Such complexed proteins can be described by one of the formulae: [0348]
  • R1-C1+R2-C2; or C1-R1+C2-R2; C1-R1+R2-C2; or C1-R1+R2-C2.
  • R[0349] 1 and R2 are as is defined above. Domains C1 and C2 are either identical or non-identical chemical structures, typically proteinaceous, which can form a non-covalent, specific association. Complexes between C1 and C2 result in a one-to-one stoichiometric relationship between R1 and R2 for each complex. Examples of domains which associate are “leucine zipper” domains of transcription factors, dimerization domains of bacterial transcription repressors and immunoglobulin constant domains. Covalent bonds link R1 and C1, and R2 and C2, respectively. As indicated in the formulae, the domains C1 and C2 can be present either at the N-terminus or C-terminus of their corresponding hematopoietic growth factor (R). These multimerization domains (C1 and C2) include those derived from the bZIP family of proteins (Abel et al., Nature 341:24-25, 1989; Landshulz et al., Science 240:1759-1764, 1988; Pu et al., Nuc. Acid Res. 21:4348-4355, 1993; Kozarides et al., Nature 336:646-651, 1988), as well as multimerization domains of the helix-loop-helix family of proteins (Abel et al., Nature 341:24-25, 1989; Murre et al., Cell 56:777-783, 1989; Tapscott et al., Science 242:405-411, 1988; Fisher et al., Genes & Dev. 5:2342-2352, 1991). Preferred multi-functional hematopoietic receptor agonists of the present invention include colony stimulating factors dimerized by virtue of their incorporation as translational multi-functional hematopoietic receptor agonists with the leucine zipper dimerization domains of the bZIP family proteins Fos and Jun. The leucine zipper domain of Jun is capable of interacting with identical domains. On the other hand, the leucine zipper domain of Fos interacts with the Jun leucine zipper domain, but does not interact with other Fos leucine zipper domains. Mixtures of Fos and Jun predominantly result in formation of Fos-Jun heterodimers. Consequently, when joined to colony stimulating factors, the Jun domain can be used to direct the formation of either homo- or heterodimers. Preferential formation of heterodimers can be achieved if one of the colony stimulating factor partners is engineered to possess the Jun leucine zipper domain while the other is engineered to possess the Fos zipper.
  • Additional peptide sequences may also be added to facilitate purification or identification of multi-functional hematopoietic receptor agonist proteins (e.g., poly-His). A highly antigenic peptide may also be added that would enable rapid assay and facile purification of the multi-functional hematopoietic receptor agonist protein by a specific monoclonal antibody. [0350]
  • “Mutant amino acid sequence,” “mutant protein”, “variant protein”, “mutein”, or “mutant polypeptide” refers to a polypeptide having an amino acid sequence which varies from a native sequence due to amino acid deletions, substitutions, or both, or is encoded by a nucleotide sequence intentionally made variant from a native sequence. “Native sequence” refers to an amino acid or nucleic acid sequence which is identical to a wild-type or native form of a gene or protein. [0351]
  • Hematopoietic growth factors can be characterized by their ability to stimulate colony formation by human hematopoietic progenitor cells. The colonies formed include erythroid, granulocyte, megakaryocyte, granulocytic macrophages and mixtures thereof. Many of the hematopoietic growth factors have demonstrated the ability to restore bone marrow function and peripheral blood cell populations to therapeutically beneficial levels in studies performed initially in primates and subsequently in humans. Many or all of these biological activities of hematopoietic growth factors involve signal transduction and high affinity receptor binding. Multi-functional hematopoietic receptor agonists of the present invention may exhibit useful properties such as having similar or greater biological activity when compared to a single factor or by having improved half-life or decreased adverse side effects, or a combination of these properties. [0352]
  • Multi-functional hematopoietic receptor agonists which have little or no agonist activity maybe useful as antagonists, as antigens for the production of antibodies for use in immunology or immunotherapy, as genetic probes or as intermediates used to construct other useful hIL-3 muteins. [0353]
  • Biological activity of the multi-functional hematopoietic receptor agonist proteins of the present invention can be determined by DNA synthesis in factor-dependent cell lines or by counting the colony forming units in an in vitro bone marrow assay. [0354]
  • The multi-functional hematopoietic receptor agonists of the present invention may have an improved therapeutic profile as compared to single acting hematopoietic agonists. For example, some multi-functional hematopoietic receptor agonists of the present invention may have a similar or more potent growth factor activity relative to other hematopoietic agonists without having a similar or corresponding increase in side-effects. [0355]
  • The present invention also includes the DNA sequences which code for the multi-functional hematopoietic receptor agonist proteins, DNA sequences which are substantially similar and perform substantially the same function, and DNA sequences which differ from the DNAs encoding the multi-functional hematopoietic receptor agonists of the invention only due to the degeneracy of the genetic code. Also included in the present invention are the oligonucleotide intermediates used to construct the mutant DNAs and the polypeptides coded for by these oligonucleotides. [0356]
  • Genetic engineering techniques now standard in the art (U.S. Pat. No. 4,935,233 and Sambrook et al., “Molecular Cloning A Laboratory Manual”, Cold Spring Harbor Laboratory, 1989) may be used in the construction of the DNA sequences of the present invention. One such method is cassette mutagenesis (Wells et al., [0357] Gene 34:315-323, 1985) in which a portion of the coding sequence in a plasmid is replaced with synthetic oligonucleotides that encode the desired amino acid substitutions in a portion of the gene between two restriction sites.
  • Pairs of complementary synthetic oligonucleotides encoding the desired gene can be made and annealed to each other. The DNA sequence of the oligonucleotide would encode sequence for amino acids of desired gene with the exception of those substituted and/or deleted from the sequence. [0358]
  • Plasmid DNA can be treated with the chosen restriction endonucleases then ligated to the annealed oligonucleotides. The ligated mixtures can be used to transform competent JM101 cells to resistance to an appropriate antibiotic. Single colonies can be picked and the plasmid DNA examined by restriction analysis and/or DNA sequencing to identify plasmids with the desired genes. [0359]
  • Cloning of the DNA sequences of the novel multifunctional hematopoietic agonists wherein at least one of the with the DNA sequence of the other colony stimulating factor may be accomplished by the use of intermediate vectors. Alternatively one gene can be cloned directly into a vector containing the other gene. Linkers and adapters can be used for joining the DNA sequences, as well as replacing lost sequences, where a restriction site was internal to the region of interest. Thus genetic material (DNA) encoding one polypeptide, peptide linker, and the other polypeptide is inserted into a suitable expression vector which is used to transform bacteria, yeast, insect cells or mammalian cells. The transformed organism is grown and the protein isolated by standard techniques. The resulting product is therefore a new protein which has a colony stimulating factor joined by a linker region to a second colony stimulating factor. [0360]
  • Another aspect of the present invention provides plasmid DNA vectors for use in the expression of these novel multi-functional hematopoietic receptor agonists. These vectors contain the novel DNA sequences described above which code for the novel polypeptides of the invention. Appropriate vectors which can transform microorganisms capable of expressing the multi-functional hematopoietic receptor agonists include expression vectors comprising nucleotide sequences coding for the multi-functional hematopoietic receptor agonists joined to transcriptional and translational regulatory sequences which are selected according to the host cells used. [0361]
  • Vectors incorporating modified sequences as described above are included in the present invention and are useful in the production of the multi-functional hematopoietic receptor agonist polypeptides. The vector employed in the method also contains selected regulatory sequences in operative association with the DNA coding sequences of the invention and which are capable of directing the replication and expression thereof in selected host cells. [0362]
  • As another aspect of the present invention, there is provided a method for producing the novel multi-functional hematopoietic receptor agonists. The method of the present invention involves culturing suitable cells or cell line, which has been transformed with a vector containing a DNA sequence coding for expression of a novel multi-functional hematopoietic receptor agonist. Suitable cells or cell lines may be bacterial cells. For example, the various strains of [0363] E. coli are well-known as host cells in the field of biotechnology. Examples of such strains include E. coli strains JM101 (Yanish-Perron et al. Gene 33: 103-119, 1985) and MON105 (Obukowicz et al., Applied Environmental Microbiology 58: 1511-1523, 1992). Also included in the present invention is the expression of the multi-functional hematopoietic receptor agonist protein utilizing a chromosomal expression vector for E. coli based on the bacteriophage Mu (Weinberg et al., Gene 126: 25-33, 1993). Various strains of B. subtilis may also be employed in this method. Many strains of yeast cells known to those skilled in the art are also available as host cells for expression of the polypeptides of the present invention. When expressed in the E. coli cytoplasm, the gene encoding the multi-functional hematopoietic receptor agonists of the present invention may also be constructed such that at the 5′ end of the gene codons are added to encode Met−2-Ala−1- or Met−1 at the N-terminus of the protein. The N termini of proteins made in the cytoplasm of E. coli are affected by post-translational processing by methionine aminopeptidase (Ben Bassat et al., J. Bac. 169:751-757, 1987) and possibly by other peptidases so that upon expression the methionine is cleaved off the N-terminus. The multi-functional hematopoietic receptor agonists of the present invention may include multi-functional hematopoietic receptor agonist polypeptides having Met−1, Ala−1 or Met−2-Ala−1 at the N-terminus. These mutant multi-functional hematopoietic receptor agonists may also be expressed in E. coli by fusing a secretion signal peptide to the N-terminus. This signal peptide is cleaved from the polypeptide as part of the secretion process.
  • Also suitable for use in the present invention are mammalian cells, such as Chinese hamster ovary cells (CHO). General methods for expression of foreign genes in mammalian cells are reviewed in Kaufman, R. J., 1987) Genetic Engineering, Principles and Methods, Vol. 9, J. K. Setlow, editor, Plenum Press, New York. An expression vector is constructed in which a strong promoter capable of functioning in mammalian cells drives transcription of a eukaryotic secretion signal peptide coding region, which is translationally joined to the coding region for the multi-functional hematopoietic receptor agonist. For example, plasmids such as pcDNA I/Neo, pRc/RSV, and pRc/CMV (obtained from Invitrogen Corp., San Diego, Calif.) can be used. The eukaryotic secretion signal peptide coding region can be from the gene itself or it can be from another secreted mammalian protein (Bayne, M. L. et al., [0364] Proc. Natl. Acad. Sci. USA 84: 2638-2642, 1987). After construction of the vector containing the gene, the vector DNA is transfected into mammalian cells. Such cells can be, for example, the COS7, HeLa, BHK, CHO, or mouse L lines. The cells can be cultured, for example, in DMEM media (JRH Scientific). The polypeptide secreted into the media can be recovered by standard biochemical approaches following transient expression for 24-72 hours after transfection of the cells or after establishment of stable cell lines following selection for antibiotic resistance. The selection of suitable mammalian host cells and methods for transformation, culture, amplification, screening and product production and purification are known in the art. See, e.g., Gething and Sambrook, Nature, 293:620-625, 1981), or alternatively, Kaufman et al, Mol. Cell. Biol., 5(7):1750-1759, 1985) or Howley et al., U.S. Pat. No. 4,419,446. Another suitable mammalian cell line is the monkey COS-1 cell line. A similarly useful mammalian cell line is the CV-1 cell line.
  • Where desired, insect cells may be utilized as host cells in the method of the present invention. See, e.g., Miller et al., [0365] Genetic Engineering, 8:277-298 (Plenum Press 1986) and references cited therein. In addition, general methods for expression of foreign genes in insect cells using Baculovirus vectors are described in: Summers, M. D. and Smith, G. E., 1987)—A manual of methods for Baculovirus vectors and insect cell culture procedures, Texas Agricultural Experiment Station Bulletin No. 1555. An expression vector is constructed comprising a Baculovirus transfer vector, in which a strong Baculovirus promoter (such as the polyhedron promoter) drives transcription of a eukaryotic secretion signal peptide coding region, which is translationally joined to the coding region for the multi-functional hematopoietic receptor agonist polypeptide. For example, the plasmid pVL1392 (obtained from Invitrogen Corp., San Diego, Calif.) can be used. After construction of the vector carrying the gene encoding the multi-functional hematopoietic receptor agonist polypeptide, two micrograms of this DNA is co-transfected with one microgram of Baculovirus DNA (see Summers & Smith, 1987) into insect cells, strain SF9. Pure recombinant Baculovirus carrying the multi-functional hematopoietic receptor agonist is used to infect cells cultured, for example, in Excell 401 serum-free medium (JRH Biosciences, Lenexa, Kans.). The multi-functional hematopoietic receptor agonist secreted into the medium can be recovered by standard biochemical approaches. Supernatants from mammalian or insect cells expressing the multi-functional hematopoietic receptor agonist protein can be first concentrated using any of a number of commercial concentration units.
  • The multi-functional hematopoietic receptor agonists of the present invention may be useful in the treatment of diseases characterized by decreased levels of either myeloid, erythroid, lymphoid, or megakaryocyte cells of the hematopoietic system or combinations thereof. In addition, they may be used to activate mature myeloid and/or lymphoid cells. Among conditions susceptible to treatment with the polypeptides of the present invention is leukopenia, a reduction in the number of circulating leukocytes (white cells) in the peripheral blood. Leukopenia may be induced by exposure to certain viruses or to radiation. It is often a side effect of various forms of cancer therapy, e.g., exposure to chemotherapeutic drugs, radiation and of infection or hemorrhage. Therapeutic treatment of leukopenia with these multi-functional hematopoietic receptor agonists of the present invention may avoid undesirable side effects caused by treatment with presently available drugs. [0366]
  • The multi-functional hematopoietic receptor agonists of the present invention may be useful in the treatment of neutropenia and, for example, in the treatment of such conditions as aplastic anemia, cyclic neutropenia, idiopathic neutropenia, Chediak-Higashi syndrome, systemic lupus erythematosus (SLE), leukemia, myelodysplastic syndrome and myelofibrosis. [0367]
  • The multi-functional hematopoietic receptor agonist of the present invention may be useful in the treatment or prevention of thrombocytopenia. Currently the only therapy for thrombocytopenia is platelet transfusion which are costly and carry the significant risks of infection (HIV, HBV) and alloimmunization. The multi-functional hematopoietic receptor agonist may alleviate or diminish the need for platelet transfusion. Severe thrombocytopenia may result from genetic defects such as Fanconi's Anemia, Wiscott-Aldrich, or May Hegglin syndromes. Acquired thrombocytopenia may result from auto- or allo-antibodies as in Immune Thrombocytopenia Purpura, Systemic Lupus Erythromatosis, hemolytic anemia, or fetal maternal incompatibility. In addition, splenomegaly, disseminated intravascular coagulation, thrombotic thrombocytopenic purpura, infection or prosthetic heart valves may result in thrombocytopenia. Severe thrombocytopenia may also result from chemotherapy and/or radiation therapy or cancer. Thrombocytopenia may also result from marrow invasion by carcinoma, lymphoma, leukemia or fibrosis. [0368]
  • The multi-functional hematopoietic receptor agonists of the present invention may be useful in the mobilization of hematopoietic progenitors and stem cells in peripheral blood. Peripheral blood derived progenitors have been shown to be effective in reconstituting patients in the setting of autologous marrow transplantation. Hematopoietic growth factors including G-CSF and GM-CSF have been shown to enhance the number of circulating progenitors and stem cells in the peripheral blood. This has simplified the procedure for peripheral stem cell collection and dramatically decreased the cost of the procedure by decreasing the number of pheresis required. The multi-functional hematopoietic receptor agonist may be useful in mobilization of stem cells and further enhance the efficacy of peripheral stem cell transplantation. [0369]
  • The multi-functional hematopoietic receptor agonists of the present invention may also be useful in the ex vivo expansion of hematopoietic progenitors and stem cells. Colony stimulating factors (CSFs), such as hIL-3, have been administered alone, co-administered with other CSFs, or in combination with bone marrow transplants subsequent to high dose chemotherapy to treat the neutropenia and thrombocytopenia which are often the result of such treatment. However the period of severe neutropenia and thrombocytopenia may not be totally eliminated. The myeloid lineage, which is comprised of monocytes (macrophages), granulocytes (including neutrophils) and megakaryocytes, is critical in preventing infections and bleeding which can be life-threatening. Neutropenia and thrombocytopenia may also be the result of disease, genetic disorders, drugs, toxins, radiation and many therapeutic treatments such as conventional oncology therapy. [0370]
  • Bone marrow transplants have been used to treat this patient population. However, several problems are associated with the use of bone marrow to reconstitute a compromised hematopoietic system including: 1) the number of stem cells in bone marrow, spleen, or peripheral blood is limited, 2) Graft Versus Host Disease, 3) graft rejection and 4) possible contamination with tumor cells. Stem cells make up a very small percentage of the nucleated cells in the bone marrow, spleen and peripheral blood. It is clear that a dose response exists such that a greater number of stem cells will enhance hematopoietic recovery. Therefore, the in vitro expansion of stem cells should enhance hematopoietic recovery and patient survival. Bone marrow from an allogeneic donor has been used to provide bone marrow for transplant. However, Graft Versus Host Disease and graft rejection limit bone marrow transplantation even in recipients with HLA-matched sibling donors. An alternative to allogeneic bone marrow transplants is autologous bone marrow transplants. In autologous bone marrow transplants, some of the patient's own marrow is harvested prior to myeloablative therapy, e.g. high dose chemotherapy, and is transplanted back into the patient afterwards. Autologous transplants eliminate the risk of Graft Versus Host Disease and graft rejection. However, autologous bone marrow transplants still present problems in terms of the limited number of stems cells in the marrow and possible contamination with tumor cells. The limited number of stem cells may be overcome by ex-vivo expansion of the stem cells. In addition, stem cells can be specifically isolated, based on the presence of specific surface antigens such as CD34+ in order to decrease tumor cell contamination of the marrow graft. [0371]
  • The following patents contain further details on separating stem cells, CD34+ cells, culturing the cells with hematopoietic factors, the use of the cells for the treatment of patients with hematopoietic disorders and the use of hematopoietic factors for cell expansion and gene therapy. [0372]
  • U.S. Pat. No. 5,061,620 relates to compositions comprising human hematopoietic stem cells provided by separating the stem cells from dedicated cells. [0373]
  • U.S. Pat. No. 5,199,942 describes a method for autologous hematopoietic cell transplantation comprising: (1) obtaining hematopoietic progenitor cells from a patient; (2) ex-vivo expansion of cells with a growth factor selected from the group consisting of IL-3, flt3 ligand, c-kit ligand, GM-CSF, IL-1, GM-CSF/IL-3 fusion protein and combinations thereof; (3) administering cellular preparation to a patient. [0374]
  • U.S. Pat. No. 5,240,856 relates to a cell separator that includes an apparatus for automatically controlling the cell separation process. [0375]
  • WO 91/16116 describes devices and methods for selectively isolating and separating target cells from a mixture of cells. [0376]
  • WO 91/18972 describes methods for in vitro culturing of bone marrow, by incubating suspension of bone marrow cells, using a hollow fiber bioreactor. [0377]
  • WO 92/18615 relates to a process for maintaining and expanding bone marrow cells, in a culture medium containing specific mixtures of cytokines, for use in transplants. [0378]
  • WO 93/08268 describes a method for selectively expanding stem cells, comprising the steps of (a) separating CD34+ stem cells from other cells and (b) incubating the separated cells in a selective medium, such that the stem cells are selectively expanded. [0379]
  • WO 93/18136 describes a process for in vitro support of mammalian cells derived from peripheral blood. [0380]
  • WO 93/18648 relates to a composition comprising human neutrophil precursor cells with a high content of myeloblasts and promyelocytes for treating genetic or acquired neutropenia. [0381]
  • WO 94/08039 describes a method of enrichment for human hematopoietic stem cells by selection for cells which express c-kit protein. [0382]
  • WO 94/11493 describes a stem cell population that are CD34+ and small in size, which are isolated using a counterflow elutriation method. [0383]
  • WO 94/27698 relates to a method combining immunoaffinity separation and continuous flow centrifugal separation for the selective separation of a nucleated heterogeneous cell population from a heterogeneous cell mixture. [0384]
  • WO 94/25848 describes a cell separation apparatus for collection and manipulation of target cells. [0385]
  • The long term culturing of highly enriched CD34+ precursors of hematopoietic progenitor cells from human bone marrow in cultures containing IL-1a, IL-3, IL-6 or GM-CSF is discussed in Brandt et al [0386] J. Clin. Invest. 86:932-941, 1990).
  • One aspect of the present invention provides a method for selective ex-vivo expansion of stem cells. The term “stem cell” refers to the totipotent hematopoietic stem cells as well as early precursors and progenitor cells which can be isolated from bone marrow, spleen or peripheral blood. The term “expansion” refers to the differentiation and proliferation of the cells. The present invention provides a method for selective ex-vivo expansion of stem cells, comprising the steps of: (a) separating stem cells from other cells, (b) culturing said separated stem cells with a selective media which contains multi-functional hematopoietic receptor agonist protein(s) and (c) harvesting said stems cells. Stem cells, as well as committed progenitor cells destined to become neutrophils, erythrocytes, platelets, etc. may be distinguished from most other cells by the presence or absence of particular progenitor marker antigens, such as CD34, that are present on the surface of these cells and/or by morphological characteristics. The phenotype for a highly enriched human stem cell fraction is reported as CD34+, Thy-1+ and lin-, but it is to be understood that the present invention is not limited to the expansion of this stem cell population. The CD34+ enriched human stem cell fraction can be separated by a number of reported methods, including affinity columns or beads, magnetic beads or flow cytometry using antibodies directed to surface antigens such as the CD34+. Further, physical separation methods such as counterflow elutriation may be used to enrich hematopoietic progenitors. The CD34+ progenitors are heterogeneous, and may be divided into several sub-populations characterized by the presence or absence of co-expression of different lineage associated cell surface associated molecules. The most immature progenitor cells do not express any known lineage associated markers, such as HLA-DR or CD38, but they may express CD90(thy-1). Other surface antigens such as CD33, CD38, CD41, CD71, HLA-DR or c-kit can also be used to selectively isolate hematopoietic progenitors. The separated cells can be incubated in selected medium in a culture flask, sterile bag or in hollow fibers. Various colony stimulating factors may be utilized in order to selectively expand cells. Representative factors that have been utilized for ex-vivo expansion of bone marrow include, c-kit ligand, IL-3, G-CSF, GM-CSF, IL-1, IL-6, IL-11, flt-3 ligand or combinations thereof. The proliferation of the stem cells can be monitored by enumerating the number of stem cells and other cells, by standard techniques (e.g. hemacytometer, CFU, LTCIC) or by flow cytometry prior and subsequent to incubation. [0387]
  • Several methods for ex-vivo expansion of stem cells have been reported utilizing a number of selection methods and expansion using various colony stimulating factors including c-kit ligand (Brandt et al., [0388] Blood 83:1507-1514 [1994], McKenna et al., Blood 86:3413-3420 [1995]), IL-3 (Brandt et al., Blood 83:1507-1514 [1994], Sato et al., Blood 82:3600-3609 [1993]), G-CSF (Sato et al., Blood 82:3600-3609 [1993]), GM-CSF (Sato et al., Blood 82:3600-3609 [1993]), IL-1 (Muench et al., Blood 81:3463-3473 [1993]), IL-6 (Sato et al., Blood 82:3600-3609 [1993]), IL-11 (Lemoli et al., Exp. Hem. 21:1668-1672 [1993], Sato et al., Blood 82:3600-3609 [1993]), flt-3 ligand (McKenna et al., Blood 86:3413 3420 [1995]) and/or combinations thereof (Brandt et al., Blood 83:1507 1514 [1994], Haylock et al., Blood 80:1405-1412 [1992], Koller et al., Biotechnology 11:358-363 [1993], (Lemoli et al., Exp. Hem. 21:1668-1672 [1993]), McKenna et al., Blood 86:3413-3420 [1995], Muench et al., Blood 81:3463-3473 [1993], Patchen et al., Biotherapy 7:13-26 [1994], Sato et al., Blood 82:3600-3609 [1993], Smith et al., Exp. Hem. 21:870-877 [1993], Steen et al., Stem Cells 12:214-224 [1994], Tsujino et al., Exp. Hem. 21:1379-1386 [1993]). Among the individual colony stimulating factors, hIL-3 has been shown to be one of the most potent in expanding peripheral blood CD34+ cells (Sato et al., Blood 82:3600-3609 [1993], Kobayashi et al., Blood 73:1836-1841 [1989]). However, no single factor has been shown to be as effective as the combination of multiple factors. The present invention provides methods for ex vivo expansion that utilize multi-functional hematopoietic receptor agonists that are more effective than a single factor alone.
  • Another aspect of the invention provides methods of sustaining and/or expanding hematopoietic precursor cells which includes inoculating the cells into a culture vessel which contains a culture medium that has been conditioned by exposure to a stromal cell line such as HS-5 (WO 96/02662, Roecklein and Torok-Strob, [0389] Blood 85:997-1105, 1995) that has been supplemented with a multi-functional hematopoietic receptor agonist of the present invention.
  • Another projected clinical use of growth factors has been in the in vitro activation of hematopoietic progenitors and stem cells for gene therapy. Due to the long life-span of hematopoietic progenitor cells and the distribution of their daughter cells throughout the entire body, hematopoietic progenitor cells are good candidates for ex vivo gene transfection. In order to have the gene of interest incorporated into the genome of the hematopoietic progenitor or stem cell one needs to stimulate cell division and DNA replication. Hematopoietic stem cells cycle at a very low frequency which means that growth factors may be useful to promote gene transduction and thereby enhance the clinical prospects for gene therapy. Potential applications of gene therapy (review Crystal, [0390] Science 270:404-410 [1995]) include; 1) the treatment of many congenital metabolic disorders and immunodeficiencies (Kay and Woo, Trends Genet. 10:253-257 [1994]), 2) neurological disorders (Friedmann, Trends Genet. 10:210-214 [1994]), 3) cancer (Culver and Blaese, Trends Genet. 10:174-178 [1994]) and 4) infectious diseases (Gilboa and Smith, Trends Genet. 10:139-144 [1994]).
  • There are a variety of methods, known to those with skill in the art, for introducing genetic material into a host cell. A number of vectors, both viral and non-viral have been developed for transferring therapeutic genes into primary cells. Viral based vectors include; 1) replication deficient recombinant retrovirus (Boris-Lawrie and [0391] Temin, Curr. Opin. Genet. Dev. 3:102-109 [1993], Boris-Lawrie and Temin, Annal. New York Acad. Sci. 716:59-71 [1994], Miller, Current Top. Microbiol. Immunol. 158:1-24 [1992]) and replication-deficient recombinant adenovirus (Berkner, BioTechniques 6:616-629 [1988], Berkner, Current Top. Microbiol. Immunol. 158:39-66 [1992], Brody and Crystal, Annal. New York Acad. Sci. 716:90-103 [1994]). Non-viral based vectors include protein/DNA complexes (Cristiano et al., PNAS USA. 90:2122-2126 [1993], Curiel et al., PNAS USA 88:8850-8854 [1991], Curiel, Annal. New York Acad. Sci. 716:36-58 [1994]), electroporation and liposome mediated delivery such as cationic liposomes (Farhood et al., Annal. New York Acad. Sci. 716:23-35 [1994]).
  • The present invention provides an improvement to the existing methods of expanding hematopoietic cells, which new genetic material has been introduced, in that it provides methods utilizing multi-functional hematopoietic receptor agonist proteins that have improved biological activity, including an activity not seen by any single colony stimulation factor. [0392]
  • Many drugs may cause bone marrow suppression or hematopoietic deficiencies. Examples of such drugs are AZT, DDI, alkylating agents and anti-metabolites used in chemotherapy, antibiotics such as chloramphenicol, penicillin, gancyclovir, daunomycin and sulfa drugs, phenothiazones, tranquilizers such as meprobamate, analgesics such as aminopyrine and dipyrone, anti-convulsants such as phenyloin or carbamazepine, antithyroids such as propylthiouracil and methimazole and diuretics. The multi-functional hematopoietic receptor agonists of the present invention may be useful in preventing or treating the bone marrow suppression or hematopoietic deficiencies which often occur in patients treated with these drugs. [0393]
  • Hematopoietic deficiencies may also occur as a result of viral, microbial or parasitic infections and as a result of treatment for renal disease or renal failure, e.g., dialysis. The multi-functional hematopoietic receptor agonists of the present invention may be useful in treating such hematopoietic deficiencies. [0394]
  • The treatment of hematopoietic deficiency may include administration of a pharmaceutical composition containing the multi-functional hematopoietic receptor agonists to a patient. The multi-functional hematopoietic receptor agonists of the present invention may also be useful for the activation and amplification of hematopoietic precursor cells by treating these cells in vitro with the multi-functional hematopoietic receptor agonist proteins of the present invention prior to injecting the cells into a patient. [0395]
  • Various immunodeficiencies, e.g., in T and/or B lymphocytes, or immune disorders, e.g., rheumatoid arthritis, may also be beneficially affected by treatment with the multi-functional hematopoietic receptor agonists of the present invention. Immunodeficiencies may be the result of viral infections, e.g., HTLVI, HTLVII, HTLVIII, severe exposure to radiation, cancer therapy or the result of other medical treatment. The multi-functional hematopoietic receptor agonists of the present invention may also be employed, alone or in combination with other colony stimulating factors, in the treatment of other blood cell deficiencies, including thrombocytopenia (platelet deficiency), or anemia. Other uses for these novel polypeptides are the in vivo and ex vivo treatment of patients recovering from bone marrow transplants, and in the development of monoclonal and polyclonal antibodies generated by standard methods for diagnostic or therapeutic use. [0396]
  • Other aspects of the present invention are methods and therapeutic compositions for treating the conditions referred to above. Such compositions comprise a therapeutically effective amount of one or more of the multi-functional hematopoietic receptor agonists of the present invention in a mixture with a pharmaceutically acceptable carrier. This composition can be administered either parenterally, intravenously or subcutaneously. When administered, the therapeutic composition for use in this invention is preferably in the form of a pyrogen-free, parenterally acceptable aqueous solution. The preparation of such a parenterally acceptable protein solution, having due regard to pH, isotonicity, stability and the like, is within the skill of the art. [0397]
  • The dosage regimen involved in a method for treating the above-described conditions will be determined by the attending physician considering various factors which modify the action of drugs, e.g., the condition, body weight, sex and diet of the patient, the severity of any infection, time of administration and other clinical factors. Generally, a daily regimen may be in the range of 0.2-150 μg/kg of multi-functional hematopoietic receptor agonist protein per kilogram of body weight. Dosages would be adjusted relative to the activity of a given multi-functional hematopoietic receptor agonist protein and it would not be unreasonable to note that dosage regimens may include doses as low as 0.1 microgram and as high as 1 milligram per kilogram of body weight per day. In addition, there may exist specific circumstances where dosages of multi-functional hematopoietic receptor agonist would be adjusted higher or lower than the range of 0.2-150 micrograms per kilogram of body weight. These include co-administration with other colony stimulating factors or IL-3 variants or growth factors; co-administration with chemotherapeutic drugs and/or radiation; the use of glycosylated multi-functional hematopoietic receptor agonist protein; and various patient-related issues mentioned earlier in this section. As indicated above, the therapeutic method and compositions may also include co-administration with other human factors. A non-exclusive list of other appropriate colony stimulating factors (CSFs), cytokines, lymphokines, hematopoietic growth factors and interleukins for simultaneous or serial co-administration with the polypeptides of the present invention includes GM-CSF, G-CSF, c-mpl ligand (also known as TPO or MGDF), M-CSF, erythropoietin (EPO), IL-1, IL-4, IL-2, IL-3, IL-5, IL-6, IL-7, IL-8, IL-9, IL-10, IL-11, IL-12, IL-13, IL-15, IL-16, LIF, flt3 ligand, and stem cell factor (SCF) also known as steel factor or c-kit ligand, or combinations thereof. The dosage recited above would be adjusted to compensate for such additional components in the therapeutic composition. Progress of the treated patient can be monitored by periodic assessment of the hematological profile, e.g., differential cell count and the like. [0398]
    • Materials and Methods
  • Unless noted otherwise, all specialty chemicals were obtained from Sigma, Co. (St. Louis, Mo.). Restriction endonucleases and T4 DNA ligase were obtained from New England Biolabs (Beverly, Mass.) or Boehringer Mannheim (Indianapolis, Ind.). [0399]
    • Transformation of E. Coli Strains
  • [0400] E. coli strains, such as DH5á™ (Life Technologies, Gaithersburg, Md.) and TG1 (Amersham Corp., Arlington Heights, Ill.) are used for transformation of ligation reactions and are the source of plasmid DNA for transfecting mammalian cells. E. coli strains, such as JM101 (Yanisch-Perron, et al., Gene, 33: 103-119, 1985) and MON1O5 (Obukowicz, et al., Appl. and Envir. Micr., 58: 1511-1523, 1992) can be used for expressing the multi-functional hematopoietic receptor agonist of the present invention in the cytoplasm or periplasmic space.
  • MON105 ATCC#55204: F—, lambda-,IN(rrnD, rrE)1, rpoD+, rpoH358 [0401]
  • DH5á™: F—, phi80dlacZdeltaM15, delta(lacZYA-argF)U169, deoR, recA1, endA1, hsdR17(rk−, mk+), phoA, supE44lamda-, thi-1, gyrA96, relA1 [0402]
  • TG1: delta(lac-pro), supE, thi-1, hsdD5/F′(traD36, proA+B+, lacIq, lacZdeltaM15) [0403]
  • JM101 ATCC#33876: delta (pro lac), supE, thi, F′(traD36, proA+B+, lacIq, lacZdeltaM15) [0404]
  • DH5á™ Subcloning efficiency cells are purchased as competent cells and are ready for transformation using the manufacturer's protocol, while both [0405] E. coli strains TG1 and MON1O5 are rendered competent to take up DNA using a CaCl2 method. Typically, 20 to 50 mL of cells are grown in LB medium (1% bacto-tryptone, 0.5% bacto-yeast extract, 150 mM NaCl) to a density of approximately 1.0 optical density unit at 600 nanometers (OD600) as measured by a Baush & Lomb Spectronic spectrophotometer (Rochester, N.Y.). The cells are collected by centrifugation and resuspended in one-fifth culture volume of CaCl2 solution (50 mM CaCl2, 10 mM Tris-Cl, pH7.4) and are held at 4° C. for 30 minutes. The cells are again collected by centrifugation and resuspended in one-tenth culture volume of CaCl2 solution. Ligated DNA is added to 0.2 mL of these cells, and the samples are held at 4° C. for 30-60 minutes. The samples are shifted to 42° C. for two minutes and 1.0 mL of LB is added prior to shaking the samples at 37° C. for one hour. Cells from these samples are spread on plates (LB medium plus 1.5% bacto-agar) containing either ampicillin (100 micrograms/mL, ug/mL) when selecting for ampicillin-resistant transformants, or spectinomycin (75 ug/mL) when selecting for spectinomycin-resistant transformants. The plates are incubated overnight at 37° C. Colonies are picked and inoculated into LB plus appropriate antibiotic (100 ug/mL ampicillin or 75 ug/mL spectinomycin) and are grown at 37° C. while shaking.
    • Methods For Creation of Genes
  • With New N-Terminus/C-Terminus [0406]
    • Method I Creation of Genes with New N-Terminus/C-Terminus Which Contain a Linker Region (L2).
  • Genes with new N-terminus/C-terminus which contain a linker region (L[0407] 2) separating the original C-terminus and N-terminus can be made essentially following the method described in L. S. Mullins, et al J. Am. Chem. Soc. 116, 5529-5533, 1994). Multiple steps of polymerase chain reaction (PCR) amplifications are used to rearrange the DNA sequence encoding the primary amino acid sequence of the protein. The steps are illustrated in FIG. 2.
  • In the first step, the first primer set (“new start” and “linker start”) is used to create and amplify, from the original gene sequence, the DNA fragment (“Fragment Start”) that contains the sequence encoding the new N-terminal portion of the new protein followed by the linker (L[0408] 2) that connects the C-terminal and N-terminal ends of the original protein. In the second step, the second primer set (“new stop” and “linker stop”) is used to create and amplify, from the original gene sequence, the DNA fragment (“Fragment Stop”) that encodes the same linker as used above, followed by the new C-terminal portion of the new protein. The “new start” and “new stop” primers are designed to include the appropriate restriction sites which allow cloning of the new gene into expression plasmids. Typical PCR conditions are one cycle 95° C. melting for two minutes; 25 cycles 94° C. denaturation for one minute, 50° C. annealing for one minute and 72° C. extension for one minute; plus one cycle 72° C. extension for seven minutes. A Perkin Elmer GeneAmp PCR Core Reagents kit is used. A 100 ul reaction contains 100 pmole of each primer and one ug of template DNA; and 1×PCR buffer, 200 uM dGTP, 200 uM dATP, 200 uM dTTP, 200 uM dCTP, 2.5 units AmpliTaq DNA polymerase and 2 mM MgCl2. PCR reactions are performed in a Model 480 DNA thermal cycler (Perkin Elmer Corporation, Norwalk, Conn.).
  • “Fragment Start” and “Fragment Stop”, which have complementary sequence in the linker region and the coding sequence for the two amino acids on both sides of the linker, are joined together in a third PCR step to make the full-length gene encoding the new protein. The DNA fragments “Fragment Start” and “Fragment Stop” are resolved on a 1% TAE gel, stained with ethidium bromide and isolated using a Qiaex Gel Extraction kit (Qiagen). These fragments are combined in equimolar quantities, heated at 70° C. for ten minutes and slow cooled to allow annealing through their shared sequence in “linker start” and “linker stop”. In the third PCR step, primers “new start” and “new stop” are added to the annealed fragments to create and amplify the full-length new N-terminus/C-terminus gene. Typical PCR conditions are one cycle 95° C. melting for two minutes; 25 cycles 94° C. denaturation for one minute, 60° C. annealing for one minute and 72° C. extension for one minute; plus one cycle 72° C. extension for seven minutes. A Perkin Elmer GeneAmp PCR Core Reagents kit is used. A 100 ul reaction contains 100 pmole of each primer and approximately 0.5 ug of DNA; and 1×PCR buffer, 200 uM dGTP, 200 uM dATP, 200 uM dTTP, 200 uM dCTP, 2.5 units AmpliTaq DNA polymerase and 2 mM MgCl2. PCR reactions are purified using a Wizard PCR Preps kit (Promega). [0409]
    • Method II Creation of Genes with New N-Terminus/C-Terminus Without a Linker Region
  • New N-terminus/C-terminus genes without a linker joining the original N-terminus and C-terminus can be made using two steps of PCR amplification and a blunt end ligation. The steps are illustrated in FIG. 3. In the first step, the primer set (“new start” and “P-bl start”) is used to create and amplify, from the original gene sequence, the DNA fragment (“Fragment Start”) that contains the sequence encoding the new N-terminal portion of the new protein. In the second step, the primer set (“new stop” and “P-bl stop”) is used to create and amplify, from gene sequence, the DNA fragment (“Fragment Stop”) that contains the sequence encoding the new C-terminal portion of the new protein. The “new start” and “new stop” primers are designed to include appropriate restriction sites which allow cloning of the new gene into expression vectors. Typical PCR conditions are one cycle 95° C. melting for two minutes; 25 cycles 94° C. denaturation for one minute, 50° C. annealing for 45 seconds and 72° C. extension for 45 seconds. Deep Vent polymerase (New England Biolabs) is used to reduce the occurrence of overhangs in conditions recommended by the manufacturer. The “P-bl start” and “P-bl stop” primers are phosphorylated at the 5′ end to aid in the subsequent blunt end ligation of “Fragment Start” and “Fragment Stop” to each other. A 100 ul reaction contained 150 pmole of each primer and one ug of template DNA; and 1×Vent buffer (New England Biolabs), 300 uM dGTP, 300 uM dATP, 300 uM dTTP, 300 uM dCTP, and 1 unit Deep Vent polymerase. PCR reactions are performed in a Model 480 DNA thermal cycler (Perkin Elmer Corporation, Norwalk, Conn.). PCR reaction products are purified using a Wizard PCR Preps kit (Promega). [0410]
  • The primers are designed to include appropriate restriction sites which allow for the cloning of the new gene into expression vectors. Typically “Fragment Start” is designed to create NcoI restriction site, and “Fragment Stop” is designed to create a HindIII restriction site. Restriction digest reactions are purified using a Magic DNA Clean-up System kit (Promega). Fragments Start and Stop are resolved on a 1% TAE gel, stained with ethidium bromide and isolated using a Qiaex Gel Extraction kit (Qiagen). These fragments are combined with and annealed to the ends of the ˜3800 base pair NcoI/HindIII vector fragment of pMON3934 by heating at 50° C. for ten minutes and allowed to slow cool. The three fragments are ligated together using T4 DNA ligase (Boehringer Mannheim). The result is a plasmid containing the full-length new N-terminus/C-terminus gene. A portion of the ligation reaction is used to transform [0411] E. coli strain DH5á cells (Life Technologies, Gaithersburg, Md.). Plasmid DNA is purified and sequence confirmed as below.
    • Method III Creation of New N-Terminus/C-Terminus Genes by Tandem-Duplication Method
  • New N-terminus/C-terminus genes can be made based on the method described in R. A. Horlick, et al [0412] Protein Eng. 5:427-431, 1992). Polymerase chain reaction (PCR) amplification of the new N-terminus/C-terminus genes is performed using a tandemly duplicated template DNA. The steps are illustrated in FIG. 3.
  • The tandemly-duplicated template DNA is created by cloning and contains two copies of the gene separated by DNA sequence encoding a linker connecting the original C- and N-terminal ends of the two copies of the gene. Specific primer sets are used to create and amplify a full-length new N terminus/C-terminus gene from the tandemly-duplicated template DNA. These primers are designed to include appropriate restriction sites which allow for the cloning of the new gene into expression vectors. Typical PCR conditions are one cycle 95° C. melting for two minutes; 25 cycles 94° C. denaturation for one minute, 50° C. annealing for one minute and 72° C. extension for one minute; plus one cycle 72° C. extension for seven minutes. A Perkin Elmer GeneAmp PCR Core Reagents kit (Perkin Elmer Corporation, Norwalk, Conn.) is used. A 100 ul reaction contains 100 pmole of each primer and one ug of template DNA; and 1×PCR buffer, 200 uM dGTP, 200 uM dATP, 200 uM dTTP, 200 uM dCTP, 2.5 units AmpliTaq DNA polymerase and 2 mM MgCl[0413] 2. PCR reactions are performed in a Model 480 DNA thermal cycler (Perkin Elmer Corporation, Norwalk, Conn.). PCR reactions are purified using a Wizard PCR Preps kit (Promega).
    • Cloning of New N-Terminus/C-Terminus Genes Into Multi-Functional Receptor Agonist Expression Vectors
  • The new N-terminus/C-terminus gene is digested with restriction endonucleases to create ends that are compatible to insertion into an expression vector containing another colony stimulating factor gene. This expression vector is likewise digested with restriction endonucleases to form compatible ends. After purification, the gene and the vector DNAs are combined and ligated using T4 DNA ligase. A portion of the ligation reaction is used to transform [0414] E. coli. Plasmid DNA is purified and sequenced to confirm the correct insert. The correct clones are grown for protein expression.
    • DNA Isolation and Characterization
  • Plasmid DNA can be isolated by a number of different methods and using commercially available kits known to those skilled in the art. A few such methods are shown herein. Plasmid DNA is isolated using the Promega Wizard™ Miniprep kit (Madison, Wis.), the Qiagen QIAwell Plasmid isolation kits (Chatsworth, Calif.) or Qiagen Plasmid Midi kit. These kits follow the same general procedure for plasmid DNA isolation. Briefly, cells are pelleted by centrifugation (5000×g), plasmid DNA released with sequential NaOH/acid treatment, and cellular debris is removed by centrifugation (10000×g). The supernatant (containing the plasmid DNA) is loaded onto a column containing a DNA-binding resin, the column is washed, and plasmid DNA eluted with TE. After screening for the colonies with the plasmid of interest, the [0415] E. coli cells are inoculated into 50-100 mls of LB plus appropriate antibiotic for overnight growth at 37° C. in an air incubator while shaking. The purified plasmid DNA is used for DNA sequencing, further restriction enzyme digestion, additional subcloning of DNA fragments and transfection into mammalian, E. coli or other cells.
    • Sequence Confirmation
  • Purified plasmid DNA is resuspended in dH[0416] 2O and quantitated by measuring the absorbance at 260/280 nm in a Bausch and Lomb Spectronic 601 UV spectrometer. DNA samples are sequenced using ABI PRISM™ DyeDeoxy™ terminator sequencing chemistry (Applied Biosystems Division of Perkin Elmer Corporation, Lincoln City, Calif.) kits (Part Number 401388 or 402078) according to the manufacturers suggested protocol usually modified by the addition of 5% DMSO to the sequencing mixture. Sequencing reactions are performed in a Model 480 DNA thermal cycler (Perkin Elmer Corporation, Norwalk, Conn.) following the recommended amplification conditions. Samples are purified to remove excess dye terminators with Centri-Sep™ spin columns (Princeton Separations, Adelphia, N.J.) and lyophilized. Fluorescent dye labeled sequencing reactions are resuspended in deionized formamide, and sequenced on denaturing 4.75% polyacrylamide-8M urea gels using an ABI Model 373A automated DNA sequencer. Overlapping DNA sequence fragments are analyzed and assembled into master DNA contigs using Sequencher v2.1 DNA analysis software (Gene Codes Corporation, Ann Arbor, Mich.).
    • Expression of Multi-Functional Receptor Agonists in Mammalian Cells
  • Mammalian Cell Transfection/Production of Conditioned Media [0417]
  • The BHK-21 cell line can be obtained from the ATCC (Rockville, Md.). The cells are cultured in Dulbecco's modified Eagle media (DMEM/high-glucose), supplemented to 2 mM (mM) L-glutamine and 10% fetal bovine serum (FBS). This formulation is designated BHK growth media. Selective media is BHK growth media supplemented with 453 units/mL hygromycin B (Calbiochem, San Diego, Calif.). The BHK-21 cell line was previously stably transfected with the HSV transactivating protein VP16, which transactivates the IE110 promoter found on the plasmid pMON3359 (See Hippenmeyer et al., [0418] Bio/Technology, pp.1037-1041, 1993). The VP16 protein drives expression of genes inserted behind the IE110 promoter. BHK-21 cells expressing the transactivating protein VP16 are designated BHK-VP16. The plasmid pMON1118 (See Highkin et al., Poultry Sci., 70: 970-981, 1991) expresses the hygromycin resistance gene from the SV40 promoter. A similar plasmid is available from ATCC, pSV2-hph.
  • BHK-VP16 cells are seeded into a 60 millimeter (mm) tissue culture dish at 3×10[0419] 5 cells per dish 24 hours prior to transfection. Cells are transfected for 16 hours in 3 mL of “OPTIMEM”™ (Gibco-BRL, Gaithersburg, Md.) containing 10 ug of plasmid DNA containing the gene of interest, 3 ug hygromycin resistance plasmid, pMON1118, and 80 ug of Gibco-BRL “LIPOFECTAMINE”™ per dish. The media is subsequently aspirated and replaced with 3 mL of growth media. At 48 hours post-transfection, media from each dish is collected and assayed for activity (transient conditioned media). The cells are removed from the dish by trypsin-EDTA, diluted 1:10 and transferred to 100 mm tissue culture dishes containing 10 mL of selective media. After approximately 7 days in selective media, resistant cells grow into colonies several millimeters in diameter. The colonies are removed from the dish with filter paper (cut to approximately the same size as the colonies and soaked in trypsin/EDTA) and transferred to individual wells of a 24 well plate containing 1 mL of selective media. After the clones are grown to confluence, the conditioned media is re-assayed, and positive clones are expanded into growth media.
    • Expression of Multi-Functional Receptor Agonists in E. Coli
  • [0420] E. coli strain MON1O5 or JM101 harboring the plasmid of interest are grown at 37° C. in M9 plus casamino acids medium with shaking in a air incubator Model G25 from New Brunswick Scientific (Edison, N.J.). Growth is monitored at OD600 until it reaches a value of 1.0 at which time Nalidixic acid (10 milligrams/mL) in 0.1 N NaOH is added to a final concentration of 50 μg/mL. The cultures are then shaken at 37° C. for three to four additional hours. A high degree of aeration is maintained throughout culture period in order to achieve maximal production of the desired gene product. The cells are examined under a light microscope for the presence of inclusion bodies (IB). One mL aliquots of the culture are removed for analysis of protein content by boiling the pelleted cells, treating them with reducing buffer and electrophoresis via SDS-PAGE (see Maniatis et al. Molecular Cloning: A Laboratory Manual, 1982). The culture is centrifuged (5000×g) to pellet the cells.
    • Inclusion Body preparation, Extraction, Refolding, Dialysis, DEAE Chromatography, and Characterization of the Multi-Functional Hematopoietic Receptor Agonists Which Accumulate as Inclusion Bodies in E. Coli Isolation of Inclusion Bodies
  • The cell pellet from a 330 mL [0421] E. coli culture is resuspended in 15 mL of sonication buffer (10 mM 2-amino-2-(hydroxymethyl) 1,3-propanediol hydrochloride (Tris-HCl), pH 8.0+1 mM ethylenediaminetetraacetic acid (EDTA). These resuspended cells are sonicated using the microtip probe of a Sonicator Cell Disruptor (Model W-375, Heat Systems-Ultrasonics, Inc., Farmingdale, New York). Three rounds of sonication in sonication buffer followed by centrifugation are employed to disrupt the cells and wash the inclusion bodies (IB). The first round of sonication is a 3 minute burst followed by a 1 minute burst, and the final two rounds of sonication are for 1 minute each.
    • Extraction and Refolding of Proteins from Inclusion Body Pellets
  • Following the final centrifugation step, the IB pellet is resuspended in 10 mL of 50 mM Tris-HCl, pH 9.5, 8 M urea and 5 mM dithiothreitol (DTT) and stirred at room temperature for approximately 45 minutes to allow for denaturation of the expressed protein. [0422]
  • The extraction solution is transferred to a beaker containing 70 mL of 5 mM Tris-HCl, pH 9.5 and 2.3 M urea and gently stirred while exposed to air at 4° C. for 18 to 48 hours to allow the proteins to refold. Refolding is monitored by analysis on a Vydac (Hesperia, Ca.) C18 reversed phase high pressure liquid chromatography (RP-HPLC) column (0.46×25 cm). A linear gradient of 40% to 65% acetonitrile, containing 0.1% trifluoroacetic acid (TFA), is employed to monitor the refold. This gradient is developed over 30 minutes at a flow rate of 1.5 mL per minute. Denatured proteins generally elute later in the gradient than the refolded proteins. [0423]
    • Purification
  • Following the refold, contaminating [0424] E. coli proteins are removed by acid precipitation. The pH of the refold solution is titrated to between pH 5.0 and pH 5.2 using 15% (v/v) acetic acid (HOAc). This solution is stirred at 4° C. for 2 hours and then centrifuged for 20 minutes at 12,000×g to pellet any insoluble protein.
  • The supernatant from the acid precipitation step is dialyzed using a Spectra/[0425] Por 3 membrane with a molecular weight cut off (MWCO) of 3,500 daltons. The dialysis is against 2 changes of 4 liters (a 50-fold excess) of 10 mM Tris-HCl, pH 8.0 for a total of 18 hours. Dialysis lowers the sample conductivity and removes urea prior to DEAE chromatography. The sample is then centrifuged (20 minutes at 12,000×g) to pellet any insoluble protein following dialysis.
  • A Bio-Rad Bio-Scale DEAE2 column (7×52 mm) is used for ion exchange chromatography. The column is equilibrated in a buffer containing 10 mM Tris-HCl, pH 8.0, and a 0-to-500 mM sodium chloride (NaCl) gradient, in equilibration buffer, over 45 column volumes is used to elute the protein. A flow rate of 1.0 mL per minute is used throughout the run. Column fractions (2.0 mL per fraction) are collected across the gradient and analyzed by RP HPLC on a Vydac (Hesperia, Ca.) C18 column (0.46×25 cm). A linear gradient of 40% to 65% acetonitrile, containing 0.1% trifluoroacetic acid (TFA), is employed. This gradient is developed over 30 minutes at a flow rate of 1.5 mL per minute. Pooled fractions are then dialyzed against 2 changes of 4 liters (50-to-500-fold excess) of 10 mM ammonium acetate (NH4Ac), pH 4.0 for a total of 18 hours. Dialysis is performed using a Spectra/[0426] Por 3 membrane with a MWCO of 3,500 daltons. Finally, the sample is sterile filtered using a 0.22 μm syringe filter (μStar LB syringe filter, Costar, Cambridge, Ma.), and stored at 4° C.
  • In some cases the folded proteins can be affinity purified using affinity reagents such as mabs or receptor subunits attached to a suitable matrix. Alternatively, (or in addition) purification can be accomplished using any of a variety of chromatographic methods such as: ion exchange, gel filtration or hydrophobic chromatography or reversed phase HPLC. [0427]
  • These and other protein purification methods are described in detail in Methods in Enzymology, Volume 182 ‘Guide to Protein Purification’ edited by Murray Deutscher, Academic Press, San Diego, Calif. (1990). [0428]
    • Protein Characterization
  • The purified protein is analyzed by RP-HPLC, electrospray mass spectrometry, and SDS-PAGE. The protein quantitation is done by amino acid composition, RP-HPLC, and Bradford protein determination. In some cases tryptic peptide mapping is performed in conjunction with electrospray mass spectrometry to confirm the identity of the protein. [0429]
    • AML Proliferation Assay for Bioactive Human Interleukin-3
  • The factor-dependent cell line AML 193 was obtained from the American Type Culture Collection (ATCC, Rockville, Md.). This cell line, established from a patient with acute myelogenous leukemia, is a growth factor dependent cell line which displayed enhanced growth in GM-CSF supplemented medium (Lange, B., et al., [0430] Blood 70: 192, 1987; Valtieri, M., et al., J. Immunol. 138:4042, 1987). The ability of AML 193 cells to proliferate in the presence of human IL-3 has also been documented. (Santoli, D., et al., J. Immunol. 139: 348, 1987). A cell line variant was used, AML 193 1.3, which was adapted for long term growth in IL-3 by washing out the growth factors and starving the cytokine dependent AML 193 cells for growth factors for 24 hours. The cells are then replated at 1×105 cells/well in a 24 well plate in media containing 100 U/mL IL-3. It took approximately 2 months for the cells to grow rapidly in IL-3. These cells are maintained as AML 193 1.3 thereafter by supplementing tissue culture medium (see below) with human IL-3.
  • AML 193 1.3 cells are washed 6 times in cold Hanks balanced salt solution (HBSS, Gibco, Grand Island, N.Y.) by centrifuging cell suspensions at 250×g for 10 minutes followed by decantation of the supernatant. Pelleted cells are resuspended in HBSS and the procedure is repeated until six wash cycles are completed. Cells washed six times by this procedure are resuspended in tissue culture medium at a density ranging from 2×10[0431] 5 to 5×105 viable cells/mL. This medium is prepared by supplementing Iscove's modified Dulbecco's Medium (IMDM, Hazelton, Lenexa, Kans.) with albumin, transferrin, lipids and 2-mercaptoethanol. Bovine albumin (Boehringer-Mannheim, Indianapolis, Ind.) is added at 500 μg/mL; human transferrin (Boehringer-Mannheim, Indianapolis, Ind.) is added at 100 μg/mL; soybean lipid (Boehringer-Mannheim, Indianapolis, Ind.) is added at 50 μg/mL; and 2-mercaptoethanol (Sigma, St. Louis, Mo.) is added at 5×10−5 M.
  • Serial dilutions of human interleukin-3 or multi-functional hematopoietic receptor agonist proteins are made in triplicate series in tissue culture medium supplemented as stated above in 96 well Costar 3596 tissue culture plates. Each well contained 50 μl of medium containing interleukin-3 or multi-functional hematopoietic receptor agonist proteins once serial dilutions are completed. Control wells contained tissue culture medium alone (negative control). AML 193 1.3 cell suspensions prepared as above are added to each well by pipetting 50 μl (2.5×10[0432] 4 cells) into each well. Tissue culture plates are incubated at 37° C. with 5% CO2 in humidified air for 3 days. On day 3, 0.5 μCi 3H-thymidine (2 Ci/mM, New England Nuclear, Boston, Mass.) is added in 50 μl of tissue culture medium. Cultures are incubated at 37° C. with 5% CO2 in humidified air for 18-24 hours. Cellular DNA is harvested onto glass filter mats (Pharmacia LKB, Gaithersburg, Md.) using a TOMTEC cell harvester (TOMTEC, Orange, Conn.) which utilized a water wash cycle followed by a 70% ethanol wash cycle. Filter mats are allowed to air dry and then placed into sample bags to which scintillation fluid (Scintiverse II, Fisher Scientific, St. Louis, Mo. or BetaPlate Scintillation Fluid, Pharmacia LKB, Gaithersburg, Md.) is added. Beta emissions of samples from individual tissue culture wells are counted in a LKB BetaPlate model 1205 scintillation counter (Pharmacia LKB, Gaithersburg, Md.) and data is expressed as counts per minute of 3H-thymidine incorporated into cells from each tissue culture well. Activity of each human interleukin-3 preparation or multi-functional hematopoietic receptor agonist protein preparation is quantitated by measuring cell proliferation (3H-thymidine incorporation) induced by graded concentrations of interleukin-3 or multi-functional hematopoietic receptor agonist. Typically, concentration ranges from 0.05 pM-105 pM are quantitated in these assays. Activity is determined by measuring the dose of interleukin-3 or multi-functional hematopoietic receptor agonist protein which provides 50% of maximal proliferation (EC50=0.5×(maximum average counts per minute of 3H-thymidine incorporated per well among triplicate cultures of all concentrations of interleukin-3 tested—background proliferation measured by 3H-thymidine incorporation observed in triplicate cultures lacking interleukin-3). This EC50 value is also equivalent to 1 unit of bioactivity. Every assay is performed with native interleukin-3 as a reference standard so that relative activity levels could be assigned.
  • Typically, the multi-functional hematopoietic receptor agonist proteins were tested in a concentration range of 2000 pM to 0.06 pM titrated in serial 2 fold dilutions. [0433]
  • Activity for each sample was determined by the concentration which gave 50% of the maximal response by fitting a four-parameter logistic model to the data. It was observed that the upper plateau (maximal response) for the sample and the standard with which it was compared did not differ. Therefore relative potency calculation for each sample was determined from EC50 estimations for the sample and the standard as indicated above. AML 193.1.3 cells proliferate in response to hIL-3, hGM-CSF and hG-CSF. Therefore the following additional assays were performed for some samples to demonstrate that the G-CSF receptor agonist portion of the multi-functional hematopoietic receptor agonist proteins was active. The proliferation assay was performed with the multi-functional hematopoietic receptor agonist plus and minus neutralizing monoclonal antibodies to the hIL-3 receptor agonist portion. In addition, a fusion molecule with the factor Xa cleavage site was cleaved then purified and the halves of the molecule were assayed for proliferative activity. These experiments showed that both components of the multi-functional hematopoietic receptor agonist proteins were active. [0434]
    • TF1 c-mpl Ligand Dependent Proliferation Assay
  • The c-mpl ligand proliferative activity can be assayed using a subclone of the pluripotential human cell line TF1 (Kitamura et al., J. Cell Physiol 140:323-334. [1989]). TF1 cells are maintained in h-IL3 (100 U/mL). To establish a sub-clone responsive to c-mpl ligand, cells are maintained in passage media containing 10% supernatant from BHK cells transfected with the gene expressing the 1-153 form of c-mpl ligand (pMON26448). Most of the cells die, but a subset of cells survive. After dilution cloning, a c-mpl ligand responsive clone is selected, and these cells are split into passage media to a density of 0.3×10[0435] 6 cells/mL the day prior to assay set-up. Passage media for these cells is the following: RPMI 1640 (Gibco), 10% FBS (Harlan, Lot #91206), 10% c-mpl ligand supernatant from transfected BHK cells, 1 mM sodium pyruvate (Gibco), 2 mM glutamine (Gibco), and 100 ug/mL penicillin-streptomycin (Gibco). The next day, cells are harvested and washed twice in RPMI or IMDM media with a final wash in the ATL, or assay media. ATL medium consists of the following:IMDM (Gibco), 500 ug/mL of bovine serum albumin, 100 ug/mL of human transferrin, 50 ug/mL soybean lipids, 4×10-8M beta-mercaptoethanol and 2 mL of A9909 (Sigma, antibiotic solution) per 1000 mL of ATL. Cells are diluted in assay media to a final density of 0.25×106 cells/mL in a 96-well low evaporation plate (Costar) to a final volume of 50 ul. Transient supernatants (conditioned media) from transfected clones are added at a volume of 50 ul as duplicate samples at a final concentration of 50% and diluted three-fold to a final dilution of 1.8%. Triplicate samples of a dose curve of IL-3 variant pMON13288 starting at 1 ng/mL and diluted using three-fold dilutions to 0.0014 ng/mL is included as a positive control. Plates are incubated at 5% CO2 and 37° C. At day six of culture, the plate is pulsed with 0.5 Ci of 3H/well (NEN) in a volume of 20 ul/well and allowed to incubate at 5% CO2 and 37° C. for four hours. The plate is harvested and counted on a Betaplate counter.
    • Other In Vitro Cell Based Proliferation Assays
  • Other in vitro cell based assays, known to those skilled in the art, may also be useful to determine the activity of the multi-functional hematopoietic receptor agonists depending on the factors that comprise the molecule in a similar manner as described in the AML 193.1.3 cell proliferation assay. The following are examples of other useful assays. [0436]
  • TF1 proliferation assay: TF1 is a pluripotential human cell line (Kitamura et al., J. Cell Physiol 140:323-334. [1989]) that responds to hIL-3. [0437]
  • 32D proliferation assay: 32D is a murine IL-3 dependent cell line which does not respond to human IL-3 but does respond to human G-CSF which is not species restricted. [0438]
  • Baf/3 proliferation assay: Baf/3 is a murine IL-3 dependent cell line which does not respond to human IL-3 or human c-mpl ligand but does respond to human G-CSF which is not species restricted. [0439]
  • T1165 proliferation assay: T1165 cells are a IL-6 dependent murine cell line (Nordan et al., 1986) which respond to IL-6 and IL-11. [0440]
  • Human Plasma Clot meg-CSF Assay: Used to assay megakaryocyte colony formation activity (Mazur et al., 1981). [0441]
    • Transfected Cell Lines
  • Cell lines such as the murine Baf/3 cell line can be transfected with a colony stimulating factor receptor, such as the human G-CSF receptor or human c-mpl receptor, which the cell line does not have. These transfected cell lines can be used to determine the activity of the ligand for which the receptor has been transfected into the cell line. [0442]
  • One such transfected Baf/3 cell line was made by cloning the cDNA encoding c-mpl from a library made from a c-mpl responsive cell line and cloned into the multiple cloning site of the plasmid pcDNA3 (Invitrogen, San Diego Calif.). Baf/3 cells were transfected with the plasmid via electroporation. The cells were grown under G418 selection in the presence of mouse IL-3 in Wehi conditioned media. Clones were established through limited dilution. [0443]
  • In a similar manner the human G-CSF receptor can be transfected into the Baf/3 cell line and used to determine the bioactivity of the multi-functional hematopoietic receptor agoinsts. [0444]
  • Analysis of c-mpl Ligand Proliferative Activity [0445]
  • Methods [0446]
  • 1. Bone Marrow Proliferation Assay [0447]
  • a. CD34+ Cell Purification: [0448]
  • Bone marrow aspirates (15-20 mL) were obtained from normal allogeneic marrow donors after informed consent. Cells were diluted 1:3 in phosphate buffered saline (PBS, Gibco-BRL), 30 mL were layered over 15 mL Histopaque-1077 (Sigma) and centrifuged for 30 minutes at 300 RCF. The mononuclear interface layer was collected and washed in PBS. CD34+ cells were enriched from the mononuclear cell preparation using an affinity column per manufacturers instructions (CellPro, Inc, Bothell Wash.). After enrichment, the purity of CD34+ cells was 70% on average as determined by using flow cytometric analysis using anti-CD34 monoclonal antibody conjugated to fluorescein and anti-CD38 conjugated to phycoerythrin (Becton Dickinson, San Jose Calif.). [0449]
  • Cells were resuspended at 40,000 cells/mL in X-Vivo 10 media (Bio-Whittaker, Walkersville, Md.) and 1 mL was plated in 12-well tissue culture plates (Costar). The growth factor rhIL-3 was added at 100 ng/mL (pMON5873) was added to some wells. hIL3 variants were used at 10 ng/mL to 100 ng/mL. Conditioned media from BHK cells transfected with plasmid encoding c-mpl ligand or multi-functional hematopoietic receptor agonists were tested by addition of 100 μl of supernatant added to 1 mL cultures (approximately a 10% dilution). Cells were incubated at 37° C. for 8-14 days at 5% CO[0450] 2 in a 37° C. humidified incubator.
  • b. Cell Harvest and Analysis: [0451]
  • At the end of the culture period a total cell count was obtained for each condition. For fluorescence analysis and ploidy determination cells were washed in megakaryocyte buffer (MK buffer, 13.6 mM sodium citrate, 1 mM theophylline, 2.2 μm PGE1, 11 mM glucose, 3% w/v BSA, in PBS, pH 7.4,) (Tomer et al., [0452] Blood 70: 1735-1742, 1987) resuspended in 500 μl of MK buffer containing anti-CD41a FITC antibody (1:200, AMAC, Westbrook, Me.) and washed in MK buffer. For DNA analysis cells were permeablized in MK buffer containing 0.5% Tween 20 (Fisher, Fair Lawn N.J.) for 20 min. on ice followed by fixation in 0.5% Tween-20 and 1% paraformaldehyde (Fisher Chemical) for 30 minutes followed by incubation in propidium iodide (Calbiochem, La Jolla Calif.) (50 μg/mL) with RNA-ase (400 U/mL) in 55% v/v MK buffer (200 mOsm) for 1-2 hours on ice. Cells were analyzed on a FACScan or Vantage flow cytometer (Becton Dickinson, San Jose, Calif.). Green fluorescence (CD41a-FITC) was collected along with linear and log signals for red fluorescence (PI) to determine DNA ploidy. All cells were collected to determine the percent of cells that were CD41+. Data analysis was performed using software by LYSIS (Becton Dickinson, San Jose, Calif.). Percent of cells expressing the CD41 antigen was obtained from flow cytometry analysis(Percent). Absolute (Abs) number of CD41+ cells/mL was calculated by: (Abs)=(Cell Count)*(Percent)/100.
  • 2. Megakaryocyte fibrin clot assay. CD34+ enriched population were isolated as described above. Cells were suspended at 25,000 cells/mL with or without cytokine(s) in a media consisting of a base Iscoves IMDM media supplemented with 0.3% BSA, 0.4 mg/mL apo-transferrin, 6.67 μM FeCl[0453] 2, 25 μg/mL CaCl2, 25 μg/mL L-asparagine, 500 μg/mL e-amino-n-caproic acid and penicillin/streptomycin. Prior to plating into 35 mm plates, thrombin was added (0.25 Units/mL) to initiate clot formation. Cells were incubated at 37° C. for 13 days at 5% CO2 in a 37° C. humidified incubator.
  • At the end of the culture period plates were fixed with methanol:acetone (1:3), air dried and stored at −200 C until staining. A peroxidase immunocytochemistry staining procedure was used (Zymed, Histostain-SP. San Francisco, Calif.) using a cocktail of primary monoclonal antibodies consisting of anti-CD41a, CD42 and CD61. Colonies were counted after staining and classified as negative, CFU-MK (small colonies, 1-2 foci and less that approx. 25 cells), BFU-MK (large, multi-foci colonies with >25 cells) or mixed colonies (mixture of both positive and negative cells. [0454]
    • Methylcellulose Assay
  • This assay reflects the ability of colony stimulating factors to stimulate normal bone marrow cells to produce different types of hematopoietic colonies in vitro (Bradley et al., [0455] Aust. Exp Biol. Sci. 44:287-300, 1966), Pluznik et al., J. Cell Comp. Physio 66:319-324, 1965).
  • Methods [0456]
  • Approximately 30 mL of fresh, normal, healthy bone marrow aspirate are obtained from individuals following informed consent. Under sterile conditions samples are diluted 1:5 with a 1×PBS (#14040.059 Life Technologies, Gaithersburg, Md.) solution in a 50 mL conical tube (#25339-50 Corning, Corning Md.). Ficoll (Histopaque 1077 Sigma H-8889) is layered under the diluted sample and centrifuged, 300×g for 30 min. The mononuclear cell band is removed and washed two times in 1×PBS and once with 1% BSA PBS (CellPro Co., Bothel, Wash.). Mononuclear cells are counted and CD34+ cells are selected using the Ceprate LC (CD34) Kit (CellPro Co., Bothel, Wash.) column. This fractionation is performed since all stem and progenitor cells within the bone marrow display CD34 surface antigen. [0457]
  • Cultures are set up in triplicate with a final volume of 1.0 mL in a 35×10 mm petri dish (Nunc#174926). Culture medium is purchased from Terry Fox Labs. (HCC-4230 medium (Terry Fox Labs, Vancouver, B.C., Canada) and erythropoietin (Amgen, Thousand Oaks, Calif.) is added to the culture media. 3,000-10,000 CD34+ cells are added per dish. Recombinant IL-3, purified from mammalian cells or [0458] E. coli, and multi-functional hematopoietic receptor agonist proteins, in conditioned media from transfected mammalian cells or purified from conditioned media from transfected mammalian cells or E. coli, are added to give final concentrations ranging from 0.001 nM to 10 nM. Recombinant hIL-3, GM-CSF, c-mpl ligand and multi-functional hematopoietic receptor agonist are supplied in house. G-CSF (Neupogen) is from Amgen (Thousand Oaks Calf.). Cultures are resuspended using a 3 cc syringe and 1.0 mL is dispensed per dish. Control (baseline response) cultures received no colony stimulating factors. Positive control cultures received conditioned media (PHA stimulated human cells: Terry Fox Lab. H2400). Cultures are incubated at 37° C., 5% CO2 in humidified air.
  • Hematopoietic colonies which are defined as greater than 50 cells are counted on the day of peak response (days 10-11) using a Nikon inverted phase microscope with a 40× objective combination. Groups of cells containing fewer than 50 cells are referred to as clusters. Alternatively colonies can be identified by spreading the colonies on a slide and stained or they can be picked, resuspended and spun onto cytospin slides for staining. [0459]
    • Human Cord Blood Hemopoietic Growth Factor Assays
  • Bone marrow cells are traditionally used for in vitro assays of hematopoietic colony stimulating factor (CSF) activity. However, human bone marrow is not always available, and there is considerable variability between donors. Umbilical cord blood is comparable to bone marrow as a source of hematopoietic stem cells and progenitors (Broxmeyer et al., [0460] PNAS USA 89:4109-113, 1992; Mayani et al., Blood 81:3252-3258, 1993). In contrast to bone marrow, cord blood is more readily available on a regular basis. There is also a potential to reduce assay variability by pooling cells obtained fresh from several donors, or to create a bank of cryopreserved cells for this purpose. By modifying the culture conditions, and/or analyzing for lineage specific markers, it is be possible to assay specifically for granulocyte/macrophage colonies (CFU-GM), for megakaryocyte CSF activity, or for high proliferative potential colony forming cell (HPP-CFC) activity.
  • Methods [0461]
  • Mononuclear cells (MNC) are isolated from cord blood within 24 hr. of collection, using a standard density gradient (1.077 g/mL Histopaque). Cord blood MNC have been further enriched for stem cells and progenitors by several procedures, including immunomagnetic selection for CD14-, CD34+ cells; panning for SBA-, CD34+ fraction using coated flasks from Applied Immune Science (Santa Clara, Calif.); and CD34+ selection using a CellPro (Bothell, Wash.) avidin column. Either freshly isolated or cryopreserved CD34+ cell enriched fractions are used for the assay. Duplicate cultures for each serial dilution of sample (concentration range from 1 pM to 1204 pM) are prepared with 1×10[0462] 4 cells in 1 ml of 0.9% methycellulose containing medium without additional growth factors (Methocult H4230 from Stem Cell Technologies, Vancouver, BC.). In some experiments, Methocult H4330 containing erythropoietin (EPO) was used instead of Methocult H4230, or Stem Cell Factor (SCF), 50 ng/mL (Biosource International, Camarillo, Calif.) was added. After culturing for 7-9 days, colonies containing>30 cells are counted. In order to rule out subjective bias in scoring, assays are scored blind.
  • Additional details about recombinant DNA methods which may be used to create the variants, express them in bacteria, mammalian cells or insect cells, purification and refold of the desired proteins and assays for determining the bioactivity of the proteins may be found in co-filed Applications WO 95/00646, WO 94/12639, WO 94/12638, WO 95/20976, WO 95/21197, WO 95/20977, WO 95/21254 and U.S. Ser. No. 08/383,035 which are hereby incorporated by reference in their entirety. Further details known to those skilled in the art may be found in T. Maniatis, et al., [0463] Molecular Cloning, A Laboratory Manual, Cold Spring Harbor Laboratory, 1982) and references cited therein, incorporated herein by reference; and in J. Sambrook, et al., Molecular Cloning, A Laboratory Manual, 2nd edition, Cold Spring Harbor Laboratory, 1989) and references cited therein, are incorporated herein by reference.
    TABLE 1
    OLIGONUCLEOTIDES
    c-mplNcoI
    ACGTCCATGGCNTCNCCNGCNCCNCCTGCTTGT (SEQ ID NO: 13)
    GCACTCCGAGTC
    N = A, C, G or T
    Ecompl
    ATGCACGAATTCCCTGACGCAGAGGGTGGA (SEQ ID NO: 14)
    c-mplHindIII
    TGACAAGCTTACCTGACGCAGAGGGTGGACCCT (SEQ ID NO: 15)
    4L-5′
    AATTCGGCAA (SEQ ID NO: 16)
    4L-3′
    CATGTTGCCG (SEQ ID NO: 17)
    5L-5′
    AATTCGGCGGCAA (SEQ ID NO: 18)
    5L-3′
    CATGTTGCCGCCG (SEQ ID NO: 19)
    8L-5′
    AATTCGGCGGCAACGGCGGCAA (SEQ ID NO: 20)
    8L-3′
    CATGTTGCCGCCGTTGCCGCCG (SEQ ID NO: 21)
    31-5′
    CGATCCATGGAGGTTCACCCTTTGCCT (SEQ ID NO: 22)
    31-3′
    GATCAAGCTTATGGGCACTGGCTCAGTCT (SEQ ID NO: 23)
    35-5′
    CGATACATGTTGCCTACACCTGTCCTG (SEQ ID NO: 24)
    35-3′
    GATCAAGCTTAAGGGTGAACCTCTGGGCA (SEQ ID NO: 25)
    39-5′
    CGATCCATGGTCCTGCTGCCTGCTGTG (SEQ ID NO: 26)
    39-3′
    GATCAAGCTTAAGGTGTAGGCAAAGGGTG (SEQ ID NO: 27)
    43-5′
    CGATCCATGGCTGTGGACTTTAGCTTGGGA (SEQ ID NO: 28)
    43-3′
    GATCAAGCTTAAGGCAGCAGGACAGGTGT (SEQ ID NO: 29)
    45-5′
    CGATCCATGGACTTTAGCTTGGGAGAA (SEQ ID NO: 30)
    45-3′
    GATCAAGCTTACACAGCAGGCAGCAGGAC (SEQ ID NO: 31)
    49-5′
    CGATCCATGGGAGAATGGAAAACCCAG (SEQ ID NO: 32)
    49-3′
    GATCAAGCTTACAAGCTAAAGTCCACAGC (SEQ ID NO: 33)
    82-5′
    CGATCCATGGGACCCACTTGCCTCTCA (SEQ ID NO: 34)
    82-3′
    GATCAAGCTTACAGTTGTCCCCGTGCTGC (SEQ ID NO: 35)
    109-5′
    CAGTCCATGGGAACCCAGCTTCCTCCA (SEQ ID NO: 36)
    109-3′
    GATCAAGCTTAAAGGAGGCTCTGCAGGGC (SEQ ID NO: 37)
    116-5′
    CGATCCATGGGCAGGACCACAGCTCAC (SEQ ID NO: 38)
    116-3′
    GATCAAGCTTACTGTGGAGGAAGCTGGGTT (SEQ ID NO: 39)
    120-5′
    CGATCCATGGCTCACAAGGATCCCAATGCC (SEQ ID NO: 40)
    120-3′
    GATCAAGCTTATGTGGTCCTGCCCTGTGG (SEQ ID NO: 41)
    123-5′
    CGATCCATGGATCCCAATGCCATCTTCCTG (SEQ ID NO: 42)
    123-3′
    GATCAAGCTTACTTGTGAGCTGTGGTCCT (SEQ ID NO: 43)
    126-5′
    CGATCCATGGCCATCTTCCTGAGCTTCCAA (SEQ ID NO: 44)
    126-3′
    GATCAAGCTTAATTGGGATCCTTGTGAGCTGT (SEQ ID NO: 45)
    SYNNOXA1.REQ
    AATTCCGTCG TAAACTGACC TTCTATCTGA (SEQ ID NO: 46)
    AAACCTTGGA GAACGCGCAG GCTCAACAGT
    ACGTAGAGGG CGGTGGAGGC TCC
    SYNNOXA2.REQ
    CCGGGGAGCC TCCACCGCCC TCTACGTACT (SEQ ID NO: 47)
    GTTGAGCCTG CGCGTTCTCC AAGGTTTTCA
    GATAGAAGGT CAGTTTACGA CGG
    L1syn.for
    GTTACCCTTG AGCAAGCGCA GGAACAACAG (SEQ ID NO: 48)
    GGTGGTGGCT CTAACTGCTC TATAATGAT
    L1syn.rev
    CGATCATTAT AGAGCAGTTA GAGCCACCAC (SEQ ID NO: 49)
    CCTGTTGTTC CTGCGCTTGC TCAAGG
    L3syn.for
    GTTACCCTTG AGCAAGCGCA GGAACAACAG (SEQ ID NO: 50)
    GGTGGTGGCT CTGGCGGTGG CAGCGGCGGC
    GGTTCTAACT GCTCTATAAT GAT
    L3syn.rev
    CGATCATTAT AGAGCAGTTA GAACCGCCGC (SEQ ID NO: 51)
    CGCTGCCACC GCCAGAGCCA CCACCCTGTT
    GTTCCTGCGC TTGCTCAAGG
    35start.seq
    GATCGACCAT GGCTCTGGAC CCGAACAACC (SEQ ID NO: 52)
    TC
    34rev.seq
    CTCGATTACG TACAAAGGTG CAGGTGGT (SEQ ID NO: 53)
    70start.seq
    GATCGACCAT GGCTAATGCA TCAGGTATTG (SEQ ID NO: 54)
    AG
    69rev.seq
    CTCGATTACG TATTCTAAGT TCTTGACA (SEQ ID NO: 55)
    91start.seq
    GATCGACCAT GGCTGCACCC TCTCGACATC (SEQ ID NO: 56)
    CA
    90rev.seq
    CTCGATTACG TAGGCCGTGG CAGAGGGC (SEQ ID NO: 57)
    101start.seq
    GATCGACCAT GGCTGCAGGT GACTGGCAAG (SEQ ID NO: 58)
    AA
    100rev.seq
    CTCGATTACG TACTTGATGA TGATTGGA (SEQ ID NO: 59)
    L-11start.seq
    GCTCTGAGAG CCGCCAGAGC CGCCAGAGGG (SEQ ID NO: 60)
    CTGCGCAAGG TGGCGTAGAA CGCG
    L-11stop.seq
    CAGCCCTCTG GCGGCTCTGG CGGCTCTCAG (SEQ ID NO: 61)
    AGCTTCCTGC TCAAGTCTTT AGAG
    P-blstart.seq
    GGGCTGCGCA AGGTGGCG (SEQ ID NO: 62)
    P-blstop.seq
    ACACCATTGG GCCCTGCCAG C (SEQ ID NO: 63)
    39start.seq
    GATCGACCAT GGCTTACAAG CTGTGCCACC (SEQ ID NO: 64)
    CC
    38stop.Seq
    CGATCGAAGC TTATTAGGTG GCACACAGCT (SEQ ID NO: 65)
    TCTCCT
    97start.seq
    GATCGACCAT GGCTCCCGAG TTGGGTCCCA (SEQ ID NO: 66)
    CC
    96stop.Seq
    CGATCGAAGC TTATTAGGAT ATCCCTTCCA (SEQ ID NO: 67)
    GGGCCT
    126start.seq
    GATCGACCAT GGCTATGGCC CCTGCCCTGC (SEQ ID NO: 68)
    AG
    125stop.Seq
    CGATCGAAGC TTATTATCCC AGTTCTTCCA (SEQ ID NO: 69)
    TCTGCT
    133start.seq
    GATCGACCAT GGCTACCCAG GGTGCCATGC (SEQ ID NO: 70)
    CG
    132stop.seq
    CGATCGAAGC TTATTAGGGC TGCAGGGCAG (SEQ ID NO: 71)
    GGGCCA
    142start.seq
    GATCGACCAT GGCTTCTGCT TTCCAGCGCC (SEQ ID NO: 72)
    GG
    141stop.Seq
    CGATCGAAGC TTATTAGGCG AAGGCCGGCA (SEQ ID NO: 73)
    TGGCAC
    GLYXA1
    GTAGAGGGCG GTGGAGGCTC C (SEQ ID NO: 74)
    GLYXA2
    CCGGGGAGCC TCCACCGCCC TCTAC (SEQ ID NO: 75)
    1GGGSfor
    TTCTACGCCA CCTTGCGCAG CCCGGCGGCG (SEQ ID NO: 76)
    GCTCTGACAT GTCTACACCA TTG
    1GGGSrev
    CAATGGTGTA GACATGTCAG AGCCGCCGCC (SEQ ID NO: 77)
    GGGCTGCGCA AGGTGGCGTA GAA
    Synnoxa1.req
    AATTCCGTCG TAAACTGACC TTCTATCTGA (SEQ ID NO: 240)
    AAACCTTGGA GAACGCGCAG GCTCAACAGT
    ACGTAGAGGG CGGTGGAGGC TCC
    Synnoxa2.req
    CCGGGGAGCC TCCACCGCCC TCTACGTACT (SEQ ID NO: 241)
    GTTGAGCCTG CGCGTTCTCC AAGGTTTTCA
    GATAGAAGGT CAGTTTACGA CGG
  • [0464]
    TABLE 2
    GENE SEQUENCES
    pMON30304 (SEQ ID NO: 78)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC
    TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGG
    TGGAGGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGT
    pMON26458 (SEQ ID NO: 79)
    TCCCCAGCTCCACCTGCTTGTGACCTCCGAGTCCTCAGTAAACTGCTTCG
    TGACTCCCATGTCCTTCACAGCAGACTGAGCCAGTGCCCAGAGGTTCACC
    CTTTGCCTACACCTGTCCTGCTGCCTGCTGTGGACTTTAGCTTGGGAGAA
    TGGAAAACCCAGATGGAGGAGACCAAGGCACAGGACATTCTGGGAGCAGT
    GACCCTTCTGCTGGAGGGAGTGATGGCAGCACGGGGACAACTGGGACCCA
    CTTGCCTCTCATCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCCTC
    CTTGGGGCCCTGCAGAGCCTCCTTGGAACCCAGCTTCCTCCACAGCGCAG
    GACCACAGCTCACAAGGATCCCAATGCCATCTTCCTGAGCTTCCAACACC
    TGCTCCGAGGAAAGGTGCGTTTCCTGATGCTTGTAGGAGGGTCCACCCTC
    TCCCTCAGGGAATTC
    pMON28548 (SEQ ID NO: 80)
    TCCCCAGCTCCACCTGCTTGTGACCTCCGAGTCCTCAGTAAACTGCTTCG
    TGACTCCCATGTCCTTCACAGCAGACTGAGCCAGTGCCCAGAGGTTCACC
    CTTTGCCTACACCTGTCCTGCTGCCTGCTGTGGACTTTAGCTTGGGAGAA
    TGGAAAACCCAGATGGAGGAGACCAAGGCACAGGACATTCTGGGAGCAGT
    GACCCTTCTGCTGGAGGGAGTGATGGCAGCACGGGGACAACTGGGACCCA
    CTTGCCTCTCATCCCTCCTGGGGCAGCTTTCTGGACACGTCCGTCTCCTC
    CTTGGGGCCCTGCAGAGCCTCCTTGGAACCCAGCTTCCTCCACAGGGCAG
    GACCACAGCTCACAAGGATCCCAATGCCATCTTCCTGAGCTTCCAACACC
    TGCTCCGAGGAAAGGTGCGTTTCCTGATGCTTGTAGGAGGGTCCACCCTC
    TGCGTCAGGGAATTCGGCGGCAACATGGCGTCTCCCGCTCCGCCTGCTTG
    TGACCTCCGAGTCCTCAGTAAACTGCTTCGTGACTCCCATGTCCTTCACA
    GCAGACTGAGCCAGTGCCCAGAGGTTCACCCTTTGCCTACACCTGTCCTG
    CTGCCTGCTGTGGACTTTAGCTTGGGAGAATGGAAAACCCAGATGGAGGA
    GACCAAGGCACAGGACATTCTCGGAGCAGTGACCCTTCTGCTGGAGGGAG
    TGATGGCAGCACGGGGACAACTGGGACCCACTTGCCTCTCATCCCTCCTG
    GGGCAGCTTTCTGGACAGGTCCGTCTCCTCCTTGGGGCCCTGCAGAGCCT
    CCTTGGAACCCAGGGCAGGACCACAGCTCACAAGGATCCCAATGCCATCT
    TCCTGAGCTTCCAACACCTGCTCCGAGGAAAGGTGCGTTTCCTGATGCTT
    GTAGGAGGGTCCACCCTCTGCGTCAGG
    pMON28500 (SEQ ID NO: 81)
    TCCCCAGCTCCACCTGCTTGTGACCTCCGAGTCCTCAGTAAACTGCTTCG
    TGACTCCCATGTCCTTCACAGCAGACTGAGCCAGTGCCCAGAGGTTCACC
    CTTTGCCTACACCTGTCCTGCTGCCTGCTGTGGACTTTAGCTTGGGAGAA
    TGGAAAACCCAGATGGAGGAGACCAAGGCACAGGACATTCTGGGAGCAGT
    GACCCTTCTGCTGGAGGGAGTGATGGCAGCACGGGGACAACTGGGACCCA
    CTTGCCTCTCATCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCCTC
    CTTGGGGCCCTGCAGAGCCTCCTTGGAACCCAGCTTCCTCCACAGGGCAG
    GACCACAGCTCACAAGGATCCCAATGCCATCTTCCTGACCTTCCAACACC
    TGCTCCGAGGAAAGGTGCGTTTCCTGATGCTTGTAGGAGGGTCCACCCTC
    TGCGTCAGGGAATTCGGCAACATGGCGTCTCCCGCTCCGCCTGCTTGTGA
    CCTCCGAGTCCTCAGTAAACTGCTTCGTGACTCCCATGTCCTTCACAGCA
    GACTGAGCCAGTGCCCAGAGGTTCACCCTTTGCCTACACCTGTCCTGCTG
    CCTGCTGTGGACTTTAGCTTGGGAGAATGGAAAACCCAGATGGAGGAGAC
    CAAGGCACAGGACATTCTGGGAGCAGTGACCCTTCTGCTGGAGGGAGTGA
    TGGCAGCACGGGGACAACTGGGACCCACTTGCCTCTCATCCCTCCTGGGG
    CAGCTTTCTGGACAGGTCCGTCTCCTCCTTGGGGCCCTGCAGAGCCTCCT
    TGGAACCCAGCTTCCTCCACAGGGCAGGACCACAGCTCACAAGGATCCCA
    ATGCCATCTTCCTGAGCTTCCAACACCTGCTCCGAGGAAAGGTGCGTTTC
    CTGATGCTTGTAGGAGGGTCCACCCTCTGCGTCAGG
    pMON28501 (SEQ ID NO: 82)
    TCCCCAGCTCCACCTGCTTGTGACCTCCGAGTCCTCAGTAAACT
    GCTTCGTGACTCCCATGTCCTTCACAGCAGACTGAGCCAGTGCCCAGAGG
    TTCACCCTTTGCCTACACCTGTCCTGCTGCCTGCTGTGGACTTTAGCTTG
    GGAGAATGGAAAACCCAGATGGAGGAGACCAAGGCACAGGACATTCTGGG
    AGCAGTGACCCTTCTGCTGGAGGGAGTGATGGCAGCACGGGGACAACTGG
    GACCCACTTGCCTCTCATCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGT
    CTCCTCCTTGGGGCCCTGCAGAGCCTCCTTGGAACCCAGCTTCCTCCACA
    GGGCAGGACCACAGCTCACAAGGATCCCAATGCCATCTTCCTGAGCTTCC
    AACACCTGCTCCGAGGAAAGGTGCGTTTCCTGATGCTTGTAGGAGGGTCC
    ACCCTCTGCGTCAGGGAATTCGGCGGCAACATGGCGTCTCCCGCTCCGCC
    TGCTTGTGACCTCCGAGTCCTCAGTAAACTGCTTCGTGACTCCCATGTCC
    TTCACAGCAGACTGAGCCAGTGCCCAGAGGTTCACCCTTTGCCTACACCT
    GTCCTGCTGCCTGCTGTGGACTTTAGCTTGGGAGAATGGAAAACCCAGAT
    GGAGGAGACCAAGGCACAGGACATTCTGGGAGCAGTGACCCTTCTGCTGG
    AGGGAGTGATGGCAGCACGGGGACAACTGGGACCCACTTGCCTCTCATCC
    CTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCCTCCTTGGGGCCCTGCA
    GAGCCTCCTTGGAACCCAGCTTCCTCCACAGGGCAGGACCACAGCTCACA
    AGGATCCCAATGCCATCTTCCTGAGCTTCCAACACCTGCTCCGAGGAAAG
    GTGCGTTTCCTGATGCTTGTAGGAGGGTCCACCCTCTGCGTCAGG
    pMON28502 (SEQ ID NO: 83)
    TCCCCAGCGCCGCCTGCTTGTGACCTCCGAGTCCTCAGTAAACTGCTTCG
    TGACTCCCATGTCCTTCACAGCAGACTGAGCCAGTGCCCAGAGGTTCACC
    CTTTGCCTACACCTGTCCTGCTGCCTGCTGTGGACTTTAGCTTGGGAGAA
    TGGAAAACCCAGATGGAGGAGACCAAGGCACAGGACATTCTGGGAGCAGT
    GACCCTTCTGCTGGAGGGAGTGATGGCAGCACGGGGACAACTGGGACCCA
    CTTGCCTCTCATCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCCTC
    CTTGGGGCCCTGCAGAGCCTCCTTGGAACCCAGCTTCCTCCACAGGGCAG
    GACCACACCTCACAAGGATCCCAATGCCATCTTCCTGAGCTTCCAACACC
    TGCTCCGAGGAAAGGTGCGTTTCCTGATGCTTGTAGGAGGGTCCACCCTC
    TGCGTCAGGGAATTCGGCGGCAACGGCGGCAACATGGCGTCCCCAGCGCC
    GCCTGCTTGTGACCTCCGAGTCCTCAGTAAACTGCTTCGTGACTCCCATG
    TCCTTCACAGCAGACTGAGCCACTGCCCAGAGGTTCACCCTTTGCCTACA
    CCTGTCCTGCTGCCTGCTGTGGACTTTAGCTTGGGAGAATGGAAAACCCA
    GATGGAGGAGACCAAGGCACAGGACATTCTGGGAGCAGTGACCCTTCTGC
    TGGAGGGAGTGATGCCAGCACGGGGACAACTGGGACCCACTTGCCTCTCA
    TCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCCTCCTTGGGGCCCT
    GCAGAGCCTCCTTGGAACCCAGCTTCCTCCACAGGGCAGGACCACAGCTC
    ACAAGGATCCCAATGCCATCTTCCTGAGCTTCCAACACCTGCTCCGAGGA
    AAGGTGCGTTTCCTGATGCTTGTAGGAGGGTCCACCCTCTGCGTCAGG
    Syntan1 (SEQ ID NO: 84)
    CATGGCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGA
    GACCACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTC
    TCTATCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGT
    AAGGGCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTC
    GTAATCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACAT
    CCAATCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGAC
    GTTCTATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGGGTGGTGGCT
    CTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACCA
    CCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTAT
    CCTCATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGGG
    CTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAAT
    CTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAAT
    CATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTCT
    ATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTAC
    Syntan3 (SEQ ID NO: 85)
      1 CATGGCTAAC TGCTCTATAA TGATCGATGA AATTATACAT
    CACTTAAAGA
     51 GACCACCTGC ACCTTTGCTG GACCCGAACA ACCTCAATGA
    CGAAGACGTC
    101 TCTATCCTGA TGGACCGAAA CCTTCGACTT CCAAACCTGG
    AGAGCTTCGT
    151 AAGGGCTGTC AAGAACTTAG AAAATGCATC AGGTATTGAG
    GCAATTCTTC
    201 GTAATCTCCA ACCATGTCTG CCCTCTGCCA CGGCCGCACC
    CTCTCGACAT
    251 CCAATCATCA TCAAGGCAGG TGACTGGCAA GAATTCCGGG
    AAAAACTGAC
    301 GTTCTATCTG GTTACCCTTG AGCAAGCGCA GGAACAACAG
    GGTGGTGGCT
    351 CTGGCGCTGG CAGCGGCGGC GGTTCTAACT GCTCTATAAT
    GATCGATGAA
    401 ATTATACATC ACTTAAAGAG ACCACCTGCA CCTTTGCTGG
    ACCCGAACAA
    451 CCTCAATGAC GAAGACGTCT CTATCCTGAT GGACCGAAAC
    CTTCGACTTC
    501 CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA
    AAATGCATCA
    551 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC
    CCTCTGCCAC
    601 GGCCGCACCC TCTCGACATC CAATCATCAT CAAGGCAGGT
    GACTGGCAAG
    651 AATTCCGGGA AAAACTGACG TTCTATCTGG TTACCCTTGA
    GCAAGCGCAG
    701 GAACAACAGT AC
    pMON31104 (SEQ ID NO: 86)
      1 ATGGCTCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT
    CTATCCTGAT
     51 GGACCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA
    AGGGCTGTCA
    101 AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG
    TAATCTCCAA
    151 CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC
    CAATCATCAT
    201 CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG
    TTCTATCTGG
    251 TTACCCTTGA GCAAGCGCAG GAACAACAGG GTGGTGGCTC
    TAACTGCTCT
    301 ATAATGATCG ATGAAATTAT ACATCACTTA AAGAGACCAC
    CTGCACCTTT
    351 GTACGTAGAG GGCGGTGGAG GCTCCCCGGG TGAACCGTCT
    GGTCCAATCT
    401 CTACTATCAA CCCGTCTCCT CCGTCTAAAG AATCTCATAA
    ATCTCCAAAC
    451 ATGGCTACCC AGGGTGCCAT GCCGGCCTTC GCCTCTGCTT
    TCCAGCGCCG
    501 GGCAGGAGGG GTCCTGGTTG CTAGCCATCT GCAGAGCTTC
    CTGGAGGTGT
    551 CGTACCGCGT TCTACGCCAC CTTGCGCAGC CCTCTGGCGG
    CTCTGGCGGC
    601 TCTCAGAGCT TCCTGCTCAA GTCTTTAGAG CAAGTGAGAA
    AGATCCAGGG
    651 CGATGGCGCA GCGCTCCAGG AGAAGCTGTG TGCCACCTAC
    AAGCTGTGCC
    701 ACCCCGAGGA GCTGGTGCTG CTCGGACACT CTCTGGGCAT
    CCCCTGGGCT
    751 CCCCTGAGCT CCTGCCCCAG CCAGGCCCCT CTCTGGGCAT
    GCTGCTTGAG
    801 CCAACTCCAT AGCGGCCTTT TCCTCTACCA GGGGCTCCTG
    CAGGCCCTGG
    851 AAGGGATATC CCCCGAGTTG GGTCCCACCT TGGACACACT
    GCAGCTGGAC
    901 GTCGCCGACT TTGCCACCAC CATCTGGCAG CAGATGGAAG
    AACTGGGAAT
    951 GGCCCCTCCC CTGCAGCCCT AATAA
    pMON31105 (SEQ ID NO: 87)
      1 ATGGCTAATG CATCAGCTAT TGAGGCAATT CTTCGTAATC
    TCCAACCATG
     51 TCTGCCCTCT GCCACGGCCG CACCCTCTCG ACATCCAATC
    ATCATCAAGG
    101 CAGGTGACTG GCAAGAATTC CGGGAAAAAC TGACGTTCTA
    TCTGGTTACC
    151 CTTGAGCAAG CGCAGGAACA ACAGGGTGGT GGCTCTAACT
    GCTCTATAAT
    201 GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA
    CCTTTGCTGG
    251 ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT
    GGACCGAAAC
    301 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA
    AGAACTTAGA
    351 ATACGTAGAG GGCGGTGGAG GCTCCCCGGG TGAACCGTCT
    GGTCCAATCT
    401 CTACTATCAA CCCGTCTCCT CCGTCTAAAG AATCTCATAA
    ATCTCCAAAC
    451 ATGGCTACCC AGGGTGCCAT GCCGGCCTTC GCCTCTGCTT
    TCCAGCGCCG
    501 GGCAGGAGGG GTCCTGGTTG CTAGCCATCT GCAGAGCTTC
    CTGGAGGTGT
    551 CGTACCGCGT TCTACGCCAC CTTGCGCAGC CCTCTGGCGG
    CTCTGGCGGC
    601 TCTCAGAGCT TCCTGCTCAA GTCTTTAGAG CAAGTGAGAA
    AGATCCAGGG
    651 CGATGGCGCA GCGCTCCAGG AGAAGCTGTG TGCCACCTAC
    AAGCTGTGCC
    701 ACCCCGAGGA GCTGGTGCTG CTCGGACACT CTCTGGGCAT
    CCCCTGGGCT
    751 CCCCTGAGCT CCTGCCCCAG CCAGGCCCTG CAGCTGGCAG
    GCTGCTTGAG
    801 CCAACTCCAT AGCGGCCTTT TCCTCTACCA GGGGCTCCTG
    CAGGCCCTGG
    851 AAGGGATATC CCCCGAGTTG GGTCCCACCT TGGACACACT
    GCAGCTGGAC
    901 GTCGCCGACT TTGCCACCAC CATCTGGCAG CAGATGGAAG
    AACTGGGAAT
    951 GGCCCCTGCC CTGCAGCCCT AATAA
    pMON31106 (SEQ ID NO: 88)
      1 ATGGCTGCAC CCTCTCGACA TCCAATCATC ATCAAGGCAG
    GTGACTGGCA
     51 AGAATTCCGG GAAAAACTGA CGTTCTATCT GGTTACCCTT
    GAGCAAGCGC
    101 AGGAACAACA GGGTGGTGGC TCTAACTGCT CTATAATGAT
    CGATGAAATT
    151 ATACATCACT TAAAGAGACC ACCTGCACCT TTGCTGGACC
    CGAACAACCT
    201 CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCTT
    CGACTTCCAA
    251 ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA
    TGCATCAGGT
    301 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT
    CTGCCACGGC
    351 CTACGTAGAG GGCGGTGGAG GCTCCCCGGG TGAACCGTCT
    GGTCCAATCT
    401 CTACTATCAA CCCGTCTCCT CCGTCTAAAG AATCTCATAA
    ATCTCCAAAC
    451 ATGGCTACCC AGGGTGCCAT GCCGGCCTTC GCCTCTGCTT
    TCCAGCGCCG
    501 GGCAGGAGGG GTCCTGGTTG CTAGCCATCT GCAGAGCTTC
    CTGGAGGTGT
    551 CGTACCGCGT TCTACGCCAC CTTGCGCAGC CCTCTGGCGG
    CTCTGGCGGC
    601 TCTCAGAGCT TCCTGCTCAA GTCTTTAGAG CAAGTGAGAA
    AGATCCAGGG
    651 CGATGGCGCA GCGCTCCAGG AGAAGCTGTG TGCCACCTAC
    AAGCTGTGCC
    701 ACCCCGAGGA GCTGGTGCTG CTCGGACACT CTCTGGGCAT
    CCCCTGGGCT
    751 CCCCTGAGCT CCTGCCCCAG CCAGGCCCTG CAGCTGGCAG
    GCTGCTTGAG
    801 CCAACTCCAT AGCGGCCTTT TCCTCTACCA GGGGCTCCTG
    CAGGCCCTGG
    851 AAGGGATATC CCCCGAGTTG GGTCCCACCT TGGACACACT
    GCAGCTGGAC
    901 GTCGCCGACT TTGCCACCAC CATCTGGCAG CAGATGGAAG
    AACTGGGAAT
    951 GGCCCCTGCC CTGCAGCCCT AATAA
    pMON31107 (SEQ ID NO: 89)
      1 ATGGCTGCAG GTGACTGGCA AGAATTCCGG GAAAAACTGA
    CGTTCTATCT
     51 GGTTACCCTT GAGCAAGCGC AGGAACAACA GGGTGGTGGC
    TCTAACTGCT
    101 CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC
    ACCTGCACCT
    151 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA
    TCCTGATGGA
    201 CCGAAACCTT CGACTTCCAA ACCTGGAGAG CTTCGTAAGG
    GCTGTCAAGA
    251 ACTTAGAAAA TGCATCAGGT ATTGAGGCAA TTCTTCGTAA
    TCTCCAACCA
    301 TGTCTGCCCT CTGCCACGGC CGCACCCTCT CGACATCCAA
    TCATCATCAA
    351 CTACGTAGAG GGCGGTGGAG GCTCCCCGGG TGAACCGTCT
    GGTCCAATCT
    401 CTACTATCAA CCCGTCTCCT CCGTCTAAAG AATCTCATAA
    ATCTCCAAAC
    451 ATGGCTACCC AGGGTGCCAT GCCGGCCTTC GCCTCTGCTT
    TCCAGCGCCG
    501 GGCAGGAGGG GTCCTGGTTG CTAGCCATCT GCACAGCTTC
    CTGGAGGTGT
    551 CGTACCGCGT TCTACGCCAC CTTGCGCAGC CCTCTGGCGG
    CTCTGGCGGC
    601 TCTCAGAGCT TCCTGCTCAA GTCTTTAGAG CAAGTGAGAA
    AGATCCAGGG
    651 CGATGGCGCA GCGCTCCAGG AGAAGCTGTG TGCCACCTAC
    AAGCTGTGCC
    701 ACCCCGAGGA GCTGGTGCTG CTCGCACACT CTCTGGGCAT
    CCCCTGGGCT
    751 CCCCTGAGCT CCTGCCCCAG CCAGGCCCTG CAGCTGGCAG
    GCTGCTTGAG
    801 CCAACTCCAT AGCGGCCTTT TCCTCTACCA GGGGCTCCTG
    CAGGCCCTGG
    851 AAGGGATATC CCCCGAGTTG GGTCCCACCT TCGACACACT
    GCAGCTGGAC
    901 GTCGCCGACT TTGCCACCAC CATCTGGCAG CAGATGGAAG
    AACTGGGAAT
    951 GGCCCCTGCC CTGCAGCCCT AATAA
    pMON31108 (SEQ ID NO: 90)
      1 ATGGCTCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT
    CTATCCTGAT
     51 GGACCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA
    AGGGCTGTCA
    101 AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG
    TAATCTCCAA
    151 CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC
    CAATCATCAT
    201 CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG
    TTCTATCTGG
    251 TTACCCTTGA GCAAGCGCAG GAACAACAGG GTGGTGGCTC
    TGGCGGTGGC
    301 AGCGGCGGCG GTTCTAACTG CTCTATAATG ATCGATGAAA
    TTATACATCA
    351 CTTAAAGAGA CCACCTGCAC CTTTGTACGT AGAGGGCGGT
    GGAGGCTCCC
    401 CGGGTGAACC GTCTGGTCCA ATCTCTACTA TCAACCCGTC
    TCCTCCGTCT
    451 AAAGAATCTC ATAAATCTCC AAACATGGCT ACCCAGGGTG
    CCATGCCGGC
    501 CTTCGCCTCT GCTTTCCAGC GCCGGGCAGG AGGGGTCCTG
    GTTGCTAGCC
    551 ATCTGCAGAG CTTCCTGGAG GTGTCGTACC GCGTTCTACG
    CCACCTTGCG
    601 CAGCCCTCTG GCGGCTCTGG CGGCTCTCAG AGCTTCCTGC
    TCAAGTCTTT
    651 AGAGCAAGTG AGAAAGATCC AGGGCGATGG CGCAGCGCTC
    CAGGAGAAGC
    701 TGTGTGCCAC CTACAAGCTG TGCCACCCCG AGGAGCTGGT
    GCTGCTCGGA
    751 CACTCTCTGG GCATCCCCTG GGCTCCCCTG AGCTCCTGCC
    CCAGCCAGGC
    801 CCTGCAGCTG GCAGGCTGCT TGAGCCAACT CCATAGCGGC
    CTTTTCCTCT
    851 ACCAGGGGCT CCTGCAGGCC CTGGAAGGGA TATCCCCCGA
    GTTGGGTCCC
    901 ACCTTGGACA CACTGCAGCT GGACGTCGCC GACTTTGCCA
    CCACCATCTG
    951 GCAGCAGATG GAAGAACTGG GAATGGCCCC TGCCCTGCAG
    CCCTAATAA
    pMON31109 (SEQ ID NO: 91)
      1 ATGGCTAATG CATCAGGTAT TGAGGCAATT CTTCGTAATC
    TCCAACCATG
     51 TCTGCCCTCT GCCACGGCCG CACCCTCTCG ACATCCAATC
    ATCATCAAGG
    101 CAGGTGACTG GCAAGAATTC CGGGAAAAAC TGACGTTCTA
    TCTGGTTACC
    151 CTTGAGCAAG CGCAGGAACA ACAGGGTGGT GGCTCTGGCG
    GTGGCAGCGG
    201 CGGCGGTTCT AACTGCTCTA TAATGATCGA TGAAATTATA
    CATCACTTAA
    251 AGAGACCACC TGCACCTTTG CTGGACCCGA ACAACCTCAA
    TGACGAAGAC
    301 GTCTCTATCC TGATGGACCG AAACCTTCGA CTTCCAAACC
    TGGAGAGCTT
    351 CGTAAGGGCT GTCAAGAACT TAGAATACGT AGAGGGCGGT
    GGAGGCTCCC
    401 CGGGTGAACC GTCTGGTCCA ATCTCTACTA TCAACCCGTC
    TCCTCCGTCT
    451 AAAGAATCTC ATAAATCTCC AAACATGGCT ACCCAGGGTG
    CCATGCCGGC
    501 CTTCGCCTCT GCTTTCCAGC GCCGGGCAGG AGGGGTCCTG
    GTTGCTAGCC
    551 ATCTGCAGAG CTTCCTGGAG GTGTCGTACC GCGTTCTACG
    CCACCTTGCG
    601 CAGCCCTCTG GCGGCTCTGG CGGCTCTCAG AGCTTCCTGC
    TCAAGTCTTT
    651 AGAGCAAGTG AGAAAGATCC AGGGCGATGG CGCAGCGCTC
    CAGGAGAAGC
    701 TGTGTGCCAC CTACAAGCTG TGCCACCCCG AGGAGCTGGT
    GCTGCTCGGA
    751 CACTCTCTGG GCATCCCCTG GGCTCCCCTG AGCTCCTGCC
    CCAGCCAGGC
    801 CCTGCAGCTG GCAGGCTGCT TGAGCCAACT CCATAGCGGC
    CTTTTCCTCT
    851 ACCAGGGGCT CCTGCAGGCC CTGGAAGGGA TATCCCCCGA
    GTTGGGTCCC
    901 ACCTTGGACA CACTGCAGCT GGACGTCGCC GACTTTGCCA
    CCACCATCTG
    951 GCAGCAGATG GAAGAACTGG GAATGGCCCC TGCCCTGCAG
    CCCTAATAA
    pMON31110 (SEQ ID NO: 92)
      1 ATGGCTGCAC CCTCTCGACA TCCAATCATC ATCAAGGCAG
    GTGACTGGCA
     51 AGAATTCCGG GAAAAACTGA CGTTCTATCT GGTTACCCTT
    GAGCAAGCGC
    101 AGGAACAACA GGGTGGTGGC TCTGGCGGTG GCAGCGGCGG
    CGGTTCTAAC
    151 TGCTCTATAA TGATCGATGA AATTATACAT CACTTAAAGA
    GACCACCTGC
    201 ACCTTTGCTG GACCCGAACA ACCTCAATGA CGAAGACGTC
    TCTATCCTGA
    251 TGGACCGAAA CCTTCGACTT CCAAACCTGG AGAGCTTCGT
    AAGGGCTGTC
    301 AAGAACTTAG AAAATGCATC AGGTATTGAG GCAATTCTTC
    GTAATCTCCA
    351 ACCATGTCTG CCCTCTGCCA CGGCCTACGT AGAGGGCGGT
    GGAGGCTCCC
    401 CGGGTGAACC GTCTGGTCCA ATCTCTACTA TCAACCCGTC
    TCCTCCGTCT
    451 AAAGAATCTC ATAAATCTCC AAACATGGCT ACCCAGGGTG
    CCATGCCGGC
    501 CTTCGCCTCT GCTTTCCAGC GCCGGGCAGG AGGGGTCCTG
    GTTGCTAGCC
    551 ATCTGCAGAG CTTCCTGGAG GTGTCGTACC GCGTTCTACG
    CCACCTTGCG
    601 CAGCCCTCTG GCGGCTCTGG CGGCTCTCAG AGCTTCCTGC
    TCAAGTCTTT
    651 AGAGCAAGTG AGAAAGATCC AGGGCGATGG CGCAGCGCTC
    CAGGAGAAGC
    701 TGTGTGCCAC CTACAAGCTG TGCCACCCCG AGGAGCTGGT
    GCTGCTCGGA
    751 CACTCTCTGG GCATCCCCTG GGCTCCCCTG AGCTCCTGCC
    CCAGCCAGGC
    801 CCTGCAGCTG GCAGGCTGCT TGAGCCAACT CCATAGCGGC
    CTTTTCCTCT
    851 ACCAGGGGCT CCTGCAGGCC CTGGAAGGGA TATCCCCCGA
    GTTGGGTCCC
    901 ACCTTGGACA CACTGCAGCT GGACGTCGCC GACTTTGCCA
    CCACCATCTG
    951 GCAGCAGATG GAAGAACTGG GAATGGCCCC TGCCCTGCAG
    CCCTAATAA
    pMON31111 (SEQ ID NO: 93)
      1 ATGGCTGCAG GTGACTGGCA AGAATTCCGG GAAAAACTGA
    CGTTCTATCT
     51 GGTTACCCTT GAGCAAGCGC AGGAACAACA GGGTGGTGGC
    TCTGGCGGTG
    101 GCAGCGCCGG CGGTTCTAAC TGCTCTATAA TGATCGATGA
    AATTATACAT
    151 CACTTAAAGA GACCACCTGC ACCTTTGCTG GACCCGAACA
    ACCTCAATGA
    201 CGAAGACGTC TCTATCCTGA TGGACCGAAA CCTTCGACTT
    CCAAACCTGG
    251 AGAGCTTCGT AAGGGCTGTC AAGAACTTAG AAAATGCATC
    AGGTATTGAG
    301 GCAATTCTTC GTAATCTCCA ACCATGTCTG CCCTCTGCCA
    CGGCCGCACC
    351 CTCTCGACAT CCAATCATCA TCAAGTACGT ACAGGGCGGT
    GGAGGCTCCC
    401 CGGGTGAACC GTCTGGTCCA ATCTCTACTA TCAACCCGTC
    TCCTCCGTCT
    451 AAAGAATCTC ATAAATCTCC AAACATGGCT ACCCAGGGTG
    CCATGCCGGC
    501 CTTCGCCTCT GCTTTCCAGC GCCGGGCAGG AGGGGTCCTG
    GTTGCTAGCC
    551 ATCTGCAGAG CTTCCTGGAG GTGTCGTACC GCGTTCTACG
    CCACCTTGCG
    601 CAGCCCTCTG GCGGCTCTGG CGGCTCTCAG AGCTTCCTGC
    TCAAGTCTTT
    651 AGAGCAAGTG AGAAAGATCC AGGGCGATGG CGCAGCGCTC
    CAGGAGAAGC
    701 TGTGTGCCAC CTACAAGCTG TGCCACCCCG AGGAGCTGGT
    GCTGCTCGGA
    751 CACTCTCTGG GCATCCCCTG GGCTCCCCTG AGCTCCTGCC
    CCAGCCAGGC
    801 CCTGCAGCTG GCAGGCTGCT TGAGCCAACT CCATAGCGGC
    CTTTTCCTCT
    851 ACCAGGGGCT CCTGCAGGCC CTGGAAGGGA TATCCCCCGA
    GTTGGGTCCC
    901 ACCTTGGACA CACTGCAGCT GGACGTCGCC GACTTTGCCA
    CCACCATCTG
    951 CCAGCAGATG GAAGAACTGG GAATGGCCCC TGCCCTGCAG
    CCCTAATAA
    pMON13182 (SEQ ID NO: 94)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GCTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG GTGGTTCTGG CGGCGGCTCC
    AACATGGCTT
    401 ACAAGCTGTG CCACCCCGAG GAGCTGGTGC TGCTCGGACA
    CTCTCTGGGC
    451 ATCCCCTGGG CTCCCCTGAG CTCCTGCCCC AGCCAGGCCC
    TGCAGCTGGC
    501 AGGCTGCTTG AGCCAACTCC ATAGCGGCCT TTTCCTCTAC
    CAGGGGCTCC
    551 TGCAGGCCCT GGAAGGGATA TCCCCCGAGT TGGGTCCCAC
    CTTGGACACA
    601 CTGCAGCTGG ACGTCGCCGA CTTTGCCACC ACCATCTGGC
    AGCAGATGGA
    651 AGAACTGGGA ATGGCCCCTG CCCTGCAGCC CACCCAGGGT
    GCCATGCCGG
    701 CCTTCGCCTC TGCTTTCCAG CGCCGGGCAG GAGGGGTCCT
    GGTTGCTAGC
    751 CATCTGCAGA GCTTCCTGGA GGTGTCGTAC CGCGTTCTAC
    GCCACCTTGC
    801 GCAGCCCTCT GGCGGCTCTG GCGGCTCTCA GAGCTTCCTG
    CTCAAGTCTT
    851 TAGAGCAAGT GAGAAACATC CAGGGCGATG GCGCAGCGCT
    CCAGGAGAAG
    901 CTGTGTGCCA CCTAATAA
    pMON13183 (SEQ ID NO: 95)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAACGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT
    ACTATCAACC
    401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT
    GGCTTACAAG
    451 CTGTGCCACC CCCAGGAGCT GGTGCTGCTC GGACACTCTC
    TGGGCATCCC
    501 CTGGGCTCCC CTGAGCTCCT GCCCCAGCCA GGCCCTGCAG
    CTGGCAGGCT
    551 GCTTGAGCCA ACTCCATAGC GGCCTTTTCC TCTACCAGGG
    GCTCCTGCAG
    601 GCCCTGGAAG GGATATCCCC CGAGTTGGGT CCCACCTTGG
    ACACACTGCA
    651 GCTGGACGTC GCCGACTTTG CCACCACCAT CTGGCAGCAG
    ATGGAAGAAC
    701 TGGGAATGGC CCCTGCCCTG CAGCCCACCC AGGGTGCCAT
    GCCGGCCTTC
    751 GCCTCTGCTT TCCAGCGCCG GGCAGGAGGG GTCCTGGTTG
    CTAGCCATCT
    801 GCAGAGCTTC CTGGAGGTGT CGTACCGCGT TCTACGCCAC
    CTTGCGCAGC
    851 CCTCTGGCGG CTCTGGCGGC TCTCAGAGCT TCCTGCTCAA
    GTCTTTAGAG
    901 CAAGTGAGAA AGATCCAGGG CGATGGCGCA GCGCTCCAGG
    AGAAGCTGTG
    951 TGCCACCTAA TAA
    pMON13184 (SEQ ID NO: 96)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG GTGGTTCTGG CGGCGGCTCC
    AACATGGCTC
    401 CCGAGTTGGG TCCCACCTTG GACACACTGC AGCTGGACGT
    CGCCGACTTT
    451 GCCACCACCA TCTGGCAGCA GATGGAAGAA CTGGGAATGG
    CCCCTGCCCT
    501 GCAGCCCACC CAGGGTGCCA TGCCGGCCTT CGCCTCTGCT
    TTCCAGCGCC
    551 GGGCAGGAGG GGTCCTGGTT GCTAGCCATC TGCAGAGCTT
    CCTGGAGGTG
    601 TCGTACCGCG TTCTACGCCA CCTTGCGCAG CCCTCTGGCG
    GCTCTGGCGG
    651 CTCTCAGAGC TTCCTGCTCA AGTCTTTAGA GCAAGTGAGA
    AAGATCCAGG
    701 GCGATGGCGC AGCGCTCCAG GAGAAGCTGT GTGCCACCTA
    CAAGCTGTGC
    751 CACCCCGAGG AGCTGGTGCT GCTCGGACAC TCTCTGGGCA
    TCCCCTGGGC
    801 TCCCCTGAGC TCCTGCCCCA GCCAGGCCCT GCAGCTGGCA
    GGCTGCTTGA
    851 GCCAACTCCA TAGCGGCCTT TTCCTCTACC AGGGGCTCCT
    GCAGGCCCTG
    901 GAAGGGATAT CCTAATAA
    pMON13185 (SEQ ID NO: 97)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAC AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT
    ACTATCAACC
    401 CGTCTCCTCC CTCTAAAGAA TCTCATAAAT CTCCAAACAT
    GGCTCCCGAG
    451 TTGGGTCCCA CCTTGGACAC ACTGCAGCTG GACGTCGCCG
    ACTTTGCCAC
    501 CACCATCTGG CAGCAGATGG AAGAACTGGG AATGGCCCCT
    GCCCTGCAGC
    551 CCACCCAGGG TGCCATGCCG GCCTTCGCCT CTGCTTTCCA
    GCGCCGCGCA
    601 GGAGGGGTCC TGGTTGCTAG CCATCTGCAG AGCTTCCTGG
    AGGTGTCGTA
    651 CCGCGTTCTA CGCCACCTTG CGCAGCCCTC TGGCGGCTCT
    GGCGGCTCTC
    701 AGAGCTTCCT GCTCAAGTCT TTAGAGCAAG TGAGAAAGAT
    CCAGGGCGAT
    751 GGCGCAGCGC TCCAGGAGAA GCTGTGTGCC ACCTACAAGC
    TGTGCCACCC
    801 CGAGGAGCTG GTGCTGCTCG GACACTCTCT GGCCATCCCC
    TGGGCTCCCC
    851 TGAGCTCCTG CCCCAGCCAG GCCCTGCAGC TGGCAGGCTG
    CTTGAGCCAA
    901 CTCCATAGCG GCCTTTTCCT CTACCAGGGG CTCCTGCAGG
    CCCTGGAAGG
    951 GATATCCTAA TAA
    pMON13186 (SEQ ID NO: 98)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG GTGGTTCTGG CGGCGGCTCC
    AACATGGCTA
    401 TGGCCCCTGC CCTGCAGCCC ACCCAGGGTG CCATGCCGGC
    CTTCGCCTCT
    451 GCTTTCCAGC GCCGGGCAGG AGGGGTCCTG GTTGCTAGCC
    ATCTGCAGAG
    501 CTTCCTGGAG GTGTCGTACC GCGTTCTACG CCACCTTGCG
    CAGCCCTCTG
    551 GCGGCTCTGG CGGCTCTCAG AGCTTCCTGC TCAAGTCTTT
    AGAGCAAGTG
    601 AGAAAGATCC AGGGCGATGG CGCAGCGCTC CAGGAGAAGC
    TGTGTGCCAC
    651 CTACAAGCTG TGCCACCCCG AGGAGCTGGT GCTGCTCGGA
    CACTCTCTGG
    701 GCATCCCCTG GGCTCCCCTG AGCTCCTGCC CCAGCCAGGC
    CCTGCAGCTG
    751 GCAGGCTGCT TGAGCCAACT CCATAGCGGC CTTTTCCTCT
    ACCAGGGGCT
    801 CCTGCAGGCC CTGGAAGGGA TATCCCCCGA GTTGGGTCCC
    ACCTTGGACA
    851 CACTGCAGCT GGACGTCGCC GACTTTGCCA CCACCATCTG
    GCAGCAGATG
    901 GAAGAACTGG GATAATAA
    pMON13187 (SEQ ID NO: 99)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTCACG
    301 TTCTATCTGG TTACCCTTCA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT
    ACTATCAACC
    401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT
    GGCTATGGCC
    451 CCTGCCCTGC AGCCCACCCA GGGTGCCATG CCGGCCTTCG
    CCTCTGCTTT
    501 CCAGCGCCGG GCAGGAGGGG TCCTGGTTGC TAGCCATCTG
    CAGAGCTTCC
    551 TGGAGGTGTC GTACCGCGTT CTACGCCACC TTGCGCAGCC
    CTCTGGCGGC
    601 TCTGGCGGCT CTCAGAGCTT CCTGCTCAAG TCTTTAGAGC
    AAGTGAGAAA
    651 GATCCAGGGC GATGGCGCAG CGCTCCAGGA GAAGCTGTGT
    GCCACCTACA
    701 AGCTGTGCCA CCCCGAGGAG CTGGTGCTGC TCGGACACTC
    TCTGGGCATC
    751 CCCTGGGCTC CCCTGAGCTC CTGCCCCAGC CAGGCCCTGC
    AGCTGGCAGG
    801 CTGCTTGAGC CAACTCCATA GCGGCCTTTT CCTCTACCAG
    GGGCTCCTGC
    851 AGGCCCTGGA AGGGATATCC CCCGAGTTGG GTCCCACCTT
    GGACACACTG
    901 CAGCTGGACG TCGCCGACTT TGCCACCACC ATCTGGCAGC
    AGATGGAAGA
    951 ACTGGGATAA TAA
    pMON13188 (SEQ ID NO: 100)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG GTGGTTCTGG CGGCGGCTCC
    AACATGGCTA
    401 CCCAGGGTGC CATGCCGGCC TTCGCCTCTG CTTTCCAGCG
    CCGGGCAGGA
    451 GGGGTCCTGG TTGCTAGCCA TCTGCAGAGC TTCCTGGAGG
    TGTCGTACCC
    501 CGTTCTACGC CACCTTGCGC AGCCCTCTGG CGGCTCTGGC
    GGCTCTCAGA
    551 GCTTCCTGCT CAAGTCTTTA GAGCAAGTGA GAAAGATCCA
    GGGCGATGGC
    601 GCAGCGCTCC AGGAGAAGCT GTGTGCCACC TACAAGCTGT
    GCCACCCCGA
    651 GGAGCTGGTG CTGCTCGGAC ACTCTCTGGG CATCCCCTGG
    GCTCCCCTGA
    701 GCTCCTGCCC CAGCCAGGCC CTGCAGCTGG CAGGCTGCTT
    GAGCCAACTC
    751 CATAGCGGCC TTTTCCTCTA CCAGGGGCTC CTGCAGGCCC
    TGGAAGGGAT
    801 ATCCCCCGAG TTGGGTCCCA CCTTGGACAC ACTGCAGCTG
    GACGTCGCCG
    851 ACTTTGCCAC CACCATCTGG CAGCAGATGG AAGAACTGGG
    AATGGCCCCT
    901 GCCCTGCAGC CCTAATAA
    pMON13189 (SEQ ID NO: 101)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTCGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT
    ACTATCAACC
    401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT
    GGCTACCCAG
    451 GGTGCCATGC CGGCCTTCGC CTCTGCTTTC CAGCGCCGGG
    CAGGAGGGGT
    501 CCTGGTTGCT AGCCATCTGC AGAGCTTCCT GGAGGTGTCG
    TACCGCGTTC
    551 TACGCCACCT TGCGCAGCCC TCTGGCGGCT CTGGCGGCTC
    TCAGAGCTTC
    601 CTGCTCAAGT CTTTAGAGCA AGTGAGAAAG ATCCAGGGCG
    ATGGCGCAGC
    651 GCTCCAGGAG AAGCTGTGTG CCACCTACAA GCTGTGCCAC
    CCCGAGGAGC
    701 TGGTGCTGCT CGGACACTCT CTGGGCATCC CCTGGGCTCC
    CCTGAGCTCC
    751 TGCCCCAGCC AGGCCCTGCA GCTGGCAGGC TGCTTGAGCC
    AACTCCATAG
    801 CGGCCTTTTC CTCTACCAGG GGCTCCTGCA GGCCCTGGAA
    GGGATATCCC
    851 CCGAGTTGGG TCCCACCTTC GACACACTCC AGCTGGACGT
    CGCCGACTTT
    901 GCCACCACCA TCTGGCAGCA GATGGAAGAA CTGGGAATGG
    CCCCTGCCCT
    951 GCAGCCCTAA TAA
    pMON13190 (SEQ ID NO: 102)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG GTGGTTCTGG CGGCGGCTCC
    AACATGGCTT
    401 CTGCTTTCCA GCGCCGGGCA GGAGGGGTCC TGGTTGCTAG
    CCATCTGCAG
    451 AGCTTCCTGG AGGTGTCGTA CCGCGTTCTA CGCCACCTTG
    CGCAGCCCTC
    501 TGGCGGCTCT GGCGGCTCTC AGAGCTTCCT GCTCAAGTCT
    TTAGAGCAAG
    551 TGAGAAAGAT CCAGGGCGAT GGCGCAGCGC TCCAGGAGAA
    GCTGTGTGCC
    601 ACCTACAAGC TGTGCCACCC CGAGGAGCTG GTGCTGCTCG
    GACACTCTCT
    651 GGGCATCCCC TGGGCTCCCC TGAGCTCCTG CCCCAGCCAG
    GCCCTGCAGC
    701 TGGCAGGCTG CTTGAGCCAA CTCCATAGCG GCCTTTTCCT
    CTACCAGGGG
    751 CTCCTGCAGG CCCTGGAAGG GATATCCCCC GAGTTGGGTC
    CCACCTTGGA
    801 CACACTGCAG CTGGACGTCG CCGACTTTGC CACCACCATC
    TGGCAGCAGA
    851 TGGAAGAACT GGGAATGGCC CCTGCCCTGC AGCCCACCCA
    GGGTGCCATG
    901 CCGGCCTTCG CCTAATAA
    pMON13191 (SEQ ID NO: 103)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT
    ACTATCAACC
    401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT
    GGCTTCTGCT
    451 TTCCAGCGCC GCGCAGGAGG GGTCCTGGTT GCTAGCCATC
    TGCAGAGCTT
    501 CCTGGAGGTG TCGTACCGCG TTCTACGCCA CCTTGCGCAG
    CCCTCTGGCG
    551 GCTCTGGCGG CTCTCAGAGC TTCCTGCTCA AGTCTTTAGA
    GCAAGTGAGA
    601 AAGATCCAGG GCGATGGCGC AGCGCTCCAG GAGAAGCTGT
    GTGCCACCTA
    651 CAAGCTGTGC CACCCCGAGG AGCTGGTGCT CCTCGGACAC
    TCTCTGGGCA
    701 TCCCCTGGGC TCCCCTGAGC TCCTGCCCCA GCCAGGCCCT
    GCAGCTGGCA
    751 CGCTGCTTGA GCCAACTCCA TAGCGGCCTT TTCCTCTACC
    AGGGGCTCCT
    801 GCAGGCCCTG GAAGGGATAT CCCCCGAGTT GGGTCCCACC
    TTGGACACAC
    851 TGCAGCTGGA CCTCGCCGAC TTTGCCACCA CCATCTGGCA
    GCAGATGGAA
    901 GAACTGGGAA TGGCCCCTGC CCTGCAGCCC ACCCACGGTG
    CCATGCCGGC
    951 CTTCGCCTAA TAA
    pMON13192 (SEQ ID NO: 104)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG GTGGTTCTGG CGGCGGCTCC
    AACATGGCTT
    401 ACAAGCTGTG CCACCCCGAG GAGCTGGTGC TGCTCGGACA
    CTCTCTGGGC
    451 ATCCCCTGGG CTCCCCTGAG CTCCTGCCCC AGCCAGGCCC
    TGCAGCTGGC
    501 AGGCTGCTTG AGCCAACTCC ATAGCGGCCT TTTCCTCTAC
    CAGGGGCTCC
    551 TGCAGGCCCT GGAAGGGATA TCCCCCGAGT TGGGTCCCAC
    CTTGGACACA
    601 CTGCAGCTGG ACGTCGCCGA CTTTGCCACC ACCATCTGGC
    AGCAGATGGA
    651 AGAACTGGGA ATGGCCCCTG CCCTGCAGCC CACCCAGGGT
    GCCATGCCGG
    701 CCTTCGCCTC TGCTTTCCAG CGCCGGGCAG GAGGGGTCCT
    GGTTGCTAGC
    751 CATCTGCAGA GCTTCCTGGA GGTGTCGTAC CGCGTTCTAC
    GCCACCTTGC
    801 GCAGCCCACA CCATTGGGCC CTGCCAGCTC CCTGCCCCAG
    AGCTTCCTGC
    851 TCAAGTCTTT AGAGCAAGTG AGAAAGATCC AGGGCGATGG
    CGCAGCGCTC
    901 CAGGAGAAGC TGTGTGCCAC CTAATAA
    pMON13193 (SEQ ID NO: 105)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT
    ACTATCAACC
    401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT
    GGCTTACAAG
    451 CTGTGCCACC CCGAGGAGCT GGTGCTGCTC GGACACTCTC
    TGGGCATCCC
    501 CTGGGCTCCC CTGAGCTCCT GCCCCAGCCA GGCCCTGCAG
    CTGGCAGGCT
    551 GCTTGAGCCA ACTCCATAGC GGCCTTTTCC TCTACCAGGG
    GCTCCTGCAG
    601 GCCCTGGAAG GGATATCCCC CGAGTTGGGT CCCACCTTGG
    ACACACTGCA
    651 GCTGGACGTC GCCGACTTTG CCACCACCAT CTGGCAGCAG
    ATGGAAGAAC
    701 TGGGAATGGC CCCTGCCCTG CAGCCCACCC AGGGTGCCAT
    GCCGGCCTTC
    751 GCCTCTGCTT TCCAGCGCCG GGCAGGAGGG GTCCTGGTTG
    CTAGCCATCT
    801 GCAGAGCTTC CTGGAGGTGT CGTACCGCGT TCTACGCCAC
    CTTGCGCAGC
    851 CCACACCATT GGGCCCTGCC AGCTCCCTGC CCCAGAGCTT
    CCTGCTCAAG
    901 TCTTTAGAGC AAGTGAGAAA GATCCAGGGC GATGGCGCAG
    CGCTCCAGGA
    951 GAAGCTGTGT GCCACCTAAT AA
    pMON25190 (SEQ ID NO: 106)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGCCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG GTGGTTCTGG CGGCGGCTCC
    AACATGGCTC
    401 CCGAGTTGGG TCCCACCTTG GACACACTGC AGCTGGACGT
    CGCCGACTTT
    451 GCCACCACCA TCTGGCAGCA GATGGAAGAA CTGGGAATGG
    CCCCTGCCCT
    501 GCAGCCCACC CAGGGTGCCA TGCCGGCCTT CGCCTCTGCT
    TTCCAGCGCC
    551 GGGCAGGAGG GGTCCTGGTT GCTAGCCATC TGCAGAGCTT
    CCTGGAGGTG
    601 TCGTACCGCG TTCTACGCCA CCTTGCGCAG CCCACACCAT
    TGGGCCCTGC
    651 CAGCTCCCTG CCCCAGAGCT TCCTGCTCAA GTCTTTAGAG
    CAAGTGAGAA
    701 AGATCCAGGG CGATGGCGCA GCGCTCCAGG AGAAGCTGTG
    TGCCACCTAC
    751 AAGCTGTGCC ACCCCGAGGA GCTGGTGCTG CTCGGACACT
    CTCTGGGCAT
    801 CCCCTGGGCT CCCCTGAGCT CCTGCCCCAG CCAGGCCCTG
    CAGCTGGCAG
    851 GCTGCTTGAG CCAACTCCAT AGCGGCCTTT TCCTCTACCA
    GGGGCTCCTG
    901 CAGGCCCTGG AAGGGATATC CTAATAA
    pMON25191 (SEQ ID NO: 107)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGC TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT
    ACTATCAACC
    401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT
    GGCTCCCGAG
    451 TTGGGTCCCA CCTTGGACAC ACTGCAGCTG GACGTCGCCG
    ACTTTGCCAC
    501 CACCATCTGG CAGCAGATGG AAGAACTGGG AATGGCCCCT
    GCCCTGCAGC
    551 CCACCCAGGG TGCCATGCCG GCCTTCGCCT CTGCTTTCCA
    GCGCCGGGCA
    601 GGAGGGGTCC TGGTTGCTAG CCATCTGCAG AGCTTCCTGG
    AGGTGTCGTA
    651 CCGCGTTCTA CGCCACCTTG CGCAGCCCAC ACCATTGGGC
    CCTGCCAGCT
    701 CCCTGCCCCA GAGCTTCCTG CTCAAGTCTT TAGAGCAAGT
    GAGAAAGATC
    751 CAGGGCGATG GCCCAGCGCT CCAGGAGAAG CTGTGTGCCA
    CCTACAAGCT
    801 GTGCCACCCC GAGGAGCTGG TGCTGCTCGG ACACTCTCTG
    GGCATCCCCT
    851 GGGCTCCCCT GAGCTCCTGC CCCAGCCAGG CCCTGCAGCT
    GGCAGGCTGC
    901 TTGAGCCAAC TCCATAGCGG CCTTTTCCTC TACCAGGGGC
    TCCTGCAGGC
    951 CCTGGAAGGG ATATCCTAAT AA
    pMON13194 (SEQ ID NO: 108)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG GTGGTTCTGG CGGCGGCTCC
    AACATGGCTA
    401 TGGCCCCTGC CCTGCAGCCC ACCCAGGGTG CCATGCCGGC
    CTTCGCCTCT
    451 GCTTTCCAGC GCCGGGCAGG AGGGGTCCTG GTTGCTAGCC
    ATCTGCAGAG
    501 CTTCCTGGAG GTGTCGTACC GCGTTCTACG CCACCTTGCG
    CAGCCCACAC
    551 CATTGGGCCC TGCCAGCTCC CTGCCCCAGA GCTTCCTGCT
    CAAGTCTTTA
    601 GAGCAAGTGA GAAAGATCCA GGGCGATGGC GCAGCGCTCC
    AGGAGAAGCT
    651 GTGTGCCACC TACAAGCTGT GCCACCCCGA GGAGCTGGTG
    CTGCTCGGAC
    701 ACTCTCTGGG CATCCCCTGG GCTCCCCTGA GCTCCTGCCC
    CAGCCAGGCC
    751 CTGCAGCTGG CAGGCTGCTT GAGCCAACTC CATAGCGGCC
    TTTTCCTCTA
    801 CCAGGGGCTC CTGCAGGCCC TGGAAGGGAT ATCCCCCGAG
    TTGGGTCCCA
    851 CCTTGGACAC ACTGCAGCTG GACGTCGCCG ACTTTGCCAC
    CACCATCTGG
    901 CAGCAGATGG AAGAACTGGG ATAATAA
    pMON13195 (SEQ ID NO: 109)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT
    ACTATCAACC
    401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT
    GGCTATGGCC
    451 CCTGCCCTGC AGCCCACCCA GGGTGCCATG CCGGCCTTCG
    CCTCTGCTTT
    501 CCAGCGCCGG GCAGGAGGGG TCCTGGTTGC TAGCCATCTG
    CAGAGCTTCC
    551 TGGAGGTGTC GTACCGCGTT CTACGCCACC TTGCGCAGCC
    CACACCATTG
    601 GGCCCTGCCA GCTCCCTGCC CCAGAGCTTC CTGCTCAAGT
    CTTTAGAGCA
    651 AGTGAGAAAG ATCCAGGGCG ATGGCGCAGC GCTCCAGGAG
    AAGCTGTGTG
    701 CCACCTACAA GCTGTGCCAC CCCGAGGAGC TGGTGCTGCT
    CGGACACTCT
    751 CTGGGCATCC CCTGGGCTCC CCTGAGCTCC TGCCCCAGCC
    AGGCCCTGCA
    801 GCTGGCAGGC TGCTTGAGCC AACTCCATAG CGGCCTTTTC
    CTCTACCAGG
    851 GGCTCCTGCA GGCCCTGGAA GGGATATCCC CCGAGTTGGG
    TCCCACCTTG
    901 GACACACTGC AGCTGGACGT CGCCGACTTT GCCACCACCA
    TCTGGCAGCA
    951 GATGGAAGAA CTGGGATAAT AA
    pMON13196 (SEQ ID NO: 110)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG GTGGTTCTGG CGGCGGCTCC
    AACATGGCTA
    401 CCCAGGGTGC CATGCCGGCC TTCGCCTCTG CTTTCCAGCG
    CCGGGCAGGA
    451 GGGGTCCTGG TTGCTAGCCA TCTGCAGAGC TTCCTGGAGG
    TGTCGTACCG
    501 CGTTCTACGC CACCTTGCGC AGCCCACACC ATTGGGCCCT
    GCCAGCTCCC
    551 TGCCCCAGAG CTTCCTGCTC AAGTCTTTAG AGCAAGTGAG
    AAAGATCCAG
    601 GGCGATGGCG CAGCGCTCCA GGAGAAGCTG TGTGCCACCT
    ACAAGCTGTG
    651 CCACCCCGAG GAGCTGGTGC TGCTCGGACA CTCTCTGGGC
    ATCCCCTGGG
    701 CTCCCCTGAG CTCCTGCCCC AGCCAGGCCC TGCAGCTGGC
    AGGCTGCTTG
    751 AGCCAACTCC ATAGCGGCCT TTTCCTCTAC CAGGGGCTCC
    TGCAGGCCCT
    801 GGAAGGGATA TCCCCCGAGT TGGGTCCCAC CTTGGACACA
    CTGCAGCTGG
    851 ACGTCGCCGA CTTTGCCACC ACCATCTGGC AGCAGATGGA
    AGAACTGGGA
    901 ATGGCCCCTG CCCTGCAGCC CTAATAA
    pMON13197 (SEQ ID NO: 111)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT
    ACTATCAACC
    401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT
    GGCTACCCAG
    451 GGTGCCATGC CGGCCTTCGC CTCTGCTTTC CAGCGCCGGG
    CAGGAGGGGT
    501 CCTGGTTGCT AGCCATCTGC AGAGCTTCCT GGAGGTGTCG
    TACCGCGTTC
    551 TACGCCACCT TGCGCAGCCC ACACCATTGG GCCCTGCCAG
    CTCCCTGCCC
    601 CAGAGCTTCC TGCTCAAGTC TTTAGAGCAA GTGAGAAAGA
    TCCAGGGCGA
    651 TGGCGCAGCG CTCCAGGAGA AGCTGTGTGC CACCTACAAG
    CTGTGCCACC
    701 CCGAGGAGCT GGTGCTGCTC GGACACTCTC TGGGCATCCC
    CTGGGCTCCC
    751 CTGAGCTCCT GCCCCAGCCA GGCCCTGCAG CTGGCAGGCT
    GCTTGAGCCA
    801 ACTCCATAGC GGCCTTTTCC TCTACCAGGC GCTCCTGCAG
    GCCCTGGAAG
    851 GGATATCCCC CGAGTTGGGT CCCACCTTGG ACACACTGCA
    GCTGGACGTC
    901 GCCGACTTTG CCACCACCAT CTGGCAGCAG ATGGAAGAAC
    TGGGAATGGC
    951 CCCTGCCCTG CAGCCCTAAT AA
    pMON13198 (SEQ ID NO: 112)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG GTGGTTCTGG CGGCGGCTCC
    AACATGGCTT
    401 CTGCTTTCCA GCGCCGGGCA GGAGGGGTCC TGGTTGCTAG
    CCATCTGCAG
    451 AGCTTCCTGG AGGTGTCGTA CCGCGTTCTA CGCCACCTTG
    CGCAGCCCAC
    501 ACCATTGGGC CCTGCCAGCT CCCTGCCCCA GAGCTTCCTG
    CTCAAGTCTT
    551 TAGAGCAAGT GAGAAAGATC CAGGGCGATG GCGCAGCGCT
    CCAGGAGAAG
    601 CTGTGTGCCA CCTACAAGCT GTGCCACCCC GAGGAGCTGG
    TGCTGCTCGG
    651 ACACTCTCTG GGCATCCCCT GGGCTCCCCT GAGCTCCTGC
    CCCAGCCAGG
    701 CCCTGCAGCT GGCAGGCTGC TTGAGCCAAC TCCATAGCGG
    CCTTTTCCTC
    751 TACCAGGGGC TCCTGCAGGC CCTGGAAGGG ATATCCCCCG
    AGTTGGGTCC
    801 CACCTTGGAC ACACTGCAGC TGGACGTCGC CGACTTTGCC
    ACCACCATCT
    851 GGCAGCAGAT GGAAGAACTG GGAATGGCCC CTGCCCTGCA
    GCCCACCCAG
    901 GGTGCCATGC CGGCCTTCGC CTAATAA
    pMON13199 (SEQ ID NO: 113)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCCCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT
    ACTATCAACC
    401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT
    GGCTTCTGCT
    451 TTCCAGCGCC GGGCAGGAGG GGTCCTGGTT GCTAGCCATC
    TGCAGAGCTT
    501 CCTGGAGGTG TCGTACCGCG TTCTACGCCA CCTTGCGCAG
    CCCACACCAT
    551 TGGGCCCTGC CAGCTCCCTG CCCCAGAGCT TCCTGCTCAA
    GTCTTTAGAG
    601 CAAGTGAGAA AGATCCAGGG CGATGGCGCA GCGCTCCAGG
    AGAAGCTGTG
    651 TGCCACCTAC AAGCTGTGCC ACCCCGAGGA GCTGGTGCTC
    CTCGGACACT
    701 CTCTGGGCAT CCCCTGGGCT CCCCTGAGCT CCTGCCCCAG
    CCAGGCCCTG
    751 CAGCTGGCAG GCTGCTTGAG CCAACTCCAT AGCGGCCTTT
    TCCTCTACCA
    801 GGGGCTCCTG CAGGCCCTGG AAGGGATATC CCCCGAGTTG
    GGTCCCACCT
    851 TGGACACACT GCAGCTGGAC GTCGCCGACT TTGCCACCAC
    CATCTGGCAG
    901 CAGATGGAAG AACTGGGAAT GGCCCCTGCC CTGCAGCCCA
    CCCAGCGTGC
    951 CATGCCGGCC TTCGCCTAAT AA
    pMON31112 (SEQ ID NO: 114)
      1 ATGGCTAACT GCTCTAACAT GATCGATGAA ATCATCACCC
    ACCTGAAGCA
     51 GCCACCGCTG CCGCTGCTGG ACTTCAACAA CCTCAATGGT
    GAAGACCAAG
    101 ATATCCTAAT GGACAATAAC CTTCGTCGTC CAAACCTCGA
    GGCATTCAAC
    151 CGTGCTGTCA AGTGTCTGCA GAATGCATCA GCAATTGAGA
    GCATTCTTAA
    201 AAATCTCCTG CCATGTCTGC CGCTAGCCAC GGCCGCACCC
    ACGCGACATC
    251 CAATCCATAT CAAGGACGGT GACTGGAATG AATTCCGTCG
    TAAACTGACC
    301 TTCTATCTGA AAACCTTGGA GAACGCGCAG GCTCAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT
    ACTATCAACC
    401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT
    GGCTACCCAG
    451 GGTGCCATGC CGGCCTTCGC CTCTGCTTTC CAGCGCCGGG
    CAGGAGGGGT
    501 CCTGGTTGCT AGCCATCTGC AGAGCTTCCT GGAGGTGTCG
    TACCGCGTTC
    551 TACGCCACCT TGCGCAGCCC TCTGGCGGCT CTGGCGGCTC
    TCAGAGCTTC
    601 CTGCTCAAGT CTTTAGAGCA AGTGAGAAAG ATCCAGGGCG
    ATGGCGCAGC
    651 GCTCCAGGAG AAGCTGTGTG CCACCTACAA GCTGTGCCAC
    CCCGAGGAGC
    701 TGGTGCTGCT CGGACACTCT CTGGGCATCC CCTGGGCTCC
    CCTGAGCTCC
    751 TGCCCCAGCC AGGCCCTGCA GCTGGCAGGC TGCTTGAGCC
    AACTCCATAG
    801 CGGCCTTTTC CTCTACCAGG GGCTCCTGCA GGCCCTGGAA
    GGGATATCCC
    851 CCGAGTTGGG TCCCACCTTG GACACACTCC AGCTGGACGT
    CGCCGACTTT
    901 GCCACCACCA TCTGGCAGCA GATGGAAGAA CTGGGAATGG
    CCCCTGCCCT
    951 GCAGCCCTAA TAA
    pMON31113 (SEQ ID NO: 115)
      1 ATGGCTAACT GCTCTAACAT GATCGATGAA ATCATCACCC
    ACCTGAAGCA
     51 GCCACCGCTG CCGCTGCTGG ACTTCAACAA CCTCAATGGT
    GAAGACCAAG
    101 ATATCCTGAT GGAAAATAAC CTTCGTCGTC CAAACCTCGA
    GGCATTCAAC
    151 CGTGCTGTCA AGTCTCTGCA GAATGCATCA GCAATTGAGA
    GCATTCTTAA
    201 AAATCTCCTG CCATGTCTGC CCCTGGCCAC GGCCGCACCC
    ACGCGACATC
    251 CAATCATCAT CCGTGACGGT GACTGGAATG AATTCCGTCG
    TAAACTGACC
    301 TTCTATCTGA AAACCTTGGA GAACGCGCAG GCTCAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT
    ACTATCAACC
    401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT
    GGCTACCCAG
    451 GGTGCCATGC CGGCCTTCGC CTCTGCTTTC CAGCGCCGGG
    CAGGAGGGGT
    501 CCTGGTTGCT AGCCATCTGC AGAGCTTCCT GGAGGTGTCG
    TACCGCGTTC
    551 TACGCCACCT TGCGCAGCCC ACACCATTGG GCCCTGCCAG
    CTCCCTGCCC
    601 CAGAGCTTCC TGCTCAAGTC TTTAGAGCAA GTGAGAAAGA
    TCCAGGGCGA
    651 TGGCGCAGCG CTCCAGGAGA AGCTGTGTGC CACCTACAAG
    CTGTGCCACC
    701 CCGAGGAGCT GGTGCTGCTC GGACACTCTC TGGGCATCCC
    CTGGGCTCCC
    751 CTGAGCTCCT GCCCCAGCCA GGCCCTGCAG CTGGCAGGCT
    GCTTGAGCCA
    801 ACTCCATAGC GGCCTTTTCC TCTACCAGGG GCTCCTGCAG
    GCCCTGGAAG
    851 GGATATCCCC CGAGTTGGGT CCCACCTTGG ACACACTGCA
    GCTGGACGTC
    901 GCCGACTTTG CCACCACCAT CTGGCAGCAG ATGGAAGAAC
    TGGGAATGGC
    951 CCCTGCCCTG CAGCCCTAAT AA
    pMON31114 (SEQ ID NO: 116)
      1 ATGGCTAACT GCTCTAACAT GATCGATGAA ATCATCACCC
    ACCTGAAGCA
     51 GCCACCGCTG CCGCTGCTGG ACTTCAACAA CCTCAATGGT
    GAAGACCAAG
    101 ATATCCTGAT GGAAAATAAC CTTCGTCGTC CAAACCTCGA
    GGCATTCAAC
    151 CGTGCTGTCA AGTCTCTGCA GAATGCATCA GCAATTGAGA
    GCATTCTTAA
    201 AAATCTCCTG CCATGTCTGC CCCTGGCCAC GGCCGCACCC
    ACGCGACATC
    251 CAATCATCAT CCGTGACGGT GACTGGAATG AATTCCGTCG
    TAAACTGACC
    301 TTCTATCTGA AAACCTTGGA GAACGCGCAG GCTCAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT
    ACTATCAACC
    401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT
    GGCTACCCAG
    451 GGTGCCATGC CGGCCTTCGC CTCTGCTTTC CAGCGCCGGG
    CAGGAGGGGT
    501 CCTGGTTGCT AGCCATCTGC AGAGCTTCCT GGAGGTGTCG
    TACCGCGTTC
    551 TACGCCACCT TGCGCAGCCC TCTGGCGGCT CTGGCGGCTC
    TCAGAGCTTC
    601 CTGCTCAAGT CTTTAGAGCA AGTGAGAAAG ATCCAGGGCG
    ATGGCGCAGC
    651 GCTCCAGGAG AAGCTGTGTG CCACCTACAA GCTGTGCCAC
    CCCCGAGGAGC
    701 TGGTGCTGCT CGGACACTCT CTGGGCATCC CCTGGGCTCC
    CCTGAGCTCC
    751 TGCCCCAGCC AGGCCCTGCA GCTGGCAGGC TGCTTGAGCC
    AACTCCATAG
    801 CGGCCTTTTC CTCTACCAGG GGCTCCTGCA GGCCCTGGAA
    GGGATATCCC
    851 CCGAGTTGGG TCCCACCTTG GACACACTGC AGCTGGACGT
    CGCCGACTTT
    901 GCCACCACCA TCTGGCAGCA GATGGAAGAA CTGGGAATGG
    CCCCTGCCCT
    951 GCAGCCCTAA TAA
    pMON31115 (SEQ ID NO: 117)
      1 ATGGCTAACT GCTCTAACAT GATCGATGAA ATCATCACCC
    ACCTGAAGCA
     51 GCCACCGCTG CCGCTGCTGG ACTTCAACAA CCTCAATGGT
    GAAGACCAAG
    101 ATATCCTAAT GGACAATAAC CTTCGTCGTC CAAACCTCGA
    GGCATTCAAC
    151 CGTGCTGTCA AGTCTCTGCA GAATGCATCA GCAATTGAGA
    GCATTCTTAA
    201 AAATCTCCTG CCATGTCTGC CGCTAGCCAC GGCCGCACCC
    ACGCGACATC
    251 CAATCCATAT CAAGGACGGT GACTGGAATG AATTCCGTCG
    TAAACTGACC
    301 TTCTATCTGA AAACCTTGGA GAACGCGCAG GCTCAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT
    ACTATCAACC
    401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT
    GGCTACCCAG
    451 GGTGCCATGC CGGCCTTCGC CTCTGCTTTC CAGCGCCGGG
    CAGGAGGGGT
    501 CCTGGTTGCT AGCCATCTGC AGAGCTTCCT GGAGGTGTCG
    TACCGCGTTC
    551 TACGCCACCT TGCGCAGCCC ACACCATTGG GCCCTGCCAG
    CTCCCTGCCC
    601 CAGAGCTTCC TGCTCAAGTC TTTAGAGCAA GTGAGAAAGA
    TCCAGGGCGA
    651 TGGCGCAGCG CTCCAGGAGA AGCTGTGTGC CACCTACAAG
    CTGTGCCACC
    701 CCGAGGAGCT GGTGCTGCTC GGACACTCTC TGGGCATCCC
    CTGGGCTCCC
    751 CTGAGCTCCT GCCCCAGCCA GGCCCTGCAG CTGGCAGGCT
    GCTTGAGCCA
    801 ACTCCATAGC GGCCTTTTCC TCTACCAGGG GCTCCTGCAG
    GCCCTGGAAG
    851 GGATATCCCC CGAGTTGGGT CCCACCTTGG ACACACTGCA
    GCTGGACGTC
    901 GCCGACTTTG CCACCACCAT CTGGCAGCAG ATGGAAGAAC
    TGGGAATGGC
    951 CCCTGCCCTG CAGCCCTAAT AA
    pMON28505 (SEQ ID NO: 118)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAAC TTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTA
    ATCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCA
    ATCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTT
    CTATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCG
    GTGGAGGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCG
    TCTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGGAGGTTCACCC
    TTTGCCTACACCTGTCCTGCTGCCTGCTGTGGACTTTAGCTTGGGAGAAT
    GGAAAACCCAGATGGAGGAGACCAAGGCACAGGACATTCTGGGAGCAGTG
    ACCCTTCTGCTGGAGGGAGTGATGGCAGCACGGGGACAACTGGGACCCAC
    TTGCCTCTCATCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCCTCC
    TTGGGGCCCTGCAGAGCCTCCTTGGAACCCAGCTTCCTCCACAGGGCAGG
    ACCACAGCTCACAAGGATCCCAATGCCATCTTCCTGAGCTTCCAACACCT
    GCTCCGAGGAAAGGTGCGTTTCCTGATGCTTGTAGGAGGGTCCACCCTCT
    GCGTCAGGGAATTCGGCGGCAACATGGCGTCTCCCGCTCCGCCTGCTTGT
    GACCTCCGAGTCCTCAGTAAACTGCTTCGTGACTCCCATGTCCTTCACAG
    CAGACTGAGCCAGTGCCCA
    pMON28506 (SEQ ID NO: 119)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGCTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC
    TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGG
    TGGAGGCTCCCCCGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGTTGCCTACACCT
    GTCCTGCTGCCTGCTGTGGACTTTAGCTTGGGAGAATGGAAAACCCAGAT
    GGAGGAGACCAAGGCACAGGACATTCTGGGAGCAGTGACCCTTCTGCTGG
    AGGGAGTGATGGCAGCACGGGGACAACTGGGACCCACTTGCCTCTCATCC
    CTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCCTCCTTGGGGCCCTGCA
    GAGCCTCCTTGGAACCCAGCTTCCTCCACAGGGCAGGACCACAGCTCACA
    AGGATCCCAATGCCATCTTCCTGAGCTTCCAACACCTGCTCCGAGGAAAG
    GTGCGTTTCCTGATGCTTGTAGGAGGGTCCACCCTCTGCGTCAGGGAATT
    CGGCGGCAACATGGCGTCTCCCGCTCCGCCTGCTTGTGACCTCCGAGTCC
    TCAGTAAACTGCTTCGTGACTCCCATGTCCTTCACAGCAGACTGAGCCAG
    TGCCCAGAGGTTCACCCT
    pMON28507 (SEQ ID NO: 120)
    CCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTCCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGCGAAAAACTGACGTTC
    TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGG
    TGGAGGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGGTCCTGCTGCCT
    GCTGTGGACTTTAGCTTGGGAGAATGGAAAACCCAGATGGAGGAGACCAA
    GGCACAGGACATTCTGGGAGCAGTGACCCTTCTGCTGGAGGGAGTGATGG
    CAGCACGGGGACAACTGGCACCCACTTGCCTCTCATCCCTCCTGGGGCAG
    CTTTCTGGACAGGTCCGTCTCCTCCTTGGGGCCCTGCAGAGCCTCCTTGG
    AACCCAGCTTCCTCCACAGGGCAGGACCACAGCTCACAAGGATCCCAATG
    CCATCTTCCTGAGCTTCCAACACCTGCTCCGAGGAAAGGTGCGTTTCCTG
    ATGCTTGTAGGAGGGTCCACCCTCTGCGTCAGCGAATTCGGCGGCAACAT
    GGCGTCTCCCGCTCCGCCTGCTTGTGACCTCCGAGTCCTCAGTAAACTGC
    TTCGTGACTCCCATGTCCTTCACAGCAGACTGAGCCAGTGCCCAGAGGTT
    CACCCTTTGCCTACACCT
    pMON28508 (SEQ ID NO: 121)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC
    TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGG
    TGGAGGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGGCTGTGGACTTT
    AGCTTGGGAGAATGGAAAACCCAGATGGAGCAGACCAAGGCACAGGACAT
    TCTGGGAGCAGTGACCCTTCTGCTGGAGGGAGTGATGGCAGCACGGGGAC
    AACTGGGACCCACTTGCCTCTCATCCCTCCTGGGGCAGCTTTCTGGACAG
    GTCCGTCTCCTCCTTGGGGCCCTGCAGAGCCTCCTTGGAACCCAGCTTCC
    TCCACAGGGCAGGACCACAGCTCACAAGGATCCCAATGCCATCTTCCTGA
    GCTTCCAACACCTGCTCCGAGGAAAGGTGCGTTTCCTGATGCTTGTAGGA
    GGGTCCACCCTCTGCGTCAGGGAATTCGGCGGCAACATGGCGTCTCCCGC
    TCCGCCTGCTTGTGACCTCCGAGTCCTCAGTAAACTGCTTCGTGACTCCC
    ATGTCCTTCACAGCAGACTGAGCCAGTGCCCAGAGGTTCACCCTTTGCCT
    ACACCTGTCCTGCTGCCT
    pMON28509 (SEQ ID NO: 122)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTCCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC
    TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGG
    TGGAGGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGGACTTTAGCTTG
    GGAGAATGGAAAACCCAGATGGAGGAGACCAAGGCACAGGACATTCTGGG
    AGCAGTGACCCTTCTGCTGGAGGGAGTGATGGCAGCACGGGGACAACTGG
    GACCCACTTGCCTCTCATCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGT
    CTCCTCCTTGGGGCCCTGCAGAGCCTCCTTGGAACCCAGCTTCCTCCACA
    GGGCAGGACCACAGCTCACAAGGATCCCAATGCCATCTTCCTGAGCTTCC
    AACACCTGCTCCGAGGAAAGGTGCGTTTCCTGATGCTTGTAGGAGGGTCC
    ACCCTCTGCGTCACGGAATTCGGCGGCAACATGGCGTCTCCCGCTCCGCC
    TGCTTGTGACCTCCGAGTCCTCAGTAAACTGCTTCGTGACTCCCATGTCC
    TTCACAGCAGACTGAGCCAGTGCCCAGAGGTTCACCCTTTGCCTACACCT
    GTCCTGCTGCCTGCTGTG
    pMON28510 (SEQ ID NO: 123)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC
    TATCGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGGT
    GGAGGCTCCCCGGGGAACCGTCTGGTCCAATCTCTACTATCAACCCGTCT
    CCTCCGTCTAAAGAATCTCATAAACTCCAAACATGGGAGAATGGAAAACC
    CAGATGGAGGAGACCAAGGCACAGGACATTCTGGAGCAGTGACCCTTCTG
    CTGGAGGGAGTGATGGCAGCACGGGGACAACTGGGACCCACTTGCTCTCA
    TCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCCTCCTTGGGGCCCT
    GCAGGCCTCCTTGGAACCCAGCTTCCTCCACAGGGCAGGACCACAGCTCA
    CAAGGATCCCAATGCATCTTCCTGAGCTTCCAACACCTGCTCCGAGGAAA
    GGTGCGTTTCCTGATGCTTGTAGGGGGTCCACCCTCTGCGTCAGCGAATT
    CGGCGGCAACATGGCGTCTCCCGCTCCGCCTGCTGTGACCTCCGAGTCCT
    CAGTAAACTGCTTCGTGACTCCCATGTCCTTCACAGCAGACTGACCAGTG
    CCCAGAGGTTCACCCTTTGCCTACACCTGTCCTGCTGCCTGCTGTGGACT
    TTAGTTG
    pMON28511 (SEQ ID NO: 124)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCCACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC
    TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGG
    TGGAGGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGGGACCCACTTGC
    CTCTCATCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCCTCCTTGG
    GGCCCTGCAGAGCCTCCTTGGAACCCAGCTTCCTCCACAGGGCAGGACCA
    CAGCTCACAAGGATCCCAATGCCATCTTCCTGAGCTTCCAACACCTGCTC
    CGAGGAAAGGTGCGTTTCCTGATGCTTGTAGGAGGGTCCACCCTCTGCGT
    CAGGGAATTCGGCGGCAACATGGCGTCTCCCGCTCCGCCTGCTTGTGACC
    TCCGAGTCCTCAGTAAACTGCTTCGTGACTCCCATGTCCTTCACAGCAGA
    CTGAGCCAGTGCCCAGAGGTTCACCCTTTGCCTACACCTGTCCTGCTGCC
    TGCTGTGGACTTTAGCTTGGGAGAATGGAAAACCCAGATGGAGGAGACCA
    AGGCACAGGACATTCTGGGAGCAGTGACCCTTCTGCTGGAGGGAGTGATG
    GCAGCACGGGGACAACTG
    pMON28512 (SEQ ID NO: 125)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC
    TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGACCGCGG
    TGGAGGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGGGAACGCAGCTT
    CCTCCACAGGGCAGGACCACAGCTCACAAGGATCCCAATGCCATCTTCCT
    GAGCTTCCAACACCTGCTCCGAGGAAAGGTGCGTTTCCTGATGCTTGTAG
    GAGGGTCCACCCTCTGCGTCAGGGAATTCGGCGGCAACATGGCGTCTCCC
    GCTCCGCCTGCTTGTGACCTCCGAGTCCTCAGTAAACTGCTTCGTGACTC
    CCATGTCCTTCACAGCAGACTGAGCCAGTGCCCAGAGGTTCACCCTTTGC
    CTACACCTGTCCTGCTGCCTGCTGTGGACTTTAGCTTGGGAGAATGGAAA
    ACCCAGATGGAGGAGACCAAGGCACAGGACATTCTGGGAGCAGTGACCCT
    TCTGCTGGAGGGAGTGATGGCAGCACGGGGACAACTGGGACCCACTTGCC
    TCTCATCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCCTCCTTGGG
    GCCCTGCAGAGCCTCCTT
    pMON28513 (SEQ ID NO: 126)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC
    TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGG
    TGGAGGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGGGCAGGACCACA
    GCTCACAAGGATCCCAATGCCATCTTCCTGAGCTTCCAACACCTGCTCCG
    AGCAAAGGTGCGTTTCCTGATGCTTGTAGCAGGGTCCACCCTCTGCGTCA
    GGGAATTCGGCGGCAACATGGCGTCTCCCGCTCCGCCTGCTTGTGACCTC
    CGAGTCCTCAGTAAACTGCTTCGTGACTCCCATGTCCTTCACAGCAGACT
    GAGCCAGTGCCCAGAGGTTCACCCTTTGCCTACACCTGTCCTGCTGCCTG
    CTCTGGACTTTAGCTTGGGAGAATGGAAAACCCAGATGGAGGAGACCAAG
    GCACAGGACATTCTGGGAGCAGTGACCCTTCTGCTGGAGGGACTGATGGC
    AGCACGGGGACAACTGGGACCCACTTGCCTCTCATCCCTCCTGGGGCAGC
    TTTCTGGACAGGTCCGTCTCCTCCTTGGGGCCCTCCAGAGCCTCCTTGGA
    ACCCAGCTTCCTCCACAG
    pMON28514 (SEQ ID NO: 127)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC
    TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGG
    TGGAGGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGGCTCACAAGGAT
    CCCAATGCCATCTTCCTGAGCTTCCAACACCTGCTCCGAGGAAAGGTGCG
    TTTCCTGATGCTTGTAGGAGGGTCCACCCTCTGCGTCAGGGAATTCGGCG
    GCAACATGGCGTCTCCCGCTCCGCCTCCTTGTGACCTCCGAGTCCTCAGT
    AAACTGCTTCGTGACTCCCATGTCCTTCACAGCAGACTGAGCCAGTGCCC
    AGAGGTTCACCCTTTGCCTACACCTGTCCTGCTGCCTGCTGTGGACTTTA
    GCTTGGGAGAATGGAAAACCCAGATGGAGGAGACCAAGGCACAGGACATT
    CTGGGAGCAGTGACCCTTCTGCTGGAGGGAGTGATGGCAGCACGGGGACA
    ACTGGGACCCACTTGCCTCTCATCCCTCCTGGGGCAGCTTTCTGGACAGG
    TCCGTCTCCTCCTTGGGGCCCTGCAGAGCCTCCTTGGAACCCAGCTTCCT
    CCACAGGGCAGGACCACA
    pMON28515 (SEQ ID NO: 128)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC
    TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGG
    TGGAGGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGGATCCCAATGCC
    ATCTTCCTGAGCTTCCAACACCTGCTCCGAGGAAAGGTGCGTTTCCTGAT
    GCTTGTAGGAGGGTCCACCCTCTGCGTCAGGGAATTCGGCGGCAACATGG
    CGTCTCCCGCTCCGCCTGCTTCTGACCTCCGAGTCCTCAGTAAACTGCTT
    CGTGACTCCCATGTCCTTCACAGCAGACTGAGCCAGTGCCCAGAGGTTCA
    CCCTTTGCCTACACCTGTCCTGCTGCCTGCTGTGGACTTTAGCTTGGGAG
    AATGGAAAACCCAGATGGAGGAGACCAAGGCACAGGACATTCTGGGAGCA
    GTGACCCTTCTGCTGGAGGGAGTGATGGCAGCACGCGGACAACTGGGACC
    CACTTGCCTCTCATCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCC
    TCCTTGGGGCCCTGCAGAGCCTCCTTGGAACCCAGCTTCCTCCACAGGGC
    AGGACCACAGCTCACAAG
    pMON28516 (SEQ ID NO: 129)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC
    TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGG
    TGGAGGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGGCCATCTTCCTG
    AGCTTCCAACACCTGCTCCGAGGAAAGGTGCGTTTCCTGATGCTTGTAGG
    AGGGTCCACCCTCTGCGTCAGGGAATTCGGCGGCAACATGGCGTCTCCCG
    CTCCGCCTGCTTGTGACCTCCGAGTCCTCAGTAAACTGCTTCGTGACTCC
    CATGTCCTTCACAGCAGACTGAGCCAGTGCCCAGAGGTTCACCCTTTGCC
    TACACCTGTCCTGCTGCCTGCTGTGGACTTTAGCTTGGGAGAATGGAAAA
    CCCAGATGGAGGAGACCAAGGCACAGGACATTCTGGGAGCAGTGACCCTT
    CTGCTGGAGGGAGTGATGGCAGCACGGGGACAACTGGGACCCACTTGCCT
    CTCATCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCCTCCTTGGGG
    CCCTGCAGAGCCTCCTTGGAACCCAGCTTCCTCCACAGGGCAGGACCACA
    GCTCACAAGGATCCCAAT
    pMON28519 (SEQ ID NO: 130)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC
    TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGG
    TGGAGGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGGAGGTTCACCCT
    TTGCCTACACCTGTCCTGCTGCCTGCTGTGGACTTTAGCTTGGGAGAATG
    GAAAACCCAGATGGAGGAGACCAAGGCACAGGACATTCTGGGAGCAGTGA
    CCCTTCTGCTGGAGGGAGTGATGGCAGCACGGGGACAACTGGGACCCACT
    TGCCTCTCATCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCCTCCT
    TGGGGCCCTGCAGAGCCTCCTTGGAACCCAGCTTCCTCCACAGGGCAGGA
    CCACAGCTCACAAGGATCCCAATGCCATCTTCCTGAGCTTCCAACACCTG
    CTCCGAGGAAAGGTGCGTTTCCTGATGCTTGTAGGAGGGTCCACCCTCTG
    CGTCAGGGAATTCGGCAACATGGCGTCTCCCGCTCCGCCTGCTTGTGACC
    TCCGAGTCCTCAGTAAACTGCTTCGTGACTCCCATGTCCTTCACAGCAGA
    CTGAGCCAGTGCCCA
    pMON28520 (SEQ ID NO: 131)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGCCAAGAATTCCGGGAAAAACTGACGTTC
    TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGG
    TGGAGGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCCT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGTTGCCTACACCT
    GTCCTGCTGCCTGCTGTGGACTTTAGCTTGGGAGAATGGAAAACCCAGAT
    GGAGGAGACCAAGGCACAGGACATTCTGGGAGCAGTGACCCTTCTGCTGG
    AGGGAGTGATGGCAGCACGGGGACAACTGGGACCCACTTGCCTCTCATCC
    CTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCCTCCTTGGGGCCCTGCA
    GAGCCTCCTTGGAACCCAGCTTCCTCCACAGGGCAGGACCACAGCTCACA
    AGGATCCCAATGCCATCTTCCTGAGCTTCCAACACCTGCTCCGAGGAAAG
    GTGCGTTTCCTGATGCTTGTAGGAGGGTCCACCCTCTGCGTCAGGGAATT
    CGGCAACATGGCGTCTCCCGCTCCGCCTGCTTGTGACCTCCGAGTCCTCA
    GTAAACTGCTTCGTGACTCCCATGTCCTTCACAGCAGACTGAGCCAGTGC
    CCAGAGGTTCACCCT
    pMON28521 (SEQ ID NO: 132)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC
    TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACCTAGAGGGCGG
    TGGAGGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGGTCCTGCTGCCT
    GCTGTGGACTTTAGCTTGGGAGAATGGAAAACCCAGATGGAGGAGACCAA
    GGCACAGGACATTCTGGGAGCAGTGACCCTTCTGCTGGAGGGAGTGATGG
    CAGCACGGGGACAACTGGGACCCACTTGCCTCTCATCCCTCCTGGGGCAG
    CTTTCTGGACAGGTCCGTCTCCTCCTTGGGGCCCTGCAGAGCCTCCTTGG
    AACCCAGCTTCCTCCACAGGGCAGGACCACAGCTCACAAGGATCCCAATG
    CCATCTTCCTGAGCTTCCAACACCTGCTCCGAGGAAAGGTGCGTTTCCTG
    ATGCTTGTAGGAGGGTCCACCCTCTGCGTCAGGGAATTCGGCAACATGGC
    GTCTCCCGCTCCGCCTGCTTGTGACCTCCGAGTCCTCAGTAAACTGCTTC
    GTGACTCCCATGTCCTTCACAGCAGACTGAGCCAGTGCCCAGAGGTTCAC
    CCTTTGCCTACACCT
    pMON28522 (SEQ ID NO: 133)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC
    TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGG
    TGGAGGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGGCTGTGGACTTT
    AGCTTGGGAGAATGGAAAACCCAGATGGAGGAGACCAAGGCACAGGACAT
    TCTGGGAGCAGTGACCCTTCTGCTGGAGGGAGTGATGGCAGCACGGGGAC
    AACTGGGACCCACTTGCCTCTCATCCCTCCTGGGCCAGCTTTCTGGACAG
    GTCCGTCTCCTCCTTGGGGCCCTGCAGAGCCTCCTTGGAACCCAGCTTCC
    TCCACAGGGCAGGACCACAGCTCACAAGGATCCCAATGCCATCTTCCTGA
    GCTTCCAACACCTGCTCCGAGGAAAGGTGCGTTTCCTGATGCTTGTAGGA
    GCGTCCACCCTCTGCCTCAGGGAATTCGGCAACATGGCGTCTCCCGCTCC
    GCCTGCTTGTGACCTCCGAGTCCTCAGTAAACTGCTTCGTGACTCCCATG
    TCCTTCACAGCAGACTGAGCCAGTGCCCAGAGGTTCACCCTTTGCCTACA
    CCTGTCCTGCTGCCT
    pMON28523 (SEQ ID NO: 134)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC
    TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGG
    TGGAGGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGGACTTTAGCTTG
    GGAGAATGGAAAACCCAGATGGAGGAGACCAAGGCACAGGACATTCTGGG
    AGCAGTGACCCTTCTGCTGGAGGGAGTGATGGCAGCACGGGGACAACTGG
    GACCCACTTGCCTCTCATCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGT
    CTCCTCCTTGGGGCCCTGCAGAGCCTCCTTGGAACCCAGCTTCCTCCACA
    GGGCAGGACCACAGCTCACAAGGATCCCAATGCCATCTTCCTGAGCTTCC
    AACACCTGCTCCGAGGAAAGGTGCGTTTCCTGATGCTTGTAGGAGGGTCC
    ACCCTCTGCGTCAGGGAATTCGGCAACATGGCGTCTCCCGCTCCGCCTGC
    TTGTGACCTCCGAGTCCTCAGTAAACTGCTTCGTGACTCCCATGTCCTTC
    ACAGCAGACTGAGCCAGTGCCCAGAGGTTCACCCTTTGCCTACACCTGTC
    CTGCTGCCTGCTGTG
    pMON28524 (SEQ ID NO: 135)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCCACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC
    TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGG
    TGGACGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGGGAGAATGCAAA
    ACCCAGATGGAGGAGACCAAGGCACAGGACATTCTGGGAGCAGTGACCCT
    TCTGCTGGAGGGAGTGATGGCAGCACGGGGACAACTGGGACCCACTTGCC
    TCTCATCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCCTCCTTGGG
    GCCCTGCAGAGCCTCCTTGGAACCCAGCTTCCTCCACAGGGCAGGACCAC
    AGCTCACAAGGATCCCAATGCCATCTTCCTGAGCTTCCAACACCTGCTCC
    GAGGAAAGGTGCGTTTCCTGATGCTTGTAGGAGGGTCCACCCTCTGCGTC
    AGGGAATTCGGCAACATGGCGTCTCCCGCTCCGCCTGCTTGTGACCTCCG
    AGTCCTCAGTAAACTGCTTCGTGACTCCCATGTCCTTCACAGCAGACTGA
    GCCAGTGCCCAGAGGTTCACCCTTTGCCTACACCTGTCCTGCTGCCTGCT
    GTGGACTTTAGCTTG
    pMON28525 (SEQ ID NO: 136)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTACAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC
    TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGG
    TGGAGGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGGGACCCACTTGC
    CTCTCATCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCCTCCTTGG
    GGCCCTGCAGAGCCTCCTTGGAACCCAGCTTCCTCCACAGGGCAGGACCA
    CAGCTCACAAGGATCCCAATGCCATCTTCCTGAGCTTCCAACACCTGCTC
    CGAGGAAAGGTGCGTTTCCTGATGCTTGTAGGAGGGTCCACCCTCTGCGT
    CAGGGAATTCGGCAACATGGCGTCTCCCGCTCCGCCTGCTTGTGACCTCC
    GAGTCCTCAGTAAACTGCTTCGTGACTCCCATGTCCTTCACAGCAGACTG
    AGCCAGTGCCCAGAGGTTCACCCTTTGCCTACACCTGTCCTGCTGCCTGC
    TGTGGACTTTAGCTTGGGAGAATGGAAAACCCAGATGGAGGAGACCAAGG
    CACAGGACATTCTGGGAGCAGTGACCCTTCTGCTGGAGGGAGTGATGGCA
    GCACGGGGACAACTG
    pMON28526 (SEQ ID NO: 137)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC
    TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGG
    TGGAGGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGGGAACCCAGCTT
    CCTCCACAGGGCAGGACCACAGCTCACAAGGATCCCAATGCCATCTTCCT
    GAGCTTCCAACACCTGCTCCGAGGAAAGGTGCGTTTCCTGATGCTTGTAG
    GAGGGTCCACCCTCTGCGTCAGGGAATTCGGCAACATGGCGTCTCCCGCT
    CCGCCTGCTTGTGACCTCCGAGTCCTCAGTAAACTGCTTCGTGACTCCCA
    TGTCCTTCACAGCAGACTGAGCCAGTGCCCAGAGGTTCACCCTTTGCCTA
    CACCTGTCCTGCTGCCTGCTGTGGACTTTAGCTTGGGAGAATGGAAAACC
    CAGATGGAGGAGACCAAGGCACAGGACATTCTGGGAGCAGTGACCCTTCT
    GCTGGAGGGAGTGATGGCAGCACGGGGACAACTGGGACCCACTTGCCTCT
    CATCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCCTCCTTGGGGCC
    CTGCAGAGCCTCCTT
    pMON28527 (SEQ ID NO: 138)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGCAAAAACTGACGTTC
    TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGG
    TGGAGCCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGGGCAGGACCACA
    GCTCACAAGGATCCCAATGCCATCTTCCTGAGCTTCCAACACCTGCTCCG
    AGGAAAGGTGCGTTTCCTGATGCTTGTAGGAGGGTCCACCCTCTGCGTCA
    GGGAATTCGGCAACATGGCGTCTCCCGCTCCGCCTGCTTGTGACCTCCGA
    GTCCTCAGTAAACTGCTTCGTGACTCCCATGTCCTTCACAGCAGACTGAG
    CCAGTGCCCAGACGTTCACCCTTTGCCTACACCTGTCCTGCTGCCTCCTG
    TGGACTTTAGCTTGGGAGAATGCAAAACCCAGATGGAGGAGACCAAGGCA
    CAGGACATTCTGGGAGCAGTGACCCTTCTGCTGGAGGGAGTGATGGCAGC
    ACGGGGACAACTGGGACCCACTTGCCTCTCATCCCTCCTGGGGCAGCTTT
    CTGGACAGGTCCGTCTCCTCCTTGGGGCCCTGCAGAGCCTCCTTGGAACC
    CAGCTTCCTCCACAG
    pMON28528 (SEQ ID NO: 139)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC
    TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGG
    TGGAGGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGGCTCACAAGGAT
    CCCAATGCCATCTTCCTGAGCTTCCAACACCTGCTCCGAGGAAAGGTGCG
    TTTCCTGATGCTTGTAGGAGGGTCCACCCTCTGCGTCAGGGAATTCGGCA
    ACATGGCGTCTCCCGCTCCGCCTGCTTGTGACCTCCGAGTCCTCAGTAAA
    CTGCTTCGTGACTCCCATGTCCTTCACAGCAGACTGAGCCAGTGCCCAGA
    GGTTCACCCTTTGCCTACACCTGTCCTGCTGCCTGCTGTGGACTTTAGCT
    TGGGAGAATGGAAAACCCAGATGGAGGAGACCAAGGCACAGGACATTCTG
    GGAGCAGTGACCCTTCTGCTGGAGGGAGTGATGGCAGCACGGGGACAACT
    GGGACCCACTTGCCTCTCATCCCTCCTGGGGCAGCTTTCTGGACAGGTCC
    GTCTCCTCCTTGGGGCCCTGCAGAGCCTCCTTGGAACCCAGCTTCCTCCA
    CAGGGCAGGACCACA
    pMON28529 (SEQ ID NO: 140)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC
    TATCTGGTTACCCTTGACCAAGCGCAGGAACAACAGTACGTAGAGGCCGG
    TGGAGGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGGATCCCAATGCC
    ATCTTCCTGAGCTTCCAACACCTGCTCCGAGGAAAGGTGCGTTTCCTGAT
    GCTTGTAGGAGGGTCCACCCTCTGCGTCAGGGAATTCGGCAACATGGCGT
    CTCCCGCTCCGCCTGCTTGTGACCTCCGAGTCCTCAGTAAACTGCTTCGT
    GACTCCCATGTCCTTCACAGCAGACTGAGCCAGTGCCCAGAGGTTCACCC
    TTTGCCTACACCTGTCCTGCTGCCTGCTGTGGACTTTAGCTTGGGAGAAT
    GGAAAACCCAGATGGAGGAGACCAAGGCACAGGACATTCTGGGAGCAGTG
    ACCCTTCTGCTGGAGGGAGTGATGGCAGCACGGCGACAACTGGGACCCAC
    TTGCCTCTCATCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCCTCC
    TTGGGGCCCTGCAGAGCCTCCTTGGAACCCAGCTTCCTCCACAGGGCAGG
    ACCACAGCTCACAAG
    pMON28530 (SEQ ID NO: 141)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC
    TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGG
    TGGAGGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGGCCATCTTCCTG
    AGCTTCCAACACCTGCTCCGAGGAAAGGTGCGTTTCCTGATGCTTGTAGG
    AGGGTCCACCCTCTGCGTCAGGGAATTCGGCAACATGGCGTCTCCCGCTC
    CGCCTGCTTGTGACCTCCGAGTCCTCAGTAAACTGCTTCGTGACTCCCAT
    GTCCTTCACAGCAGACTGAGCCAGTGCCCAGAGGTTCACCCTTTGCCTAC
    ACCTGTCCTGCTGCCTGCTGTGGACTTTAGCTTGGGAGAATGGAAAACCC
    AGATGGAGGAGACCAAGGCACAGGACATTCTGGGAGCAGTGACCCTTCTG
    CTGGAGGGAGTGATGGCAGCACGGGGACAACTGGGACCCACTTGCCTCTC
    ATCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCCTCCTTGGGGCCC
    TGCAGAGCCTCCTTGGAACCCAGCTTCCTCCACAGGGCAGGACCACAGCT
    CACAAGGATCCCAAT
    pMON28533 (SEQ ID NO: 142)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTGACTTCCAAACCTGGAGAGCTTCGTAAGGG
    CTGTCAAGAACTTAGAAAATGCATCAGGTATGAGGCAATTCTTCGTAATC
    TCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGCATCCAATCA
    TCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTCTAT
    TGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGGTGGA
    GGCTCCCCGGTAACCGTCTGGTCCAATCTCTACTATCAACCCGTCTCCTC
    CGTCTAAAGAATCTCATAAATCTCCAAACATGGAGGTTCACCCTTTGCCT
    ACACCTGTCCTGCTGCCTGCTGTGGACTTTAGCTTGCGAGAATGGAAAAC
    CCAGATGGAGGAGACCAAGGCACAGGACATTCTGGGAGCAGTGACCCTTC
    TGCTGGAGGGAGTGATGGCAGCACGGGGACAACTGGGACCCACTTGCCTC
    TCATCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCCTCCTTGGGGC
    CCTGCAGAGCCTCCTTGGAACCCAGCTTCCTCCACAGGGCAGGACCACAG
    CTCACAAGGATCCCAATGCCATCTTCCTGAGCTTCCAACACCTGCTCCGA
    GGAAAGGTGCGTTTCCTGATGCTTGTAGGAGGGTCCACCCTCTGCGTCAG
    GGAATTCGGCGGCAACGGCGGCAACATGGCGTCCCCAGCGCCGCCTGCTT
    GTGACCTCCGAGTCCTCAGTAAACTGCTTCGTGACTCCCATGTCCTTCAC
    AGCAGACTGAGCCAGTGCCCA
    pMON28534 (SEQ ID NO: 143)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC
    TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGG
    TGGAGGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGTTGCCTACACCT
    GTCCTGCTGCCTGCTGTCGACTTTAGCTTGGGAGAATGGAAAACCCAGAT
    GGAGGAGACCAAGGCACAGGACATTCTGGGAGCAGTGACCCTTCTGCTGG
    AGGGAGTGATGGCAGCACGGGGACAACTGGGACCCACTTGCCTCTCATCC
    CTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCCTCCTTGGCGCCCTGCA
    GAGCCTCCTTGGAACCCAGCTTCCTCCACAGGGCAGGACCACAGCTCACA
    AGGATCCCAATGCCATCTTCCTGAGCTTCCAACACCTGCTCCGAGGAAAG
    GTGCGTTTCCTGATGCTTGTAGGAGGGTCCACCCTCTGCGTCAGGGAATT
    CGGCGGCAACGGCGGCAACATGGCGTCCCCAGCGCCGCCTGCTTGTGACC
    TCCGAGTCCTCAGTAAACTGCTTCGTGACTCCCATGTCCTTCACAGCAGA
    CTGAGCCAGTGCCCAGAGGTTCACCCT
    pMON28535 (SEQ ID NO: 144)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC
    TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGG
    TGGAGGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGGTCCTGCTGCCT
    GCTGTGGACTTTAGCTTGGGAGAATGGAAAACCCAGATGGAGGAGACCAA
    GGCACAGGACATTCTGGGAGCAGTGACCCTTCTGCTGGAGGGAGTGATGG
    CAGCACGGGGACAACTGGGACCCACTTGCCTCTCATCCCTCCTGGGGCAG
    CTTTCTGGACAGGTCCGTCTCCTCCTTGGGGCCCTGCAGAGCCTCCTTGG
    AACCCAGCTTCCTCCACAGGGCAGGACCACAGCTCACAAGGATCCCAATG
    CCATCTTCCTGAGCTTCCAACACCTGCTCCGAGGAAAGGTGCGTTTCCTG
    ATGCTTGTAGGAGGGTCCACCCTCTGCGTCAGGGAATTCGGCGGCAACGG
    CGGCAACATGGCGTCCCCAGCGCCGCCTGCTTGTGACCTCCGAGT CCTC
    AGTAAACTGCTTCGTGACTCCCATGTCCTTCACAGCAGACTGAGCCAGTG
    CCCAGAGGTTCACCCTTTGCCTACACCT
    pMON28536 (SEQ ID NO: 145)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC
    TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGG
    TGGAGGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGGCTGTGGACTTT
    AGCTTGGGAGAATGGAAAACCCAGATGGAGGAGACCAAGGCACAGGACAT
    TCTGGGAGCAGTGACCCTTCTGCTGGAGGGAGTGATGGCAGCACGGGGAC
    AACTGGGACCCACTTGCCTCTCATCCCTCCTGGGGCAGCTTTCTGGACAG
    GTCCGTCTCCTCCTTGGGGCCCTGCAGAGCCTCCTTGGAACCCAGCTTCC
    TCCACAGGGCAGGACCACAGCTCACAAGGATCCCAATGCCATCTTCCTGA
    GCTTCCAACACCTGCTCCGAGGAAAGGTGCGTTTCCTGATGCTTGTAGGA
    GGGTCCACCCTCTGCGTCAGGGAATTCGGCGGCAACGGCGGCAACATGGC
    GTCCCCAGCGCCGCCTGCTTGTGACCTCCGAGTCCTCAGTAAACTGCTTC
    GTGACTCCCATGTCCTTCACAGCAGACTGAGCCAGTGCCCAGAGGTTCAC
    CCTTTGCCTACACCTGTCCTGCTGCCT
    pMON28537 (SEQ ID NO: 146)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC
    TATCTGGTTACCCTTCAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGG
    TGGAGGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTGCAAACATGGACTTTAGCTTG
    GGAGAATGGAAAACCCAGATGGAGGAGACCAAGGCACAGGACATTCTGGG
    AGCAGTGACCCTTCTGCTGGAGGGAGTGATGGCAGCACGGGGACAACTGG
    GACCCACTTGCCTCTCATCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGT
    CTCCTCCTTGGGGCCCTGCAGAGCCTCCTTGGAACCCAGCTTCCTCCACA
    GGGCAGGACCACAGCTCACAAGGATCCCAATGCCATCTTCCTGAGCTTCC
    AACACCTGCTCCGAGGAAAGGTGCGTTTCCTGATGCTTGTAGGAGGGTCC
    ACCCTCTGCGTCAGGGAATTCGGCGGCAACGGCGGCAACATGGCGTCCCC
    AGCGCCGCCTGCTTGTGACCTCCGAGTCCTCAGTAAACTGCTTCGTGACT
    CCCATGTCCTTCACAGCAGACTGAGCCAGTGCCCAGAGGTTCACCCTTTG
    CCTACACCTGTCCTGCTGCCTGCTGTG
    pMON28538 (SEQ ID NO: 147)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC
    TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGCCGG
    TGGAGGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGGGAGAATGGAAA
    ACCCAGATGGAGGAGACCAAGGCACAGGACATTCTGGGAGCAGTGACCCT
    TCTGCTGGAGGGAGTGATGGCAGCACGGGGACAACTGGGACCCACTTGCC
    TCTCATCCCTCCTCGGGCAGCTTTCTGGACAGGTCCGTCTCCTCCTTGGG
    GCCCTGCAGAGCCTCCTTGGAACCCAGCTTCCTCCACAGGGCAGGACCAC
    AGCTCACAAGGATCCCAATGCCATCTTCCTGAGCTTCCAACACCTGCTCC
    GAGGAAAGGTGCGTTTCCTGATGCTTGTAGGAGGGTCCACCCTCTGCGTC
    AGGGAATTCGGCGGCAACGGCGGCAACATGGCGTCCCCAGCGCCGCCTGC
    TTGTGACCTCCGAGTCCTCAGTAAACTGCTTCGTGACTCCCATGTCCTTC
    ACAGCAGACTGAGCCAGTGCCCACAGGTTCACCCTTTGCCTACACCTGTC
    CTGCTGCCTGCTGTGGACTTTAGCTTG
    pMON28539 (SEQ ID NO: 148)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC
    TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGG
    TGGAGGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGGGACCCACTTGC
    CTCTCATCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCCTCCTTGG
    GGCCCTGCAGAGCCTCCTTGGAACCCAGCTTCCTCCACAGGGGAGGACCA
    CAGCTCACAAGGATCCCAATGCCATCTTCCTGAGCTTCCAACACCTGCTC
    CGAGGAAAGGTGCGTTTCCTGATGCTTGTAGGAGGGTCCACCCTCTGCGT
    CAGGGAATTCGGCGGCAACGGCGGCAACATGGCGTCCCCACCGCCGCCTG
    CTTGTGACCTCCGAGTCCTCAGTAAACTGCTTCGTGACTCCCATGTCCTT
    CACAGCAGACTGAGCCAGTGCCCAGAGGTTCACCCTTTGCCTACACCTGT
    CCTGCTGCCTGCTGTGGACTTTAGCTTGGGAGAATGGAAAACCCAGATGG
    AGGAGACCAAGGCACAGGACATTCTGGGAGCAGTGACCCTTCTGCTGGAG
    GGAGTGATGGCAGCACGGGGACAACTG
    pMON28540 (SEQ ID NO: 149)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC
    TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGCGCGG
    TGGAGGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGGGAACCCAGCTT
    CCTCCACAGGGCAGGACCACAGCTCACAAGGATCCCAATGCCATCTTCCT
    GAGCTTCCAACACCTGCTCCGAGGAAAGGTGCGTTTCCTGATCCTTGTAG
    GAGGGTCCACCCTCTGCGTCAGGGAATTCGGCGGCAACGGCGGCAACATG
    GCGTCCCCAGCGCCGCCTGCTTGTGACCTCCGAGTCCTCAGTAAACTGCT
    TCGTGACTCCCATGTCCTTCACAGCAGACTGAGCCAGTGCCCAGAGGTTC
    ACCCTTTGCCTACACCTGTCCTGCTGCCTGCTGTGGACTTTAGCTTGGGA
    GAATGGAAAACCCAGATGGAGGAGACCAAGGCACAGGACATTCTGGGAGC
    AGTGACCCTTCTGCTGGAGGGAGTGATGGCAGCACGGGGACAACTGGGAC
    CCACTTGCCTCTCATCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTC
    CTCCTTGGGGCCCTGCAGAGCCTCCTT
    pMON28541 (SEQ ID NO: 150)
    CCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC
    TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGG
    TGGAGGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGGGCAGGACCACA
    GCTCACAAGGATCCCAATGCCATCTTCCTGAGCTTCCAACACCTGCTCCG
    AGGAAAGGTGCGTTTCCTGATGCTTGTAGGAGGGTCCACCCTCTGCGTCA
    GGGAATTCGGCGGCAACGGCGGCAACATGGCGTCCCCAGCGCCGCCTGCT
    TGTGACCTCCGAGTCCTCAGTAAACTGCTTCGTGACTCCCATGTCCTTCA
    CAGCAGACTGAGCCAGTGCCCAGAGGTTCACCCTTTGCCTACACCTGTCC
    TGCTGCCTGCTGTGGACTTTAGCTTGGGAGAATGGAAAACCCAGATGGAG
    GAGACCAAGGCACAGGACATTCTGGGAGCAGTGACCCTTCTGCTGGAGGG
    AGTGATGGCAGCACGGGGACAACTGGGACCCACTTGCCTCTCATCCCTCC
    TGGGGCAGCTTTCTGGACAGGTCCGTCTCCTCCTTGGGGCCCTGCAGAGC
    CTCCTTGGAACCCAGCTTCCTCCACAG
    pMON28542 (SEQ ID NO: 151)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC
    TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGG
    TGGAGGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGGCTCACAAGGAT
    CCCAATGCCATCTTCCTGAGCTTCCAACACCTGCTCCGAGGAAAGGTGCG
    TTTCCTGATGCTTGTAGGAGGGTCCACCCTCTGCGTCAGGGAATTCGGCG
    GCAACGGCGGCAACATGGCGTCCCCAGCGCCGCCTGCTTGTGACCTCCGA
    GTCCTCAGTAAACTGCTTCGTGACTCCCATGTCCTTCACAGCAGACTGAG
    CCAGTGCCCAGAGGTTCACCCTTTGCCTACACCTGTCCTGCTGCCTGCTG
    TGGACTTTAGCTTGGGAGAATGGAAAACCCAGATGGAGGAGACCAAGGCA
    CAGGACATTCTGGGAGCAGTGACCCTTCTGCTGGAGGGAGTGATGGCAGC
    ACGGGGACAACTGGGACCCACTTGCCTCTCATCCCTCCTGGGGCAGCTTT
    CTGGACAGGTCCGTCTCCTCCTTGGGGCCCTGCAGAGCCTCCTTGGAACC
    CAGCTTCCTCCACAGGGCAGGACCACA
    pMON28543 (SEQ ID NO: 152)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGCCAAGAATTCCGGGAAAAACTGACGTTC
    TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGG
    TGGAGGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGGATCCCAATGCC
    ATCTTCCTGAGCTTCCAACACCTGCTCCGAGGAAAGGTGCGTTTCCTGAT
    GCTTGTAGCAGGGTCCACCCTCTGCGTCAGGGAATTCGGCGGCAACGGCG
    GCAACATGGCGTCCCCAGCGCCGCCTGCTTGTGACCTCCGAGTCCTCAGT
    AAACTGCTTCGTGACTCCCATGTCCTTCACAGCAGACTGAGCCAGTGCCC
    AGAGGTTCACCCTTTGCCTACACCTGTCCTGCTGCCTGCTGTGGACTTTA
    GCTTGGGAGAATGGAAAACCCAGATGGAGGAGACCAAGGCACAGGACATT
    CTGGGAGCAGTGACCCTTCTGCTGGAGGGAGTGATGGCAGCACGGGGACA
    ACTGGGACCCACTTGCCTCTCATCCCTCCTGGGGCAGCTTTCTGGACAGG
    TCCGTCTCCTCCTTGGGGCCCTGCAGAGCCTCCTTGGAACCCAGCTTCCT
    CCACAGGGCAGGACCACAGCTCACAAG
    pMON28544 (SEQ ID NO: 153)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC
    TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGG
    TGGAGGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGGCCATCTTCCTG
    AGCTTCCAACACCTGCTCCGAGGAAAGGTGCGTTTCCTGATGCTTGTAGG
    AGGGTCCACCCTCTGCGTCAGGGAATTCGGCGGCAACGGCGGCAACATGG
    CGTCCCCAGCGCCGCCTGCTTGTGACCTCCGAGTCCTCAGTAAACTGCTT
    CGTGACTCCCATGTCCTTCACAGCAGACTGAGCCAGTGCCCAGAGGTTCA
    CCCTTTGCCTACACCTGTCCTGCTGCCTGCTGTGGACTTTAGCTTGGGAG
    AATGGAAAACCCAGATGGAGGAGACCAAGGCACAGGACATTCTGGGAGCA
    GTGACCCTTCTGCTGGACGGAGTGATGGCAGCACGGGGACAACTGGGACC
    CACTTGCCTCTCATCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCC
    TCCTTGGGGCCCTGCAGAGCCTCCTTGGAACCCAGCTTCCTCCACAGGGC
    AGGACCACAGCTCACAAGGATCCCAAT
    pMON28545 (SEQ ID NO: 154)
    GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACC
    ACCTGCACCTTTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTA
    TCCTGATGGACCGAAACCTTCGACTTCCAAACCTGGAGAGCTTCGTAAGG
    GCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAGGCAATTCTTCGTAA
    TCTCCAACCATGTCTCCCCTCTGCCACGGCCGCACCCTCTCGACATCCAA
    TCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC
    TATCTGGTTACCCTTGAGCAACCGCAGGAACAACAGTACGTAGAGGGCGG
    TGGAGGCTCCCCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGT
    CTCCTCCGTCTAAAGAATCTCATAAATCTCCAAACATGGATCCCAATGCC
    ATCTTCCTGAGCTTCCAACACCTGCTCCGAGGAAAGGTGCGTTTCCTGAT
    GCTTGTAGGAGGGTCCACCCTCTGCGTCAGGGAATTCGGCGGCAACATGG
    CGTCTCCCGCTCCGCCTGCTTGTGACCTCCGAGTCCTCAGTAAACTGCTT
    CGTGACTCCCATGTCCTTCACAGCAGACTGAGCCAGTGCCCAGAGGTTCA
    CCCTTTGCCTACACCTGTCCTGCTGCCTGCTGTGGACTTTAGCTTGGGAG
    AATGGAAAACCCAGATGGAGGAGACCAAGGCACAGGACATTCTGGGAGCA
    GTGACCCTTCTGCTGGAGGGAGTGATGGCAGCACGGGGACAACTGGGACC
    CACTTGCCTCTCATCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCC
    TCCTTGGGGCCCTGCAGAGCCTCCTTGGAACCCAGGGCAGGACCACAGCT
    CACAAG
    pMON15981 (SEQ ID NO: 155)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT
    ACTATCAACC
    401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT
    GTCTTACAAG
    451 CTGTGCCACC CCGAGGAGCT GGTGCTGCCTC GGACACTCTC
    TGGGCATCCC
    501 CTGGGCTCCC CTGAGCTCCT GCCCCAGCCA GGCCCTGCAG
    CTGGCAGGCT
    551 GCTTGAGCCA ACTCCATAGC GGCCTTTTCC TCTACCAGGG
    GCTCCTGCAG
    601 GCCCTGGAAG GGATATCCCC CGAGTTGGGT CCCACCTTGG
    ACACACTGCA
    651 GCTGGACGTC GCCGACTTTG CCACCACCAT CTGGCAGCAG
    ATGGAAGAAC
    701 TGGGAATGGC CCCTGCCCTG CAGCCCACCC AGGGTGCCAT
    GCCGGCCTTC
    751 GCCTCTGCTT TCCAGCGCCG GGCAGGAGGG GTCCTGGTTG
    CTAGCCATCT
    801 GCAGAGCTTC CTGGAGGTGT CGTACCGCGT TCTACGCCAC
    CTTGCGCAGC
    851 CCGGCGGCGG CTCTGACATG GCTACACCAT TAGGCCCTGC
    CAGCTCCCTG
    901 CCCCAGAGCT TCCTGCTCAA GTCTTTAGAG CAAGTGAGGA
    AGATCCAGGG
    951 CGATGGCGCA GCGCTCCAGG AGAAGCTGTG TGCCACCTAA
    TAA;
    pMON15982 (SEQ ID NO: 156)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT
    ACTATCAACC
    401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT
    GTCTCCCGAG
    451 TTGGGTCCCA CCTTGGACAC ACTGCAGCTG GACGTCGCCG
    ACTTTGCCAC
    501 CACCATCTGG CAGCAGATGG AAGAACTGGG AATGGCCCCT
    GCCCTGCAGC
    551 CCACCCAGGG TGCCATGCCG GCCTTCGCCT CTGCTTTCCA
    GCGCCGGGCA
    601 GGAGGGGTCC TGGTTGCTAC CCATCTGCAG AGCTTCCTGG
    AGGTGTCGTA
    651 CCGCGTTCTA CGCCACCTTG CGCAGCCCGG CGGCGGCTCT
    GACATGGCTA
    701 CACCATTAGG CCCTGCCAGC TCCCTGCCCC AGAGCTTCCT
    GCTCAAGTCT
    751 TTAGAGCAAG TGAGGAAGAT CCAGGGCGAT GGCGCAGCGC
    TCCAGGAGAA
    801 GCTGTGTGCC ACCTACAAGC TGTGCCACCC CGAGGAGCTG
    GTGCTGCTCG
    851 GACACTCTCT GGGCATCCCC TGGGCTCCCC TGAGCTCCTG
    CCCCAGCCAG
    901 GCCCTGCAGC TGGCAGGCTG CTTGAGCCAA CTCCATAGCG
    GCCTTTTCCT
    951 CTACCAGGGG CTCCTGCAGG CCCTGGAAGG GATATCCTAA
    TAA;
    pMON15965 (SEQ ID NO: 157)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCCAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA
    CAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT
    ACTATCAACC
    401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT
    GTCTTCTGCT
    451 TTCCAGCGCC GGGCAGGAGG GGTCCTGGTT GCTAGCCATC
    TGCAGAGCTT
    501 CCTGGAGGTG TCGTACCGCG TTCTACGCCA CCTTGCGCAG
    CCCGGCGGCG
    551 GCTCTGACAT GGCTACACCA TTAGGCCCTG CCAGCTCCCT
    GCCCCAGAGC
    601 TTCCTGCTCA AGTCTTTAGA GCAAGTGAGG AAGATCCAGG
    GCGATGGCGC
    651 AGCGCTCCAG GAGAAGCTGT GTGCCACCTA CAAGCTGTGC
    CACCCCGAGG
    701 AGCTGGTGCT GCTCGGACAC TCTCTGGGCA TCCCCTGGGC
    TCCCCTGAGC
    751 TCCTGCCCCA GCCAGGCCCT GCAGCTGGCA GGCTGCTTGA
    GCCAACTCCA
    801 TAGCGGCCTT TTCCTCTACC AGGGGCTCCT GCAGGCCCTG
    GAAGGGATAT
    851 CCCCCGAGTT GGGTCCCACC TTGGACACAC TGCAGCTGGA
    CGTCGCCGAC
    901 TTTGCCACCA CCATCTGGCA GCAGATGGAA GAACTGGGAA
    TGGCCCCTGC
    951 CCTGCAGCCC ACCCAGGGTG CCATGCCGGC CTTCGCCTAA
    TAA
    pMON15966 (SEQ ID NO: 158)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGC
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT
    ACTATCAACC
    401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT
    GTCTATGGCC
    451 CCTGCCCTGC AGCCCACCCA GGGTGCCATG CCGGCCTTCG
    CCTCTGCTTT
    501 CCAGCGCCGG GCAGGAGGGG TCCTGGTTGC TAGCCATCTG
    CAGAGCTTCC
    551 TGGAGGTGTC GTACCGCGTT CTACGCCACC TTGCGCAGCC
    CGGCGGCGGC
    601 TCTGACATGG CTACACCATT AGGCCCTGCC AGCTCCCTGC
    CCCAGAGCTT
    651 CCTGCTCAAG TCTTTAGAGC AAGTGAGGAA GATCCAGGGC
    GATGGCGCAG
    701 CGCTCCAGGA GAAGCTGTGT GCCACCTACA AGCTGTGCCA
    CCCCGAGGAG
    751 CTGGTGCTGC TCGGACACTC TCTGGGCATC CCCTGGGCTC
    CCCTGAGCTC
    801 CTGCCCCAGC CAGGCCCTGC AGCTGGCAGG CTGCTTGAGC
    CAACTCCATA
    851 GCGGCCTTTT CCTCTACCAG GGGCTCCTGC AGGCCCTGGA
    AGGGATATCC
    901 CCCGAGTTGG GTCCCACCTT GGACACACTG CAGCTGGACG
    TCGCCGACTT
    951 TGCCACCACC ATCTGGCAGC AGATGGAAGA ACTGGGATAA
    TAA
    pMON15967 (SEQ ID NO: 159)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTACA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT
    ACTATCAACC
    401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT
    GTCTACCCAG
    451 GGTGCCATGC CGGCCTTCGC CTCTGCTTTC CAGCGCCGGG
    CAGGAGGGGT
    501 CCTGGTTGCT AGCCATCTGC AGAGCTTCCT GGAGGTGTCG
    TACCGCGTTC
    551 TACGCCACCT TGCGCAGCCC GGCGGCGGCT CTGACATGGC
    TACACCATTA
    601 GGCCCTGCCA GCTCCCTGCC CCAGAGCTTC CTGCTCAAGT
    CTTTAGAGCA
    651 AGTGAGGAAG ATCCAGGGCG ATGGCGCAGC GCTCCAGGAG
    AAGCTGTGTG
    701 CCACCTACAA GCTGTGCCAC CCCGAGGAGC TGGTGCTGCT
    CGGACACTCT
    751 CTGGGCATCC CCTGGGCTCC CCTGAGCTCC TGCCCCAGCC
    AGGCCCTGCA
    801 GCTGGCAGGC TGCTTGAGCC AACTCCATAG CGGCCTTTTC
    CTCTACCAGG
    851 GGCTCCTGCA GGCCCTGGAA GGGATATCCC CCGAGTTGGG
    TCCCACCTTG
    901 GACACACTCC AGCTGGACGT CGCCGACTTT GCCACCACCA
    TCTGGCAGCA
    951 GATGGAAGAA CTGGGAATGG CCCCTGCCCT GCAGCCCTAA
    TAA
    pMON15960 (SEQ ID NO: 160)
      1 ATGGCTACAC CATTGGGCCC TGCCAGCTCC CTGCCCCAGA
    GCTTCCTGCT
     51 CAAGTCTTTA GAGCAAGTGA GGAAGATCCA GGGCGATGGC
    GCAGCGCTCC
    101 AGGAGAAGCT GTGTGCCACC TACAAGCTGT CCCACCCCGA
    GGAGCTGGTG
    151 CTGCTCGGAC ACTCTCTGGG CATCCCCTGG GCTCCCCTGA
    GCTCCTGCCC
    201 CAGCCAGGCC CTGCAGCTGG CAGGCTGCTT GAGCCAACTC
    CATAGCGGCC
    251 TTTTCCTCTA CCAGGGGCTC CTGCAGGCCC TGGAAGGGAT
    ATCCCCCGAG
    301 TTGGGTCCCA CCTTGGACAC ACTGCAGCTG GACGTCGCCG
    ACTTTGCCAC
    351 CACCATCTGG CAGCAGATGG AAGAACTGGG AATGGCCCCT
    GCCCTGCAGC
    401 CCACCCAGGG TGCCATGCCG GCCTTCGCCT CTGCTTTCCA
    GCGCCGGGCA
    451 GGAGGGGTCC TGGTTGCTAG CCATCTGCAG AGCTTCCTGG
    AGGTGTCGTA
    501 CCGCGTTCTA CGCCACCTTG CGCAGCCCGG CGGCGGCTCT
    GACATGGCTA
    551 CACCATTGGG CCCTGCCAGC TCCCTGCCCC AGAGCTTCCT
    GCTCAAGTCT
    601 TTAGAGCAAG TGAGGAAGAT CCAGGGCGAT GGCGCAGCGC
    TCCAGGAGAA
    651 GCTGTGTGCC ACCTACAAGC TGTGCCACCC CGAGGAGCTG
    GTGCTGCTCG
    701 GACACTCTCT GGGCATCCCC TGGGCTCCCC TGAGCTCCTG
    CCCCAGCCAG
    751 GCCCTGCAGC TGGCAGGCTG CTTGAGCCAA CTCCATAGCG
    GCCTTTTCCT
    801 CTACCAGGGG CTCCTGCAGG CCCTGGAAGG GATATCCCCC
    GAGTTGGGTC
    851 CCACCTTGGA CACACTCCAG CTGGACGTCG CCGACTTTGC
    CACCACCATC
    901 TGGCAGCAGA TGGAAGAACT GGGAATGGCC CCTGCCCTGC
    AGCCCACCCA
    100 TCCTGGTTGC TAGCCATCTG CAGAGCTTCC TGGAGGTGTC
    GTACCGCGTT
    105 CTACGCCACC TTGCGCAGCC CTGATAA
    PMON32132 (SEQ ID NO: 249)
    TCTCCCGCTCCGCCTGCTTGTGACCTCCGAGTCCTCAGTAAACTGCTTCG
    TGACTCCCATGTCCTTCACAGCAGACTGAGCCAGTGCCCAGAGGTTCACC
    CTTTGCCTACACCTGTCCTGCTGCCTGCTGTGGACTTTAGCTTGGGAGAA
    TGGAAAACCCAGATGGAGGAGACCAAGGCACAGGACATTCTGGGAGCAGT
    GACCCTTCTGCTGGAGGGAGTGATGGCAGCACGGGGACAACTGGGACCCA
    CTTGCCTCTCATCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCCTC
    CTTGGGGCCCTGCAGAGCCTCCTTGGAACCCAGCTTCCTCCACAGGGCAG
    GACCACAGCTCACAAGGATCCCAATGCCATCTTCCTGAGCTTCCAACACC
    TGCTCCGAGGAAAGGTGCGTTTCCTGATGCTTGTAGGAGGGTCCACCCTC
    TGCGTCAGG
    PMON32133 (SEQ ID NO: 250)
    TCTCCCGCTCCGCCTGCTTGTGACCTCCGAGTCCTCAGTAAACTGCTTCG
    TGACTCCCATGTCCTTCACAGCAGACTGAGCCAGTGCCCAGAGGTTCACC
    CTTTGCCTACACCTGTCCTGCTGCCTGCTGTGGACTTTAGCTTGGGAGAA
    TGGAAAACCCAGATGGAGGAGACCAAGGCACAGGACATTCTGGGAGCAGT
    GACCCTTCTGCTGGAGGGAGTGATGGCAGCACGGGGACAACTGGGACCCA
    CTTGCCTCTCATCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCCTC
    CTTGGGGCCCTGCAGAGCCTCCTTGGAACCCAGGGCAGGACCACAGCTCA
    CAAGGATCCCAATGCCATCTTCCTGAGCTTCCAACACCTGCTCCGAGGAA
    AGGTGCGTTTCCTGATGCTTGTAGGAGGGTCCACCCTCTGCGTCAGG
    pMON32134 (SEQ ID NO: 251)
    TCCCCAGCGCCGCCTGCTTGTCACCTCCGAGTCCTCAGTAAACTGCTTCG
    TGACTCCCATGTCCTTCACAGCAGACTGAGCCAGTGCCCAGAGGTTCACC
    CTTTGCCTACACCTGTCCTGCTGCCTGCTGTGGACTTTAGCTTGGGAGAA
    TGGAAAACCCAGATGGAGGAGACCAAGGCACAGGACATTCTGGGAGCAGT
    GACCCTTCTGCTGGAGGGAGTGATGGCAGCACGGGGACAACTGGGACCCA
    CTTGCCTCTCATCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCCTC
    CTTGGGGCCCTGCAGAGCCTCCTTGGAACCCACCTTCCTCCACAGGGCAG
    GACCACAGCTCACAAGGATCCCAATGCCATCTTCCTGAGCTTCCAACACC
    TGCTCCGAGGAAAGGTGCGTTTCCTGATGCTTGTAGGAGGGTCCACCCTC
    TGCGTCAGG
    Pmon13181 (SEQ ID NO: 257)
      1 CCATGGCTAA CTGCTCTATA ATGATCGATG AAATTATACA
    TCACTTAAAG
     51 AGACCACCTG CACCTTTGCT GGACCCGAAC AACCTCAATG
    ACGAAGACGT
    101 CTCTATCCTG ATGGATCGAA ACCTTCGACT TCCAAACCTG
    GAGAGCTTCG
    151 TAAGGGCTGT CAAGAACTTA GAAAATGCAT CAGGTATTGA
    GGCAATTCTT
    201 CGTAATCTCC AACCATGTCT GCCCTCTGCC ACGGCCGCAC
    CCTCTCGACA
    251 TCCAATCATC ATCAAGGCAG GTGACTGGCA AGAATTCCGG
    GAAAAACTGA
    301 CGTTCTATCT GGTTACCCTT GAGCAAGCGC AGGAACAACA
    GTACGTAgag
    351 ggcggtggag gctcCCCGGG TGAACCGTCT GGTCCAATCT
    CTACTATCAA
    401 CCCGTCTCCT CCGTCTAAAG AATCTCATAA ATCTCCAAAC
    ATGTAAGGTA
    451 CCGCATGCAA GCTT
    Pmon13180.Seg (SEQ ID NO: 258)
      1 CCATGGCTAA CTGCTCTATA ATGATCGATG AAATTATACA
    TCACTTAAAG
     51 AGACCACGTG CACCTTTGCT GGACCCGAAC AACCTCAATG
    ACGAAGACGT
    101 CTCTATCCTG ATGGATCGAA ACCTTCGACT TCCAAACCTG
    GAGAGCTTCG
    151 TAAGGGCTGT CAAGAACTTA GAAAATGCAT CAGGTATTGA
    GGCAATTCTT
    201 CGTAATCTCC AACCATGTCT GCCCTCTGCC ACGGCCGCAC
    CCTCTCGACA
    251 TCCAATCATC ATCAAGGCAG GTGACTGGCA AGAATTCCGG
    GAAAAACTGA
    301 CGTTCTATCT GGTTACCCTT GAGCAAGCGC AGGAACAACA
    GTACGTAgag
    351 ggcggtggag gctcCCCGCG TGGTGGTTCT GGCGGCGGCT
    CCAACATGTA
    401 AGGTACCGCA TGCAAGCTT
    pmon16017.seq (SEQ ID NO: 259)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 ACGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT
    ACTATCAACC
    401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT
    GGCTTTAGGC
    451 CCTGCCAGCT CCCTGCCCCA GAGCTTCCTG CTCAAGTCTT
    TAGAGCAAGT
    501 GAGGAAGATC CAGGGCGATG GCGCAGCGCT CCAGGAGAAG
    CTGTGTGCCA
    551 CCTACAAGCT GTGCCACCCC GAGGAGCTGG TGCTGCTCGG
    ACACTCTCTG
    601 GGCATCCCCT GGGCTCCCCT GAGCTCCTGC CCCAGCCAGG
    CCCTGCAGCT
    651 GGCAGGCTGC TTGAGCCAAC TCCATAGCGG CCTTTTCCTC
    TACCAGGGGC
    701 TCCTGCAGGC CCTGGAAGGG ATATCCCCCG AGTTGGGTCC
    CACCTTGGAC
    751 ACACTGCAGC TGGACGTCGC CGACTTTGCC ACCACCATCT
    GGCAGCAGAT
    801 GGAAGAACTG GGAATGGCCC CTGCCCTGCA GCCCACCCAG
    GGTGCCATGC
    851 CGGCCTTCGC CTCTGCTTTC CAGCGCCGGG CAGGAGGGGT
    CCTGGTTGCT
    901 AGCCATCTGC AGAGCTTCCT GGAGGTGTCG TACCGCGTTC
    TACGCCACCT
    951 TGCGCAGCCC GACATGGCTA CACCA
    pmon16018.seq (SEQ ID NO: 260)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT
    ACTATCAACC
    401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT
    GGCTCAGAGC
    451 TTCCTGCTCA AGTCTTTAGA GCAAGTGAGG AAGATCCAGG
    GCGATGGCGC
    501 AGCGCTCCAG GAGAAGCTGT GTGCCACCTA CAAGCTGTGC
    CACCCCGAGG
    551 AGCTGGTGCT GCTCGGACAC TCTCTGGGCA TCCCCTGGGC
    TCCCCTGAGC
    601 TCCTGCCCCA GCCAGGCCCT GCAGCTGGCA GGCTGCTTGA
    GCCAACTCCA
    651 TAGCGGCCTT TTCCTCTACC AGGGGCTCCT GCAGGCCCTG
    GAAGGGATAT
    701 CCCCCGAGTT GGGTCCCACC TTGGACACAC TGCAGCTGGA
    CGTCGCCGAC
    751 TTTGCCACCA CCATCTGGCA GCAGATGGAA GAACTGGGAA
    TGGCCCCTGC
    801 CCTGCAGCCC ACCCAGGGTG CCATGCCGGC CTTCGCCTCT
    GCTTTCCAGC
    851 GCCGGGCAGG AGGGGTCCTG GTTGCTAGCC ATCTGCAGAG
    CTTCCTGGAG
    901 GTGTCGTACC GCGTTCTACG CCACCTTGCG CAGCCCGACA
    TGGCTACACC
    951 ATTAGGCCCT GCCAGCTCCC TGCCC
    pmon16019.seq (SEQ ID NO: 261)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT
    ACTATCAACC
    401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT
    GGCTTTCCTG
    451 CTCAAGTCTT TAGAGCAAGT GAGGAAGATC CAGGGCGATG
    GCGCAGCGCT
    501 CCAGGAGAAG CTGTGTGCCA CCTACAAGCT GTGCCACCCC
    GAGGAGCTGG
    551 TGCTGCTCGG ACACTCTCTG GGCATCCCCT GGGCTCCCCT
    GAGCTCCTGC
    601 CCCAGCCACG CCCTGCAGCT GGCAGGCTGC TTGAGCCAAC
    TCCATAGCGG
    651 CCTTTTCCTC TACCAGGGGC TCCTGCAGGC CCTGGAAGGG
    ATATCCCCCG
    701 AGTTGGGTCC CACCTTGGAC ACACTGCAGC TGGACGTCGC
    CGACTTTGCC
    751 ACCACCATCT GGCAGCAGAT GGAAGAACTG GGAATGGCCC
    CTGCCCTGCA
    801 GCCCACCCAG GGTGCCATGC CGGCCTTCGC CTCTGCTTTC
    CAGCGCCGGG
    851 CAGGAGGGGT CCTGGTTGCT AGCCATCTGC AGAGCTTCCT
    GGAGGTGTCG
    901 TACCGCGTTC TACGCCACCT TGCGCAGCCC GACATGGCTA
    CACCATTAGG
    951 CCCTGCCAGC TCCCTGCCCC AGAGC
    pmon16020.seq (SEQ ID NO: 262)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT
    ACTATCAACC
    401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT
    GGCTGAGCAA
    451 GTGAGGAAGA TCCAGGGCGA TGGCGCAGCG CTCCAGGAGA
    AGCTGTGTGC
    501 CACCTACAAG CTGTGCCACC CCGAGGAGCT GGTGCTGCTC
    GGACACTCTC
    551 TGGGCATCCC CTGGGCTCCC CTGAGCTCCT GCCCCAGCCA
    GGCCCTGCAG
    601 CTGGCAGGCT GCTTGAGCCA ACTCCATAGC GGCCTTTTCC
    TCTACCAGGG
    651 GCTCCTGCAG GCCCTGGAAG GGATATCCCC CGAGTTGGGT
    CCCACCTTGG
    701 ACACACTGCA GCTGGACGTC GCCGACTTTG CCACCACCAT
    CTGGCAGCAG
    751 ATGGAAGAAC TGGGAATGGC CCCTGCCCTG CAGCCCACCC
    AGGGTGCCAT
    801 GCCGGCCTTC GCCTCTGCTT TCCAGCGCCG GGCAGGAGGG
    GTCCTGGTTG
    851 CTAGCCATCT GCAGAGCTTC CTGGAGGTGT CGTACCGCGT
    TCTACGCCAC
    901 CTTGCGCAGC CCGACATGGC TACACCATTA GGCCCTGCCA
    GCTCCCTGCC
    951 CCAGAGCTTC CTGCTCAAGT CTTTA
    pmon16021.seq (SEQ ID NO: 263)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT
    ACTATCAACC
    401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT
    GGCTCTGCTC
    451 GGACACTCTC TGGGCATCCC CTGGGCTCCC CTGAGCTCCT
    GCCCCAGCCA
    501 GGCCCTGCAG CTGGCAGGCT GCTTGAGCCA ACTCCATAGC
    GGCCTTTTCC
    551 TCTACCAGGG GCTCCTGCAG GCCCTGGAAG GGATATCCCC
    CGAGTTGGGT
    601 CCCACCTTGG ACACACTGCA GCTGGACGTC GCCGACTTTG
    CCACCACCAT
    651 CTGGCAGCAG ATGGAAGAAC TGGGAATGGC CCCTGCCCTG
    CAGCCCACCC
    701 AGGGTGCCAT GCCGGCCTTC GCCTCTGCTT TCCAGCGCCG
    GGCAGGAGGG
    751 GTCCTGGTTG CTAGCCATCT GCAGACCTTC CTGGAGGTGT
    CGTACCGCGT
    801 TCTACGCCAC CTTGCGCAGC CCGACATGGC TACACCATTA
    GGCCCTGCCA
    851 GCTCCCTGCC CCAGAGCTTC CTGCTCAAGT CTTTAGAGCA
    AGTGAGGAAG
    901 ATCCAGGGCG ATGGCGCAGC GCTCCAGGAG AAGCTGTGTG
    CCACCTACAA
    951 GCTGTGCCAC CCCGAGGAGC TGGTG
    pmon16022.seq (SEQ ID NO: 264)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGCCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT
    ACTATCAACC
    401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT
    GGCTCCCCTG
    451 AGCTCCTGCC CCAGCCAGGC CCTGCAGCTG GCAGGCTGCT
    TGAGCCAACT
    501 CCATAGCGGC CTTTTCCTCT ACCAGGGCCT CCTGCAGGCC
    CTGGAAGGGA
    551 TATCCCCCGA GTTGGGTCCC ACCTTGGACA CACTGCAGCT
    GGACGTCGCC
    601 GACTTTGCCA CCACCATCTG GCAGCAGATG GAAGAACTGG
    GAATGGCCCC
    651 TGCCCTGCAG CCCACCCAGG GTGCCATGCC GGCCTTCGCC
    TCTGCTTTCC
    701 AGCGCCGGGC AGGAGGGGTC CTGGTTGCTA GCCATCTGCA
    GAGCTTCCTG
    751 GAGGTGTCGT ACCGCGTTCT ACGCCACCTT GCGCAGCCCG
    ACATCGCTAC
    801 ACCATTAGGC CCTGCCAGCT CCCTGCCCCA GAGCTTCCTG
    CTCAAGTCTT
    851 TAGAGCAAGT GAGGAAGATC CAGGGCGATG GCGCAGCGCT
    CCAGGAGAAG
    901 CTGTGTGCCA CCTACAAGCT GTGCCACCCC GAGGAGCTGG
    TGCTGCTCGG
    951 ACACTCTCTG GGCATCCCCT GGGCT
    pmon16023.seq (SEQ ID NO: 265)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT
    ACTATCAACC
    401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT
    GGCTCAGGCC
    451 CTGCAGCTGG CAGGCTGCTT GAGCCAACTC CATAGCGGCC
    TTTTCCTCTA
    501 CCAGGGGCTC CTGCAGGCCC TGGAAGGGAT ATCCCCCGAG
    TTGGGTCCCA
    551 CCTTGGACAC ACTGCAGCTG GACGTCGCCG ACTTTGCCAC
    CACCATCTGG
    601 CAGCAGATGG AAGAACTGGG AATGGCCCCT GCCCTGCAGC
    CCACCCAGGG
    651 TGCCATGCCG GCCTTCGCCT CTGCTTTCCA GCGCCGGGCA
    GGAGGGGTCC
    701 TGGTTGCTAG CCATCTGCAG AGCTTCCTGG AGGTGTCGTA
    CCGCGTTCTA
    751 CGCCACCTTG CGCAGCCCGA CATGGCTACA CCATTAGGCC
    CTGCCAGCTC
    801 CCTGCCCCAG AGCTTCCTGC TCAAGTCTTT AGAGCAAGTG
    AGGAAGATCC
    851 AGGGCGATGG CGCACCGCTC CAGGAGAAGC TGTGTGCCAC
    CTACAAGCTG
    901 TGCCACCCCG AGGAGCTGGT GCTGCTCGGA CACTCTCTGG
    GCATCCCCTG
    951 GGCTCCCCTG AGCTCCTGCC CCAGC
    pmon16024.seq (SEQ ID NO: 266)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT
    ACTATCAACC
    401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT
    GGCTCTGCAG
    451 CTGGCAGGCT GCTTGAGCCA ACTCCATAGC GGCCTTTTCC
    TCTACCAGGG
    501 GCTCCTGCAG GCCCTGGAAG GGATATCCCC CGAGTTGGGT
    CCCACCTTGG
    551 ACACACTGCA GCTGGACGTC GCCGACTTTG CCACCACCAT
    CTGGCAGCAG
    601 ATGGAAGAAC TGGCAATGGC CCCTGCCCTG CAGCCCACCC
    AGGGTGCCAT
    651 GCCGGCCTTC GCCTCTGCTT TCCAGCGCCG GGCAGGAGGG
    GTCCTGGTTG
    701 CTAGCCATCT GCAGAGCTTC CTGGAGGTGT CGTACCGCGT
    TCTACGCCAC
    751 CTTGCGCAGC CCGACATGGC TACACCATTA GGCCCTGCCA
    GCTCCCTGCC
    801 CCAGAGCTTC CTGCTCAAGT CTTTAGAGCA AGTGAGGAAG
    ATCCAGGGCG
    851 ATGGCGCAGC GCTCCAGGAG AAGCTGTGTG CCACCTACAA
    GCTGTGCCAC
    901 CCCGAGGAGC TGGTGCTGCT CGGACACTCT CTGGGCATCC
    CCTGGGCTCC
    951 CCTGAGCTCC TGCCCCAGCC AGGCC
    pmon16125.seq (SEQ ID NO: 267)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT
    ACTATCAACC
    401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT
    GGCTCTGGCA
    451 GGCTGCTTGA GCCAACTCCA TAGCGGCCTT TTCCTCTACC
    AGGGGCTCCT
    501 GCAGGCCCTG GAAGGGATAT CCCCCGAGTT GGGTCCCACC
    TTGGACACAC
    551 TGCAGCTGGA CGTCGCCGAC TTTGCCACCA CCATCTGGCA
    GCAGATGGAA
    601 GAACTGGGAA TGGCCCCTGC CCTGCAGCCC ACCCAGGGTG
    CCATGCCGGC
    651 CTTCGCCTCT GCTTTCCAGC GCCGGGCAGG AGGGGTCCTG
    GTTGCTAGCC
    701 ATCTGCAGAG CTTCCTGGAG GTGTCGTACC GCGTTCTACG
    CCACCTTGCG
    751 CAGCCCGACA TGGCTACACC ATTAGGCCCT GCCAGCTCCC
    TGCCCCAGAG
    801 CTTCCTGCTC AAGTCTTTAG AGCAAGTGAG GAAGATCCAG
    GGCGATGGCG
    851 CAGCGCTCCA GGAGAAGCTG TGTGCCACCT ACAAGCTGTG
    CCACCCCGAG
    901 GAGCTGGTGC TGCTCGGACA CTCTCTGGGC ATCCCCTGGG
    CTCCCCTGAG
    951 CTCCTGCCCC AGCCAGGCCC TGCAG
    pmon16026.seq (SEQ ID NO: 268)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT
    ACTATCAACC
    401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT
    GGCTGAACTG
    451 GGAATGGCCC CTGCCCTGCA GCCCACCCAG GGTGCCATGC
    CGGCCTTCGC
    501 CTCTGCTTTC CAGCGCCGGG CAGGAGGGGT CCTGGTTGCT
    AGCCATCTGC
    551 AGAGCTTCCT GGAGGTGTCG TACCGCGTTC TACGCCACCT
    TGCGCAGCCC
    601 GACATGGCTA CACCATTAGG CCCTGCCAGC TCCCTGCCCC
    AGAGCTTCCT
    651 GCTCAAGTCT TTAGAGCAAG TGAGGAAGAT CCAGGGCGAT
    GGCGCAGCGC
    701 TCCAGGAGAA GCTGTGTGCC ACCTACAAGC TGTGCCACCC
    CGAGGAGCTG
    751 GTGCTGCTCG GACACTCTCT GGGCATCCCC TGGGCTCCCC
    TGAGCTCCTG
    801 CCCCAGCCAG GCCCTGCAGC TGGCAGGCTG CTTGAGCCAA
    CTCCATAGCG
    851 GCCTTTTCCT CTACCAGGGG CTCCTGCAGG CCCTGGAAGG
    GATATCCCCC
    901 GAGTTGGGTC CCACCTTGGA CACACTGCAG CTGGACGTCG
    CCGACTTTGC
    951 CACCACCATC TGGCAGCAGA TGGAA
    pmon16027.seq (SEQ ID NO: 269)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT
    ACTATCAACC
    401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT
    GGCTGGAATG
    451 GCCCCTGCCC TGCAGCCCAC CCAGGGTGCC ATGCCGGCCT
    TCGCCTCTGC
    501 TTTCCAGCGC CGGGCAGGAG GGGTCCTGGT TGCTAGCCAT
    CTGCAGAGCT
    551 TCCTGGAGGT GTCGTACCGC GTTCTACGCC ACCTTGCGCA
    GCCCGACATG
    601 GCTACACCAT TAGGCCCTGC CAGCTCCCTG CCCCAGAGCT
    TCCTGCTCAA
    651 GTCTTTAGAG CAAGTGAGGA AGATCCAGGG CGATGGCGCA
    GCGCTCCAGG
    701 AGAAGCTGTG TGCCACCTAC AAGCTGTGCC ACCCCGAGGA
    GCTGGTGCTG
    751 CTCGGACACT CTCTGGGCAT CCCCTGGGCT CCCCTGAGCT
    CCTGCCCCAG
    801 CCAGGCCCTG CAGCTGGCAG GCTGCTTGAG CCAACTCCAT
    AGCGGCCTTT
    851 TCCTCTACCA GGGGCTCCTG CAGGCCCTGG AAGGGATATC
    CCCCGAGTTG
    901 GGTCCCACCT TGGACACACT GCAGCTGGAC GTCGCCGACT
    TTGCCACCAC
    951 CATCTGGCAG CAGATGGAAG AACTG
    pmon16028.seq (SEQ ID NO: 270)
      1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC
    ACTTAAAGAG
     51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC
    GAAGACGTCT
    101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA
    GAGCTTCGTA
    151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG
    CAATTCTTCG
    201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC
    TCTCGACATC
    251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA
    AAAACTGACG
    301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT
    ACGTAGAGGG
    351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT
    ACTATCAACC
    401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT
    GGCTAGCTTC
    451 CTGGAGGTGT CGTACCGCGT TCTACGCCAC CTTGCGCAGC
    CCGACATGGC
    501 TACACCATTA GGCCCTGCCA GCTCCCTGCC CCAGAGCTTC
    CTGCTCAAGT
    551 CTTTAGAGCA AGTGAGGAAG ATCCAGGGCG ATGGCGCAGC
    GCTCCAGGAG
    601 AAGCTGTGTG CCACCTACAA GCTGTGCCAC CCCGAGGAGC
    TGGTGCTGCT
    651 CGGACACTCT CTGGGCATCC CCTGGGCTCC CCTGAGCTCC
    TGCCCCAGCC
    701 AGGCCCTGCA GCTGGCAGGC TGCTTGAGCC AACTCCATAG
    CGGCCTTTTC
    751 CTCTACCAGG GGCTCCTGCA GGCCCTGGAA GGGATATCCC
    CCGAGTTGGG
    801 TCCCACCTTG GACACACTGC AGCTGGACGT CGCCGACTTT
    GCCACCACCA
    851 TCTGGCAGCA GATGGAAGAA CTGGGAATGG CCCCTGCCCT
    GCAGCCCACC
    901 CAGGGTGCCA TGCCGGCCTT CGCCTCTGCT TTCCAGCGCC
    GGGCAGGAGG
    951 GGTCCTGGTT GCTAGCCATC TGCAG
    (SEQ ID NO: 286)
      1 ATGGCTGGAC CCACTTGCCT CTCATCCCTC CTGGGGCAGC
    TTTCTGGACA
     51 GGTCCGTCTC CTCCTTGGGG CCCTGCAGAG CCTCCTTGGA
    ACCCAGCTTC
    101 CTCCACAGGG CAGGACCACA GCTCACAAGG ATCCCAATGC
    CATCTTCCTG
    151 AGCTTCCAAC ACCTGCTCCG AGGAAAGGTG CGTTTCCTGA
    TGCTTGTAGG
    201 AGGGTCCACC CTCGCCGTCA GGGAATTCGG CGGCAACATG
    GCGTCTCCGG
    251 CGCCGCCTGC TGCTGACCTC CGAGTCCTCA GTAAACTGCT
    TCGTGACTCC
    301 CATGTCCTTC ACACCAGACT GAGCCAGTGC CCAGAGGTTC
    ACCCTTTGCC
    351 TACACCTGTC CTGCTGCCTG CTGTGGACTT TAGCTTGGGA
    GAATGGAAAA
    401 CCCAGATGGA GGAGACCAAG GCACAGGACA TTCTGGGAGC
    AGTGACCCTT
    451 CTGCTGGAGG GAGTGATGGC AGCACGGGGA CAACTG
    (SEQ ID NO: 287)
      1 ATGGCTGGCA GGACCACAGC TCACAAGGAT CCCAATGCCA
    TCTTCCTGAG
     51 CTTCCAACAC CTGCTCCGAG GAAAGGTGCG TTTCCTGATG
    CTTGTAGGAG
    101 GGTCCACCCT CGCCGTCAGG GAATTCGGCG GCAACATGGC
    GTCTCCGGCG
    151 CCGCCTGCTG CTGACCTCCG AGTCCTCAGT AAACTGCTTC
    GTGACTCCCA
    201 TGTCCTTCAC AGCAGACTGA GCCAGTGCCC AGAGGTTCAC
    CCTTTGCCTA
    251 CACCTGTCCT GCTGCCTGCT GTGGACTTTA GCTTGGGAGA
    ATGGAAAACC
    301 CAGATGGAGG AGACCAAGGC ACAGGACATT CTGGGAGCAG
    TGACCCTTCT
    351 GCTGGAGGGA GTGATGGCAG CACGGGGACA ACTGGGACCC
    ACTTGCCTCT
    401 CATCCCTCCT GGGGCAGCTT TCTGGACAGG TCCGTCTCCT
    CCTTGGGGCC
    451 CTGCAGAGCC TCCTTGGAAC CCAGCTTCCT CCACAG
  • [0465]
    TABLE 3
    PROTEIN SEQUENCES
    pMON26458pep
    SerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeuArgAspSerHis (SEQ ID NO:161)
    ValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuProThrProValLeu
    LeuProAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGluGluThrLysAla
    GlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAlaAlaArgGlyGln
    LeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGlnValArgLeuLeu
    LeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeuProProGlnGlyArgThrThrAla
    HisLysAspProAsnAlaIlePheLeuSerPheGlnHisLeuLeuArgGlyLysValArg
    PheLeuMetLeuValGlyGlySerThrLeuCysValArgGluPhe
    pMON28548pep
    SerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeuArgAspSerHis (SEQ ID NO:162)
    ValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuProThrProValLeu
    LeuProAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGluGluThrLysAla
    GlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAlaAlaArgGlyGln
    LeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGlnValArgLeuLeu
    LeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeuProProGlnGlyArgThrThrAla
    HisLysAspProAsnAlaIlePheLeuSerPheGlnHisLeuLeuArgGlyLysValArg
    PheLeuMetLeuValGlyGlySerThrLeuCysValArgGluPheGlyGlyAsnMetAla
    SerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeuArgAspSerHis
    ValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuProThrProValLeu
    LeuProAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGluGluThrLysAla
    GlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAlaAlaArgGlyGln
    LeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGlnValArgLeuLeu
    LeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnGlyArgThrThrAlaRisLysAspPro
    AsnAlaIlePheLeuSerPheGlnHisLeuLeuArgGlyLysValArgPheLeuMetLeu
    ValGlyGlySerThrLeuCysValArg
    pMON28500
    SerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeuArgAspSerHisValLeu (SEQ ID NO:163)
    HisSerArgLeuSerGlnCysProGluValHisProLeuProThrProValLeuLeuProAlaVal
    AspPheSerLeuGlyGluTrpLysThrGlnMetGluGluThrLysAlaGlnAspIleLeuGlyAla
    ValThrLeuLeuLeuGluGlyValMetAlaAlaArgGlyGlnLeuGlyProThrCysLeuSerSer
    LeuLeuGlyGlnLeuSerGlyGlnValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThr
    GlnLeuProProGlnGlyArgThrThrAlaHisLysAspProAsnAlaIlePheLeuSerPheGln
    HisLeuLeuArgGlyLysValArgPheLeuMetLeuValGlyGlySerThrLeuCysValArgGlu
    PheGlyAsnMetAlaSerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeuArg
    AspSerHisValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuProThrProVal
    LeuLeuProAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGluGluThrLysAlaGln
    AspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAlaAlaArgGlyGlnLeuGlyPro
    ThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGlnValArgLeuLeuLeuGlyAlaLeuGln
    SerLeuLeuGlyThrGlnLeuProProGlnGlyArgThrThrAlaHisLysAspProAsnAlaIle
    PheLeuSerPheGlnHisLeuLeuArgGlyLysValArgPheLeuMetLeuValGlyGlySerThr
    LeuCysValArg
    pMON28501
    SerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeuArgAspSerHis (SEQ ID NO:164)
    ValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuProThrProValLeu
    LeuProAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGluGluThrLysAla
    GlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAlaAlaArgGlyGln
    LeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGlnValArgLeuLeu
    LeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeuProProGlnGlyArgThrThrAla
    HisLysAspProAsnAlaIlePheLeuSerPheGlnHisLeuLeuArgGlyLysValArg
    PheLeuMetLeuValGlyGlySerThrLeuCysValArgGluPheGlyGlyAsnMetAla
    SerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeuArgAspSerHis
    ValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuProThrProValLeu
    LeuProAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGluGluThrLysAla
    GlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAlaAlaArgGlyGln
    LeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGlnValArgLeuLeu
    LeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeuProProGlnGlyArgThrThrAla
    HisLysAspProAsnAlallePheLeuSerPheGlnHisLeuLeuArgGlyLysValArg
    PheLeuMetLeuValGlyGlySerThrLeuCysValArg
    pMON28502
    SerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeuArgAspSerHis (SEQ ID NO:165)
    ValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuProThrProValLeu
    LeuProAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGluGluThrLysAla
    GlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAlaAlaArgGlyGln
    LeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGlnValArgLeuLeu
    LeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeuProProGlnGlyArgThrThrAla
    HisLysAspProAsnAlaIlePheLeuSerPheGlnHisLeuLeuArgGlyLysValArg
    PheLeuMetLeuValGlyGlySerThrLeuCysValArgGluPheGlyGlyAsnGlyGly
    AsnMetAlaSerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeuArg
    AspSerHisValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuProThr
    ProValLeuLeuProAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGluGlu
    ThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAlaAla
    ArgGlyGlnLeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGlnVal
    ArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeuProProGlnGlyArg
    ThrThrAlaHisLysAspProAsnAlallePheLeuSerPheGlnHisLeuLeuArgGly
    LysValArgPheLeuMetLeuValGlyGlySerThrLeuCysValArg
    13182.Pept
    Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:166)
    Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp
    Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu
    Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile
    Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr
    Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp
    Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu
    Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro
    Gly Gly Gly Ser Gly Gly Gly Ser Asn Met Ala Tyr Lys Leu Cys
    His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro
    Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala
    Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly
    Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr
    Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile
    Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro
    Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg
    Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu
    Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Ser Gly Gly
    Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val
    Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys
    Ala Thr
    13183.Pept
    Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:167)
    Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp
    Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu
    Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile
    Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr
    Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp
    Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu
    Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro
    Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro
    Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Tyr Lys Leu Cys
    His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro
    Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala
    Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly
    Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr
    Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile
    Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro
    Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg
    Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu
    Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Ser Gly Gly
    Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val
    Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys
    Ala Thr
    13184.Pept
    Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:168)
    Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp
    Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu
    Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile
    Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr
    Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp
    Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu
    Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro
    Gly Gly Gly Ser Gly Gly Gly Ser Asn Met Ala Pro Glu Leu Gly
    Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr
    Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu
    Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln
    Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe
    Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Ser
    Gly Gly Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Glu
    Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys
    Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu
    Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys
    Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His
    Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly
    Ile Ser
    13185.Pept
    Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:169)
    Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp
    Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu
    Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile
    Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr
    Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp
    Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu
    Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro
    Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro
    Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Pro Glu Leu Gly
    Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr
    Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu
    Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln
    Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe
    Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Ser
    Gly Gly Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Glu
    Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys
    Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu
    Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys
    Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His
    Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly
    Ile Ser
    13186.Pept
    Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:170)
    Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp
    Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu
    Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile
    Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr
    Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp
    Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu
    Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro
    Gly Gly Gly Ser Gly Gly Gly Ser Asn Met Ala Met Ala Pro Ala
    Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe
    Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser
    Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro
    Ser Gly Gly Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu
    Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu
    Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val
    Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser
    Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu
    His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu
    Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu
    Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu
    Leu Gly
    13187.Pept
    Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:171)
    Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp
    Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu
    Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile
    Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr
    Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp
    Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu
    Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro
    Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro
    Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Met Ala Pro Ala
    Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe
    Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser
    Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro
    Ser Gly Gly Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu
    Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu
    Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val
    Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser
    Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu
    His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu
    Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu
    Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu
    Leu Gly
    13188.Pept
    Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:172)
    Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp
    Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu
    Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile
    Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr
    Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp
    Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu
    Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro
    Gly Gly Gly Ser Gly Gly Gly Ser Asn Met Ala Thr Gln Gly Ala
    Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val
    Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg
    Val Leu Arg His Leu Ala Gln Pro Ser Gly Gly Ser Gly Gly Ser
    Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln
    Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys
    Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly
    Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln
    Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr
    Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly
    Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr
    Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu
    Gln Pro
    13189.Pept
    Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:173)
    Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp
    Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu
    Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile
    Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr
    Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp
    Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu
    Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro
    Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro
    Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Thr Gln Gly Ala
    Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val
    Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg
    Val Leu Arg His Leu Ala Gln Pro Ser Gly Gly Ser Gly Gly Ser
    Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln
    Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys
    Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly
    Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln
    Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr
    Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly
    Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr
    Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu
    Gln Pro
    13190.Pept
    Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:174)
    Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp
    Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu
    Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile
    Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr
    Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp
    Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu
    Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro
    Gly Gly Gly Ser Gly Gly Gly Ser Asn Met Ala Ser Ala Phe Gln
    Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe
    Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Ser
    Gly Gly Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Glu
    Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys
    Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu
    Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys
    Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His
    Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly
    Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp
    Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu
    Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala
    Phe Ala
    13191.Pept
    Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:175)
    Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp
    Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu
    Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile
    Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr
    Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp
    Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu
    Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro
    Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro
    Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Ser Ala Phe Gln
    Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe
    Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Ser
    Gly Gly Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Glu
    Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys
    Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu
    Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys
    Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His
    Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly
    Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp
    Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu
    Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala
    Phe Ala
    13192.Pept
    Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:176)
    Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp
    Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu
    Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile
    Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr
    Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp
    Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu
    Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro
    Gly Gly Gly Ser Gly Gly Gly Ser Asn Met Ala Tyr Lys Leu Cys
    His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro
    Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala
    Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly
    Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr
    Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile
    Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro
    Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg
    Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu
    Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Thr Pro Leu
    Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu
    Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu
    Lys Leu Cys Ala Thr
    13193.Pept
    Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:177)
    Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp
    Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu
    Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile
    Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr
    Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp
    Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu
    Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro
    Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro
    Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Tyr Lys Leu Cys
    His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro
    Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala
    Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly
    Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr
    Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile
    Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro
    Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg
    Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu
    Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Thr Pro Leu
    Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu
    Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu
    Lys Leu Cys Ala Thr
    25190.Pept
    Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:178)
    Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp
    Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu
    Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile
    Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr
    Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp
    Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu
    Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro
    Gly Gly Gly Ser Gly Gly Gly Ser Asn Met Ala Pro Glu Leu Gly
    Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr
    Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu
    Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln
    Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe
    Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Thr
    Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys
    Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu
    Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu
    Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu
    Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser
    Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala
    Leu Glu Gly Ile Ser
    pMON25191.Pep
    Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:179)
    Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp
    Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu
    Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile
    Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr
    Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp
    Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu
    Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro
    Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro
    Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Pro Glu Leu Gly
    Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr
    Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu
    Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln
    Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe
    Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Thr
    Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys
    Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu
    Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu
    Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu
    Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser
    Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala
    Leu Glu Gly Ile Ser
    13194.Pept
    Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:180)
    Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp
    Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu
    Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile
    Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr
    Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp
    Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu
    Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro
    Gly Gly Gly Ser Gly Gly Gly Ser Asn Met Ala Met Ala Pro Ala
    Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe
    Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser
    Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro
    Thr Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu
    Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala
    Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu
    Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro
    Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu
    Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln
    Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr
    Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln
    Met Glu Glu Leu Gly
    13195.Pept
    Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:181)
    Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp
    Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu
    Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile
    Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr
    Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp
    Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu
    Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro
    Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro
    Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Met Ala Pro Ala
    Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe
    Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser
    Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro
    Thr Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu
    Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala
    Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu
    Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro
    Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu
    Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln
    Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr
    Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln
    Met Glu Glu Leu Gly
    13196.Pept
    Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:182)
    Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp
    Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu
    Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile
    Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr
    Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp
    Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu
    Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro
    Gly Gly Gly Ser Gly Gly Gly Ser Asn Met Ala Thr Gln Gly Ala
    Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val
    Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg
    Val Leu Arg His Leu Ala Gln Pro Thr Pro Leu Gly Pro Ala Ser
    Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg
    Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala
    Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His
    Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln
    Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu
    Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro
    Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp
    Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala
    Pro Ala Leu Gln Pro
    13197.Pept
    Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:183)
    Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp
    Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu
    Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile
    Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr
    Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp
    Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu
    Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro
    Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro
    Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Thr Gln Gly Ala
    Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val
    Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg
    Val Leu Arg His Leu Ala Gln Pro Thr Pro Leu Gly Pro Ala Ser
    Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg
    Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala
    Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His
    Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln
    Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu
    Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro
    Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp
    Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala
    Pro Ala Leu Gln Pro
    13198.Pept
    Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:184)
    Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp
    Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu
    Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile
    Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr
    Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp
    Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu
    Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro
    Gly Gly Gly Ser Gly Gly Gly Ser Asn Met Ala Ser Ala Phe Gln
    Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe
    Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Thr
    Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys
    Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu
    Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu
    Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu
    Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser
    Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala
    Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu
    Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met
    Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala
    Met Pro Ala Phe Ala
    13199.Pept
    Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:185)
    Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp
    Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu
    Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile
    Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr
    Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp
    Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu
    Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro
    Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro
    Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Ser Ala Phe Gln
    Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe
    Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Thr
    Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys
    Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu
    Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu
    Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu
    Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser
    Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala
    Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu
    Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met
    Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala
    Met Pro Ala Phe Ala
    31104.Pep
    Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met (SEQ ID NO:186)
    Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala
    Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg
    Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg
    His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu
    Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln
    Gln Gly Gly Gly Ser Asn Cys Ser Ile Met Ile Asp Glu Ile Ile
    His His Leu Lys Arg Pro Pro Ala Pro Leu Tyr Val Glu Gly Gly
    Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn
    Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala
    Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg
    Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu
    Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Ser Gly Gly
    Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val
    Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys
    Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly
    His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser
    Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly
    Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser
    Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala
    Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met
    Ala Pro Ala Leu Gln Pro
    31105.Pep
    Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys (SEQ ID NO:187)
    Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile
    Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr
    Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Gly Gly Gly Ser
    Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg
    Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp
    Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu
    Ser Phe Val Arg Ala Val Lys Asn Leu Glu Tyr Val Glu Gly Gly
    Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn
    Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala
    Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg
    Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu
    Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Ser Gly Gly
    Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val
    Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys
    Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly
    His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser
    Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly
    Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser
    Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala
    Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met
    Ala Pro Ala Leu Gln Pro
    31106.Pep
    Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln (SEQ ID NO:188)
    Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln
    Ala Gln Glu Gln Gln Gly Gly Gly Ser Asn Cys Ser Ile Met Ile
    Asp Glu Ile Ile His His Leu Lys Arg Pro Pro Ala Pro Leu Leu
    Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met Asp
    Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val
    Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn
    Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Tyr Val Glu Gly Gly
    Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn
    Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala
    Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg
    Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu
    Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Ser Gly Gly
    Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val
    Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys
    Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly
    His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser
    Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly
    Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser
    Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala
    Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met
    Ala Pro Ala Leu Gln Pro
    31107.Pep
    Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu (SEQ ID NO:189)
    Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Gly Gly Gly Ser Asn
    Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg Pro
    Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val
    Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser
    Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu
    Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala
    Ala Pro Ser Arg His Pro Ile Ile Ile Lys Tyr Val Glu Gly Gly
    Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn
    Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala
    Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg
    Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu
    Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Ser Gly Gly
    Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val
    Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys
    Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly
    His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser
    Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly
    Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser
    Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala
    Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met
    Ala Pro Ala Leu Gln Pro
    31108.Pep
    Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met (SEQ ID NO:190)
    Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala
    Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg
    Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg
    His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu
    Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln
    Gln Gly Gly Gly Ser Gly Gly Gly Ser Gly Gly Gly Ser Asn Cys
    Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg Pro Pro
    Ala Pro Leu Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro
    Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu
    Ser His Lys Ser Pro Asn Met Ala Thr Gln Gly Ala Met Pro Ala
    Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala
    Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg
    His Leu Ala Gln Pro Ser Gly Gly Ser Gly Gly Ser Gln Ser Phe
    Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly
    Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His
    Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp
    Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly
    Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu
    Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu
    Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp
    Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro
    31109.Pep
    Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys (SEQ ID NO:191)
    Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile
    Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr
    Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Gly Gly Gly Ser
    Gly Gly Gly Ser Gly Gly Gly Ser Asn Cys Ser Ile Met Ile Asp
    Glu Ile Ile His His Leu Lys Arg Pro Pro Ala Pro Leu Leu Asp
    Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met Asp Arg
    Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys
    Asn Leu Glu Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro
    Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu
    Ser His Lys Ser Pro Asn Met Ala Thr Gln Gly Ala Met Pro Ala
    Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala
    Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg
    His Leu Ala Gln Pro Ser Gly Gly Ser Gly Gly Ser Gln Ser Phe
    Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly
    Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His
    Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp
    Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly
    Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu
    Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu
    Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp
    Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro
    31110.Pep
    Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln (SEQ ID NO:192)
    Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln
    Ala Gln Glu Gln Gln Gly Gly Gly Ser Gly Gly Gly Ser Gly Gly
    Gly Ser Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu
    Lys Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp
    Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn
    Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser
    Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser
    Ala Thr Ala Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro
    Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu
    Ser His Lys Ser Pro Asn Met Ala Thr Gln Gly Ala Met Pro Ala
    Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala
    Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg
    His Leu Ala Gln Pro Ser Gly Gly Ser Gly Gly Ser Gln Ser Phe
    Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly
    Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His
    Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp
    Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly
    Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu
    Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu
    Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp
    Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro
    31111.Pep
    Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu (SEQ ID NO:193)
    Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Gly Gly Gly Ser Gly
    Gly Gly Ser Gly Gly Gly Ser Asn Cys Ser Ile Met Ile Asp Glu
    Ile Ile His His Leu Lys Arg Pro Pro Ala Pro Leu Leu Asp Pro
    Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met Asp Arg Asn
    Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn
    Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln
    Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile
    Ile Ile Lys Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro
    Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu
    Ser His Lys Ser Pro Asn Met Ala Thr Gln Gly Ala Met Pro Ala
    Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala
    Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg
    His Leu Ala Gln Pro Ser Gly Gly Ser Gly Gly Ser Gln Ser Phe
    Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly
    Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His
    Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp
    Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly
    Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu
    Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu
    Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp
    Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro
    pMON15981
    1 MetAlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAla (SEQ ID NO:194)
    ProLeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsn
    LeuArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSer
    GlyIleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaPro
    SerArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThr
    PheTyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGly
    SerProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGlu
    SerHisLysSerProAsnMetAlaTyrLysLeuCysHisProGluGluLeuValLeuLeu
    GlyHisSerLeuGlyIleProTrpAlaProLeuSerSerCysProSerGlnAlaLeuGln
    LeuAlaGlyCysLeuSerGlnLeuHisSerGlyLeuPheLeuTyrGlnGlyLeuLeuGln
    AlaLeuGluGlyIleSerProGluLeuGlyProThrLeuAspThrLeuGlnLeuAspVal
    AlaAspPheAlaThrThrIleTrpGlnGlnMetGluGluLeuGlyMetAlaProAlaLeu
    GlnProThrGlnGlyAlaMetProAlaPheAlaSerAlaPheGlnArgArgAlaGlyGly
    ValLeuValAlaSerHisLeuGlnSerPheLeuGluValSerTyrArgValLeuArgHis
    LeuAlaGlnProGlyGlyGlySerAspMetAlaThrProLeuGlyProAlaSerSerLeu
    ProGlnSerPheLeuLeuLysSerLeuGluGlnValArgLysIleGlnGlyAspGlyAla
    AlaLeuGlnGluLysLeuCysAlaThr
    pMON15982
    MetAlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAla (SEQ ID NO:195)
    ProLeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsn
    LeuArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSer
    GlyIleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaPro
    SerArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThr
    PheTyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGly
    SerProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGlu
    SerHisLysSerProAsnMetAlaProGluLeuGlyProThrLeuAspThrLeuGlnLeu
    AspValAlaAspPheAlaThrThrIleTrpGlnGlnMetGluGluLeuGlyMetAlaPro
    AlaLeuGlnProThrGlnGlyAlaMetProAlaPheAlaSerAlaPheGlnArgArgAla
    GlyGlyValLeuValAlaSerHisLeuGlnSerPheLeuGluValSerTyrArgValLeu
    ArgHisLeuAlaGlnProGlyGlyGlySerAspMetAlaThrProLeuGlyProAlaSer
    SerLeuProGlnSerPheLeuLeuLysSerLeuGluGlnValArgLysIleGlnGlyAsp
    GlyAlaAlaLeuGlnGluLysLeuCysAlaThrTyrLysLeuCysHisProGluGluLeu
    ValLeuLeuGlyHisSerLeuGlyIleProTrpAlaProLeuSerSerCysProSerGln
    AlaLeuGlnLeuAlaGlyCysLeuSerGlnLeuHisSerGlyLeuPheLeuTyrGlnGly
    LeuLeuGlnAlaLeuGluGlyIleSer
    pMON15965
    MetAlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAla (SEQ ID NO:196)
    ProLeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsn
    LeuArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSer
    GlyIleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaPro
    SerArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThr
    PheTyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGly
    SerProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGlu
    SerHisLysSerProAsnMetAlaSerAlaPheGlnArgArgAlaGlyGlyValLeuVal
    AlaSerHisLeuGlnSerPheLeuGluValSerTyrArgValLeuArgHisLeuAlaGln
    ProGlyGlyGlySerAspMetAlaThrProLeuGlyProAlaSerSerLeuProGlnSer
    PheLeuLeuLysSerLeuGluGlnValArgLysIleGlnGlyAspGlyAlaAlaLeuGln
    GluLysLeuCysAlaThrTyrLysLeuCysHisProGluGluLeuValLeuLeuGlyHis
    SerLeuGlyIleProTrpAlaProLeuSerSerCysProSerGlnAlaLeuGlnLeuAla
    GlyCysLeuSerGlnLeuHisSerGlyLeuPheLeuTyrGlnGlyLeuLeuGlnAlaLeu
    GluGlyIleSerProGluLeuGlyProThrLeuAspThrLeuGlnLeuAspValAlaAsp
    PheAlaThrThrIleTrpGlnGlnMetGluGluLeuGlyMetAlaProAlaLeuGlnPro
    ThrGlnGlyAlaMetProAlaPheAla
    pMON15966
    MetAlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAla (SEQ ID NO:197)
    ProLeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsn
    LeuArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSer
    GlyIleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaPro
    SerArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThr
    PheTyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGly
    SerProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGlu
    SerHisLysSerProAsnMetAlaMetAlaProAlaLeuGlnProThrGlnGlyAlaMet
    ProAlaPheAlaSerAlaPheGlnArgArgAlaGlyGlyValLeuValAlaSerHisLeu
    GlnSerPheLeuGluValSerTyrArgValLeuArgRisLeuAlaGlnProGlyGlyGly
    SerAspMetAlaThrProLeuGlyProAlaSerSerLeuProGlnSerPheLeuLeuLys
    SerLeuGluGlnValArgLysIleGlnGlyAspGlyAlaAlaLeuGlnGluLysLeuCys
    AlaThrTyrLysLeuCysHisProGluGluLeuValLeuLeuGlyHisSerLeuGlyIle
    ProTrpAlaProLeuSerSerCysProSerGlnAlaLeuGlnLeuAlaGlyCysLeuSer
    GlnLeuHisSerGlyLeuPheLeuTyrGlnGlyLeuLeuGlnAlaLeuGluGlyIleSer
    ProGluLeuGlyProThrLeuAspThrLeuGlnLeuAspValAlaAspPheAlaThrThr
    IleTrpGlnGlnMetGluGluLeuGly
    pMON15967
    MetAlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAla (SEQ ID NO:198)
    ProLeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsn
    LeuArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSer
    GlyIleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaPro
    SerArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThr
    PheTyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGly
    SerProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGlu
    SerHisLysSerProAsnMetAlaThrGlnGlyAlaMetProAlaPheAlaSerAlaPhe
    GlnArgArgAlaGlyGlyValLeuValAlaSerHisLeuGlnSerPheLeuGluValSer
    TyrArgValLeuArgHisLeuAlaGlnProGlyGlyGlySerAspMetAlaThrProLeu
    GlyProAlaSerSerLeuProGlnSerPheLeuLeuLysSerLeuGluGlnValArgLys
    IleGlnGlyAspGlyAlaAlaLeuGlnGluLysLeuCysAlaThrTyrLysLeuCysHis
    ProGluGluLeuValLeuLeuGlyHisSerLeuGlyIleProTrpAlaProLeuSerSer
    CysProSerGlnAlaLeuGlnLeuAlaGlyCysLeuSerGlnLeuHisSerGlyLeuPhe
    LeuTyrGlnGlyLeuLeuGlnAlaLeuGluGlyIleSerProGluLeuGlyProThrLeu
    AspThrLeuGlnLeuAspValAlaAspPheAlaThrThrIleTrpGlnGlnMetGluGlu
    LeuGlyMetAlaProAlaLeuGlnPro
    pMON31112.pep
    MetAlaAsnCysSerAsnMetIleAspGluIleIleThrHisLeuLysGlnProProLeu (SEQ ID NO:199)
    ProLeuLeuAspPheAsnAsnLeuAsnGlyGluAspGlnAspIleLeuMetAspAsnAsn
    LeuArgArgProAsnLeuGluAlaPheAsnArgAlaValLysSerLeuGlnAsnAlaSer
    AlaIleGluSerIleLeuLysAsnLeuLeuProCysLeuProLeuAlaThrAlaAlaPro
    ThrArgHisProIleHisIleLysAspGlyAspTrpAsnGluPheArgArgLysLeuThr
    PheTyrLeuLysThrLeuGluAsnAlaGlnAlaGlnGlnTyrValGluGlyGlyGlyGly
    SerProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGlu
    SerHisLysSerProAsnMetAlaThrGlnGlyAlaMetProAlaPheAlaSerAlaPhe
    GlnArgArgAlaGlyGlyValLeuValAlaSerHisLeuGlnSerPheLeuGluValSer
    TyrArgValLeuArgHisLeuAlaGlnProSerGlyGlySerGlyGlySerGlnSerPhe
    LeuLeuLysSerLeuGluGlnValArgLysIleGlnGlyAspGlyAlaAlaLeuGlnGlu
    LysLeuCysAlaThrTyrLysLeuCysHisProGluGluLeuValLeuLeuGlyHisSer
    LeuGlyIleProTrpAlaProLeuSerSerCysProSerGlnAlaLeuGlnLeuAlaGly
    CysLeuSerGlnLeuHisSerGlyLeuPheLeuTyrGlnGlyLeuLeuGlnAlaLeuGlu
    GlyIleSerProGluLeuGlyProThrLeuAspThrLeuGlnLeuAspValAlaAspPhe
    AlaThrThrIleTrpGlnGlnMetGluGluLeuGlyMetAlaProAlaLeuGlnPro
    pMON31113.pep
    MetAlaAsnCysSerAsnMetIleAspGluIleIleThrHisLeuLysGlnProProLeu (SEQ ID NO:200)
    ProLeuLeuAspPheAsnAsnLeuAsnGlyGluAspGlnAspIleLeuMetGluAsnAsn
    LeuArgArgProAsnLeuGluAlaPheAsnArgAlaValLysSerLeuGlnAsnAlaSer
    AlaIleGluSerIleLeuLysAsnLeuLeuProCysLeuProLeuAlaThrAlaAlaPro
    ThrArgHisProIleIleIleArgAspGlyAspTrpAsnGluPheArgArgLysLeuThr
    PheTyrLeuLysThrLeuGluAsnAlaGlnAlaGlnGlnTyrValGluGlyGlyGlyGly
    SerProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGlu
    SerHisLysSerProAsnMetAlaThrGlnGlyAlaMetProAlaPheAlaSerAlaPhe
    GlnArgArgAlaGlyGlyValLeuValAlaSerHisLeuGlnSerPheLeuGluValSer
    TyrArgValLeuArgHisLeuAlaGlnProThrProLeuGlyProAlaSerSerLeuPro
    GlnSerPheLeuLeuLysSerLeuGluGlnValArgLysIleGlnGlyAspGlyAlaAla
    LeuGlnGluLysLeuCysAlaThrTyrLysLeuCysHisProGluGluLeuValLeuLeu
    GlyHisSerLeuGlyIleProTrpAlaProLeuSerSerCysProSerGlnAlaLeuGln
    LeuAlaGlyCysLeuSerGlnLeuHisSerGlyLeuPheLeuTyrGlnGlyLeuLeuGln
    AlaLeuGluGlyIleSerProGluLeuGlyProThrLeuAspThrLeuGlnLeuAspVal
    AlaAspPheAlaThrThrIleTrpGlnGlnMetGluGluLeuGlyMetAlaProAlaLeu
    GlnPro
    pMON31114.pep
    MetAlaAsnCysSerAsnMetIleAspGluIleIleThrHisLeuLysGlnProProLeu (SEQ ID NO:201)
    ProLeuLeuAspPheAsnAsnLeuAsnGlyGluAspGlnAspIleLeuMetGluAsnAsn
    LeuArgArgProAsnLeuGluAlaPheAsnArgAlaValLysSerLeuGlnAsnAlaSer
    AlaIleGluSerIleLeuLysAsnLeuLeuProCysLeuProLeuAlaThrAlaAlaPro
    ThrArgHisProIleIleIleArgAspGlyAspTrpAsnGluPheArgArgLysLeuThr
    PheTyrLeuLysThrLeuGluAsnAlaGlnAlaGlnGlnTyrValGluGlyGlyGlyGly
    SerProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGlu
    SerHisLysSerProAsnMetAlaThrGlnGlyAlaMetProAlaPheAlaSerAlaPhe
    GlnArgArgAlaGlyGlyValLeuValAlaSerHisLeuGlnSerPheLeuGluValSer
    TyrArgValLeuArgHisLeuAlaGlnProSerGlyGlySerGlyGlySerGlnSerPhe
    LeuLeuLysSerLeuGluGlnValArgLysIleGlnGlyAspGlyAlaAlaLeuGlnGlu
    LysLeuCysAlaThrTyrLysLeuCysHisProGluGluLeuValLeuLeuGlyHisSer
    LeuGlyIleProTrpAlaProLeuSerSerCysProSerGlnAlaLeuGlnLeuAlaGly
    CysLeuSerGlnLeuHisSerGlyLeuPheLeuTyrGlnGlyLeuLeuGlnAlaLeuGlu
    GlyIleSerProGluLeuGlyProThrLeuAspThrLeuGlnLeuAspValAlaAspPhe
    AlaThrThrIleTrpGlnGlnMetGluGluLeuGlyMetAlaProAlaLeuGlnPro
    pMON31115.pep
    MetAlaAsnCysSerAsnMetIleAspGluIleIleThrHisLeuLysGlnProProLeu (SEQ ID NO:202)
    ProLeuLeuAspPheAsnAsnLeuAsnGlyGluAspGlnAspIleLeuMetAspAsnAsn
    LeuArgArgProAsnLeuGluAlaPheAsnArgAlaValLysSerLeuGlnAsnAlaSer
    AlaIleGluSerIleLeuLysAsnLeuLeuProCysLeuProLeuAlaThrAlaAlaPro
    ThrArgHisProIleHisIleLysAspGlyAspTrpAsnGluPheArgArgLysLeuThr
    PheTyrLeuLysThrLeuGluAsnAlaGlnAlaGlnGlnTyrValGluGlyGlyGlyGly
    SerProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGlu
    SerHisLysSerProAsnMetAlaThrGlnGlyAlaMetProAlaPheAlaSerAlaPhe
    GlnArgArgAlaGlyGlyValLeuValAlaSerHisLeuGlnSerPheLeuGluValSer
    TyrArgValLeuArgHisLeuAlaGlnProThrProLeuGlyProAlaSerSerLeuPro
    GlnSerPheLeuLeuLysSerLeuGluGlnValArgLysIleGlnGlyAspGlyAlaAla
    LeuGlnGluLysLeuCysAlaThrTyrLysLeuCysHisProGluGluLeuValLeuLeu
    GlyHisSerLeuGlyIleProTrpAlaProLeuSerSerCysProSerGlnAlaLeuGln
    LeuAlaGlyCysLeuSerGlnLeuHisSerGlyLeuPheLeuTyrGlnGlyLeuLeuGln
    AlaLeuGluGlyIleSerProGluLeuGlyProThrLeuAspThrLeuGlnLeuAspVal
    AlaAspPheAlaThrThrIleTrpGlnGlnMetGluGluLeuGlyMetAlaProAlaLeu
    GlnPro
    pMON28505
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:203)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetGluValHisProLeuProThrProValLeuLeuProAlaVal
    AspPheSerLeuGlyGluTrpLysThrGlnMetGluGluThrLysAlaGlnAspIleLeu
    GlyAlaValThrLeuLeuLeuGluGlyValMetAlaAlaArgGlyGlnLeuGlyProThr
    CysLeuSerSerLeuLeuGlyGlnLeuSerGlyGlnValArgLeuLeuLeuGlyAlaLeu
    GlnSerLeuLeuGlyThrGlnLeuProProGlnGlyArgThrThrAlaHisLysAspPro
    AsnAlaIlePheLeuSerPheGlnHisLeuLeuArgGlyLysValArgPheLeuMetLeu
    ValGlyGlySerThrLeuCysValArgGluPheGlyGlyAsnMetAlaSerProAlaPro
    ProAlaCysAspLeuArgValLeuSerLysLeuLeuArgAspSerHisValLeuHisSer
    ArgLeuSerGlnCysPro
    pMON28506
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:204)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetLeuProThrProValLeuLeuProAlaValAspPheSerLeu
    GlyGluTrpLysThrGlnMetGluGluThrLysAlaGlnAspIleLeuGlyAlaValThr
    LeuLeuLeuGluGlyValMetAlaAlaArgGlyGlnLeuGlyProThrCysLeuSerSer
    LeuLeuGlyGlnLeuSerGlyGlnValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeu
    GlyThrGlnLeuProProGlnGlyArgThrThrAlaHisLysAspProAsnAlaIlePhe
    LeuSerPheGlnHisLeuLeuArgGlyLysValArgPheLeuMetLeuValGlyGlySer
    ThrLeuCysValArgGluPheGlyGlyAsnMetAlaSerProAlaProProAlaCysAsp
    LeuArgValLeuSerLysLeuLeuArgAspSerHisValLeuHisSerArgLeuSerGln
    CysProGluValHisPro
    pMON28507
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:205)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetValLeuLeuProAlaValAspPheSerLeuGlyGluTrpLys
    ThrGlnMetGluGluThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGlu
    GlyValMetAlaAlaArgGlyGlnLeuGlyProThrCysLeuSerSerLeuLeuGlyGln
    LeuSerGlyGlnValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeu
    ProProGlnGlyArgThrThrAlaHisLysAspProAsnAlaIlePheLeuSerPheGln
    HisLeuLeuArgGlyLysValArgPheLeuMetLeuValGlyGlySerThrLeuCysVal
    ArgGluPheGlyGlyAsnMetAlaSerProAlaProProAlaCysAspLeuArgValLeu
    SerLysLeuLeuArgAspSerHisValLeuHisSerArgLeuSerGlnCysProGluVal
    HisProLeuProThrPro
    pMON28508
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:206)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGlu
    GluThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAla
    AlaArgGlyGlnLeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGln
    ValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeuProProGlnGly
    ArgThrThrAlaHisLysAspProAsnAlaIlePheLeuSerPheGlnHisLeuLeuArg
    GlyLysValArgPheLeuMetLeuValGlyGlySerThrLeuCysValArgGluPheGly
    GlyAsnMetAlaSerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeu
    ArgAspSerHisValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuPro
    ThrProValLeuLeuPro
    pMON28509
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:207)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetAspPheSerLeuGlyGluTrpLysThrGlnMetGluGluThr
    LysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAlaAlaArg
    GlyGlnLeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGlnValArg
    LeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeuProProGlnGlyArgThr
    ThrAlaHisLysAspProAsnAlaIlePheLeuSerPheGlnHisLeuLeuArgGlyLys
    ValArgPheLeuMetLeuValGlyGlySerThrLeuCysValArgGluPheGlyGlyAsn
    MetAlaSerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeuArgAsp
    SerHisValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuProThrPro
    ValLeuLeuProAlaVal
    pMON28510
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:208)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetGlyGluTrpLysThrGlnMetGluGluThrLysAlaGlnAsp
    IleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAlaAlaArgGlyGlnLeuGly
    ProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGlnValArgLeuLeuLeuGly
    AlaLeuGlnSerLeuLeuGlyThrGlnLeuProProGlnGlyArgThrThrAlaHisLys
    AspProAsnAlaIlePheLeuSerPheGlnHisLeuLeuArgGlyLysValArgPheLeu
    MetLeuValGlyGlySerThrLeuCysValArgGluPheGlyGlyAsnMetAlaSerPro
    AlaProProAlaCysAspLeuArgValLeuSerLysLeuLeuArgAspSerHisValLeu
    HisSerArgLeuSerGlnCysProGluValHisProLeuProThrProValLeuLeuPro
    AlaValAspPheSerLeu
    pMON28511
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:209)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGly
    GlnValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeuProProGln
    GlyArgThrThrAlaHisLysAspProAsnAlaIlePheLeuSerPheGlnHisLeuLeu
    ArgGlyLysValArgPheLeuMetLeuValGlyGlySerThrLeuCysValArgGluPhe
    GlyGlyAsnMetAlaSerProAlaProProAlaCysAspLeuArgValLeuSerLysLeu
    LeuArgAspSerHisValLeuHisSerArgLeuSerGlnCysProGluValHisProLeu
    ProThrProValLeuLeuProAlaValAspPheSerLeuGlyGluTrpLysThrGlnMet
    GluGluThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMet
    AlaAlaArgGlyGlnLeu
    pMON28512
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:210)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetGlyThrGlnLeuProProGlnGlyArgThrThrAlaHisLys
    AspProAsnAlaIlePheLeuSerPheGlnHisLeuLeuArgGlyLysValArgPheLeu
    MetLeuValGlyGlySerThrLeuCysValArgGluPheGlyGlyAsnMetAlaSerPro
    AlaProProAlaCysAspLeuArgValLeuSerLysLeuLeuArgAspSerHisValLeu
    HisSerArgLeuSerGlnCysProGluValHisProLeuProThrProValLeuLeuPro
    AlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGluGluThrLysAlaGlnAsp
    IleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAlaAlaArgGlyGlnLeuGly
    ProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGlnValArgLeuLeuLeuGly
    AlaLeuGlnSerLeuLeu
    pMON28513
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:211)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetGlyArgThrThrAlaHisLysAspProAsnAlaIlePheLeu
    SerPheGlnHisLeuLeuArgGlyLysValArgPheLeuMetLeuValGlyGlySerThr
    LeuCysValArgGluPheGlyGlyAsnMetAlaSerProAlaProProAlaCysAspLeu
    ArgValLeuSerLysLeuLeuArgAspSerHisValLeuHisSerArgLeuSerGlnCys
    ProGluValHisProLeuProThrProValLeuLeuProAlaValAspPheSerLeuGly
    GluTrpLysThrGlnMetGluGluThrLysAlaGlnAspIleLeuGlyAlaValThrLeu
    LeuLeuGluGlyValMetAlaAlaArgGlyGlnLeuGlyProThrCysLeuSerSerLeu
    LeuGlyGlnLeuSerGlyGlnValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGly
    ThrGlnLeuProProGln
    pMON28514
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:212)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerC-lyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetAlaHisLysAspProAsnAlaIlePheLeuSerPheGlnHis
    LeuLeuArgGlyLysValArgPheLeuMetLeuValGlyGlySerThrLeuCysValArg
    GluPheGlyGlyAsnMetAlaSerProAlaProProAlaCysAspLeuArgValLeuSer
    LysLeuLeuArgAspSerHisValLeuHisSerArgLeuSerGlnCysProGluValHis
    ProLeuProThrProValLeuLeuProAlaValAspPheSerLeuGlyGluTrpLysThr
    GlnMetGluGluThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGly
    ValMetAlaAlaArgGlyGlnLeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeu
    SerGlyGlnValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeuPro
    ProGlnGlyArgThrThr
    pMON28515
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:213)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetAspProAsnAlaIlePheLeuSerPheGlnHisLeuLeuArg
    GlyLysValArgPheLeuMetLeuValGlyGlySerThrLeuCysValArgGluPheGly
    GlyAsnMetAlaSerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeu
    ArgAspSerHisValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuPro
    ThrProValLeuLeuProAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGlu
    GluThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAla
    AlaArgGlyGlnLeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGln
    ValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeuProProGlnGly
    ArgThrThrAlaHisLys
    pMON28516
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:214)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetAlaIlePheLeuSerPheGlnHisLeuLeuArgGlyLysVal
    ArgPheLeuMetLeuValGlyGlySerThrLeuCysValArgGluPheGlyGlyAsnMet
    AlaSerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeuArgAspSer
    HisValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuProThrProVal
    LeuLeuProAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGluGluThrLys
    AlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAlaAlaArgGly
    GlnLeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGlnValArgLeu
    LeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeuProProGlnGlyArgThrThr
    AlaHisLysAspProAsn
    pMON28519
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:215)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetGluValHisProLeuProThrProValLeuLeuProAlaVal
    AspPheSerLeuGlyGluTrpLysThrGlnMetGluGluThrLysAlaGlnAspIleLeu
    GlyAlaValThrLeuLeuLeuGluGlyValMetAlaAlaArgGlyGlnLeuGlyProThr
    CysLeuSerSerLeuLeuGlyGlnLeuSerGlyGlnValArgLeuLeuLeuGlyAlaLeu
    GlnSerLeuLeuGlyThrGlnLeuProProGlnGlyArgThrThrAlaHisLysAspPro
    AsnAlaIlePheLeuSerPheGlnHisLeuLeuArgGlyLysValArgPheLeuMetLeu
    ValGlyGlySerThrLeuCysValArgGluPheGlyAsnMetAlaSerProAlaProPro
    AlaCysAspLeuArgValLeuSerLysLeuLeuArgAspSerHisValLeuHisSerArg
    LeuSerGlnCysPro
    pMON28520
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:216)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetLeuProThrProValLeuLeuProAlaValAspPheSerLeu
    GlyGluTrpLysThrGlnMetGluGluThrLysAlaGlnAspIleLeuGlyAlaValThr
    LeuLeuLeuGluGlyValMetAlaAlaArgGlyGlnLeuGlyProThrCysLeuSerSer
    LeuLeuGlyGlnLeuSerGlyGlnValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeu
    GlyThrGlnLeuProProGlnGlyArgThrThrAlaHisLysAspProAsnAlaIlePhe
    LeuSerPheGlnHisLeuLeuArgGlyLysValArgPheLeuMetLeuValGlyGlySer
    ThrLeuCysValArgGluPheGlyAsnMetAlaSerProAlaProProAlaCysAspLeu
    ArgValLeuSerLysLeuLeuArgAspSerHisValLeuHisSerArgLeuSerGlnCys
    ProGluValHisPro
    pMON28521
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:217)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetValLeuLeuProAlaValAspPheSerLeuGlyGluTrpLys
    ThrGlnMetGluGluThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGlu
    GlyValMetAlaAlaArgGlyGlnLeuGlyProThrCysLeuSerSerLeuLeuGlyGln
    LeuSerGlyGlnValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeu
    ProProGlnGlyArgThrThrAlaHisLysAspProAsnAlaIlePheLeuSerPheGln
    HisLeuLeuArgGlyLysValArgPheLeuMetLeuValGlyGlySerThrLeuCysVal
    ArgGluPheGlyAsnMetAlaSerProAlaProProAlaCysAspLeuArgValLeuSer
    LysLeuLeuArgAspSerHisValLeuHisSerArgLeuSerGlnCysProGluValHis
    ProLeuProThrPro
    pMON28522
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:218)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetAlaValAspPheSerLeuGlyGluTrpLysmrelnMetGlu
    GluThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAla
    AlaArgGlyGlnLeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGln
    ValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeuProProGlnGly
    ArgThrThrAlaHisLysAspProAsnAlaIlePheLeuSerPheGlnHisLeuLeuArg
    GlyLysValArgPheLeuMetLeuValGlyGlySerThrLeuCysValArgGluPheGly
    AsnMetAlaSerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeuArg
    AspSerHisValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuProThr
    ProValLeuLeuPro
    pMON28523
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:219)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetAspPheSerLeuGlyGluTrpLysThrGlnMetGluGluThr
    LysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAlaAlaArg
    GlyGlnLeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGlnValArg
    LeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeuProProGlnGlyArgThr
    ThrAlaHisLysAspProAsnAlaIlePheLeuSerPheGlnHisLeuLeuArgGlyLys
    ValArgPheLeuMetLeuValGlyGlySerThrLeuCysValArgGluPheGlyAsnMet
    AlaSerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeuArgAspSer
    HisValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuProThrProVal
    LeuLeuProAlaVal
    pMON28524
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:220)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetGlyGluTrpLysThrGlnMetGluGluThrLysAlaGlnAsp
    IleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAlaAlaArgGlyGlnLeuGly
    ProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGlnValArgLeuLeuLeuGly
    AlaLeuGlnSerLeuLeuGlyThrGlnLeuProProGlnGlyArgThrThrAlaHisLys
    AspProAsnAlaIlePheLeuSerPheGlnHisLeuLeuArgGlyLysValArgPheLeu
    MetLeuValGlyGlySerThrLeuCysValArgGluPheGlyAsnMetAlaSerProAla
    ProProAlaCysAspLeuArgValLeuSerLysLeuLeuArgAspSerHisValLeuHis
    SerArgLeuSerGlnCysProGluValHisProLeuProThrProValLeuLeuProAla
    ValAspPheSerLeu
    pMON28525
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:221)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGly
    GlnValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeuProProGln
    GlyArgThrThrAlaHisLysAspProAsnAlaIlePheLeuSerPheGlnHisLeuLeu
    ArgGlyLysValArgPheLeuMetLeuValGlyGlySerThrLeuCysValArgGluPhe
    GlyAsnMetAlaSerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeu
    ArgAspSerHisValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuPro
    ThrProValLeuLeuProAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGlu
    GluThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAla
    AlaArgGlyGlnLeu
    pMON28526
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:222)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetGlyThrGlnLeuProProGlnGlyArgThrThrAlaHisLys
    AspProAsnAlaIlePheLeuSerPheGlnHisLeuLeuArgGlyLysValArgPheLeu
    MetLeuValGlyGlySerThrLeuCysValArgGluPheGlyAsnMetAlaSerProAla
    ProProAlaCysAspLeuArgValLeuSerLysLeuLeuArgAspSerHisValLeuHis
    SerArgLeuSerGlnCysProGluValHisProLeuProThrProValLeuLeuProAla
    ValAspPheSerLeuGlyGluTrpLysThrGlnMetGluGluThrLysAlaGlnAspIle
    LeuGlyAlaValThrLeuLeuLeuGluGlyValMetAlaAlaArgGlyGlnLeuGlyPro
    ThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGlnValArgLeuLeuLeuGlyAla
    LeuGlnSerLeuLeu
    pMON28527
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:223)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetGlyArgThrThrAlaHisLysAspProAsnAlaIlePheLeu
    SerPheGlnHisLeuLeuArgGlyLysValArgPheLeuMetLeuValGlyGlySerThr
    LeuCysValArgGluPheGlyAsnMetAlaSerProAlaProProAlaCysAspLeuArg
    ValLeuSerLysLeuLeuArgAspSerHisValLeuHisSerArgLeuSerGlnCysPro
    GluValHisProLeuProThrProValLeuLeuProAlaValAspPheSerLeuGlyGlu
    TrpLysThrGlnMetGluGluThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeu
    LeuGluGlyValMetAlaAlaArgGlyGlnLeuGlyProThrCysLeuSerSerLeuLeu
    GlyGlnLeuSerGlyGlnValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThr
    GlnLeuProProGln
    pMON28528
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:224)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetAlaHisLysAspProAsnAlaIlePheLeuSerPheGlnHis
    LeuLeuArgGlyLysValArgPheLeuMetLeuValGlyGlySerThrLeuCysValArg
    GluPheGlyAsnMetAlaSerProAlaProProAlaCysAspLeuArgValLeuSerLys
    LeuLeuArgAspSerHisValLeuHisSerArgLeuSerGlnCysProGluValHisPro
    LeuProThrProValLeuLeuProAlaValAspPheSerLeuGlyGluTrpLysThrGln
    MetGluGluThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyVal
    MetAlaAlaArgGlyGlnLeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSer
    GlyGlnValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeuProPro
    GlnGlyArgThrThr
    pMON28529
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:225)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetAspProAsnAlaIlePheLeuSerPheGlnHisLeuLeuArg
    GlyLysValArgPheLeuMetLeuValGlyGlySerThrLeuCysValArgGluPheGly
    AsnMetAlaSerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeuArg
    AspSerHisValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuProThr
    ProValLeuLeuProAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGluGlu
    ThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAlaAla
    ArgGlyGlnLeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGlnVal
    ArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeuProProGlnGlyArg
    ThrThrAlaHisLys
    pMON28530
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:226)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetAlaIlePheLeuSerPheGlnHisLeuLeuArgGlyLysVal
    ArgPheLeuMetLeuValGlyGlySerThrLeuCysValArgGluPheGlyAsnMetAla
    SerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeuArgAspSerHis
    ValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuProThrProValLeu
    LeuProAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGluGluThrLysAla
    GlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAlaAlaArgGlyGln
    LeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGlnValArgLeuLeu
    LeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeuProProGlnGlyArgThrThrAla
    HisLysAspProAsn
    pMON28533
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:227)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetGluValHisProLeuProThrProValLeuLeuProAlaVal
    AspPheSerLeuGlyGluTrpLysThrGlnMetGluGluThrLysAlaGlnAspIleLeu
    GlyAlaValThrLeuLeuLeuGluGlyValMetAlaAlaArgGlyGlnLeuGlyProThr
    CysLeuSerSerLeuLeuGlyGlnLeuSerGlyGlnValArgLeuLeuLeuGlyAlaLeu
    GlnSerLeuLeuGlyThrGlnLeuProProGlnGlyArgThrThrAlaHisLysAspPro
    AsnAlaIlePheLeuSerPheGlnHisLeuLeuArgGlyLysValArgPheLeuMetLeu
    ValGlyGlySerThrLeuCysValArgGluPheGlyGlyAsnGlyGlyAsnMetAlaSer
    ProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeuArgAspSerHisVal
    LeuHisSerArgLeuSerGlnCysPro
    pMON28534
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:228)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetLeuProThrProValLeuLeuProAlaValAspPheSerLeu
    GlyGluTrpLysThrGlnMetGluGluThrLysAlaGlnAspIleLeuGlyAlaValThr
    LeuLeuLeuGluGlyValMetAlaAlaArgGlyGlnLeuGlyProThrCysLeuSerSer
    LeuLeuGlyGlnLeuSerGlyGlnValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeu
    GlyThrGlnLeuProProGlnGlyArgThrThrAlaHisLysAspProAsnAlaIlePhe
    LeuSerPheGlnHisLeuLeuArgGlyLysValArgPheLeuMetLeuValGlyGlySer
    ThrLeuCysValArgGluPheGlyGlyAsnGlyGlyAsnMetAlaSerProAlaProPro
    AlaCysAspLeuArgValLeuSerLysLeuLeuArgAspSerHisValLeuHisSerArg
    LeuSerGlnCysProGluValHisPro
    pMON28535
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:229)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetValLeuLeuProAlaValAspPheSerLeuGlyGluTrpLys
    ThrGlnMetGluGluThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGlu
    GlyValMetAlaAlaArgGlyGlnLeuGlyProThrCysLeuSerSerLeuLeuGlyGln
    LeuSerGlyGlnValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeu
    ProProGlnGlyArgThrThrAlaHisLysAspProAsnAlaIlePheLeuSerPheGln
    HisLeuLeuArgGlyLysValArgPheLeuMetLeuValGlyGlySerThrLeuCysVal
    ArgGluPheGlyGlyAsnGlyGlyAsnMetAlaSerProAlaProProAlaCysAspLeu
    ArgValLeuSerLysLeuLeuArgAspSerHisValLeuHisSerArgLeuSerGlnCys
    ProGluValHisProLeuProThrPro
    pMON28536
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:230)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGlu
    GluThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAla
    AlaArgGlyGlnLeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGln
    ValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeuProProGlnGly
    ArgThrThrAlaHisLysAspProAsnAlaIlePheLeuSerPheGlnHisLeuLeuArg
    GlyLysValArgPheLeuMetLeuValGlyGlySerThrLeuCysValArgGluPheGly
    GlyAsnGlyGlyAsnMetAlaSerProAlaProProAlaCysAspLeuArgValLeuSer
    LysLeuLeuArgAspSerHisValLeuHisSerArgLeuSerGlnCysProGluValHis
    ProLeuProThrProValLeuLeuPro
    pMON28537
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:231)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGlubysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetAspPheSerLeuGlyGluTrpLysThrGlnMetGluGluThr
    LysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAlaAlaArg
    GlyGlnLeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGlnValArg
    LeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeuProProGlnGlyArgThr
    ThrAlaHisLysAspProAsnAlaIlePheLeuSerPheGlnHisLeuLeuArgGlyLys
    ValArgPheLeuMetLeuValGlyGlySerThrLeuCysValArgGluPheGlyGlyAsn
    GlyGlyAsnMetAlaSerProAlaProProAlaCysAspLeuArgValLeuSerLysLeu
    LeuArgAspSerHisValLeuHisSerArgLeuSerGlnCysProGluValHisProLeu
    ProThrProValLeuLeuProAlaVal
    pMON28538
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:232)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetGlyGluTrpLysThrGlnMetGluGluThrLysAlaGlnAsp
    IleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAlaAlaArgGlyGlnLeuGly
    ProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGlnValArgLeuLeuLeuGly
    AlaLeuGlnSerLeuLeuGlyThrClnLeuProProGlnGlyArgThrThrAlaHisLys
    AspProAsnAlaIlePheLeuSerPheGlnHisLeuLeuArgGlyLysValArgPheLeu
    MetLeuValGlyGlySerThrLeuCysValArgGluPheGlyGlyAsnGlyGlyAsnMet
    AlaSerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeuArgAspSer
    HisValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuProThrProVal
    LeuLeuProAlaValAspPheSerLeu
    pMON28539
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:233)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGly
    GlnValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeuProProGln
    GlyArgThrThrAlaHisLysAspProAsnAlaIlePheLeuSerPheGlnHisLeuLeu
    ArgGlyLysValArgPheLeuMetLeuValGlyGlySerThrLeuCysValArgGluPhe
    GlyGlyAsnGlyGlyAsnMetAlaSerProAlaProProAlaCysAspLeuArgValLeu
    SerLysLeuLeuArgAspSerHisValLeuHisSerArgLeuSerGlnCysProGluVal
    HisProLeuProThrProValLeuLeuProAlaValAspPheSerLeuGlyGluTrpLys
    ThrGlnMetGluGluThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGlu
    GlyValMetAlaAlaArgGlyGlnLeu
    pMON28540
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:234)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetGlyThrGlnLeuProProGlnGlyArgThrThrAlaHisLys
    AspProAsnAlaIlePheLeuSerPheGlnHisLeuLeuArgGlyLysValArgPheLeu
    MetLeuValGlyGlySerThrLeuCysValArgGluPheGlyGlyAsnGlyGlyAsnMet
    AlaSerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeuArgAspSer
    HisValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuProThrProVal
    LeuLeuProAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGluGluThrLys
    AlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAlaAlaArgGly
    GlnLeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGlnValArgLeu
    LeuLeuGlyAlaLeuGlnSerLeuLeu
    pMON28541
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:235)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetGlyArgThrThrAlaHisLysAspProAsnAlaIlePheLeu
    SerPheGlnHisLeuLeuArgGlyLysValArgPheLeuMetLeuValGlyGlySerThr
    LeuCysValArgGluPheGlyGlyAsnGlyGlyAsnMetAlaSerProAlaProProAla
    CysAspLeuArgValLeuSerLysLeuLeuArgAspSerHisValLeuHisSerArgLeu
    SerGlnCysProGluValHisProLeuProThrProValLeuLeuProAlaValAspPhe
    SerLeuGlyGluTrpLysThrGlnMetGluGluThrLysAlaGlnAspIleLeuGlyAla
    ValThrLeuLeuLeuGluGlyValMetAlaAlaArgGlyGlnLeuGlyProThrCysLeu
    SerSerLeuLeuGlyGlnLeuSerGlyGlnValArgLeuLeuLeuGlyAlaLeuGlnSer
    LeuLeuGlyThrGlnLeuProProGln
    pMON28542
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:236)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetAlaHisLysAspProAsnAlaIlePheLeuSerPheGlnHis
    LeuLeuArgGlyLysValArgPheLeuMetLeuValGlyGlySerThrLeuCysValArg
    GluPheGlyGlyAsnGlyGlyAsnMetAlaSerProAlaProProAlaCysAspLeuArg
    ValLeuSerLysLeuLeuArgAspSerHisValLeuHisSerArgLeuSerGlncysPro
    GluValHisProLeuProThrProValLeuLeuProAlaValAspPheSerLeuGlyGlu
    TrpLysThrGlnMetGluGluThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeu
    LeuGluGlyValMetAlaAlaArgGlyGlnLeuGlyProThrCysLeuSerSerLeuLeu
    GlyGlnLeuSerGlyGlnValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThr
    GlnLeuProProGlnGlyArgThrThr
    pMON28543
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:237)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetAspProAsnAlaIlePheLeuSerPheGlnHisLeuLeuArg
    GlyLysValArgPheLeuMetLeuValGlyGlySerThrLeuCysValArgGluPheGly
    GlyAsnGlyGlyAsnMetAlaSerProAlaProProAlaCysAspLeuArgValLeuSer
    LysLeuLeuArgAspSerHisValLeuHisSerArgLeuSerGlnCysProGluValHis
    ProLeuProThrProValLeuLeuProAlaValAspPheSerLeuGlyGluTrpLysThr
    GlnMetGluGluThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGly
    ValMetAlaAlaArgGlyGlnLeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeu
    SerGlyGlnValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeuPro
    ProGlnGlyArgThrThrAlaHisLys
    pMON28544
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:238)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetAlaIlePheLeuSerPheGlnHisLeuLeuArgGlyLysVal
    ArgPheLeuMetLeuValGlyGlySerThrLeuCysValArgGluPheGlyGlyAsnGly
    GlyAsnMetAlaSerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeu
    ArgAspSerHisValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuPro
    ThrProValLeuLeuProAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGlu
    GluThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAla
    AlaArgGlyGlnLeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGln
    ValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeuProProGlnGly
    ArgThrThrAlaHisLysAspProAsn
    pMON28545
    AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:239)
    LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu
    ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly
    IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer
    ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe
    TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer
    ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer
    HisLysSerProAsnMetAspProAsnAlaIlePheLeuSerPheGlnHisLeuLeuArg
    GlyLysValArgPheLeuMetLeuValGlyGlySerThrLeuCysValArgGluPheGly
    GlyAsnMetAlaSerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeu
    ArgAspSerHisValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuPro
    ThrProValLeuLeuProAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGlu
    GluThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAla
    AlaArgGlyGlnLeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGln
    ValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnGlyArgThrThrAla
    HisLys
    pMON32132
    SerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeuArgAspSerHis (SEQ ID NO:252)
    ValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuProThrProValLeu
    LeuProAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGluGluThrLysAla
    GlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAlaAlaArgGlyGln
    LeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGlnValArgLeuLeu
    LeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeuProProGlnGlyArgThrThrAla
    HisLysAspProAsnAlaIlePheLeuSerPheGlnHisLeuLeuArgGlyLysValArg
    PheLeuMetLeuValGlyGlySerThrLeuCysValArg
    PMON32133
    SerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeuArgAspSerHis (SEQ ID NO:253)
    ValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuProThrProValLeu
    LeuProAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGluGluThrLysAla
    GlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAlaAlaArgGlyGln
    LeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGlnValArgLeuLeu
    LeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnGlyArgThrThrAlaHisLysAspPro
    AsnAlaIlePheLeuSerPheGlnHisLeuLeuArgGlyLysValArgPheLeuMetLeu
    ValGlyGlySerThrLeuCysValArg
    PMON32134
    SerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeuArgAspSerHis (SEQ ID NO: 254)
    ValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuProThrProValLeu
    LeuProAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGluGluThrLysAla
    GlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAlaAlaArgGlyGln
    LeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGlnValArgLeuLeu
    LeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeuProProGlnGlyArgThrThrAla
    HisLysAspProAsnAlaIlePheLeuSerPheGlnHisLeuLeuArgGlyLysValArg
    PheLeuMetLeuValGlyGlySerThrLeuCysValArg
    pmon16017.pep
     1 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu (SEQ ID NO:271)
     16 Lys Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp
     31 Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn
     46 Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser
     61 Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser
     76 Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly
     91 Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr
    106 Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly
    121 Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser
    136 Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Leu Gly
    151 Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu
    166 Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys
    181 Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu
    196 Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys
    211 Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His
    226 Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly
    241 Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp
    256 Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu
    271 Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala
    286 Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala
    301 Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg
    316 His Leu Ala Gln Pro Asp Met Ala Thr Pro
    pmon16018.pep
     1 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu (SEQ ID NO:272)
     16 Lys Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp
     31 Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn
     46 Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser
     61 Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser
     76 Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly
     31 Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr
    106 Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly
    121 Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser
    136 Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Leu Gly
    151 Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu
    176 Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys
    191 Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu
    206 Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys
    221 Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His
    236 Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly
    251 Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp
    266 Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu
    281 Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala
    296 Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala
    311 Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg
    326 His Leu Ala Gln Pro Asp Met Ala Thr Pro
    pmon16019.pep
     1 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu (SEQ ID NO:273)
     16 Lys Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp
     31 Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn
     46 Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser
     61 Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser
     76 Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly
     91 Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr
    106 Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly
    121 Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser
    136 Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Phe Leu
    151 Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala
    166 Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro
    181 Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala
    196 Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys
    211 Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu
    226 Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp
    241 Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln
    256 Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro Thr Gln
    271 Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly
    286 Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser
    301 Tyr Arg Val Leu Arg His Leu Ala Gln Pro Asp Met Ala Thr Pro
    316 Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser
    pmon16020.pep
     1 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu (SEQ ID NO:274)
     16 Lys Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp
     31 Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn
     46 Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser
     61 Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser
     76 Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly
     91 Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr
    106 Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly
    121 Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser
    136 Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Glu Gln
    151 Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu
    166 Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu
    181 Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro
    196 Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser
    211 Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile
    226 Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val
    241 Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly
    256 Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe
    271 Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser
    286 His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His
    301 Leu Ala Gln Pro Asp Met Ala Thr Pro Leu Gly Pro Ala Ser Ser
    316 Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu
    pmon16021.pep
     1 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu (SEQ ID NO:275)
     16 Lys Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp
     31 Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn
     46 Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser
     61 Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser
     76 Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly
     91 Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr
    106 Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly
    121 Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser
    136 Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Leu Leu
    151 Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro
    166 Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser
    181 Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile
    196 Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val
    211 Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly
    226 Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe
    241 Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser
    256 His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His
    271 Leu Ala Gln Pro Asp Met Ala Thr Pro Leu Gly Pro Ala Ser Ser
    286 Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys
    301 Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr
    316 Tyr Lys Leu Cys His Pro Glu Glu Leu Val
    pmon16022.pep
     1 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu (SEQ ID NO:276)
     16 Lys Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp
     31 Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn
     46 Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser
     61 Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser
     76 Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly
     91 Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr
    106 Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly
    121 Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser
    136 Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Pro Leu
    151 Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser
    166 Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala
    181 Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu
    196 Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met
    211 Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala
    226 Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val
    241 Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg
    256 Val Leu Arg His Leu Ala Gln Pro Asp Met Ala Thr Pro Leu Gly
    271 Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu
    286 Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys
    301 Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu
    316 Leu Gly His Ser Leu Gly Ile Pro Trp Ala
    pmon16023.pep
     1 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu (SEQ ID NO:277)
     16 Lys Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp
     31 Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn
     46 Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser
     61 Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser
     76 Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly
     91 Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr
    106 Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly
    121 Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser
    136 Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Gln Ala
    151 Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe
    166 Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu
    181 Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe
    196 Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro
    211 Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala
    226 Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln
    241 Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln
    256 Pro Asp Met Ala Thr Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln
    271 Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly
    286 Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu
    301 Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile
    316 Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser
    pmon16024.pep
     1 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu (SEQ ID NO:278)
     16 Lys Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp
     31 Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn
     46 Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser
     61 Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser
     76 Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly
     91 Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr
    106 Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly
    121 Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser
    136 Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Leu Gln
    151 Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr
    166 Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly
    181 Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr
    196 Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu
    211 Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln
    226 Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe
    241 Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Asp
    256 Met Ala Thr Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe
    271 Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly
    286 Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His
    301 Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp
    316 Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala
    pmon16025.pep
     1 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu (SEQ ID NO:279)
     16 Lys Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp
     31 Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn
     46 Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser
     61 Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser
     76 Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly
     91 Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr
    106 Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly
    121 Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser
    136 Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Leu Ala
    151 Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly
    166 Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr
    181 Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile
    196 Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro
    211 Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg
    226 Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu
    241 Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Asp Met Ala
    256 Thr Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu
    271 Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala
    286 Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu
    301 Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro
    316 Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln
    pmon16026.pep
     1 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu (SEQ ID NO:280)
     16 Lys Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp
     31 Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn
     46 Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser
     61 Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser
     76 Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly
     91 Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr
    106 Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly
    121 Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser
    136 Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Glu Leu
    151 Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala
    166 Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala
    181 Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg
    196 His Leu Ala Gln Pro Asp Met Ala Thr Pro Leu Gly Pro Ala Ser
    211 Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg
    226 Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala
    241 Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His
    256 Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln
    271 Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu
    286 Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro
    301 Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp
    316 Phe Ala Thr Thr Ile Trp Gln Gln Met Glu
    pmon16027.pep
     1 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu (SEQ ID NO:281)
     16 Lys Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp
     31 Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn
     46 Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser
     61 Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser
     76 Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly
     91 Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr
    106 Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly
    121 Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser
    136 Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Gly Met
    151 Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala
    166 Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His
    181 Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu
    196 Ala Gln Pro Asp Met Ala Thr Pro Leu Gly Pro Ala Ser Ser Leu
    211 Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile
    226 Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr
    241 Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu
    256 Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu
    271 Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu
    286 Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu
    301 Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala
    316 Thr Thr Ile Trp Gln Gln Met Glu Glu Leu
    pmon16028.pep
     1 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu (SEQ ID NO:282)
     16 Lys Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp
     31 Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn
     46 Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser
     61 Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser
     76 Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly
     91 Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr
    106 Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly
    121 Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser
    136 Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Ser Phe
    151 Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Asp
    166 Met Ala Thr Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe
    181 Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly
    196 Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His
    211 Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp
    226 Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly
    241 Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu
    256 Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu
    271 Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp
    286 Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro Thr
    301 Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala
    316 Gly Gly Val Leu Val Ala Ser His Leu Gln
    MetAlaGlyArgThrThrAlaHisLysAspProAsnAlaIlePheLeuSerPheGlnHis (SEQ ID NO:284)
    LeuLeuArgGlyLysValArgPheLeuMetLeuValGlyGlySerThrLeuAlaValArg
    GluPheGlyGlyAsnMetAlaSerProAlaProProAlaAlaAspLeuArgValLeuSer
    LysLeuLeuArgAspSerHisValLeuHisSerArgLeuSerGlnCysProGluValHis
    ProLeuProThrProValLeuLeuProAlaValAspPheSerLeuGlyGluTrpLysThr
    GlnMetGluGluThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGly
    ValMetAlaAlaArgGlyGlnLeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeu
    SerGlyGlnValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeuPro
    ProGln;
    MetAlaGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGlnValArgLeu (SEQ ID NO:285)
    LeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeuProProGlnGlyArgThrThr
    AlaHisLysAspProAsnAlaIlePheLeuSerPheGlnHisLeuLeuArgGlyLysVal
    ArgPheLeuMetLeuValGlyGlySerThrLeuAlaValArgGluPheGlyGlyAsnMet
    AlaSerProAlaProProAlaAlaAspLeuArgValLeuSerLysLeuLeuArgAspSer
    HisValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuProThrProVal
    LeuLeuProAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGluGluThrLys
    AlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAlaAlaArgGly
    GlnLeu
  • [0466]
  • 1 313 174 amino acids amino acid unknown unknown protein Modified-site 1 /note= “Xaa at position 1 is Thr, Ser, Arg, Tyr or Gly;” Modified-site 2 /note= “Xaa at position 2 is Pro or Leu;” Modified-site 3 /note= “Xaa at position 3 is Leu, Arg, Tyr or Ser;” Modified-site 13 /note= “Xaa at position 13 is Phe, Ser, His, Thr or Pro;” Modified-site 16 /note= “Xaa at position 16 is Lys, Pro, Ser, thr or His;” Modified-site 17 /note= “Xaa at position 17 is Cys, Ser, Gly, Ala, Ile, Tyr or Arg;” Modified-site 18 /note= “Xaa at position 18 is Leu, Thr, Pro, His, Ile or Cys;” Modified-site 22 /note= “Xaa at position 22 is Arg, Tyr, Ser, Thr or Ala;” Modified-site 24 /note= “Xaa at position 24 is Ile, Pro, Tyr or Leu;” Modified-site 27 /note= “Xaa at position 27 is Asp, or Gly;” Modified-site 30 /note= “Xaa at position 30 is Ala, Ile, Leu or Gly;” Modified-site 34 /note= “Xaa at position 34 is Lys or Ser;” Modified-site 36 /note= “Xaa at position 36 is Cys or Ser;” Modified-site 42 /note= “Xaa at position 42 is Cys or Ser;” Modified-site 43 /note= “Xaa at position 43 is His, Thr, Gly, Val, Lys, Trp, Ala, Arg, Cys, or Leu;” Modified-site 44 /note= “Xaa at position 44 is Pro, Gly, Arg, Asp, Val, Ala, His, Trp, Gln, or Thr;” Modified-site 46 /note= “Xaa at position 46 is Glu, Arg, Phe, Arg, Ile or Ala;” Modified-site 47 /note= “Xaa at position 47 is Leu or Thr;” Modified-site 49 /note= “Xaa at position 49 is Leu, Phe, Arg or Ser;” Modified-site 50 /note= “Xaa at position 50 is Leu, Ile, His, Pro or Tyr;” Modified-site 54 /note= “Xaa at position 54 is Leu or His;” Modified-site 64 /note= “Xaa at position 64 is Cys or Ser;” Modified-site 67 /note= “Xaa at position 67 is Gln, Lys, Leu or Cys;” Modified-site 70 /note= “Xaa at position 70 is Gln, Pro, Leu, Arg or Ser;” Modified-site 74 /note= “Xaa at position 74 is Cys or Ser;” Modified-site 104 /note= “Xaa at position 104 is Asp, Gly or Val;” Modified-site 108 /note= “Xaa at position 108 is Leu, Ala, Val, Arg, Trp, Gln or Gly;” Modified-site 115 /note= “Xaa at position 115 is Thr, His, Leu or Ala;” Modified-site 123 /note= “Xaa at position 123 is Glu, Arg, Phe or Thr” Modified-site 144 /note= “Xaa at position 144 is Phe, His, Arg, Pro, Leu, Gln or Glu;” Modified-site 146 /note= “Xaa at position 146 is Arg or Gln;” Modified-site 147 /note= “Xaa at position 147 is Arg or Gln;” Modified-site 156 /note= “Xaa at position 156 is His, Gly or Ser;” Modified-site 159 /note= “Xaa at position 159 is Ser, Arg, Thr, Tyr, Val or Gly;” Modified-site 162 /note= “Xaa at position 162 is Glu, Leu, Gly or Trp;” Modified-site 163 /note= “Xaa at position 163 is Val, Gly, Arg or Ala;” Modified-site 169 /note= “Xaa at position 169 is Arg, Ser, Leu, Arg or Cys;” Modified-site 170 /note= “Xaa at position 170 is His, Arg or Ser;” 1 Xaa Xaa Xaa Gly Pro Ala Ser Ser Leu Pro Gln Ser Xaa Leu Leu Xa 1 5 10 15 Xaa Xaa Glu Gln Val Xaa Lys Xaa Gln Gly Xaa Gly Ala Xaa Leu Gl 20 25 30 Glu Xaa Leu Xaa Ala Thr Tyr Lys Leu Xaa Xaa Xaa Glu Xaa Xaa Va 35 40 45 Xaa Xaa Gly His Ser Xaa Gly Ile Pro Trp Ala Pro Leu Ser Ser Xa 50 55 60 Pro Ser Xaa Ala Leu Xaa Leu Ala Gly Xaa Leu Ser Gln Leu His Se 65 70 75 80 Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Se 85 90 95 Pro Glu Leu Gly Pro Thr Leu Xaa Thr Leu Gln Xaa Asp Val Ala As 100 105 110 Phe Ala Xaa Thr Ile Trp Gln Gln Met Glu Xaa Leu Gly Met Ala Pr 115 120 125 Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Xa 130 135 140 Gln Xaa Xaa Ala Gly Gly Val Leu Val Ala Ser Xaa Leu Gln Xaa Ph 145 150 155 160 Leu Xaa Xaa Ser Tyr Arg Val Leu Xaa Xaa Leu Ala Gln Pro 165 170 133 amino acids amino acid single linear protein Modified-site 17 /note= “Xaa at position 17 is Ser, Lys, Gly, Asp, Met, Gln, or Arg;” Modified-site 18 /note= “Xaa at position 18 is Asn, His, Leu, Ile, Phe, Arg, or Gln;” Modified-site 19 /note= “Xaa at position 19 is Met, Phe, Ile, Arg, Gly, Ala, or Cys;” Modified-site 20 /note= “Xaa at position 20 is Ile, Cys, Gln, Glu, Arg, Pro, or Ala;” Modified-site 21 /note= “Xaa at position 21 is Asp, Phe, Lys, Arg, Ala, Gly, Glu, Gln, Asn, Thr, Ser or Val;” Modified-site 22 /note= “Xaa at position 22 is Glu, Trp, Pro, Ser, Ala, His, Asp, Asn, Gln, Leu, Val or Gly;” Modified-site 23 /note= “Xaa at position 23 is Ile, Val, Ala, Gly, Trp, Lys, Phe, Leu, Ser, or Arg;” Modified-site 24 /note= “Xaa at position 24 is Ile, Gly, Val, Arg, Ser, Phe, Leu;” Modified-site 25 /note= “Xaa at position 25 is Thr, His, Gly, Gln, Arg, Pro, or Ala;” Modified-site 26 /note= “Xaa at position 26 is His, Thr, Phe, Gly, Arg, Ala, Trp;” Modified-site 27 /note= “Xaa at position 27 is Leu, Gly, Arg, Thr, Ser, or Ala;” Modified-site 28 /note= “Xaa at position 28 is Lys, Arg, Leu, Gln, Gly, Pro, Val or Trp;” Modified-site 29 /note= “Xaa at position 29 is Gln, Asn, Leu, Pro, Arg, or Val;” Modified-site 30 /note= “Xaa at position 30 is Pro, His, Thr, Gly, Asp, Gln, Ser, Leu, or L...” Modified-site 31 /note= “Xaa at position 31 is Pro, Asp, Gly, Ala, Arg, Leu, or Gln;” Modified-site 32 /note= “Xaa at position 32 is Leu, Val, Arg, Gln, Asn, Gly, Ala, or Glu;” Modified-site 33 /note= “Xaa at position 33 is Pro, Leu, Gln, Ala, Thr, or Glu;” Modified-site 34 /note= “Xaa at position 34 is Leu, Val, Gly, Ser, Lys, Glu, Gln, Thr, Arg, Ala, Phe, Ile or Met;” Modified-site 35 /note= “Xaa at position 35 is Leu, Ala, Gly, Asn, Pro, Gln, or Val;” Modified-site 36 /note= “Xaa at position 36 is Asp, Leu, or Val;” Modified-site 37 /note= “Xaa at position 37 is Phe, Ser, Pro, Trp, or Ile;” Modified-site 38 /note= “Xaa at position 38 is Asn, or Ala;” Modified-site 40 /note= “Xaa at position 40 is Leu, Trp, or Arg;” Modified-site 41 /note= “Xaa at position 41 is Asn, Cys, Arg, Leu, His, Met, or pro;” Modified-site 42 /note= “Xaa at position 42 is Gly, Asp, Ser, Cys, Asn, Lys, Thr, Leu, Val, Glu, Phe, Tyr, Ile, Met or Ala;” Modified-site 43 /note= “Xaa at position 43 is Glu, Asn, Tyr, Leu, Phe, Asp, Ala, Cys, Gln, Arg, Thr, Gly, or Ser;” Modified-site 44 /note= “Xaa at position 44 is Asp, Ser, Leu, Arg, Lys, Thr, Met, Trp, Glu, Asn, Gln, Ala or Pro;” Modified-site 45 /note= “Xaa at position 45 is Gln, Pro, Phe, Val, Met, Leu, Thr, Lys, Trp, Asp, Asn, Arg, Ser, Ala, Ile, Glu or His;” Modified-site 46 /note= “Xaa at position 46 is Asp, Phe, Ser, Thr, Cys, Glu, Asn, Gln, Lys, His, Ala, Tyr, Ile, Val or Gly;” Modified-site 47 /note= “Xaa at position 47 is Ile, Gly, Val, Ser, Arg, Pro, or His;” Modified-site 48 /note= “Xaa at position 48 is Leu, Ser, Cys, Arg, Ile, His, Phe, Glu, Lys, Thr, Ala, Met, Val or Asn;” Modified-site 49 /note= “Xaa at position 49 is Met, Arg, Ala, Gly, Pro, Asn, His, or Asp;” Modified-site 50 /note= “Xaa at position 50 is Glu, Leu, Thr, Asp, Tyr, Lys, Asn, Ser, Ala, Ile, Val, His, Phe, Met or Gln;” Modified-site 51 /note= “Xaa at position 51 is Asn, Arg, Met, Pro, Ser, Thr, or his;” Modified-site 52 /note= “Xaa at position 52 is Asn, His, Arg, Leu, Gly, Ser, or Thr;” Modified-site 53 /note= “Xaa at position 53 is Leu, Thr, Ala, Gly, Glu, Pro, Lys, Ser, or M...” Modified-site 54 /note= “Xaa at position 54 is Arg, Asp, Ile, Ser, Val, Thr, Gln, Asn, Lys, His, Ala or Leu;” Modified-site 55 /note= “Xaa at position 55 is Arg, Thr, Val, Ser, Leu, or Gly;” Modified-site 56 /note= “Xaa at position 56 is Pro, Gly, Cys, Ser, Gln, Glu, Arg, His, Thr, Ala, Tyr, Phe, Leu, Val or Lys;” Modified-site 57 /note= “Xaa at position 57 is Asn or Gly;” Modified-site 58 /note= “Xaa at position 58 is Leu, Ser, Asp, Arg, Gln, Val, or Cys;” Modified-site 59 /note= “Xaa at position 59 is Glu, Tyr, His, Leu, Pro, or Arg;” Modified-site 60 /note= “Xaa at position 60 is Ala, Ser, Pro, Tyr, Asn, or Thr;” Modified-site 61 /note= “Xaa at position 61 is Phe, Asn, Glu, Pro, Lys, Arg, or Ser;” Modified-site 62 /note= “Xaa at position 62 is Asn, His, Val, Arg, Pro, Thr, Asp, or Ile;” Modified-site 63 /note= “Xaa at position 63 is Arg, Tyr, Trp, Lys, Ser, His, Pro, or Val;” Modified-site 64 /note= “Xaa at position 64 is Ala, Asn, Pro, Ser, or Lys;” Modified-site 65 /note= “Xaa at position 65 is Val, Thr, Pro, His, Leu, Phe, or Ser;” Modified-site 66 /note= “Xaa at position 66 is Lys, Ile, Arg, Val, Asn, Glu, or Ser;” Modified-site 67 /note= “Xaa at postion 67 is Ser, Ala, Phe, Val, Gly, Asn, Ile, Pro, or His;” Modified-site 68 /note= “Xaa at position 68 is Leu, Val, Trp, Ser, Ile, Phe, Thr, or His;” Modified-site 69 /note= “Xaa at position 69 is Gln, Ala, Pro, Thr, Glu, Arg, Trp, Gly, or L...” Modified-site 70 /note= “Xaa at position 70 is Asn, Leu, Val, Trp, pro, or Ala;” Modified-site 71 /note= “Xaa at position 71 is Ala, Met, Leu, Pro, Arg, Glu, Thr, Gln, Trp, or Asn;” Modified-site 72 /note= “Xaa at position 72 is Ser, Glu, Met, Ala, His, Asn, Arg, or Asp;” Modified-site 73 /note= “Xaa at position 73 is Ala, Glu, Asp, Leu, Ser, Gly, Thr, or Arg;” Modified-site 74 /note= “Xaa at position 74 is Ile, Met, Thr, Pro, Arg, Gly, Ala;” Modified-site 75 /note= “Xaa at position 75 is Glu, Lys, Gly, Asp, Pro, Trp, Arg, Ser, Gln, or Leu;” Modified-site 76 /note= “Xaa at position 76 is Ser, Val, Ala, Asn, Trp, Glu, Pro, Gly, or A...” Modified-site 77 /note= “Xaa at position 77 is Ile, Ser, Arg, Thr, or Leu;” Modified-site 78 /note= “Xaa at position 78 is Leu, Ala, Ser, Glu, Phe, Gly, or Arg;” Modified-site 79 /note= “Xaa at position 79 is Lys, Thr, Asn, Met, Arg, Ile, Gly, or Asp;” Modified-site 80 /note= “Xaa position at 80 is Asn, Trp, Val, Gly, Thr, Leu, Glu, or Arg;” Modified-site 81 /note= “Xaa at position 81 is Leu, Gln, Gly, Ala, Trp, Arg, Val, or Lys;” Modified-site 82 /note= “Xaa at position 82 is Leu, Gln, Lys, Trp, Arg, Asp, Glu, Asn, His, Thr, Ser, Ala, Tyr, Phe, Ile, Met or Val;” Modified-site 83 /note= “Xaa at position 83 is Pro, Ala, Thr, Trp, Arg, or Met;” Modified-site 84 /note= “Xaa at position 84 is Cys, Glu, Gly, Arg, Met, or Val;” Modified-site 85 /note= “Xaa at position 85 is Leu, Asn, Val, or Gln;” Modified-site 86 /note= “Xaa at position 86 is Pro, Cys, Arg, Ala, or Lys;” Modified-site 87 /note= “Xaa at position 87 is Leu, Ser, Trp, or Gly;” Modified-site 88 /note= “Xaa at position 88 is Ala, Lys, Arg, Val, or Trp;” Modified-site 89 /note= “Xaa at position 89 is Thr, Asp, Cys, Leu, Val, Glu, His, Asn, or S...” Modified-site 90 /note= “Xaa at position 90 is Ala, Pro, Ser, Thr, Gly, Asp, Ile, or ,Met;” Modified-site 91 /note= “Xaa at position 91 is Ala, Pro, Ser, Thr, Phe, Leu, Asp, or His;” Modified-site 92 /note= “Xaa at position 92 is Pro, Phe, Arg, Ser, Lys, His, Ala, Gly, Ile or Leu;” Modified-site 93 /note= “Xaa at position 93 is Thr, Asp, Ser, Asn, Pro, Ala, Leu, or Arg;” Modified-site 94 /note= “Xaa at position 94 is Arg, Ile, Ser, Glu, Leu, Val, Gln, Lys, His, Ala, or Pro;” Modified-site 95 /note= “Xaa at position 95 is His, Gln, Pro, Arg, Val, Leu, Gly, Thr, Asn, Lys, Ser, Ala, Trp, Phe, Ile, or Tyr;” Modified-site 96 /note= “Xaa at position 96 is Pro, Lys, Tyr, Gly, Ile, or Thr;” Modified-site 97 /note= “Xaa at position 97 is Ile, Val, Lys, Ala, or Asn;” Modified-site 98 /note= “Xaa at position 98 is His, Ile, Asn, Leu, Asp, Ala, Thr, Glu, Gln, Ser, Phe, Met, Val, Lys, Arg, Tyr, or Pro;” Modified-site 99 /note= “Xaa at position 99 is Ile, Leu, Arg, Asp, Val, Pro, Gln, Gly, Ser, Phe, or His;” Modified-site 100 /note= “Xaa at position 100 is Lys, Tyr, Leu, His, Arg, Ile, Ser, Gln, or ...” Modified-site 101 /note= “Xaa at position is Asp, Pro, Met, Lys, His, Thr, Val, Tyr, Glu, Asn, Ser, Ala, Gly, Ile, Leu, or Gln;” Modified-site 102 /note= “Xaa at position 102 is Gly, Leu, Glu, Lys, Ser, Tyr, or Pro;” Modified-site 103 /note= “Xaa at position 103 is Asp, or Ser;” Modified-site 104 /note= “Xaa at position 104 is Trp, Val, Cys, Tyr, Thr, Met, Pro, Leu, Gln, Lys, Ala, Phe, or Gly;” Modified-site 105 /note= “Xaa at position 105 is Asn, Pro, Ala, Phe, Ser, Trp, Gln, Tyr, Leu, Lys, Ile, Asp, or His;” Modified-site 106 /note= “Xaa at position 106 is Glu, Ser, Ala, Lys, Thr, Ile, Gly, or Pro;” Modified-site 108 /note= “Xaa at position 108 is Arg, Lys, Asp, Leu, Thr, Ile, Gln, His, Ser, Ala or Pro;” Modified-site 109 /note= “Xaa at position 109 is Arg, Thr, Pro, Glu, Tyr, Leu, Ser, or Gly;” Modified-site 110 /note= “Xaa at position 110 is Lys, Ala, Asn, Thr, Leu, Arg, Gln, His, Glu, Ser, or Trp;” Modified-site 111 /note= “Xaa at position 111 is Leu, Ile, Arg, Asp, or Met;” Modified-site 112 /note= “Xaa at position 112 is Thr, Val, Gln, Tyr, Glu, His, Ser, or Phe;” Modified-site 113 /note= “Xaa at position 113 is Phe, Ser, Cys, His, Gly, Trp, Tyr, Asp, Lys, Leu, Ile, Val or Asn;” Modified-site 114 /note= “Xaa at position 114 is Tyr, Cys, His, Ser, Trp, Arg, or Leu;” Modified-site 115 /note= “Xaa at position 115 is Leu, Asn, Val, Pro, Arg, Ala, His, Thr, Trp, or Met;” Modified-site 116 /note= “Xaa at position 116 is Lys, Leu, Pro, Thr, Met, Asp, Val, Glu, Arg, Trp, Ser, Asn, His, Ala, Tyr, Phe, Gln, or Ile;” Modified-site 117 /note= “Xaa at position 117 is Thr, Ser, Asn, Ile, Trp, Lys, or Pro;” Modified-site 118 /note= “Xaa at position 118 is Leu, Ser, Pro, Ala, Glu, Cys, Asp, or Tyr;” Modified-site 119 /note= “Xaa at position 119 is Glu, Ser, Lys, Pro, leu, Thr, Tyr, or Arg;” Modified-site 120 /note= “Xaa at position 120 is Asn, Ala, Pro, Leu, His, Val, or Gln;” Modified-site 121 /note= “Xaa at position 121 is Ala, Ser, Ile, Asn, Pro, Lys, Asp, or Gly;” Modified-site 122 /note= “Xaa at position 122 is Gln, Ser, Met, Trp, Arg, Phe, Pro, His, Ile, Tyr, or Cys;” Modified-site 123 /note= “Xaa at position 123 is Ala, Met, Glu, His, Ser, Pro, Tyr, or Leu;” 2 Ala Pro Met Thr Gln Thr Thr Ser Leu Lys Thr Ser Trp Val Asn Cy 1 5 10 15 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xa 20 25 30 Xaa Xaa Xaa Xaa Xaa Xaa Asn Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xa 35 40 45 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xa 50 55 60 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xa 65 70 75 80 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xa 85 90 95 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Phe Xaa Xaa Xaa Xaa Xa 100 105 110 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Gln Gln Thr Thr Le 115 120 125 Ser Leu Ala Ile Phe 130 332 amino acids amino acid unknown unknown protein Modified-site 112 /note= “position 112 is deleted or Leu, Ala, Val, Ile, Pro, Phe, Trp, or M...” Modified-site 113 /note= “position 113 is deleted or Pro, Phe, Ala, Leu, Ile, Trp, or Met” Modified-site 114 /note= “position 114 is deleted or Pro, Phe, Ala, Val, Leu, Ile, Trp or Met” Modified-site 115 /note= “position 115 is deleted or Gln, Gly, Ser, Thr, Tyr or Asn” 3 Ser Pro Ala Pro Pro Ala Cys Asp Leu Arg Val Leu Ser Lys Leu Le 1 5 10 15 Arg Asp Ser His Val Leu His Ser Arg Leu Ser Gln Cys Pro Glu Va 20 25 30 His Pro Leu Pro Thr Pro Val Leu Leu Pro Ala Val Asp Phe Ser Le 35 40 45 Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln Asp Ile Le 50 55 60 Gly Ala Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Arg Gly Gl 65 70 75 80 Leu Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gly Gl 85 90 95 Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Thr Gln Xa 100 105 110 Xaa Xaa Xaa Gly Arg Thr Thr Ala His Lys Asp Pro Asn Ala Ile Ph 115 120 125 Leu Ser Phe Gln His Leu Leu Arg Gly Lys Val Arg Phe Leu Met Le 130 135 140 Val Gly Gly Ser Thr Leu Cys Val Arg Arg Ala Pro Pro Thr Thr Al 145 150 155 160 Val Pro Ser Arg Thr Ser Leu Val Leu Thr Leu Asn Glu Leu Pro As 165 170 175 Arg Thr Ser Gly Leu Leu Glu Thr Asn Phe Thr Ala Ser Ala Arg Th 180 185 190 Thr Gly Ser Gly Leu Leu Lys Trp Gln Gln Gly Phe Arg Ala Lys Il 195 200 205 Pro Gly Leu Leu Asn Gln Thr Ser Arg Ser Leu Asp Gln Ile Pro Gl 210 215 220 Tyr Leu Asn Arg Ile His Glu Leu Leu Asn Gly Thr Arg Gly Leu Ph 225 230 235 240 Pro Gly Pro Ser Arg Arg Thr Leu Gly Ala Pro Asp Ile Ser Ser Gl 245 250 255 Thr Ser Asp Thr Gly Ser Leu Pro Pro Asn Leu Gln Pro Gly Tyr Se 260 265 270 Pro Ser Pro Thr His Pro Pro Thr Gly Gln Tyr Thr Leu Phe Pro Le 275 280 285 Pro Pro Thr Leu Pro Thr Pro Val Val Gln Leu His Pro Leu Leu Pr 290 295 300 Asp Pro Ser Ala Pro Thr Pro Thr Pro Thr Ser Pro Leu Leu Asn Th 305 310 315 320 Ser Tyr Thr His Ser Gln Asn Leu Ser Gln Glu Gly 325 330 5 base pairs nucleic acid unknown unknown peptide 4 GYSRN 5 3 amino acids amino acid unknown unknown peptide Peptide 1 /note= “where x=(glyglyglyglyser)n and where n is an interger” 5 Xaa Ala Ala 1 3 amino acids amino acid unknown unknown peptide Peptide 1 Peptide 1 /note= “where Xaa =(glyglyglyglyglyser)n and where n is an integer” 6 Xaa Ala Ala 1 3 amino acids amino acid unknown unknown peptide Peptide 1 /note= “where xaa = (gly(n)ser)m and where n is an integer and m is an int...” 7 Xaa Ala Ala 1 3 amino acids amino acid unknown unknown peptide Peptide 1 /note= “where Xaa=(alaglyser)n and where n is an integer” 8 Xaa Ala Ala 1 36 amino acids amino acid unknown linear protein 9 Gly Gly Gly Ser Gly Gly Gly Ser Gly Gly Gly Ser Glu Gly Gly Gl 1 5 10 15 Ser Glu Gly Gly Gly Ser Glu Gly Gly Gly Ser Glu Gly Gly Gly Se 20 25 30 Gly Gly Gly Ser 35 24 amino acids amino acid unknown unknown peptide 10 Ile Ser Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pr 1 5 10 15 Ser Lys Glu Ser His Lys Ser Pro 20 28 amino acids amino acid unknown unknown peptide 11 Ile Glu Gly Arg Ile Ser Glu Pro Ser Gly Pro Ile Ser Thr Ile As 1 5 10 15 Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro 20 25 4 amino acids amino acid unknown unknown peptide 12 Gly Gly Gly Ser 1 45 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 13 ACGTCCATGG CNTCNCCNGC NCCNCCTGCT TGTGCACTCC GAGTC 45 30 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 14 ATGCACGAAT TCCCTGACGC AGAGGGTGGA 30 33 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 15 TGACAAGCTT ACCTGACGCA GAGGGTGGAC CCT 33 10 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 16 AATTCGGCAA 10 10 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 17 CATGTTGCCG 10 13 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 18 AATTCGGCGG CAA 13 13 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 19 CATGTTGCCG CCG 13 22 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 20 AATTCGGCGG CAACGGCGGC AA 22 22 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 21 CATGTTGCCG CCGTTGCCGC CG 22 27 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 22 CGATCCATGG AGGTTCACCC TTTGCCT 27 29 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 23 GATCAAGCTT ATGGGCACTG GCTCAGTCT 29 27 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 24 CGATACATGT TGCCTACACC TGTCCTG 27 29 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 25 GATCAAGCTT AAGGGTGAAC CTCTGGGCA 29 27 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 26 CGATCCATGG TCCTGCTGCC TGCTGTG 27 29 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 27 GATCAAGCTT AAGGTGTAGG CAAAGGGTG 29 30 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 28 CGATCCATGG CTGTGGACTT TAGCTTGGGA 30 29 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 29 GATCAAGCTT AAGGCAGCAG GACAGGTGT 29 27 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 30 CGATCCATGG ACTTTAGCTT GGGAGAA 27 29 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 31 GATCAAGCTT ACACAGCAGG CAGCAGGAC 29 27 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 32 CGATCCATGG GAGAATGGAA AACCCAG 27 29 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 33 GATCAAGCTT ACAAGCTAAA GTCCACAGC 29 27 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 34 CGATCCATGG GACCCACTTG CCTCTCA 27 29 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 35 GATCAAGCTT ACAGTTGTCC CCGTGCTGC 29 27 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 36 CAGTCCATGG GAACCCAGCT TCCTCCA 27 29 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 37 GATCAAGCTT AAAGGAGGCT CTGCAGGGC 29 27 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 38 CGATCCATGG GCAGGACCAC AGCTCAC 27 30 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 39 GATCAAGCTT ACTGTGGAGG AAGCTGGGTT 30 30 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 40 CGATCCATGG CTCACAAGGA TCCCAATGCC 30 29 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 41 GATCAAGCTT ATGTGGTCCT GCGCTGTGG 29 30 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 42 CGATCCATGG ATCCCAATGC CATCTTCCTG 30 29 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 43 GATCAAGCTT ACTTGTGAGC TGTGGTCCT 29 30 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 44 CGATCCATGG CCATCTTCCT GAGCTTCCAA 30 32 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 45 GATCAAGCTT AATTGGGATC CTTGTGAGCT GT 32 83 base pairs nucleic acid unknown unknown other nucleic acid /desc = “SYNTHETIC” 46 AATTCCGTCG TAAACTGACC TTCTATCTGA AAACCTTGGA GAACGCGCAG GCTCAACAGT 60 ACGTAGAGGG CGGTGGAGGC TCC 83 83 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 47 CCGGGGAGCC TCCACCGCCC TCTACGTACT GTTGAGCCTG CGCGTTCTCC AAGGTTTTCA 60 GATAGAAGGT CAGTTTACGA CGG 83 59 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 48 GTTACCCTTG AGCAAGCGCA GGAACAACAG GGTGGTGGCT CTAACTGCTC TATAATGAT 59 56 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 49 CGATCATTAT AGAGCAGTTA GAGCCACCAC CCTGTTGTTC CTGCGCTTGC TCAAGG 56 80 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 50 GTTACCCTTG AGCAAGCGCA GGAACAACAG GGTGGTGGCT CTGGCGGTGG CAGCGGCGGC 60 GGTTCTAACT GCTCTATAAT 80 80 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 51 CGATCATTAT AGAGCAGTTA GAACCGCCGC CGCTGCCACC GCCAGAGCCA CCACCCTGTT 60 GTTCCTGCGC TTGCTCAAGG 80 30 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 52 GATCGACCAT GGCTCTGGAC CCGAACAACC 30 28 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 53 CTCGATTACG TACAAAGGTG CAGGTGGT 28 32 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 54 GATCGACCAT GGCTAATGCA TCAGGTATTG AG 32 28 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 55 CTCGATTACG TATTCTAAGT TCTTGACA 28 32 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 56 GATCGACCAT GGCTGCACCC TCTCGACATC CA 32 28 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 57 CTCGATTACG TAGGCCGTGG CAGAGGGC 28 32 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 58 GATCGACCAT GGCTGCAGGT GACTGGCAAG AA 32 28 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 59 CTCGATTACG TACTTGATGA TGATTGGA 28 54 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 60 GCTCTGAGAG CCGCCAGAGC CGCCAGAGGG CTGCGCAAGG TGGCGTAGAA CGCG 54 54 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 61 CAGCCCTCTG GCGGCTCTGG CGGCTCTCAG AGCTTCCTGC TCAAGTCTTT AGAG 54 18 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 62 GGGCTGCGCA AGGTGGCG 18 21 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 63 ACACCATTGG GCCCTGCCAG C 21 32 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 64 GATCGACCAT GGCTTACAAG CTGTGCCACC CC 32 36 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 65 CGATCGAAGC TTATTAGGTG GCACACAGCT TCTCCT 36 32 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 66 GATCGACCAT GGCTCCCGAG TTGGGTCCCA CC 32 36 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 67 CGATCGAAGC TTATTAGGAT ATCCCTTCCA GGGCCT 36 32 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 68 GATCGACCAT GGCTATGGCC CCTGCCCTGC AG 32 36 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 69 CGATCGAAGC TTATTATCCC AGTTCTTCCA TCTGCT 36 32 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 70 GATCGACCAT GGCTACCCAG GGTGCCATGC CG 32 36 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 71 CGATCGAAGC TTATTAGGGC TGCAGGGCAG GGGCCA 36 36 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 72 CGATCGAAGC TTATTAGGGC TGCAGGGCAG GGGCCA 36 36 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 73 CGATCGAAGC TTATTAGGCG AAGGCCGGCA TGGCAC 36 21 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 74 GTAGAGGGCG GTGGAGGCTC C 21 25 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 75 CCGGGGAGCC TCCACCGCCC TCTAC 25 53 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 76 TTCTACGCCA CCTTGCGCAG CCCGGCGGCG GCTCTGACAT GTCTACACCA TTG 53 53 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 77 CAATGGTGTA GACATGTCAG AGCCGCCGCC GGGCTGCGCA AGGTGGCGTA GAA 53 439 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 78 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGT 439 465 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 79 TCCCCAGCTC CACCTGCTTG TGACCTCCGA GTCCTCAGTA AACTGCTTCG TGACTCCCAT 60 GTCCTTCACA GCAGACTGAG CCAGTGCCCA GAGGTTCACC CTTTGCCTAC ACCTGTCCT 120 CTGCCTGCTG TGGACTTTAG CTTGGGAGAA TGGAAAACCC AGATGGAGGA GACCAAGGC 180 CAGGACATTC TGGGAGCAGT GACCCTTCTG CTGGAGGGAG TGATGGCAGC ACGGGGACA 240 CTGGGACCCA CTTGCCTCTC ATCCCTCCTG GGGCAGCTTT CTGGACAGGT CCGTCTCCT 300 CTTGGGGCCC TGCAGAGCCT CCTTGGAACC CAGCTTCCTC CACAGGGCAG GACCACAGC 360 CACAAGGATC CCAATGCCAT CTTCCTGAGC TTCCAACACC TGCTCCGAGG AAAGGTGCG 420 TTCCTGATGC TTGTAGGAGG GTCCACCCTC TGCGTCAGGG AATTC 465 927 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 80 TCCCCAGCTC CACCTGCTTG TGACCTCCGA GTCCTCAGTA AACTGCTTCG TGACTCCCAT 60 GTCCTTCACA GCAGACTGAG CCAGTGCCCA GAGGTTCACC CTTTGCCTAC ACCTGTCCT 120 CTGCCTGCTG TGGACTTTAG CTTGGGAGAA TGGAAAACCC AGATGGAGGA GACCAAGGC 180 CAGGACATTC TGGGAGCAGT GACCCTTCTG CTGGAGGGAG TGATGGCAGC ACGGGGACA 240 CTGGGACCCA CTTGCCTCTC ATCCCTCCTG GGGCAGCTTT CTGGACAGGT CCGTCTCCT 300 CTTGGGGCCC TGCAGAGCCT CCTTGGAACC CAGCTTCCTC CACAGGGCAG GACCACAGC 360 CACAAGGATC CCAATGCCAT CTTCCTGAGC TTCCAACACC TGCTCCGAGG AAAGGTGCG 420 TTCCTGATGC TTGTAGGAGG GTCCACCCTC TGCGTCAGGG AATTCGGCGG CAACATGGC 480 TCTCCCGCTC CGCCTGCTTG TGACCTCCGA GTCCTCAGTA AACTGCTTCG TGACTCCCA 540 GTCCTTCACA GCAGACTGAG CCAGTGCCCA GAGGTTCACC CTTTGCCTAC ACCTGTCCT 600 CTGCCTGCTG TGGACTTTAG CTTGGGAGAA TGGAAAACCC AGATGGAGGA GACCAAGGC 660 CAGGACATTC TGGGAGCAGT GACCCTTCTG CTGGAGGGAG TGATGGCAGC ACGGGGACA 720 CTGGGACCCA CTTGCCTCTC ATCCCTCCTG GGGCAGCTTT CTGGACAGGT CCGTCTCCT 780 CTTGGGGCCC TGCAGAGCCT CCTTGGAACC CAGGGCAGGA CCACAGCTCA CAAGGATCC 840 AATGCCATCT TCCTGAGCTT CCAACACCTG CTCCGAGGAA AGGTGCGTTT CCTGATGCT 900 GTAGGAGGGT CCACCCTCTG CGTCAGG 927 936 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 81 TCCCCAGCTC CACCTGCTTG TGACCTCCGA GTCCTCAGTA AACTGCTTCG TGACTCCCAT 60 GTCCTTCACA GCAGACTGAG CCAGTGCCCA GAGGTTCACC CTTTGCCTAC ACCTGTCCT 120 CTGCCTGCTG TGGACTTTAG CTTGGGAGAA TGGAAAACCC AGATGGAGGA GACCAAGGC 180 CAGGACATTC TGGGAGCAGT GACCCTTCTG CTGGAGGGAG TGATGGCAGC ACGGGGACA 240 CTGGGACCCA CTTGCCTCTC ATCCCTCCTG GGGCAGCTTT CTGGACAGGT CCGTCTCCT 300 CTTGGGGCCC TGCAGAGCCT CCTTGGAACC CAGCTTCCTC CACAGGGCAG GACCACAGC 360 CACAAGGATC CCAATGCCAT CTTCCTGAGC TTCCAACACC TGCTCCGAGG AAAGGTGCG 420 TTCCTGATGC TTGTAGGAGG GTCCACCCTC TGCGTCAGGG AATTCGGCAA CATGGCGTC 480 CCCGCTCCGC CTGCTTGTGA CCTCCGAGTC CTCAGTAAAC TGCTTCGTGA CTCCCATGT 540 CTTCACAGCA GACTGAGCCA GTGCCCAGAG GTTCACCCTT TGCCTACACC TGTCCTGCT 600 CCTGCTGTGG ACTTTAGCTT GGGAGAATGG AAAACCCAGA TGGAGGAGAC CAAGGCACA 660 GACATTCTGG GAGCAGTGAC CCTTCTGCTG GAGGGAGTGA TGGCAGCACG GGGACAACT 720 GGACCCACTT GCCTCTCATC CCTCCTGGGG CAGCTTTCTG GACAGGTCCG TCTCCTCCT 780 GGGGCCCTGC AGAGCCTCCT TGGAACCCAG CTTCCTCCAC AGGGCAGGAC CACAGCTCA 840 AAGGATCCCA ATGCCATCTT CCTGAGCTTC CAACACCTGC TCCGAGGAAA GGTGCGTTT 900 CTGATGCTTG TAGGAGGGTC CACCCTCTGC GTCAGG 936 939 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 82 TCCCCAGCTC CACCTGCTTG TGACCTCCGA GTCCTCAGTA AACTGCTTCG TGACTCCCAT 60 GTCCTTCACA GCAGACTGAG CCAGTGCCCA GAGGTTCACC CTTTGCCTAC ACCTGTCCT 120 CTGCCTGCTG TGGACTTTAG CTTGGGAGAA TGGAAAACCC AGATGGAGGA GACCAAGGC 180 CAGGACATTC TGGGAGCAGT GACCCTTCTG CTGGAGGGAG TGATGGCAGC ACGGGGACA 240 CTGGGACCCA CTTGCCTCTC ATCCCTCCTG GGGCAGCTTT CTGGACAGGT CCGTCTCCT 300 CTTGGGGCCC TGCAGAGCCT CCTTGGAACC CAGCTTCCTC CACAGGGCAG GACCACAGC 360 CACAAGGATC CCAATGCCAT CTTCCTGAGC TTCCAACACC TGCTCCGAGG AAAGGTGCG 420 TTCCTGATGC TTGTAGGAGG GTCCACCCTC TGCGTCAGGG AATTCGGCGG CAACATGGC 480 TCTCCCGCTC CGCCTGCTTG TGACCTCCGA GTCCTCAGTA AACTGCTTCG TGACTCCCA 540 GTCCTTCACA GCAGACTGAG CCAGTGCCCA GAGGTTCACC CTTTGCCTAC ACCTGTCCT 600 CTGCCTGCTG TGGACTTTAG CTTGGGAGAA TGGAAAACCC AGATGGAGGA GACCAAGGC 660 CAGGACATTC TGGGAGCAGT GACCCTTCTG CTGGAGGGAG TGATGGCAGC ACGGGGACA 720 CTGGGACCCA CTTGCCTCTC ATCCCTCCTG GGGCAGCTTT CTGGACAGGT CCGTCTCCT 780 CTTGGGGCCC TGCAGAGCCT CCTTGGAACC CAGCTTCCTC CACAGGGCAG GACCACAGC 840 CACAAGGATC CCAATGCCAT CTTCCTGAGC TTCCAACACC TGCTCCGAGG AAAGGTGCG 900 TTCCTGATGC TTGTAGGAGG GTCCACCCTC TGCGTCAGG 939 948 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 83 TCCCCAGCGC CGCCTGCTTG TGACCTCCGA GTCCTCAGTA AACTGCTTCG TGACTCCCAT 60 GTCCTTCACA GCAGACTGAG CCAGTGCCCA GAGGTTCACC CTTTGCCTAC ACCTGTCCT 120 CTGCCTGCTG TGGACTTTAG CTTGGGAGAA TGGAAAACCC AGATGGAGGA GACCAAGGC 180 CAGGACATTC TGGGAGCAGT GACCCTTCTG CTGGAGGGAG TGATGGCAGC ACGGGGACA 240 CTGGGACCCA CTTGCCTCTC ATCCCTCCTG GGGCAGCTTT CTGGACAGGT CCGTCTCCT 300 CTTGGGGCCC TGCAGAGCCT CCTTGGAACC CAGCTTCCTC CACAGGGCAG GACCACAGC 360 CACAAGGATC CCAATGCCAT CTTCCTGAGC TTCCAACACC TGCTCCGAGG AAAGGTGCG 420 TTCCTGATGC TTGTAGGAGG GTCCACCCTC TGCGTCAGGG AATTCGGCGG CAACGGCGG 480 AACATGGCGT CCCCAGCGCC GCCTGCTTGT GACCTCCGAG TCCTCAGTAA ACTGCTTCG 540 GACTCCCATG TCCTTCACAG CAGACTGAGC CAGTGCCCAG AGGTTCACCC TTTGCCTAC 600 CCTGTCCTGC TGCCTGCTGT GGACTTTAGC TTGGGAGAAT GGAAAACCCA GATGGAGGA 660 ACCAAGGCAC AGGACATTCT GGGAGCAGTG ACCCTTCTGC TGGAGGGAGT GATGGCAGC 720 CGGGGACAAC TGGGACCCAC TTGCCTCTCA TCCCTCCTGG GGCAGCTTTC TGGACAGGT 780 CGTCTCCTCC TTGGGGCCCT GCAGAGCCTC CTTGGAACCC AGCTTCCTCC ACAGGGCAG 840 ACCACAGCTC ACAAGGATCC CAATGCCATC TTCCTGAGCT TCCAACACCT GCTCCGAGG 900 AAGGTGCGTT TCCTGATGCT TGTAGGAGGG TCCACCCTCT GCGTCAGG 948 688 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 84 CATGGCTAAC TGCTCTATAA TGATCGATGA AATTATACAT CACTTAAAGA GACCACCTGC 60 ACCTTTGCTG GACCCGAACA ACCTCAATGA CGAAGACGTC TCTATCCTGA TGGACCGAA 120 CCTTCGACTT CCAAACCTGG AGAGCTTCGT AAGGGCTGTC AAGAACTTAG AAAATGCAT 180 AGGTATTGAG GCAATTCTTC GTAATCTCCA ACCATGTCTG CCCTCTGCCA CGGCCGCAC 240 CTCTCGACAT CCAATCATCA TCAAGGCAGG TGACTGGCAA GAATTCCGGG AAAAACTGA 300 GTTCTATCTG GTTACCCTTG AGCAAGCGCA GGAACAACAG GGTGGTGGCT CTAACTGCT 360 TATAATGATC GATGAAATTA TACATCACTT AAAGAGACCA CCTGCACCTT TGCTGGACC 420 GAACAACCTC AATGACGAAG ACGTCTCTAT CCTGATGGAC CGAAACCTTC GACTTCCAA 480 CCTGGAGAGC TTCGTAAGGG CTGTCAAGAA CTTAGAAAAT GCATCAGGTA TTGAGGCAA 540 TCTTCGTAAT CTCCAACCAT GTCTGCCCTC TGCCACGGCC GCACCCTCTC GACATCCAA 600 CATCATCAAG GCAGGTGACT GGCAAGAATT CCGGGAAAAA CTGACGTTCT ATCTGGTTA 660 CCTTGAGCAA GCGCAGGAAC AACAGTAC 688 712 base pairs nucleic acid unknown unknown other nucleic acid /desc = “SYNTHETIC” 85 CATGGCTAAC TGCTCTATAA TGATCGATGA AATTATACAT CACTTAAAGA GACCACCTGC 60 ACCTTTGCTG GACCCGAACA ACCTCAATGA CGAAGACGTC TCTATCCTGA TGGACCGAA 120 CCTTCGACTT CCAAACCTGG AGAGCTTCGT AAGGGCTGTC AAGAACTTAG AAAATGCAT 180 AGGTATTGAG GCAATTCTTC GTAATCTCCA ACCATGTCTG CCCTCTGCCA CGGCCGCAC 240 CTCTCGACAT CCAATCATCA TCAAGGCAGG TGACTGGCAA GAATTCCGGG AAAAACTGA 300 GTTCTATCTG GTTACCCTTG AGCAAGCGCA GGAACAACAG GGTGGTGGCT CTGGCGGTG 360 CAGCGGCGGC GGTTCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGA 420 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGA 480 GGACCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAG 540 AAATGCATCA GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCA 600 GGCCGCACCC TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGG 660 AAAACTGACG TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT AC 712 975 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 86 ATGGCTCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGACCGAAAC 60 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 120 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 180 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 240 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGG GTGGTGGCTC TAACTGCTC 300 ATAATGATCG ATGAAATTAT ACATCACTTA AAGAGACCAC CTGCACCTTT GTACGTAGA 360 GGCGGTGGAG GCTCCCCGGG TGAACCGTCT GGTCCAATCT CTACTATCAA CCCGTCTCC 420 CCGTCTAAAG AATCTCATAA ATCTCCAAAC ATGGCTACCC AGGGTGCCAT GCCGGCCTT 480 GCCTCTGCTT TCCAGCGCCG GGCAGGAGGG GTCCTGGTTG CTAGCCATCT GCAGAGCTT 540 CTGGAGGTGT CGTACCGCGT TCTACGCCAC CTTGCGCAGC CCTCTGGCGG CTCTGGCGG 600 TCTCAGAGCT TCCTGCTCAA GTCTTTAGAG CAAGTGAGAA AGATCCAGGG CGATGGCGC 660 GCGCTCCAGG AGAAGCTGTG TGCCACCTAC AAGCTGTGCC ACCCCGAGGA GCTGGTGCT 720 CTCGGACACT CTCTGGGCAT CCCCTGGGCT CCCCTGAGCT CCTGCCCCAG CCAGGCCCT 780 CAGCTGGCAG GCTGCTTGAG CCAACTCCAT AGCGGCCTTT TCCTCTACCA GGGGCTCCT 840 CAGGCCCTGG AAGGGATATC CCCCGAGTTG GGTCCCACCT TGGACACACT GCAGCTGGA 900 GTCGCCGACT TTGCCACCAC CATCTGGCAG CAGATGGAAG AACTGGGAAT GGCCCCTGC 960 CTGCAGCCCT AATAA 975 975 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 87 ATGGCTCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGACCGAAAC 60 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 120 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 180 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 240 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGG GTGGTGGCTC TAACTGCTC 300 ATAATGATCG ATGAAATTAT ACATCACTTA AAGAGACCAC CTGCACCTTT GTACGTAGA 360 GGCGGTGGAG GCTCCCCGGG TGAACCGTCT GGTCCAATCT CTACTATCAA CCCGTCTCC 420 CCGTCTAAAG AATCTCATAA ATCTCCAAAC ATGGCTACCC AGGGTGCCAT GCCGGCCTT 480 GCCTCTGCTT TCCAGCGCCG GGCAGGAGGG GTCCTGGTTG CTAGCCATCT GCAGAGCTT 540 CTGGAGGTGT CGTACCGCGT TCTACGCCAC CTTGCGCAGC CCTCTGGCGG CTCTGGCGG 600 TCTCAGAGCT TCCTGCTCAA GTCTTTAGAG CAAGTGAGAA AGATCCAGGG CGATGGCGC 660 GCGCTCCAGG AGAAGCTGTG TGCCACCTAC AAGCTGTGCC ACCCCGAGGA GCTGGTGCT 720 CTCGGACACT CTCTGGGCAT CCCCTGGGCT CCCCTGAGCT CCTGCCCCAG CCAGGCCCT 780 CAGCTGGCAG GCTGCTTGAG CCAACTCCAT AGCGGCCTTT TCCTCTACCA GGGGCTCCT 840 CAGGCCCTGG AAGGGATATC CCCCGAGTTG GGTCCCACCT TGGACACACT GCAGCTGGA 900 GTCGCCGACT TTGCCACCAC CATCTGGCAG CAGATGGAAG AACTGGGAAT GGCCCCTGC 960 CTGCAGCCCT AATAA 975 975 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 88 ATGGCTGCAC CCTCTCGACA TCCAATCATC ATCAAGGCAG GTGACTGGCA AGAATTCCGG 60 GAAAAACTGA CGTTCTATCT GGTTACCCTT GAGCAAGCGC AGGAACAACA GGGTGGTGG 120 TCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACC 180 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 240 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 300 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CTACGTAGA 360 GGCGGTGGAG GCTCCCCGGG TGAACCGTCT GGTCCAATCT CTACTATCAA CCCGTCTCC 420 CCGTCTAAAG AATCTCATAA ATCTCCAAAC ATGGCTACCC AGGGTGCCAT GCCGGCCTT 480 GCCTCTGCTT TCCAGCGCCG GGCAGGAGGG GTCCTGGTTG CTAGCCATCT GCAGAGCTT 540 CTGGAGGTGT CGTACCGCGT TCTACGCCAC CTTGCGCAGC CCTCTGGCGG CTCTGGCGG 600 TCTCAGAGCT TCCTGCTCAA GTCTTTAGAG CAAGTGAGAA AGATCCAGGG CGATGGCGC 660 GCGCTCCAGG AGAAGCTGTG TGCCACCTAC AAGCTGTGCC ACCCCGAGGA GCTGGTGCT 720 CTCGGACACT CTCTGGGCAT CCCCTGGGCT CCCCTGAGCT CCTGCCCCAG CCAGGCCCT 780 CAGCTGGCAG GCTGCTTGAG CCAACTCCAT AGCGGCCTTT TCCTCTACCA GGGGCTCCT 840 CAGGCCCTGG AAGGGATATC CCCCGAGTTG GGTCCCACCT TGGACACACT GCAGCTGGA 900 GTCGCCGACT TTGCCACCAC CATCTGGCAG CAGATGGAAG AACTGGGAAT GGCCCCTGC 960 CTGCAGCCCT AATAA 975 975 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 89 ATGGCTGCAG GTGACTGGCA AGAATTCCGG GAAAAACTGA CGTTCTATCT GGTTACCCTT 60 GAGCAAGCGC AGGAACAACA GGGTGGTGGC TCTAACTGCT CTATAATGAT CGATGAAAT 120 ATACATCACT TAAAGAGACC ACCTGCACCT TTGCTGGACC CGAACAACCT CAATGACGA 180 GACGTCTCTA TCCTGATGGA CCGAAACCTT CGACTTCCAA ACCTGGAGAG CTTCGTAAG 240 GCTGTCAAGA ACTTAGAAAA TGCATCAGGT ATTGAGGCAA TTCTTCGTAA TCTCCAACC 300 TGTCTGCCCT CTGCCACGGC CGCACCCTCT CGACATCCAA TCATCATCAA GTACGTAGA 360 GGCGGTGGAG GCTCCCCGGG TGAACCGTCT GGTCCAATCT CTACTATCAA CCCGTCTCC 420 CCGTCTAAAG AATCTCATAA ATCTCCAAAC ATGGCTACCC AGGGTGCCAT GCCGGCCTT 480 GCCTCTGCTT TCCAGCGCCG GGCAGGAGGG GTCCTGGTTG CTAGCCATCT GCAGAGCTT 540 CTGGAGGTGT CGTACCGCGT TCTACGCCAC CTTGCGCAGC CCTCTGGCGG CTCTGGCGG 600 TCTCAGAGCT TCCTGCTCAA GTCTTTAGAG CAAGTGAGAA AGATCCAGGG CGATGGCGC 660 GCGCTCCAGG AGAAGCTGTG TGCCACCTAC AAGCTGTGCC ACCCCGAGGA GCTGGTGCT 720 CTCGGACACT CTCTGGGCAT CCCCTGGGCT CCCCTGAGCT CCTGCCCCAG CCAGGCCCT 780 CAGCTGGCAG GCTGCTTGAG CCAACTCCAT AGCGGCCTTT TCCTCTACCA GGGGCTCCT 840 CAGGCCCTGG AAGGGATATC CCCCGAGTTG GGTCCCACCT TGGACACACT GCAGCTGGA 900 GTCGCCGACT TTGCCACCAC CATCTGGCAG CAGATGGAAG AACTGGGAAT GGCCCCTGC 960 CTGCAGCCCT AATAA 975 999 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 90 ATGGCTCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGACCGAAAC 60 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 120 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 180 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 240 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGG GTGGTGGCTC TGGCGGTGG 300 AGCGGCGGCG GTTCTAACTG CTCTATAATG ATCGATGAAA TTATACATCA CTTAAAGAG 360 CCACCTGCAC CTTTGTACGT AGAGGGCGGT GGAGGCTCCC CGGGTGAACC GTCTGGTCC 420 ATCTCTACTA TCAACCCGTC TCCTCCGTCT AAAGAATCTC ATAAATCTCC AAACATGGC 480 ACCCAGGGTG CCATGCCGGC CTTCGCCTCT GCTTTCCAGC GCCGGGCAGG AGGGGTCCT 540 GTTGCTAGCC ATCTGCAGAG CTTCCTGGAG GTGTCGTACC GCGTTCTACG CCACCTTGC 600 CAGCCCTCTG GCGGCTCTGG CGGCTCTCAG AGCTTCCTGC TCAAGTCTTT AGAGCAAGT 660 AGAAAGATCC AGGGCGATGG CGCAGCGCTC CAGGAGAAGC TGTGTGCCAC CTACAAGCT 720 TGCCACCCCG AGGAGCTGGT GCTGCTCGGA CACTCTCTGG GCATCCCCTG GGCTCCCCT 780 AGCTCCTGCC CCAGCCAGGC CCTGCAGCTG GCAGGCTGCT TGAGCCAACT CCATAGCGG 840 CTTTTCCTCT ACCAGGGGCT CCTGCAGGCC CTGGAAGGGA TATCCCCCGA GTTGGGTCC 900 ACCTTGGACA CACTGCAGCT GGACGTCGCC GACTTTGCCA CCACCATCTG GCAGCAGAT 960 GAAGAACTGG GAATGGCCCC TGCCCTGCAG CCCTAATAA 999 999 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 91 ATGGCTAATG CATCAGGTAT TGAGGCAATT CTTCGTAATC TCCAACCATG TCTGCCCTCT 60 GCCACGGCCG CACCCTCTCG ACATCCAATC ATCATCAAGG CAGGTGACTG GCAAGAATT 120 CGGGAAAAAC TGACGTTCTA TCTGGTTACC CTTGAGCAAG CGCAGGAACA ACAGGGTGG 180 GGCTCTGGCG GTGGCAGCGG CGGCGGTTCT AACTGCTCTA TAATGATCGA TGAAATTAT 240 CATCACTTAA AGAGACCACC TGCACCTTTG CTGGACCCGA ACAACCTCAA TGACGAAGA 300 GTCTCTATCC TGATGGACCG AAACCTTCGA CTTCCAAACC TGGAGAGCTT CGTAAGGGC 360 GTCAAGAACT TAGAATACGT AGAGGGCGGT GGAGGCTCCC CGGGTGAACC GTCTGGTCC 420 ATCTCTACTA TCAACCCGTC TCCTCCGTCT AAAGAATCTC ATAAATCTCC AAACATGGC 480 ACCCAGGGTG CCATGCCGGC CTTCGCCTCT GCTTTCCAGC GCCGGGCAGG AGGGGTCCT 540 GTTGCTAGCC ATCTGCAGAG CTTCCTGGAG GTGTCGTACC GCGTTCTACG CCACCTTGC 600 CAGCCCTCTG GCGGCTCTGG CGGCTCTCAG AGCTTCCTGC TCAAGTCTTT AGAGCAAGT 660 AGAAAGATCC AGGGCGATGG CGCAGCGCTC CAGGAGAAGC TGTGTGCCAC CTACAAGCT 720 TGCCACCCCG AGGAGCTGGT GCTGCTCGGA CACTCTCTGG GCATCCCCTG GGCTCCCCT 780 AGCTCCTGCC CCAGCCAGGC CCTGCAGCTG GCAGGCTGCT TGAGCCAACT CCATAGCGG 840 CTTTTCCTCT ACCAGGGGCT CCTGCAGGCC CTGGAAGGGA TATCCCCCGA GTTGGGTCC 900 ACCTTGGACA CACTGCAGCT GGACGTCGCC GACTTTGCCA CCACCATCTG GCAGCAGAT 960 GAAGAACTGG GAATGGCCCC TGCCCTGCAG CCCTAATAA 999 999 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 92 ATGGCTGCAC CCTCTCGACA TCCAATCATC ATCAAGGCAG GTGACTGGCA AGAATTCCGG 60 GAAAAACTGA CGTTCTATCT GGTTACCCTT GAGCAAGCGC AGGAACAACA GGGTGGTGG 120 TCTGGCGGTG GCAGCGGCGG CGGTTCTAAC TGCTCTATAA TGATCGATGA AATTATACA 180 CACTTAAAGA GACCACCTGC ACCTTTGCTG GACCCGAACA ACCTCAATGA CGAAGACGT 240 TCTATCCTGA TGGACCGAAA CCTTCGACTT CCAAACCTGG AGAGCTTCGT AAGGGCTGT 300 AAGAACTTAG AAAATGCATC AGGTATTGAG GCAATTCTTC GTAATCTCCA ACCATGTCT 360 CCCTCTGCCA CGGCCTACGT AGAGGGCGGT GGAGGCTCCC CGGGTGAACC GTCTGGTCC 420 ATCTCTACTA TCAACCCGTC TCCTCCGTCT AAAGAATCTC ATAAATCTCC AAACATGGC 480 ACCCAGGGTG CCATGCCGGC CTTCGCCTCT GCTTTCCAGC GCCGGGCAGG AGGGGTCCT 540 GTTGCTAGCC ATCTGCAGAG CTTCCTGGAG GTGTCGTACC GCGTTCTACG CCACCTTGC 600 CAGCCCTCTG GCGGCTCTGG CGGCTCTCAG AGCTTCCTGC TCAAGTCTTT AGAGCAAGT 660 AGAAAGATCC AGGGCGATGG CGCAGCGCTC CAGGAGAAGC TGTGTGCCAC CTACAAGCT 720 TGCCACCCCG AGGAGCTGGT GCTGCTCGGA CACTCTCTGG GCATCCCCTG GGCTCCCCT 780 AGCTCCTGCC CCAGCCAGGC CCTGCAGCTG GCAGGCTGCT TGAGCCAACT CCATAGCGG 840 CTTTTCCTCT ACCAGGGGCT CCTGCAGGCC CTGGAAGGGA TATCCCCCGA GTTGGGTCC 900 ACCTTGGACA CACTGCAGCT GGACGTCGCC GACTTTGCCA CCACCATCTG GCAGCAGAT 960 GAAGAACTGG GAATGGCCCC TGCCCTGCAG CCCTAATAA 999 999 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 93 ATGGCTGCAG GTGACTGGCA AGAATTCCGG GAAAAACTGA CGTTCTATCT GGTTACCCTT 60 GAGCAAGCGC AGGAACAACA GGGTGGTGGC TCTGGCGGTG GCAGCGGCGG CGGTTCTAA 120 TGCTCTATAA TGATCGATGA AATTATACAT CACTTAAAGA GACCACCTGC ACCTTTGCT 180 GACCCGAACA ACCTCAATGA CGAAGACGTC TCTATCCTGA TGGACCGAAA CCTTCGACT 240 CCAAACCTGG AGAGCTTCGT AAGGGCTGTC AAGAACTTAG AAAATGCATC AGGTATTGA 300 GCAATTCTTC GTAATCTCCA ACCATGTCTG CCCTCTGCCA CGGCCGCACC CTCTCGACA 360 CCAATCATCA TCAAGTACGT AGAGGGCGGT GGAGGCTCCC CGGGTGAACC GTCTGGTCC 420 ATCTCTACTA TCAACCCGTC TCCTCCGTCT AAAGAATCTC ATAAATCTCC AAACATGGC 480 ACCCAGGGTG CCATGCCGGC CTTCGCCTCT GCTTTCCAGC GCCGGGCAGG AGGGGTCCT 540 GTTGCTAGCC ATCTGCAGAG CTTCCTGGAG GTGTCGTACC GCGTTCTACG CCACCTTGC 600 CAGCCCTCTG GCGGCTCTGG CGGCTCTCAG AGCTTCCTGC TCAAGTCTTT AGAGCAAGT 660 AGAAAGATCC AGGGCGATGG CGCAGCGCTC CAGGAGAAGC TGTGTGCCAC CTACAAGCT 720 TGCCACCCCG AGGAGCTGGT GCTGCTCGGA CACTCTCTGG GCATCCCCTG GGCTCCCCT 780 AGCTCCTGCC CCAGCCAGGC CCTGCAGCTG GCAGGCTGCT TGAGCCAACT CCATAGCGG 840 CTTTTCCTCT ACCAGGGGCT CCTGCAGGCC CTGGAAGGGA TATCCCCCGA GTTGGGTCC 900 ACCTTGGACA CACTGCAGCT GGACGTCGCC GACTTTGCCA CCACCATCTG GCAGCAGAT 960 GAAGAACTGG GAATGGCCCC TGCCCTGCAG CCCTAATAA 999 918 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 94 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGACCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG GTGGTTCTGG CGGCGGCTCC AACATGGCTT ACAAGCTGTG CCACCCCGA 420 GAGCTGGTGC TGCTCGGACA CTCTCTGGGC ATCCCCTGGG CTCCCCTGAG CTCCTGCCC 480 AGCCAGGCCC TGCAGCTGGC AGGCTGCTTG AGCCAACTCC ATAGCGGCCT TTTCCTCTA 540 CAGGGGCTCC TGCAGGCCCT GGAAGGGATA TCCCCCGAGT TGGGTCCCAC CTTGGACAC 600 CTGCAGCTGG ACGTCGCCGA CTTTGCCACC ACCATCTGGC AGCAGATGGA AGAACTGGG 660 ATGGCCCCTG CCCTGCAGCC CACCCAGGGT GCCATGCCGG CCTTCGCCTC TGCTTTCCA 720 CGCCGGGCAG GAGGGGTCCT GGTTGCTAGC CATCTGCAGA GCTTCCTGGA GGTGTCGTA 780 CGCGTTCTAC GCCACCTTGC GCAGCCCTCT GGCGGCTCTG GCGGCTCTCA GAGCTTCCT 840 CTCAAGTCTT TAGAGCAAGT GAGAAAGATC CAGGGCGATG GCGCAGCGCT CCAGGAGAA 900 CTGTGTGCCA CCTAATAA 918 963 base pa irs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 95 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGACCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC CGTCTCCTCC GTCTAAAGA 420 TCTCATAAAT CTCCAAACAT GGCTTACAAG CTGTGCCACC CCGAGGAGCT GGTGCTGCT 480 GGACACTCTC TGGGCATCCC CTGGGCTCCC CTGAGCTCCT GCCCCAGCCA GGCCCTGCA 540 CTGGCAGGCT GCTTGAGCCA ACTCCATAGC GGCCTTTTCC TCTACCAGGG GCTCCTGCA 600 GCCCTGGAAG GGATATCCCC CGAGTTGGGT CCCACCTTGG ACACACTGCA GCTGGACGT 660 GCCGACTTTG CCACCACCAT CTGGCAGCAG ATGGAAGAAC TGGGAATGGC CCCTGCCCT 720 CAGCCCACCC AGGGTGCCAT GCCGGCCTTC GCCTCTGCTT TCCAGCGCCG GGCAGGAGG 780 GTCCTGGTTG CTAGCCATCT GCAGAGCTTC CTGGAGGTGT CGTACCGCGT TCTACGCCA 840 CTTGCGCAGC CCTCTGGCGG CTCTGGCGGC TCTCAGAGCT TCCTGCTCAA GTCTTTAGA 900 CAAGTGAGAA AGATCCAGGG CGATGGCGCA GCGCTCCAGG AGAAGCTGTG TGCCACCTA 960 TAA 963 918 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 96 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGACCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG GTGGTTCTGG CGGCGGCTCC AACATGGCTC CCGAGTTGGG TCCCACCTT 420 GACACACTGC AGCTGGACGT CGCCGACTTT GCCACCACCA TCTGGCAGCA GATGGAAGA 480 CTGGGAATGG CCCCTGCCCT GCAGCCCACC CAGGGTGCCA TGCCGGCCTT CGCCTCTGC 540 TTCCAGCGCC GGGCAGGAGG GGTCCTGGTT GCTAGCCATC TGCAGAGCTT CCTGGAGGT 600 TCGTACCGCG TTCTACGCCA CCTTGCGCAG CCCTCTGGCG GCTCTGGCGG CTCTCAGAG 660 TTCCTGCTCA AGTCTTTAGA GCAAGTGAGA AAGATCCAGG GCGATGGCGC AGCGCTCCA 720 GAGAAGCTGT GTGCCACCTA CAAGCTGTGC CACCCCGAGG AGCTGGTGCT GCTCGGACA 780 TCTCTGGGCA TCCCCTGGGC TCCCCTGAGC TCCTGCCCCA GCCAGGCCCT GCAGCTGGC 840 GGCTGCTTGA GCCAACTCCA TAGCGGCCTT TTCCTCTACC AGGGGCTCCT GCAGGCCCT 900 GAAGGGATAT CCTAATAA 918 963 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 97 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGACCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC CGTCTCCTCC GTCTAAAGA 420 TCTCATAAAT CTCCAAACAT GGCTCCCGAG TTGGGTCCCA CCTTGGACAC ACTGCAGCT 480 GACGTCGCCG ACTTTGCCAC CACCATCTGG CAGCAGATGG AAGAACTGGG AATGGCCCC 540 GCCCTGCAGC CCACCCAGGG TGCCATGCCG GCCTTCGCCT CTGCTTTCCA GCGCCGGGC 600 GGAGGGGTCC TGGTTGCTAG CCATCTGCAG AGCTTCCTGG AGGTGTCGTA CCGCGTTCT 660 CGCCACCTTG CGCAGCCCTC TGGCGGCTCT GGCGGCTCTC AGAGCTTCCT GCTCAAGTC 720 TTAGAGCAAG TGAGAAAGAT CCAGGGCGAT GGCGCAGCGC TCCAGGAGAA GCTGTGTGC 780 ACCTACAAGC TGTGCCACCC CGAGGAGCTG GTGCTGCTCG GACACTCTCT GGGCATCCC 840 TGGGCTCCCC TGAGCTCCTG CCCCAGCCAG GCCCTGCAGC TGGCAGGCTG CTTGAGCCA 900 CTCCATAGCG GCCTTTTCCT CTACCAGGGG CTCCTGCAGG CCCTGGAAGG GATATCCTA 960 TAA 963 918 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 98 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGACCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG GTGGTTCTGG CGGCGGCTCC AACATGGCTA TGGCCCCTGC CCTGCAGCC 420 ACCCAGGGTG CCATGCCGGC CTTCGCCTCT GCTTTCCAGC GCCGGGCAGG AGGGGTCCT 480 GTTGCTAGCC ATCTGCAGAG CTTCCTGGAG GTGTCGTACC GCGTTCTACG CCACCTTGC 540 CAGCCCTCTG GCGGCTCTGG CGGCTCTCAG AGCTTCCTGC TCAAGTCTTT AGAGCAAGT 600 AGAAAGATCC AGGGCGATGG CGCAGCGCTC CAGGAGAAGC TGTGTGCCAC CTACAAGCT 660 TGCCACCCCG AGGAGCTGGT GCTGCTCGGA CACTCTCTGG GCATCCCCTG GGCTCCCCT 720 AGCTCCTGCC CCAGCCAGGC CCTGCAGCTG GCAGGCTGCT TGAGCCAACT CCATAGCGG 780 CTTTTCCTCT ACCAGGGGCT CCTGCAGGCC CTGGAAGGGA TATCCCCCGA GTTGGGTCC 840 ACCTTGGACA CACTGCAGCT GGACGTCGCC GACTTTGCCA CCACCATCTG GCAGCAGAT 900 GAAGAACTGG GATAATAA 918 963 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 99 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGACCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC CGTCTCCTCC GTCTAAAGA 420 TCTCATAAAT CTCCAAACAT GGCTATGGCC CCTGCCCTGC AGCCCACCCA GGGTGCCAT 480 CCGGCCTTCG CCTCTGCTTT CCAGCGCCGG GCAGGAGGGG TCCTGGTTGC TAGCCATCT 540 CAGAGCTTCC TGGAGGTGTC GTACCGCGTT CTACGCCACC TTGCGCAGCC CTCTGGCGG 600 TCTGGCGGCT CTCAGAGCTT CCTGCTCAAG TCTTTAGAGC AAGTGAGAAA GATCCAGGG 660 GATGGCGCAG CGCTCCAGGA GAAGCTGTGT GCCACCTACA AGCTGTGCCA CCCCGAGGA 720 CTGGTGCTGC TCGGACACTC TCTGGGCATC CCCTGGGCTC CCCTGAGCTC CTGCCCCAG 780 CAGGCCCTGC AGCTGGCAGG CTGCTTGAGC CAACTCCATA GCGGCCTTTT CCTCTACCA 840 GGGCTCCTGC AGGCCCTGGA AGGGATATCC CCCGAGTTGG GTCCCACCTT GGACACACT 900 CAGCTGGACG TCGCCGACTT TGCCACCACC ATCTGGCAGC AGATGGAAGA ACTGGGATA 960 TAA 963 918 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 100 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGACCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG GTGGTTCTGG CGGCGGCTCC AACATGGCTA CCCAGGGTGC CATGCCGGC 420 TTCGCCTCTG CTTTCCAGCG CCGGGCAGGA GGGGTCCTGG TTGCTAGCCA TCTGCAGAG 480 TTCCTGGAGG TGTCGTACCG CGTTCTACGC CACCTTGCGC AGCCCTCTGG CGGCTCTGG 540 GGCTCTCAGA GCTTCCTGCT CAAGTCTTTA GAGCAAGTGA GAAAGATCCA GGGCGATGG 600 GCAGCGCTCC AGGAGAAGCT GTGTGCCACC TACAAGCTGT GCCACCCCGA GGAGCTGGT 660 CTGCTCGGAC ACTCTCTGGG CATCCCCTGG GCTCCCCTGA GCTCCTGCCC CAGCCAGGC 720 CTGCAGCTGG CAGGCTGCTT GAGCCAACTC CATAGCGGCC TTTTCCTCTA CCAGGGGCT 780 CTGCAGGCCC TGGAAGGGAT ATCCCCCGAG TTGGGTCCCA CCTTGGACAC ACTGCAGCT 840 GACGTCGCCG ACTTTGCCAC CACCATCTGG CAGCAGATGG AAGAACTGGG AATGGCCCC 900 GCCCTGCAGC CCTAATAA 918 963 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 101 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGACCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC CGTCTCCTCC GTCTAAAGA 420 TCTCATAAAT CTCCAAACAT GGCTACCCAG GGTGCCATGC CGGCCTTCGC CTCTGCTTT 480 CAGCGCCGGG CAGGAGGGGT CCTGGTTGCT AGCCATCTGC AGAGCTTCCT GGAGGTGTC 540 TACCGCGTTC TACGCCACCT TGCGCAGCCC TCTGGCGGCT CTGGCGGCTC TCAGAGCTT 600 CTGCTCAAGT CTTTAGAGCA AGTGAGAAAG ATCCAGGGCG ATGGCGCAGC GCTCCAGGA 660 AAGCTGTGTG CCACCTACAA GCTGTGCCAC CCCGAGGAGC TGGTGCTGCT CGGACACTC 720 CTGGGCATCC CCTGGGCTCC CCTGAGCTCC TGCCCCAGCC AGGCCCTGCA GCTGGCAGG 780 TGCTTGAGCC AACTCCATAG CGGCCTTTTC CTCTACCAGG GGCTCCTGCA GGCCCTGGA 840 GGGATATCCC CCGAGTTGGG TCCCACCTTG GACACACTGC AGCTGGACGT CGCCGACTT 900 GCCACCACCA TCTGGCAGCA GATGGAAGAA CTGGGAATGG CCCCTGCCCT GCAGCCCTA 960 TAA 963 918 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 102 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGACCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG GTGGTTCTGG CGGCGGCTCC AACATGGCTT CTGCTTTCCA GCGCCGGGC 420 GGAGGGGTCC TGGTTGCTAG CCATCTGCAG AGCTTCCTGG AGGTGTCGTA CCGCGTTCT 480 CGCCACCTTG CGCAGCCCTC TGGCGGCTCT GGCGGCTCTC AGAGCTTCCT GCTCAAGTC 540 TTAGAGCAAG TGAGAAAGAT CCAGGGCGAT GGCGCAGCGC TCCAGGAGAA GCTGTGTGC 600 ACCTACAAGC TGTGCCACCC CGAGGAGCTG GTGCTGCTCG GACACTCTCT GGGCATCCC 660 TGGGCTCCCC TGAGCTCCTG CCCCAGCCAG GCCCTGCAGC TGGCAGGCTG CTTGAGCCA 720 CTCCATAGCG GCCTTTTCCT CTACCAGGGG CTCCTGCAGG CCCTGGAAGG GATATCCCC 780 GAGTTGGGTC CCACCTTGGA CACACTGCAG CTGGACGTCG CCGACTTTGC CACCACCAT 840 TGGCAGCAGA TGGAAGAACT GGGAATGGCC CCTGCCCTGC AGCCCACCCA GGGTGCCAT 900 CCGGCCTTCG CCTAATAA 918 963 base pairs nucleic acid unknown unknown other nucleic acid /desc = “SYNTHETIC” 103 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGACCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC CGTCTCCTCC GTCTAAAGA 420 TCTCATAAAT CTCCAAACAT GGCTTCTGCT TTCCAGCGCC GGGCAGGAGG GGTCCTGGT 480 GCTAGCCATC TGCAGAGCTT CCTGGAGGTG TCGTACCGCG TTCTACGCCA CCTTGCGCA 540 CCCTCTGGCG GCTCTGGCGG CTCTCAGAGC TTCCTGCTCA AGTCTTTAGA GCAAGTGAG 600 AAGATCCAGG GCGATGGCGC AGCGCTCCAG GAGAAGCTGT GTGCCACCTA CAAGCTGTG 660 CACCCCGAGG AGCTGGTGCT GCTCGGACAC TCTCTGGGCA TCCCCTGGGC TCCCCTGAG 720 TCCTGCCCCA GCCAGGCCCT GCAGCTGGCA GGCTGCTTGA GCCAACTCCA TAGCGGCCT 780 TTCCTCTACC AGGGGCTCCT GCAGGCCCTG GAAGGGATAT CCCCCGAGTT GGGTCCCAC 840 TTGGACACAC TGCAGCTGGA CGTCGCCGAC TTTGCCACCA CCATCTGGCA GCAGATGGA 900 GAACTGGGAA TGGCCCCTGC CCTGCAGCCC ACCCAGGGTG CCATGCCGGC CTTCGCCTA 960 TAA 963 927 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 104 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGACCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG GTGGTTCTGG CGGCGGCTCC AACATGGCTT ACAAGCTGTG CCACCCCGA 420 GAGCTGGTGC TGCTCGGACA CTCTCTGGGC ATCCCCTGGG CTCCCCTGAG CTCCTGCCC 480 AGCCAGGCCC TGCAGCTGGC AGGCTGCTTG AGCCAACTCC ATAGCGGCCT TTTCCTCTA 540 CAGGGGCTCC TGCAGGCCCT GGAAGGGATA TCCCCCGAGT TGGGTCCCAC CTTGGACAC 600 CTGCAGCTGG ACGTCGCCGA CTTTGCCACC ACCATCTGGC AGCAGATGGA AGAACTGGG 660 ATGGCCCCTG CCCTGCAGCC CACCCAGGGT GCCATGCCGG CCTTCGCCTC TGCTTTCCA 720 CGCCGGGCAG GAGGGGTCCT GGTTGCTAGC CATCTGCAGA GCTTCCTGGA GGTGTCGTA 780 CGCGTTCTAC GCCACCTTGC GCAGCCCACA CCATTGGGCC CTGCCAGCTC CCTGCCCCA 840 AGCTTCCTGC TCAAGTCTTT AGAGCAAGTG AGAAAGATCC AGGGCGATGG CGCAGCGCT 900 CAGGAGAAGC TGTGTGCCAC CTAATAA 927 972 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 105 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGACCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC CGTCTCCTCC GTCTAAAGA 420 TCTCATAAAT CTCCAAACAT GGCTTACAAG CTGTGCCACC CCGAGGAGCT GGTGCTGCT 480 GGACACTCTC TGGGCATCCC CTGGGCTCCC CTGAGCTCCT GCCCCAGCCA GGCCCTGCA 540 CTGGCAGGCT GCTTGAGCCA ACTCCATAGC GGCCTTTTCC TCTACCAGGG GCTCCTGCA 600 GCCCTGGAAG GGATATCCCC CGAGTTGGGT CCCACCTTGG ACACACTGCA GCTGGACGT 660 GCCGACTTTG CCACCACCAT CTGGCAGCAG ATGGAAGAAC TGGGAATGGC CCCTGCCCT 720 CAGCCCACCC AGGGTGCCAT GCCGGCCTTC GCCTCTGCTT TCCAGCGCCG GGCAGGAGG 780 GTCCTGGTTG CTAGCCATCT GCAGAGCTTC CTGGAGGTGT CGTACCGCGT TCTACGCCA 840 CTTGCGCAGC CCACACCATT GGGCCCTGCC AGCTCCCTGC CCCAGAGCTT CCTGCTCAA 900 TCTTTAGAGC AAGTGAGAAA GATCCAGGGC GATGGCGCAG CGCTCCAGGA GAAGCTGTG 960 GCCACCTAAT AA 972 927 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 106 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGACCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG GTGGTTCTGG CGGCGGCTCC AACATGGCTC CCGAGTTGGG TCCCACCTT 420 GACACACTGC AGCTGGACGT CGCCGACTTT GCCACCACCA TCTGGCAGCA GATGGAAGA 480 CTGGGAATGG CCCCTGCCCT GCAGCCCACC CAGGGTGCCA TGCCGGCCTT CGCCTCTGC 540 TTCCAGCGCC GGGCAGGAGG GGTCCTGGTT GCTAGCCATC TGCAGAGCTT CCTGGAGGT 600 TCGTACCGCG TTCTACGCCA CCTTGCGCAG CCCACACCAT TGGGCCCTGC CAGCTCCCT 660 CCCCAGAGCT TCCTGCTCAA GTCTTTAGAG CAAGTGAGAA AGATCCAGGG CGATGGCGC 720 GCGCTCCAGG AGAAGCTGTG TGCCACCTAC AAGCTGTGCC ACCCCGAGGA GCTGGTGCT 780 CTCGGACACT CTCTGGGCAT CCCCTGGGCT CCCCTGAGCT CCTGCCCCAG CCAGGCCCT 840 CAGCTGGCAG GCTGCTTGAG CCAACTCCAT AGCGGCCTTT TCCTCTACCA GGGGCTCCT 900 CAGGCCCTGG AAGGGATATC CTAATAA 927 972 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 107 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGACCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC CGTCTCCTCC GTCTAAAGA 420 TCTCATAAAT CTCCAAACAT GGCTCCCGAG TTGGGTCCCA CCTTGGACAC ACTGCAGCT 480 GACGTCGCCG ACTTTGCCAC CACCATCTGG CAGCAGATGG AAGAACTGGG AATGGCCCC 540 GCCCTGCAGC CCACCCAGGG TGCCATGCCG GCCTTCGCCT CTGCTTTCCA GCGCCGGGC 600 GGAGGGGTCC TGGTTGCTAG CCATCTGCAG AGCTTCCTGG AGGTGTCGTA CCGCGTTCT 660 CGCCACCTTG CGCAGCCCAC ACCATTGGGC CCTGCCAGCT CCCTGCCCCA GAGCTTCCT 720 CTCAAGTCTT TAGAGCAAGT GAGAAAGATC CAGGGCGATG GCGCAGCGCT CCAGGAGAA 780 CTGTGTGCCA CCTACAAGCT GTGCCACCCC GAGGAGCTGG TGCTGCTCGG ACACTCTCT 840 GGCATCCCCT GGGCTCCCCT GAGCTCCTGC CCCAGCCAGG CCCTGCAGCT GGCAGGCTG 900 TTGAGCCAAC TCCATAGCGG CCTTTTCCTC TACCAGGGGC TCCTGCAGGC CCTGGAAGG 960 ATATCCTAAT AA 972 927 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 108 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGACCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG GTGGTTCTGG CGGCGGCTCC AACATGGCTA TGGCCCCTGC CCTGCAGCC 420 ACCCAGGGTG CCATGCCGGC CTTCGCCTCT GCTTTCCAGC GCCGGGCAGG AGGGGTCCT 480 GTTGCTAGCC ATCTGCAGAG CTTCCTGGAG GTGTCGTACC GCGTTCTACG CCACCTTGC 540 CAGCCCACAC CATTGGGCCC TGCCAGCTCC CTGCCCCAGA GCTTCCTGCT CAAGTCTTT 600 GAGCAAGTGA GAAAGATCCA GGGCGATGGC GCAGCGCTCC AGGAGAAGCT GTGTGCCAC 660 TACAAGCTGT GCCACCCCGA GGAGCTGGTG CTGCTCGGAC ACTCTCTGGG CATCCCCTG 720 GCTCCCCTGA GCTCCTGCCC CAGCCAGGCC CTGCAGCTGG CAGGCTGCTT GAGCCAACT 780 CATAGCGGCC TTTTCCTCTA CCAGGGGCTC CTGCAGGCCC TGGAAGGGAT ATCCCCCGA 840 TTGGGTCCCA CCTTGGACAC ACTGCAGCTG GACGTCGCCG ACTTTGCCAC CACCATCTG 900 CAGCAGATGG AAGAACTGGG ATAATAA 927 972 base pairs nucleic acid single linear other nucleic acid /desc = “DNA (synthetic)” 109 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGACCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC CGTCTCCTCC GTCTAAAGA 420 TCTCATAAAT CTCCAAACAT GGCTATGGCC CCTGCCCTGC AGCCCACCCA GGGTGCCAT 480 CCGGCCTTCG CCTCTGCTTT CCAGCGCCGG GCAGGAGGGG TCCTGGTTGC TAGCCATCT 540 CAGAGCTTCC TGGAGGTGTC GTACCGCGTT CTACGCCACC TTGCGCAGCC CACACCATT 600 GGCCCTGCCA GCTCCCTGCC CCAGAGCTTC CTGCTCAAGT CTTTAGAGCA AGTGAGAAA 660 ATCCAGGGCG ATGGCGCAGC GCTCCAGGAG AAGCTGTGTG CCACCTACAA GCTGTGCCA 720 CCCGAGGAGC TGGTGCTGCT CGGACACTCT CTGGGCATCC CCTGGGCTCC CCTGAGCTC 780 TGCCCCAGCC AGGCCCTGCA GCTGGCAGGC TGCTTGAGCC AACTCCATAG CGGCCTTTT 840 CTCTACCAGG GGCTCCTGCA GGCCCTGGAA GGGATATCCC CCGAGTTGGG TCCCACCTT 900 GACACACTGC AGCTGGACGT CGCCGACTTT GCCACCACCA TCTGGCAGCA GATGGAAGA 960 CTGGGATAAT AA 972 927 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 110 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGACCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG GTGGTTCTGG CGGCGGCTCC AACATGGCTA CCCAGGGTGC CATGCCGGC 420 TTCGCCTCTG CTTTCCAGCG CCGGGCAGGA GGGGTCCTGG TTGCTAGCCA TCTGCAGAG 480 TTCCTGGAGG TGTCGTACCG CGTTCTACGC CACCTTGCGC AGCCCACACC ATTGGGCCC 540 GCCAGCTCCC TGCCCCAGAG CTTCCTGCTC AAGTCTTTAG AGCAAGTGAG AAAGATCCA 600 GGCGATGGCG CAGCGCTCCA GGAGAAGCTG TGTGCCACCT ACAAGCTGTG CCACCCCGA 660 GAGCTGGTGC TGCTCGGACA CTCTCTGGGC ATCCCCTGGG CTCCCCTGAG CTCCTGCCC 720 AGCCAGGCCC TGCAGCTGGC AGGCTGCTTG AGCCAACTCC ATAGCGGCCT TTTCCTCTA 780 CAGGGGCTCC TGCAGGCCCT GGAAGGGATA TCCCCCGAGT TGGGTCCCAC CTTGGACAC 840 CTGCAGCTGG ACGTCGCCGA CTTTGCCACC ACCATCTGGC AGCAGATGGA AGAACTGGG 900 ATGGCCCCTG CCCTGCAGCC CTAATAA 927 972 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 111 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGACCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC CGTCTCCTCC GTCTAAAGA 420 TCTCATAAAT CTCCAAACAT GGCTACCCAG GGTGCCATGC CGGCCTTCGC CTCTGCTTT 480 CAGCGCCGGG CAGGAGGGGT CCTGGTTGCT AGCCATCTGC AGAGCTTCCT GGAGGTGTC 540 TACCGCGTTC TACGCCACCT TGCGCAGCCC ACACCATTGG GCCCTGCCAG CTCCCTGCC 600 CAGAGCTTCC TGCTCAAGTC TTTAGAGCAA GTGAGAAAGA TCCAGGGCGA TGGCGCAGC 660 CTCCAGGAGA AGCTGTGTGC CACCTACAAG CTGTGCCACC CCGAGGAGCT GGTGCTGCT 720 GGACACTCTC TGGGCATCCC CTGGGCTCCC CTGAGCTCCT GCCCCAGCCA GGCCCTGCA 780 CTGGCAGGCT GCTTGAGCCA ACTCCATAGC GGCCTTTTCC TCTACCAGGG GCTCCTGCA 840 GCCCTGGAAG GGATATCCCC CGAGTTGGGT CCCACCTTGG ACACACTGCA GCTGGACGT 900 GCCGACTTTG CCACCACCAT CTGGCAGCAG ATGGAAGAAC TGGGAATGGC CCCTGCCCT 960 CAGCCCTAAT AA 972 927 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 112 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGACCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG GTGGTTCTGG CGGCGGCTCC AACATGGCTT CTGCTTTCCA GCGCCGGGC 420 GGAGGGGTCC TGGTTGCTAG CCATCTGCAG AGCTTCCTGG AGGTGTCGTA CCGCGTTCT 480 CGCCACCTTG CGCAGCCCAC ACCATTGGGC CCTGCCAGCT CCCTGCCCCA GAGCTTCCT 540 CTCAAGTCTT TAGAGCAAGT GAGAAAGATC CAGGGCGATG GCGCAGCGCT CCAGGAGAA 600 CTGTGTGCCA CCTACAAGCT GTGCCACCCC GAGGAGCTGG TGCTGCTCGG ACACTCTCT 660 GGCATCCCCT GGGCTCCCCT GAGCTCCTGC CCCAGCCAGG CCCTGCAGCT GGCAGGCTG 720 TTGAGCCAAC TCCATAGCGG CCTTTTCCTC TACCAGGGGC TCCTGCAGGC CCTGGAAGG 780 ATATCCCCCG AGTTGGGTCC CACCTTGGAC ACACTGCAGC TGGACGTCGC CGACTTTGC 840 ACCACCATCT GGCAGCAGAT GGAAGAACTG GGAATGGCCC CTGCCCTGCA GCCCACCCA 900 GGTGCCATGC CGGCCTTCGC CTAATAA 927 972 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 113 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGACCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC CGTCTCCTCC GTCTAAAGA 420 TCTCATAAAT CTCCAAACAT GGCTTCTGCT TTCCAGCGCC GGGCAGGAGG GGTCCTGGT 480 GCTAGCCATC TGCAGAGCTT CCTGGAGGTG TCGTACCGCG TTCTACGCCA CCTTGCGCA 540 CCCACACCAT TGGGCCCTGC CAGCTCCCTG CCCCAGAGCT TCCTGCTCAA GTCTTTAGA 600 CAAGTGAGAA AGATCCAGGG CGATGGCGCA GCGCTCCAGG AGAAGCTGTG TGCCACCTA 660 AAGCTGTGCC ACCCCGAGGA GCTGGTGCTG CTCGGACACT CTCTGGGCAT CCCCTGGGC 720 CCCCTGAGCT CCTGCCCCAG CCAGGCCCTG CAGCTGGCAG GCTGCTTGAG CCAACTCCA 780 AGCGGCCTTT TCCTCTACCA GGGGCTCCTG CAGGCCCTGG AAGGGATATC CCCCGAGTT 840 GGTCCCACCT TGGACACACT GCAGCTGGAC GTCGCCGACT TTGCCACCAC CATCTGGCA 900 CAGATGGAAG AACTGGGAAT GGCCCCTGCC CTGCAGCCCA CCCAGGGTGC CATGCCGGC 960 TTCGCCTAAT AA 972 963 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 114 ATGGCTAACT GCTCTAACAT GATCGATGAA ATCATCACCC ACCTGAAGCA GCCACCGCTG 60 CCGCTGCTGG ACTTCAACAA CCTCAATGGT GAAGACCAAG ATATCCTAAT GGACAATAA 120 CTTCGTCGTC CAAACCTCGA GGCATTCAAC CGTGCTGTCA AGTCTCTGCA GAATGCATC 180 GCAATTGAGA GCATTCTTAA AAATCTCCTG CCATGTCTGC CGCTAGCCAC GGCCGCACC 240 ACGCGACATC CAATCCATAT CAAGGACGGT GACTGGAATG AATTCCGTCG TAAACTGAC 300 TTCTATCTGA AAACCTTGGA GAACGCGCAG GCTCAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC CGTCTCCTCC GTCTAAAGA 420 TCTCATAAAT CTCCAAACAT GGCTACCCAG GGTGCCATGC CGGCCTTCGC CTCTGCTTT 480 CAGCGCCGGG CAGGAGGGGT CCTGGTTGCT AGCCATCTGC AGAGCTTCCT GGAGGTGTC 540 TACCGCGTTC TACGCCACCT TGCGCAGCCC TCTGGCGGCT CTGGCGGCTC TCAGAGCTT 600 CTGCTCAAGT CTTTAGAGCA AGTGAGAAAG ATCCAGGGCG ATGGCGCAGC GCTCCAGGA 660 AAGCTGTGTG CCACCTACAA GCTGTGCCAC CCCGAGGAGC TGGTGCTGCT CGGACACTC 720 CTGGGCATCC CCTGGGCTCC CCTGAGCTCC TGCCCCAGCC AGGCCCTGCA GCTGGCAGG 780 TGCTTGAGCC AACTCCATAG CGGCCTTTTC CTCTACCAGG GGCTCCTGCA GGCCCTGGA 840 GGGATATCCC CCGAGTTGGG TCCCACCTTG GACACACTGC AGCTGGACGT CGCCGACTT 900 GCCACCACCA TCTGGCAGCA GATGGAAGAA CTGGGAATGG CCCCTGCCCT GCAGCCCTA 960 TAA 963 972 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 115 ATGGCTAACT GCTCTAACAT GATCGATGAA ATCATCACCC ACCTGAAGCA GCCACCGCTG 60 CCGCTGCTGG ACTTCAACAA CCTCAATGGT GAAGACCAAG ATATCCTGAT GGAAAATAA 120 CTTCGTCGTC CAAACCTCGA GGCATTCAAC CGTGCTGTCA AGTCTCTGCA GAATGCATC 180 GCAATTGAGA GCATTCTTAA AAATCTCCTG CCATGTCTGC CCCTGGCCAC GGCCGCACC 240 ACGCGACATC CAATCATCAT CCGTGACGGT GACTGGAATG AATTCCGTCG TAAACTGAC 300 TTCTATCTGA AAACCTTGGA GAACGCGCAG GCTCAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC CGTCTCCTCC GTCTAAAGA 420 TCTCATAAAT CTCCAAACAT GGCTACCCAG GGTGCCATGC CGGCCTTCGC CTCTGCTTT 480 CAGCGCCGGG CAGGAGGGGT CCTGGTTGCT AGCCATCTGC AGAGCTTCCT GGAGGTGTC 540 TACCGCGTTC TACGCCACCT TGCGCAGCCC ACACCATTGG GCCCTGCCAG CTCCCTGCC 600 CAGAGCTTCC TGCTCAAGTC TTTAGAGCAA GTGAGAAAGA TCCAGGGCGA TGGCGCAGC 660 CTCCAGGAGA AGCTGTGTGC CACCTACAAG CTGTGCCACC CCGAGGAGCT GGTGCTGCT 720 GGACACTCTC TGGGCATCCC CTGGGCTCCC CTGAGCTCCT GCCCCAGCCA GGCCCTGCA 780 CTGGCAGGCT GCTTGAGCCA ACTCCATAGC GGCCTTTTCC TCTACCAGGG GCTCCTGCA 840 GCCCTGGAAG GGATATCCCC CGAGTTGGGT CCCACCTTGG ACACACTGCA GCTGGACGT 900 GCCGACTTTG CCACCACCAT CTGGCAGCAG ATGGAAGAAC TGGGAATGGC CCCTGCCCT 960 CAGCCCTAAT AA 972 963 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 116 ATGGCTAACT GCTCTAACAT GATCGATGAA ATCATCACCC ACCTGAAGCA GCCACCGCTG 60 CCGCTGCTGG ACTTCAACAA CCTCAATGGT GAAGACCAAG ATATCCTGAT GGAAAATAA 120 CTTCGTCGTC CAAACCTCGA GGCATTCAAC CGTGCTGTCA AGTCTCTGCA GAATGCATC 180 GCAATTGAGA GCATTCTTAA AAATCTCCTG CCATGTCTGC CCCTGGCCAC GGCCGCACC 240 ACGCGACATC CAATCATCAT CCGTGACGGT GACTGGAATG AATTCCGTCG TAAACTGAC 300 TTCTATCTGA AAACCTTGGA GAACGCGCAG GCTCAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC CGTCTCCTCC GTCTAAAGA 420 TCTCATAAAT CTCCAAACAT GGCTACCCAG GGTGCCATGC CGGCCTTCGC CTCTGCTTT 480 CAGCGCCGGG CAGGAGGGGT CCTGGTTGCT AGCCATCTGC AGAGCTTCCT GGAGGTGTC 540 TACCGCGTTC TACGCCACCT TGCGCAGCCC TCTGGCGGCT CTGGCGGCTC TCAGAGCTT 600 CTGCTCAAGT CTTTAGAGCA AGTGAGAAAG ATCCAGGGCG ATGGCGCAGC GCTCCAGGA 660 AAGCTGTGTG CCACCTACAA GCTGTGCCAC CCCGAGGAGC TGGTGCTGCT CGGACACTC 720 CTGGGCATCC CCTGGGCTCC CCTGAGCTCC TGCCCCAGCC AGGCCCTGCA GCTGGCAGG 780 TGCTTGAGCC AACTCCATAG CGGCCTTTTC CTCTACCAGG GGCTCCTGCA GGCCCTGGA 840 GGGATATCCC CCGAGTTGGG TCCCACCTTG GACACACTGC AGCTGGACGT CGCCGACTT 900 GCCACCACCA TCTGGCAGCA GATGGAAGAA CTGGGAATGG CCCCTGCCCT GCAGCCCTA 960 TAA 963 972 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 117 ATGGCTAACT GCTCTAACAT GATCGATGAA ATCATCACCC ACCTGAAGCA GCCACCGCTG 60 CCGCTGCTGG ACTTCAACAA CCTCAATGGT GAAGACCAAG ATATCCTAAT GGACAATAA 120 CTTCGTCGTC CAAACCTCGA GGCATTCAAC CGTGCTGTCA AGTCTCTGCA GAATGCATC 180 GCAATTGAGA GCATTCTTAA AAATCTCCTG CCATGTCTGC CGCTAGCCAC GGCCGCACC 240 ACGCGACATC CAATCCATAT CAAGGACGGT GACTGGAATG AATTCCGTCG TAAACTGAC 300 TTCTATCTGA AAACCTTGGA GAACGCGCAG GCTCAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC CGTCTCCTCC GTCTAAAGA 420 TCTCATAAAT CTCCAAACAT GGCTACCCAG GGTGCCATGC CGGCCTTCGC CTCTGCTTT 480 CAGCGCCGGG CAGGAGGGGT CCTGGTTGCT AGCCATCTGC AGAGCTTCCT GGAGGTGTC 540 TACCGCGTTC TACGCCACCT TGCGCAGCCC ACACCATTGG GCCCTGCCAG CTCCCTGCC 600 CAGAGCTTCC TGCTCAAGTC TTTAGAGCAA GTGAGAAAGA TCCAGGGCGA TGGCGCAGC 660 CTCCAGGAGA AGCTGTGTGC CACCTACAAG CTGTGCCACC CCGAGGAGCT GGTGCTGCT 720 GGACACTCTC TGGGCATCCC CTGGGCTCCC CTGAGCTCCT GCCCCAGCCA GGCCCTGCA 780 CTGGCAGGCT GCTTGAGCCA ACTCCATAGC GGCCTTTTCC TCTACCAGGG GCTCCTGCA 840 GCCCTGGAAG GGATATCCCC CGAGTTGGGT CCCACCTTGG ACACACTGCA GCTGGACGT 900 GCCGACTTTG CCACCACCAT CTGGCAGCAG ATGGAAGAAC TGGGAATGGC CCCTGCCCT 960 CAGCCCTAAT AA 972 918 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 118 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGGA GGTTCACCCT TTGCCTACAC CTGTCCTGCT GCCTGCTGT 480 GACTTTAGCT TGGGAGAATG GAAAACCCAG ATGGAGGAGA CCAAGGCACA GGACATTCT 540 GGAGCAGTGA CCCTTCTGCT GGAGGGAGTG ATGGCAGCAC GGGGACAACT GGGACCCAC 600 TGCCTCTCAT CCCTCCTGGG GCAGCTTTCT GGACAGGTCC GTCTCCTCCT TGGGGCCCT 660 CAGAGCCTCC TTGGAACCCA GCTTCCTCCA CAGGGCAGGA CCACAGCTCA CAAGGATCC 720 AATGCCATCT TCCTGAGCTT CCAACACCTG CTCCGAGGAA AGGTGCGTTT CCTGATGCT 780 GTAGGAGGGT CCACCCTCTG CGTCAGGGAA TTCGGCGGCA ACATGGCGTC TCCCGCTCC 840 CCTGCTTGTG ACCTCCGAGT CCTCAGTAAA CTGCTTCGTG ACTCCCATGT CCTTCACAG 900 AGACTGAGCC AGTGCCCA 918 918 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 119 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGTT GCCTACACCT GTCCTGCTGC CTGCTGTGGA CTTTAGCTT 480 GGAGAATGGA AAACCCAGAT GGAGGAGACC AAGGCACAGG ACATTCTGGG AGCAGTGAC 540 CTTCTGCTGG AGGGAGTGAT GGCAGCACGG GGACAACTGG GACCCACTTG CCTCTCATC 600 CTCCTGGGGC AGCTTTCTGG ACAGGTCCGT CTCCTCCTTG GGGCCCTGCA GAGCCTCCT 660 GGAACCCAGC TTCCTCCACA GGGCAGGACC ACAGCTCACA AGGATCCCAA TGCCATCTT 720 CTGAGCTTCC AACACCTGCT CCGAGGAAAG GTGCGTTTCC TGATGCTTGT AGGAGGGTC 780 ACCCTCTGCG TCAGGGAATT CGGCGGCAAC ATGGCGTCTC CCGCTCCGCC TGCTTGTGA 840 CTCCGAGTCC TCAGTAAACT GCTTCGTGAC TCCCATGTCC TTCACAGCAG ACTGAGCCA 900 TGCCCAGAGG TTCACCCT 918 918 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 120 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGGT CCTGCTGCCT GCTGTGGACT TTAGCTTGGG AGAATGGAA 480 ACCCAGATGG AGGAGACCAA GGCACAGGAC ATTCTGGGAG CAGTGACCCT TCTGCTGGA 540 GGAGTGATGG CAGCACGGGG ACAACTGGGA CCCACTTGCC TCTCATCCCT CCTGGGGCA 600 CTTTCTGGAC AGGTCCGTCT CCTCCTTGGG GCCCTGCAGA GCCTCCTTGG AACCCAGCT 660 CCTCCACAGG GCAGGACCAC AGCTCACAAG GATCCCAATG CCATCTTCCT GAGCTTCCA 720 CACCTGCTCC GAGGAAAGGT GCGTTTCCTG ATGCTTGTAG GAGGGTCCAC CCTCTGCGT 780 AGGGAATTCG GCGGCAACAT GGCGTCTCCC GCTCCGCCTG CTTGTGACCT CCGAGTCCT 840 AGTAAACTGC TTCGTGACTC CCATGTCCTT CACAGCAGAC TGAGCCAGTG CCCAGAGGT 900 CACCCTTTGC CTACACCT 918 918 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 121 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGGC TGTGGACTTT AGCTTGGGAG AATGGAAAAC CCAGATGGA 480 GAGACCAAGG CACAGGACAT TCTGGGAGCA GTGACCCTTC TGCTGGAGGG AGTGATGGC 540 GCACGGGGAC AACTGGGACC CACTTGCCTC TCATCCCTCC TGGGGCAGCT TTCTGGACA 600 GTCCGTCTCC TCCTTGGGGC CCTGCAGAGC CTCCTTGGAA CCCAGCTTCC TCCACAGGG 660 AGGACCACAG CTCACAAGGA TCCCAATGCC ATCTTCCTGA GCTTCCAACA CCTGCTCCG 720 GGAAAGGTGC GTTTCCTGAT GCTTGTAGGA GGGTCCACCC TCTGCGTCAG GGAATTCGG 780 GGCAACATGG CGTCTCCCGC TCCGCCTGCT TGTGACCTCC GAGTCCTCAG TAAACTGCT 840 CGTGACTCCC ATGTCCTTCA CAGCAGACTG AGCCAGTGCC CAGAGGTTCA CCCTTTGCC 900 ACACCTGTCC TGCTGCCT 918 918 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 122 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGGA CTTTAGCTTG GGAGAATGGA AAACCCAGAT GGAGGAGAC 480 AAGGCACAGG ACATTCTGGG AGCAGTGACC CTTCTGCTGG AGGGAGTGAT GGCAGCACG 540 GGACAACTGG GACCCACTTG CCTCTCATCC CTCCTGGGGC AGCTTTCTGG ACAGGTCCG 600 CTCCTCCTTG GGGCCCTGCA GAGCCTCCTT GGAACCCAGC TTCCTCCACA GGGCAGGAC 660 ACAGCTCACA AGGATCCCAA TGCCATCTTC CTGAGCTTCC AACACCTGCT CCGAGGAAA 720 GTGCGTTTCC TGATGCTTGT AGGAGGGTCC ACCCTCTGCG TCAGGGAATT CGGCGGCAA 780 ATGGCGTCTC CCGCTCCGCC TGCTTGTGAC CTCCGAGTCC TCAGTAAACT GCTTCGTGA 840 TCCCATGTCC TTCACAGCAG ACTGAGCCAG TGCCCAGAGG TTCACCCTTT GCCTACACC 900 GTCCTGCTGC CTGCTGTG 918 907 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 123 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCGGTTAC CCTTGAGCAA GCGCAGGAAC AACAGTACGT AGAGGGCGGT GGAGGCTCC 360 CGGGGAACCG TCTGGTCCAA TCTCTACTAT CAACCCGTCT CCTCCGTCTA AAGAATCTC 420 TAAACTCCAA ACATGGGAGA ATGGAAAACC CAGATGGAGG AGACCAAGGC ACAGGACAT 480 CTGGAGCAGT GACCCTTCTG CTGGAGGGAG TGATGGCAGC ACGGGGACAA CTGGGACCC 540 CTTGCTCTCA TCCCTCCTGG GGCAGCTTTC TGGACAGGTC CGTCTCCTCC TTGGGGCCC 600 GCAGGCCTCC TTGGAACCCA GCTTCCTCCA CAGGGCAGGA CCACAGCTCA CAAGGATCC 660 AATGCATCTT CCTGAGCTTC CAACACCTGC TCCGAGGAAA GGTGCGTTTC CTGATGCTT 720 TAGGGGGTCC ACCCTCTGCG TCAGGGAATT CGGCGGCAAC ATGGCGTCTC CCGCTCCGC 780 TGCTGTGACC TCCGAGTCCT CAGTAAACTG CTTCGTGACT CCCATGTCCT TCACAGCAG 840 CTGACCAGTG CCCAGAGGTT CACCCTTTGC CTACACCTGT CCTGCTGCCT GCTGTGGAC 900 TTAGTTG 907 918 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 124 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGGG ACCCACTTGC CTCTCATCCC TCCTGGGGCA GCTTTCTGG 480 CAGGTCCGTC TCCTCCTTGG GGCCCTGCAG AGCCTCCTTG GAACCCAGCT TCCTCCACA 540 GGCAGGACCA CAGCTCACAA GGATCCCAAT GCCATCTTCC TGAGCTTCCA ACACCTGCT 600 CGAGGAAAGG TGCGTTTCCT GATGCTTGTA GGAGGGTCCA CCCTCTGCGT CAGGGAATT 660 GGCGGCAACA TGGCGTCTCC CGCTCCGCCT GCTTGTGACC TCCGAGTCCT CAGTAAACT 720 CTTCGTGACT CCCATGTCCT TCACAGCAGA CTGAGCCAGT GCCCAGAGGT TCACCCTTT 780 CCTACACCTG TCCTGCTGCC TGCTGTGGAC TTTAGCTTGG GAGAATGGAA AACCCAGAT 840 GAGGAGACCA AGGCACAGGA CATTCTGGGA GCAGTGACCC TTCTGCTGGA GGGAGTGAT 900 GCAGCACGGG GACAACTG 918 848 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 125 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGGG AACCCAGCTT CCTCCACAGG GCAGGACCAC AGCTCACAA 480 GATCCCAATG CCATCTTCCT GAGCTTCCAA CACCTGCTCC GAGGAAAGGT GCGTTTCCT 540 ATGCTTGTAG GAGGGTCCAC CCTCTGCGTC AGGGAATTCG GCGGCAACAT GGCGTCTCC 600 GCTCCGCCTG CTTGTGACCT CCGAGTCCTC AGTAAACTGC TTCGTGACTC CCATGTCCT 660 CACAGCAGAC TGAGCCAGTG CCCAGAGGTT CACCCTTTGC CTACACCTGT CCTGCTGCC 720 GCTGTGGACT TTAGCTTGGG AGAATGGAAA ACCCAGATGG AGGAGACCAA GGCACAGGA 780 ATTCTGGGAG CAGTGACCCT TCTGCTGGAG GGAGTGATGG CAGCACGGGG ACAACTGGG 840 CCCACTTG 848 918 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 126 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGGG CAGGACCACA GCTCACAAGG ATCCCAATGC CATCTTCCT 480 AGCTTCCAAC ACCTGCTCCG AGGAAAGGTG CGTTTCCTGA TGCTTGTAGG AGGGTCCAC 540 CTCTGCGTCA GGGAATTCGG CGGCAACATG GCGTCTCCCG CTCCGCCTGC TTGTGACCT 600 CGAGTCCTCA GTAAACTGCT TCGTGACTCC CATGTCCTTC ACAGCAGACT GAGCCAGTG 660 CCAGAGGTTC ACCCTTTGCC TACACCTGTC CTGCTGCCTG CTGTGGACTT TAGCTTGGG 720 GAATGGAAAA CCCAGATGGA GGAGACCAAG GCACAGGACA TTCTGGGAGC AGTGACCCT 780 CTGCTGGAGG GAGTGATGGC AGCACGGGGA CAACTGGGAC CCACTTGCCT CTCATCCCT 840 CTGGGGCAGC TTTCTGGACA GGTCCGTCTC CTCCTTGGGG CCCTGCAGAG CCTCCTTGG 900 ACCCAGCTTC CTCCACAG 918 918 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 127 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGGC TCACAAGGAT CCCAATGCCA TCTTCCTGAG CTTCCAACA 480 CTGCTCCGAG GAAAGGTGCG TTTCCTGATG CTTGTAGGAG GGTCCACCCT CTGCGTCAG 540 GAATTCGGCG GCAACATGGC GTCTCCCGCT CCGCCTGCTT GTGACCTCCG AGTCCTCAG 600 AAACTGCTTC GTGACTCCCA TGTCCTTCAC AGCAGACTGA GCCAGTGCCC AGAGGTTCA 660 CCTTTGCCTA CACCTGTCCT GCTGCCTGCT GTGGACTTTA GCTTGGGAGA ATGGAAAAC 720 CAGATGGAGG AGACCAAGGC ACAGGACATT CTGGGAGCAG TGACCCTTCT GCTGGAGGG 780 GTGATGGCAG CACGGGGACA ACTGGGACCC ACTTGCCTCT CATCCCTCCT GGGGCAGCT 840 TCTGGACAGG TCCGTCTCCT CCTTGGGGCC CTGCAGAGCC TCCTTGGAAC CCAGCTTCC 900 CCACAGGGCA GGACCACA 918 918 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 128 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGGA TCCCAATGCC ATCTTCCTGA GCTTCCAACA CCTGCTCCG 480 GGAAAGGTGC GTTTCCTGAT GCTTGTAGGA GGGTCCACCC TCTGCGTCAG GGAATTCGG 540 GGCAACATGG CGTCTCCCGC TCCGCCTGCT TGTGACCTCC GAGTCCTCAG TAAACTGCT 600 CGTGACTCCC ATGTCCTTCA CAGCAGACTG AGCCAGTGCC CAGAGGTTCA CCCTTTGCC 660 ACACCTGTCC TGCTGCCTGC TGTGGACTTT AGCTTGGGAG AATGGAAAAC CCAGATGGA 720 GAGACCAAGG CACAGGACAT TCTGGGAGCA GTGACCCTTC TGCTGGAGGG AGTGATGGC 780 GCACGGGGAC AACTGGGACC CACTTGCCTC TCATCCCTCC TGGGGCAGCT TTCTGGACA 840 GTCCGTCTCC TCCTTGGGGC CCTGCAGAGC CTCCTTGGAA CCCAGCTTCC TCCACAGGG 900 AGGACCACAG CTCACAAG 918 918 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 129 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGGC CATCTTCCTG AGCTTCCAAC ACCTGCTCCG AGGAAAGGT 480 CGTTTCCTGA TGCTTGTAGG AGGGTCCACC CTCTGCGTCA GGGAATTCGG CGGCAACAT 540 GCGTCTCCCG CTCCGCCTGC TTGTGACCTC CGAGTCCTCA GTAAACTGCT TCGTGACTC 600 CATGTCCTTC ACAGCAGACT GAGCCAGTGC CCAGAGGTTC ACCCTTTGCC TACACCTGT 660 CTGCTGCCTG CTGTGGACTT TAGCTTGGGA GAATGGAAAA CCCAGATGGA GGAGACCAA 720 GCACAGGACA TTCTGGGAGC AGTGACCCTT CTGCTGGAGG GAGTGATGGC AGCACGGGG 780 CAACTGGGAC CCACTTGCCT CTCATCCCTC CTGGGGCAGC TTTCTGGACA GGTCCGTCT 840 CTCCTTGGGG CCCTGCAGAG CCTCCTTGGA ACCCAGCTTC CTCCACAGGG CAGGACCAC 900 GCTCACAAGG ATCCCAAT 918 915 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 130 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGGA GGTTCACCCT TTGCCTACAC CTGTCCTGCT GCCTGCTGT 480 GACTTTAGCT TGGGAGAATG GAAAACCCAG ATGGAGGAGA CCAAGGCACA GGACATTCT 540 GGAGCAGTGA CCCTTCTGCT GGAGGGAGTG ATGGCAGCAC GGGGACAACT GGGACCCAC 600 TGCCTCTCAT CCCTCCTGGG GCAGCTTTCT GGACAGGTCC GTCTCCTCCT TGGGGCCCT 660 CAGAGCCTCC TTGGAACCCA GCTTCCTCCA CAGGGCAGGA CCACAGCTCA CAAGGATCC 720 AATGCCATCT TCCTGAGCTT CCAACACCTG CTCCGAGGAA AGGTGCGTTT CCTGATGCT 780 GTAGGAGGGT CCACCCTCTG CGTCAGGGAA TTCGGCAACA TGGCGTCTCC CGCTCCGCC 840 GCTTGTGACC TCCGAGTCCT CAGTAAACTG CTTCGTGACT CCCATGTCCT TCACAGCAG 900 CTGAGCCAGT GCCCA 915 915 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 131 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGTT GCCTACACCT GTCCTGCTGC CTGCTGTGGA CTTTAGCTT 480 GGAGAATGGA AAACCCAGAT GGAGGAGACC AAGGCACAGG ACATTCTGGG AGCAGTGAC 540 CTTCTGCTGG AGGGAGTGAT GGCAGCACGG GGACAACTGG GACCCACTTG CCTCTCATC 600 CTCCTGGGGC AGCTTTCTGG ACAGGTCCGT CTCCTCCTTG GGGCCCTGCA GAGCCTCCT 660 GGAACCCAGC TTCCTCCACA GGGCAGGACC ACAGCTCACA AGGATCCCAA TGCCATCTT 720 CTGAGCTTCC AACACCTGCT CCGAGGAAAG GTGCGTTTCC TGATGCTTGT AGGAGGGTC 780 ACCCTCTGCG TCAGGGAATT CGGCAACATG GCGTCTCCCG CTCCGCCTGC TTGTGACCT 840 CGAGTCCTCA GTAAACTGCT TCGTGACTCC CATGTCCTTC ACAGCAGACT GAGCCAGTG 900 CCAGAGGTTC ACCCT 915 915 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 132 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGGT CCTGCTGCCT GCTGTGGACT TTAGCTTGGG AGAATGGAA 480 ACCCAGATGG AGGAGACCAA GGCACAGGAC ATTCTGGGAG CAGTGACCCT TCTGCTGGA 540 GGAGTGATGG CAGCACGGGG ACAACTGGGA CCCACTTGCC TCTCATCCCT CCTGGGGCA 600 CTTTCTGGAC AGGTCCGTCT CCTCCTTGGG GCCCTGCAGA GCCTCCTTGG AACCCAGCT 660 CCTCCACAGG GCAGGACCAC AGCTCACAAG GATCCCAATG CCATCTTCCT GAGCTTCCA 720 CACCTGCTCC GAGGAAAGGT GCGTTTCCTG ATGCTTGTAG GAGGGTCCAC CCTCTGCGT 780 AGGGAATTCG GCAACATGGC GTCTCCCGCT CCGCCTGCTT GTGACCTCCG AGTCCTCAG 840 AAACTGCTTC GTGACTCCCA TGTCCTTCAC AGCAGACTGA GCCAGTGCCC AGAGGTTCA 900 CCTTTGCCTA CACCT 915 915 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 133 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGGC TGTGGACTTT AGCTTGGGAG AATGGAAAAC CCAGATGGA 480 GAGACCAAGG CACAGGACAT TCTGGGAGCA GTGACCCTTC TGCTGGAGGG AGTGATGGC 540 GCACGGGGAC AACTGGGACC CACTTGCCTC TCATCCCTCC TGGGGCAGCT TTCTGGACA 600 GTCCGTCTCC TCCTTGGGGC CCTGCAGAGC CTCCTTGGAA CCCAGCTTCC TCCACAGGG 660 AGGACCACAG CTCACAAGGA TCCCAATGCC ATCTTCCTGA GCTTCCAACA CCTGCTCCG 720 GGAAAGGTGC GTTTCCTGAT GCTTGTAGGA GGGTCCACCC TCTGCGTCAG GGAATTCGG 780 AACATGGCGT CTCCCGCTCC GCCTGCTTGT GACCTCCGAG TCCTCAGTAA ACTGCTTCG 840 GACTCCCATG TCCTTCACAG CAGACTGAGC CAGTGCCCAG AGGTTCACCC TTTGCCTAC 900 CCTGTCCTGC TGCCT 915 915 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 134 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGGA CTTTAGCTTG GGAGAATGGA AAACCCAGAT GGAGGAGAC 480 AAGGCACAGG ACATTCTGGG AGCAGTGACC CTTCTGCTGG AGGGAGTGAT GGCAGCACG 540 GGACAACTGG GACCCACTTG CCTCTCATCC CTCCTGGGGC AGCTTTCTGG ACAGGTCCG 600 CTCCTCCTTG GGGCCCTGCA GAGCCTCCTT GGAACCCAGC TTCCTCCACA GGGCAGGAC 660 ACAGCTCACA AGGATCCCAA TGCCATCTTC CTGAGCTTCC AACACCTGCT CCGAGGAAA 720 GTGCGTTTCC TGATGCTTGT AGGAGGGTCC ACCCTCTGCG TCAGGGAATT CGGCAACAT 780 GCGTCTCCCG CTCCGCCTGC TTGTGACCTC CGAGTCCTCA GTAAACTGCT TCGTGACTC 840 CATGTCCTTC ACAGCAGACT GAGCCAGTGC CCAGAGGTTC ACCCTTTGCC TACACCTGT 900 CTGCTGCCTG CTGTG 915 915 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 135 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGGG AGAATGGAAA ACCCAGATGG AGGAGACCAA GGCACAGGA 480 ATTCTGGGAG CAGTGACCCT TCTGCTGGAG GGAGTGATGG CAGCACGGGG ACAACTGGG 540 CCCACTTGCC TCTCATCCCT CCTGGGGCAG CTTTCTGGAC AGGTCCGTCT CCTCCTTGG 600 GCCCTGCAGA GCCTCCTTGG AACCCAGCTT CCTCCACAGG GCAGGACCAC AGCTCACAA 660 GATCCCAATG CCATCTTCCT GAGCTTCCAA CACCTGCTCC GAGGAAAGGT GCGTTTCCT 720 ATGCTTGTAG GAGGGTCCAC CCTCTGCGTC AGGGAATTCG GCAACATGGC GTCTCCCGC 780 CCGCCTGCTT GTGACCTCCG AGTCCTCAGT AAACTGCTTC GTGACTCCCA TGTCCTTCA 840 AGCAGACTGA GCCAGTGCCC AGAGGTTCAC CCTTTGCCTA CACCTGTCCT GCTGCCTGC 900 GTGGACTTTA GCTTG 915 915 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 136 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGGG ACCCACTTGC CTCTCATCCC TCCTGGGGCA GCTTTCTGG 480 CAGGTCCGTC TCCTCCTTGG GGCCCTGCAG AGCCTCCTTG GAACCCAGCT TCCTCCACA 540 GGCAGGACCA CAGCTCACAA GGATCCCAAT GCCATCTTCC TGAGCTTCCA ACACCTGCT 600 CGAGGAAAGG TGCGTTTCCT GATGCTTGTA GGAGGGTCCA CCCTCTGCGT CAGGGAATT 660 GGCAACATGG CGTCTCCCGC TCCGCCTGCT TGTGACCTCC GAGTCCTCAG TAAACTGCT 720 CGTGACTCCC ATGTCCTTCA CAGCAGACTG AGCCAGTGCC CAGAGGTTCA CCCTTTGCC 780 ACACCTGTCC TGCTGCCTGC TGTGGACTTT AGCTTGGGAG AATGGAAAAC CCAGATGGA 840 GAGACCAAGG CACAGGACAT TCTGGGAGCA GTGACCCTTC TGCTGGAGGG AGTGATGGC 900 GCACGGGGAC AACTG 915 915 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 137 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGGG AACCCAGCTT CCTCCACAGG GCAGGACCAC AGCTCACAA 480 GATCCCAATG CCATCTTCCT GAGCTTCCAA CACCTGCTCC GAGGAAAGGT GCGTTTCCT 540 ATGCTTGTAG GAGGGTCCAC CCTCTGCGTC AGGGAATTCG GCAACATGGC GTCTCCCGC 600 CCGCCTGCTT GTGACCTCCG AGTCCTCAGT AAACTGCTTC GTGACTCCCA TGTCCTTCA 660 AGCAGACTGA GCCAGTGCCC AGAGGTTCAC CCTTTGCCTA CACCTGTCCT GCTGCCTGC 720 GTGGACTTTA GCTTGGGAGA ATGGAAAACC CAGATGGAGG AGACCAAGGC ACAGGACAT 780 CTGGGAGCAG TGACCCTTCT GCTGGAGGGA GTGATGGCAG CACGGGGACA ACTGGGACC 840 ACTTGCCTCT CATCCCTCCT GGGGCAGCTT TCTGGACAGG TCCGTCTCCT CCTTGGGGC 900 CTGCAGAGCC TCCTT 915 915 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 138 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGGG CAGGACCACA GCTCACAAGG ATCCCAATGC CATCTTCCT 480 AGCTTCCAAC ACCTGCTCCG AGGAAAGGTG CGTTTCCTGA TGCTTGTAGG AGGGTCCAC 540 CTCTGCGTCA GGGAATTCGG CAACATGGCG TCTCCCGCTC CGCCTGCTTG TGACCTCCG 600 GTCCTCAGTA AACTGCTTCG TGACTCCCAT GTCCTTCACA GCAGACTGAG CCAGTGCCC 660 GAGGTTCACC CTTTGCCTAC ACCTGTCCTG CTGCCTGCTG TGGACTTTAG CTTGGGAGA 720 TGGAAAACCC AGATGGAGGA GACCAAGGCA CAGGACATTC TGGGAGCAGT GACCCTTCT 780 CTGGAGGGAG TGATGGCAGC ACGGGGACAA CTGGGACCCA CTTGCCTCTC ATCCCTCCT 840 GGGCAGCTTT CTGGACAGGT CCGTCTCCTC CTTGGGGCCC TGCAGAGCCT CCTTGGAAC 900 CAGCTTCCTC CACAG 915 915 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 139 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGGC TCACAAGGAT CCCAATGCCA TCTTCCTGAG CTTCCAACA 480 CTGCTCCGAG GAAAGGTGCG TTTCCTGATG CTTGTAGGAG GGTCCACCCT CTGCGTCAG 540 GAATTCGGCA ACATGGCGTC TCCCGCTCCG CCTGCTTGTG ACCTCCGAGT CCTCAGTAA 600 CTGCTTCGTG ACTCCCATGT CCTTCACAGC AGACTGAGCC AGTGCCCAGA GGTTCACCC 660 TTGCCTACAC CTGTCCTGCT GCCTGCTGTG GACTTTAGCT TGGGAGAATG GAAAACCCA 720 ATGGAGGAGA CCAAGGCACA GGACATTCTG GGAGCAGTGA CCCTTCTGCT GGAGGGAGT 780 ATGGCAGCAC GGGGACAACT GGGACCCACT TGCCTCTCAT CCCTCCTGGG GCAGCTTTC 840 GGACAGGTCC GTCTCCTCCT TGGGGCCCTG CAGAGCCTCC TTGGAACCCA GCTTCCTCC 900 CAGGGCAGGA CCACA 915 915 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 140 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGGA TCCCAATGCC ATCTTCCTGA GCTTCCAACA CCTGCTCCG 480 GGAAAGGTGC GTTTCCTGAT GCTTGTAGGA GGGTCCACCC TCTGCGTCAG GGAATTCGG 540 AACATGGCGT CTCCCGCTCC GCCTGCTTGT GACCTCCGAG TCCTCAGTAA ACTGCTTCG 600 GACTCCCATG TCCTTCACAG CAGACTGAGC CAGTGCCCAG AGGTTCACCC TTTGCCTAC 660 CCTGTCCTGC TGCCTGCTGT GGACTTTAGC TTGGGAGAAT GGAAAACCCA GATGGAGGA 720 ACCAAGGCAC AGGACATTCT GGGAGCAGTG ACCCTTCTGC TGGAGGGAGT GATGGCAGC 780 CGGGGACAAC TGGGACCCAC TTGCCTCTCA TCCCTCCTGG GGCAGCTTTC TGGACAGGT 840 CGTCTCCTCC TTGGGGCCCT GCAGAGCCTC CTTGGAACCC AGCTTCCTCC ACAGGGCAG 900 ACCACAGCTC ACAAG 915 915 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 141 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGGC CATCTTCCTG AGCTTCCAAC ACCTGCTCCG AGGAAAGGT 480 CGTTTCCTGA TGCTTGTAGG AGGGTCCACC CTCTGCGTCA GGGAATTCGG CAACATGGC 540 TCTCCCGCTC CGCCTGCTTG TGACCTCCGA GTCCTCAGTA AACTGCTTCG TGACTCCCA 600 GTCCTTCACA GCAGACTGAG CCAGTGCCCA GAGGTTCACC CTTTGCCTAC ACCTGTCCT 660 CTGCCTGCTG TGGACTTTAG CTTGGGAGAA TGGAAAACCC AGATGGAGGA GACCAAGGC 720 CAGGACATTC TGGGAGCAGT GACCCTTCTG CTGGAGGGAG TGATGGCAGC ACGGGGACA 780 CTGGGACCCA CTTGCCTCTC ATCCCTCCTG GGGCAGCTTT CTGGACAGGT CCGTCTCCT 840 CTTGGGGCCC TGCAGAGCCT CCTTGGAACC CAGCTTCCTC CACAGGGCAG GACCACAGC 900 CACAAGGATC CCAAT 915 921 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 142 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 GACTTCCAAA CCTGGAGAGC TTCGTAAGGG CTGTCAAGAA CTTAGAAAAT GCATCAGGT 180 TGAGGCAATT CTTCGTAATC TCCAACCATG TCTGCCCTCT GCCACGGCCG CACCCTCTC 240 CATCCAATCA TCATCAAGGC AGGTGACTGG CAAGAATTCC GGGAAAAACT GACGTTCTA 300 TGGTTACCCT TGAGCAAGCG CAGGAACAAC AGTACGTAGA GGGCGGTGGA GGCTCCCCG 360 TAACCGTCTG GTCCAATCTC TACTATCAAC CCGTCTCCTC CGTCTAAAGA ATCTCATAA 420 TCTCCAAACA TGGAGGTTCA CCCTTTGCCT ACACCTGTCC TGCTGCCTGC TGTGGACTT 480 AGCTTGGGAG AATGGAAAAC CCAGATGGAG GAGACCAAGG CACAGGACAT TCTGGGAGC 540 GTGACCCTTC TGCTGGAGGG AGTGATGGCA GCACGGGGAC AACTGGGACC CACTTGCCT 600 TCATCCCTCC TGGGGCAGCT TTCTGGACAG GTCCGTCTCC TCCTTGGGGC CCTGCAGAG 660 CTCCTTGGAA CCCAGCTTCC TCCACAGGGC AGGACCACAG CTCACAAGGA TCCCAATGC 720 ATCTTCCTGA GCTTCCAACA CCTGCTCCGA GGAAAGGTGC GTTTCCTGAT GCTTGTAGG 780 GGGTCCACCC TCTGCGTCAG GGAATTCGGC GGCAACGGCG GCAACATGGC GTCCCCAGC 840 CCGCCTGCTT GTGACCTCCG AGTCCTCAGT AAACTGCTTC GTGACTCCCA TGTCCTTCA 900 AGCAGACTGA GCCAGTGCCC A 921 927 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 143 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGTT GCCTACACCT GTCCTGCTGC CTGCTGTGGA CTTTAGCTT 480 GGAGAATGGA AAACCCAGAT GGAGGAGACC AAGGCACAGG ACATTCTGGG AGCAGTGAC 540 CTTCTGCTGG AGGGAGTGAT GGCAGCACGG GGACAACTGG GACCCACTTG CCTCTCATC 600 CTCCTGGGGC AGCTTTCTGG ACAGGTCCGT CTCCTCCTTG GGGCCCTGCA GAGCCTCCT 660 GGAACCCAGC TTCCTCCACA GGGCAGGACC ACAGCTCACA AGGATCCCAA TGCCATCTT 720 CTGAGCTTCC AACACCTGCT CCGAGGAAAG GTGCGTTTCC TGATGCTTGT AGGAGGGTC 780 ACCCTCTGCG TCAGGGAATT CGGCGGCAAC GGCGGCAACA TGGCGTCCCC AGCGCCGCC 840 GCTTGTGACC TCCGAGTCCT CAGTAAACTG CTTCGTGACT CCCATGTCCT TCACAGCAG 900 CTGAGCCAGT GCCCAGAGGT TCACCCT 927 927 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 144 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGGT CCTGCTGCCT GCTGTGGACT TTAGCTTGGG AGAATGGAA 480 ACCCAGATGG AGGAGACCAA GGCACAGGAC ATTCTGGGAG CAGTGACCCT TCTGCTGGA 540 GGAGTGATGG CAGCACGGGG ACAACTGGGA CCCACTTGCC TCTCATCCCT CCTGGGGCA 600 CTTTCTGGAC AGGTCCGTCT CCTCCTTGGG GCCCTGCAGA GCCTCCTTGG AACCCAGCT 660 CCTCCACAGG GCAGGACCAC AGCTCACAAG GATCCCAATG CCATCTTCCT GAGCTTCCA 720 CACCTGCTCC GAGGAAAGGT GCGTTTCCTG ATGCTTGTAG GAGGGTCCAC CCTCTGCGT 780 AGGGAATTCG GCGGCAACGG CGGCAACATG GCGTCCCCAG CGCCGCCTGC TTGTGACCT 840 CGAGTCCTCA GTAAACTGCT TCGTGACTCC CATGTCCTTC ACAGCAGACT GAGCCAGTG 900 CCAGAGGTTC ACCCTTTGCC TACACCT 927 927 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 145 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGGC TGTGGACTTT AGCTTGGGAG AATGGAAAAC CCAGATGGA 480 GAGACCAAGG CACAGGACAT TCTGGGAGCA GTGACCCTTC TGCTGGAGGG AGTGATGGC 540 GCACGGGGAC AACTGGGACC CACTTGCCTC TCATCCCTCC TGGGGCAGCT TTCTGGACA 600 GTCCGTCTCC TCCTTGGGGC CCTGCAGAGC CTCCTTGGAA CCCAGCTTCC TCCACAGGG 660 AGGACCACAG CTCACAAGGA TCCCAATGCC ATCTTCCTGA GCTTCCAACA CCTGCTCCG 720 GGAAAGGTGC GTTTCCTGAT GCTTGTAGGA GGGTCCACCC TCTGCGTCAG GGAATTCGG 780 GGCAACGGCG GCAACATGGC GTCCCCAGCG CCGCCTGCTT GTGACCTCCG AGTCCTCAG 840 AAACTGCTTC GTGACTCCCA TGTCCTTCAC AGCAGACTGA GCCAGTGCCC AGAGGTTCA 900 CCTTTGCCTA CACCTGTCCT GCTGCCT 927 927 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 146 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGGA CTTTAGCTTG GGAGAATGGA AAACCCAGAT GGAGGAGAC 480 AAGGCACAGG ACATTCTGGG AGCAGTGACC CTTCTGCTGG AGGGAGTGAT GGCAGCACG 540 GGACAACTGG GACCCACTTG CCTCTCATCC CTCCTGGGGC AGCTTTCTGG ACAGGTCCG 600 CTCCTCCTTG GGGCCCTGCA GAGCCTCCTT GGAACCCAGC TTCCTCCACA GGGCAGGAC 660 ACAGCTCACA AGGATCCCAA TGCCATCTTC CTGAGCTTCC AACACCTGCT CCGAGGAAA 720 GTGCGTTTCC TGATGCTTGT AGGAGGGTCC ACCCTCTGCG TCAGGGAATT CGGCGGCAA 780 GGCGGCAACA TGGCGTCCCC AGCGCCGCCT GCTTGTGACC TCCGAGTCCT CAGTAAACT 840 CTTCGTGACT CCCATGTCCT TCACAGCAGA CTGAGCCAGT GCCCAGAGGT TCACCCTTT 900 CCTACACCTG TCCTGCTGCC TGCTGTG 927 927 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 147 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGGG AGAATGGAAA ACCCAGATGG AGGAGACCAA GGCACAGGA 480 ATTCTGGGAG CAGTGACCCT TCTGCTGGAG GGAGTGATGG CAGCACGGGG ACAACTGGG 540 CCCACTTGCC TCTCATCCCT CCTGGGGCAG CTTTCTGGAC AGGTCCGTCT CCTCCTTGG 600 GCCCTGCAGA GCCTCCTTGG AACCCAGCTT CCTCCACAGG GCAGGACCAC AGCTCACAA 660 GATCCCAATG CCATCTTCCT GAGCTTCCAA CACCTGCTCC GAGGAAAGGT GCGTTTCCT 720 ATGCTTGTAG GAGGGTCCAC CCTCTGCGTC AGGGAATTCG GCGGCAACGG CGGCAACAT 780 GCGTCCCCAG CGCCGCCTGC TTGTGACCTC CGAGTCCTCA GTAAACTGCT TCGTGACTC 840 CATGTCCTTC ACAGCAGACT GAGCCAGTGC CCAGAGGTTC ACCCTTTGCC TACACCTGT 900 CTGCTGCCTG CTGTGGACTT TAGCTTG 927 927 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 148 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGGG ACCCACTTGC CTCTCATCCC TCCTGGGGCA GCTTTCTGG 480 CAGGTCCGTC TCCTCCTTGG GGCCCTGCAG AGCCTCCTTG GAACCCAGCT TCCTCCACA 540 GGCAGGACCA CAGCTCACAA GGATCCCAAT GCCATCTTCC TGAGCTTCCA ACACCTGCT 600 CGAGGAAAGG TGCGTTTCCT GATGCTTGTA GGAGGGTCCA CCCTCTGCGT CAGGGAATT 660 GGCGGCAACG GCGGCAACAT GGCGTCCCCA GCGCCGCCTG CTTGTGACCT CCGAGTCCT 720 AGTAAACTGC TTCGTGACTC CCATGTCCTT CACAGCAGAC TGAGCCAGTG CCCAGAGGT 780 CACCCTTTGC CTACACCTGT CCTGCTGCCT GCTGTGGACT TTAGCTTGGG AGAATGGAA 840 ACCCAGATGG AGGAGACCAA GGCACAGGAC ATTCTGGGAG CAGTGACCCT TCTGCTGGA 900 GGAGTGATGG CAGCACGGGG ACAACTG 927 927 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 149 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGGG AACCCAGCTT CCTCCACAGG GCAGGACCAC AGCTCACAA 480 GATCCCAATG CCATCTTCCT GAGCTTCCAA CACCTGCTCC GAGGAAAGGT GCGTTTCCT 540 ATGCTTGTAG GAGGGTCCAC CCTCTGCGTC AGGGAATTCG GCGGCAACGG CGGCAACAT 600 GCGTCCCCAG CGCCGCCTGC TTGTGACCTC CGAGTCCTCA GTAAACTGCT TCGTGACTC 660 CATGTCCTTC ACAGCAGACT GAGCCAGTGC CCAGAGGTTC ACCCTTTGCC TACACCTGT 720 CTGCTGCCTG CTGTGGACTT TAGCTTGGGA GAATGGAAAA CCCAGATGGA GGAGACCAA 780 GCACAGGACA TTCTGGGAGC AGTGACCCTT CTGCTGGAGG GAGTGATGGC AGCACGGGG 840 CAACTGGGAC CCACTTGCCT CTCATCCCTC CTGGGGCAGC TTTCTGGACA GGTCCGTCT 900 CTCCTTGGGG CCCTGCAGAG CCTCCTT 927 927 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 150 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGGG CAGGACCACA GCTCACAAGG ATCCCAATGC CATCTTCCT 480 AGCTTCCAAC ACCTGCTCCG AGGAAAGGTG CGTTTCCTGA TGCTTGTAGG AGGGTCCAC 540 CTCTGCGTCA GGGAATTCGG CGGCAACGGC GGCAACATGG CGTCCCCAGC GCCGCCTGC 600 TGTGACCTCC GAGTCCTCAG TAAACTGCTT CGTGACTCCC ATGTCCTTCA CAGCAGACT 660 AGCCAGTGCC CAGAGGTTCA CCCTTTGCCT ACACCTGTCC TGCTGCCTGC TGTGGACTT 720 AGCTTGGGAG AATGGAAAAC CCAGATGGAG GAGACCAAGG CACAGGACAT TCTGGGAGC 780 GTGACCCTTC TGCTGGAGGG AGTGATGGCA GCACGGGGAC AACTGGGACC CACTTGCCT 840 TCATCCCTCC TGGGGCAGCT TTCTGGACAG GTCCGTCTCC TCCTTGGGGC CCTGCAGAG 900 CTCCTTGGAA CCCAGCTTCC TCCACAG 927 927 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 151 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGGC TCACAAGGAT CCCAATGCCA TCTTCCTGAG CTTCCAACA 480 CTGCTCCGAG GAAAGGTGCG TTTCCTGATG CTTGTAGGAG GGTCCACCCT CTGCGTCAG 540 GAATTCGGCG GCAACGGCGG CAACATGGCG TCCCCAGCGC CGCCTGCTTG TGACCTCCG 600 GTCCTCAGTA AACTGCTTCG TGACTCCCAT GTCCTTCACA GCAGACTGAG CCAGTGCCC 660 GAGGTTCACC CTTTGCCTAC ACCTGTCCTG CTGCCTGCTG TGGACTTTAG CTTGGGAGA 720 TGGAAAACCC AGATGGAGGA GACCAAGGCA CAGGACATTC TGGGAGCAGT GACCCTTCT 780 CTGGAGGGAG TGATGGCAGC ACGGGGACAA CTGGGACCCA CTTGCCTCTC ATCCCTCCT 840 GGGCAGCTTT CTGGACAGGT CCGTCTCCTC CTTGGGGCCC TGCAGAGCCT CCTTGGAAC 900 CAGCTTCCTC CACAGGGCAG GACCACA 927 927 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 152 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGGA TCCCAATGCC ATCTTCCTGA GCTTCCAACA CCTGCTCCG 480 GGAAAGGTGC GTTTCCTGAT GCTTGTAGGA GGGTCCACCC TCTGCGTCAG GGAATTCGG 540 GGCAACGGCG GCAACATGGC GTCCCCAGCG CCGCCTGCTT GTGACCTCCG AGTCCTCAG 600 AAACTGCTTC GTGACTCCCA TGTCCTTCAC AGCAGACTGA GCCAGTGCCC AGAGGTTCA 660 CCTTTGCCTA CACCTGTCCT GCTGCCTGCT GTGGACTTTA GCTTGGGAGA ATGGAAAAC 720 CAGATGGAGG AGACCAAGGC ACAGGACATT CTGGGAGCAG TGACCCTTCT GCTGGAGGG 780 GTGATGGCAG CACGGGGACA ACTGGGACCC ACTTGCCTCT CATCCCTCCT GGGGCAGCT 840 TCTGGACAGG TCCGTCTCCT CCTTGGGGCC CTGCAGAGCC TCCTTGGAAC CCAGCTTCC 900 CCACAGGGCA GGACCACAGC TCACAAG 927 927 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 153 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGGC CATCTTCCTG AGCTTCCAAC ACCTGCTCCG AGGAAAGGT 480 CGTTTCCTGA TGCTTGTAGG AGGGTCCACC CTCTGCGTCA GGGAATTCGG CGGCAACGG 540 GGCAACATGG CGTCCCCAGC GCCGCCTGCT TGTGACCTCC GAGTCCTCAG TAAACTGCT 600 CGTGACTCCC ATGTCCTTCA CAGCAGACTG AGCCAGTGCC CAGAGGTTCA CCCTTTGCC 660 ACACCTGTCC TGCTGCCTGC TGTGGACTTT AGCTTGGGAG AATGGAAAAC CCAGATGGA 720 GAGACCAAGG CACAGGACAT TCTGGGAGCA GTGACCCTTC TGCTGGAGGG AGTGATGGC 780 GCACGGGGAC AACTGGGACC CACTTGCCTC TCATCCCTCC TGGGGCAGCT TTCTGGACA 840 GTCCGTCTCC TCCTTGGGGC CCTGCAGAGC CTCCTTGGAA CCCAGCTTCC TCCACAGGG 900 AGGACCACAG CTCACAAGGA TCCCAAT 927 906 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 154 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCACCT 60 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCT 120 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGG 180 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCTC 240 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGTT 300 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCTC 360 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAATC 420 CATAAATCTC CAAACATGGA TCCCAATGCC ATCTTCCTGA GCTTCCAACA CCTGCTCCG 480 GGAAAGGTGC GTTTCCTGAT GCTTGTAGGA GGGTCCACCC TCTGCGTCAG GGAATTCGG 540 GGCAACATGG CGTCTCCCGC TCCGCCTGCT TGTGACCTCC GAGTCCTCAG TAAACTGCT 600 CGTGACTCCC ATGTCCTTCA CAGCAGACTG AGCCAGTGCC CAGAGGTTCA CCCTTTGCC 660 ACACCTGTCC TGCTGCCTGC TGTGGACTTT AGCTTGGGAG AATGGAAAAC CCAGATGGA 720 GAGACCAAGG CACAGGACAT TCTGGGAGCA GTGACCCTTC TGCTGGAGGG AGTGATGGC 780 GCACGGGGAC AACTGGGACC CACTTGCCTC TCATCCCTCC TGGGGCAGCT TTCTGGACA 840 GTCCGTCTCC TCCTTGGGGC CCTGCAGAGC CTCCTTGGAA CCCAGGGCAG GACCACAGC 900 CACAAG 906 993 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 155 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGATCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC CGTCTCCTCC GTCTAAAGA 420 TCTCATAAAT CTCCAAACAT GTCTTACAAG CTGTGCCACC CCGAGGAGCT GGTGCTGCT 480 GGACACTCTC TGGGCATCCC CTGGGCTCCC CTGAGCTCCT GCCCCAGCCA GGCCCTGCA 540 CTGGCAGGCT GCTTGAGCCA ACTCCATAGC GGCCTTTTCC TCTACCAGGG GCTCCTGCA 600 GCCCTGGAAG GGATATCCCC CGAGTTGGGT CCCACCTTGG ACACACTGCA GCTGGACGT 660 GCCGACTTTG CCACCACCAT CTGGCAGCAG ATGGAAGAAC TGGGAATGGC CCCTGCCCT 720 CAGCCCACCC AGGGTGCCAT GCCGGCCTTC GCCTCTGCTT TCCAGCGCCG GGCAGGAGG 780 GTCCTGGTTG CTAGCCATCT GCAGAGCTTC CTGGAGGTGT CGTACCGCGT TCTACGCCA 840 CTTGCGCAGC CCGGCGGCGG CTCTGACATG GCTACACCAT TAGGCCCTGC CAGCTCCCT 900 CCCCAGAGCT TCCTGCTCAA GTCTTTAGAG CAAGTGAGGA AGATCCAGGG CGATGGCGC 960 GCGCTCCAGG AGAAGCTGTG TGCCACCTAA TAA 993 993 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 156 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGATCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC CGTCTCCTCC GTCTAAAGA 420 TCTCATAAAT CTCCAAACAT GTCTCCCGAG TTGGGTCCCA CCTTGGACAC ACTGCAGCT 480 GACGTCGCCG ACTTTGCCAC CACCATCTGG CAGCAGATGG AAGAACTGGG AATGGCCCC 540 GCCCTGCAGC CCACCCAGGG TGCCATGCCG GCCTTCGCCT CTGCTTTCCA GCGCCGGGC 600 GGAGGGGTCC TGGTTGCTAG CCATCTGCAG AGCTTCCTGG AGGTGTCGTA CCGCGTTCT 660 CGCCACCTTG CGCAGCCCGG CGGCGGCTCT GACATGGCTA CACCATTAGG CCCTGCCAG 720 TCCCTGCCCC AGAGCTTCCT GCTCAAGTCT TTAGAGCAAG TGAGGAAGAT CCAGGGCGA 780 GGCGCAGCGC TCCAGGAGAA GCTGTGTGCC ACCTACAAGC TGTGCCACCC CGAGGAGCT 840 GTGCTGCTCG GACACTCTCT GGGCATCCCC TGGGCTCCCC TGAGCTCCTG CCCCAGCCA 900 GCCCTGCAGC TGGCAGGCTG CTTGAGCCAA CTCCATAGCG GCCTTTTCCT CTACCAGGG 960 CTCCTGCAGG CCCTGGAAGG GATATCCTAA TAA 993 993 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 157 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGATCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC CGTCTCCTCC GTCTAAAGA 420 TCTCATAAAT CTCCAAACAT GTCTTCTGCT TTCCAGCGCC GGGCAGGAGG GGTCCTGGT 480 GCTAGCCATC TGCAGAGCTT CCTGGAGGTG TCGTACCGCG TTCTACGCCA CCTTGCGCA 540 CCCGGCGGCG GCTCTGACAT GGCTACACCA TTAGGCCCTG CCAGCTCCCT GCCCCAGAG 600 TTCCTGCTCA AGTCTTTAGA GCAAGTGAGG AAGATCCAGG GCGATGGCGC AGCGCTCCA 660 GAGAAGCTGT GTGCCACCTA CAAGCTGTGC CACCCCGAGG AGCTGGTGCT GCTCGGACA 720 TCTCTGGGCA TCCCCTGGGC TCCCCTGAGC TCCTGCCCCA GCCAGGCCCT GCAGCTGGC 780 GGCTGCTTGA GCCAACTCCA TAGCGGCCTT TTCCTCTACC AGGGGCTCCT GCAGGCCCT 840 GAAGGGATAT CCCCCGAGTT GGGTCCCACC TTGGACACAC TGCAGCTGGA CGTCGCCGA 900 TTTGCCACCA CCATCTGGCA GCAGATGGAA GAACTGGGAA TGGCCCCTGC CCTGCAGCC 960 ACCCAGGGTG CCATGCCGGC CTTCGCCTAA TAA 993 993 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 158 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGATCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC CGTCTCCTCC GTCTAAAGA 420 TCTCATAAAT CTCCAAACAT GTCTATGGCC CCTGCCCTGC AGCCCACCCA GGGTGCCAT 480 CCGGCCTTCG CCTCTGCTTT CCAGCGCCGG GCAGGAGGGG TCCTGGTTGC TAGCCATCT 540 CAGAGCTTCC TGGAGGTGTC GTACCGCGTT CTACGCCACC TTGCGCAGCC CGGCGGCGG 600 TCTGACATGG CTACACCATT AGGCCCTGCC AGCTCCCTGC CCCAGAGCTT CCTGCTCAA 660 TCTTTAGAGC AAGTGAGGAA GATCCAGGGC GATGGCGCAG CGCTCCAGGA GAAGCTGTG 720 GCCACCTACA AGCTGTGCCA CCCCGAGGAG CTGGTGCTGC TCGGACACTC TCTGGGCAT 780 CCCTGGGCTC CCCTGAGCTC CTGCCCCAGC CAGGCCCTGC AGCTGGCAGG CTGCTTGAG 840 CAACTCCATA GCGGCCTTTT CCTCTACCAG GGGCTCCTGC AGGCCCTGGA AGGGATATC 900 CCCGAGTTGG GTCCCACCTT GGACACACTG CAGCTGGACG TCGCCGACTT TGCCACCAC 960 ATCTGGCAGC AGATGGAAGA ACTGGGATAA TAA 993 993 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 159 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGATCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC CGTCTCCTCC GTCTAAAGA 420 TCTCATAAAT CTCCAAACAT GTCTACCCAG GGTGCCATGC CGGCCTTCGC CTCTGCTTT 480 CAGCGCCGGG CAGGAGGGGT CCTGGTTGCT AGCCATCTGC AGAGCTTCCT GGAGGTGTC 540 TACCGCGTTC TACGCCACCT TGCGCAGCCC GGCGGCGGCT CTGACATGGC TACACCATT 600 GGCCCTGCCA GCTCCCTGCC CCAGAGCTTC CTGCTCAAGT CTTTAGAGCA AGTGAGGAA 660 ATCCAGGGCG ATGGCGCAGC GCTCCAGGAG AAGCTGTGTG CCACCTACAA GCTGTGCCA 720 CCCGAGGAGC TGGTGCTGCT CGGACACTCT CTGGGCATCC CCTGGGCTCC CCTGAGCTC 780 TGCCCCAGCC AGGCCCTGCA GCTGGCAGGC TGCTTGAGCC AACTCCATAG CGGCCTTTT 840 CTCTACCAGG GGCTCCTGCA GGCCCTGGAA GGGATATCCC CCGAGTTGGG TCCCACCTT 900 GACACACTGC AGCTGGACGT CGCCGACTTT GCCACCACCA TCTGGCAGCA GATGGAAGA 960 CTGGGAATGG CCCCTGCCCT GCAGCCCTAA TAA 993 1027 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 160 ATGGCTACAC CATTGGGCCC TGCCAGCTCC CTGCCCCAGA GCTTCCTGCT CAAGTCTTTA 60 GAGCAAGTGA GGAAGATCCA GGGCGATGGC GCAGCGCTCC AGGAGAAGCT GTGTGCCAC 120 TACAAGCTGT GCCACCCCGA GGAGCTGGTG CTGCTCGGAC ACTCTCTGGG CATCCCCTG 180 GCTCCCCTGA GCTCCTGCCC CAGCCAGGCC CTGCAGCTGG CAGGCTGCTT GAGCCAACT 240 CATAGCGGCC TTTTCCTCTA CCAGGGGCTC CTGCAGGCCC TGGAAGGGAT ATCCCCCGA 300 TTGGGTCCCA CCTTGGACAC ACTGCAGCTG GACGTCGCCG ACTTTGCCAC CACCATCTG 360 CAGCAGATGG AAGAACTGGG AATGGCCCCT GCCCTGCAGC CCACCCAGGG TGCCATGCC 420 GCCTTCGCCT CTGCTTTCCA GCGCCGGGCA GGAGGGGTCC TGGTTGCTAG CCATCTGCA 480 AGCTTCCTGG AGGTGTCGTA CCGCGTTCTA CGCCACCTTG CGCAGCCCGG CGGCGGCTC 540 GACATGGCTA CACCATTGGG CCCTGCCAGC TCCCTGCCCC AGAGCTTCCT GCTCAAGTC 600 TTAGAGCAAG TGAGGAAGAT CCAGGGCGAT GGCGCAGCGC TCCAGGAGAA GCTGTGTGC 660 ACCTACAAGC TGTGCCACCC CGAGGAGCTG GTGCTGCTCG GACACTCTCT GGGCATCCC 720 TGGGCTCCCC TGAGCTCCTG CCCCAGCCAG GCCCTGCAGC TGGCAGGCTG CTTGAGCCA 780 CTCCATAGCG GCCTTTTCCT CTACCAGGGG CTCCTGCAGG CCCTGGAAGG GATATCCCC 840 GAGTTGGGTC CCACCTTGGA CACACTGCAG CTGGACGTCG CCGACTTTGC CACCACCAT 900 TGGCAGCAGA TGGAAGAACT GGGAATGGCC CCTGCCCTGC AGCCCACCCA TCCTGGTTG 960 TAGCCATCTG CAGAGCTTCC TGGAGGTGTC GTACCGCGTT CTACGCCACC TTGCGCAG 1020 CTGATAA 1027 155 amino acids amino acid unknown unknown peptide 161 Ser Pro Ala Pro Pro Ala Cys Asp Leu Arg Val Leu Ser Lys Leu Le 1 5 10 15 Arg Asp Ser His Val Leu His Ser Arg Leu Ser Gln Cys Pro Glu Va 20 25 30 His Pro Leu Pro Thr Pro Val Leu Leu Pro Ala Val Asp Phe Ser Le 35 40 45 Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln Asp Ile Le 50 55 60 Gly Ala Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Arg Gly Gl 65 70 75 80 Leu Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gly Gl 85 90 95 Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Thr Gln Le 100 105 110 Pro Pro Gln Gly Arg Thr Thr Ala His Lys Asp Pro Asn Ala Ile Ph 115 120 125 Leu Ser Phe Gln His Leu Leu Arg Gly Lys Val Arg Phe Leu Met Le 130 135 140 Val Gly Gly Ser Thr Leu Cys Val Arg Glu Phe 145 150 155 309 amino acids amino acid unknown unknown peptide 162 Ser Pro Ala Pro Pro Ala Cys Asp Leu Arg Val Leu Ser Lys Leu Le 1 5 10 15 Arg Asp Ser His Val Leu His Ser Arg Leu Ser Gln Cys Pro Glu Va 20 25 30 His Pro Leu Pro Thr Pro Val Leu Leu Pro Ala Val Asp Phe Ser Le 35 40 45 Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln Asp Ile Le 50 55 60 Gly Ala Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Arg Gly Gl 65 70 75 80 Leu Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gly Gl 85 90 95 Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Thr Gln Le 100 105 110 Pro Pro Gln Gly Arg Thr Thr Ala His Lys Asp Pro Asn Ala Ile Ph 115 120 125 Leu Ser Phe Gln His Leu Leu Arg Gly Lys Val Arg Phe Leu Met Le 130 135 140 Val Gly Gly Ser Thr Leu Cys Val Arg Glu Phe Gly Gly Asn Met Al 145 150 155 160 Ser Pro Ala Pro Pro Ala Cys Asp Leu Arg Val Leu Ser Lys Leu Le 165 170 175 Arg Asp Ser His Val Leu His Ser Arg Leu Ser Gln Cys Pro Glu Va 180 185 190 His Pro Leu Pro Thr Pro Val Leu Leu Pro Ala Val Asp Phe Ser Le 195 200 205 Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln Asp Ile Le 210 215 220 Gly Ala Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Arg Gly Gl 225 230 235 240 Leu Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gly Gl 245 250 255 Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Thr Gln Gl 260 265 270 Arg Thr Thr Ala His Lys Asp Pro Asn Ala Ile Phe Leu Ser Phe Gl 275 280 285 His Leu Leu Arg Gly Lys Val Arg Phe Leu Met Leu Val Gly Gly Se 290 295 300 Thr Leu Cys Val Arg 305 312 amino acids amino acid unknown unknown peptide 163 Ser Pro Ala Pro Pro Ala Cys Asp Leu Arg Val Leu Ser Lys Leu Le 1 5 10 15 Arg Asp Ser His Val Leu His Ser Arg Leu Ser Gln Cys Pro Glu Va 20 25 30 His Pro Leu Pro Thr Pro Val Leu Leu Pro Ala Val Asp Phe Ser Le 35 40 45 Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln Asp Ile Le 50 55 60 Gly Ala Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Arg Gly Gl 65 70 75 80 Leu Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gly Gl 85 90 95 Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Thr Gln Le 100 105 110 Pro Pro Gln Gly Arg Thr Thr Ala His Lys Asp Pro Asn Ala Ile Ph 115 120 125 Leu Ser Phe Gln His Leu Leu Arg Gly Lys Val Arg Phe Leu Met Le 130 135 140 Val Gly Gly Ser Thr Leu Cys Val Arg Glu Phe Gly Asn Met Ala Se 145 150 155 160 Pro Ala Pro Pro Ala Cys Asp Leu Arg Val Leu Ser Lys Leu Leu Ar 165 170 175 Asp Ser His Val Leu His Ser Arg Leu Ser Gln Cys Pro Glu Val Hi 180 185 190 Pro Leu Pro Thr Pro Val Leu Leu Pro Ala Val Asp Phe Ser Leu Gl 195 200 205 Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln Asp Ile Leu Gl 210 215 220 Ala Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Arg Gly Gln Le 225 230 235 240 Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gly Gln Va 245 250 255 Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Thr Gln Leu Pr 260 265 270 Pro Gln Gly Arg Thr Thr Ala His Lys Asp Pro Asn Ala Ile Phe Le 275 280 285 Ser Phe Gln His Leu Leu Arg Gly Lys Val Arg Phe Leu Met Leu Va 290 295 300 Gly Gly Ser Thr Leu Cys Val Arg 305 310 313 amino acids amino acid unknown unknown peptide 164 Ser Pro Ala Pro Pro Ala Cys Asp Leu Arg Val Leu Ser Lys Leu Le 1 5 10 15 Arg Asp Ser His Val Leu His Ser Arg Leu Ser Gln Cys Pro Glu Va 20 25 30 His Pro Leu Pro Thr Pro Val Leu Leu Pro Ala Val Asp Phe Ser Le 35 40 45 Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln Asp Ile Le 50 55 60 Gly Ala Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Arg Gly Gl 65 70 75 80 Leu Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gly Gl 85 90 95 Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Thr Gln Le 100 105 110 Pro Pro Gln Gly Arg Thr Thr Ala His Lys Asp Pro Asn Ala Ile Ph 115 120 125 Leu Ser Phe Gln His Leu Leu Arg Gly Lys Val Arg Phe Leu Met Le 130 135 140 Val Gly Gly Ser Thr Leu Cys Val Arg Glu Phe Gly Gly Asn Met Al 145 150 155 160 Ser Pro Ala Pro Pro Ala Cys Asp Leu Arg Val Leu Ser Lys Leu Le 165 170 175 Arg Asp Ser His Val Leu His Ser Arg Leu Ser Gln Cys Pro Glu Va 180 185 190 His Pro Leu Pro Thr Pro Val Leu Leu Pro Ala Val Asp Phe Ser Le 195 200 205 Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln Asp Ile Le 210 215 220 Gly Ala Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Arg Gly Gl 225 230 235 240 Leu Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gly Gl 245 250 255 Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Thr Gln Le 260 265 270 Pro Pro Gln Gly Arg Thr Thr Ala His Lys Asp Pro Asn Ala Ile Ph 275 280 285 Leu Ser Phe Gln His Leu Leu Arg Gly Lys Val Arg Phe Leu Met Le 290 295 300 Val Gly Gly Ser Thr Leu Cys Val Arg 305 310 316 amino acids amino acid unknown unknown peptide 165 Ser Pro Ala Pro Pro Ala Cys Asp Leu Arg Val Leu Ser Lys Leu Le 1 5 10 15 Arg Asp Ser His Val Leu His Ser Arg Leu Ser Gln Cys Pro Glu Va 20 25 30 His Pro Leu Pro Thr Pro Val Leu Leu Pro Ala Val Asp Phe Ser Le 35 40 45 Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln Asp Ile Le 50 55 60 Gly Ala Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Arg Gly Gl 65 70 75 80 Leu Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gly Gl 85 90 95 Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Thr Gln Le 100 105 110 Pro Pro Gln Gly Arg Thr Thr Ala His Lys Asp Pro Asn Ala Ile Ph 115 120 125 Leu Ser Phe Gln His Leu Leu Arg Gly Lys Val Arg Phe Leu Met Le 130 135 140 Val Gly Gly Ser Thr Leu Cys Val Arg Glu Phe Gly Gly Asn Gly Gl 145 150 155 160 Asn Met Ala Ser Pro Ala Pro Pro Ala Cys Asp Leu Arg Val Leu Se 165 170 175 Lys Leu Leu Arg Asp Ser His Val Leu His Ser Arg Leu Ser Gln Cy 180 185 190 Pro Glu Val His Pro Leu Pro Thr Pro Val Leu Leu Pro Ala Val As 195 200 205 Phe Ser Leu Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gl 210 215 220 Asp Ile Leu Gly Ala Val Thr Leu Leu Leu Glu Gly Val Met Ala Al 225 230 235 240 Arg Gly Gln Leu Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Le 245 250 255 Ser Gly Gln Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gl 260 265 270 Thr Gln Leu Pro Pro Gln Gly Arg Thr Thr Ala His Lys Asp Pro As 275 280 285 Ala Ile Phe Leu Ser Phe Gln His Leu Leu Arg Gly Lys Val Arg Ph 290 295 300 Leu Met Leu Val Gly Gly Ser Thr Leu Cys Val Arg 305 310 315 302 amino acids amino acid unknown unknown peptide 166 Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg Pr 1 5 10 15 Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Se 20 25 30 Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Va 35 40 45 Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Le 50 55 60 Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Ar 65 70 75 80 His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Ly 85 90 95 Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Ty 100 105 110 Val Glu Gly Gly Gly Gly Ser Pro Gly Gly Gly Ser Gly Gly Gly Se 115 120 125 Asn Met Ala Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gl 130 135 140 His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gl 145 150 155 160 Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Ph 165 170 175 Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Le 180 185 190 Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Th 195 200 205 Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gl 210 215 220 Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Ar 225 230 235 240 Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Va 245 250 255 Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Ser Gly Gly Ser Gl 260 265 270 Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Il 275 280 285 Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr 290 295 300 317 amino acids amino acid unknown unknown peptide 167 Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg Pr 1 5 10 15 Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Se 20 25 30 Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Va 35 40 45 Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Le 50 55 60 Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Ar 65 70 75 80 His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Ly 85 90 95 Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Ty 100 105 110 Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Se 115 120 125 Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro As 130 135 140 Met Ala Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly Hi 145 150 155 160 Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Al 165 170 175 Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Le 180 185 190 Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gl 195 200 205 Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Th 210 215 220 Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pr 225 230 235 240 Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Al 245 250 255 Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Se 260 265 270 Tyr Arg Val Leu Arg His Leu Ala Gln Pro Ser Gly Gly Ser Gly Gl 275 280 285 Ser Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gl 290 295 300 Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr 305 310 315 302 amino acids amino acid unknown unknown peptide 168 Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg Pr 1 5 10 15 Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Se 20 25 30 Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Va 35 40 45 Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Le 50 55 60 Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Ar 65 70 75 80 His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Ly 85 90 95 Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Ty 100 105 110 Val Glu Gly Gly Gly Gly Ser Pro Gly Gly Gly Ser Gly Gly Gly Se 115 120 125 Asn Met Ala Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu As 130 135 140 Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gl 145 150 155 160 Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Al 165 170 175 Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Le 180 185 190 Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gl 195 200 205 Pro Ser Gly Gly Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Le 210 215 220 Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Ly 225 230 235 240 Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Le 245 250 255 Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Se 260 265 270 Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Le 275 280 285 Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser 290 295 300 317 amino acids amino acid unknown unknown peptide 169 Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg Pr 1 5 10 15 Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Se 20 25 30 Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Va 35 40 45 Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Le 50 55 60 Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Ar 65 70 75 80 His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Ly 85 90 95 Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Ty 100 105 110 Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Se 115 120 125 Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro As 130 135 140 Met Ala Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Va 145 150 155 160 Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Me 165 170 175 Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Se 180 185 190 Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gl 195 200 205 Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pr 210 215 220 Ser Gly Gly Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Gl 225 230 235 240 Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Le 245 250 255 Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gl 260 265 270 His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gl 275 280 285 Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Ph 290 295 300 Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser 305 310 315 302 amino acids amino acid unknown unknown peptide 170 Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg Pr 1 5 10 15 Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Se 20 25 30 Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Va 35 40 45 Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Le 50 55 60 Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Ar 65 70 75 80 His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Ly 85 90 95 Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Ty 100 105 110 Val Glu Gly Gly Gly Gly Ser Pro Gly Gly Gly Ser Gly Gly Gly Se 115 120 125 Asn Met Ala Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pr 130 135 140 Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Al 145 150 155 160 Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg Hi 165 170 175 Leu Ala Gln Pro Ser Gly Gly Ser Gly Gly Ser Gln Ser Phe Leu Le 180 185 190 Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Le 195 200 205 Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Le 210 215 220 Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Se 225 230 235 240 Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu Hi 245 250 255 Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Il 260 265 270 Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Al 275 280 285 Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly 290 295 300 317 amino acids amino acid unknown unknown peptide 171 Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg Pr 1 5 10 15 Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Se 20 25 30 Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Va 35 40 45 Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Le 50 55 60 Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Ar 65 70 75 80 His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Ly 85 90 95 Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Ty 100 105 110 Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Se 115 120 125 Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro As 130 135 140 Met Ala Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Al 145 150 155 160 Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Se 165 170 175 His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Le 180 185 190 Ala Gln Pro Ser Gly Gly Ser Gly Gly Ser Gln Ser Phe Leu Leu Ly 195 200 205 Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gl 210 215 220 Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Va 225 230 235 240 Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cy 245 250 255 Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Se 260 265 270 Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Se 275 280 285 Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala As 290 295 300 Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly 305 310 315 302 amino acids amino acid unknown unknown peptide 172 Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg Pr 1 5 10 15 Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Se 20 25 30 Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Va 35 40 45 Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Le 50 55 60 Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Ar 65 70 75 80 His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Ly 85 90 95 Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Ty 100 105 110 Val Glu Gly Gly Gly Gly Ser Pro Gly Gly Gly Ser Gly Gly Gly Se 115 120 125 Asn Met Ala Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gl 130 135 140 Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Le 145 150 155 160 Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Ser Gly Gl 165 170 175 Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Ar 180 185 190 Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Th 195 200 205 Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Le 210 215 220 Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gl 225 230 235 240 Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gl 245 250 255 Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Th 260 265 270 Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Tr 275 280 285 Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro 290 295 300 317 amino acids amino acid unknown unknown peptide 173 Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg Pr 1 5 10 15 Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Se 20 25 30 Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Va 35 40 45 Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Le 50 55 60 Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Ar 65 70 75 80 His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Ly 85 90 95 Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Ty 100 105 110 Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Se 115 120 125 Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro As 130 135 140 Met Ala Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Ar 145 150 155 160 Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Gl 165 170 175 Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Ser Gly Gly Se 180 185 190 Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Ly 195 200 205 Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Ty 210 215 220 Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gl 225 230 235 240 Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Le 245 250 255 Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gl 260 265 270 Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Le 275 280 285 Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gl 290 295 300 Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro 305 310 315 302 amino acids amino acid unknown unknown peptide 174 Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg Pr 1 5 10 15 Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Se 20 25 30 Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Va 35 40 45 Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Le 50 55 60 Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Ar 65 70 75 80 His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Ly 85 90 95 Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Ty 100 105 110 Val Glu Gly Gly Gly Gly Ser Pro Gly Gly Gly Ser Gly Gly Gly Se 115 120 125 Asn Met Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Al 130 135 140 Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg Hi 145 150 155 160 Leu Ala Gln Pro Ser Gly Gly Ser Gly Gly Ser Gln Ser Phe Leu Le 165 170 175 Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Le 180 185 190 Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Le 195 200 205 Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Se 210 215 220 Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu Hi 225 230 235 240 Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Il 245 250 255 Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Al 260 265 270 Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Al 275 280 285 Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala 290 295 300 317 amino acids amino acid unknown unknown peptide 175 Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg Pr 1 5 10 15 Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Se 20 25 30 Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Va 35 40 45 Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Le 50 55 60 Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Ar 65 70 75 80 His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Ly 85 90 95 Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Ty 100 105 110 Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Se 115 120 125 Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro As 130 135 140 Met Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Se 145 150 155 160 His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Le 165 170 175 Ala Gln Pro Ser Gly Gly Ser Gly Gly Ser Gln Ser Phe Leu Leu Ly 180 185 190 Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gl 195 200 205 Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Va 210 215 220 Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cy 225 230 235 240 Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Se 245 250 255 Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Se 260 265 270 Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala As 275 280 285 Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pr 290 295 300 Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala 305 310 315 305 amino acids amino acid unknown unknown peptide 176 Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg Pr 1 5 10 15 Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Se 20 25 30 Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Va 35 40 45 Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Le 50 55 60 Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Ar 65 70 75 80 His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Ly 85 90 95 Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Ty 100 105 110 Val Glu Gly Gly Gly Gly Ser Pro Gly Gly Gly Ser Gly Gly Gly Se 115 120 125 Asn Met Ala Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gl 130 135 140 His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gl 145 150 155 160 Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Ph 165 170 175 Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Le 180 185 190 Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Th 195 200 205 Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gl 210 215 220 Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Ar 225 230 235 240 Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Va 245 250 255 Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Thr Pro Leu Gly Pr 260 265 270 Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Va 275 280 285 Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Al 290 295 300 Thr 305 320 amino acids amino acid unknown unknown peptide 177 Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg Pr 1 5 10 15 Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Se 20 25 30 Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Va 35 40 45 Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Le 50 55 60 Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Ar 65 70 75 80 His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Ly 85 90 95 Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Ty 100 105 110 Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Se 115 120 125 Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro As 130 135 140 Met Ala Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly Hi 145 150 155 160 Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Al 165 170 175 Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Le 180 185 190 Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gl 195 200 205 Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Th 210 215 220 Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pr 225 230 235 240 Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Al 245 250 255 Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Se 260 265 270 Tyr Arg Val Leu Arg His Leu Ala Gln Pro Thr Pro Leu Gly Pro Al 275 280 285 Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Ar 290 295 300 Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Th 305 310 315 320 305 amino acids amino acid unknown unknown peptide 178 Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg Pr 1 5 10 15 Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Se 20 25 30 Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Va 35 40 45 Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Le 50 55 60 Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Ar 65 70 75 80 His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Ly 85 90 95 Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Ty 100 105 110 Val Glu Gly Gly Gly Gly Ser Pro Gly Gly Gly Ser Gly Gly Gly Se 115 120 125 Asn Met Ala Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu As 130 135 140 Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gl 145 150 155 160 Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Al 165 170 175 Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Le 180 185 190 Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gl 195 200 205 Pro Thr Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Le 210 215 220 Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Le 225 230 235 240 Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Le 245 250 255 Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Se 260 265 270 Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu Hi 275 280 285 Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Il 290 295 300 Ser 305 320 amino acids amino acid unknown unknown peptide 179 Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg Pr 1 5 10 15 Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Se 20 25 30 Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Va 35 40 45 Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Le 50 55 60 Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Ar 65 70 75 80 His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Ly 85 90 95 Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Ty 100 105 110 Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Se 115 120 125 Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro As 130 135 140 Met Ala Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Va 145 150 155 160 Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Me 165 170 175 Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Se 180 185 190 Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gl 195 200 205 Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pr 210 215 220 Thr Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Ly 225 230 235 240 Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gl 245 250 255 Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Va 260 265 270 Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cy 275 280 285 Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Se 290 295 300 Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Se 305 310 315 320 305 amino acids amino acid unknown unknown peptide 180 Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg Pr 1 5 10 15 Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Se 20 25 30 Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Va 35 40 45 Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Le 50 55 60 Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Ar 65 70 75 80 His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Ly 85 90 95 Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Ty 100 105 110 Val Glu Gly Gly Gly Gly Ser Pro Gly Gly Gly Ser Gly Gly Gly Se 115 120 125 Asn Met Ala Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pr 130 135 140 Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Al 145 150 155 160 Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg Hi 165 170 175 Leu Ala Gln Pro Thr Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Se 180 185 190 Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gl 195 200 205 Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pr 210 215 220 Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pr 225 230 235 240 Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Se 245 250 255 Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Le 260 265 270 Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Le 275 280 285 Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Le 290 295 300 Gly 305 320 amino acids amino acid unknown unknown peptide 181 Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg Pr 1 5 10 15 Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Se 20 25 30 Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Va 35 40 45 Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Le 50 55 60 Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Ar 65 70 75 80 His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Ly 85 90 95 Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Ty 100 105 110 Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Se 115 120 125 Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro As 130 135 140 Met Ala Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Al 145 150 155 160 Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Se 165 170 175 His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Le 180 185 190 Ala Gln Pro Thr Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Ph 195 200 205 Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Al 210 215 220 Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Gl 225 230 235 240 Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Le 245 250 255 Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gl 260 265 270 Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Gl 275 280 285 Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu As 290 295 300 Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gl 305 310 315 320 305 amino acids amino acid unknown unknown peptide 182 Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg Pr 1 5 10 15 Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Se 20 25 30 Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Va 35 40 45 Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Le 50 55 60 Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Ar 65 70 75 80 His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Ly 85 90 95 Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Ty 100 105 110 Val Glu Gly Gly Gly Gly Ser Pro Gly Gly Gly Ser Gly Gly Gly Se 115 120 125 Asn Met Ala Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gl 130 135 140 Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Le 145 150 155 160 Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Thr Pro Le 165 170 175 Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu Gl 180 185 190 Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Le 195 200 205 Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gl 210 215 220 His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gl 225 230 235 240 Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Ph 245 250 255 Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Le 260 265 270 Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Th 275 280 285 Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gl 290 295 300 Pro 305 320 amino acids amino acid unknown unknown peptide 183 Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg Pr 1 5 10 15 Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Se 20 25 30 Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Va 35 40 45 Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Le 50 55 60 Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Ar 65 70 75 80 His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Ly 85 90 95 Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Ty 100 105 110 Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Se 115 120 125 Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro As 130 135 140 Met Ala Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Ar 145 150 155 160 Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Gl 165 170 175 Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Thr Pro Leu Gl 180 185 190 Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu Gl 195 200 205 Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cy 210 215 220 Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly Hi 225 230 235 240 Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Al 245 250 255 Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Le 260 265 270 Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gl 275 280 285 Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Th 290 295 300 Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pr 305 310 315 320 305 amino acids amino acid unknown unknown peptide 184 Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg Pr 1 5 10 15 Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Se 20 25 30 Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Va 35 40 45 Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Le 50 55 60 Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Ar 65 70 75 80 His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Ly 85 90 95 Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Ty 100 105 110 Val Glu Gly Gly Gly Gly Ser Pro Gly Gly Gly Ser Gly Gly Gly Se 115 120 125 Asn Met Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Al 130 135 140 Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg Hi 145 150 155 160 Leu Ala Gln Pro Thr Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Se 165 170 175 Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gl 180 185 190 Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pr 195 200 205 Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pr 210 215 220 Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Se 225 230 235 240 Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Le 245 250 255 Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Le 260 265 270 Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Le 275 280 285 Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Ph 290 295 300 Ala 305 320 amino acids amino acid unknown unknown peptide 185 Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg Pr 1 5 10 15 Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Se 20 25 30 Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Va 35 40 45 Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Le 50 55 60 Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Ar 65 70 75 80 His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Ly 85 90 95 Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Ty 100 105 110 Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Se 115 120 125 Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro As 130 135 140 Met Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Se 145 150 155 160 His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Le 165 170 175 Ala Gln Pro Thr Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Ph 180 185 190 Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Al 195 200 205 Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Gl 210 215 220 Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Le 225 230 235 240 Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gl 245 250 255 Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Gl 260 265 270 Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu As 275 280 285 Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gl 290 295 300 Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Al 305 310 315 320 321 amino acids amino acid unknown unknown peptide 186 Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met As 1 5 10 15 Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Ly 20 25 30 Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gl 35 40 45 Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Il 50 55 60 Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Ty 65 70 75 80 Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Gly Gly Gly Ser As 85 90 95 Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg Pro Pr 100 105 110 Ala Pro Leu Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Se 115 120 125 Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser Hi 130 135 140 Lys Ser Pro Asn Met Ala Thr Gln Gly Ala Met Pro Ala Phe Ala Se 145 150 155 160 Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gl 165 170 175 Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pr 180 185 190 Ser Gly Gly Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Gl 195 200 205 Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Le 210 215 220 Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gl 225 230 235 240 His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gl 245 250 255 Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Ph 260 265 270 Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Le 275 280 285 Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Th 290 295 300 Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gl 305 310 315 320 Pro 321 amino acids amino acid unknown unknown peptide 187 Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Le 1 5 10 15 Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Al 20 25 30 Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Th 35 40 45 Leu Glu Gln Ala Gln Glu Gln Gln Gly Gly Gly Ser Asn Cys Ser Il 50 55 60 Met Ile Asp Glu Ile Ile His His Leu Lys Arg Pro Pro Ala Pro Le 65 70 75 80 Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met As 85 90 95 Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Ly 100 105 110 Asn Leu Glu Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Se 115 120 125 Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser Hi 130 135 140 Lys Ser Pro Asn Met Ala Thr Gln Gly Ala Met Pro Ala Phe Ala Se 145 150 155 160 Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gl 165 170 175 Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pr 180 185 190 Ser Gly Gly Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Gl 195 200 205 Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Le 210 215 220 Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gl 225 230 235 240 His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gl 245 250 255 Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Ph 260 265 270 Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Le 275 280 285 Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Th 290 295 300 Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gl 305 310 315 320 Pro 321 amino acids amino acid unknown unknown peptide 188 Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Gl 1 5 10 15 Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gl 20 25 30 Glu Gln Gln Gly Gly Gly Ser Asn Cys Ser Ile Met Ile Asp Glu Il 35 40 45 Ile His His Leu Lys Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn As 50 55 60 Leu Asn Asp Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Le 65 70 75 80 Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Al 85 90 95 Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Se 100 105 110 Ala Thr Ala Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Se 115 120 125 Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser Hi 130 135 140 Lys Ser Pro Asn Met Ala Thr Gln Gly Ala Met Pro Ala Phe Ala Se 145 150 155 160 Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gl 165 170 175 Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pr 180 185 190 Ser Gly Gly Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Gl 195 200 205 Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Le 210 215 220 Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gl 225 230 235 240 His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gl 245 250 255 Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Ph 260 265 270 Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Le 275 280 285 Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Th 290 295 300 Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gl 305 310 315 320 Pro 321 amino acids amino acid unknown unknown peptide 189 Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Va 1 5 10 15 Thr Leu Glu Gln Ala Gln Glu Gln Gln Gly Gly Gly Ser Asn Cys Se 20 25 30 Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg Pro Pro Ala Pr 35 40 45 Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Me 50 55 60 Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Va 65 70 75 80 Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Le 85 90 95 Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Il 100 105 110 Ile Ile Lys Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Se 115 120 125 Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser Hi 130 135 140 Lys Ser Pro Asn Met Ala Thr Gln Gly Ala Met Pro Ala Phe Ala Se 145 150 155 160 Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gl 165 170 175 Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pr 180 185 190 Ser Gly Gly Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Gl 195 200 205 Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Le 210 215 220 Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gl 225 230 235 240 His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gl 245 250 255 Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Ph 260 265 270 Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Le 275 280 285 Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Th 290 295 300 Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gl 305 310 315 320 Pro 329 amino acids amino acid unknown unknown peptide 190 Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met As 1 5 10 15 Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Ly 20 25 30 Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gl 35 40 45 Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Il 50 55 60 Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Ty 65 70 75 80 Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Gly Gly Gly Ser Gl 85 90 95 Gly Gly Ser Gly Gly Gly Ser Asn Cys Ser Ile Met Ile Asp Glu Il 100 105 110 Ile His His Leu Lys Arg Pro Pro Ala Pro Leu Tyr Val Glu Gly Gl 115 120 125 Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pr 130 135 140 Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Thr Gl 145 150 155 160 Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gl 165 170 175 Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Ar 180 185 190 Val Leu Arg His Leu Ala Gln Pro Ser Gly Gly Ser Gly Gly Ser Gl 195 200 205 Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly As 210 215 220 Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys Hi 225 230 235 240 Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Al 245 250 255 Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Le 260 265 270 Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Al 275 280 285 Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gl 290 295 300 Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Gl 305 310 315 320 Leu Gly Met Ala Pro Ala Leu Gln Pro 325 329 amino acids amino acid unknown unknown peptide 191 Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Le 1 5 10 15 Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Al 20 25 30 Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Th 35 40 45 Leu Glu Gln Ala Gln Glu Gln Gln Gly Gly Gly Ser Gly Gly Gly Se 50 55 60 Gly Gly Gly Ser Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His Hi 65 70 75 80 Leu Lys Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn As 85 90 95 Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Le 100 105 110 Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Tyr Val Glu Gly Gl 115 120 125 Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pr 130 135 140 Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Thr Gl 145 150 155 160 Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gl 165 170 175 Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Ar 180 185 190 Val Leu Arg His Leu Ala Gln Pro Ser Gly Gly Ser Gly Gly Ser Gl 195 200 205 Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly As 210 215 220 Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys Hi 225 230 235 240 Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Al 245 250 255 Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Le 260 265 270 Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Al 275 280 285 Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gl 290 295 300 Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Gl 305 310 315 320 Leu Gly Met Ala Pro Ala Leu Gln Pro 325 329 amino acids amino acid unknown unknown peptide 192 Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Gl 1 5 10 15 Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gl 20 25 30 Glu Gln Gln Gly Gly Gly Ser Gly Gly Gly Ser Gly Gly Gly Ser As 35 40 45 Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg Pro Pr 50 55 60 Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Il 65 70 75 80 Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Ar 85 90 95 Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Ar 100 105 110 Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Tyr Val Glu Gly Gl 115 120 125 Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pr 130 135 140 Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Thr Gl 145 150 155 160 Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gl 165 170 175 Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Ar 180 185 190 Val Leu Arg His Leu Ala Gln Pro Ser Gly Gly Ser Gly Gly Ser Gl 195 200 205 Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly As 210 215 220 Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys Hi 225 230 235 240 Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Al 245 250 255 Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Le 260 265 270 Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Al 275 280 285 Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gl 290 295 300 Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Gl 305 310 315 320 Leu Gly Met Ala Pro Ala Leu Gln Pro 325 299 amino acids amino acid unknown unknown peptide 193 Gly Gly Ser Gly Gly Gly Ser Asn Cys Ser Ile Met Ile Asp Glu Il 1 5 10 15 Ile His His Leu Lys Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn As 20 25 30 Leu Asn Asp Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Le 35 40 45 Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Al 50 55 60 Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Se 65 70 75 80 Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Tyr Val Gl 85 90 95 Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Il 100 105 110 Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Al 115 120 125 Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Al 130 135 140 Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Se 145 150 155 160 Tyr Arg Val Leu Arg His Leu Ala Gln Pro Ser Gly Gly Ser Gly Gl 165 170 175 Ser Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gl 180 185 190 Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Le 195 200 205 Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pr 210 215 220 Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gl 225 230 235 240 Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Le 245 250 255 Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Th 260 265 270 Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Me 275 280 285 Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro 290 295 329 amino acids amino acid unknown unknown peptide 194 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Ly 1 5 10 15 Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu As 20 25 30 Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Se 35 40 45 Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Al 50 55 60 Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pr 65 70 75 80 Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Ar 85 90 95 Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gl 100 105 110 Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pr 115 120 125 Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Se 130 135 140 Pro Asn Met Ala Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Le 145 150 155 160 Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Se 165 170 175 Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Le 180 185 190 Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Gl 195 200 205 Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Al 210 215 220 Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Le 225 230 235 240 Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Ar 245 250 255 Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Gl 260 265 270 Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Gly Gly Gly Se 275 280 285 Asp Met Ala Thr Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Ph 290 295 300 Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Al 305 310 315 320 Ala Leu Gln Glu Lys Leu Cys Ala Thr 325 329 amino acids amino acid unknown unknown peptide 195 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Ly 1 5 10 15 Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu As 20 25 30 Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Se 35 40 45 Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Al 50 55 60 Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pr 65 70 75 80 Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Ar 85 90 95 Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gl 100 105 110 Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pr 115 120 125 Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Se 130 135 140 Pro Asn Met Ala Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Le 145 150 155 160 Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Le 165 170 175 Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Ph 180 185 190 Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser Hi 195 200 205 Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Al 210 215 220 Gln Pro Gly Gly Gly Ser Asp Met Ala Thr Pro Leu Gly Pro Ala Se 225 230 235 240 Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Ly 245 250 255 Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Ty 260 265 270 Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gl 275 280 285 Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Le 290 295 300 Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gl 305 310 315 320 Leu Leu Gln Ala Leu Glu Gly Ile Ser 325 329 amino acids amino acid unknown unknown peptide 196 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Ly 1 5 10 15 Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu As 20 25 30 Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Se 35 40 45 Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Al 50 55 60 Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pr 65 70 75 80 Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Ar 85 90 95 Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gl 100 105 110 Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pr 115 120 125 Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Se 130 135 140 Pro Asn Met Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Va 145 150 155 160 Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Ar 165 170 175 His Leu Ala Gln Pro Gly Gly Gly Ser Asp Met Ala Thr Pro Leu Gl 180 185 190 Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu Gl 195 200 205 Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cy 210 215 220 Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly Hi 225 230 235 240 Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Al 245 250 255 Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Le 260 265 270 Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gl 275 280 285 Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Th 290 295 300 Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pr 305 310 315 320 Thr Gln Gly Ala Met Pro Ala Phe Ala 325 329 amino acids amino acid unknown unknown peptide 197 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Ly 1 5 10 15 Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu As 20 25 30 Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Se 35 40 45 Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Al 50 55 60 Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pr 65 70 75 80 Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Ar 85 90 95 Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gl 100 105 110 Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pr 115 120 125 Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Se 130 135 140 Pro Asn Met Ala Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Me 145 150 155 160 Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Va 165 170 175 Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Ar 180 185 190 His Leu Ala Gln Pro Gly Gly Gly Ser Asp Met Ala Thr Pro Leu Gl 195 200 205 Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu Gl 210 215 220 Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cy 225 230 235 240 Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly Hi 245 250 255 Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Al 260 265 270 Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Le 275 280 285 Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gl 290 295 300 Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Th 305 310 315 320 Ile Trp Gln Gln Met Glu Glu Leu Gly 325 329 amino acids amino acid unknown unknown peptide 198 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Ly 1 5 10 15 Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu As 20 25 30 Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Se 35 40 45 Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Al 50 55 60 Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pr 65 70 75 80 Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Ar 85 90 95 Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gl 100 105 110 Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pr 115 120 125 Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Se 130 135 140 Pro Asn Met Ala Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Ph 145 150 155 160 Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Ph 165 170 175 Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Gly Gl 180 185 190 Gly Ser Asp Met Ala Thr Pro Leu Gly Pro Ala Ser Ser Leu Pro Gl 195 200 205 Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly As 210 215 220 Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys Hi 225 230 235 240 Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Al 245 250 255 Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Le 260 265 270 Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Al 275 280 285 Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gl 290 295 300 Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Gl 305 310 315 320 Leu Gly Met Ala Pro Ala Leu Gln Pro 325 319 amino acids amino acid unknown unknown peptide 199 Met Ala Asn Cys Ser Asn Met Ile Asp Glu Ile Ile Thr His Leu Ly 1 5 10 15 Gln Pro Pro Leu Pro Leu Leu Asp Phe Asn Asn Leu Asn Gly Glu As 20 25 30 Gln Asp Ile Leu Met Asp Asn Asn Leu Arg Arg Pro Asn Leu Glu Al 35 40 45 Phe Asn Arg Ala Val Lys Ser Leu Gln Asn Ala Ser Ala Ile Glu Se 50 55 60 Ile Leu Lys Asn Leu Leu Pro Cys Leu Pro Leu Ala Thr Ala Ala Pr 65 70 75 80 Thr Arg His Pro Ile His Ile Lys Asp Gly Asp Trp Asn Glu Phe Ar 85 90 95 Arg Lys Leu Thr Phe Tyr Leu Lys Thr Leu Glu Asn Ala Gln Ala Gl 100 105 110 Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pr 115 120 125 Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Se 130 135 140 Pro Asn Met Ala Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Ph 145 150 155 160 Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Ph 165 170 175 Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Ser Gl 180 185 190 Gly Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Va 195 200 205 Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Al 210 215 220 Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Se 225 230 235 240 Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Le 245 250 255 Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Ty 260 265 270 Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pr 275 280 285 Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Il 290 295 300 Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro 305 310 315 322 amino acids amino acid unknown unknown peptide 200 Met Ala Asn Cys Ser Asn Met Ile Asp Glu Ile Ile Thr His Leu Ly 1 5 10 15 Gln Pro Pro Leu Pro Leu Leu Asp Phe Asn Asn Leu Asn Gly Glu As 20 25 30 Gln Asp Ile Leu Met Glu Asn Asn Leu Arg Arg Pro Asn Leu Glu Al 35 40 45 Phe Asn Arg Ala Val Lys Ser Leu Gln Asn Ala Ser Ala Ile Glu Se 50 55 60 Ile Leu Lys Asn Leu Leu Pro Cys Leu Pro Leu Ala Thr Ala Ala Pr 65 70 75 80 Thr Arg His Pro Ile Ile Ile Arg Asp Gly Asp Trp Asn Glu Phe Ar 85 90 95 Arg Lys Leu Thr Phe Tyr Leu Lys Thr Leu Glu Asn Ala Gln Ala Gl 100 105 110 Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pr 115 120 125 Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Se 130 135 140 Pro Asn Met Ala Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Ph 145 150 155 160 Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Ph 165 170 175 Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Thr Pr 180 185 190 Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Le 195 200 205 Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Ly 210 215 220 Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Le 225 230 235 240 Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Se 245 250 255 Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Le 260 265 270 Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Gl 275 280 285 Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Al 290 295 300 Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Le 305 310 315 320 Gln Pro 319 amino acids amino acid unknown unknown peptide 201 Met Ala Asn Cys Ser Asn Met Ile Asp Glu Ile Ile Thr His Leu Ly 1 5 10 15 Gln Pro Pro Leu Pro Leu Leu Asp Phe Asn Asn Leu Asn Gly Glu As 20 25 30 Gln Asp Ile Leu Met Glu Asn Asn Leu Arg Arg Pro Asn Leu Glu Al 35 40 45 Phe Asn Arg Ala Val Lys Ser Leu Gln Asn Ala Ser Ala Ile Glu Se 50 55 60 Ile Leu Lys Asn Leu Leu Pro Cys Leu Pro Leu Ala Thr Ala Ala Pr 65 70 75 80 Thr Arg His Pro Ile Ile Ile Arg Asp Gly Asp Trp Asn Glu Phe Ar 85 90 95 Arg Lys Leu Thr Phe Tyr Leu Lys Thr Leu Glu Asn Ala Gln Ala Gl 100 105 110 Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pr 115 120 125 Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Se 130 135 140 Pro Asn Met Ala Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Ph 145 150 155 160 Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Ph 165 170 175 Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Ser Gl 180 185 190 Gly Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Va 195 200 205 Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Al 210 215 220 Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Se 225 230 235 240 Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Le 245 250 255 Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Ty 260 265 270 Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pr 275 280 285 Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Il 290 295 300 Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro 305 310 315 322 amino acids amino acid unknown unknown peptide 202 Met Ala Asn Cys Ser Asn Met Ile Asp Glu Ile Ile Thr His Leu Ly 1 5 10 15 Gln Pro Pro Leu Pro Leu Leu Asp Phe Asn Asn Leu Asn Gly Glu As 20 25 30 Gln Asp Ile Leu Met Asp Asn Asn Leu Arg Arg Pro Asn Leu Glu Al 35 40 45 Phe Asn Arg Ala Val Lys Ser Leu Gln Asn Ala Ser Ala Ile Glu Se 50 55 60 Ile Leu Lys Asn Leu Leu Pro Cys Leu Pro Leu Ala Thr Ala Ala Pr 65 70 75 80 Thr Arg His Pro Ile His Ile Lys Asp Gly Asp Trp Asn Glu Phe Ar 85 90 95 Arg Lys Leu Thr Phe Tyr Leu Lys Thr Leu Glu Asn Ala Gln Ala Gl 100 105 110 Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pr 115 120 125 Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Se 130 135 140 Pro Asn Met Ala Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Ph 145 150 155 160 Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Ph 165 170 175 Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Thr Pr 180 185 190 Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Le 195 200 205 Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Ly 210 215 220 Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Le 225 230 235 240 Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Se 245 250 255 Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Le 260 265 270 Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Gl 275 280 285 Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Al 290 295 300 Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Le 305 310 315 320 Gln Pro 306 amino acids amino acid unknown unknown peptide 203 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Glu Val His Pro Leu Pro Thr Pro Val Leu Leu Pro Ala Va 145 150 155 160 Asp Phe Ser Leu Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Al 165 170 175 Gln Asp Ile Leu Gly Ala Val Thr Leu Leu Leu Glu Gly Val Met Al 180 185 190 Ala Arg Gly Gln Leu Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gl 195 200 205 Leu Ser Gly Gln Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Le 210 215 220 Gly Thr Gln Leu Pro Pro Gln Gly Arg Thr Thr Ala His Lys Asp Pr 225 230 235 240 Asn Ala Ile Phe Leu Ser Phe Gln His Leu Leu Arg Gly Lys Val Ar 245 250 255 Phe Leu Met Leu Val Gly Gly Ser Thr Leu Cys Val Arg Glu Phe Gl 260 265 270 Gly Asn Met Ala Ser Pro Ala Pro Pro Ala Cys Asp Leu Arg Val Le 275 280 285 Ser Lys Leu Leu Arg Asp Ser His Val Leu His Ser Arg Leu Ser Gl 290 295 300 Cys Pro 305 306 amino acids amino acid unknown unknown peptide 204 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Leu Pro Thr Pro Val Leu Leu Pro Ala Val Asp Phe Ser Le 145 150 155 160 Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln Asp Ile Le 165 170 175 Gly Ala Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Arg Gly Gl 180 185 190 Leu Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gly Gl 195 200 205 Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Thr Gln Le 210 215 220 Pro Pro Gln Gly Arg Thr Thr Ala His Lys Asp Pro Asn Ala Ile Ph 225 230 235 240 Leu Ser Phe Gln His Leu Leu Arg Gly Lys Val Arg Phe Leu Met Le 245 250 255 Val Gly Gly Ser Thr Leu Cys Val Arg Glu Phe Gly Gly Asn Met Al 260 265 270 Ser Pro Ala Pro Pro Ala Cys Asp Leu Arg Val Leu Ser Lys Leu Le 275 280 285 Arg Asp Ser His Val Leu His Ser Arg Leu Ser Gln Cys Pro Glu Va 290 295 300 His Pro 305 306 amino acids amino acid unknown unknown peptide 205 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Val Leu Leu Pro Ala Val Asp Phe Ser Leu Gly Glu Trp Ly 145 150 155 160 Thr Gln Met Glu Glu Thr Lys Ala Gln Asp Ile Leu Gly Ala Val Th 165 170 175 Leu Leu Leu Glu Gly Val Met Ala Ala Arg Gly Gln Leu Gly Pro Th 180 185 190 Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gly Gln Val Arg Leu Le 195 200 205 Leu Gly Ala Leu Gln Ser Leu Leu Gly Thr Gln Leu Pro Pro Gln Gl 210 215 220 Arg Thr Thr Ala His Lys Asp Pro Asn Ala Ile Phe Leu Ser Phe Gl 225 230 235 240 His Leu Leu Arg Gly Lys Val Arg Phe Leu Met Leu Val Gly Gly Se 245 250 255 Thr Leu Cys Val Arg Glu Phe Gly Gly Asn Met Ala Ser Pro Ala Pr 260 265 270 Pro Ala Cys Asp Leu Arg Val Leu Ser Lys Leu Leu Arg Asp Ser Hi 275 280 285 Val Leu His Ser Arg Leu Ser Gln Cys Pro Glu Val His Pro Leu Pr 290 295 300 Thr Pro 305 306 amino acids amino acid unknown unknown peptide 206 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Ala Val Asp Phe Ser Leu Gly Glu Trp Lys Thr Gln Met Gl 145 150 155 160 Glu Thr Lys Ala Gln Asp Ile Leu Gly Ala Val Thr Leu Leu Leu Gl 165 170 175 Gly Val Met Ala Ala Arg Gly Gln Leu Gly Pro Thr Cys Leu Ser Se 180 185 190 Leu Leu Gly Gln Leu Ser Gly Gln Val Arg Leu Leu Leu Gly Ala Le 195 200 205 Gln Ser Leu Leu Gly Thr Gln Leu Pro Pro Gln Gly Arg Thr Thr Al 210 215 220 His Lys Asp Pro Asn Ala Ile Phe Leu Ser Phe Gln His Leu Leu Ar 225 230 235 240 Gly Lys Val Arg Phe Leu Met Leu Val Gly Gly Ser Thr Leu Cys Va 245 250 255 Arg Glu Phe Gly Gly Asn Met Ala Ser Pro Ala Pro Pro Ala Cys As 260 265 270 Leu Arg Val Leu Ser Lys Leu Leu Arg Asp Ser His Val Leu His Se 275 280 285 Arg Leu Ser Gln Cys Pro Glu Val His Pro Leu Pro Thr Pro Val Le 290 295 300 Leu Pro 305 306 amino acids amino acid unknown unknown peptide 207 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Asp Phe Ser Leu Gly Glu Trp Lys Thr Gln Met Glu Glu Th 145 150 155 160 Lys Ala Gln Asp Ile Leu Gly Ala Val Thr Leu Leu Leu Glu Gly Va 165 170 175 Met Ala Ala Arg Gly Gln Leu Gly Pro Thr Cys Leu Ser Ser Leu Le 180 185 190 Gly Gln Leu Ser Gly Gln Val Arg Leu Leu Leu Gly Ala Leu Gln Se 195 200 205 Leu Leu Gly Thr Gln Leu Pro Pro Gln Gly Arg Thr Thr Ala His Ly 210 215 220 Asp Pro Asn Ala Ile Phe Leu Ser Phe Gln His Leu Leu Arg Gly Ly 225 230 235 240 Val Arg Phe Leu Met Leu Val Gly Gly Ser Thr Leu Cys Val Arg Gl 245 250 255 Phe Gly Gly Asn Met Ala Ser Pro Ala Pro Pro Ala Cys Asp Leu Ar 260 265 270 Val Leu Ser Lys Leu Leu Arg Asp Ser His Val Leu His Ser Arg Le 275 280 285 Ser Gln Cys Pro Glu Val His Pro Leu Pro Thr Pro Val Leu Leu Pr 290 295 300 Ala Val 305 306 amino acids amino acid unknown unknown peptide 208 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln As 145 150 155 160 Ile Leu Gly Ala Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Ar 165 170 175 Gly Gln Leu Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Se 180 185 190 Gly Gln Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Th 195 200 205 Gln Leu Pro Pro Gln Gly Arg Thr Thr Ala His Lys Asp Pro Asn Al 210 215 220 Ile Phe Leu Ser Phe Gln His Leu Leu Arg Gly Lys Val Arg Phe Le 225 230 235 240 Met Leu Val Gly Gly Ser Thr Leu Cys Val Arg Glu Phe Gly Gly As 245 250 255 Met Ala Ser Pro Ala Pro Pro Ala Cys Asp Leu Arg Val Leu Ser Ly 260 265 270 Leu Leu Arg Asp Ser His Val Leu His Ser Arg Leu Ser Gln Cys Pr 275 280 285 Glu Val His Pro Leu Pro Thr Pro Val Leu Leu Pro Ala Val Asp Ph 290 295 300 Ser Leu 305 306 amino acids amino acid unknown unknown peptide 209 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gl 145 150 155 160 Gln Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Thr Gl 165 170 175 Leu Pro Pro Gln Gly Arg Thr Thr Ala His Lys Asp Pro Asn Ala Il 180 185 190 Phe Leu Ser Phe Gln His Leu Leu Arg Gly Lys Val Arg Phe Leu Me 195 200 205 Leu Val Gly Gly Ser Thr Leu Cys Val Arg Glu Phe Gly Gly Asn Me 210 215 220 Ala Ser Pro Ala Pro Pro Ala Cys Asp Leu Arg Val Leu Ser Lys Le 225 230 235 240 Leu Arg Asp Ser His Val Leu His Ser Arg Leu Ser Gln Cys Pro Gl 245 250 255 Val His Pro Leu Pro Thr Pro Val Leu Leu Pro Ala Val Asp Phe Se 260 265 270 Leu Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln Asp Il 275 280 285 Leu Gly Ala Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Arg Gl 290 295 300 Gln Leu 305 306 amino acids amino acid unknown unknown peptide 210 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Gly Thr Gln Leu Pro Pro Gln Gly Arg Thr Thr Ala His Ly 145 150 155 160 Asp Pro Asn Ala Ile Phe Leu Ser Phe Gln His Leu Leu Arg Gly Ly 165 170 175 Val Arg Phe Leu Met Leu Val Gly Gly Ser Thr Leu Cys Val Arg Gl 180 185 190 Phe Gly Gly Asn Met Ala Ser Pro Ala Pro Pro Ala Cys Asp Leu Ar 195 200 205 Val Leu Ser Lys Leu Leu Arg Asp Ser His Val Leu His Ser Arg Le 210 215 220 Ser Gln Cys Pro Glu Val His Pro Leu Pro Thr Pro Val Leu Leu Pr 225 230 235 240 Ala Val Asp Phe Ser Leu Gly Glu Trp Lys Thr Gln Met Glu Glu Th 245 250 255 Lys Ala Gln Asp Ile Leu Gly Ala Val Thr Leu Leu Leu Glu Gly Va 260 265 270 Met Ala Ala Arg Gly Gln Leu Gly Pro Thr Cys Leu Ser Ser Leu Le 275 280 285 Gly Gln Leu Ser Gly Gln Val Arg Leu Leu Leu Gly Ala Leu Gln Se 290 295 300 Leu Leu 305 306 amino acids amino acid unknown unknown peptide 211 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Gly Arg Thr Thr Ala His Lys Asp Pro Asn Ala Ile Phe Le 145 150 155 160 Ser Phe Gln His Leu Leu Arg Gly Lys Val Arg Phe Leu Met Leu Va 165 170 175 Gly Gly Ser Thr Leu Cys Val Arg Glu Phe Gly Gly Asn Met Ala Se 180 185 190 Pro Ala Pro Pro Ala Cys Asp Leu Arg Val Leu Ser Lys Leu Leu Ar 195 200 205 Asp Ser His Val Leu His Ser Arg Leu Ser Gln Cys Pro Glu Val Hi 210 215 220 Pro Leu Pro Thr Pro Val Leu Leu Pro Ala Val Asp Phe Ser Leu Gl 225 230 235 240 Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln Asp Ile Leu Gl 245 250 255 Ala Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Arg Gly Gln Le 260 265 270 Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gly Gln Va 275 280 285 Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Thr Gln Leu Pr 290 295 300 Pro Gln 305 306 amino acids amino acid unknown unknown peptide 212 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Ala His Lys Asp Pro Asn Ala Ile Phe Leu Ser Phe Gln Hi 145 150 155 160 Leu Leu Arg Gly Lys Val Arg Phe Leu Met Leu Val Gly Gly Ser Th 165 170 175 Leu Cys Val Arg Glu Phe Gly Gly Asn Met Ala Ser Pro Ala Pro Pr 180 185 190 Ala Cys Asp Leu Arg Val Leu Ser Lys Leu Leu Arg Asp Ser His Va 195 200 205 Leu His Ser Arg Leu Ser Gln Cys Pro Glu Val His Pro Leu Pro Th 210 215 220 Pro Val Leu Leu Pro Ala Val Asp Phe Ser Leu Gly Glu Trp Lys Th 225 230 235 240 Gln Met Glu Glu Thr Lys Ala Gln Asp Ile Leu Gly Ala Val Thr Le 245 250 255 Leu Leu Glu Gly Val Met Ala Ala Arg Gly Gln Leu Gly Pro Thr Cy 260 265 270 Leu Ser Ser Leu Leu Gly Gln Leu Ser Gly Gln Val Arg Leu Leu Le 275 280 285 Gly Ala Leu Gln Ser Leu Leu Gly Thr Gln Leu Pro Pro Gln Gly Ar 290 295 300 Thr Thr 305 306 amino acids amino acid unknown unknown peptide 213 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Asp Pro Asn Ala Ile Phe Leu Ser Phe Gln His Leu Leu Ar 145 150 155 160 Gly Lys Val Arg Phe Leu Met Leu Val Gly Gly Ser Thr Leu Cys Va 165 170 175 Arg Glu Phe Gly Gly Asn Met Ala Ser Pro Ala Pro Pro Ala Cys As 180 185 190 Leu Arg Val Leu Ser Lys Leu Leu Arg Asp Ser His Val Leu His Se 195 200 205 Arg Leu Ser Gln Cys Pro Glu Val His Pro Leu Pro Thr Pro Val Le 210 215 220 Leu Pro Ala Val Asp Phe Ser Leu Gly Glu Trp Lys Thr Gln Met Gl 225 230 235 240 Glu Thr Lys Ala Gln Asp Ile Leu Gly Ala Val Thr Leu Leu Leu Gl 245 250 255 Gly Val Met Ala Ala Arg Gly Gln Leu Gly Pro Thr Cys Leu Ser Se 260 265 270 Leu Leu Gly Gln Leu Ser Gly Gln Val Arg Leu Leu Leu Gly Ala Le 275 280 285 Gln Ser Leu Leu Gly Thr Gln Leu Pro Pro Gln Gly Arg Thr Thr Al 290 295 300 His Lys 305 306 amino acids amino acid unknown unknown peptide 214 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Ala Ile Phe Leu Ser Phe Gln His Leu Leu Arg Gly Lys Va 145 150 155 160 Arg Phe Leu Met Leu Val Gly Gly Ser Thr Leu Cys Val Arg Glu Ph 165 170 175 Gly Gly Asn Met Ala Ser Pro Ala Pro Pro Ala Cys Asp Leu Arg Va 180 185 190 Leu Ser Lys Leu Leu Arg Asp Ser His Val Leu His Ser Arg Leu Se 195 200 205 Gln Cys Pro Glu Val His Pro Leu Pro Thr Pro Val Leu Leu Pro Al 210 215 220 Val Asp Phe Ser Leu Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Ly 225 230 235 240 Ala Gln Asp Ile Leu Gly Ala Val Thr Leu Leu Leu Glu Gly Val Me 245 250 255 Ala Ala Arg Gly Gln Leu Gly Pro Thr Cys Leu Ser Ser Leu Leu Gl 260 265 270 Gln Leu Ser Gly Gln Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Le 275 280 285 Leu Gly Thr Gln Leu Pro Pro Gln Gly Arg Thr Thr Ala His Lys As 290 295 300 Pro Asn 305 305 amino acids amino acid unknown unknown peptide 215 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Glu Val His Pro Leu Pro Thr Pro Val Leu Leu Pro Ala Va 145 150 155 160 Asp Phe Ser Leu Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Al 165 170 175 Gln Asp Ile Leu Gly Ala Val Thr Leu Leu Leu Glu Gly Val Met Al 180 185 190 Ala Arg Gly Gln Leu Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gl 195 200 205 Leu Ser Gly Gln Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Le 210 215 220 Gly Thr Gln Leu Pro Pro Gln Gly Arg Thr Thr Ala His Lys Asp Pr 225 230 235 240 Asn Ala Ile Phe Leu Ser Phe Gln His Leu Leu Arg Gly Lys Val Ar 245 250 255 Phe Leu Met Leu Val Gly Gly Ser Thr Leu Cys Val Arg Glu Phe Gl 260 265 270 Asn Met Ala Ser Pro Ala Pro Pro Ala Cys Asp Leu Arg Val Leu Se 275 280 285 Lys Leu Leu Arg Asp Ser His Val Leu His Ser Arg Leu Ser Gln Cy 290 295 300 Pro 305 305 amino acids amino acid unknown unknown peptide 216 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Leu Pro Thr Pro Val Leu Leu Pro Ala Val Asp Phe Ser Le 145 150 155 160 Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln Asp Ile Le 165 170 175 Gly Ala Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Arg Gly Gl 180 185 190 Leu Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gly Gl 195 200 205 Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Thr Gln Le 210 215 220 Pro Pro Gln Gly Arg Thr Thr Ala His Lys Asp Pro Asn Ala Ile Ph 225 230 235 240 Leu Ser Phe Gln His Leu Leu Arg Gly Lys Val Arg Phe Leu Met Le 245 250 255 Val Gly Gly Ser Thr Leu Cys Val Arg Glu Phe Gly Asn Met Ala Se 260 265 270 Pro Ala Pro Pro Ala Cys Asp Leu Arg Val Leu Ser Lys Leu Leu Ar 275 280 285 Asp Ser His Val Leu His Ser Arg Leu Ser Gln Cys Pro Glu Val Hi 290 295 300 Pro 305 305 amino acids amino acid unknown unknown peptide 217 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Val Leu Leu Pro Ala Val Asp Phe Ser Leu Gly Glu Trp Ly 145 150 155 160 Thr Gln Met Glu Glu Thr Lys Ala Gln Asp Ile Leu Gly Ala Val Th 165 170 175 Leu Leu Leu Glu Gly Val Met Ala Ala Arg Gly Gln Leu Gly Pro Th 180 185 190 Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gly Gln Val Arg Leu Le 195 200 205 Leu Gly Ala Leu Gln Ser Leu Leu Gly Thr Gln Leu Pro Pro Gln Gl 210 215 220 Arg Thr Thr Ala His Lys Asp Pro Asn Ala Ile Phe Leu Ser Phe Gl 225 230 235 240 His Leu Leu Arg Gly Lys Val Arg Phe Leu Met Leu Val Gly Gly Se 245 250 255 Thr Leu Cys Val Arg Glu Phe Gly Asn Met Ala Ser Pro Ala Pro Pr 260 265 270 Ala Cys Asp Leu Arg Val Leu Ser Lys Leu Leu Arg Asp Ser His Va 275 280 285 Leu His Ser Arg Leu Ser Gln Cys Pro Glu Val His Pro Leu Pro Th 290 295 300 Pro 305 305 amino acids amino acid unknown unknown peptide 218 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Ala Val Asp Phe Ser Leu Gly Glu Trp Lys Thr Gln Met Gl 145 150 155 160 Glu Thr Lys Ala Gln Asp Ile Leu Gly Ala Val Thr Leu Leu Leu Gl 165 170 175 Gly Val Met Ala Ala Arg Gly Gln Leu Gly Pro Thr Cys Leu Ser Se 180 185 190 Leu Leu Gly Gln Leu Ser Gly Gln Val Arg Leu Leu Leu Gly Ala Le 195 200 205 Gln Ser Leu Leu Gly Thr Gln Leu Pro Pro Gln Gly Arg Thr Thr Al 210 215 220 His Lys Asp Pro Asn Ala Ile Phe Leu Ser Phe Gln His Leu Leu Ar 225 230 235 240 Gly Lys Val Arg Phe Leu Met Leu Val Gly Gly Ser Thr Leu Cys Va 245 250 255 Arg Glu Phe Gly Asn Met Ala Ser Pro Ala Pro Pro Ala Cys Asp Le 260 265 270 Arg Val Leu Ser Lys Leu Leu Arg Asp Ser His Val Leu His Ser Ar 275 280 285 Leu Ser Gln Cys Pro Glu Val His Pro Leu Pro Thr Pro Val Leu Le 290 295 300 Pro 305 305 amino acids amino acid unknown unknown peptide 219 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Asp Phe Ser Leu Gly Glu Trp Lys Thr Gln Met Glu Glu Th 145 150 155 160 Lys Ala Gln Asp Ile Leu Gly Ala Val Thr Leu Leu Leu Glu Gly Va 165 170 175 Met Ala Ala Arg Gly Gln Leu Gly Pro Thr Cys Leu Ser Ser Leu Le 180 185 190 Gly Gln Leu Ser Gly Gln Val Arg Leu Leu Leu Gly Ala Leu Gln Se 195 200 205 Leu Leu Gly Thr Gln Leu Pro Pro Gln Gly Arg Thr Thr Ala His Ly 210 215 220 Asp Pro Asn Ala Ile Phe Leu Ser Phe Gln His Leu Leu Arg Gly Ly 225 230 235 240 Val Arg Phe Leu Met Leu Val Gly Gly Ser Thr Leu Cys Val Arg Gl 245 250 255 Phe Gly Asn Met Ala Ser Pro Ala Pro Pro Ala Cys Asp Leu Arg Va 260 265 270 Leu Ser Lys Leu Leu Arg Asp Ser His Val Leu His Ser Arg Leu Se 275 280 285 Gln Cys Pro Glu Val His Pro Leu Pro Thr Pro Val Leu Leu Pro Al 290 295 300 Val 305 305 amino acids amino acid unknown unknown peptide 220 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln As 145 150 155 160 Ile Leu Gly Ala Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Ar 165 170 175 Gly Gln Leu Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Se 180 185 190 Gly Gln Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Th 195 200 205 Gln Leu Pro Pro Gln Gly Arg Thr Thr Ala His Lys Asp Pro Asn Al 210 215 220 Ile Phe Leu Ser Phe Gln His Leu Leu Arg Gly Lys Val Arg Phe Le 225 230 235 240 Met Leu Val Gly Gly Ser Thr Leu Cys Val Arg Glu Phe Gly Asn Me 245 250 255 Ala Ser Pro Ala Pro Pro Ala Cys Asp Leu Arg Val Leu Ser Lys Le 260 265 270 Leu Arg Asp Ser His Val Leu His Ser Arg Leu Ser Gln Cys Pro Gl 275 280 285 Val His Pro Leu Pro Thr Pro Val Leu Leu Pro Ala Val Asp Phe Se 290 295 300 Leu 305 305 amino acids amino acid unknown unknown peptide 221 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gl 145 150 155 160 Gln Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Thr Gl 165 170 175 Leu Pro Pro Gln Gly Arg Thr Thr Ala His Lys Asp Pro Asn Ala Il 180 185 190 Phe Leu Ser Phe Gln His Leu Leu Arg Gly Lys Val Arg Phe Leu Me 195 200 205 Leu Val Gly Gly Ser Thr Leu Cys Val Arg Glu Phe Gly Asn Met Al 210 215 220 Ser Pro Ala Pro Pro Ala Cys Asp Leu Arg Val Leu Ser Lys Leu Le 225 230 235 240 Arg Asp Ser His Val Leu His Ser Arg Leu Ser Gln Cys Pro Glu Va 245 250 255 His Pro Leu Pro Thr Pro Val Leu Leu Pro Ala Val Asp Phe Ser Le 260 265 270 Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln Asp Ile Le 275 280 285 Gly Ala Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Arg Gly Gl 290 295 300 Leu 305 305 amino acids amino acid unknown unknown peptide 222 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Gly Thr Gln Leu Pro Pro Gln Gly Arg Thr Thr Ala His Ly 145 150 155 160 Asp Pro Asn Ala Ile Phe Leu Ser Phe Gln His Leu Leu Arg Gly Ly 165 170 175 Val Arg Phe Leu Met Leu Val Gly Gly Ser Thr Leu Cys Val Arg Gl 180 185 190 Phe Gly Asn Met Ala Ser Pro Ala Pro Pro Ala Cys Asp Leu Arg Va 195 200 205 Leu Ser Lys Leu Leu Arg Asp Ser His Val Leu His Ser Arg Leu Se 210 215 220 Gln Cys Pro Glu Val His Pro Leu Pro Thr Pro Val Leu Leu Pro Al 225 230 235 240 Val Asp Phe Ser Leu Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Ly 245 250 255 Ala Gln Asp Ile Leu Gly Ala Val Thr Leu Leu Leu Glu Gly Val Me 260 265 270 Ala Ala Arg Gly Gln Leu Gly Pro Thr Cys Leu Ser Ser Leu Leu Gl 275 280 285 Gln Leu Ser Gly Gln Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Le 290 295 300 Leu 305 305 amino acids amino acid unknown unknown peptide 223 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Gly Arg Thr Thr Ala His Lys Asp Pro Asn Ala Ile Phe Le 145 150 155 160 Ser Phe Gln His Leu Leu Arg Gly Lys Val Arg Phe Leu Met Leu Va 165 170 175 Gly Gly Ser Thr Leu Cys Val Arg Glu Phe Gly Asn Met Ala Ser Pr 180 185 190 Ala Pro Pro Ala Cys Asp Leu Arg Val Leu Ser Lys Leu Leu Arg As 195 200 205 Ser His Val Leu His Ser Arg Leu Ser Gln Cys Pro Glu Val His Pr 210 215 220 Leu Pro Thr Pro Val Leu Leu Pro Ala Val Asp Phe Ser Leu Gly Gl 225 230 235 240 Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln Asp Ile Leu Gly Al 245 250 255 Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Arg Gly Gln Leu Gl 260 265 270 Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gly Gln Val Ar 275 280 285 Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Thr Gln Leu Pro Pr 290 295 300 Gln 305 305 amino acids amino acid unknown unknown peptide 224 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Gly Arg Thr Thr Ala His Lys Asp Pro Asn Ala Ile Phe Le 145 150 155 160 Ser Phe Gln His Leu Leu Arg Gly Lys Val Arg Phe Leu Met Leu Va 165 170 175 Gly Gly Ser Thr Leu Cys Val Arg Glu Phe Gly Asn Met Ala Ser Pr 180 185 190 Ala Pro Pro Ala Cys Asp Leu Arg Val Leu Ser Lys Leu Leu Arg As 195 200 205 Ser His Val Leu His Ser Arg Leu Ser Gln Cys Pro Glu Val His Pr 210 215 220 Leu Pro Thr Pro Val Leu Leu Pro Ala Val Asp Phe Ser Leu Gly Gl 225 230 235 240 Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln Asp Ile Leu Gly Al 245 250 255 Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Arg Gly Gln Leu Gl 260 265 270 Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gly Gln Val Ar 275 280 285 Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Thr Gln Leu Pro Pr 290 295 300 Gln 305 305 amino acids amino acid unknown unknown peptide 225 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Asp Pro Asn Ala Ile Phe Leu Ser Phe Gln His Leu Leu Ar 145 150 155 160 Gly Lys Val Arg Phe Leu Met Leu Val Gly Gly Ser Thr Leu Cys Va 165 170 175 Arg Glu Phe Gly Asn Met Ala Ser Pro Ala Pro Pro Ala Cys Asp Le 180 185 190 Arg Val Leu Ser Lys Leu Leu Arg Asp Ser His Val Leu His Ser Ar 195 200 205 Leu Ser Gln Cys Pro Glu Val His Pro Leu Pro Thr Pro Val Leu Le 210 215 220 Pro Ala Val Asp Phe Ser Leu Gly Glu Trp Lys Thr Gln Met Glu Gl 225 230 235 240 Thr Lys Ala Gln Asp Ile Leu Gly Ala Val Thr Leu Leu Leu Glu Gl 245 250 255 Val Met Ala Ala Arg Gly Gln Leu Gly Pro Thr Cys Leu Ser Ser Le 260 265 270 Leu Gly Gln Leu Ser Gly Gln Val Arg Leu Leu Leu Gly Ala Leu Gl 275 280 285 Ser Leu Leu Gly Thr Gln Leu Pro Pro Gln Gly Arg Thr Thr Ala Hi 290 295 300 Lys 305 305 amino acids amino acid unknown unknown peptide 226 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Ala Ile Phe Leu Ser Phe Gln His Leu Leu Arg Gly Lys Va 145 150 155 160 Arg Phe Leu Met Leu Val Gly Gly Ser Thr Leu Cys Val Arg Glu Ph 165 170 175 Gly Asn Met Ala Ser Pro Ala Pro Pro Ala Cys Asp Leu Arg Val Le 180 185 190 Ser Lys Leu Leu Arg Asp Ser His Val Leu His Ser Arg Leu Ser Gl 195 200 205 Cys Pro Glu Val His Pro Leu Pro Thr Pro Val Leu Leu Pro Ala Va 210 215 220 Asp Phe Ser Leu Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Al 225 230 235 240 Gln Asp Ile Leu Gly Ala Val Thr Leu Leu Leu Glu Gly Val Met Al 245 250 255 Ala Arg Gly Gln Leu Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gl 260 265 270 Leu Ser Gly Gln Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Le 275 280 285 Gly Thr Gln Leu Pro Pro Gln Gly Arg Thr Thr Ala His Lys Asp Pr 290 295 300 Asn 305 309 amino acids amino acid unknown unknown peptide 227 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Leu Pro Thr Pro Val Leu Leu Pro Ala Val Asp Phe Ser Le 145 150 155 160 Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln Asp Ile Le 165 170 175 Gly Ala Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Arg Gly Gl 180 185 190 Leu Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gly Gl 195 200 205 Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Thr Gln Le 210 215 220 Pro Pro Gln Gly Arg Thr Thr Ala His Lys Asp Pro Asn Ala Ile Ph 225 230 235 240 Leu Ser Phe Gln His Leu Leu Arg Gly Lys Val Arg Phe Leu Met Le 245 250 255 Val Gly Gly Ser Thr Leu Cys Val Arg Glu Phe Gly Gly Asn Gly Gl 260 265 270 Asn Met Ala Ser Pro Ala Pro Pro Ala Cys Asp Leu Arg Val Leu Se 275 280 285 Lys Leu Leu Arg Asp Ser His Val Leu His Ser Arg Leu Ser Gln Cy 290 295 300 Pro Glu Val His Pro 305 309 amino acids amino acid unknown unknown peptide 228 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Leu Pro Thr Pro Val Leu Leu Pro Ala Val Asp Phe Ser Le 145 150 155 160 Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln Asp Ile Le 165 170 175 Gly Ala Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Arg Gly Gl 180 185 190 Leu Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gly Gl 195 200 205 Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Thr Gln Le 210 215 220 Pro Pro Gln Gly Arg Thr Thr Ala His Lys Asp Pro Asn Ala Ile Ph 225 230 235 240 Leu Ser Phe Gln His Leu Leu Arg Gly Lys Val Arg Phe Leu Met Le 245 250 255 Val Gly Gly Ser Thr Leu Cys Val Arg Glu Phe Gly Gly Asn Gly Gl 260 265 270 Asn Met Ala Ser Pro Ala Pro Pro Ala Cys Asp Leu Arg Val Leu Se 275 280 285 Lys Leu Leu Arg Asp Ser His Val Leu His Ser Arg Leu Ser Gln Cy 290 295 300 Pro Glu Val His Pro 305 309 amino acids amino acid unknown unknown peptide 229 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Val Leu Leu Pro Ala Val Asp Phe Ser Leu Gly Glu Trp Ly 145 150 155 160 Thr Gln Met Glu Glu Thr Lys Ala Gln Asp Ile Leu Gly Ala Val Th 165 170 175 Leu Leu Leu Glu Gly Val Met Ala Ala Arg Gly Gln Leu Gly Pro Th 180 185 190 Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gly Gln Val Arg Leu Le 195 200 205 Leu Gly Ala Leu Gln Ser Leu Leu Gly Thr Gln Leu Pro Pro Gln Gl 210 215 220 Arg Thr Thr Ala His Lys Asp Pro Asn Ala Ile Phe Leu Ser Phe Gl 225 230 235 240 His Leu Leu Arg Gly Lys Val Arg Phe Leu Met Leu Val Gly Gly Se 245 250 255 Thr Leu Cys Val Arg Glu Phe Gly Gly Asn Gly Gly Asn Met Ala Se 260 265 270 Pro Ala Pro Pro Ala Cys Asp Leu Arg Val Leu Ser Lys Leu Leu Ar 275 280 285 Asp Ser His Val Leu His Ser Arg Leu Ser Gln Cys Pro Glu Val Hi 290 295 300 Pro Leu Pro Thr Pro 305 309 amino acids amino acid unknown unknown peptide 230 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Ala Val Asp Phe Ser Leu Gly Glu Trp Lys Thr Gln Met Gl 145 150 155 160 Glu Thr Lys Ala Gln Asp Ile Leu Gly Ala Val Thr Leu Leu Leu Gl 165 170 175 Gly Val Met Ala Ala Arg Gly Gln Leu Gly Pro Thr Cys Leu Ser Se 180 185 190 Leu Leu Gly Gln Leu Ser Gly Gln Val Arg Leu Leu Leu Gly Ala Le 195 200 205 Gln Ser Leu Leu Gly Thr Gln Leu Pro Pro Gln Gly Arg Thr Thr Al 210 215 220 His Lys Asp Pro Asn Ala Ile Phe Leu Ser Phe Gln His Leu Leu Ar 225 230 235 240 Gly Lys Val Arg Phe Leu Met Leu Val Gly Gly Ser Thr Leu Cys Va 245 250 255 Arg Glu Phe Gly Gly Asn Gly Gly Asn Met Ala Ser Pro Ala Pro Pr 260 265 270 Ala Cys Asp Leu Arg Val Leu Ser Lys Leu Leu Arg Asp Ser His Va 275 280 285 Leu His Ser Arg Leu Ser Gln Cys Pro Glu Val His Pro Leu Pro Th 290 295 300 Pro Val Leu Leu Pro 305 309 amino acids amino acid unknown unknown peptide 231 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Asp Phe Ser Leu Gly Glu Trp Lys Thr Gln Met Glu Glu Th 145 150 155 160 Lys Ala Gln Asp Ile Leu Gly Ala Val Thr Leu Leu Leu Glu Gly Va 165 170 175 Met Ala Ala Arg Gly Gln Leu Gly Pro Thr Cys Leu Ser Ser Leu Le 180 185 190 Gly Gln Leu Ser Gly Gln Val Arg Leu Leu Leu Gly Ala Leu Gln Se 195 200 205 Leu Leu Gly Thr Gln Leu Pro Pro Gln Gly Arg Thr Thr Ala His Ly 210 215 220 Asp Pro Asn Ala Ile Phe Leu Ser Phe Gln His Leu Leu Arg Gly Ly 225 230 235 240 Val Arg Phe Leu Met Leu Val Gly Gly Ser Thr Leu Cys Val Arg Gl 245 250 255 Phe Gly Gly Asn Gly Gly Asn Met Ala Ser Pro Ala Pro Pro Ala Cy 260 265 270 Asp Leu Arg Val Leu Ser Lys Leu Leu Arg Asp Ser His Val Leu Hi 275 280 285 Ser Arg Leu Ser Gln Cys Pro Glu Val His Pro Leu Pro Thr Pro Va 290 295 300 Leu Leu Pro Ala Val 305 309 amino acids amino acid unknown unknown peptide 232 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln As 145 150 155 160 Ile Leu Gly Ala Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Ar 165 170 175 Gly Gln Leu Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Se 180 185 190 Gly Gln Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Th 195 200 205 Gln Leu Pro Pro Gln Gly Arg Thr Thr Ala His Lys Asp Pro Asn Al 210 215 220 Ile Phe Leu Ser Phe Gln His Leu Leu Arg Gly Lys Val Arg Phe Le 225 230 235 240 Met Leu Val Gly Gly Ser Thr Leu Cys Val Arg Glu Phe Gly Gly As 245 250 255 Gly Gly Asn Met Ala Ser Pro Ala Pro Pro Ala Cys Asp Leu Arg Va 260 265 270 Leu Ser Lys Leu Leu Arg Asp Ser His Val Leu His Ser Arg Leu Se 275 280 285 Gln Cys Pro Glu Val His Pro Leu Pro Thr Pro Val Leu Leu Pro Al 290 295 300 Val Asp Phe Ser Leu 305 309 amino acids amino acid unknown unknown peptide 233 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gl 145 150 155 160 Gln Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Thr Gl 165 170 175 Leu Pro Pro Gln Gly Arg Thr Thr Ala His Lys Asp Pro Asn Ala Il 180 185 190 Phe Leu Ser Phe Gln His Leu Leu Arg Gly Lys Val Arg Phe Leu Me 195 200 205 Leu Val Gly Gly Ser Thr Leu Cys Val Arg Glu Phe Gly Gly Asn Gl 210 215 220 Gly Asn Met Ala Ser Pro Ala Pro Pro Ala Cys Asp Leu Arg Val Le 225 230 235 240 Ser Lys Leu Leu Arg Asp Ser His Val Leu His Ser Arg Leu Ser Gl 245 250 255 Cys Pro Glu Val His Pro Leu Pro Thr Pro Val Leu Leu Pro Ala Va 260 265 270 Asp Phe Ser Leu Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Al 275 280 285 Gln Asp Ile Leu Gly Ala Val Thr Leu Leu Leu Glu Gly Val Met Al 290 295 300 Ala Arg Gly Gln Leu 305 309 amino acids amino acid unknown unknown peptide 234 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Gly Thr Gln Leu Pro Pro Gln Gly Arg Thr Thr Ala His Ly 145 150 155 160 Asp Pro Asn Ala Ile Phe Leu Ser Phe Gln His Leu Leu Arg Gly Ly 165 170 175 Val Arg Phe Leu Met Leu Val Gly Gly Ser Thr Leu Cys Val Arg Gl 180 185 190 Phe Gly Gly Asn Gly Gly Asn Met Ala Ser Pro Ala Pro Pro Ala Cy 195 200 205 Asp Leu Arg Val Leu Ser Lys Leu Leu Arg Asp Ser His Val Leu Hi 210 215 220 Ser Arg Leu Ser Gln Cys Pro Glu Val His Pro Leu Pro Thr Pro Va 225 230 235 240 Leu Leu Pro Ala Val Asp Phe Ser Leu Gly Glu Trp Lys Thr Gln Me 245 250 255 Glu Glu Thr Lys Ala Gln Asp Ile Leu Gly Ala Val Thr Leu Leu Le 260 265 270 Glu Gly Val Met Ala Ala Arg Gly Gln Leu Gly Pro Thr Cys Leu Se 275 280 285 Ser Leu Leu Gly Gln Leu Ser Gly Gln Val Arg Leu Leu Leu Gly Al 290 295 300 Leu Gln Ser Leu Leu 305 309 amino acids amino acid unknown unknown peptide 235 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Gly Arg Thr Thr Ala His Lys Asp Pro Asn Ala Ile Phe Le 145 150 155 160 Ser Phe Gln His Leu Leu Arg Gly Lys Val Arg Phe Leu Met Leu Va 165 170 175 Gly Gly Ser Thr Leu Cys Val Arg Glu Phe Gly Gly Asn Gly Gly As 180 185 190 Met Ala Ser Pro Ala Pro Pro Ala Cys Asp Leu Arg Val Leu Ser Ly 195 200 205 Leu Leu Arg Asp Ser His Val Leu His Ser Arg Leu Ser Gln Cys Pr 210 215 220 Glu Val His Pro Leu Pro Thr Pro Val Leu Leu Pro Ala Val Asp Ph 225 230 235 240 Ser Leu Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln As 245 250 255 Ile Leu Gly Ala Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Ar 260 265 270 Gly Gln Leu Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Se 275 280 285 Gly Gln Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Th 290 295 300 Gln Leu Pro Pro Gln 305 309 amino acids amino acid unknown unknown peptide 236 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Ala His Lys Asp Pro Asn Ala Ile Phe Leu Ser Phe Gln Hi 145 150 155 160 Leu Leu Arg Gly Lys Val Arg Phe Leu Met Leu Val Gly Gly Ser Th 165 170 175 Leu Cys Val Arg Glu Phe Gly Gly Asn Gly Gly Asn Met Ala Ser Pr 180 185 190 Ala Pro Pro Ala Cys Asp Leu Arg Val Leu Ser Lys Leu Leu Arg As 195 200 205 Ser His Val Leu His Ser Arg Leu Ser Gln Cys Pro Glu Val His Pr 210 215 220 Leu Pro Thr Pro Val Leu Leu Pro Ala Val Asp Phe Ser Leu Gly Gl 225 230 235 240 Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln Asp Ile Leu Gly Al 245 250 255 Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Arg Gly Gln Leu Gl 260 265 270 Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gly Gln Val Ar 275 280 285 Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Thr Gln Leu Pro Pr 290 295 300 Gln Gly Arg Thr Thr 305 309 amino acids amino acid unknown unknown peptide 237 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Asp Pro Asn Ala Ile Phe Leu Ser Phe Gln His Leu Leu Ar 145 150 155 160 Gly Lys Val Arg Phe Leu Met Leu Val Gly Gly Ser Thr Leu Cys Va 165 170 175 Arg Glu Phe Gly Gly Asn Gly Gly Asn Met Ala Ser Pro Ala Pro Pr 180 185 190 Ala Cys Asp Leu Arg Val Leu Ser Lys Leu Leu Arg Asp Ser His Va 195 200 205 Leu His Ser Arg Leu Ser Gln Cys Pro Glu Val His Pro Leu Pro Th 210 215 220 Pro Val Leu Leu Pro Ala Val Asp Phe Ser Leu Gly Glu Trp Lys Th 225 230 235 240 Gln Met Glu Glu Thr Lys Ala Gln Asp Ile Leu Gly Ala Val Thr Le 245 250 255 Leu Leu Glu Gly Val Met Ala Ala Arg Gly Gln Leu Gly Pro Thr Cy 260 265 270 Leu Ser Ser Leu Leu Gly Gln Leu Ser Gly Gln Val Arg Leu Leu Le 275 280 285 Gly Ala Leu Gln Ser Leu Leu Gly Thr Gln Leu Pro Pro Gln Gly Ar 290 295 300 Thr Thr Ala His Lys 305 309 amino acids amino acid unknown unknown peptide 238 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Ala Ile Phe Leu Ser Phe Gln His Leu Leu Arg Gly Lys Va 145 150 155 160 Arg Phe Leu Met Leu Val Gly Gly Ser Thr Leu Cys Val Arg Glu Ph 165 170 175 Gly Gly Asn Gly Gly Asn Met Ala Ser Pro Ala Pro Pro Ala Cys As 180 185 190 Leu Arg Val Leu Ser Lys Leu Leu Arg Asp Ser His Val Leu His Se 195 200 205 Arg Leu Ser Gln Cys Pro Glu Val His Pro Leu Pro Thr Pro Val Le 210 215 220 Leu Pro Ala Val Asp Phe Ser Leu Gly Glu Trp Lys Thr Gln Met Gl 225 230 235 240 Glu Thr Lys Ala Gln Asp Ile Leu Gly Ala Val Thr Leu Leu Leu Gl 245 250 255 Gly Val Met Ala Ala Arg Gly Gln Leu Gly Pro Thr Cys Leu Ser Se 260 265 270 Leu Leu Gly Gln Leu Ser Gly Gln Val Arg Leu Leu Leu Gly Ala Le 275 280 285 Gln Ser Leu Leu Gly Thr Gln Leu Pro Pro Gln Gly Arg Thr Thr Al 290 295 300 His Lys Asp Pro Asn 305 302 amino acids amino acid unknown unknown peptide 239 Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Ar 1 5 10 15 Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Va 20 25 30 Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Ph 35 40 45 Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Il 50 55 60 Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Se 65 70 75 80 Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Gl 85 90 95 Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gl 100 105 110 Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Il 115 120 125 Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pr 130 135 140 Asn Met Asp Pro Asn Ala Ile Phe Leu Ser Phe Gln His Leu Leu Ar 145 150 155 160 Gly Lys Val Arg Phe Leu Met Leu Val Gly Gly Ser Thr Leu Cys Va 165 170 175 Arg Glu Phe Gly Gly Asn Met Ala Ser Pro Ala Pro Pro Ala Cys As 180 185 190 Leu Arg Val Leu Ser Lys Leu Leu Arg Asp Ser His Val Leu His Se 195 200 205 Arg Leu Ser Gln Cys Pro Glu Val His Pro Leu Pro Thr Pro Val Le 210 215 220 Leu Pro Ala Val Asp Phe Ser Leu Gly Glu Trp Lys Thr Gln Met Gl 225 230 235 240 Glu Thr Lys Ala Gln Asp Ile Leu Gly Ala Val Thr Leu Leu Leu Gl 245 250 255 Gly Val Met Ala Ala Arg Gly Gln Leu Gly Pro Thr Cys Leu Ser Se 260 265 270 Leu Leu Gly Gln Leu Ser Gly Gln Val Arg Leu Leu Leu Gly Ala Le 275 280 285 Gln Ser Leu Leu Gly Thr Gln Gly Arg Thr Thr Ala His Lys 290 295 300 83 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 240 AATTCCGTCG TAAACTGACC TTCTATCTGA AAACCTTGGA GAACGCGCAG GCTCAACAGT 60 ACGTAGAGGG CGGTGGAGGC TCC 83 83 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 241 CCGGGGAGCC TCCACCGCCC TCTACGTACT GTTGAGCCTG CGCGTTCTCC AAGGTTTTCA 60 GATAGAAGGT CAGTTTACGA CGG 83 8 amino acids amino acid unknown unknown peptide 242 Gly Gly Gly Ser Gly Gly Gly Ser 1 5 12 amino acids amino acid unknown unknown peptide 243 Gly Gly Gly Ser Gly Gly Gly Ser Gly Gly Gly Ser 1 5 10 7 amino acids amino acid unknown unknown peptide 244 Ser Gly Gly Ser Gly Gly Ser 1 5 6 amino acids amino acid unknown unknown peptide 245 Glu Phe Gly Asn Met Ala 1 5 7 amino acids amino acid unknown unknown peptide 246 Glu Phe Gly Gly Asn Met Ala 1 5 10 amino acids amino acid unknown unknown peptide 247 Glu Phe Gly Gly Asn Gly Gly Asn Met Ala 1 5 10 7 amino acids amino acid unknown unknown peptide 248 Gly Gly Ser Asp Met Ala Gly 1 5 459 base pairs nucleic acid unknown unknown other nucleic acid /desc = “SYNTHETIC” 249 TCTCCCGCTC CGCCTGCTTG TGACCTCCGA GTCCTCAGTA AACTGCTTCG TGACTCCCAT 60 GTCCTTCACA GCAGACTGAG CCAGTGCCCA GAGGTTCACC CTTTGCCTAC ACCTGTCCT 120 CTGCCTGCTG TGGACTTTAG CTTGGGAGAA TGGAAAACCC AGATGGAGGA GACCAAGGC 180 CAGGACATTC TGGGAGCAGT GACCCTTCTG CTGGAGGGAG TGATGGCAGC ACGGGGACA 240 CTGGGACCCA CTTGCCTCTC ATCCCTCCTG GGGCAGCTTT CTGGACAGGT CCGTCTCCT 300 CTTGGGGCCC TGCAGAGCCT CCTTGGAACC CAGCTTCCTC CACAGGGCAG GACCACAGC 360 CACAAGGATC CCAATGCCAT CTTCCTGAGC TTCCAACACC TGCTCCGAGG AAAGGTGCG 420 TTCCTGATGC TTGTAGGAGG GTCCACCCTC TGCGTCAGG 459 447 base pairs nucleic acid unknown unknown other nucleic acid /desc = “SYNTHETIC” 250 TCTCCCGCTC CGCCTGCTTG TGACCTCCGA GTCCTCAGTA AACTGCTTCG TGACTCCCAT 60 GTCCTTCACA GCAGACTGAG CCAGTGCCCA GAGGTTCACC CTTTGCCTAC ACCTGTCCT 120 CTGCCTGCTG TGGACTTTAG CTTGGGAGAA TGGAAAACCC AGATGGAGGA GACCAAGGC 180 CAGGACATTC TGGGAGCAGT GACCCTTCTG CTGGAGGGAG TGATGGCAGC ACGGGGACA 240 CTGGGACCCA CTTGCCTCTC ATCCCTCCTG GGGCAGCTTT CTGGACAGGT CCGTCTCCT 300 CTTGGGGCCC TGCAGAGCCT CCTTGGAACC CAGGGCAGGA CCACAGCTCA CAAGGATCC 360 AATGCCATCT TCCTGAGCTT CCAACACCTG CTCCGAGGAA AGGTGCGTTT CCTGATGCT 420 GTAGGAGGGT CCACCCTCTG CGTCAGG 447 459 base pairs nucleic acid unknown unknown other nucleic acid /desc = “SYNTHETIC” 251 TCCCCAGCGC CGCCTGCTTG TGACCTCCGA GTCCTCAGTA AACTGCTTCG TGACTCCCAT 60 GTCCTTCACA GCAGACTGAG CCAGTGCCCA GAGGTTCACC CTTTGCCTAC ACCTGTCCT 120 CTGCCTGCTG TGGACTTTAG CTTGGGAGAA TGGAAAACCC AGATGGAGGA GACCAAGGC 180 CAGGACATTC TGGGAGCAGT GACCCTTCTG CTGGAGGGAG TGATGGCAGC ACGGGGACA 240 CTGGGACCCA CTTGCCTCTC ATCCCTCCTG GGGCAGCTTT CTGGACAGGT CCGTCTCCT 300 CTTGGGGCCC TGCAGAGCCT CCTTGGAACC CAGCTTCCTC CACAGGGCAG GACCACAGC 360 CACAAGGATC CCAATGCCAT CTTCCTGAGC TTCCAACACC TGCTCCGAGG AAAGGTGCG 420 TTCCTGATGC TTGTAGGAGG GTCCACCCTC TGCGTCAGG 459 153 amino acids amino acid unknown unknown peptide 252 Ser Pro Ala Pro Pro Ala Cys Asp Leu Arg Val Leu Ser Lys Leu Le 1 5 10 15 Arg Asp Ser His Val Leu His Ser Arg Leu Ser Gln Cys Pro Glu Va 20 25 30 His Pro Leu Pro Thr Pro Val Leu Leu Pro Ala Val Asp Phe Ser Le 35 40 45 Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln Asp Ile Le 50 55 60 Gly Ala Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Arg Gly Gl 65 70 75 80 Leu Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gly Gl 85 90 95 Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Thr Gln Le 100 105 110 Pro Pro Gln Gly Arg Thr Thr Ala His Lys Asp Pro Asn Ala Ile Ph 115 120 125 Leu Ser Phe Gln His Leu Leu Arg Gly Lys Val Arg Phe Leu Met Le 130 135 140 Val Gly Gly Ser Thr Leu Cys Val Arg 145 150 149 amino acids amino acid unknown unknown peptide 253 Ser Pro Ala Pro Pro Ala Cys Asp Leu Arg Val Leu Ser Lys Leu Le 1 5 10 15 Arg Asp Ser His Val Leu His Ser Arg Leu Ser Gln Cys Pro Glu Va 20 25 30 His Pro Leu Pro Thr Pro Val Leu Leu Pro Ala Val Asp Phe Ser Le 35 40 45 Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln Asp Ile Le 50 55 60 Gly Ala Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Arg Gly Gl 65 70 75 80 Leu Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gly Gl 85 90 95 Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Thr Gln Gl 100 105 110 Arg Thr Thr Ala His Lys Asp Pro Asn Ala Ile Phe Leu Ser Phe Gl 115 120 125 His Leu Leu Arg Gly Lys Val Arg Phe Leu Met Leu Val Gly Gly Se 130 135 140 Thr Leu Cys Val Arg 145 153 amino acids amino acid unknown unknown peptide 254 Ser Pro Ala Pro Pro Ala Cys Asp Leu Arg Val Leu Ser Lys Leu Le 1 5 10 15 Arg Asp Ser His Val Leu His Ser Arg Leu Ser Gln Cys Pro Glu Va 20 25 30 His Pro Leu Pro Thr Pro Val Leu Leu Pro Ala Val Asp Phe Ser Le 35 40 45 Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln Asp Ile Le 50 55 60 Gly Ala Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Arg Gly Gl 65 70 75 80 Leu Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gly Gl 85 90 95 Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Thr Gln Le 100 105 110 Pro Pro Gln Gly Arg Thr Thr Ala His Lys Asp Pro Asn Ala Ile Ph 115 120 125 Leu Ser Phe Gln His Leu Leu Arg Gly Lys Val Arg Phe Leu Met Le 130 135 140 Val Gly Gly Ser Thr Leu Cys Val Arg 145 150 64 base pairs nucleic acid unknown unknown other nucleic acid /desc = “SYNTHETIC” 255 GGATCCACCA TGAGCCGCCT GCCCGTCCTG CTCCTGCTCC AACTCCTGGT CCGCCCCGCC 60 ATGG 64 153 amino acids amino acid unknown unknown protein Modified-site 112 /note= “position 112 is deleted or Leu, Ala,VAl, Ile, Pro, Phe, Trp or Met” Modified-site 113 /note= “positoin 113 is deleted or Pro, Phe, Ala, Val, Leu, Ile, Trp or Met” Modified-site 114 /note= “position 114 is deleted or Pro, Phe, Ala, Val, Leu, Ile, Trp or Met” Modified-site 115 /note= “positon 115 is deleted or Gln, Gly, Ser, Thr, Tyr, or Asn” 256 Ser Pro Ala Pro Pro Ala Cys Asp Leu Arg Val Leu Ser Lys Leu Le 1 5 10 15 Arg Asp Ser His Val Leu His Ser Arg Leu Ser Gln Cys Pro Glu Va 20 25 30 His Pro Leu Pro Thr Pro Val Leu Leu Pro Ala Val Asp Phe Ser Le 35 40 45 Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln Asp Ile Le 50 55 60 Gly Ala Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Arg Gly Gl 65 70 75 80 Leu Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gly Gl 85 90 95 Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Thr Gln Xa 100 105 110 Xaa Xaa Xaa Gly Arg Thr Thr Ala His Lys Asp Pro Asn Ala Ile Ph 115 120 125 Leu Ser Phe Gln His Leu Leu Arg Gly Lys Val Arg Phe Leu Met Le 130 135 140 Val Gly Gly Ser Thr Leu Cys Val Arg 145 150 464 base pairs nucleic acid unknown unknown other nucleic acid /desc = “SYNTHETIC” 257 CCATGGCTAA CTGCTCTATA ATGATCGATG AAATTATACA TCACTTAAAG AGACCACCTG 60 CACCTTTGCT GGACCCGAAC AACCTCAATG ACGAAGACGT CTCTATCCTG ATGGATCGA 120 ACCTTCGACT TCCAAACCTG GAGAGCTTCG TAAGGGCTGT CAAGAACTTA GAAAATGCA 180 CAGGTATTGA GGCAATTCTT CGTAATCTCC AACCATGTCT GCCCTCTGCC ACGGCCGCA 240 CCTCTCGACA TCCAATCATC ATCAAGGCAG GTGACTGGCA AGAATTCCGG GAAAAACTG 300 CGTTCTATCT GGTTACCCTT GAGCAAGCGC AGGAACAACA GTACGTAGAG GGCGGTGGA 360 GCTCCCCGGG TGAACCGTCT GGTCCAATCT CTACTATCAA CCCGTCTCCT CCGTCTAAA 420 AATCTCATAA ATCTCCAAAC ATGTAAGGTA CCGCATGCAA GCTT 464 100 base pairs nucleic acid unknown unknown other nucleic acid /desc = “SYNTHETIC” 258 AAAACAAGAA GAAAGGCGAT AAAAAGGTTG TGGTAAGAGA AATGGATAAA AAGGGGTCGG 60 GGAAGGAAGG TGGGAGTTAA AAAAGAGGAA GTAGGTCAAG 100 11808 base pairs nucleic acid unknown unknown other nucleic acid /desc = “synthetic” 259 ACGTACTCCA TGGCTAACTG CTCTATAATG ATCGATGAAA TTATACATCA CTTAAAGAGA 60 CCACCTGCAC CTTTGCTGGA CCCGAACAAC CTCAATGACG AAGACGTCTC TATCCTGAT 120 GATCGAAACC TTCGACTTCC AAACCTGGAG AGCTTCGTAA GGGCTGTCAA GAACTTAGA 180 AATGCATCAG GTATTGAGGC AATTCTTCGT AATCTCCAAC CATGTCTGCC CTCTGCCAC 240 GCCGCACCCT CTCGACATCC AATCATCATC AAGGCAGGTG ACTGGCAAGA ATTCCGGGA 300 AAACTGACGT TCTATCTGGT TACCCTTGAG CAAGCGCAGG AACAACAGTA CGTAGAGGG 360 GGTGGAGGCT CCCCGGGTGA ACCGTCTGGT CCAATCTCTA CTATCAACCC GTCTCCTCC 420 TCTAAAGAAT CTCATAAATC TCCAAACATG GCTTTAGGCC CTGCCAGCTC CCTGCCCCA 480 AGCTTCCTGC TCAAGTCTTT AGAGCAAGTG AGGAAGATCC AGGGCGATGG CGCAGCGCT 540 CAGGAGAAGC TGTGTGCCAC CTACAAGCTG TGCCACCCCG AGGAGCTGGT GCTGCTCGG 600 CACTCTCTGG GCATCCCCTG GGCTCCCCTG AGCTCCTGCC CCAGCCAGGC CCTGCAGCT 660 GCAGGCTGCT TGAGCCAACT CCATAGCGGC CTTTTCCTCT ACCAGGGGCT CCTGCAGGC 720 CTGGAAGGGA TATCCCCCGA GTTGGGTCCC ACCTTGGACA CACTGCAGCT GGACGTCGC 780 GACTTTGCCA CCACCATCTG GCAGCAGATG GAAGAACTGG GAATGGCCCC TGCCCTGCA 840 CCCACCCAGG GTGCCATGCC GGCCTTCGCC TCTGCTTTCC AGCGCCGGGC AGGAGGGGT 900 CTGGTTGCTA GCCATCTGCA GAGCTTCCTG GAGGTGTCGT ACCGCGTTCT ACGCCACCT 960 GCGCAGCCCG ACATGGCTAC ACCAACGTAC TCCATGGCTA ACTGCTCTAT AATGATCG 1020 GAAATTATAC ATCACTTAAA GAGACCACCT GCACCTTTGC TGGACCCGAA CAACCTCA 1080 GACGAAGACG TCTCTATCCT GATGGATCGA AACCTTCGAC TTCCAAACCT GGAGAGCT 1140 GTAAGGGCTG TCAAGAACTT AGAAAATGCA TCAGGTATTG AGGCAATTCT TCGTAATC 1200 CAACCATGTC TGCCCTCTGC CACGGCCGCA CCCTCTCGAC ATCCAATCAT CATCAAGG 1260 GGTGACTGGC AAGAATTCCG GGAAAAACTG ACGTTCTATC TGGTTACCCT TGAGCAAG 1320 CAGGAACAAC AGTACGTAGA GGGCGGTGGA GGCTCCCCGG GTGAACCGTC TGGTCCAA 1380 TCTACTATCA ACCCGTCTCC TCCGTCTAAA GAATCTCATA AATCTCCAAA CATGGCTC 1440 AGCTTCCTGC TCAAGTCTTT AGAGCAAGTG AGGAAGATCC AGGGCGATGG CGCAGCGC 1500 CAGGAGAAGC TGTGTGCCAC CTACAAGCTG TGCCACCCCG AGGAGCTGGT GCTGCTCG 1560 CACTCTCTGG GCATCCCCTG GGCTCCCCTG AGCTCCTGCC CCAGCCAGGC CCTGCAGC 1620 GCAGGCTGCT TGAGCCAACT CCATAGCGGC CTTTTCCTCT ACCAGGGGCT CCTGCAGG 1680 CTGGAAGGGA TATCCCCCGA GTTGGGTCCC ACCTTGGACA CACTGCAGCT GGACGTCG 1740 GACTTTGCCA CCACCATCTG GCAGCAGATG GAAGAACTGG GAATGGCCCC TGCCCTGC 1800 CCCACCCAGG GTGCCATGCC GGCCTTCGCC TCTGCTTTCC AGCGCCGGGC AGGAGGGG 1860 CTGGTTGCTA GCCATCTGCA GAGCTTCCTG GAGGTGTCGT ACCGCGTTCT ACGCCACC 1920 GCGCAGCCCG ACATGGCTAC ACCATTAGGC CCTGCCAGCT CCCTGCCCAC GTACTCCA 1980 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCAC 2040 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA TCGAAACC 2100 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAG 2160 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCT 2220 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGT 2280 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCT 2340 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAAT 2400 CATAAATCTC CAAACATGGC TTTCCTGCTC AAGTCTTTAG AGCAAGTGAG GAAGATCC 2460 GGCGATGGCG CAGCGCTCCA GGAGAAGCTG TGTGCCACCT ACAAGCTGTG CCACCCCG 2520 GAGCTGGTGC TGCTCGGACA CTCTCTGGGC ATCCCCTGGG CTCCCCTGAG CTCCTGCC 2580 AGCCAGGCCC TGCAGCTGGC AGGCTGCTTG AGCCAACTCC ATAGCGGCCT TTTCCTCT 2640 CAGGGGCTCC TGCAGGCCCT GGAAGGGATA TCCCCCGAGT TGGGTCCCAC CTTGGACA 2700 CTGCAGCTGG ACGTCGCCGA CTTTGCCACC ACCATCTGGC AGCAGATGGA AGAACTGG 2760 ATGGCCCCTG CCCTGCAGCC CACCCAGGGT GCCATGCCGG CCTTCGCCTC TGCTTTCC 2820 CGCCGGGCAG GAGGGGTCCT GGTTGCTAGC CATCTGCAGA GCTTCCTGGA GGTGTCGT 2880 CGCGTTCTAC GCCACCTTGC GCAGCCCGAC ATGGCTACAC CATTAGGCCC TGCCAGCT 2940 CTGCCCCAGA GCACGTACTC CATGGCTAAC TGCTCTATAA TGATCGATGA AATTATAC 3000 CACTTAAAGA GACCACCTGC ACCTTTGCTG GACCCGAACA ACCTCAATGA CGAAGACG 3060 TCTATCCTGA TGGATCGAAA CCTTCGACTT CCAAACCTGG AGAGCTTCGT AAGGGCTG 3120 AAGAACTTAG AAAATGCATC AGGTATTGAG GCAATTCTTC GTAATCTCCA ACCATGTC 3180 CCCTCTGCCA CGGCCGCACC CTCTCGACAT CCAATCATCA TCAAGGCAGG TGACTGGC 3240 GAATTCCGGG AAAAACTGAC GTTCTATCTG GTTACCCTTG AGCAAGCGCA GGAACAAC 3300 TACGTAGAGG GCGGTGGAGG CTCCCCGGGT GAACCGTCTG GTCCAATCTC TACTATCA 3360 CCGTCTCCTC CGTCTAAAGA ATCTCATAAA TCTCCAAACA TGGCTGAGCA AGTGAGGA 3420 ATCCAGGGCG ATGGCGCAGC GCTCCAGGAG AAGCTGTGTG CCACCTACAA GCTGTGCC 3480 CCCGAGGAGC TGGTGCTGCT CGGACACTCT CTGGGCATCC CCTGGGCTCC CCTGAGCT 3540 TGCCCCAGCC AGGCCCTGCA GCTGGCAGGC TGCTTGAGCC AACTCCATAG CGGCCTTT 3600 CTCTACCAGG GGCTCCTGCA GGCCCTGGAA GGGATATCCC CCGAGTTGGG TCCCACCT 3660 GACACACTGC AGCTGGACGT CGCCGACTTT GCCACCACCA TCTGGCAGCA GATGGAAG 3720 CTGGGAATGG CCCCTGCCCT GCAGCCCACC CAGGGTGCCA TGCCGGCCTT CGCCTCTG 3780 TTCCAGCGCC GGGCAGGAGG GGTCCTGGTT GCTAGCCATC TGCAGAGCTT CCTGGAGG 3840 TCGTACCGCG TTCTACGCCA CCTTGCGCAG CCCGACATGG CTACACCATT AGGCCCTG 3900 AGCTCCCTGC CCCAGAGCTT CCTGCTCAAG TCTTTAACGT ACTCCATGGC TAACTGCT 3960 ATAATGATCG ATGAAATTAT ACATCACTTA AAGAGACCAC CTGCACCTTT GCTGGACC 4020 AACAACCTCA ATGACGAAGA CGTCTCTATC CTGATGGATC GAAACCTTCG ACTTCCAA 4080 CTGGAGAGCT TCGTAAGGGC TGTCAAGAAC TTAGAAAATG CATCAGGTAT TGAGGCAA 4140 CTTCGTAATC TCCAACCATG TCTGCCCTCT GCCACGGCCG CACCCTCTCG ACATCCAA 4200 ATCATCAAGG CAGGTGACTG GCAAGAATTC CGGGAAAAAC TGACGTTCTA TCTGGTTA 4260 CTTGAGCAAG CGCAGGAACA ACAGTACGTA GAGGGCGGTG GAGGCTCCCC GGGTGAAC 4320 TCTGGTCCAA TCTCTACTAT CAACCCGTCT CCTCCGTCTA AAGAATCTCA TAAATCTC 4380 AACATGGCTC TGCTCGGACA CTCTCTGGGC ATCCCCTGGG CTCCCCTGAG CTCCTGCC 4440 AGCCAGGCCC TGCAGCTGGC AGGCTGCTTG AGCCAACTCC ATAGCGGCCT TTTCCTCT 4500 CAGGGGCTCC TGCAGGCCCT GGAAGGGATA TCCCCCGAGT TGGGTCCCAC CTTGGACA 4560 CTGCAGCTGG ACGTCGCCGA CTTTGCCACC ACCATCTGGC AGCAGATGGA AGAACTGG 4620 ATGGCCCCTG CCCTGCAGCC CACCCAGGGT GCCATGCCGG CCTTCGCCTC TGCTTTCC 4680 CGCCGGGCAG GAGGGGTCCT GGTTGCTAGC CATCTGCAGA GCTTCCTGGA GGTGTCGT 4740 CGCGTTCTAC GCCACCTTGC GCAGCCCGAC ATGGCTACAC CATTAGGCCC TGCCAGCT 4800 CTGCCCCAGA GCTTCCTGCT CAAGTCTTTA GAGCAAGTGA GGAAGATCCA GGGCGATG 4860 GCAGCGCTCC AGGAGAAGCT GTGTGCCACC TACAAGCTGT GCCACCCCGA GGAGCTGG 4920 ACGTACTCCA TGGCTAACTG CTCTATAATG ATCGATGAAA TTATACATCA CTTAAAGA 4980 CCACCTGCAC CTTTGCTGGA CCCGAACAAC CTCAATGACG AAGACGTCTC TATCCTGA 5040 GATCGAAACC TTCGACTTCC AAACCTGGAG AGCTTCGTAA GGGCTGTCAA GAACTTAG 5100 AATGCATCAG GTATTGAGGC AATTCTTCGT AATCTCCAAC CATGTCTGCC CTCTGCCA 5160 GCCGCACCCT CTCGACATCC AATCATCATC AAGGCAGGTG ACTGGCAAGA ATTCCGGG 5220 AAACTGACGT TCTATCTGGT TACCCTTGAG CAAGCGCAGG AACAACAGTA CGTAGAGG 5280 GGTGGAGGCT CCCCGGGTGA ACCGTCTGGT CCAATCTCTA CTATCAACCC GTCTCCTC 5340 TCTAAAGAAT CTCATAAATC TCCAAACATG GCTCCCCTGA GCTCCTGCCC CAGCCAGG 5400 CTGCAGCTGG CAGGCTGCTT GAGCCAACTC CATAGCGGCC TTTTCCTCTA CCAGGGGC 5460 CTGCAGGCCC TGGAAGGGAT ATCCCCCGAG TTGGGTCCCA CCTTGGACAC ACTGCAGC 5520 GACGTCGCCG ACTTTGCCAC CACCATCTGG CAGCAGATGG AAGAACTGGG AATGGCCC 5580 GCCCTGCAGC CCACCCAGGG TGCCATGCCG GCCTTCGCCT CTGCTTTCCA GCGCCGGG 5640 GGAGGGGTCC TGGTTGCTAG CCATCTGCAG AGCTTCCTGG AGGTGTCGTA CCGCGTTC 5700 CGCCACCTTG CGCAGCCCGA CATGGCTACA CCATTAGGCC CTGCCAGCTC CCTGCCCC 5760 AGCTTCCTGC TCAAGTCTTT AGAGCAAGTG AGGAAGATCC AGGGCGATGG CGCAGCGC 5820 CAGGAGAAGC TGTGTGCCAC CTACAAGCTG TGCCACCCCG AGGAGCTGGT GCTGCTCG 5880 CACTCTCTGG GCATCCCCTG GGCTACGTAC TCCATGGCTA ACTGCTCTAT AATGATCG 5940 GAAATTATAC ATCACTTAAA GAGACCACCT GCACCTTTGC TGGACCCGAA CAACCTCA 6000 GACGAAGACG TCTCTATCCT GATGGATCGA AACCTTCGAC TTCCAAACCT GGAGAGCT 6060 GTAAGGGCTG TCAAGAACTT AGAAAATGCA TCAGGTATTG AGGCAATTCT TCGTAATC 6120 CAACCATGTC TGCCCTCTGC CACGGCCGCA CCCTCTCGAC ATCCAATCAT CATCAAGG 6180 GGTGACTGGC AAGAATTCCG GGAAAAACTG ACGTTCTATC TGGTTACCCT TGAGCAAG 6240 CAGGAACAAC AGTACGTAGA GGGCGGTGGA GGCTCCCCGG GTGAACCGTC TGGTCCAA 6300 TCTACTATCA ACCCGTCTCC TCCGTCTAAA GAATCTCATA AATCTCCAAA CATGGCTC 6360 GCCCTGCAGC TGGCAGGCTG CTTGAGCCAA CTCCATAGCG GCCTTTTCCT CTACCAGG 6420 CTCCTGCAGG CCCTGGAAGG GATATCCCCC GAGTTGGGTC CCACCTTGGA CACACTGC 6480 CTGGACGTCG CCGACTTTGC CACCACCATC TGGCAGCAGA TGGAAGAACT GGGAATGG 6540 CCTGCCCTGC AGCCCACCCA GGGTGCCATG CCGGCCTTCG CCTCTGCTTT CCAGCGCC 6600 GCAGGAGGGG TCCTGGTTGC TAGCCATCTG CAGAGCTTCC TGGAGGTGTC GTACCGCG 6660 CTACGCCACC TTGCGCAGCC CGACATGGCT ACACCATTAG GCCCTGCCAG CTCCCTGC 6720 CAGAGCTTCC TGCTCAAGTC TTTAGAGCAA GTGAGGAAGA TCCAGGGCGA TGGCGCAG 6780 CTCCAGGAGA AGCTGTGTGC CACCTACAAG CTGTGCCACC CCGAGGAGCT GGTGCTGC 6840 GGACACTCTC TGGGCATCCC CTGGGCTCCC CTGAGCTCCT GCCCCAGCAC GTACTCCA 6900 GCTAACTGCT CTATAATGAT CGATGAAATT ATACATCACT TAAAGAGACC ACCTGCAC 6960 TTGCTGGACC CGAACAACCT CAATGACGAA GACGTCTCTA TCCTGATGGA TCGAAACC 7020 CGACTTCCAA ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAG 7080 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC CGCACCCT 7140 CGACATCCAA TCATCATCAA GGCAGGTGAC TGGCAAGAAT TCCGGGAAAA ACTGACGT 7200 TATCTGGTTA CCCTTGAGCA AGCGCAGGAA CAACAGTACG TAGAGGGCGG TGGAGGCT 7260 CCGGGTGAAC CGTCTGGTCC AATCTCTACT ATCAACCCGT CTCCTCCGTC TAAAGAAT 7320 CATAAATCTC CAAACATGGC TCTGCAGCTG GCAGGCTGCT TGAGCCAACT CCATAGCG 7380 CTTTTCCTCT ACCAGGGGCT CCTGCAGGCC CTGGAAGGGA TATCCCCCGA GTTGGGTC 7440 ACCTTGGACA CACTGCAGCT GGACGTCGCC GACTTTGCCA CCACCATCTG GCAGCAGA 7500 GAAGAACTGG GAATGGCCCC TGCCCTGCAG CCCACCCAGG GTGCCATGCC GGCCTTCG 7560 TCTGCTTTCC AGCGCCGGGC AGGAGGGGTC CTGGTTGCTA GCCATCTGCA GAGCTTCC 7620 GAGGTGTCGT ACCGCGTTCT ACGCCACCTT GCGCAGCCCG ACATGGCTAC ACCATTAG 7680 CCTGCCAGCT CCCTGCCCCA GAGCTTCCTG CTCAAGTCTT TAGAGCAAGT GAGGAAGA 7740 CAGGGCGATG GCGCAGCGCT CCAGGAGAAG CTGTGTGCCA CCTACAAGCT GTGCCACC 7800 GAGGAGCTGG TGCTGCTCGG ACACTCTCTG GGCATCCCCT GGGCTCCCCT GAGCTCCT 7860 CCCAGCCAGG CCACGTACTC CATGGCTAAC TGCTCTATAA TGATCGATGA AATTATAC 7920 CACTTAAAGA GACCACCTGC ACCTTTGCTG GACCCGAACA ACCTCAATGA CGAAGACG 7980 TCTATCCTGA TGGATCGAAA CCTTCGACTT CCAAACCTGG AGAGCTTCGT AAGGGCTG 8040 AAGAACTTAG AAAATGCATC AGGTATTGAG GCAATTCTTC GTAATCTCCA ACCATGTC 8100 CCCTCTGCCA CGGCCGCACC CTCTCGACAT CCAATCATCA TCAAGGCAGG TGACTGGC 8160 GAATTCCGGG AAAAACTGAC GTTCTATCTG GTTACCCTTG AGCAAGCGCA GGAACAAC 8220 TACGTAGAGG GCGGTGGAGG CTCCCCGGGT GAACCGTCTG GTCCAATCTC TACTATCA 8280 CCGTCTCCTC CGTCTAAAGA ATCTCATAAA TCTCCAAACA TGGCTCTGGC AGGCTGCT 8340 AGCCAACTCC ATAGCGGCCT TTTCCTCTAC CAGGGGCTCC TGCAGGCCCT GGAAGGGA 8400 TCCCCCGAGT TGGGTCCCAC CTTGGACACA CTGCAGCTGG ACGTCGCCGA CTTTGCCA 8460 ACCATCTGGC AGCAGATGGA AGAACTGGGA ATGGCCCCTG CCCTGCAGCC CACCCAGG 8520 GCCATGCCGG CCTTCGCCTC TGCTTTCCAG CGCCGGGCAG GAGGGGTCCT GGTTGCTA 8580 CATCTGCAGA GCTTCCTGGA GGTGTCGTAC CGCGTTCTAC GCCACCTTGC GCAGCCCG 8640 ATGGCTACAC CATTAGGCCC TGCCAGCTCC CTGCCCCAGA GCTTCCTGCT CAAGTCTT 8700 GAGCAAGTGA GGAAGATCCA GGGCGATGGC GCAGCGCTCC AGGAGAAGCT GTGTGCCA 8760 TACAAGCTGT GCCACCCCGA GGAGCTGGTG CTGCTCGGAC ACTCTCTGGG CATCCCCT 8820 GCTCCCCTGA GCTCCTGCCC CAGCCAGGCC CTGCAGACGT ACTCCATGGC TAACTGCT 8880 ATAATGATCG ATGAAATTAT ACATCACTTA AAGAGACCAC CTGCACCTTT GCTGGACC 8940 AACAACCTCA ATGACGAAGA CGTCTCTATC CTGATGGATC GAAACCTTCG ACTTCCAA 9000 CTGGAGAGCT TCGTAAGGGC TGTCAAGAAC TTAGAAAATG CATCAGGTAT TGAGGCAA 9060 CTTCGTAATC TCCAACCATG TCTGCCCTCT GCCACGGCCG CACCCTCTCG ACATCCAA 9120 ATCATCAAGG CAGGTGACTG GCAAGAATTC CGGGAAAAAC TGACGTTCTA TCTGGTTA 9180 CTTGAGCAAG CGCAGGAACA ACAGTACGTA GAGGGCGGTG GAGGCTCCCC GGGTGAAC 9240 TCTGGTCCAA TCTCTACTAT CAACCCGTCT CCTCCGTCTA AAGAATCTCA TAAATCTC 9300 AACATGGCTG AACTGGGAAT GGCCCCTGCC CTGCAGCCCA CCCAGGGTGC CATGCCGG 9360 TTCGCCTCTG CTTTCCAGCG CCGGGCAGGA GGGGTCCTGG TTGCTAGCCA TCTGCAGA 9420 TTCCTGGAGG TGTCGTACCG CGTTCTACGC CACCTTGCGC AGCCCGACAT GGCTACAC 9480 TTAGGCCCTG CCAGCTCCCT GCCCCAGAGC TTCCTGCTCA AGTCTTTAGA GCAAGTGA 9540 AAGATCCAGG GCGATGGCGC AGCGCTCCAG GAGAAGCTGT GTGCCACCTA CAAGCTGT 9600 CACCCCGAGG AGCTGGTGCT GCTCGGACAC TCTCTGGGCA TCCCCTGGGC TCCCCTGA 9660 TCCTGCCCCA GCCAGGCCCT GCAGCTGGCA GGCTGCTTGA GCCAACTCCA TAGCGGCC 9720 TTCCTCTACC AGGGGCTCCT GCAGGCCCTG GAAGGGATAT CCCCCGAGTT GGGTCCCA 9780 TTGGACACAC TGCAGCTGGA CGTCGCCGAC TTTGCCACCA CCATCTGGCA GCAGATGG 9840 ACGTACTCCA TGGCTAACTG CTCTATAATG ATCGATGAAA TTATACATCA CTTAAAGA 9900 CCACCTGCAC CTTTGCTGGA CCCGAACAAC CTCAATGACG AAGACGTCTC TATCCTGA 9960 GATCGAAACC TTCGACTTCC AAACCTGGAG AGCTTCGTAA GGGCTGTCAA GAACTTA 10020 AATGCATCAG GTATTGAGGC AATTCTTCGT AATCTCCAAC CATGTCTGCC CTCTGCC 10080 GCCGCACCCT CTCGACATCC AATCATCATC AAGGCAGGTG ACTGGCAAGA ATTCCGG 10140 AAACTGACGT TCTATCTGGT TACCCTTGAG CAAGCGCAGG AACAACAGTA CGTAGAG 10200 GGTGGAGGCT CCCCGGGTGA ACCGTCTGGT CCAATCTCTA CTATCAACCC GTCTCCT 10260 TCTAAAGAAT CTCATAAATC TCCAAACATG GCTGGAATGG CCCCTGCCCT GCAGCCC 10320 CAGGGTGCCA TGCCGGCCTT CGCCTCTGCT TTCCAGCGCC GGGCAGGAGG GGTCCTG 10380 GCTAGCCATC TGCAGAGCTT CCTGGAGGTG TCGTACCGCG TTCTACGCCA CCTTGCG 10440 CCCGACATGG CTACACCATT AGGCCCTGCC AGCTCCCTGC CCCAGAGCTT CCTGCTC 10500 TCTTTAGAGC AAGTGAGGAA GATCCAGGGC GATGGCGCAG CGCTCCAGGA GAAGCTG 10560 GCCACCTACA AGCTGTGCCA CCCCGAGGAG CTGGTGCTGC TCGGACACTC TCTGGGC 10620 CCCTGGGCTC CCCTGAGCTC CTGCCCCAGC CAGGCCCTGC AGCTGGCAGG CTGCTTG 10680 CAACTCCATA GCGGCCTTTT CCTCTACCAG GGGCTCCTGC AGGCCCTGGA AGGGATA 10740 CCCGAGTTGG GTCCCACCTT GGACACACTG CAGCTGGACG TCGCCGACTT TGCCACC 10800 ATCTGGCAGC AGATGGAAGA ACTGACGTAC TCCATGGCTA ACTGCTCTAT AATGATC 10860 GAAATTATAC ATCACTTAAA GAGACCACCT GCACCTTTGC TGGACCCGAA CAACCTC 10920 GACGAAGACG TCTCTATCCT GATGGATCGA AACCTTCGAC TTCCAAACCT GGAGAGC 10980 GTAAGGGCTG TCAAGAACTT AGAAAATGCA TCAGGTATTG AGGCAATTCT TCGTAAT 11040 CAACCATGTC TGCCCTCTGC CACGGCCGCA CCCTCTCGAC ATCCAATCAT CATCAAG 11100 GGTGACTGGC AAGAATTCCG GGAAAAACTG ACGTTCTATC TGGTTACCCT TGAGCAA 11160 CAGGAACAAC AGTACGTAGA GGGCGGTGGA GGCTCCCCGG GTGAACCGTC TGGTCCA 11220 TCTACTATCA ACCCGTCTCC TCCGTCTAAA GAATCTCATA AATCTCCAAA CATGGCT 11280 TTCCTGGAGG TGTCGTACCG CGTTCTACGC CACCTTGCGC AGCCCGACAT GGCTACA 11340 TTAGGCCCTG CCAGCTCCCT GCCCCAGAGC TTCCTGCTCA AGTCTTTAGA GCAAGTG 11400 AAGATCCAGG GCGATGGCGC AGCGCTCCAG GAGAAGCTGT GTGCCACCTA CAAGCTG 11460 CACCCCGAGG AGCTGGTGCT GCTCGGACAC TCTCTGGGCA TCCCCTGGGC TCCCCTG 11520 TCCTGCCCCA GCCAGGCCCT GCAGCTGGCA GGCTGCTTGA GCCAACTCCA TAGCGGC 11580 TTCCTCTACC AGGGGCTCCT GCAGGCCCTG GAAGGGATAT CCCCCGAGTT GGGTCCC 11640 TTGGACACAC TGCAGCTGGA CGTCGCCGAC TTTGCCACCA CCATCTGGCA GCAGATG 11700 GAACTGGGAA TGGCCCCTGC CCTGCAGCCC ACCCAGGGTG CCATGCCGGC CTTCGCC 11760 GCTTTCCAGC GCCGGGCAGG AGGGGTCCTG GTTGCTAGCC ATCTGCAG 11808 975 base pairs nucleic acid unknown unknown other nucleic acid /desc = “synthetic” 260 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGATCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC CGTCTCCTCC GTCTAAAGA 420 TCTCATAAAT CTCCAAACAT GGCTCAGAGC TTCCTGCTCA AGTCTTTAGA GCAAGTGAG 480 AAGATCCAGG GCGATGGCGC AGCGCTCCAG GAGAAGCTGT GTGCCACCTA CAAGCTGTG 540 CACCCCGAGG AGCTGGTGCT GCTCGGACAC TCTCTGGGCA TCCCCTGGGC TCCCCTGAG 600 TCCTGCCCCA GCCAGGCCCT GCAGCTGGCA GGCTGCTTGA GCCAACTCCA TAGCGGCCT 660 TTCCTCTACC AGGGGCTCCT GCAGGCCCTG GAAGGGATAT CCCCCGAGTT GGGTCCCAC 720 TTGGACACAC TGCAGCTGGA CGTCGCCGAC TTTGCCACCA CCATCTGGCA GCAGATGGA 780 GAACTGGGAA TGGCCCCTGC CCTGCAGCCC ACCCAGGGTG CCATGCCGGC CTTCGCCTC 840 GCTTTCCAGC GCCGGGCAGG AGGGGTCCTG GTTGCTAGCC ATCTGCAGAG CTTCCTGGA 900 GTGTCGTACC GCGTTCTACG CCACCTTGCG CAGCCCGACA TGGCTACACC ATTAGGCCC 960 GCCAGCTCCC TGCCC 975 975 base pairs nucleic acid unknown unknown other nucleic acid /desc = “synthetic” 261 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGATCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC CGTCTCCTCC GTCTAAAGA 420 TCTCATAAAT CTCCAAACAT GGCTCAGAGC TTCCTGCTCA AGTCTTTAGA GCAAGTGAG 480 AAGATCCAGG GCGATGGCGC AGCGCTCCAG GAGAAGCTGT GTGCCACCTA CAAGCTGTG 540 CACCCCGAGG AGCTGGTGCT GCTCGGACAC TCTCTGGGCA TCCCCTGGGC TCCCCTGAG 600 TCCTGCCCCA GCCAGGCCCT GCAGCTGGCA GGCTGCTTGA GCCAACTCCA TAGCGGCCT 660 TTCCTCTACC AGGGGCTCCT GCAGGCCCTG GAAGGGATAT CCCCCGAGTT GGGTCCCAC 720 TTGGACACAC TGCAGCTGGA CGTCGCCGAC TTTGCCACCA CCATCTGGCA GCAGATGGA 780 GAACTGGGAA TGGCCCCTGC CCTGCAGCCC ACCCAGGGTG CCATGCCGGC CTTCGCCTC 840 GCTTTCCAGC GCCGGGCAGG AGGGGTCCTG GTTGCTAGCC ATCTGCAGAG CTTCCTGGA 900 GTGTCGTACC GCGTTCTACG CCACCTTGCG CAGCCCGACA TGGCTACACC ATTAGGCCC 960 GCCAGCTCCC TGCCC 975 975 base pairs nucleic acid unknown unknown other nucleic acid /desc = “synthetic” 262 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGATCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC CGTCTCCTCC GTCTAAAGA 420 TCTCATAAAT CTCCAAACAT GGCTGAGCAA GTGAGGAAGA TCCAGGGCGA TGGCGCAGC 480 CTCCAGGAGA AGCTGTGTGC CACCTACAAG CTGTGCCACC CCGAGGAGCT GGTGCTGCT 540 GGACACTCTC TGGGCATCCC CTGGGCTCCC CTGAGCTCCT GCCCCAGCCA GGCCCTGCA 600 CTGGCAGGCT GCTTGAGCCA ACTCCATAGC GGCCTTTTCC TCTACCAGGG GCTCCTGCA 660 GCCCTGGAAG GGATATCCCC CGAGTTGGGT CCCACCTTGG ACACACTGCA GCTGGACGT 720 GCCGACTTTG CCACCACCAT CTGGCAGCAG ATGGAAGAAC TGGGAATGGC CCCTGCCCT 780 CAGCCCACCC AGGGTGCCAT GCCGGCCTTC GCCTCTGCTT TCCAGCGCCG GGCAGGAGG 840 GTCCTGGTTG CTAGCCATCT GCAGAGCTTC CTGGAGGTGT CGTACCGCGT TCTACGCCA 900 CTTGCGCAGC CCGACATGGC TACACCATTA GGCCCTGCCA GCTCCCTGCC CCAGAGCTT 960 CTGCTCAAGT CTTTA 975 975 base pairs nucleic acid unknown unknown other nucleic acid /desc = “synthetic” 263 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGATCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC CGTCTCCTCC GTCTAAAGA 420 TCTCATAAAT CTCCAAACAT GGCTCTGCTC GGACACTCTC TGGGCATCCC CTGGGCTCC 480 CTGAGCTCCT GCCCCAGCCA GGCCCTGCAG CTGGCAGGCT GCTTGAGCCA ACTCCATAG 540 GGCCTTTTCC TCTACCAGGG GCTCCTGCAG GCCCTGGAAG GGATATCCCC CGAGTTGGG 600 CCCACCTTGG ACACACTGCA GCTGGACGTC GCCGACTTTG CCACCACCAT CTGGCAGCA 660 ATGGAAGAAC TGGGAATGGC CCCTGCCCTG CAGCCCACCC AGGGTGCCAT GCCGGCCTT 720 GCCTCTGCTT TCCAGCGCCG GGCAGGAGGG GTCCTGGTTG CTAGCCATCT GCAGAGCTT 780 CTGGAGGTGT CGTACCGCGT TCTACGCCAC CTTGCGCAGC CCGACATGGC TACACCATT 840 GGCCCTGCCA GCTCCCTGCC CCAGAGCTTC CTGCTCAAGT CTTTAGAGCA AGTGAGGAA 900 ATCCAGGGCG ATGGCGCAGC GCTCCAGGAG AAGCTGTGTG CCACCTACAA GCTGTGCCA 960 CCCGAGGAGC TGGTG 975 975 base pairs nucleic acid unknown unknown other nucleic acid /desc = “synthetic” 264 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGATCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC CGTCTCCTCC GTCTAAAGA 420 TCTCATAAAT CTCCAAACAT GGCTCCCCTG AGCTCCTGCC CCAGCCAGGC CCTGCAGCT 480 GCAGGCTGCT TGAGCCAACT CCATAGCGGC CTTTTCCTCT ACCAGGGGCT CCTGCAGGC 540 CTGGAAGGGA TATCCCCCGA GTTGGGTCCC ACCTTGGACA CACTGCAGCT GGACGTCGC 600 GACTTTGCCA CCACCATCTG GCAGCAGATG GAAGAACTGG GAATGGCCCC TGCCCTGCA 660 CCCACCCAGG GTGCCATGCC GGCCTTCGCC TCTGCTTTCC AGCGCCGGGC AGGAGGGGT 720 CTGGTTGCTA GCCATCTGCA GAGCTTCCTG GAGGTGTCGT ACCGCGTTCT ACGCCACCT 780 GCGCAGCCCG ACATGGCTAC ACCATTAGGC CCTGCCAGCT CCCTGCCCCA GAGCTTCCT 840 CTCAAGTCTT TAGAGCAAGT GAGGAAGATC CAGGGCGATG GCGCAGCGCT CCAGGAGAA 900 CTGTGTGCCA CCTACAAGCT GTGCCACCCC GAGGAGCTGG TGCTGCTCGG ACACTCTCT 960 GGCATCCCCT GGGCT 975 975 base pairs nucleic acid unknown unknown other nucleic acid /desc = “synthetic” 265 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGATCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC CGTCTCCTCC GTCTAAAGA 420 TCTCATAAAT CTCCAAACAT GGCTCAGGCC CTGCAGCTGG CAGGCTGCTT GAGCCAACT 480 CATAGCGGCC TTTTCCTCTA CCAGGGGCTC CTGCAGGCCC TGGAAGGGAT ATCCCCCGA 540 TTGGGTCCCA CCTTGGACAC ACTGCAGCTG GACGTCGCCG ACTTTGCCAC CACCATCTG 600 CAGCAGATGG AAGAACTGGG AATGGCCCCT GCCCTGCAGC CCACCCAGGG TGCCATGCC 660 GCCTTCGCCT CTGCTTTCCA GCGCCGGGCA GGAGGGGTCC TGGTTGCTAG CCATCTGCA 720 AGCTTCCTGG AGGTGTCGTA CCGCGTTCTA CGCCACCTTG CGCAGCCCGA CATGGCTAC 780 CCATTAGGCC CTGCCAGCTC CCTGCCCCAG AGCTTCCTGC TCAAGTCTTT AGAGCAAGT 840 AGGAAGATCC AGGGCGATGG CGCAGCGCTC CAGGAGAAGC TGTGTGCCAC CTACAAGCT 900 TGCCACCCCG AGGAGCTGGT GCTGCTCGGA CACTCTCTGG GCATCCCCTG GGCTCCCCT 960 AGCTCCTGCC CCAGC 975 975 base pairs nucleic acid unknown unknown other nucleic acid /desc = “synthetic” 266 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGATCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC CGTCTCCTCC GTCTAAAGA 420 TCTCATAAAT CTCCAAACAT GGCTCTGCAG CTGGCAGGCT GCTTGAGCCA ACTCCATAG 480 GGCCTTTTCC TCTACCAGGG GCTCCTGCAG GCCCTGGAAG GGATATCCCC CGAGTTGGG 540 CCCACCTTGG ACACACTGCA GCTGGACGTC GCCGACTTTG CCACCACCAT CTGGCAGCA 600 ATGGAAGAAC TGGGAATGGC CCCTGCCCTG CAGCCCACCC AGGGTGCCAT GCCGGCCTT 660 GCCTCTGCTT TCCAGCGCCG GGCAGGAGGG GTCCTGGTTG CTAGCCATCT GCAGAGCTT 720 CTGGAGGTGT CGTACCGCGT TCTACGCCAC CTTGCGCAGC CCGACATGGC TACACCATT 780 GGCCCTGCCA GCTCCCTGCC CCAGAGCTTC CTGCTCAAGT CTTTAGAGCA AGTGAGGAA 840 ATCCAGGGCG ATGGCGCAGC GCTCCAGGAG AAGCTGTGTG CCACCTACAA GCTGTGCCA 900 CCCGAGGAGC TGGTGCTGCT CGGACACTCT CTGGGCATCC CCTGGGCTCC CCTGAGCTC 960 TGCCCCAGCC AGGCC 975 975 base pairs nucleic acid unknown unknown other nucleic acid /desc = “synthetic” 267 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGATCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC CGTCTCCTCC GTCTAAAGA 420 TCTCATAAAT CTCCAAACAT GGCTCTGGCA GGCTGCTTGA GCCAACTCCA TAGCGGCCT 480 TTCCTCTACC AGGGGCTCCT GCAGGCCCTG GAAGGGATAT CCCCCGAGTT GGGTCCCAC 540 TTGGACACAC TGCAGCTGGA CGTCGCCGAC TTTGCCACCA CCATCTGGCA GCAGATGGA 600 GAACTGGGAA TGGCCCCTGC CCTGCAGCCC ACCCAGGGTG CCATGCCGGC CTTCGCCTC 660 GCTTTCCAGC GCCGGGCAGG AGGGGTCCTG GTTGCTAGCC ATCTGCAGAG CTTCCTGGA 720 GTGTCGTACC GCGTTCTACG CCACCTTGCG CAGCCCGACA TGGCTACACC ATTAGGCCC 780 GCCAGCTCCC TGCCCCAGAG CTTCCTGCTC AAGTCTTTAG AGCAAGTGAG GAAGATCCA 840 GGCGATGGCG CAGCGCTCCA GGAGAAGCTG TGTGCCACCT ACAAGCTGTG CCACCCCGA 900 GAGCTGGTGC TGCTCGGACA CTCTCTGGGC ATCCCCTGGG CTCCCCTGAG CTCCTGCCC 960 AGCCAGGCCC TGCAG 975 975 base pairs nucleic acid single linear other nucleic acid /desc = “synthetic” 268 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGATCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC CGTCTCCTCC GTCTAAAGA 420 TCTCATAAAT CTCCAAACAT GGCTGAACTG GGAATGGCCC CTGCCCTGCA GCCCACCCA 480 GGTGCCATGC CGGCCTTCGC CTCTGCTTTC CAGCGCCGGG CAGGAGGGGT CCTGGTTGC 540 AGCCATCTGC AGAGCTTCCT GGAGGTGTCG TACCGCGTTC TACGCCACCT TGCGCAGCC 600 GACATGGCTA CACCATTAGG CCCTGCCAGC TCCCTGCCCC AGAGCTTCCT GCTCAAGTC 660 TTAGAGCAAG TGAGGAAGAT CCAGGGCGAT GGCGCAGCGC TCCAGGAGAA GCTGTGTGC 720 ACCTACAAGC TGTGCCACCC CGAGGAGCTG GTGCTGCTCG GACACTCTCT GGGCATCCC 780 TGGGCTCCCC TGAGCTCCTG CCCCAGCCAG GCCCTGCAGC TGGCAGGCTG CTTGAGCCA 840 CTCCATAGCG GCCTTTTCCT CTACCAGGGG CTCCTGCAGG CCCTGGAAGG GATATCCCC 900 GAGTTGGGTC CCACCTTGGA CACACTGCAG CTGGACGTCG CCGACTTTGC CACCACCAT 960 TGGCAGCAGA TGGAA 975 975 base pairs nucleic acid unknown unknown other nucleic acid /desc = “synthetic” 269 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGATCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC CGTCTCCTCC GTCTAAAGA 420 TCTCATAAAT CTCCAAACAT GGCTGGAATG GCCCCTGCCC TGCAGCCCAC CCAGGGTGC 480 ATGCCGGCCT TCGCCTCTGC TTTCCAGCGC CGGGCAGGAG GGGTCCTGGT TGCTAGCCA 540 CTGCAGAGCT TCCTGGAGGT GTCGTACCGC GTTCTACGCC ACCTTGCGCA GCCCGACAT 600 GCTACACCAT TAGGCCCTGC CAGCTCCCTG CCCCAGAGCT TCCTGCTCAA GTCTTTAGA 660 CAAGTGAGGA AGATCCAGGG CGATGGCGCA GCGCTCCAGG AGAAGCTGTG TGCCACCTA 720 AAGCTGTGCC ACCCCGAGGA GCTGGTGCTG CTCGGACACT CTCTGGGCAT CCCCTGGGC 780 CCCCTGAGCT CCTGCCCCAG CCAGGCCCTG CAGCTGGCAG GCTGCTTGAG CCAACTCCA 840 AGCGGCCTTT TCCTCTACCA GGGGCTCCTG CAGGCCCTGG AAGGGATATC CCCCGAGTT 900 GGTCCCACCT TGGACACACT GCAGCTGGAC GTCGCCGACT TTGCCACCAC CATCTGGCA 960 CAGATGGAAG AACTG 975 975 base pairs nucleic acid unknown unknown other nucleic acid /desc = “synthetic” 270 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG ACCACCTGCA 60 CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGATCGAAA 120 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA AAATGCATC 180 GGTATTGAGG CAATTCTTCG TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACC 240 TCTCGACATC CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGAC 300 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG CGGTGGAGG 360 TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC CGTCTCCTCC GTCTAAAGA 420 TCTCATAAAT CTCCAAACAT GGCTAGCTTC CTGGAGGTGT CGTACCGCGT TCTACGCCA 480 CTTGCGCAGC CCGACATGGC TACACCATTA GGCCCTGCCA GCTCCCTGCC CCAGAGCTT 540 CTGCTCAAGT CTTTAGAGCA AGTGAGGAAG ATCCAGGGCG ATGGCGCAGC GCTCCAGGA 600 AAGCTGTGTG CCACCTACAA GCTGTGCCAC CCCGAGGAGC TGGTGCTGCT CGGACACTC 660 CTGGGCATCC CCTGGGCTCC CCTGAGCTCC TGCCCCAGCC AGGCCCTGCA GCTGGCAGG 720 TGCTTGAGCC AACTCCATAG CGGCCTTTTC CTCTACCAGG GGCTCCTGCA GGCCCTGGA 780 GGGATATCCC CCGAGTTGGG TCCCACCTTG GACACACTGC AGCTGGACGT CGCCGACTT 840 GCCACCACCA TCTGGCAGCA GATGGAAGAA CTGGGAATGG CCCCTGCCCT GCAGCCCAC 900 CAGGGTGCCA TGCCGGCCTT CGCCTCTGCT TTCCAGCGCC GGGCAGGAGG GGTCCTGGT 960 GCTAGCCATC TGCAG 975 325 amino acids amino acid unknown unknown peptide 271 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Ly 1 5 10 15 Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu As 20 25 30 Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Se 35 40 45 Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Al 50 55 60 Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pr 65 70 75 80 Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Ar 85 90 95 Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gl 100 105 110 Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pr 115 120 125 Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Se 130 135 140 Pro Asn Met Ala Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe Le 145 150 155 160 Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Al 165 170 175 Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Gl 180 185 190 Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Se 195 200 205 Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Le 210 215 220 His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gl 225 230 235 240 Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Va 245 250 255 Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Me 260 265 270 Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Se 275 280 285 Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gl 290 295 300 Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pr 305 310 315 320 Asp Met Ala Thr Pro 325 325 amino acids amino acid unknown unknown peptide 272 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Ly 1 5 10 15 Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu As 20 25 30 Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Se 35 40 45 Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Al 50 55 60 Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pr 65 70 75 80 Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Ar 85 90 95 Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gl 100 105 110 Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pr 115 120 125 Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Se 130 135 140 Pro Asn Met Ala Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe Le 145 150 155 160 Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Al 165 170 175 Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Gl 180 185 190 Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Se 195 200 205 Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Le 210 215 220 His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gl 225 230 235 240 Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Va 245 250 255 Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Me 260 265 270 Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Se 275 280 285 Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gl 290 295 300 Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pr 305 310 315 320 Asp Met Ala Thr Pro 325 325 amino acids amino acid unknown unknown peptide 273 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Ly 1 5 10 15 Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu As 20 25 30 Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Se 35 40 45 Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Al 50 55 60 Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pr 65 70 75 80 Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Ar 85 90 95 Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gl 100 105 110 Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pr 115 120 125 Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Se 130 135 140 Pro Asn Met Ala Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Il 145 150 155 160 Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Ly 165 170 175 Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Il 180 185 190 Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Al 195 200 205 Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Le 210 215 220 Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu As 225 230 235 240 Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gl 245 250 255 Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Al 260 265 270 Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Le 275 280 285 Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Le 290 295 300 Arg His Leu Ala Gln Pro Asp Met Ala Thr Pro Leu Gly Pro Ala Se 305 310 315 320 Ser Leu Pro Gln Ser 325 325 amino acids amino acid unknown unknown peptide 274 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Ly 1 5 10 15 Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu As 20 25 30 Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Se 35 40 45 Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Al 50 55 60 Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pr 65 70 75 80 Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Ar 85 90 95 Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gl 100 105 110 Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pr 115 120 125 Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Se 130 135 140 Pro Asn Met Ala Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Al 145 150 155 160 Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Gl 165 170 175 Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Se 180 185 190 Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Le 195 200 205 His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gl 210 215 220 Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Va 225 230 235 240 Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Me 245 250 255 Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Se 260 265 270 Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gl 275 280 285 Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pr 290 295 300 Asp Met Ala Thr Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Ph 305 310 315 320 Leu Leu Lys Ser Leu 325 325 amino acids amino acid unknown unknown peptide 275 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Ly 1 5 10 15 Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu As 20 25 30 Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Se 35 40 45 Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Al 50 55 60 Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pr 65 70 75 80 Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Ar 85 90 95 Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gl 100 105 110 Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pr 115 120 125 Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Se 130 135 140 Pro Asn Met Ala Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pr 145 150 155 160 Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Se 165 170 175 Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Le 180 185 190 Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Le 195 200 205 Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Le 210 215 220 Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Ph 225 230 235 240 Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser Hi 245 250 255 Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Al 260 265 270 Gln Pro Asp Met Ala Thr Pro Leu Gly Pro Ala Ser Ser Leu Pro Gl 275 280 285 Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly As 290 295 300 Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys Hi 305 310 315 320 Pro Glu Glu Leu Val 325 325 amino acids amino acid unknown unknown peptide 276 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Ly 1 5 10 15 Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu As 20 25 30 Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Se 35 40 45 Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Al 50 55 60 Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pr 65 70 75 80 Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Ar 85 90 95 Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gl 100 105 110 Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pr 115 120 125 Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Se 130 135 140 Pro Asn Met Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Le 145 150 155 160 Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gl 165 170 175 Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Le 180 185 190 Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gl 195 200 205 Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gl 210 215 220 Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Va 225 230 235 240 Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Va 245 250 255 Leu Arg His Leu Ala Gln Pro Asp Met Ala Thr Pro Leu Gly Pro Al 260 265 270 Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Ar 275 280 285 Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Th 290 295 300 Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Le 305 310 315 320 Gly Ile Pro Trp Ala 325 325 amino acids amino acid unknown unknown peptide 277 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Ly 1 5 10 15 Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu As 20 25 30 Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Se 35 40 45 Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Al 50 55 60 Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pr 65 70 75 80 Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Ar 85 90 95 Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gl 100 105 110 Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pr 115 120 125 Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Se 130 135 140 Pro Asn Met Ala Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Le 145 150 155 160 His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gl 165 170 175 Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Va 180 185 190 Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Me 195 200 205 Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Se 210 215 220 Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gl 225 230 235 240 Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pr 245 250 255 Asp Met Ala Thr Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Ph 260 265 270 Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Al 275 280 285 Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Gl 290 295 300 Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Le 305 310 315 320 Ser Ser Cys Pro Ser 325 325 amino acids amino acid unknown unknown peptide 278 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Ly 1 5 10 15 Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu As 20 25 30 Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Se 35 40 45 Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Al 50 55 60 Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pr 65 70 75 80 Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Ar 85 90 95 Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gl 100 105 110 Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pr 115 120 125 Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Se 130 135 140 Pro Asn Met Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Se 145 150 155 160 Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Se 165 170 175 Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala As 180 185 190 Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pr 195 200 205 Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Ph 210 215 220 Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Ph 225 230 235 240 Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Asp Me 245 250 255 Ala Thr Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Le 260 265 270 Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Le 275 280 285 Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Le 290 295 300 Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Se 305 310 315 320 Cys Pro Ser Gln Ala 325 325 amino acids amino acid unknown unknown peptide 279 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Ly 1 5 10 15 Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu As 20 25 30 Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Se 35 40 45 Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Al 50 55 60 Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pr 65 70 75 80 Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Ar 85 90 95 Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gl 100 105 110 Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pr 115 120 125 Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Se 130 135 140 Pro Asn Met Ala Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Le 145 150 155 160 Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Gl 165 170 175 Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Al 180 185 190 Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Le 195 200 205 Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Ar 210 215 220 Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Gl 225 230 235 240 Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Asp Met Ala Th 245 250 255 Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys Se 260 265 270 Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Gl 275 280 285 Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Le 290 295 300 Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pr 305 310 315 320 Ser Gln Ala Leu Gln 325 325 amino acids amino acid unknown unknown peptide 280 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Ly 1 5 10 15 Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu As 20 25 30 Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Se 35 40 45 Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Al 50 55 60 Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pr 65 70 75 80 Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Ar 85 90 95 Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gl 100 105 110 Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pr 115 120 125 Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Se 130 135 140 Pro Asn Met Ala Glu Leu Gly Met Ala Pro Ala Leu Gln Pro Thr Gl 145 150 155 160 Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gl 165 170 175 Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Ar 180 185 190 Val Leu Arg His Leu Ala Gln Pro Asp Met Ala Thr Pro Leu Gly Pr 195 200 205 Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Va 210 215 220 Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Al 225 230 235 240 Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Se 245 250 255 Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Le 260 265 270 Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Ty 275 280 285 Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pr 290 295 300 Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Il 305 310 315 320 Trp Gln Gln Met Glu 325 325 amino acids amino acid unknown unknown peptide 281 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Ly 1 5 10 15 Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu As 20 25 30 Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Se 35 40 45 Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Al 50 55 60 Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pr 65 70 75 80 Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Ar 85 90 95 Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gl 100 105 110 Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pr 115 120 125 Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Se 130 135 140 Pro Asn Met Ala Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Al 145 150 155 160 Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Le 165 170 175 Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Le 180 185 190 Arg His Leu Ala Gln Pro Asp Met Ala Thr Pro Leu Gly Pro Ala Se 195 200 205 Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Ly 210 215 220 Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Ty 225 230 235 240 Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gl 245 250 255 Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Le 260 265 270 Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gl 275 280 285 Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Le 290 295 300 Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gl 305 310 315 320 Gln Met Glu Glu Leu 325 325 amino acids amino acid unknown unknown peptide 282 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Ly 1 5 10 15 Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu As 20 25 30 Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Se 35 40 45 Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Al 50 55 60 Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pr 65 70 75 80 Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Ar 85 90 95 Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gl 100 105 110 Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pr 115 120 125 Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Se 130 135 140 Pro Asn Met Ala Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg Hi 145 150 155 160 Leu Ala Gln Pro Asp Met Ala Thr Pro Leu Gly Pro Ala Ser Ser Le 165 170 175 Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gl 180 185 190 Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Le 195 200 205 Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pr 210 215 220 Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gl 225 230 235 240 Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Le 245 250 255 Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Th 260 265 270 Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Me 275 280 285 Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Me 290 295 300 Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Va 305 310 315 320 Ala Ser His Leu Gln 325 153 amino acids amino acid unknown unknown peptide Modified-site 7 /note= “Xaa at position 7 is Ser or Ala;” Modified-site 112 /note= “Xaa at position 112 is deleted or Leu, Ala, Val, Ile, Pro, Phe, Trp, or Met;” Modified-site 113 /note= “Xaa at position 113 is deleted or Pro, Phe, Ala, Val, Leu, Ile, Trp, or Met;” Modified-site 114 /note= “Xaa at position 114 is deleted or Pro, Phe, Ala, Val, Leu, Ile, Trp, or Met;” Modified-site 115 /note= “Xaa at position 115 is deleted or Gln, Gly, Ser, Thr, Tyr, or Asn;” Modified-site 151 /note= “Xaa at position 151 is Ser or Ala;” 283 Ser Pro Ala Pro Pro Ala Xaa Asp Leu Arg Val Leu Ser Lys Leu Le 1 5 10 15 Arg Asp Ser His Val Leu His Ser Arg Leu Ser Gln Cys Pro Glu Va 20 25 30 His Pro Leu Pro Thr Pro Val Leu Leu Pro Ala Val Asp Phe Ser Le 35 40 45 Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln Asp Ile Le 50 55 60 Gly Ala Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Arg Gly Gl 65 70 75 80 Leu Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gly Gl 85 90 95 Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Thr Gln Xa 100 105 110 Xaa Xaa Xaa Gly Arg Thr Thr Ala His Lys Asp Pro Asn Ala Ile Ph 115 120 125 Leu Ser Phe Gln His Leu Leu Arg Gly Lys Val Arg Phe Leu Met Le 130 135 140 Val Gly Gly Ser Thr Leu Xaa Val Arg 145 150 162 amino acids amino acid unknown unknown peptide 284 Met Ala Gly Arg Thr Thr Ala His Lys Asp Pro Asn Ala Ile Phe Le 1 5 10 15 Ser Phe Gln His Leu Leu Arg Gly Lys Val Arg Phe Leu Met Leu Va 20 25 30 Gly Gly Ser Thr Leu Ala Val Arg Glu Phe Gly Gly Asn Met Ala Se 35 40 45 Pro Ala Pro Pro Ala Ala Asp Leu Arg Val Leu Ser Lys Leu Leu Ar 50 55 60 Asp Ser His Val Leu His Ser Arg Leu Ser Gln Cys Pro Glu Val Hi 65 70 75 80 Pro Leu Pro Thr Pro Val Leu Leu Pro Ala Val Asp Phe Ser Leu Gl 85 90 95 Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln Asp Ile Leu Gl 100 105 110 Ala Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Arg Gly Gln Le 115 120 125 Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gly Gln Va 130 135 140 Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Thr Gln Leu Pr 145 150 155 160 Pro Gln 162 amino acids amino acid unknown unknown peptide 285 Met Ala Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gl 1 5 10 15 Gln Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Thr Gl 20 25 30 Leu Pro Pro Gln Gly Arg Thr Thr Ala His Lys Asp Pro Asn Ala Il 35 40 45 Phe Leu Ser Phe Gln His Leu Leu Arg Gly Lys Val Arg Phe Leu Me 50 55 60 Leu Val Gly Gly Ser Thr Leu Ala Val Arg Glu Phe Gly Gly Asn Me 65 70 75 80 Ala Ser Pro Ala Pro Pro Ala Ala Asp Leu Arg Val Leu Ser Lys Le 85 90 95 Leu Arg Asp Ser His Val Leu His Ser Arg Leu Ser Gln Cys Pro Gl 100 105 110 Val His Pro Leu Pro Thr Pro Val Leu Leu Pro Ala Val Asp Phe Se 115 120 125 Leu Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln Asp Il 130 135 140 Leu Gly Ala Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Arg Gl 145 150 155 160 Gln Leu 180 amino acids amino acid unknown unknown peptide 286 Ala Thr Gly Gly Cys Thr Gly Gly Ala Cys Cys Cys Ala Cys Thr Th 1 5 10 15 Gly Cys Cys Thr Cys Thr Cys Ala Thr Cys Cys Cys Thr Cys Cys Th 20 25 30 Gly Gly Gly Gly Cys Ala Gly Cys Thr Thr Thr Cys Thr Gly Gly Al 35 40 45 Cys Ala Gly Gly Thr Cys Cys Gly Thr Cys Thr Cys Cys Thr Cys Cy 50 55 60 Thr Thr Gly Gly Gly Gly Cys Cys Cys Thr Gly Cys Ala Gly Ala Gl 65 70 75 80 Cys Cys Thr Cys Cys Thr Thr Gly Gly Ala Ala Cys Cys Cys Ala Gl 85 90 95 Cys Thr Thr Cys Cys Thr Cys Cys Ala Cys Ala Gly Gly Gly Cys Al 100 105 110 Gly Gly Ala Cys Cys Ala Cys Ala Gly Cys Thr Cys Ala Cys Ala Al 115 120 125 Gly Gly Ala Thr Cys Cys Cys Ala Ala Thr Gly Cys Cys Ala Thr Cy 130 135 140 Thr Thr Cys Cys Thr Gly Ala Gly Cys Thr Thr Cys Cys Ala Ala Cy 145 150 155 160 Ala Cys Cys Thr Gly Cys Thr Cys Cys Gly Ala Gly Gly Ala Ala Al 165 170 175 Gly Gly Thr Gly 180 486 base pairs nucleic acid unknown unknown other nucleic acid /desc = ”synthetic“ 287 ATGGCTGGCA GGACCACAGC TCACAAGGAT CCCAATGCCA TCTTCCTGAG CTTCCAACAC 60 CTGCTCCGAG GAAAGGTGCG TTTCCTGATG CTTGTAGGAG GGTCCACCCT CGCCGTCAG 120 GAATTCGGCG GCAACATGGC GTCTCCGGCG CCGCCTGCTG CTGACCTCCG AGTCCTCAG 180 AAACTGCTTC GTGACTCCCA TGTCCTTCAC AGCAGACTGA GCCAGTGCCC AGAGGTTCA 240 CCTTTGCCTA CACCTGTCCT GCTGCCTGCT GTGGACTTTA GCTTGGGAGA ATGGAAAAC 300 CAGATGGAGG AGACCAAGGC ACAGGACATT CTGGGAGCAG TGACCCTTCT GCTGGAGGG 360 GTGATGGCAG CACGGGGACA ACTGGGACCC ACTTGCCTCT CATCCCTCCT GGGGCAGCT 420 TCTGGACAGG TCCGTCTCCT CCTTGGGGCC CTGCAGAGCC TCCTTGGAAC CCAGCTTCC 480 CCACAG 486 531 base pairs nucleic acid unknown unknown other nucleic acid /desc = ”synthetic“ 288 CAGAGCTTCC TGCTCAAGTC TTTAGAGCAA GTGAGGAAGA TCCAGGGCGA TGGCGCAGCG 60 CTCCAGGAGA AGCTGTGTGC CACCTACAAG CTGTGCCACC CCGAGGAGCT GGTGCTGCT 120 GGACACTCTC TGGGCATCCC CTGGGCTCCC CTGAGCTCCT GCCCCAGCCA GGCCCTGCA 180 CTGGCAGGCT GCTTGAGCCA ACTCCATAGC GGCCTTTTCC TCTACCAGGG GCTCCTGCA 240 GCCCTGGAAG GGATATCCCC CGAGTTGGGT CCCACCTTGG ACACACTGCA GCTGGACGT 300 GCCGACTTTG CCACCACCAT CTGGCAGCAG ATGGAAGAAC TGGGAATGGC CCCTGCCCT 360 CAGCCCACCC AGGGTGCCAT GCCGGCCTTC GCCTCTGCTT TCCAGCGCCG GGCAGGAGG 420 GTCCTGGTTG CTAGCCATCT GCAGAGCTTC CTGGAGGTGT CGTACCGCGT TCTACGCCA 480 CTTGCGCAGC CCGACATGGC TACACCATTA GGCCCTGCCA GCTCCCTGCC C 531 531 base pairs nucleic acid unknown unknown other nucleic acid /desc = ”synthetic“ 289 GAACTGGGAA TGGCCCCTGC CCTGCAGCCC ACCCAGGGTG CCATGCCGGC CTTCGCCTCT 60 GCTTTCCAGC GCCGGGCAGG AGGGGTCCTG GTTGCTAGCC ATCTGCAGAG CTTCCTGGA 120 GTGTCGTACC GCGTTCTACG CCACCTTGCG CAGCCCGACA TGGCTACACC ATTAGGCCC 180 GCCAGCTCCC TGCCCCAGAG CTTCCTGCTC AAGTCTTTAG AGCAAGTGAG GAAGATCCA 240 GGCGATGGCG CAGCGCTCCA GGAGAAGCTG TGTGCCACCT ACAAGCTGTG CCACCCCGA 300 GAGCTGGTGC TGCTCGGACA CTCTCTGGGC ATCCCCTGGG CTCCCCTGAG CTCCTGCCC 360 AGCCAGGCCC TGCAGCTGGC AGGCTGCTTG AGCCAACTCC ATAGCGGCCT TTTCCTCTA 420 CAGGGGCTCC TGCAGGCCCT GGAAGGGATA TCCCCCGAGT TGGGTCCCAC CTTGGACAC 480 CTGCAGCTGG ACGTCGCCGA CTTTGCCACC ACCATCTGGC AGCAGATGGA A 531 531 base pairs nucleic acid unknown unknown other nucleic acid /desc = ”synthetic“ 290 GGAATGGCCC CTGCCCTGCA GCCCACCCAG GGTGCCATGC CGGCCTTCGC CTCTGCTTTC 60 CAGCGCCGGG CAGGAGGGGT CCTGGTTGCT AGCCATCTGC AGAGCTTCCT GGAGGTGTC 120 TACCGCGTTC TACGCCACCT TGCGCAGCCC GACATGGCTA CACCATTAGG CCCTGCCAG 180 TCCCTGCCCC AGAGCTTCCT GCTCAAGTCT TTAGAGCAAG TGAGGAAGAT CCAGGGCGA 240 GGCGCAGCGC TCCAGGAGAA GCTGTGTGCC ACCTACAAGC TGTGCCACCC CGAGGAGCT 300 GTGCTGCTCG GACACTCTCT GGGCATCCCC TGGGCTCCCC TGAGCTCCTG CCCCAGCCA 360 GCCCTGCAGC TGGCAGGCTG CTTGAGCCAA CTCCATAGCG GCCTTTTCCT CTACCAGGG 420 CTCCTGCAGG CCCTGGAAGG GATATCCCCC GAGTTGGGTC CCACCTTGGA CACACTGCA 480 CTGGACGTCG CCGACTTTGC CACCACCATC TGGCAGCAGA TGGAAGAACT G 531 531 base pairs nucleic acid unknown unknown other nucleic acid /desc = ”synthetic“ 291 TTCCTGCTCA AGTCTTTAGA GCAAGTGAGG AAGATCCAGG GCGATGGCGC AGCGCTCCAG 60 GAGAAGCTGT GTGCCACCTA CAAGCTGTGC CACCCCGAGG AGCTGGTGCT GCTCGGACA 120 TCTCTGGGCA TCCCCTGGGC TCCCCTGAGC TCCTGCCCCA GCCAGGCCCT GCAGCTGGC 180 GGCTGCTTGA GCCAACTCCA TAGCGGCCTT TTCCTCTACC AGGGGCTCCT GCAGGCCCT 240 GAAGGGATAT CCCCCGAGTT GGGTCCCACC TTGGACACAC TGCAGCTGGA CGTCGCCGA 300 TTTGCCACCA CCATCTGGCA GCAGATGGAA GAACTGGGAA TGGCCCCTGC CCTGCAGCC 360 ACCCAGGGTG CCATGCCGGC CTTCGCCTCT GCTTTCCAGC GCCGGGCAGG AGGGGTCCT 420 GTTGCTAGCC ATCTGCAGAG CTTCCTGGAG GTGTCGTACC GCGTTCTACG CCACCTTGC 480 CAGCCCGACA TGGCTACACC ATTAGGCCCT GCCAGCTCCC TGCCCCAGAG C 531 531 base pairs nucleic acid unknown unknown other nucleic acid /desc = ”synthetic“ 292 AGCTTCCTGG AGGTGTCGTA CCGCGTTCTA CGCCACCTTG CGCAGCCCGA CATGGCTACA 60 CCATTAGGCC CTGCCAGCTC CCTGCCCCAG AGCTTCCTGC TCAAGTCTTT AGAGCAAGT 120 AGGAAGATCC AGGGCGATGG CGCAGCGCTC CAGGAGAAGC TGTGTGCCAC CTACAAGCT 180 TGCCACCCCG AGGAGCTGGT GCTGCTCGGA CACTCTCTGG GCATCCCCTG GGCTCCCCT 240 AGCTCCTGCC CCAGCCAGGC CCTGCAGCTG GCAGGCTGCT TGAGCCAACT CCATAGCGG 300 CTTTTCCTCT ACCAGGGGCT CCTGCAGGCC CTGGAAGGGA TATCCCCCGA GTTGGGTCC 360 ACCTTGGACA CACTGCAGCT GGACGTCGCC GACTTTGCCA CCACCATCTG GCAGCAGAT 420 GAAGAACTGG GAATGGCCCC TGCCCTGCAG CCCACCCAGG GTGCCATGCC GGCCTTCGC 480 TCTGCTTTCC AGCGCCGGGC AGGAGGGGTC CTGGTTGCTA GCCATCTGCA G 531 531 base pairs nucleic acid unknown unknown other nucleic acid /desc = ”synthetic“ 293 AGCTTCCTGG AGGTGTCGTA CCGCGTTCTA CGCCACCTTG CGCAGCCCGA CATGGCTACA 60 CCATTAGGCC CTGCCAGCTC CCTGCCCCAG AGCTTCCTGC TCAAGTCTTT AGAGCAAGT 120 AGGAAGATCC AGGGCGATGG CGCAGCGCTC CAGGAGAAGC TGTGTGCCAC CTACAAGCT 180 TGCCACCCCG AGGAGCTGGT GCTGCTCGGA CACTCTCTGG GCATCCCCTG GGCTCCCCT 240 AGCTCCTGCC CCAGCCAGGC CCTGCAGCTG GCAGGCTGCT TGAGCCAACT CCATAGCGG 300 CTTTTCCTCT ACCAGGGGCT CCTGCAGGCC CTGGAAGGGA TATCCCCCGA GTTGGGTCC 360 ACCTTGGACA CACTGCAGCT GGACGTCGCC GACTTTGCCA CCACCATCTG GCAGCAGAT 420 GAAGAACTGG GAATGGCCCC TGCCCTGCAG CCCACCCAGG GTGCCATGCC GGCCTTCGC 480 TCTGCTTTCC AGCGCCGGGC AGGAGGGGTC CTGGTTGCTA GCCATCTGCA G 531 531 base pairs nucleic acid unknown unknown other nucleic acid /desc = ”synthetic“ 294 TTAGGCCCTG CCAGCTCCCT GCCCCAGAGC TTCCTGCTCA AGTCTTTAGA GCAAGTGAGG 60 AAGATCCAGG GCGATGGCGC AGCGCTCCAG GAGAAGCTGT GTGCCACCTA CAAGCTGTG 120 CACCCCGAGG AGCTGGTGCT GCTCGGACAC TCTCTGGGCA TCCCCTGGGC TCCCCTGAG 180 TCCTGCCCCA GCCAGGCCCT GCAGCTGGCA GGCTGCTTGA GCCAACTCCA TAGCGGCCT 240 TTCCTCTACC AGGGGCTCCT GCAGGCCCTG GAAGGGATAT CCCCCGAGTT GGGTCCCAC 300 TTGGACACAC TGCAGCTGGA CGTCGCCGAC TTTGCCACCA CCATCTGGCA GCAGATGGA 360 GAACTGGGAA TGGCCCCTGC CCTGCAGCCC ACCCAGGGTG CCATGCCGGC CTTCGCCTC 420 GCTTTCCAGC GCCGGGCAGG AGGGGTCCTG GTTGCTAGCC ATCTGCAGAG CTTCCTGGA 480 GTGTCGTACC GCGTTCTACG CCACCTTGCG CAGCCCGACA TGGCTACACC A 531 531 base pairs nucleic acid unknown unknown other nucleic acid /desc = ”synthetic“ 295 CTGCTCGGAC ACTCTCTGGG CATCCCCTGG GCTCCCCTGA GCTCCTGCCC CAGCCAGGCC 60 CTGCAGCTGG CAGGCTGCTT GAGCCAACTC CATAGCGGCC TTTTCCTCTA CCAGGGGCT 120 CTGCAGGCCC TGGAAGGGAT ATCCCCCGAG TTGGGTCCCA CCTTGGACAC ACTGCAGCT 180 GACGTCGCCG ACTTTGCCAC CACCATCTGG CAGCAGATGG AAGAACTGGG AATGGCCCC 240 GCCCTGCAGC CCACCCAGGG TGCCATGCCG GCCTTCGCCT CTGCTTTCCA GCGCCGGGC 300 GGAGGGGTCC TGGTTGCTAG CCATCTGCAG AGCTTCCTGG AGGTGTCGTA CCGCGTTCT 360 CGCCACCTTG CGCAGCCCGA CATGGCTACA CCATTAGGCC CTGCCAGCTC CCTGCCCCA 420 AGCTTCCTGC TCAAGTCTTT AGAGCAAGTG AGGAAGATCC AGGGCGATGG CGCAGCGCT 480 CAGGAGAAGC TGTGTGCCAC CTACAAGCTG TGCCACCCCG AGGAGCTGGT G 531 531 base pairs nucleic acid unknown unknown other nucleic acid /desc = ”synthetic“ 296 CCCCTGAGCT CCTGCCCCAG CCAGGCCCTG CAGCTGGCAG GCTGCTTGAG CCAACTCCAT 60 AGCGGCCTTT TCCTCTACCA GGGGCTCCTG CAGGCCCTGG AAGGGATATC CCCCGAGTT 120 GGTCCCACCT TGGACACACT GCAGCTGGAC GTCGCCGACT TTGCCACCAC CATCTGGCA 180 CAGATGGAAG AACTGGGAAT GGCCCCTGCC CTGCAGCCCA CCCAGGGTGC CATGCCGGC 240 TTCGCCTCTG CTTTCCAGCG CCGGGCAGGA GGGGTCCTGG TTGCTAGCCA TCTGCAGAG 300 TTCCTGGAGG TGTCGTACCG CGTTCTACGC CACCTTGCGC AGCCCGACAT GGCTACACC 360 TTAGGCCCTG CCAGCTCCCT GCCCCAGAGC TTCCTGCTCA AGTCTTTAGA GCAAGTGAG 420 AAGATCCAGG GCGATGGCGC AGCGCTCCAG GAGAAGCTGT GTGCCACCTA CAAGCTGTG 480 CACCCCGAGG AGCTGGTGCT GCTCGGACAC TCTCTGGGCA TCCCCTGGGC T 531 531 base pairs nucleic acid unknown unknown other nucleic acid /desc = ”synthetic“ 297 CAGGCCCTGC AGCTGGCAGG CTGCTTGAGC CAACTCCATA GCGGCCTTTT CCTCTACCAG 60 GGGCTCCTGC AGGCCCTGGA AGGGATATCC CCCGAGTTGG GTCCCACCTT GGACACACT 120 CAGCTGGACG TCGCCGACTT TGCCACCACC ATCTGGCAGC AGATGGAAGA ACTGGGAAT 180 GCCCCTGCCC TGCAGCCCAC CCAGGGTGCC ATGCCGGCCT TCGCCTCTGC TTTCCAGCG 240 CGGGCAGGAG GGGTCCTGGT TGCTAGCCAT CTGCAGAGCT TCCTGGAGGT GTCGTACCG 300 GTTCTACGCC ACCTTGCGCA GCCCGACATG GCTACACCAT TAGGCCCTGC CAGCTCCCT 360 CCCCAGAGCT TCCTGCTCAA GTCTTTAGAG CAAGTGAGGA AGATCCAGGG CGATGGCGC 420 GCGCTCCAGG AGAAGCTGTG TGCCACCTAC AAGCTGTGCC ACCCCGAGGA GCTGGTGCT 480 CTCGGACACT CTCTGGGCAT CCCCTGGGCT CCCCTGAGCT CCTGCCCCAG C 531 531 base pairs nucleic acid unknown unknown other nucleic acid /desc = ”synthetic“ 298 CTGCAGCTGG CAGGCTGCTT GAGCCAACTC CATAGCGGCC TTTTCCTCTA CCAGGGGCTC 60 CTGCAGGCCC TGGAAGGGAT ATCCCCCGAG TTGGGTCCCA CCTTGGACAC ACTGCAGCT 120 GACGTCGCCG ACTTTGCCAC CACCATCTGG CAGCAGATGG AAGAACTGGG AATGGCCCC 180 GCCCTGCAGC CCACCCAGGG TGCCATGCCG GCCTTCGCCT CTGCTTTCCA GCGCCGGGC 240 GGAGGGGTCC TGGTTGCTAG CCATCTGCAG AGCTTCCTGG AGGTGTCGTA CCGCGTTCT 300 CGCCACCTTG CGCAGCCCGA CATGGCTACA CCATTAGGCC CTGCCAGCTC CCTGCCCCA 360 AGCTTCCTGC TCAAGTCTTT AGAGCAAGTG AGGAAGATCC AGGGCGATGG CGCAGCGCT 420 CAGGAGAAGC TGTGTGCCAC CTACAAGCTG TGCCACCCCG AGGAGCTGGT GCTGCTCGG 480 CACTCTCTGG GCATCCCCTG GGCTCCCCTG AGCTCCTGCC CCAGCCAGGC C 531 531 base pairs nucleic acid unknown unknown other nucleic acid /desc = ”synthetic“ 299 CTGGCAGGCT GCTTGAGCCA ACTCCATAGC GGCCTTTTCC TCTACCAGGG GCTCCTGCAG 60 GCCCTGGAAG GGATATCCCC CGAGTTGGGT CCCACCTTGG ACACACTGCA GCTGGACGT 120 GCCGACTTTG CCACCACCAT CTGGCAGCAG ATGGAAGAAC TGGGAATGGC CCCTGCCCT 180 CAGCCCACCC AGGGTGCCAT GCCGGCCTTC GCCTCTGCTT TCCAGCGCCG GGCAGGAGG 240 GTCCTGGTTG CTAGCCATCT GCAGAGCTTC CTGGAGGTGT CGTACCGCGT TCTACGCCA 300 CTTGCGCAGC CCGACATGGC TACACCATTA GGCCCTGCCA GCTCCCTGCC CCAGAGCTT 360 CTGCTCAAGT CTTTAGAGCA AGTGAGGAAG ATCCAGGGCG ATGGCGCAGC GCTCCAGGA 420 AAGCTGTGTG CCACCTACAA GCTGTGCCAC CCCGAGGAGC TGGTGCTGCT CGGACACTC 480 CTGGGCATCC CCTGGGCTCC CCTGAGCTCC TGCCCCAGCC AGGCCCTGCA G 531 177 amino acids amino acid unknown unknown peptide 300 Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gl 1 5 10 15 Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cy 20 25 30 His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Tr 35 40 45 Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cy 50 55 60 Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gl 65 70 75 80 Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Le 85 90 95 Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Gl 100 105 110 Glu Leu Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pr 115 120 125 Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Al 130 135 140 Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg Hi 145 150 155 160 Leu Ala Gln Pro Asp Met Ala Thr Pro Leu Gly Pro Ala Ser Ser Le 165 170 175 Pro 177 amino acids amino acid unknown unknown peptide 301 Glu Leu Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pr 1 5 10 15 Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Al 20 25 30 Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg Hi 35 40 45 Leu Ala Gln Pro Asp Met Ala Thr Pro Leu Gly Pro Ala Ser Ser Le 50 55 60 Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gl 65 70 75 80 Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Le 85 90 95 Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pr 100 105 110 Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gl 115 120 125 Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Le 130 135 140 Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Th 145 150 155 160 Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Me 165 170 175 Glu 177 amino acids amino acid unknown unknown peptide 302 Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Ph 1 5 10 15 Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser Hi 20 25 30 Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Al 35 40 45 Gln Pro Asp Met Ala Thr Pro Leu Gly Pro Ala Ser Ser Leu Pro Gl 50 55 60 Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly As 65 70 75 80 Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys Hi 85 90 95 Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Al 100 105 110 Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Le 115 120 125 Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Al 130 135 140 Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gl 145 150 155 160 Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Gl 165 170 175 Leu 177 amino acids amino acid unknown unknown peptide 303 Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gl 1 5 10 15 Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pr 20 25 30 Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pr 35 40 45 Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Se 50 55 60 Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Le 65 70 75 80 Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Le 85 90 95 Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Le 100 105 110 Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Ph 115 120 125 Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser Hi 130 135 140 Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Al 145 150 155 160 Gln Pro Asp Met Ala Thr Pro Leu Gly Pro Ala Ser Ser Leu Pro Gl 165 170 175 Ser 177 amino acids amino acid unknown unknown peptide 304 Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pr 1 5 10 15 Asp Met Ala Thr Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Ph 20 25 30 Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Al 35 40 45 Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Gl 50 55 60 Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Le 65 70 75 80 Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gl 85 90 95 Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Gl 100 105 110 Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu As 115 120 125 Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gl 130 135 140 Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Al 145 150 155 160 Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Le 165 170 175 Gln 177 amino acids amino acid unknown unknown peptide 305 Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Ly 1 5 10 15 Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Le 20 25 30 Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Se 35 40 45 Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Le 50 55 60 Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Gl 65 70 75 80 Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Al 85 90 95 Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Le 100 105 110 Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Ar 115 120 125 Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Gl 130 135 140 Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Asp Met Ala Th 145 150 155 160 Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys Se 165 170 175 Leu 177 amino acids amino acid unknown unknown peptide 306 Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Le 1 5 10 15 Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Ly 20 25 30 Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Le 35 40 45 Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Se 50 55 60 Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Le 65 70 75 80 Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Gl 85 90 95 Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Al 100 105 110 Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Le 115 120 125 Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Ar 130 135 140 Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Gl 145 150 155 160 Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Asp Met Ala Th 165 170 175 Pro 177 amino acids amino acid unknown unknown peptide 307 Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cy 1 5 10 15 Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Se 20 25 30 Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Se 35 40 45 Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala As 50 55 60 Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pr 65 70 75 80 Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Ph 85 90 95 Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Ph 100 105 110 Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Asp Me 115 120 125 Ala Thr Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Le 130 135 140 Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Le 145 150 155 160 Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Le 165 170 175 Val 177 amino acids amino acid unknown unknown peptide 308 Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Le 1 5 10 15 Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Al 20 25 30 Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gl 35 40 45 Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Gl 50 55 60 Leu Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Al 65 70 75 80 Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Se 85 90 95 His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Le 100 105 110 Ala Gln Pro Asp Met Ala Thr Pro Leu Gly Pro Ala Ser Ser Leu Pr 115 120 125 Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gl 130 135 140 Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cy 145 150 155 160 His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Tr 165 170 175 Ala 177 amino acids amino acid unknown unknown peptide 309 Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Le 1 5 10 15 Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Gl 20 25 30 Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Al 35 40 45 Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Le 50 55 60 Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Ar 65 70 75 80 Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Gl 85 90 95 Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Asp Met Ala Th 100 105 110 Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys Se 115 120 125 Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Gl 130 135 140 Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Le 145 150 155 160 Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pr 165 170 175 Ser 177 amino acids amino acid unknown unknown peptide 310 Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Le 1 5 10 15 Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gl 20 25 30 Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Th 35 40 45 Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pr 50 55 60 Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Al 65 70 75 80 Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Se 85 90 95 Tyr Arg Val Leu Arg His Leu Ala Gln Pro Asp Met Ala Thr Pro Le 100 105 110 Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu Gl 115 120 125 Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Le 130 135 140 Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gl 145 150 155 160 His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gl 165 170 175 Ala 177 amino acids amino acid unknown unknown peptide 311 Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gl 1 5 10 15 Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Th 20 25 30 Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Tr 35 40 45 Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro Thr Gl 50 55 60 Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gl 65 70 75 80 Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Ar 85 90 95 Val Leu Arg His Leu Ala Gln Pro Asp Met Ala Thr Pro Leu Gly Pr 100 105 110 Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Va 115 120 125 Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Al 130 135 140 Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Se 145 150 155 160 Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Le 165 170 175 Gln 177 amino acids amino acid unknown unknown peptide 312 His Leu Ala Gln Pro Asp Met Ala Thr Pro Leu Gly Pro Ala Ser Se 1 5 10 15 Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Il 20 25 30 Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Ly 35 40 45 Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Il 50 55 60 Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Al 65 70 75 80 Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Le 85 90 95 Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu As 100 105 110 Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gl 115 120 125 Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Al 130 135 140 Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Le 145 150 155 160 Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Le 165 170 175 Arg 531 base pairs nucleic acid unknown unknown other nucleic acid /desc = ”synthetic“ 313 CACCTTGCGC AGCCCGACAT GGCTACACCA TTAGGCCCTG CCAGCTCCCT GCCCCAGAGC 60 TTCCTGCTCA AGTCTTTAGA GCAAGTGAGG AAGATCCAGG GCGATGGCGC AGCGCTCCA 120 GAGAAGCTGT GTGCCACCTA CAAGCTGTGC CACCCCGAGG AGCTGGTGCT GCTCGGACA 180 TCTCTGGGCA TCCCCTGGGC TCCCCTGAGC TCCTGCCCCA GCCAGGCCCT GCAGCTGGC 240 GGCTGCTTGA GCCAACTCCA TAGCGGCCTT TTCCTCTACC AGGGGCTCCT GCAGGCCCT 300 GAAGGGATAT CCCCCGAGTT GGGTCCCACC TTGGACACAC TGCAGCTGGA CGTCGCCGA 360 TTTGCCACCA CCATCTGGCA GCAGATGGAA GAACTGGGAA TGGCCCCTGC CCTGCAGCC 420 ACCCAGGGTG CCATGCCGGC CTTCGCCTCT GCTTTCCAGC GCCGGGCAGG AGGGGTCCT 480 GTTGCTAGCC ATCTGCAGAG CTTCCTGGAG GTGTCGTACC GCGTTCTACG C 531

Claims (47)

We claim the following:
1. A hematopoietic protein comprising; an amino acid sequence of the formula:
R1-L1-R2, R2-L1-R1, R1-R2, or R2-R1
wherein R1 and R2 are independently selected from the group consisting of:
(I) A polypeptide comprising a modified human G-CSF amino acid sequence selected from the group consisting of:
(a) an amino acid sequence of the formula:
1                                   10 (SEQ ID NO: 1) Xaa Xaa Xaa Gly Pro Ala Ser Ser Leu Pro Gln Ser Xaa                         20 Leu Leu Xaa Xaa Xaa Glu Gln Val Xaa Lys Xaa Gln Gly Xaa Gly     30                                      40 Ala Xaa Leu Gln Glu Xaa Leu Xaa Ala Thr Tyr Lys Leu Xaa Xaa                         50 Xaa Glu Xaa Xaa Val Xaa Xaa Gly His Ser Xaa Gly Ile Pro Trp     60                                      70 Ala Pro Leu Ser Ser Xaa Pro Ser Xaa Ala Leu Xaa Leu Ala Gly                         80 Xaa Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu     90                                      100 Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu                         110 Xaa Thr Leu Gln Xaa Asp Val Ala Asp Phe Ala Xaa Thr Ile Trp     120                                     130 Gln Gln Met Glu Xaa Xaa Gly Met Ala Pro Ala Leu Gln Pro Thr                         140 Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Xaa Gln Xaa Xaa Ala     150                                     160 Gly Gly Val Leu Val Ala Ser Xaa Leu Gln Xaa Phe Leu Xaa Xaa                         170 Ser Tyr Arg Val Leu Xaa Xaa Leu Ala Gln Pro
wherein
Xaa at position 1 is Thr, Ser, Arg, Tyr or Gly;
Xaa at position 2 is Pro or Leu;
Xaa at position 3 is Leu, Arg, Tyr or Ser;
Xaa at position 13 is Phe, Ser, His, Thr or Pro;
Xaa at position 16 is Lys, Pro, Ser, Thr or His;
Xaa at position 17 is Cys, Ser, Gly, Ala, Ile, Tyr or Arg;
Xaa at position 18 is Leu, Thr, Pro, His, Ile or Cys;
Xaa at position 22 is Arg, Tyr, Ser, Thr or Ala;
Xaa at position 24 is Ile, Pro, Tyr or Leu;
Xaa at position 27 is Asp, or Gly;
Xaa at position 30 is Ala, Ile, Leu or Gly;
Xaa at position 34 is Lys or Ser;
Xaa at position 36 is Cys or Ser;
Xaa at position 42 is Cys or Ser;
Xaa at position 43 is His, Thr, Gly, Val, Lys, Trp, Ala, Arg, Cys, or Leu;
Xaa at position 44 is Pro, Gly, Arg, Asp, Val, Ala, His, Trp, Gln, or Thr;
Xaa at position 46 is Glu, Arg, Phe, Arg, Ile or Ala;
Xaa at position 47 is Leu or Thr;
Xaa at position 49 is Leu, Phe, Arg or Ser;
Xaa at position 50 is Leu, Ile, His, Pro or Tyr;
Xaa at position 54 is Leu or His;
Xaa at position 64 is Cys or Ser;
Xaa at position 67 is Gln, Lys, Leu or Cys;
Xaa at position 70 is Gln, Pro, Leu, Arg or Ser;
Xaa at position 74 is Cys or Ser;
Xaa at position 104 is Asp, Gly or Val;
Xaa at position 108 is Leu, Ala, Val, Arg, Trp, Gln or Gly;
Xaa at position 115 is Thr, His, Leu or Ala;
Xaa at position 120 is Gln, Gly, Arg, Lys or His
Xaa at position 123 is Glu, Arg, Phe or Thr
Xaa at position 144 is Phe, His, Arg, Pro, Leu, Gln or Glu;
Xaa at position 146 is Arg or Gln;
Xaa at position 147 is Arg or Gln;
Xaa at position 156 is His, Gly or Ser;
Xaa at position 159 is Ser, Arg, Thr, Tyr, Val or Gly;
Xaa at position 162 is Glu, Leu, Gly or Trp;
Xaa at position 163 is Val, Gly, Arg or Ala;
Xaa at position 169 is Arg, Ser, Leu, Arg or Cys;
Xaa at position 170 is His, Arg or Ser;
wherein optionally 1-11 amino acids from the N-terminus and 1-5 from the C-terminus can optionally be deleted from said modified human G-CSF amino acid sequence; and
wherein the N-terminus is joined to the C-terminus directly or through a linker capable of joining the N-terminus to the C-terminus and having new C- and N-termini at amino acids:
38-39 39-40 40-41 41-42 42-43 43-44 45-46 48-49 49-50 52-53 53-54 54-55 55-56 56-57 57-58 58-59 59-60 60-61 61-62 62-63 63-64 64-65 65-66 66-67 67-68 68-69 69-70 70-71 71-72 91-92 92-93 93-94 94-95 95-96 96-97 97-98 98-99  99-100 123-124 124-125 125-126 126-127 128-129 128-129 129-130 130-131 131-132 132-133 133-134 134-135 135-136 136-137 137-138 138-139 139-140 140-141 141-142 or 142-143 respectively; and
(b) an amino acid sequence of the formula:
1                                   10 (SEQ ID NO: 1) Xaa Xaa Xaa Gly Pro Ala Ser Ser Leu Pro Gln Ser Xaa                         20 Leu Leu Xaa Xaa Xaa Glu Gln Val Xaa Lys Xaa Gln Gly Xaa Gly     30                                      40 Ala Xaa Leu Gln Glu Xaa Leu Xaa Ala Thr Tyr Lys Leu Xaa Xaa                         50 Xaa Glu Xaa Xaa Val Xaa Xaa Gly His Ser Xaa Gly Ile Pro Trp     60                                      70 Ala Pro Leu Ser Ser Xaa Pro Ser Xaa Ala Leu Xaa Leu Ala Gly                         80 Xaa Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu     90                                      100 Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu                         110 Xaa Thr Leu Gln Xaa Asp Val Ala Asp Phe Ala Xaa Thr Ile Trp     120                                     130 Gln Gln Met Glu Xaa Xaa Gly Met Ala Pro Ala Leu Gln Pro Thr                         140 Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Xaa Gln Xaa Xaa Ala     150                                     160 Gly Gly Val Leu Val Ala Ser Xaa Leu Gln Xaa Phe Leu Xaa Xaa                         170 Ser Tyr Arg Val Leu Xaa Xaa Leu Ala Gln Pro
wherein
Xaa at position 1 is Thr, Ser, Arg, Tyr or Gly;
Xaa at position 2 is Pro or Leu;
Xaa at position 3 is Leu, Arg, Tyr or Ser;
Xaa at position 13 is Phe, Ser, His, Thr or Pro;
Xaa at position 16 is Lys, Pro, Ser, Thr or His;
Xaa at position 17 is Cys, Ser, Gly, Ala, Ile, Tyr or Arg;
Xaa at position 18 is Leu, Thr, Pro, His, Ile or Cys;
Xaa at position 22 is Arg, Tyr, Ser, Thr or Ala;
Xaa at position 24 is Ile, Pro, Tyr or Leu;
Xaa at position 27 is Asp, or Gly;
Xaa at position 30 is Ala, Ile, Leu or Gly;
Xaa at position 34 is Lys or Ser;
Xaa at position 36 is Cys or Ser;
Xaa at position 42 is Cys or Ser;
Xaa at position 43 is His, Thr, Gly, Val, Lys, Trp, Ala, Arg, Cys, or Leu;
Xaa at position 44 is Pro, Gly, Arg, Asp, Val, Ala, His, Trp, Gln, or Thr;
Xaa at position 46 is Glu, Arg, Phe, Arg, Ile or Ala;
Xaa at position 47 is Leu or Thr;
Xaa at position 49 is Leu, Phe, Arg or Ser;
Xaa at position 50 is Leu, Ile, His, Pro or Tyr;
Xaa at position 54 is Leu or His;
Xaa at position 64 is Cys or Ser;
Xaa at position 67 is Gln, Lys, Leu or Cys;
Xaa at position 70 is Gln, Pro, Leu, Arg or Ser;
Xaa at position 74 is Cys or Ser;
Xaa at position 104 is Asp, Gly or Val;
Xaa at position 108 is Leu, Ala, Val, Arg, Trp, Gln or Gly;
Xaa at position 115 is Thr, His, Leu or Ala;
Xaa at position 120 is Gln, Gly, Arg, Lys or His
Xaa at position 123 is Glu, Arg, Phe or Thr
Xaa at position 144 is Phe, His, Arg, Pro, Leu, Gln or Glu;
Xaa at position 146 is Arg or Gln;
Xaa at position 147 is Arg or Gln;
Xaa at position 156 is His, Gly or Ser;
Xaa at position 159 is Ser, Arg, Thr, Tyr, Val or Gly;
Xaa at position 162 is Glu, Leu, Gly or Trp;
Xaa at position 163 is Val, Gly, Arg or Ala;
Xaa at position 169 is Arg, Ser, Leu, Arg or Cys;
Xaa at position 170 is His, Arg or Ser,
wherein optionally 1-11 amino acids from the N-terminus and 1-5 from the C-terminus can be deleted;
wherein the N-terminus is joined to the C-terminus directly or through a linker capable of joining the N-terminus to the C-terminus and having new C- and N-terminus at amino acids:
2-3
10-11
12-13
18-19
122-123
158-159
169-170;
(II) A polypeptide comprising; a modified human IL-3 amino acid sequence of the formula: Ala Pro Met Thr Gln Thr Thr Ser Leu Lys Thr Ser Trp Val Asn (SEQ ID NO: 2) 1               5                   10                  15 Cys Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 20                  25                  30 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Asn Xaa Xaa Xaa Xaa Xaa Xaa                 35                  40                  45 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 50                  55                  60 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 65                  70                  75 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 80                  85                  90 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 95                  100                 105 Xaa Phe Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 110                 115                 120 Xaa Xaa Xaa Gln Gln Thr Thr Leu Ser Leu Ala Ile Phe                 125                 130
wherein Xaa at position 17 is Ser, Lys, Gly, Asp, Met, Gln, or Arg;
Xaa at position 18 is Asn, His, Leu, Ile, Phe, Arg, or Gln;
Xaa at position 19 is Met, Phe, Ile, Arg, Gly, Ala, or Cys;
Xaa at position 20 is Ile, Cys, Gln, Glu, Arg, Pro, or Ala;
Xaa at position 21 is Asp, Phe, Lys, Arg, Ala, Gly, Glu, Gln, Asn, Thr, Ser or Val;
Xaa at position 22 is Glu, Trp, Pro, Ser, Ala, His, Asp, Asn, Gln, Leu, Val or Gly;
Xaa at position 23 is Ile, Val, Ala, Gly, Trp, Lys, Phe, Leu, Ser, or Arg;
Xaa at position 24 is Ile, Gly, Val, Arg, Ser, Phe, or Leu;
Xaa at position 25 is Thr, His, Gly, Gln, Arg, Pro, or Ala;
Xaa at position 26 is His, Thr, Phe, Gly, Arg, Ala, or Trp;
Xaa at position 27 is Leu, Gly, Arg, Thr, Ser, or Ala;
Xaa at position 28 is Lys, Arg, Leu, Gln, Gly, Pro, Val or Trp;
Xaa at position 29 is Gln, Asn, Leu, Pro, Arg, or Val;
Xaa at position 30 is Pro, His, Thr, Gly, Asp, Gln, Ser, Leu, or Lys;
Xaa at position 31 is Pro, Asp, Gly, Ala, Arg, Leu, or Gln;
Xaa at position 32 is Leu, Val, Arg, Gln, Asn, Gly, Ala, or Glu;
Xaa at position 33 is Pro, Leu, Gln, Ala, Thr, or Glu;
Xaa at position 34 is Leu, Val, Gly, Ser, Lys, Glu, Gln, Thr, Arg, Ala, Phe, Ile or Met;
Xaa at position 35 is Leu, Ala, Gly, Asn, Pro, Gln, or Val;
Xaa at position 36 is Asp, Leu, or Val;
Xaa at position 37 is Phe, Ser, Pro, Trp, or Ile;
Xaa at position 38 is Asn, or Ala;
Xaa at position 40 is Leu, Trp, or Arg;
Xaa at position 41 is Asn, Cys, Arg, Leu, His, Met, or Pro;
Xaa at position 42 is Gly, Asp, Ser, Cys, Asn, Lys, Thr, Leu, Val, Glu, Phe, Tyr, Ile, Met or Ala;
Xaa at position 43 is Glu, Asn, Tyr, Leu, Phe, Asp, Ala, Cys, Gln, Arg, Thr, Gly or Ser;
Xaa at position 44 is Asp, Ser, Leu, Arg, Lys, Thr, Met, Trp, Glu, Asn, Gln, Ala or Pro;
Xaa at position 45 is Gln, Pro, Phe, Val, Met, Leu, Thr, Lys, Trp, Asp, Asn, Arg, Ser, Ala, Ile, Glu or His;
Xaa at position 46 is Asp, Phe, Ser, Thr, Cys, Glu, Asn, Gln, Lys, His, Ala, Tyr, Ile, Val or Gly;
Xaa at position 47 is Ile, Gly, Val, Ser, Arg, Pro, or His;
Xaa at position 48 is Leu, Ser, Cys, Arg, Ile, His, Phe, Glu, Lys, Thr, Ala, Met, Val or Asn;
Xaa at position 49 is Met, Arg, Ala, Gly, Pro, Asn, His, or Asp;
Xaa at position 50 is Glu, Leu, Thr, Asp, Tyr, Lys, Asn, Ser, Ala, Ile, Val, His, Phe, Met or Gln;
Xaa at position 51 is Asn, Arg, Met, Pro, Ser, Thr, or His;
Xaa at position 52 is Asn, His, Arg, Leu, Gly, Ser, or Thr;
Xaa at position 53 is Leu, Thr, Ala, Gly, Glu, Pro, Lys, Ser, or Met;
Xaa at position 54 is Arg, Asp, Ile, Ser, Val, Thr, Gln, Asn, Lys, His, Ala or Leu;
Xaa at position 55 is Arg, Thr, Val, Ser, Leu, or Gly;
Xaa at position 56 is Pro, Gly, Cys, Ser, Gln, Glu, Arg, His, Thr, Ala, Tyr, Phe, Leu, Val or Lys;
Xaa at position 57 is Asn or Gly;
Xaa at position 58 is Leu, Ser, Asp, Arg, Gln, Val, or Cys;
Xaa at position 59 is Glu Tyr, His, Leu, Pro, or Arg;
Xaa at position 60 is Ala, Ser, Pro, Tyr, Asn, or Thr;
Xaa at position 61 is Phe, Asn, Glu, Pro, Lys, Arg, or Ser;
Xaa at position 62 is Asn, His, Val, Arg, Pro, Thr, Asp, or Ile;
Xaa at position 63 is Arg, Tyr, Trp, Lys, Ser, His, Pro, or Val;
Xaa at position 64 is Ala, Asn, Pro, Ser, or Lys;
Xaa at position 65 is Val, Thr, Pro, His, Leu, Phe, or Ser;
Xaa at position 66 is Lys, Ile, Arg, Val, Asn, Glu, or Ser;
Xaa at position 67 is Ser, Ala, Phe, Val, Gly, Asn, Ile, Pro, or His;
Xaa at position 68 is Leu, Val, Trp, Ser, Ile, Phe, Thr, or His;
Xaa at position 69 is Gln, Ala, Pro, Thr, Glu, Arg, Trp, Gly, or Leu;
Xaa at position 70 is Asn, Leu, Val, Trp, Pro, or Ala;
Xaa at position 71 is Ala, Met, Leu, Pro, Arg, Glu, Thr, Gln, Trp, or Asn;
Xaa at position 72 is Ser, Glu, Met, Ala, His, Asn, Arg, or Asp;
Xaa at position 73 is Ala, Glu, Asp, Leu, Ser, Gly, Thr, or Arg;
Xaa at position 74 is Ile, Met, Thr, Pro, Arg, Gly, Ala;
Xaa at position 75 is Glu, Lys, Gly, Asp, Pro, Trp, Arg, Ser, Gln, or Leu;
Xaa at position 76 is Ser, Val, Ala, Asn, Trp, Glu, Pro, Gly, or Asp;
Xaa at position 77 is Ile, Ser, Arg, Thr, or Leu;
Xaa at position 78 is Leu, Ala, Ser, Glu, Phe, Gly, or Arg;
Xaa at position 79 is Lys, Thr, Asn, Met, Arg, Ile, Gly, or Asp;
Xaa at position 80 is Asn, Trp, Val, Gly, Thr, Leu, Glu, or Arg;
Xaa at position 81 is Leu, Gln, Gly, Ala, Trp, Arg, Val, or Lys;
Xaa at position 82 is Leu, Gln, Lys, Trp, Arg, Asp, Glu, Asn, His, Thr, Ser, Ala, Tyr, Phe, Ile, Met or Val;
Xaa at position 83 is Pro, Ala, Thr, Trp, Arg, or Met;
Xaa at position 84 is Cys, Glu, Gly, Arg, Met, or Val;
Xaa at position 85 is Leu, Asn, Val, or Gln;
Xaa at position 86 is Pro, Cys, Arg, Ala, or Lys;
Xaa at position 87 is Leu, Ser, Trp, or Gly;
Xaa at position 88 is Ala, Lys, Arg, Val, or Trp;
Xaa at position 89 is Thr, Asp, Cys, Leu, Val, Glu, His, Asn, or Ser;
Xaa at position 90 is Ala, Pro, Ser, Thr, Gly, Asp, Ile, or Met;
Xaa at position 91 is Ala, Pro, Ser, Thr, Phe, Leu, Asp, or His;
Xaa at position 92 is Pro, Phe, Arg, Ser, Lys, His, Ala, Gly, Ile or Leu;
Xaa at position 93 is Thr, Asp, Ser, Asn, Pro, Ala, Leu, or Arg;
Xaa at position 94 is Arg, Ile, Ser, Glu, Leu, Val, Gln, Lys, His, Ala, or Pro;
Xaa at position 95 is His, Gln, Pro, Arg, Val, Leu, Gly, Thr, Asn, Lys, Ser, Ala, Trp, Phe, Ile, or Tyr;
Xaa at position 96 is Pro, Lys, Tyr, Gly, Ile, or Thr;
Xaa at position 97 is Ile, Val, Lys, Ala, or Asn;
Xaa at position 98 is His, Ile, Asn, Leu, Asp, Ala, Thr, Glu, Gln, Ser, Phe, Met, Val, Lys, Arg, Tyr or Pro;
Xaa at position 99 is Ile, Leu, Arg, Asp, Val, Pro, Gln, Gly, Ser, Phe, or His;
Xaa at position 100 is Lys, Tyr, Leu, His, Arg, Ile, Ser, Gln, or Pro;
Xaa at position 101 is Asp, Pro, Met, Lys, His, Thr, Val, Tyr, Glu, Asn, Ser, Ala, Gly, Ile, Leu, or Gln;
Xaa at position 102 is Gly, Leu, Glu, Lys, Ser, Tyr, or Pro;
Xaa at position 103 is Asp, or Ser;
Xaa at position 104 is Trp, Val, Cys, Tyr, Thr, Met, Pro, Leu, Gln, Lys, Ala, Phe, or Gly;
Xaa at position 105 is Asn, Pro, Ala, Phe, Ser, Trp, Gln, Tyr, Leu, Lys, Ile, Asp, or His;
Xaa at position 106 is Glu, Ser, Ala, Lys, Thr, Ile, Gly, or Pro;
Xaa at position 108 is Arg, Lys, Asp, Leu, Thr, Ile, Gln, His, Ser, Ala or Pro;
Xaa at position 109 is Arg, Thr, Pro, Glu, Tyr, Leu, Ser, or Gly;
Xaa at position 110 is Lys, Ala, Asn, Thr, Leu, Arg, Gln, His, Glu, Ser, or Trp;
Xaa at position 111 is Leu, Ile, Arg, Asp, or Met;
Xaa at position 112 is Thr, Val, Gln, Tyr, Glu, His, Ser, or Phe;
Xaa at position 113 is Phe, Ser, Cys, His, Gly, Trp, Tyr, Asp, Lys, Leu, Ile, Val or Asn;
Xaa at position 114 is Tyr, Cys, His, Ser, Trp, Arg, or Leu;
Xaa at position 115 is Leu, Asn, Val, Pro, Arg, Ala, His, Thr, Trp, or Met;
Xaa at position 116 is Lys, Leu, Pro, Thr, Met, Asp, Val, Glu, Arg, Trp, Ser, Asn, His, Ala, Tyr, Phe, Gln, or Ile;
Xaa at position 117 is Thr, Ser, Asn, Ile, Trp, Lys, or Pro;
Xaa at position 118 is Leu, Ser, Pro, Ala, Glu, Cys, Asp, or Tyr;
Xaa at position 119 is Glu, Ser, Lys, Pro, Leu, Thr, Tyr, or Arg;
Xaa at position 120 is Asn, Ala, Pro, Leu, His, Val, or Gln;
Xaa at position 121 is Ala, Ser, Ile, Asn, Pro, Lys, Asp, or Gly;
Xaa at position 122 is Gln, Ser, Met, Trp, Arg, Phe, Pro, His, Ile, Tyr, or Cys;
Xaa at position 123 is Ala, Met, Glu, His, Ser, Pro, Tyr, or Leu;
wherein from 1 to 14 amino acids can optionally be deleted from the N-terminus and/or from 1 to 15 amino acids can optionally be deleted from the C-terminus of said modified human IL-3 amino acid sequence; wherein from 0 to 44 of the amino acids designated by Xaa are different from the corresponding amino acids of native (1-133) human interleukin-3; and
wherein the N-terminus is joined to the C-terminus directly or through a linker (L2), capable of joining the N-terminus to the C-terminus and having new C- and N-termini at amino acids:
26-27 27-28 28-29 29-30 30-31 31-32 32-33 33-34 34-35 35-36 36-37 37-38 38-39 39-40 40-41 41-42 49-50 50-51 51-52 52-53 53-54 54-55 64-65 65-66 66-67 67-68 68-69 69-70 70-71 71-72 72-73 82-83 83-84 84-85 85-86 86-87 87-88 88-89 89-90 90-91 91-92 92-93 97-98 98-99  99-100 100-101 101-102 102-103 or 103-104 respectively;
(III) A polypeptide comprising; a modified human c-mpl ligand amino acid sequence selected from the group consisiting of:
(a) an amino acid sequence of the formula: SerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeuArgAspSer (SEQ ID NO: 256) 1           5              10             15 HisValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuProThrPro 20             25             30             35 ValLeuLeuProAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGluGlu    40             45             50             55 ThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAla       60             65             70             75 AlaArgGlyGlnLeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGly          80             85             90             95 GlnValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnXaaXaaXaa             100            105            110 XaaGlyArgThrThrAlaHisLysAspProAsnAlaIlepheLeuSerPheGlnHis 115            120            125            130 LeuLeuArgGlyLysValArgPheLeuMetLeuValGlyGlySerThrLeuCysVal    135            140            145            150 Arg 153
wherein
Xaa at position 112 is deleted or Leu, Ala, Val, Ile, Pro, Phe, Trp, or Met;
Xaa at position 113 is deleted or Pro, Phe, Ala, Val, Leu, Ile, Trp, or Met;
Xaa at position 114 is deleted or Pro, Phe, Ala, Val, Leu, Ile, Trp, or Met;
Xaa at position 115 is deleted or Gln, Gly, Ser, Thr, Tyr, or Asn; and
wherein the N-terminus is joined to the C-terminus directly or through a linker (L2) capable of joining the N-terminus to the C-terminus and having new C- and N-termini at amino acids:
26-27 27-28 28-29 29-30 30-31 32-33 33-34 34-35 36-37 37-38 38-39 40-41 41-42 42-43 43-44 44-45 46-47 47-48 48-49 50-51 51-52 52-53 53-54 54-55 55-56 56-57 57-58 58-59 59-60 78-79 79-80 80-81 81-82 82-83 83-84 84-85 85-86 86-87 87-88 88-89 108-109 109-110 110-111 111-112 112-113 113-114 114-115 115-116 116-117 117-118 118-119 119-120 120-121 121-122 122-123 123-124 124-125 125-126 126-127 or 127-128 respectively; and
(b) an amino acid sequence of the formula:
SerProAlaProProAlaXaaAspLeuArgValLeuSerLysLeuLeuArgAspSer (SEQ ID NO: 283) 1           5              10             15 HisValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuProThrPro 20             25             30             35 ValLeuLeuProAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGluGlu    40             45             50             55 ThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAla       60             65             70             75 AlaArgGlyGlnLeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGly          80             85             90             95 GlnValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnXaaXaaXaa             100            105            110 XaaGlyArgThrThrAlaHisLysAspProAsnAlaIlePheLeuSerPheGlnHis 115            120            125            130 LeuLeuArgGlyLysValArgPheLeuMetLeuValGlyGlySerThrLeuXaaVal    135            140            145            150 Arg 153
wherein
Xaa at position 7 is Ser or Ala;
Xaa at position 112 is deleted or Leu, Ala, Val, Ile, Pro, Phe, Trp, or Met;
Xaa at position 113 is deleted or Pro, Phe, Ala, Val, Leu, Ile, Trp, or Met;
Xaa at position 114 is deleted or Pro, Phe, Ala, Val, Leu, Ile, Trp, or Met;
Xaa at position 115 is deleted or Gln, Gly, Ser, Thr, Tyr, or Asn;
Xaa at position 151 is Ser or Ala,
wherein the N-terminus is joined to the C-terminus directly or through a linker capable of joining the N-terminus to the C-terminus and having new C- and N-termini at amino acids:
26-27 27-28 28-29 29-30 30-31 32-33 33-34 34-35 36-37 37-38 38-39 40-41 41-42 42-43 43-44 44-45 46-47 47-48 48-49 50-51 51-52 52-53 53-54 54-55 55-56 56-57 57-58 58-59 59-60 78-79 79-80 80-81 81-82 82-83 83-84 84-85 85-86 86-87 87-88 88-89 108-109 109-110 110-111 111-112 112-113 113-114 114-115 115-116 116-117 117-118 118-119 119-120 120-121 121-122 122-123 123-124 124-125 125-126 126-127 or 127-128;
(IV) A polypeptide comprising; a modified human IL-3 amino acid sequence of the formula:
Ala Pro Met Thr Gln Thr Thr Ser Leu Lys Thr Ser Trp Val Asn (SEQ ID NO: 2) 1               5                   10                  15 Cys Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 20                  25                  30 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Asn Xaa Xaa Xaa Xaa Xaa Xaa                 35                  40                  45 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 50                  55                  60 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 65                  70                  75 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 80                  85                  90 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 95                  100                 105 Xaa Phe Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 110                 115                 120 Xaa Xaa Xaa Gln Gln Thr Thr Leu Ser Leu Ala Ile Phe                 125                 130
wherein Xaa at position 17 is Ser, Lys, Gly, Asp, Met, Gln, or Arg;
Xaa at position 18 is Asn, His, Leu, Ile, Phe, Arg, or Gln;
Xaa at position 19 is Met, Phe, Ile, Arg, Gly, Ala, or Cys;
Xaa at position 20 is Ile, Cys, Gln, Glu, Arg, Pro, or Ala;
Xaa at position 21 is Asp, Phe, Lys, Arg, Ala, Gly, Glu, Gln, Asn, Thr, Ser or Val;
Xaa at position 22 is Glu, Trp, Pro, Ser, Ala, His, Asp, Asn, Gln, Leu, Val or Gly;
Xaa at position 23 is Ile, Val, Ala, Gly, Trp, Lys, Phe, Leu, Ser, or Arg;
Xaa at position 24 is Ile, Gly, Val, Arg, Ser, Phe, or Leu;
Xaa at position 25 is Thr, His, Gly, Gln, Arg, Pro, or Ala;
Xaa at position 26 is His, Thr, Phe, Gly, Arg, Ala, or Trp;
Xaa at position 27 is Leu, Gly, Arg, Thr, Ser, or Ala;
Xaa at position 28 is Lys, Arg, Leu, Gln, Gly, Pro, Val or Trp;
Xaa at position 29 is Gln, Asn, Leu, Pro, Arg, or Val;
Xaa at position 30 is Pro, His, Thr, Gly, Asp, Gln, Ser, Leu, or Lys;
Xaa at position 31 is Pro, Asp, Gly, Ala, Arg, Leu, or Gln;
Xaa at position 32 is Leu, Val, Arg, Gln, Asn, Gly, Ala, or Glu;
Xaa at position 33 is Pro, Leu, Gln, Ala, Thr, or Glu;
Xaa at position 34 is Leu, Val, Gly, Ser, Lys, Glu, Gln, Thr, Arg, Ala, Phe, Ile or Met;
Xaa at position 35 is Leu, Ala, Gly, Asn, Pro, Gln, or Val;
Xaa at position 36 is Asp, Leu, or Val;
Xaa at position 37 is Phe, Ser, Pro, Trp, or Ile;
Xaa at position 38 is Asn, or Ala;
Xaa at position 40 is Leu, Trp, or Arg;
Xaa at position 41 is Asn, Cys, Arg, Leu, His, Met, or Pro;
Xaa at position 42 is Gly, Asp, Ser, Cys, Asn, Lys, Thr, Leu, Val, Glu, Phe, Tyr, Ile, Met or Ala;
Xaa at position 43 is Glu, Asn, Tyr, Leu, Phe, Asp, Ala, Cys, Gln, Arg, Thr, Gly or Ser;
Xaa at position 44 is Asp, Ser, Leu, Arg, Lys, Thr, Met, Trp, Glu, Asn, Gln, Ala or Pro;
Xaa at position 45 is Gln, Pro, Phe, Val, Met, Leu, Thr, Lys, Trp, Asp, Asn, Arg, Ser, Ala, Ile, Glu or His;
Xaa at position 46 is Asp, Phe, Ser, Thr, Cys, Glu, Asn, Gln, Lys, His, Ala, Tyr, Ile, Val or Gly;
Xaa at position 47 is Ile, Gly, Val, Ser, Arg, Pro, or His;
Xaa at position 48 is Leu, Ser, Cys, Arg, Ile, His, Phe, Glu, Lys, Thr, Ala, Met, Val or Asn;
Xaa at position 49 is Met, Arg, Ala, Gly, Pro, Asn, His, or Asp;
Xaa at position 50 is Glu, Leu, Thr, Asp, Tyr, Lys, Asn, Ser, Ala, Ile, Val, His, Phe, Met or Gln;
Xaa at position 51 is Asn, Arg, Met, Pro, Ser, Thr, or His;
Xaa at position 52 is Asn, His, Arg, Leu, Gly, Ser, or Thr;
Xaa at position 53 is Leu, Thr, Ala, Gly, Glu, Pro, Lys, Ser, or Met;
Xaa at position 54 is Arg, Asp, Ile, Ser, Val, Thr, Gln, Asn, Lys, His, Ala or Leu;
Xaa at position 55 is Arg, Thr, Val, Ser, Leu, or Gly;
Xaa at position 56 is Pro, Gly, Cys, Ser, Gln, Glu, Arg, His, Thr, Ala, Tyr, Phe, Leu, Val or Lys;
Xaa at position 57 is Asn or Gly;
Xaa at position 58 is Leu, Ser, Asp, Arg, Gln, Val, or Cys;
Xaa at position 59 is Glu Tyr, His, Leu, Pro, or Arg;
Xaa at position 60 is Ala, Ser, Pro, Tyr, Asn, or Thr;
Xaa at position 61 is Phe, Asn, Glu, Pro, Lys, Arg, or Ser;
Xaa at position 62 is Asn, His, Val, Arg, Pro, Thr, Asp, or Ile;
Xaa at position 63 is Arg, Tyr, Trp, Lys, Ser, His, Pro, or Val;
Xaa at position 64 is Ala, Asn, Pro, Ser, or Lys;
Xaa at position 65 is Val, Thr, Pro, His, Leu, Phe, or Ser;
Xaa at position 66 is Lys, Ile, Arg, Val, Asn, Glu, or Ser;
Xaa at position 67 is Ser, Ala, Phe, Val, Gly, Asn, Ile, Pro, or His;
Xaa at position 68 is Leu, Val, Trp, Ser, Ile, Phe, Thr, or His;
Xaa at position 69 is Gln, Ala, Pro, Thr, Glu, Arg, Trp, Gly, or Leu;
Xaa at position 70 is Asn, Leu, Val, Trp, Pro, or Ala;
Xaa at position 71 is Ala, Met, Leu, Pro, Arg, Glu, Thr, Gln, Trp, or Asn;
Xaa at position 72 is Ser, Glu, Met, Ala, His, Asn, Arg, or Asp;
Xaa at position 73 is Ala, Glu, Asp, Leu, Ser, Gly, Thr, or Arg;
Xaa at position 74 is Ile, Met, Thr, Pro, Arg, Gly, Ala;
Xaa at position 75 is Glu, Lys, Gly, Asp, Pro, Trp, Arg, Ser, Gln, or Leu;
Xaa at position 76 is Ser, Val, Ala, Asn, Trp, Glu, Pro, Gly, or Asp;
Xaa at position 77 is Ile, Ser, Arg, Thr, or Leu;
Xaa at position 78 is Leu, Ala, Ser, Glu, Phe, Gly, or Arg;
Xaa at position 79 is Lys, Thr, Asn, Met, Arg, Ile, Gly, or Asp;
Xaa at position 80 is Asn, Trp, Val, Gly, Thr, Leu, Glu, or Arg;
Xaa at position 81 is Leu, Gln, Gly, Ala, Trp, Arg, Val, or Lys;
Xaa at position 82 is Leu, Gln, Lys, Trp, Arg, Asp, Glu, Asn, His, Thr, Ser, Ala, Tyr, Phe, Ile, Met or Val;
Xaa at position 83 is Pro, Ala, Thr, Trp, Arg, or Met;
Xaa at position 84 is Cys, Glu, Gly, Arg, Met, or Val;
Xaa at position 85 is Leu, Asn, Val, or Gln;
Xaa at position 86 is Pro, Cys, Arg, Ala, or Lys;
Xaa at position 87 is Leu, Ser, Trp, or Gly;
Xaa at position 88 is Ala, Lys, Arg, Val, or Trp;
Xaa at position 89 is Thr, Asp, Cys, Leu, Val, Glu, His, Asn, or Ser;
Xaa at position 90 is Ala, Pro, Ser, Thr, Gly, Asp, Ile, or Met;
Xaa at position 91 is Ala, Pro, Ser, Thr, Phe, Leu, Asp, or His;
Xaa at position 92 is Pro, Phe, Arg, Ser, Lys, His, Ala, Gly, Ile or Leu;
Xaa at position 93 is Thr, Asp, Ser, Asn, Pro, Ala, Leu, or Arg;
Xaa at position 94 is Arg, Ile, Ser, Glu, Leu, Val, Gln, Lys, His, Ala, or Pro;
Xaa at position 95 is His, Gln, Pro, Arg, Val, Leu, Gly, Thr, Asn, Lys, Ser, Ala, Trp, Phe, Ile, or Tyr;
Xaa at position 96 is Pro, Lys, Tyr, Gly, Ile, or Thr;
Xaa at position 97 is Ile, Val, Lys, Ala, or Asn;
Xaa at position 98 is His, Ile, Asn, Leu, Asp, Ala, Thr, Glu, Gln, Ser, Phe, Met, Val, Lys, Arg, Tyr or Pro;
Xaa at position 99 is Ile, Leu, Arg, Asp, Val, Pro, Gln, Gly, Ser, Phe, or His;
Xaa at position 100 is Lys, Tyr, Leu, His, Arg, Ile, Ser, Gln, or Pro;
Xaa at position 101 is Asp, Pro, Met, Lys, His, Thr, Val, Tyr, Glu, Asn, Ser, Ala, Gly, Ile, Leu, or Gln;
Xaa at position 102 is Gly, Leu, Glu, Lys, Ser, Tyr, or Pro;
Xaa at position 103 is Asp, or Ser;
Xaa at position 104 is Trp, Val, Cys, Tyr, Thr, Met, Pro, Leu, Gln, Lys, Ala, Phe, or Gly;
Xaa at position 105 is Asn, Pro, Ala, Phe, Ser, Trp, Gln, Tyr, Leu, Lys, Ile, Asp, or His;
Xaa at position 106 is Glu, Ser, Ala, Lys, Thr, Ile, Gly, or Pro;
Xaa at position 108 is Arg, Lys, Asp, Leu, Thr, Ile, Gln, His, Ser, Ala or Pro;
Xaa at position 109 is Arg, Thr, Pro, Glu, Tyr, Leu, Ser, or Gly;
Xaa at position 110 is Lys, Ala, Asn, Thr, Leu, Arg, Gln, His, Glu, Ser, or Trp;
Xaa at position 111 is Leu, Ile, Arg, Asp, or Met;
Xaa at position 112 is Thr, Val, Gln, Tyr, Glu, His, Ser, or Phe;
Xaa at position 113 is Phe, Ser, Cys, His, Gly, Trp, Tyr, Asp, Lys, Leu, Ile, Val or Asn;
Xaa at position 114 is Tyr, Cys, His, Ser, Trp, Arg, or Leu;
Xaa at position 115 is Leu, Asn, Val, Pro, Arg, Ala, His, Thr, Trp, or Met;
Xaa at position 116 is Lys, Leu, Pro, Thr, Met, Asp, Val, Glu, Arg, Trp, Ser, Asn, His, Ala, Tyr, Phe, Gln, or Ile;
Xaa at position 117 is Thr, Ser, Asn, Ile, Trp, Lys, or Pro;
Xaa at position 118 is Leu, Ser, Pro, Ala, Glu, Cys, Asp, or Tyr;
Xaa at position 119 is Glu, Ser, Lys, Pro, Leu, Thr, Tyr, or Arg;
Xaa at position 120 is Asn, Ala, Pro, Leu, His, Val, or Gln;
Xaa at position 121 is Ala, Ser, Ile, Asn, Pro, Lys, Asp, or Gly;
Xaa at position 122 is Gln, Ser, Met, Trp, Arg, Phe, Pro, His, Ile, Tyr, or Cys;
Xaa at position 123 is Ala, Met, Glu, His, Ser, Pro, Tyr, or Leu,
wherein from 1 to 14 amino acids can optionally be deleted from the N-terminus and/or from 1 to 15 amino acids can optionally be deleted from the C-terminus of said modified human IL-3 amino acid sequence; and wherein from 1 to 44 of the amino acids designated by Xaa are different from the corresponding amino acids of native (1-133) human interleukin-3; and
(V) a colony stimulating factor;
and wherein L1 is a linker capable of linking R1 to R2;
with the proviso that at least R1 or R2 is selected from the polypeptide of formula (I), (II), or (III); and
said hematopoietic protein can optionally be immediately preceded by (methionine−1), (alanine−1) or (methionine−2, alanine−1).
2. A hematopoietic protein comprising; an amino acid sequence of the formula:
R1-L1-R2, R2-L1-R1, R1-R2, or R2-R1
wherein R1 and R2 are independently selected from the group consisting of:
(I) A polypeptide comprising; a modified human G-CSF amino acid sequence of the formula:
1                                   10 (SEQ ID NO: 1) Xaa Xaa Xaa Gly Pro Ala Ser Ser Leu Pro Gln Ser Xaa                         20 Leu Leu Xaa Xaa Xaa Glu Gln Val Xaa Lys Xaa Gln Gly Xaa Gly 30                                      40 Ala Xaa Leu Gln Glu Xaa Leu Xaa Ala Thr Tyr Lys Leu Xaa Xaa                         50 Xaa Glu Xaa Xaa Val Xaa Xaa Gly His Ser Xaa Gly Ile Pro Trp 60                                      70 Ala Pro Leu Ser Ser Xaa Pro Ser Xaa Ala Leu Xaa Leu Ala Gly                         80 Xaa Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu 90                                      100 Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu                         110 Xaa Thr Leu Gln Xaa Asp Val Ala Asp Phe Ala Xaa Thr Ile Trp 120                                     130 Gln Gln Met Glu Xaa Xaa Gly Met Ala Pro Ala Leu Gln Pro Thr                         140 Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Xaa Gln Xaa Xaa Ala 150                                     160 Gly Gly Val Leu Val Ala Ser Xaa Leu Gln Xaa Phe Leu Xaa Xaa                         170 Ser Tyr Arg Val Leu Xaa Xaa Leu Ala Gln Pro
wherein
Xaa at position 1 is Thr, Ser, Arg, Tyr or Gly;
Xaa at position 2 is Pro or Leu;
Xaa at position 3 is Leu, Arg, Tyr or Ser;
Xaa at position 13 is Phe, Ser, His, Thr or Pro;
Xaa at position 16 is Lys, Pro, Ser, Thr or His;
Xaa at position 17 is Cys, Ser, Gly, Ala, Ile, Tyr or Arg;
Xaa at position 18 is Leu, Thr, Pro, His, Ile or Cys;
Xaa at position 22 is Arg, Tyr, Ser, Thr or Ala;
Xaa at position 24 is Ile, Pro, Tyr or Leu;
Xaa at position 27 is Asp, or Gly;
Xaa at position 30 is Ala, Ile, Leu or Gly;
Xaa at position 34 is Lys or Ser;
Xaa at position 36 is Cys or Ser;
Xaa at position 42 is Cys or Ser;
Xaa at position 43 is His, Thr, Gly, Val, Lys, Trp, Ala, Arg, Cys, or Leu;
Xaa at position 44 is Pro, Gly, Arg, Asp, Val, Ala, His, Trp, Gln, or Thr;
Xaa at position 46 is Glu, Arg, Phe, Arg, Ile or Ala;
Xaa at position 47 is Leu or Thr;
Xaa at position 49 is Leu, Phe, Arg or Ser;
Xaa at position 50 is Leu, Ile, His, Pro or Tyr;
Xaa at position 54 is Leu or His;
Xaa at position 64 is Cys or Ser;
Xaa at position 67 is Gln, Lys, Leu or Cys;
Xaa at position 70 is Gln, Pro, Leu, Arg or Ser;
Xaa at position 74 is Cys or Ser;
Xaa at position 104 is Asp, Gly or Val;
Xaa at position 108 is Leu, Ala, Val, Arg, Trp, Gln or Gly;
Xaa at position 115 is Thr, His, Leu or Ala;
Xaa at position 120 is Gln, Gly, Arg, Lys or His
Xaa at position 123 is Glu, Arg, Phe or Thr
Xaa at position 144 is Phe, His, Arg, Pro, Leu, Gln or Glu;
Xaa at position 146 is Arg or Gln;
Xaa at position 147 is Arg or Gln;
Xaa at position 156 is His, Gly or Ser;
Xaa at position 159 is Ser, Arg, Thr, Tyr, Val or Gly;
Xaa at position 162 is Glu, Leu, Gly or Trp;
Xaa at position 163 is Val, Gly, Arg or Ala;
Xaa at position 169 is Arg, Ser, Leu, Arg or Cys;
Xaa at position 170 is His, Arg or Ser,
wherein optionally 1-11 amino acids from the N-terminus and 1-5 from the C-terminus can optionally be deleted from said modified human G-CSF amino acid sequence; and
wherein the N-terminus is joined to the C-terminus directly or through a linker capable of joining the N-terminus to the C-terminus and having new C- and N-termini at amino acids;
38-39 39-40 40-41 41-42 42-43 43-44 45-46 48-49 49-50 52-53 53-54 54-55 55-56 56-57 57-58 58-59 59-60 60-61 61-62 62-63 63-64 64-65 65-66 66-67 67-68 68-69 69-70 70-71 71-72 91-92 92-93 93-94 94-95 95-96 96-97 97-98 98-99  99-100 123-124 124-125 125-126 126-127 128-129 128-129 129-130 130-131 131-132 132-133 133-134 134-135 135-136 136-137 137-138 138-139 139-140 140-141 141-142 or 142-143 respectively;
(II) A polypeptide comprising; a modified human IL-3 amino acid sequence of the formula:
Ala Pro Met Thr Gln Thr Thr Ser Leu Lys Thr Ser Trp Val Asn (SEQ ID NO: 2) 1               5                   10                  15 Cys Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 20                  25                  30 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Asn Xaa Xaa Xaa Xaa Xaa Xaa                 35                  40                  45 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 50                  55                  60 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 65                  70                  75 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 80                  85                  90 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 95                  100                 105 Xaa Phe Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 110                 115                 120 Xaa Xaa Xaa Gln Gln Thr Thr Leu Ser Leu Ala Ile Phe                 125                 130
wherein Xaa at position 17 is Ser, Lys, Gly, Asp, Met, Gln, or Arg;
Xaa at position 18 is Asn, His, Leu, Ile, Phe, Arg, or Gln;
Xaa at position 19 is Met, Phe, Ile, Arg, Gly, Ala, or Cys;
Xaa at position 20 is Ile, Cys, Gln, Glu, Arg, Pro, or Ala;
Xaa at position 21 is Asp, Phe, Lys, Arg, Ala, Gly, Glu, Gln, Asn, Thr, Ser or Val;
Xaa at position 22 is Glu, Trp, Pro, Ser, Ala, His, Asp, Asn, Gln, Leu, Val or Gly;
Xaa at position 23 is Ile, Val, Ala, Gly, Trp, Lys, Phe, Leu, Ser, or Arg;
Xaa at position 24 is Ile, Gly, Val, Arg, Ser, Phe, or Leu;
Xaa at position 25 is Thr, His, Gly, Gln, Arg, Pro, or Ala;
Xaa at position 26 is His, Thr, Phe, Gly, Arg, Ala, or Trp;
Xaa at position 27 is Leu, Gly, Arg, Thr, Ser, or Ala;
Xaa at position 28 is Lys, Arg, Leu, Gln, Gly, Pro, Val or Trp;
Xaa at position 29 is Gln, Asn, Leu, Pro, Arg, or Val;
Xaa at position 30 is Pro, His, Thr, Gly, Asp, Gln, Ser, Leu, or Lys;
Xaa at position 31 is Pro, Asp, Gly, Ala, Arg, Leu, or Gln;
Xaa at position 32 is Leu, Val, Arg, Gln, Asn, Gly, Ala, or Glu;
Xaa at position 33 is Pro, Leu, Gln, Ala, Thr, or Glu;
Xaa at position 34 is Leu, Val, Gly, Ser, Lys, Glu, Gln, Thr, Arg, Ala, Phe, Ile or Met;
Xaa at position 35 is Leu, Ala, Gly, Asn, Pro, Gln, or Val;
Xaa at position 36 is Asp, Leu, or Val;
Xaa at position 37 is Phe, Ser, Pro, Trp, or Ile;
Xaa at position 38 is Asn, or Ala;
Xaa at position 40 is Leu, Trp, or Arg;
Xaa at position 41 is Asn, Cys, Arg, Leu, His, Met, or Pro;
Xaa at position 42 is Gly, Asp, Ser, Cys, Asn, Lys, Thr, Leu, Val, Glu, Phe, Tyr, Ile, Met or Ala;
Xaa at position 43 is Glu, Asn, Tyr, Leu, Phe, Asp, Ala, Cys, Gln, Arg, Thr, Gly or Ser;
Xaa at position 44 is Asp, Ser, Leu, Arg, Lys, Thr, Met, Trp, Glu, Asn, Gln, Ala or Pro;
Xaa at position 45 is Gln, Pro, Phe, Val, Met, Leu, Thr, Lys, Trp, Asp, Asn, Arg, Ser, Ala, Ile, Glu or His;
Xaa at position 46 is Asp, Phe, Ser, Thr, Cys, Glu, Asn, Gln, Lys, His, Ala, Tyr, Ile, Val or Gly;
Xaa at position 47 is Ile, Gly, Val, Ser, Arg, Pro, or His;
Xaa at position 48 is Leu, Ser, Cys, Arg, Ile, His, Phe; Glu, Lys, Thr, Ala, Met, Val or Asn;
Xaa at position 49 is Met, Arg, Ala, Gly, Pro, Asn, His, or Asp;
Xaa at position 50 is Glu, Leu, Thr, Asp, Tyr, Lys, Asn, Ser, Ala, Ile, Val, His, Phe, Met or Gln;
Xaa at position 51 is Asn, Arg, Met, Pro, Ser, Thr, or His;
Xaa at position 52 is Asn, His, Arg, Leu, Gly, Ser, or Thr;
Xaa at position 53 is Leu, Thr, Ala, Gly, Glu, Pro, Lys, Ser, or Met;
Xaa at position 54 is Arg, Asp, Ile, Ser, Val, Thr, Gln, Asn, Lys, His, Ala or Leu;
Xaa at position 55 is Arg, Thr, Val, Ser, Leu, or Gly;
Xaa at position 56 is Pro, Gly, Cys, Ser, Gln, Glu, Arg, His, Thr, Ala, Tyr, Phe, Leu, Val or Lys;
Xaa at position 57 is Asn or Gly;
Xaa at position 58 is Leu, Ser, Asp, Arg, Gln, Val, or Cys;
Xaa at position 59 is Glu Tyr, His, Leu, Pro, or Arg;
Xaa at position 60 is Ala, Ser, Pro, Tyr, Asn, or Thr;
Xaa at position 61 is Phe, Asn, Glu, Pro, Lys, Arg, or Ser;
Xaa at position 62 is Asn, His, Val, Arg, Pro, Thr, Asp, or Ile;
Xaa at position 63 is Arg, Tyr, Trp, Lys, Ser, His, Pro, or Val;
Xaa at position 64 is Ala, Asn, Pro, Ser, or Lys;
Xaa at position 65 is Val, Thr, Pro, His, Leu, Phe, or Ser;
Xaa at position 66 is Lys, Ile, Arg, Val, Asn, Glu, or Ser;
Xaa at position 67 is Ser, Ala, Phe, Val, Gly, Asn, Ile, Pro, or His;
Xaa at position 68 is Leu, Val, Trp, Ser, Ile, Phe, Thr, or His;
Xaa at position 69 is Gln, Ala, Pro, Thr, Glu, Arg, Trp, Gly, or Leu;
Xaa at position 70 is Asn, Leu, Val, Trp, Pro, or Ala;
Xaa at position 71 is Ala, Met, Leu, Pro, Arg, Glu, Thr, Gln, Trp, or Asn;
Xaa at position 72 is Ser, Glu, Met, Ala, His, Asn, Arg, or Asp;
Xaa at position 73 is Ala, Glu, Asp, Leu, Ser, Gly, Thr, or Arg;
Xaa at position 74 is Ile, Met, Thr, Pro, Arg, Gly, Ala;
Xaa at position 75 is Glu, Lys, Gly, Asp, Pro, Trp, Arg, Ser, Gln, or Leu;
Xaa at position 76 is Ser, Val, Ala, Asn, Trp, Glu, Pro, Gly, or Asp;
Xaa at position 77 is Ile, Ser, Arg, Thr, or Leu;
Xaa at position 78 is Leu, Ala, Ser, Glu, Phe, Gly, or Arg;
Xaa at position 79 is Lys, Thr, Asn, Met, Arg, Ile, Gly, or Asp;
Xaa at position 80 is Asn, Trp, Val, Gly, Thr, Leu, Glu, or Arg;
Xaa at position 81 is Leu, Gln, Gly, Ala, Trp, Arg, Val, or Lys;
Xaa at position 82 is Leu, Gln, Lys, Trp, Arg, Asp, Glu, Asn, His, Thr, Ser, Ala, Tyr, Phe, Ile, Met or Val;
Xaa at position 83 is Pro, Ala, Thr, Trp, Arg, or Met;
Xaa at position 84 is Cys, Glu, Gly, Arg, Met, or Val;
Xaa at position 85 is Leu, Asn, Val, or Gln;
Xaa at position 86 is Pro, Cys, Arg, Ala, or Lys;
Xaa at position 87 is Leu, Ser, Trp, or Gly;
Xaa at position 88 is Ala, Lys, Arg, Val, or Trp;
Xaa at position 89 is Thr, Asp, Cys, Leu, Val, Glu, His, Asn, or Ser;
Xaa at position 90 is Ala, Pro, Ser, Thr, Gly, Asp, Ile, or Met;
Xaa at position 91 is Ala, Pro, Ser, Thr, Phe, Leu, Asp, or His;
Xaa at position 92 is Pro, Phe, Arg, Ser, Lys, His, Ala, Gly, Ile Leu;
Xaa at position 93 is Thr, Asp, Ser, Asn, Pro, Ala, Leu, or Arg;
Xaa at position 94 is Arg, Ile, Ser, Glu, Leu, Val, Gln, Lys, His, Ala, or Pro;
Xaa at position 95 is His, Gln, Pro, Arg, Val, Leu, Gly, Thr, Asn, Lys, Ser, Ala, Trp, Phe, Ile, or Tyr;
Xaa at position 96 is Pro, Lys, Tyr, Gly, Ile, or Thr;
Xaa at position 97 is Ile, Val, Lys, Ala, or Asn;
Xaa at position 98 is His, Ile, Asn, Leu, Asp, Ala, Thr, Glu, Gln, Ser, Phe, Met, Val, Lys, Arg, Tyr or Pro;
Xaa at position 99 is Ile, Leu, Arg, Asp, Val, Pro, Gln, Gly, Ser, Phe, or His;
Xaa at position 100 is Lys, Tyr, Leu, His, Arg, Ile, Ser, Gln, or Pro;
Xaa at position 101 is Asp, Pro, Met, Lys, His, Thr, Val, Tyr, Glu, Asn, Ser, Ala, Gly, Ile, Leu, or Gln;
Xaa at position 102 is Gly, Leu, Glu, Lys, Ser, Tyr, or Pro;
Xaa at position 103 is Asp, or Ser;
Xaa at position 104 is Trp, Val, Cys, Tyr, Thr, Met, Pro, Leu, Gln, Lys, Ala, Phe, or Gly;
Xaa at position 105 is Asn, Pro, Ala, Phe, Ser, Trp, Gln, Tyr, Leu, Lys, Ile, Asp, or His;
Xaa at position 106 is Glu, Ser, Ala, Lys, Thr, Ile, Gly, or Pro;
Xaa at position 108 is Arg, Lys, Asp, Leu, Thr, Ile, Gln, His, Ser, Ala or Pro;
Xaa at position 109 is Arg, Thr, Pro, Glu, Tyr, Leu, Ser, or Gly;
Xaa at position 110 is Lys, Ala, Asn, Thr, Leu, Arg, Gln, His, Glu, Ser, or Trp;
Xaa at position 111 is Leu, Ile, Arg, Asp, or Met;
Xaa at position 112 is Thr, Val, Gln, Tyr, Glu, His, Ser, or Phe;
Xaa at position 113 is Phe, Ser, Cys, His, Gly, Trp, Tyr, Asp, Lys, Leu, Ile, Val or Asn;
Xaa at position 114 is Tyr, Cys, His, Ser, Trp, Arg, or Leu;
Xaa at position 115 is Leu, Asn, Val, Pro, Arg, Ala, His, Thr, Trp, or Met;
Xaa at position 116 is Lys, Leu, Pro, Thr, Met, Asp, Val, Glu, Arg, Trp, Ser, Asn, His, Ala, Tyr, Phe, Gln, or Ile;
Xaa at position 117 is Thr, Ser, Asn, Ile, Trp, Lys, or Pro;
Xaa at position 118 is Leu, Ser, Pro, Ala, Glu, Cys, Asp, or Tyr;
Xaa at position 119 is Glu, Ser, Lys, Pro, Leu, Thr, Tyr, or Arg;
Xaa at position 120 is Asn, Ala, Pro, Leu, His, Val, or Gln;
Xaa at position 121 is Ala, Ser, Ile, Asn, Pro, Lys, Asp, or Gly;
Xaa at position 122 is Gln, Ser, Met, Trp, Arg, Phe, Pro, His, Ile, Tyr, or Cys;
Xaa at position 123 is Ala, Met, Glu, His, Ser, Pro, Tyr, or Leu,
wherein from 1 to 14 amino acids can optionally be deleted from the N-terminus and/or from 1 to 15 amino acids can optionally be deleted from the C-terminus of said modified human IL-3 amino acid sequence; wherein from 0 to 44 of the amino acids designated by Xaa are different from the corresponding amino acids of native (1-133) human interleukin-3; and
wherein the N-terminus is joined to the C-terminus directly or through a linker (L2), capable of joining the N-terminus to the C-terminus and having new C- and N-termini at amino acids:
26-27 49-50 83-84 27-28 50-51 84-85 28-29 51-52 85-86 29-30 52-53 86-87 30-31 53-54 87-88 31-32 54-55 88-89 32-33 64-65 89-90 33-34 65-66 90-91 34-35 66-67 91-92 35-36 67-68 92-93 36-37 68-69 97-98 37-38 69-70 98-99 38-39 70-71  99-100 39-40 71-72 100-101 40-41 72-73 101-102 41-42 82-83 102-103 or 103-104 respectively;
(III) A polypeptide comprising; a modified human c-mpl ligand amino acid sequence of the formula:
SerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeuArgAspSer (SEQ ID NO: 256) 1           5              10             15 HisValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuProThrPro 20             25             30             35 ValLeuLeuProAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGluGlu    40             45             50             55 ThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAla       60             65             70             75 AlaArgGlyGlnLeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGly          80             85             90             95 GlnValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnXaaXaaXaa             100            105            110 XaaGlyArgThrThrAlaHisLysAspProAsnAlaIlePheLeuSerPheGlnHis 115            120            125            130 LeuLeuArgGlyLysValArgPheLeuMetLeuValGlyGlySerThrLeuCysVal    135            140            145            150 Arg 153
wherein
Xaa at position 112 is deleted or Leu, Ala, Val, Ile, Pro, Phe, Trp, or Met;
Xaa at position 113 is deleted or Pro, Phe, Ala, Val, Leu, Ile, Trp, or Met;
Xaa at position 114 is deleted or Pro, Phe, Ala, Val, Leu, Ile, Trp, or Met;
Xaa at position 115 is deleted or Gln, Gly, Ser, Thr, Tyr, or Asn,
wherein the N-terminus is joined to the C-terminus directly or through a linker (L2) capable of joining the N-terminus to the C-terminus and having new C- and N-termini at amino acids:
26-27 51-52 108-109 27-28 52-53 109-110 28-29 53-54 110-111 29-30 54-55 111-112 30-31 55-56 112-113 32-33 56-57 113-114 33-34 57-58 114-115 34-35 58-59 115-116 36-37 59-60 116-117 37-38 78-79 117-118 38-39 79-80 118-119 40-41 80-81 119-120 41-42 81-82 120-121 42-43 82-83 121-122 43-44 83-84 122-123 44-45 84-85 123-124 46-47 85-86 124-125 47-48 86-87 125-126 48-49 87-88 126-127 50-51 88-89 or 127-128 respectively;
(IV) A polypeptide comprising; a modified human IL-3 amino acid sequence of the formula:
Ala Pro Met Thr Gln Thr Thr Ser Leu Lys Thr Ser Trp Val Asn (SEQ ID NO: 2) 1               5                   10                  15 Cys Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 20                  25                  30 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Asn Xaa Xaa Xaa Xaa Xaa Xaa                 35                  40                  45 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 50                  55                  60 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 65                  70                  75 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 80                  85                  90 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 95                  100                 105 Xaa Phe Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 110                 115                 120 Xaa Xaa Xaa Gln Gln Thr Thr Leu Ser Leu Ala Ile Phe                 125                 130
wherein Xaa at position 17 is Ser, Lys, Gly, Asp, Met, Gln, or Arg;
Xaa at position 18 is Asn, His, Leu, Ile, Phe, Arg, or Gln;
Xaa at position 19 is Met, Phe, Ile, Arg, Gly, Ala, or Cys;
Xaa at position 20 is Ile, Cys, Gln, Glu, Arg, Pro, or Ala;
Xaa at position 21 is Asp, Phe, Lys, Arg, Ala, Gly, Glu, Gln, Asn, Thr, Ser or Val;
Xaa at position 22 is Glu, Trp, Pro, Ser, Ala, His, Asp, Asn, Gln, Leu, Val or Gly;
Xaa at position 23 is Ile, Val, Ala, Gly, Trp, Lys, Phe, Leu, Ser, or Arg;
Xaa at position 24 is Ile, Gly, Val, Arg, Ser, Phe, or Leu;
Xaa at position 25 is Thr, His, Gly, Gln, Arg, Pro, or Ala;
Xaa at position 26 is His, Thr, Phe, Gly, Arg, Ala, or Trp;
Xaa at position 27 is Leu, Gly, Arg, Thr, Ser, or Ala;
Xaa at position 28 is Lys, Arg, Leu, Gln, Gly, Pro, Val or Trp;
Xaa at position 29 is Gln, Asn, Leu, Pro, Arg, or Val;
Xaa at position 30 is Pro, His, Thr, Gly, Asp, Gln, Ser, Leu, or Lys;
Xaa at position 31 is Pro, Asp, Gly, Ala, Arg, Leu, or Gln;
Xaa at position 32 is Leu, Val, Arg, Gln, Asn, Gly, Ala, or Glu;
Xaa at position 33 is Pro, Leu, Gln, Ala, Thr, or Glu;
Xaa at position 34 is Leu, Val, Gly, Ser, Lys, Glu, Gln, Thr, Arg, Ala, Phe, Ile or Met;
Xaa at position 35 is Leu, Ala, Gly, Asn, Pro, Gln, or Val;
Xaa at position 36 is Asp, Leu, or Val;
Xaa at position 37 is Phe, Ser, Pro, Trp, or Ile;
Xaa at position 38 is Asn, or Ala;
Xaa at position 40 is Leu, Trp, or Arg;
Xaa at position 41 is Asn, Cys, Arg, Leu, His, Met, or Pro;
Xaa at position 42 is Gly, Asp, Ser, Cys, Asn, Lys, Thr, Leu, Val, Glu, Phe, Tyr, Ile, Met or Ala;
Xaa at position 43 is Glu, Asn, Tyr, Leu, Phe, Asp, Ala, Cys, Gln, Arg, Thr, Gly or Ser;
Xaa at position 44 is Asp, Ser, Leu, Arg, Lys, Thr, Met, Trp, Glu, Asn, Gln, Ala or Pro;
Xaa at position 45 is Gln, Pro, Phe, Val, Met, Leu, Thr, Lys, Trp, Asp, Asn, Arg, Ser, Ala, Ile, Glu or His; Xaa at position 46 is Asp, Phe, Ser, Thr, Cys, Glu, Asn, Gln, Lys, His, Ala, Tyr, Ile, Val or Gly;
Xaa at position 47 is Ile, Gly, Val, Ser, Arg, Pro, or His;
Xaa at position 48 is Leu, Ser, Cys, Arg, Ile, His, Phe, Glu, Lys, Thr, Ala, Met, Val or Asn;
Xaa at position 49 is Met, Arg, Ala, Gly, Pro, Asn, His, or Asp;
Xaa at position 50 is Glu, Leu, Thr, Asp, Tyr, Lys, Asn, Ser, Ala, Ile, Val, His, Phe, Met or Gln;
Xaa at position 51 is Asn, Arg, Met, Pro, Ser, Thr, or His;
Xaa at position 52 is Asn, His, Arg, Leu, Gly, Ser, or Thr;
Xaa at position 53 is Leu, Thr, Ala, Gly, Glu, Pro, Lys, Ser, or Met;
Xaa at position 54 is Arg, Asp, Ile, Ser, Val, Thr, Gln, Asn, Lys, His, Ala or Leu;
Xaa at position 55 is Arg, Thr, Val, Ser, Leu, or Gly;
Xaa at position 56 is Pro, Gly, Cys, Ser, Gln, Glu, Arg, His, Thr, Ala, Tyr, Phe, Leu, Val or Lys;
Xaa at position 57 is Asn or Gly;
Xaa at position 58 is Leu, Ser, Asp, Arg, Gln, Val, or Cys;
Xaa at position 59 is Glu Tyr, His, Leu, Pro, or Arg;
Xaa at position 60 is Ala, Ser, Pro, Tyr, Asn, or Thr;
Xaa at position 61 is Phe, Asn, Glu, Pro, Lys, Arg, or Ser;
Xaa at position 62 is Asn, His, Val, Arg, Pro, Thr, Asp, or Ile;
Xaa at position 63 is Arg, Tyr, Trp, Lys, Ser, His, Pro, or Val;
Xaa at position 64 is Ala, Asn, Pro, Ser, or Lys;
Xaa at position 65 is Val, Thr, Pro, His, Leu, Phe, or Ser;
Xaa at position 66 is Lys, Ile, Arg, Val, Asn, Glu, or Ser;
Xaa at position 67 is Ser, Ala, Phe, Val, Gly, Asn, Ile, Pro, or His;
Xaa at position 68 is Leu, Val, Trp, Ser, Ile, Phe, Thr, or His;
Xaa at position 69 is Gln, Ala, Pro, Thr, Glu, Arg, Trp, Gly, or Leu;
Xaa at position 70 is Asn, Leu, Val, Trp, Pro, or Ala;
Xaa at position 71 is Ala, Met, Leu, Pro, Arg, Glu, Thr, Gln, Trp, or Asn;
Xaa at position 72 is Ser, Glu, Met, Ala, His, Asn, Arg, or Asp;
Xaa at position 73 is Ala, Glu, Asp, Leu, Ser, Gly, Thr, or Arg;
Xaa at position 74 is Ile, Met, Thr, Pro, Arg, Gly, Ala;
Xaa at position 75 is Glu, Lys, Gly, Asp, Pro, Trp, Arg, Ser, Gln, or Leu;
Xaa at position 76 is Ser, Val, Ala, Asn, Trp, Glu, Pro, Gly, or Asp;
Xaa at position 77 is Ile, Ser, Arg, Thr, or Leu;
Xaa at position 78 is Leu, Ala, Ser, Glu, Phe, Gly, or Arg;
Xaa at position 79 is Lys, Thr, Asn, Met, Arg, Ile, Gly, or Asp;
Xaa at position 80 is Asn, Trp, Val, Gly, Thr, Leu, Glu, or Arg;
Xaa at position 81 is Leu, Gln, Gly, Ala, Trp, Arg, Val, or Lys;
Xaa at position 82 is Leu, Gln, Lys, Trp, Arg, Asp, Glu, Asn, His, Thr, Ser, Ala, Tyr, Phe, Ile, Met or Val;
Xaa at position 83 is Pro, Ala, Thr, Trp, Arg, or Met;
Xaa at position 84 is Cys, Glu, Gly, Arg, Met, or Val;
Xaa at position 85 is Leu, Asn, Val, or Gln;
Xaa at position 86 is Pro, Cys, Arg, Ala, or Lys;
Xaa at position 87 is Leu, Ser, Trp, or Gly;
Xaa at position 88 is Ala, Lys, Arg, Val, or Trp;
Xaa at position 89 is Thr, Asp, Cys, Leu, Val, Glu, His, Asn, or Ser;
Xaa at position 90 is Ala, Pro, Ser, Thr, Gly, Asp, Ile, or Met;
Xaa at position 91 is Ala, Pro, Ser, Thr, Phe, Leu, Asp, or His;
Xaa at position 92 is Pro, Phe, Arg, Ser, Lys, His, Ala, Gly, Ile or Leu;
Xaa at position 93 is Thr, Asp, Ser, Asn, Pro, Ala, Leu, or Arg;
Xaa at position 94 is Arg, Ile, Ser, Glu, Leu, Val, Gln, Lys, His, Ala, or Pro;
Xaa at position 95 is His, Gln, Pro, Arg, Val, Leu, Gly, Thr, Asn, Lys, Ser, Ala, Trp, Phe, Ile, or Tyr;
Xaa at position 96 is Pro, Lys, Tyr, Gly, Ile, or Thr;
Xaa at position 97 is Ile, Val, Lys, Ala, or Asn;
Xaa at position 98 is His, Ile, Asn, Leu, Asp, Ala, Thr, Glu, Gln, Ser, Phe, Met, Val, Lys, Arg, Tyr or Pro;
Xaa at position 99 is Ile, Leu, Arg, Asp, Val, Pro, Gln, Gly, Ser, Phe, or His;
Xaa at position 100 is Lys, Tyr, Leu, His, Arg, Ile, Ser, Gln, or Pro;
Xaa at position 101 is Asp, Pro, Met, Lys, His, Thr, Val, Tyr, Glu, Asn, Ser, Ala, Gly, Ile, Leu, or Gln;
Xaa at position 102 is Gly, Leu, Glu, Lys, Ser, Tyr, or Pro;
Xaa at position 103 is Asp, or Ser;
Xaa at position 104 is Trp, Val, Cys, Tyr, Thr, Met, Pro, Leu, Gln, Lys, Ala, Phe, or Gly;
Xaa at position 105 is Asn, Pro, Ala, Phe, Ser, Trp, Gln, Tyr, Leu, Lys, Ile, Asp, or His;
Xaa at position 106 is Glu, Ser, Ala, Lys, Thr, Ile, Gly, or Pro;
Xaa at position 108 is Arg, Lys, Asp, Leu, Thr, Ile, Gln, His, Ser, Ala or Pro;
Xaa at position 109 is Arg, Thr, Pro, Glu, Tyr, Leu, Ser, or Gly;
Xaa at position 110 is Lys, Ala, Asn, Thr, Leu, Arg, Gln, His, Glu, Ser, or Trp;
Xaa at position 111 is Leu, Ile, Arg, Asp, or Met;
Xaa at position 112 is Thr, Val, Gln, Tyr, Glu, His, Ser, or Phe;
Xaa at position 113 is Phe, Ser, Cys, His, Gly, Trp, Tyr, Asp, Lys, Leu, Ile, Val or Asn;
Xaa at position 114 is Tyr, Cys, His, Ser, Trp, Arg, or Leu;
Xaa at position 115 is Leu, Asn, Val, Pro, Arg, Ala, His, Thr, Trp, or Met;
Xaa at position 116 is Lys, Leu, Pro, Thr, Met, Asp, Val, Glu, Arg, Trp, Ser, Asn, His, Ala, Tyr, Phe, Gln, or Ile;
Xaa at position 117 is Thr, Ser, Asn, Ile, Trp, Lys, or Pro;
Xaa at position 118 is Leu, Ser, Pro, Ala, Glu, Cys, Asp, or Tyr;
Xaa at position 119 is Glu, Ser, Lys, Pro, Leu, Thr, Tyr, or Arg;
Xaa at position 120 is Asn, Ala, Pro, Leu, His, Val, or Gln;
Xaa at position 121 is Ala, Ser, Ile, Asn, Pro, Lys, Asp, or Gly;
Xaa at position 122 is Gln, Ser, Met, Trp, Arg, Phe, Pro, His, Ile, Tyr, or Cys;
Xaa at position 123 is Ala, Met, Glu, His, Ser, Pro, Tyr, or Leu;
wherein from 1 to 14 amino acids can optionally be deleted from the N-terminus and/or from 1 to 15 amino acids can optionally be deleted from the C-terminus of said modified human IL-3 amino acid sequence; and wherein from 1 to 44 of the amino acids designated by Xaa are different from the corresponding amino acids of native (1-133) human interleukin-3; and
(V) a colony stimulating factor
wherein L1 is a linker capable of linking R1 to R2
with the proviso that at least R1 or R2 is selected from the polypeptide of formula (I), (II), or (III) and
said hematopoietic protein can optionally be immediately preceded by (methionine−1), (alanine−1) or (methionine−2, alanine−1).
3. A hematopoietic protein comprising an amino acid sequence of the formula:
R1-L1-R2, R2-L1-R1, R1-R2, or R2-R1
wherein R1 and R2 are independently selected from the group consisting of:
(I) A polypeptide comprising; a modified human G-CSF amino acid sequence of the formula:
1                                   10 Xaa Xaa Xaa Gly Pro Ala Ser Ser Leu Pro Gln Ser Xaa (SEQ ID NO: 1)                         20 Leu Leu Xaa Xaa Xaa Glu Gln Val Xaa Lys Xaa Gln Gly Xaa Gly     30                                      40 Ala Xaa Leu Gln Glu Xaa Leu Xaa Ala Thr Tyr Lys Leu Xaa Xaa                         50 Xaa Glu Xaa Xaa Val Xaa Xaa Gly His Ser Xaa Gly Ile Pro Trp     60                                      70 Ala Pro Leu Ser Ser Xaa Pro Ser Xaa Ala Leu Xaa Leu Ala Gly                         80 Xaa Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu     90                                      100 Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu                         110 Xaa Thr Leu Gln Xaa Asp Val Ala Asp Phe Ala Xaa Thr Ile Trp     120                                     130 Gln Gln Met Glu Xaa Xaa Gly Met Ala Pro Ala Leu Gln Pro Thr                         140 Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Xaa Gln Xaa Xaa Ala     150                                     160 Gly Gly Val Leu Val Ala Ser Xaa Leu Gln Xaa Phe Leu Xaa Xaa                         170 Ser Tyr Arg Val Leu Xaa Xaa Leu Ala Gln Pro
wherein
Xaa at position 1 is Thr, Ser, Arg, Tyr or Gly;
Xaa at position 2 is Pro or Leu;
Xaa at position 3 is Leu, Arg, Tyr or Ser;
Xaa at position 13 is Phe, Ser, His, Thr or Pro;
Xaa at position 16 is Lys, Pro, Ser, Thr or His;
Xaa at position 17 is Cys, Ser, Gly, Ala, Ile, Tyr or Arg;
Xaa at position 18 is Leu, Thr, Pro, His, Ile or Cys;
Xaa at position 22 is Arg, Tyr, Ser, Thr or Ala;
Xaa at position 24 is Ile, Pro, Tyr or Leu;
Xaa at position 27 is Asp, or Gly;
Xaa at position 30 is Ala, Ile, Leu or Gly;
Xaa at position 34 is Lys or Ser;
Xaa at position 36 is Cys or Ser;
Xaa at position 42 is Cys or Ser;
Xaa at position 43 is His, Thr, Gly, Val, Lys, Trp, Ala, Arg, Cys, or Leu;
Xaa at position 44 is Pro, Gly, Arg, Asp, Val, Ala, His, Trp, Gln, or Thr;
Xaa at position 46 is Glu, Arg, Phe, Arg, Ile or Ala;
Xaa at position 47 is Leu or Thr;
Xaa at position 49 is Leu, Phe, Arg or Ser;
Xaa at position 50 is Leu, Ile, His, Pro or Tyr;
Xaa at position 54 is Leu or His;
Xaa at position 64 is Cys or Ser;
Xaa at position 67 is Gln, Lys, Leu or Cys;
Xaa at position 70 is Gln, Pro, Leu, Arg or Ser;
Xaa at position 74 is Cys or Ser;
Xaa at position 104 is Asp, Gly or Val;
Xaa at position 108 is Leu, Ala, Val, Arg, Trp, Gln or Gly;
Xaa at position 115 is Thr, His, Leu or Ala;
Xaa at position 120 is Gln, Gly, Arg, Lys or His
Xaa at position 123 is Glu, Arg, Phe or Thr
Xaa at position 144 is Phe, His, Arg, Pro, Leu, Gln or Glu;
Xaa at position 146 is Arg or Gln;
Xaa at position 147 is Arg or Gln;
Xaa at position 156 is His, Gly or Ser;
Xaa at position 159 is Ser, Arg, Thr, Tyr, Val or Gly;
Xaa at position 162 is Glu, Leu, Gly or Trp;
Xaa at position 163 is Val, Gly, Arg or Ala;
Xaa at position 169 is Arg, Ser, Leu, Arg or Cys;
Xaa at position 170 is His, Arg or Ser,
wherein optionally 1-11 amino acids from the N-terminus and 1-5 from the C-terminus can be deleted from said modified human G-CSF amino acid sequence; and
wherein the N-terminus is joined to the C-terminus directly or through a linker capable of joining the N-terminus to the C-terminus and having new C- and N-termini at amino acids:
38-39 62-63 123-124 39-40 63-64 124-125 40-41 64-65 125-126 41-42 65-66 126-127 42-43 66-67 128-129 43-44 67-68 128-129 45-46 68-69 129-130 48-49 69-70 130-131 49-50 70-71 131-132 52-53 71-72 132-133 53-54 91-92 133-134 54-55 92-93 134-135 55-56 93-94 135-136 56-57 94-95 136-137 57-58 95-96 137-138 58-59 96-97 138-139 59-60 97-98 139-140 60-61 98-99 140-141 61-62  99-100 141-142 or 142-143 respectively;
(II) A polypeptide comprising; a modified human IL-3 amino acid sequence of the formula:
Ala Pro Met Thr Gln Thr Thr Ser Leu Lys Thr Ser Trp Val Asn (SEQ ID NO: 2) 1               5                   10                  15 Cys Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 20                  25                  30 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Asn Xaa Xaa Xaa Xaa Xaa Xaa                 35                  40                  45 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 50                  55                  60 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 65                  70                  75 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 80                  85                  90 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 95                  100                 105 Xaa Phe Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 110                 115                 120 Xaa Xaa Xaa Gln Gln Thr Thr Leu Ser Leu Ala Ile Phe                 125                 130
wherein Xaa at position 17 is Ser, Lys, Gly, Asp, Met, Gln, or Arg;
Xaa at position 18 is Asn, His, Leu, Ile, Phe, Arg, or Gln;
Xaa at position 19 is Met, Phe, Ile, Arg, Gly, Ala, or Cys;
Xaa at position 20 is Ile, Cys, Gln, Glu, Arg, Pro, or Ala;
Xaa at position 21 is Asp, Phe, Lys, Arg, Ala, Gly, Glu, Gln, Asn, Thr, Ser or Val;
Xaa at position 22 is Glu, Trp, Pro, Ser, Ala, His, Asp, Asn, Gln, Leu, Val or Gly;
Xaa at position 23 is Ile, Val, Ala, Gly, Trp, Lys, Phe, Leu, Ser, or Arg;
Xaa at position 24 is Ile, Gly, Val, Arg, Ser, Phe, or Leu;
Xaa at position 25 is Thr, His, Gly, Gln, Arg, Pro, or Ala;
Xaa at position 26 is His, Thr, Phe, Gly, Arg, Ala, or Trp;
Xaa at position 27 is Leu, Gly, Arg, Thr, Ser, or Ala;
Xaa at position 28 is Lys, Arg, Leu, Gln, Gly, Pro, Val or Trp;
Xaa at position 29 is Gln, Asn, Leu, Pro, Arg, or Val;
Xaa at position 30 is Pro, His, Thr, Gly, Asp, Gln, Ser, Leu, or Lys;
Xaa at position 31 is Pro, Asp, Gly, Ala, Arg, Leu, or Gln;
Xaa at position 32 is Leu, Val, Arg, Gln, Asn, Gly, Ala, or Glu;
Xaa at position 33 is Pro, Leu, Gln, Ala, Thr, or Glu;
Xaa at position 34 is Leu, Val, Gly, Ser, Lys, Glu, Gln, Thr, Arg, Ala, Phe, Ile or Met;
Xaa at position 35 is Leu, Ala, Gly, Asn, Pro, Gln, or Val;
Xaa at position 36 is Asp, Leu, or Val;
Xaa at position 37 is Phe, Ser, Pro, Trp, or Ile;
Xaa at position 38 is Asn, or Ala;
Xaa at position 40 is Leu, Trp, or Arg;
Xaa at position 41 is Asn, Cys, Arg, Leu, His, Met, or Pro;
Xaa at position 42 is Gly, Asp, Ser, Cys, Asn, Lys, Thr, Leu, Val, Glu, Phe, Tyr, Ile, Met or Ala;
Xaa at position 43 is Glu, Asn, Tyr, Leu, Phe, Asp, Ala, Cys, Gln, Arg, Thr, Gly or Ser;
Xaa at position 44 is Asp, Ser, Leu, Arg, Lys, Thr, Met, Trp, Glu, Asn, Gln, Ala or Pro;
Xaa at position 45 is Gln, Pro, Phe, Val, Met, Leu, Thr, Lys, Trp, Asp, Asn, Arg, Ser, Ala, Ile, Glu or His;
Xaa at position 46 is Asp, Phe, Ser, Thr, Cys, Glu, Asn, Gln, Lys, His, Ala, Tyr, Ile, Val or Gly;
Xaa at position 47 is Ile, Gly, Val, Ser, Arg, Pro, or His;
Xaa at position 48 is Leu, Ser, Cys, Arg, Ile, His, Phe, Glu, Lys, Thr, Ala, Met, Val or Asn;
Xaa at position 49 is Met, Arg, Ala, Gly, Pro, Asn, His, or Asp;
Xaa at position 50 is Glu, Leu, Thr, Asp, Tyr, Lys, Asn, Ser, Ala, Ile, Val, His, Phe, Met or Gln;
Xaa at position 51 is Asn, Arg, Met, Pro, Ser, Thr, or His;
Xaa at position 52 is Asn, His, Arg, Leu, Gly, Ser, or Thr;
Xaa at position 53 is Leu, Thr, Ala, Gly, Glu, Pro, Lys, Ser, or Met;
Xaa at position 54 is Arg, Asp, Ile, Ser, Val, Thr, Gln, Asn, Lys, His, Ala or Leu;
Xaa at position 55 is Arg, Thr, Val, Ser, Leu, or Gly;
Xaa at position 56 is Pro, Gly, Cys, Ser, Gln, Glu, Arg, His, Thr, Ala, Tyr, Phe, Leu, Val or Lys;
Xaa at position 57 is Asn or Gly;
Xaa at position 58 is Leu, Ser, Asp, Arg, Gln, Val, or Cys;
Xaa at position 59 is Glu Tyr, His, Leu, Pro, or Arg;
Xaa at position 60 is Ala, Ser, Pro, Tyr, Asn, or Thr;
Xaa at position 61 is Phe, Asn, Glu, Pro, Lys, Arg, or Ser;
Xaa at position 62 is Asn, His, Val, Arg, Pro, Thr, Asp, or Ile;
Xaa at position 63 is Arg, Tyr, Trp, Lys, Ser, His, Pro, or Val;
Xaa at position 64 is Ala, Asn, Pro, Ser, or Lys;
Xaa at position 65 is Val, Thr, Pro, His, Leu, Phe, or Ser;
Xaa at position 66 is Lys, Ile, Arg, Val, Asn, Glu, or Ser;
Xaa at position 67 is Ser, Ala, Phe, Val, Gly, Asn, Ile, Pro, or His;
Xaa at position 68 is Leu, Val, Trp, Ser, Ile, Phe, Thr, or His;
Xaa at position 69 is Gln, Ala, Pro, Thr, Glu, Arg, Trp, Gly, or Leu;
Xaa at position 70 is Asn, Leu, Val, Trp, Pro, or Ala;
Xaa at position 71 is Ala, Met, Leu, Pro, Arg, Glu, Thr, Gln, Trp, or Asn;
Xaa at position 72 is Ser, Glu, Met, Ala, His, Asn, Arg, or Asp;
Xaa at position 73 is Ala, Glu, Asp, Leu, Ser, Gly, Thr, or Arg;
Xaa at position 74 is Ile, Met, Thr, Pro, Arg, Gly, Ala;
Xaa at position 75 is Glu, Lys, Gly, Asp, Pro, Trp, Arg, Ser, Gln, or Leu;
Xaa at position 76 is Ser, Val, Ala, Asn, Trp, Glu, Pro, Gly, or Asp;
Xaa at position 77 is Ile, Ser, Arg, Thr, or Leu;
Xaa at position 78 is Leu, Ala, Ser, Glu, Phe, Gly, or Arg;
Xaa at position 79 is Lys, Thr, Asn, Met, Arg, Ile, Gly, or Asp;
Xaa at position 80 is Asn, Trp, Val, Gly, Thr, Leu, Glu, or Arg;
Xaa at position 81 is Leu, Gln, Gly, Ala, Trp, Arg, Val, or Lys;
Xaa at position 82 is Leu, Gln, Lys, Trp, Arg, Asp, Glu, Asn, His, Thr, Ser, Ala, Tyr, Phe, Ile, Met or Val;
Xaa at position 83 is Pro, Ala, Thr, Trp, Arg, or Met;
Xaa at position 84 is Cys, Glu, Gly, Arg, Met, or Val;
Xaa at position 85 is Leu, Asn, Val, or Gln;
Xaa at position 86 is Pro, Cys, Arg, Ala, or Lys;
Xaa at position 87 is Leu, Ser, Trp, or Gly;
Xaa at position 88 is Ala, Lys, Arg, Val, or Trp;
Xaa at position 89 is Thr, Asp, Cys, Leu, Val, Glu, His, Asn, or Ser;
Xaa at position 90 is Ala, Pro, Ser, Thr, Gly, Asp, Ile, or Met;
Xaa at position 91 is Ala, Pro, Ser, Thr, Phe, Leu, Asp, or His;
Xaa at position 92 is Pro, Phe, Arg, Ser, Lys, His, Ala, Gly, Ile or Leu;
Xaa at position 93 is Thr, Asp, Ser, Asn, Pro, Ala, Leu, or Arg;
Xaa at position 94 is Arg, Ile, Ser, Glu, Leu, Val, Gln, Lys, His, Ala, or Pro;
Xaa at position 95 is His, Gln, Pro, Arg, Val, Leu, Gly, Thr, Asn, Lys, Ser, Ala, Trp, Phe, Ile, or Tyr;
Xaa at position 96 is Pro, Lys, Tyr, Gly, Ile, or Thr;
Xaa at position 97 is Ile, Val, Lys, Ala, or Asn;
Xaa at position 98 is His, Ile, Asn, Leu, Asp, Ala, Thr, Glu, Gln, Ser, Phe, Met, Val, Lys, Arg, Tyr or Pro;
Xaa at position 99 is Ile, Leu, Arg, Asp, Val, Pro, Gln, Gly, Ser, Phe, or His;
Xaa at position 100 is Lys, Tyr, Leu, His, Arg, Ile, Ser, Gln, or Pro;
Xaa at position 101 is Asp, Pro, Met, Lys, His, Thr, Val, Tyr, Glu, Asn, Ser, Ala, Gly, Ile, Leu, or Gln;
Xaa at position 102 is Gly, Leu, Glu, Lys, Ser, Tyr, or Pro;
Xaa at position 103 is Asp, or Ser;
Xaa at position 104 is Trp, Val, Cys, Tyr, Thr, Met, Pro, Leu, Gln, Lys, Ala, Phe, or Gly;
Xaa at position 105 is Asn, Pro, Ala, Phe, Ser, Trp, Gln, Tyr, Leu, Lys, Ile, Asp, or His;
Xaa at position 106 is Glu, Ser, Ala, Lys, Thr, Ile, Gly, or Pro;
Xaa at position 108 is Arg, Lys, Asp, Leu, Thr, Ile, Gln, His, Ser, Ala or Pro;
Xaa at position 109 is Arg, Thr, Pro, Glu, Tyr, Leu, Ser, or Gly;
Xaa at position 110 is Lys, Ala, Asn, Thr, Leu, Arg, Gln, His, Glu, Ser, or Trp;
Xaa at position 111 is Leu, Ile, Arg, Asp, or Met;
Xaa at position 112 is Thr, Val, Gln, Tyr, Glu, His, Ser, or Phe;
Xaa at position 113 is Phe, Ser, Cys, His, Gly, Trp, Tyr, Asp, Lys, Leu, Ile, Val or Asn;
Xaa at position 114 is Tyr, Cys, His, Ser, Trp, Arg, or Leu;
Xaa at position 115 is Leu, Asn, Val, Pro, Arg, Ala, His, Thr, Trp, or Met;
Xaa at position 116 is Lys, Leu, Pro, Thr, Met, Asp, Val, Glu, Arg, Trp, Ser, Asn, His, Ala, Tyr, Phe, Gln, or Ile;
Xaa at position 117 is Thr, Ser, Asn, Ile, Trp, Lys, or Pro;
Xaa at position 118 is Leu, Ser, Pro, Ala, Glu, Cys, Asp, or Tyr;
Xaa at position 119 is Glu, Ser, Lys, Pro, Leu, Thr, Tyr, or Arg;
Xaa at position 120 is Asn, Ala, Pro, Leu, His, Val, or Gln;
Xaa at position 121 is Ala, Ser, Ile, Asn, Pro, Lys, Asp, or Gly;
Xaa at position 122 is Gln, Ser, Met, Trp, Arg, Phe, Pro, His, Ile, Tyr, or Cys;
Xaa at position 123 is Ala, Met, Glu, His, Ser, Pro, Tyr, or Leu,
wherein from 1 to 14 amino acids can optionally be deleted from the N-terminus and/or from 1 to 15 amino acids can optionally be deleted from the C-terminus of said modified human IL-3 amino acid sequence; and wherein from 0 to 44 of the amino acids designated by Xaa are different from the corresponding amino acids of native (1-133) human interleukin-3; and
wherein the N-terminus is joined to the C-terminus directly or through a linker (L2) capable of joining the N-terminus to the C-terminus and having new C- and N-termini at amino acids:
26-27 49-50 83-84 27-28 50-51 84-85 28-29 51-52 85-86 29-30 52-53 86-87 30-31 53-54 87-88 31-32 54-55 88-89 32-33 64-65 89-90 33-34 65-66 90-91 34-35 66-67 91-92 35-36 67-68 92-93 36-37 68-69 97-98 37-38 69-70 98-99 38-39 70-71  99-100 39-40 71-72 100-101 40-41 72-73 101-102 41-42 82-83 102-103 or 103-104 respectively;
(III) A polypeptide comprising; a modified human c-mpl ligand amino acid sequence of the formula:
SerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeuArgAspSer (SEQ ID NO: 256) 1           5              10             15 HisValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuProThrPro 20             25             30             35 ValLeuLeuProAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGluGlu    40             45             50             55 ThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAla       60             65             70             75 AlaArgGlyGlnLeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGly          80             85             90             95 GlnValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnXaaXaaXaa             100            105            110 XaaGlyArgThrThrAlaHisLysAspProAsnAlaIlePheLeuSerPheGlnHis 115            120            125            130 LeuLeuArgGlyLysValArgPheLeuMetLeuValGlyGlySerThrLeuCysVal    135            140            145            150 Arg 153
wherein
Xaa at position 112 is deleted or Leu, Ala, Val, Ile, Pro, Phe, Trp, or Met;
Xaa at position 113 is deleted or Pro, Phe, Ala, Val, Leu, Ile, Trp, or Met;
Xaa at position 114 is deleted or Pro, Phe, Ala, Val, Leu, Ile, Trp, or Met;
Xaa at position 115 is deleted or Gln, Gly, Ser, Thr, Tyr, or Asn; and
wherein the N-terminus is joined to the C-terminus directly or through a linker (L2) capable of joining the N-terminus to the C-terminus and having new C- and N-termini at amino acids:
52-53 108-109 53-54 109-110 54-55 110-111 55-56 111-112 56-57 112-113 57-58 113-114 58-59 114-115 59-60 115-116 78-79 116-117 79-80 117-118 80-81 118-119 81-82 119-120 82-83 120-121 83-84 121-122 84-85 122-123 85-86 123-124 86-87 124-125 87-88 125-126 88-89 126-127 or 127-128 respectively;
(IV) A polypeptide comprising; a modified human IL-3 amino acid sequence of the formula:
Ala Pro Met Thr Gln Thr Thr Ser Leu Lys Thr Ser Trp Val Asn (SEQ ID NO: 2) 1               5                   10                  15 Cys Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 20                  25                  30 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Asn Xaa Xaa Xaa Xaa Xaa Xaa                 35                  40                  45 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 50                  55                  60 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 65                  70                  75 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 80                  85                  90 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 95                  100                 105 Xaa Phe Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 110                 115                 120 Xaa Xaa Xaa Gln Gln Thr Thr Leu Ser Leu Ala Ile Phe                 125                 130
wherein Xaa at position 17 is Ser, Lys, Gly, Asp, Met, Gln, or Arg;
Xaa at position 18 is Asn, His, Leu, Ile, Phe, Arg, or Gln;
Xaa at position 19 is Met, Phe, Ile, Arg, Gly, Ala, or Cys;
Xaa at position 20 is Ile, Cys, Gln, Glu, Arg, Pro, or Ala;
Xaa at position 21 is Asp, Phe, Lys, Arg, Ala, Gly, Glu, Gln, Asn, Thr, Ser or Val;
Xaa at position 22 is Glu, Trp, Pro, Ser, Ala, His, Asp, Asn, Gln, Leu, Val or Gly;
Xaa at position 23 is Ile, Val, Ala, Gly, Trp, Lys, Phe, Leu, Ser, or Arg;
Xaa at position 24 is Ile, Gly, Val, Arg, Ser, Phe, or Leu;
Xaa at position 25 is Thr, His, Gly, Gln, Arg, Pro, or Ala;
Xaa at position 26 is His, Thr, Phe, Gly, Arg, Ala, or Trp;
Xaa at position 27 is Leu, Gly, Arg, Thr, Ser, or Ala;
Xaa at position 28 is Lys, Arg, Leu, Gln, Gly, Pro, Val or Trp;
Xaa at position 29 is Gln, Asn, Leu, Pro, Arg, or Val;
Xaa at position 30 is Pro, His, Thr, Gly, Asp, Gln, Ser, Leu, or Lys;
Xaa at position 31 is Pro, Asp, Gly, Ala, Arg, Leu, or Gln;
Xaa at position 32 is Leu, Val, Arg, Gln, Asn, Gly, Ala, or Glu;
Xaa at position 33 is Pro, Leu, Gln, Ala, Thr, or Glu;
Xaa at position 34 is Leu, Val, Gly, Ser, Lys, Glu, Gln, Thr, Arg, Ala, Phe, Ile or Met;
Xaa at position 35 is Leu, Ala, Gly, Asn, Pro, Gln, or Val;
Xaa at position 36 is Asp, Leu, or Val;
Xaa at position 37 is Phe, Ser, Pro, Trp, or Ile;
Xaa at position 38 is Asn, or Ala;
Xaa at position 40 is Leu, Trp, or Arg;
Xaa at position 41 is Asn, Cys, Arg, Leu, His, Met, or Pro;
Xaa at position 42 is Gly, Asp, Ser, Cys, Asn, Lys, Thr, Leu, Val, Glu, Phe, Tyr, Ile, Met or Ala;
Xaa at position 43 is Glu, Asn, Tyr, Leu, Phe, Asp, Ala, Cys, Gln, Arg, Thr, Gly or Ser;
Xaa at position 44 is Asp, Ser, Leu, Arg, Lys, Thr, Met, Trp, Glu, Asn, Gln, Ala or Pro;
Xaa at position 45 is Gln, Pro, Phe, Val, Met, Leu, Thr, Lys, Trp, Asp, Asn, Arg, Ser, Ala, Ile, Glu or His;
Xaa at position 46 is Asp, Phe, Ser, Thr, Cys, Glu, Asn, Gln, Lys, His, Ala, Tyr, Ile, Val or Gly;
Xaa at position 47 is Ile, Gly, Val, Ser, Arg, Pro, or His;
Xaa at position 48 is Leu, Ser, Cys, Arg, Ile, His, Phe, Glu, Lys, Thr, Ala, Met, Val or Asn;
Xaa at position 49 is Met, Arg, Ala, Gly, Pro, Asn, His, or Asp;
Xaa at position 50 is Glu, Leu, Thr, Asp, Tyr, Lys, Asn, Ser, Ala, Ile, Val, His, Phe, Met or Gln;
Xaa at position 51 is Asn, Arg, Met, Pro, Ser, Thr, or His;
Xaa at position 52 is Asn, His, Arg, Leu, Gly, Ser, or Thr;
Xaa at position 53 is Leu, Thr, Ala, Gly, Glu, Pro, Lys, Ser, or Met;
Xaa at position 54 is Arg, Asp, Ile, Ser, Val, Thr, Gln, Asn, Lys, His, Ala or Leu;
Xaa at position 55 is Arg, Thr, Val, Ser, Leu, or Gly;
Xaa at position 56 is Pro, Gly, Cys, Ser, Gln, Glu, Arg, His, Thr, Ala, Tyr, Phe, Leu, Val or Lys;
Xaa at position 57 is Asn or Gly;
Xaa at position 58 is Leu, Ser, Asp, Arg, Gln, Val, or Cys;
Xaa at position 59 is Glu Tyr, His, Leu, Pro, or Arg;
Xaa at position 60 is Ala, Ser, Pro, Tyr, Asn, or Thr;
Xaa at position 61 is Phe, Asn, Glu, Pro, Lys, Arg, or Ser;
Xaa at position 62 is Asn, His, Val, Arg, Pro, Thr, Asp, or Ile;
Xaa at position 63 is Arg, Tyr, Trp, Lys, Ser, His, Pro, or Val;
Xaa at position 64 is Ala, Asn, Pro, Ser, or Lys;
Xaa at position 65 is Val, Thr, Pro, His, Leu, Phe, or Ser;
Xaa at position 66 is Lys, Ile, Arg, Val, Asn, Glu, or Ser;
Xaa at position 67 is Ser, Ala, Phe, Val, Gly, Asn, Ile, Pro, or His;
Xaa at position 68 is Leu, Val, Trp, Ser, Ile, Phe, Thr, or His;
Xaa at position 69 is Gln, Ala, Pro, Thr, Glu, Arg, Trp, Gly, or Leu;
Xaa at position 70 is Asn, Leu, Val, Trp, Pro, or Ala;
Xaa at position 71 is Ala, Met, Leu, Pro, Arg, Glu, Thr, Gln, Trp, or Asn;
Xaa at position 72 is Ser, Glu, Met, Ala, His, Asn, Arg, or Asp;
Xaa at position 73 is Ala, Glu, Asp, Leu, Ser, Gly, Thr, or Arg;
Xaa at position 74 is Ile, Met, Thr, Pro, Arg, Gly, Ala;
Xaa at position 75 is Glu, Lys, Gly, Asp, Pro, Trp, Arg, Ser, Gln, or Leu;
Xaa at position 76 is Ser, Val, Ala, Asn, Trp, Glu, Pro, Gly, or Asp;
Xaa at position 77 is Ile, Ser, Arg, Thr, or Leu;
Xaa at position 78 is Leu, Ala, Ser, Glu, Phe, Gly, or Arg;
Xaa at position 79 is Lys, Thr, Asn, Met, Arg, Ile, Gly, or Asp;
Xaa at position 80 is Asn, Trp, Val, Gly, Thr, Leu, Glu, or Arg;
Xaa at position 81 is Leu, Gln, Gly, Ala, Trp, Arg, Val, or Lys;
Xaa at position 82 is Leu, Gln, Lys, Trp, Arg, Asp, Glu, Asn, His, Thr, Ser, Ala, Tyr, Phe, Ile, Met or Val;
Xaa at position 83 is Pro, Ala, Thr, Trp, Arg, or Met;
Xaa at position 84 is Cys, Glu, Gly, Arg, Met, or Val;
Xaa at position 85 is Leu, Asn, Val, or Gln;
Xaa at position 86 is Pro, Cys, Arg, Ala, or Lys;
Xaa at position 87 is Leu, Ser, Trp, or Gly;
Xaa at position 88 is Ala, Lys, Arg, Val, or Trp;
Xaa at position 89 is Thr, Asp, Cys, Leu, Val, Glu, His, Asn, or Ser;
Xaa at position 90 is Ala, Pro, Ser, Thr, Gly, Asp, Ile, or Met;
Xaa at position 91 is Ala, Pro, Ser, Thr, Phe, Leu, Asp, or His;
Xaa at position 92 is Pro, Phe, Arg, Ser, Lys, His, Ala, Gly, Ile or Leu;
Xaa at position 93 is Thr, Asp, Ser, Asn, Pro, Ala, Leu, or Arg;
Xaa at position 94 is Arg, Ile, Ser, Glu, Leu, Val, Gln, Lys, His, Ala, or Pro;
Xaa at position 95 is His, Gln, Pro, Arg, Val, Leu, Gly, Thr, Asn, Lys, Ser, Ala, Trp, Phe, Ile, or Tyr;
Xaa at position 96 is Pro, Lys, Tyr, Gly, Ile, or Thr;
Xaa at position 97 is Ile, Val, Lys, Ala, or Asn;
Xaa at position 98 is His, Ile, Asn, Leu, Asp, Ala, Thr, Glu, Gln, Ser, Phe, Met, Val, Lys, Arg, Tyr or Pro;
Xaa at position 99 is Ile, Leu, Arg, Asp, Val, Pro, Gln, Gly, Ser, Phe, or His;
Xaa at position 100 is Lys, Tyr, Leu, His, Arg, Ile, Ser, Gln, or Pro;
Xaa at position 101 is Asp, Pro, Met, Lys, His, Thr, Val, Tyr, Glu, Asn, Ser, Ala, Gly, Ile, Leu, or Gln;
Xaa at position 102 is Gly, Leu, Glu, Lys, Ser, Tyr, or Pro;
Xaa at position 103 is Asp, or Ser;
Xaa at position 104 is Trp, Val, Cys, Tyr, Thr, Met, Pro, Leu, Gln, Lys, Ala, Phe, or Gly;
Xaa at position 105 is Asn, Pro, Ala, Phe, Ser, Trp, Gln, Tyr, Leu, Lys, Ile, Asp, or His;
Xaa at position 106 is Glu, Ser, Ala, Lys, Thr, Ile, Gly, or Pro;
Xaa at position 108 is Arg, Lys, Asp, Leu, Thr, Ile, Gln, His, Ser, Ala or Pro;
Xaa at position 109 is Arg, Thr, Pro, Glu, Tyr, Leu, Ser, or Gly;
Xaa at position 110 is Lys, Ala, Asn, Thr, Leu, Arg, Gln, His, Glu, Ser, or Trp;
Xaa at position 111 is Leu, Ile, Arg, Asp, or Met;
Xaa at position 112 is Thr, Val, Gln, Tyr, Glu, His, Ser, or Phe;
Xaa at position 113 is Phe, Ser, Cys, His, Gly, Trp, Tyr, Asp, Lys, Leu, Ile, Val or Asn;
Xaa at position 114 is Tyr, Cys, His, Ser, Trp, Arg, or Leu;
Xaa at position 115 is Leu, Asn, Val, Pro, Arg, Ala, His, Thr, Trp, or Met;
Xaa at position 116 is Lys, Leu, Pro, Thr, Met, Asp, Val, Glu, Arg, Trp, Ser, Asn, His, Ala, Tyr, Phe, Gln, or Ile;
Xaa at position 117 is Thr, Ser, Asn, Ile, Trp, Lys, or Pro;
Xaa at position 118 is Leu, Ser, Pro, Ala, Glu, Cys, Asp, or Tyr;
Xaa at position 119 is Glu, Ser, Lys, Pro, Leu, Thr, Tyr, or Arg;
Xaa at position 120 is Asn, Ala, Pro, Leu, His, Val, or Gln;
Xaa at position 121 is Ala, Ser, Ile, Asn, Pro, Lys, Asp, or Gly;
Xaa at position 122 is Gln, Ser, Met, Trp, Arg, Phe, Pro, His, Ile, Tyr, or Cys;
Xaa at position 123 is Ala, Met, Glu, His, Ser, Pro, Tyr, or Leu,
wherein from 1 to 14 amino acids can optionally be deleted from the N-terminus and/or from 1 to 15 amino acids can optionally be deleted from the C-terminus of said modified human IL-3 amino acid sequence; and wherein from 1 to 44 of the amino acids designated by Xaa are different from the corresponding amino acids of native (1-133) human interleukin-3, and
(V) a colony stimulating factor;
and wherein L1 is a linker capable of linking R1 to R2
with the proviso that at least R1 or R2 is selected from the polypeptide of formula (I), (II), or (III); and
said hematopoietic protein can optionally be immediately preceded by (methionine−1), (alanine−1) or (methionine−2, alanine−1).
4. The hematopoietic protein as recited in claim 1 wherein the polypeptide of (IV) is selected from the from the group consisting of:
Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys (SEQ ID NO: 225) Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Ala Glu Asp Val Asp Ile Leu Met Glu Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln; Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys (SEQ ID NO: 226) Arg Pro Pro Asn Pro Leu Leu Asp Pro Asn Asn Leu Asn Ser Glu Asp Met Asp Ile Leu Met Glu Arg Asn Leu Arg Thr Pro Asn Leu Leu Ala Phe Val Arg Ala Val Lys His Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln; Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys (SEQ ID NO: 227) Val Pro Pro Ala Pro Leu Leu Asp Ser Asn Asn Leu Asn Ser Glu Asp Met Asp Ile Leu Met Glu Arg Asn Leu Arg Leu Pro Asn Leu Leu Ala Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln; and Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO: 228) Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln.
5. The hematopoietic protein as recited in claim 2 wherein the polypeptide of (IV) is selected from the from the group consisting of:
Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys (SEQ ID NO: 225) Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Ala Glu Asp Val Asp Ile Leu Met Glu Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln; Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys (SEQ ID NO: 226) Arg Pro Pro Asn Pro Leu Leu Asp Pro Asn Asn Leu Asn Ser Glu Asp Met Asp Ile Leu Met Glu Arg Asn Leu Arg Thr Pro Asn Leu Leu Ala Phe Val Arg Ala Val Lys His Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln; Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys (SEQ ID NO: 227) Val Pro Pro Ala Pro Leu Leu Asp Ser Asn Asn Leu Asn Ser Glu Asp Met Asp Ile Leu Met Glu Arg Asn Leu Arg Leu Pro Asn Leu Leu Ala Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln; and Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO: 228) Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln.
6. The hematopoietic protein as recited in claim 3 wherein the polypeptide of (IV) is selected from the from the group consisting of:
Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys (SEQ ID NO: 225) Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Ala Glu Asp Val Asp Ile Leu Met Glu Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln; Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys (SEQ ID NO: 226) Arg Pro Pro Asn Pro Leu Leu Asp Pro Asn Asn Leu Asn Ser Glu Asp Met Asp Ile Leu Met Glu Arg Asn Leu Arg Thr Pro Asn Leu Leu Ala Phe Val Arg Ala Val Lys His Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln; Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys (SEQ ID NO: 227) Val Pro Pro Ala Pro Leu Leu Asp Ser Asn Asn Leu Asn Ser Glu Asp Met Asp Ile Leu Met Glu Arg Asn Leu Arg Leu Pro Asn Leu Leu Ala Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln; and Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO: 228) Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln.
7. A hematopoietic protein comprising; an amino acid sequence of the formula:
R1-L1-R2, R2-L1-R1, R1-R2, or R2-R1
wherein R1 is a polypeptide comprising; a modified human G-CSF amino acid sequence of the formula:
1                                   10 Xaa Xaa Xaa Gly Pro Ala Ser Ser Leu Pro Gln Ser Xaa (SEQ ID NO: 1)                         20 Leu Leu Xaa Xaa Xaa Glu Gln Val Xaa Lys Xaa Gln Gly Xaa Gly     30                                      40 Ala Xaa Leu Gln Glu Xaa Leu Xaa Ala Thr Tyr Lys Leu Xaa Xaa                         50 Xaa Glu Xaa Xaa Val Xaa Xaa Gly His Ser Xaa Gly Ile Pro Trp     60                                      70 Ala Pro Leu Ser Ser Xaa Pro Ser Xaa Ala Leu Xaa Leu Ala Gly                         80 Xaa Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu     90                                      100 Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu                         110 Xaa Thr Leu Gln Xaa Asp Val Ala Asp Phe Ala Xaa Thr Ile Trp     120                                     130 Gln Gln Met Glu Xaa Xaa Gly Met Ala Pro Ala Leu Gln Pro Thr                         140 Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Xaa Gln Xaa Xaa Ala     150                                     160 Gly Gly Val Leu Val Ala Ser Xaa Leu Gln Xaa Phe Leu Xaa Xaa                         170 Ser Tyr Arg Val Leu Xaa Xaa Leu Ala Gln Pro
wherein
Xaa at position 1 is Thr, Ser, Arg, Tyr or Gly;
Xaa at position 2 is Pro or Leu;
Xaa at position 3 is Leu, Arg, Tyr or Ser;
Xaa at position 13 is Phe, Ser, His, Thr or Pro;
Xaa at position 16 is Lys, Pro, Ser, Thr or His;
Xaa at position 17 is Cys, Ser, Gly, Ala, Ile, Tyr or Arg;
Xaa at position 18 is Leu, Thr, Pro, His, Ile or Cys;
Xaa at position 22 is Arg, Tyr, Ser, Thr or Ala;
Xaa at position 24 is Ile, Pro, Tyr or Leu;
Xaa at position 27 is Asp, or Gly;
Xaa at position 30 is Ala, Ile, Leu or Gly;
Xaa at position 34 is Lys or Ser;
Xaa at position 36 is Cys or Ser;
Xaa at position 42 is Cys or Ser;
Xaa at position 43 is His, Thr, Gly, Val, Lys, Trp, Ala, Arg, Cys, or Leu;
Xaa at position 44 is Pro, Gly, Arg, Asp, Val, Ala, His, Trp, Gln, or Thr;
Xaa at position 46 is Glu, Arg, Phe, Arg, Ile or Ala;
Xaa at position 47 is Leu or Thr;
Xaa at position 49 is Leu, Phe, Arg or Ser;
Xaa at position 50 is Leu, Ile, His, Pro or Tyr;
Xaa at position 54 is Leu or His;
Xaa at position 64 is Cys or Ser;
Xaa at position 67 is Gln, Lys, Leu or Cys;
Xaa at position 70 is Gln, Pro, Leu, Arg or Ser;
Xaa at position 74 is Cys or Ser;
Xaa at position 104 is Asp, Gly or Val;
Xaa at position 108 is Leu, Ala, Val, Arg, Trp, Gln or Gly;
Xaa at position 115 is Thr, His, Leu or Ala;
Xaa at position 120 is Gln, Gly, Arg, Lys or His
Xaa at position 123 is Glu, Arg, Phe or Thr
Xaa at position 144 is Phe, His, Arg, Pro, Leu, Gln or Glu;
Xaa at position 146 is Arg or Gln;
Xaa at position 147 is Arg or Gln;
Xaa at position 156 is His, Gly or Ser;
Xaa at position 159 is Ser, Arg, Thr, Tyr, Val or Gly;
Xaa at position 162 is Glu, Leu, Gly or Trp;
Xaa at position 163 is Val, Gly, Arg or Ala;
Xaa at position 169 is Arg, Ser, Leu, Arg or Cys;
Xaa at position 170 is His, Arg or Ser,
wherein optionally 1-11 amino acids from the N-terminus and 1-5 from the C-terminus can be deleted from said modified human G-CSF amino acid sequence; and
wherein the N-terminus is joined to the C-terminus directly or through a linker capable of joining the N-terminus to the C-terminus and having new C- and N-termini at amino acids:
38-39 62-63 123-124 39-40 63-64 124-125 40-41 64-65 125-126 41-42 65-66 126-127 42-43 66-67 128-129 43-44 67-68 128-129 45-46 68-69 129-130 48-49 69-70 130-131 49-50 70-71 131-132 52-53 71-72 132-133 53-54 91-92 133-134 54-55 92-93 134-135 55-56 93-94 135-136 56-57 94-95 136-137 57-58 95-96 137-138 58-59 96-97 138-139 59-60 97-98 139-140 60-61 98-99 140-141 61-62  99-100 141-142
or 142-143 respectively,
wherein R2 is a polypeptide comprising; a modified human IL-3 amino acid sequence of the formula:
Ala Pro Met Thr Gln Thr Thr Ser Leu Lys Thr Ser Trp Val Asn (SEQ ID NO: 2) 1               5                   10                  15 Cys Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 20                  25                  30 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Asn Xaa Xaa Xaa Xaa Xaa Xaa                 35                  40                  45 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 50                  55                  60 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 65                  70                  75 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 80                  85                  90 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 95                  100                 105 Xaa Phe Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 110                 115                 120 Xaa Xaa Xaa Gln Gln Thr Thr Leu Ser Leu Ala Ile Phe                 125                 130
wherein Xaa at position 17 is Ser, Lys, Gly, Asp, Met, Gln, or Arg;
Xaa at position 18 is Asn, His, Leu, Ile, Phe, Arg, or Gln;
Xaa at position 19 is Met, Phe, Ile, Arg, Gly, Ala, or Cys;
Xaa at position 20 is Ile, Cys, Gln, Glu, Arg, Pro, or Ala;
Xaa at position 21 is Asp, Phe, Lys, Arg, Ala, Gly, Glu, Gln, Asn, Thr, Ser or Val;
Xaa at position 22 is Glu, Trp, Pro, Ser, Ala, His, Asp, Asn, Gln, Leu, Val or Gly;
Xaa at position 23 is Ile, Val, Ala, Gly, Trp, Lys, Phe, Leu, Ser, or Arg;
Xaa at position 24 is Ile, Gly, Val, Arg, Ser, Phe, or Leu;
Xaa at position 25 is Thr, His, Gly, Gln, Arg, Pro, or Ala;
Xaa at position 26 is His, Thr, Phe, Gly, Arg, Ala, or Trp;
Xaa at position 27 is Leu, Gly, Arg, Thr, Ser, or Ala;
Xaa at position 28 is Lys, Arg, Leu, Gln, Gly, Pro, Val or Trp;
Xaa at position 29 is Gln, Asn, Leu, Pro, Arg, or Val;
Xaa at position 30 is Pro, His, Thr, Gly, Asp, Gln, Ser, Leu, or Lys;
Xaa at position 31 is Pro, Asp, Gly, Ala, Arg, Leu, or Gln;
Xaa at position 32 is Leu, Val, Arg, Gln, Asn, Gly, Ala, or Glu;
Xaa at position 33 is Pro, Leu, Gln, Ala, Thr, or Glu;
Xaa at position 34 is Leu, Val, Gly, Ser, Lys, Glu, Gln, Thr, Arg, Ala, Phe, Ile or Met;
Xaa at position 35 is Leu, Ala, Gly, Asn, Pro, Gln, or Val;
Xaa at position 36 is Asp, Leu, or Val;
Xaa at position 37 is Phe, Ser, Pro, Trp, or Ile;
Xaa at position 38 is Asn, or Ala;
Xaa at position 40 is Leu, Trp, or Arg;
Xaa at position 41 is Asn, Cys, Arg, Leu, His, Met, or Pro;
Xaa at position 42 is Gly, Asp, Ser, Cys, Asn, Lys, Thr, Leu, Val, Glu, Phe, Tyr, Ile, Met or Ala;
Xaa at position 43 is Glu, Asn, Tyr, Leu, Phe, Asp, Ala, Cys, Gln, Arg, Thr, Gly or Ser;
Xaa at position 44 is Asp, Ser, Leu, Arg, Lys, Thr, Met, Trp, Glu, Asn, Gln, Ala or Pro;
Xaa at position 45 is Gln, Pro, Phe, Val, Met, Leu, Thr, Lys, Trp, Asp, Asn, Arg, Ser, Ala, Ile, Glu or His;
Xaa at position 46 is Asp, Phe, Ser, Thr, Cys, Glu, Asn, Gln, Lys, His, Ala, Tyr, Ile, Val or Gly;
Xaa at position 47 is Ile, Gly, Val, Ser, Arg, Pro, or His;
Xaa at position 48 is Leu, Ser, Cys, Arg, Ile, His, Phe, Glu, Lys, Thr, Ala, Met, Val or Asn;
Xaa at position 49 is Met, Arg, Ala, Gly, Pro, Asn, His, or Asp;
Xaa at position 50 is Glu, Leu, Thr, Asp, Tyr, Lys, Asn, Ser, Ala, Ile, Val, His, Phe, Met or Gln;
Xaa at position 51 is Asn, Arg, Met, Pro, Ser, Thr, or His;
Xaa at position 52 is Asn, His, Arg, Leu, Gly, Ser, or Thr;
Xaa at position 53 is Leu, Thr, Ala, Gly, Glu, Pro, Lys, Ser, or Met;
Xaa at position 54 is Arg, Asp, Ile, Ser, Val, Thr, Gln, Asn, Lys, His, Ala or Leu;
Xaa at position 55 is Arg, Thr, Val, Ser, Leu, or Gly;
Xaa at position 56 is Pro, Gly, Cys, Ser, Gln, Glu, Arg, His, Thr, Ala, Tyr, Phe, Leu, Val or Lys;
Xaa at position 57 is Asn or Gly;
Xaa at position 58 is Leu, Ser, Asp, Arg, Gln, Val, or Cys;
Xaa at position 59 is Glu Tyr, His, Leu, Pro, or Arg;
Xaa at position 60 is Ala, Ser, Pro, Tyr, Asn, or Thr;
Xaa at position 61 is Phe, Asn, Glu, Pro, Lys, Arg, or Ser;
Xaa at position 62 is Asn, His, Val, Arg, Pro, Thr, Asp, or Ile;
Xaa at position 63 is Arg, Tyr, Trp, Lys, Ser, His, Pro, or Val;
Xaa at position 64 is Ala, Asn, Pro, Ser, or Lys;
Xaa at position 65 is Val, Thr, Pro, His, Leu, Phe, or Ser;
Xaa at position 66 is Lys, Ile, Arg, Val, Asn, Glu, or Ser;
Xaa at position 67 is Ser, Ala, Phe, Val, Gly, Asn, Ile, Pro, or His;
Xaa at position 68 is Leu, Val, Trp, Ser, Ile, Phe, Thr, or His;
Xaa at position 69 is Gln, Ala, Pro, Thr, Glu, Arg, Trp, Gly, or Leu;
Xaa at position 70 is Asn, Leu, Val, Trp, Pro, or Ala;
Xaa at position 71 is Ala, Met, Leu, Pro, Arg, Glu, Thr, Gln, Trp, or Asn;
Xaa at position 72 is Ser, Glu, Met, Ala, His, Asn, Arg, or Asp;
Xaa at position 73 is Ala, Glu, Asp, Leu, Ser, Gly, Thr, or Arg;
Xaa at position 74 is Ile, Met, Thr, Pro, Arg, Gly, Ala;
Xaa at position 75 is Glu, Lys, Gly, Asp, Pro, Trp, Arg, Ser, Gln, or Leu;
Xaa at position 76 is Ser, Val, Ala, Asn, Trp, Glu, Pro, Gly, or Asp;
Xaa at position 77 is Ile, Ser, Arg, Thr, or Leu;
Xaa at position 78 is Leu, Ala, Ser, Glu, Phe, Gly, or Arg;
Xaa at position 79 is Lys, Thr, Asn, Met, Arg, Ile, Gly, or Asp;
Xaa at position 80 is Asn, Trp, Val, Gly, Thr, Leu, Glu, or Arg;
Xaa at position 81 is Leu, Gln, Gly, Ala, Trp, Arg, Val, or Lys;
Xaa at position 82 is Leu, Gln, Lys, Trp, Arg, Asp, Glu, Asn, His, Thr, Ser, Ala, Tyr, Phe, Ile, Met or Val;
Xaa at position 83 is Pro, Ala, Thr, Trp, Arg, or Met;
Xaa at position 84 is Cys, Glu, Gly, Arg, Met, or Val;
Xaa at position 85 is Leu, Asn, Val, or Gln;
Xaa at position 86 is Pro, Cys, Arg, Ala, or Lys;
Xaa at position 87 is Leu, Ser, Trp, or Gly;
Xaa at position 88 is Ala, Lys, Arg, Val, or Trp;
Xaa at position 89 is Thr, Asp, Cys, Leu, Val, Glu, His, Asn, or Ser;
Xaa at position 90 is Ala, Pro, Ser, Thr, Gly, Asp, Ile, or Met;
Xaa at position 91 is Ala, Pro, Ser, Thr, Phe, Leu, Asp, or His;
Xaa at position 92 is Pro, Phe, Arg, Ser, Lys, His, Ala, Gly, Ile or Leu;
Xaa at position 93 is Thr, Asp, Ser, Asn, Pro, Ala, Leu, or Arg;
Xaa at position 94 is Arg, Ile, Ser, Glu, Leu, Val, Gln, Lys, His, Ala, or Pro;
Xaa at position 95 is His, Gln, Pro, Arg, Val, Leu, Gly, Thr, Asn, Lys, Ser, Ala, Trp, Phe, Ile, or Tyr;
Xaa at position 96 is Pro, Lys, Tyr, Gly, Ile, or Thr;
Xaa at position 97 is Ile, Val, Lys, Ala, or Asn;
Xaa at position 98 is His, Ile, Asn, Leu, Asp, Ala, Thr, Glu, Gln, Ser, Phe, Met, Val, Lys, Arg, Tyr or Pro;
Xaa at position 99 is Ile, Leu, Arg, Asp, Val, Pro, Gln, Gly, Ser, Phe, or His;
Xaa at position 100 is Lys, Tyr, Leu, His, Arg, Ile, Ser, Gln, or Pro;
Xaa at position 101 is Asp, Pro, Met, Lys, His, Thr, Val, Tyr, Glu, Asn, Ser, Ala, Gly, Ile, Leu, or Gln;
Xaa at position 102 is Gly, Leu, Glu, Lys, Ser, Tyr, or Pro;
Xaa at position 103 is Asp, or Ser;
Xaa at position 104 is Trp, Val, Cys, Tyr, Thr, Met, Pro, Leu, Gln, Lys, Ala, Phe, or Gly;
Xaa at position 105 is Asn, Pro, Ala, Phe, Ser, Trp, Gln, Tyr, Leu, Lys, Ile, Asp, or His;
Xaa at position 106 is Glu, Ser, Ala, Lys, Thr, Ile, Gly, or Pro;
Xaa at position 108 is Arg, Lys, Asp, Leu, Thr, Ile, Gln, His, Ser, Ala or Pro;
Xaa at position 109 is Arg, Thr, Pro, Glu, Tyr, Leu, Ser, or Gly;
Xaa at position 110 is Lys, Ala, Asn, Thr, Leu, Arg, Gln, His, Glu, Ser, or Trp;
Xaa at position 111 is Leu, Ile, Arg, Asp, or Met;
Xaa at position 112 is Thr, Val, Gln, Tyr, Glu, His, Ser, or Phe;
Xaa at position 113 is Phe, Ser, Cys, His, Gly, Trp, Tyr, Asp, Lys, Leu, Ile, Val or Asn;
Xaa at position 114 is Tyr, Cys, His, Ser, Trp, Arg, or Leu;
Xaa at position 115 is Leu, Asn, Val, Pro, Arg, Ala, His, Thr, Trp, or Met;
Xaa at position 116 is Lys, Leu, Pro, Thr, Met, Asp, Val, Glu, Arg, Trp, Ser, Asn, His, Ala, Tyr, Phe, Gln, or Ile;
Xaa at position 117 is Thr, Ser, Asn, Ile, Trp, Lys, or Pro;
Xaa at position 118 is Leu, Ser, Pro, Ala, Glu, Cys, Asp, or Tyr;
Xaa at position 119 is Glu, Ser, Lys, Pro, Leu, Thr, Tyr, or Arg;
Xaa at position 120 is Asn, Ala, Pro, Leu, His, Val, or Gln;
Xaa at position 121 is Ala, Ser, Ile, Asn, Pro, Lys, Asp, or Gly;
Xaa at position 122 is Gln, Ser, Met, Trp, Arg, Phe, Pro, His, Ile, Tyr, or Cys;
Xaa at position 123 is Ala, Met, Glu, His, Ser, Pro, Tyr, or Leu,
wherein from 1 to 14 amino acids can optionally be deleted from the N-terminus and/or from 1 to 15 amino acids can optionally be deleted from the C-terminus of said modified human interleukin-3 amino acid sequence; and wherein from 0 to 44 of the amino acids designated by Xaa are different from the corresponding amino acids of native (1-133) human interleukin-3 and
wherein the N-terminus is joined to the C-terminus directly or through a linker (L2) capable of joining the N-terminus to the C-terminus and having new C- and N-termini at amino acids:
26-27 49-50 83-84 27-28 50-51 84-85 28-29 51-52 85-86 29-30 52-53 86-87 30-31 53-54 87-88 31-32 54-55 88-89 32-33 64-65 89-90 33-34 65-66 90-91 34-35 66-67 91-92 35-36 67-68 92-93 36-37 68-69 97-98 37-38 69-70 98-99 38-39 70-71  99-100 39-40 71-72 100-101 40-41 72-73 101-102 41-42 82-83 102-103 or 103-104 respectively;
wherein L1 is a linker capable of linking R1 to R2 and
said hematopoietic protein can optionally be immediately preceded by (methionine−1), (alanine−1) or (methionine−2, alanine−1).
8. A hematopoietic protein comprising; an amino acid sequence of the formula:
R1-L1-R2, R2-L1-R1, R1-R2, or R2-R1
wherein R1 is a polypeptide comprising; a modified human G-CSF amino acid sequence of the formula:
1                                   10 Xaa Xaa Xaa Gly Pro Ala Ser Ser Leu Pro Gln Ser Xaa (SEQ ID NO: 1)                         20 Leu Leu Xaa Xaa Xaa Glu Gln Val Xaa Lys Xaa Gln Gly Xaa Gly     30                                      40 Ala Xaa Leu Gln Glu Xaa Leu Xaa Ala Thr Tyr Lys Leu Xaa Xaa                         50 Xaa Glu Xaa Xaa Val Xaa Xaa Gly His Ser Xaa Gly Ile Pro Trp     60                                      70 Ala Pro Leu Ser Ser Xaa Pro Ser Xaa Ala Leu Xaa Leu Ala Gly                         80 Xaa Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu     90                                      100 Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu                         110 Xaa Thr Leu Gln Xaa Asp Val Ala Asp Phe Ala Xaa Thr Ile Trp     120                                     130 Gln Gln Met Glu Xaa Xaa Gly Met Ala Pro Ala Leu Gln Pro Thr                         140 Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Xaa Gln Xaa Xaa Ala     150                                     160 Gly Gly Val Leu Val Ala Ser Xaa Leu Gln Xaa Phe Leu Xaa Xaa                         170 Ser Tyr Arg Val Leu Xaa Xaa Leu Ala Gln Pro
wherein
Xaa at position 1 is Thr, Ser, Arg, Tyr or Gly;
Xaa at position 2 is Pro or Leu;
Xaa at position 3 is Leu, Arg, Tyr or Ser;
Xaa at position 13 is Phe, Ser, His, Thr or Pro;
Xaa at position 16 is Lys, Pro, Ser, Thr or His;
Xaa at position 17 is Cys, Ser, Gly, Ala, Ile, Tyr or Arg;
Xaa at position 18 is Leu, Thr, Pro, His, Ile or Cys;
Xaa at position 22 is Arg, Tyr, Ser, Thr or Ala;
Xaa at position 24 is Ile, Pro, Tyr or Leu;
Xaa at position 27 is Asp, or Gly;
Xaa at position 30 is Ala, Ile, Leu or Gly;
Xaa at position 34 is Lys or Ser;
Xaa at position 36 is Cys or Ser;
Xaa at position 42 is Cys or Ser;
Xaa at position 43 is His, Thr, Gly, Val, Lys, Trp, Ala, Arg, Cys, or Leu;
Xaa at position 44 is Pro, Gly, Arg, Asp, Val, Ala, His, Trp, Gln, or Thr;
Xaa at position 46 is Glu, Arg, Phe, Arg, Ile or Ala;
Xaa at position 47 is Leu or Thr;
Xaa at position 49 is Leu, Phe, Arg or Ser;
Xaa at position 50 is Leu, Ile, His, Pro or Tyr;
Xaa at position 54 is Leu or His;
Xaa at position 64 is Cys or Ser;
Xaa at position 67 is Gln, Lys, Leu or Cys;
Xaa at position 70 is Gln, Pro, Leu, Arg or Ser;
Xaa at position 74 is Cys or Ser;
Xaa at position 104 is Asp, Gly or Val;
Xaa at position 108 is Leu, Ala, Val, Arg, Trp, Gln or Gly;
Xaa at position 115 is Thr, His, Leu or Ala;
Xaa at position 120 is Gln, Gly, Arg, Lys or His
Xaa at position 123 is Glu, Arg, Phe or Thr
Xaa at position 144 is Phe, His, Arg, Pro, Leu, Gln or Glu;
Xaa at position 146 is Arg or Gln;
Xaa at position 147 is Arg or Gln;
Xaa at position 156 is His, Gly or Ser;
Xaa at position 159 is Ser, Arg, Thr, Tyr, Val or Gly;
Xaa at position 162 is Glu, Leu, Gly or Trp;
Xaa at position 163 is Val, Gly, Arg or Ala;
Xaa at position 169 is Arg, Ser, Leu, Arg or Cys;
Xaa at position 170 is His, Arg or Ser;
wherein optionally 1-11 amino acids from the N-terminus and 1-5 from the C-terminus can be deleted from said modified human G-CSF amino acid sequence and
wherein the N-terminus is joined to the C-terminus directly or through a linker capable of joining the N-terminus to the C-terminus and having new C- and N-termini at amino acids:
38-39 62-63 123-124 39-40 63-64 124-125 40-41 64-65 125-126 41-42 65-66 126-127 42-43 66-67 128-129 43-44 67-68 128-129 45-46 68-69 129-130 48-49 69-70 130-131 49-50 70-71 131-132 52-53 71-72 132-133 53-54 91-92 133-134 54-55 92-93 134-135 55-56 93-94 135-136 56-57 94-95 136-137 57-58 95-96 137-138 58-59 96-97 138-139 59-60 97-98 139-140 60-61 98-99 140-141 61-62  99-100 141-142 or 142-143 respectively;
R2 is a polypeptide comprising a modified human IL-3 amino acid sequence of the formula:
Ala Pro Met Thr Gln Thr Thr Ser Leu Lys Thr Ser Trp Val Asn (SEQ ID NO:2) 1               5                   10                  15 Cys Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 20                  25                  30 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Asn Xaa Xaa Xaa Xaa Xaa Xaa                 35                  40                  45 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 50                  55                  60 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 65                  70                  75 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 80                  85                  90 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 95                  100                 105 Xaa Phe Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 110                 115                 120 Xaa Xaa Xaa Gln Gln Thr Thr Leu Ser Leu Ala Ile Phe                 125                  130
wherein Xaa at position 17 is Ser, Lys, Gly, Asp, Met, Gln, or Arg;
Xaa at position 18 is Asn, His, Leu, Ile, Phe, Arg, or Gln;
Xaa at position 19 is Met, Phe, Ile, Arg, Gly, Ala, or Cys;
Xaa at position 20 is Ile, Cys, Gln, Glu, Arg, Pro, or Ala;
Xaa at position 21 is Asp, Phe, Lys, Arg, Ala, Gly, Glu, Gln, Asn, Thr, Ser or Val;
Xaa at position 22 is Glu, Trp, Pro, Ser, Ala, His, Asp, Asn, Gln, Leu, Val or Gly;
Xaa at position 23 is Ile, Val, Ala, Gly, Trp, Lys, Phe, Leu, Ser, or Arg;
Xaa at position 24 is Ile, Gly, Val, Arg, Ser, Phe, or Leu;
Xaa at position 25 is Thr, His, Gly, Gln, Arg, Pro, or Ala;
Xaa at position 26 is His, Thr, Phe, Gly, Arg, Ala, or Trp;
Xaa at position 27 is Leu, Gly, Arg, Thr, Ser, or Ala;
Xaa at position 28 is Lys, Arg, Leu, Gln, Gly, Pro, Val or Trp;
Xaa at position 29 is Gln, Asn, Leu, Pro, Arg, or Val;
Xaa at position 30 is Pro, His, Thr, Gly, Asp, Gln, Ser, Leu, or Lys;
Xaa at position 31 is Pro, Asp, Gly, Ala, Arg, Leu, or Gln;
Xaa at position 32 is Leu, Val, Arg, Gln, Asn, Gly, Ala, or Glu;
Xaa at position 33 is Pro, Leu, Gln, Ala, Thr, or Glu;
Xaa at position 34 is Leu, Val, Gly, Ser, Lys, Glu, Gln, Thr, Arg, Ala, Phe, Ile or Met;
Xaa at position 35 is Leu, Ala, Gly, Asn, Pro, Gln, or Val;
Xaa at position 36 is Asp, Leu, or Val;
Xaa at position 37 is Phe, Ser, Pro, Trp, or Ile;
Xaa at position 38 is Asn, or Ala;
Xaa at position 40 is Leu, Trp, or Arg;
Xaa at position 41 is Asn, Cys, Arg, Leu, His, Met, or Pro;
Xaa at position 42 is Gly, Asp, Ser, Cys, Asn, Lys, Thr, Leu, Val, Glu, Phe, Tyr, Ile, Met or Ala;
Xaa at position 43 is Glu, Asn, Tyr, Leu, Phe, Asp, Ala, Cys, Gln, Arg, Thr, Gly or Ser;
Xaa at position 44 is Asp, Ser, Leu, Arg, Lys, Thr, Met, Trp, Glu, Asn, Gln, Ala or Pro;
Xaa at position 45 is Gln, Pro, Phe, Val, Met, Leu, Thr, Lys, Trp, Asp, Asn, Arg, Ser, Ala, Ile, Glu or His;
Xaa at position 46 is Asp, Phe, Ser, Thr, Cys, Glu, Asn, Gln, Lys, His, Ala, Tyr, Ile, Val or Gly;
Xaa at position 47 is Ile, Gly, Val, Ser, Arg, Pro, or His;
Xaa at position 48 is Leu, Ser, Cys, Arg, Ile, His, Phe, Glu, Lys, Thr, Ala, Met, Val or Asn;
Xaa at position 49 is Met, Arg, Ala, Gly, Pro, Asn, His, or Asp;
Xaa at position 50 is Glu, Leu, Thr, Asp, Tyr, Lys, Asn, Ser, Ala, Ile, Val, His, Phe, Met or Gln;
Xaa at position 51 is Asn, Arg, Met, Pro, Ser, Thr, or His;
Xaa at position 52 is Asn, His, Arg, Leu, Gly, Ser, or Thr;
Xaa at position 53 is Leu, Thr, Ala, Gly, Glu, Pro, Lys, Ser, or Met;
Xaa at position 54 is Arg, Asp, Ile, Ser, Val, Thr, Gln, Asn, Lys, His, Ala or Leu;
Xaa at position 55 is Arg, Thr, Val, Ser, Leu, or Gly;
Xaa at position 56 is Pro, Gly, Cys, Ser, Gln, Glu, Arg, His, Thr, Ala, Tyr, Phe, Leu, Val or Lys;
Xaa at position 57 is Asn or Gly;
Xaa at position 58 is Leu, Ser, Asp, Arg, Gln, Val, or Cys;
Xaa at position 59 is Glu Tyr, His, Leu, Pro, or Arg;
Xaa at position 60 is Ala, Ser, Pro, Tyr, Asn, or Thr;
Xaa at position 61 is Phe, Asn, Glu, Pro, Lys, Arg, or Ser;
Xaa at position 62 is Asn, His, Val, Arg, Pro, Thr, Asp, or Ile;
Xaa at position 63 is Arg, Tyr, Trp, Lys, Ser, His, Pro, or Val;
Xaa at position 64 is Ala, Asn, Pro, Ser, or Lys;
Xaa at position 65 is Val, Thr, Pro, His, Leu, Phe, or Ser;
Xaa at position 66 is Lys, Ile, Arg, Val, Asn, Glu, or Ser;
Xaa at position 67 is Ser, Ala, Phe, Val, Gly, Asn, Ile, Pro, or His;
Xaa at position 68 is Leu, Val, Trp, Ser, Ile, Phe, Thr, or His;
Xaa at position 69 is Gln, Ala, Pro, Thr, Glu, Arg, Trp, Gly, or Leu;
Xaa at position 70 is Asn, Leu, Val, Trp, Pro, or Ala;
Xaa at position 71 is Ala, Met, Leu, Pro, Arg, Glu, Thr, Gln, Trp, or Asn;
Xaa at position 72 is Ser, Glu, Met, Ala, His, Asn, Arg, or Asp;
Xaa at position 73 is Ala, Glu, Asp, Leu, Ser, Gly, Thr, or Arg;
Xaa at position 74 is Ile, Met, Thr, Pro, Arg, Gly, Ala;
Xaa at position 75 is Glu, Lys, Gly, Asp, Pro, Trp, Arg, Ser, Gln, or Leu;
Xaa at position 76 is Ser, Val, Ala, Asn, Trp, Glu, Pro, Gly, or Asp;
Xaa at position 77 is Ile, Ser, Arg, Thr, or Leu;
Xaa at position 78 is Leu, Ala, Ser, Glu, Phe, Gly, or Arg;
Xaa at position 79 is Lys, Thr, Asn, Met, Arg, Ile, Gly, or Asp;
Xaa at position 80 is Asn, Trp, Val, Gly, Thr, Leu, Glu, or Arg;
Xaa at position 81 is Leu, Gln, Gly, Ala, Trp, Arg, Val, or Lys;
Xaa at position 82 is Leu, Gln, Lys, Trp, Arg, Asp, Glu, Asn, His, Thr, Ser, Ala, Tyr, Phe, Ile, Met or Val;
Xaa at position 83 is Pro, Ala, Thr, Trp, Arg, or Met;
Xaa at position 84 is Cys, Glu, Gly, Arg, Met, or Val;
Xaa at position 85 is Leu, Asn, Val, or Gln;
Xaa at position 86 is Pro, Cys, Arg, Ala, or Lys;
Xaa at position 87 is Leu, Ser, Trp, or Gly;
Xaa at position 88 is Ala, Lys, Arg, Val, or Trp;
Xaa at position 89 is Thr, Asp, Cys, Leu, Val, Glu, His, Asn, or Ser;
Xaa at position 90 is Ala, Pro, Ser, Thr, Gly, Asp, Ile, or Met;
Xaa at position 91 is Ala, Pro, Ser, Thr, Phe, Leu, Asp, or His;
Xaa at position 92 is Pro, Phe, Arg, Ser, Lys, His, Ala, Gly, Ile or Leu;
Xaa at position 93 is Thr, Asp, Ser, Asn, Pro, Ala, Leu, or Arg;
Xaa at position 94 is Arg, Ile, Ser, Glu, Leu, Val, Gln, Lys, His, Ala, or Pro;
Xaa at position 95 is His, Gln, Pro, Arg, Val, Leu, Gly, Thr, Asn, Lys, Ser, Ala, Trp, Phe, Ile, or Tyr;
Xaa at position 96 is Pro, Lys, Tyr, Gly, Ile, or Thr;
Xaa at position 97 is Ile, Val, Lys, Ala, or Asn;
Xaa at position 98 is His, Ile, Asn, Leu, Asp, Ala, Thr, Glu, Gln, Ser, Phe, Met, Val, Lys, Arg, Tyr or Pro;
Xaa at position 99 is Ile, Leu, Arg, Asp, Val, Pro, Gln, Gly, Ser, Phe, or His;
Xaa at position 100 is Lys, Tyr, Leu, His, Arg, Ile, Ser, Gln, or Pro;
Xaa at position 101 is Asp, Pro, Met, Lys, His, Thr, Val, Tyr, Glu, Asn, Ser, Ala, Gly, Ile, Leu, or Gln;
Xaa at position 102 is Gly, Leu, Glu, Lys, Ser, Tyr, or Pro;
Xaa at position 103 is Asp, or Ser;
Xaa at position 104 is Trp, Val, Cys, Tyr, Thr, Met, Pro, Leu, Gln, Lys, Ala, Phe, or Gly;
Xaa at position 105 is Asn, Pro, Ala, Phe, Ser, Trp, Gln, Tyr, Leu, Lys, Ile, Asp, or His;
Xaa at position 106 is Glu, Ser, Ala, Lys, Thr, Ile, Gly, or Pro;
Xaa at position 108 is Arg, Lys, Asp, Leu, Thr, Ile, Gln, His, Ser, Ala or Pro;
Xaa at position 109 is Arg, Thr, Pro, Glu, Tyr, Leu, Ser, or Gly;
Xaa at position 110 is Lys, Ala, Asn, Thr, Leu, Arg, Gln, His, Glu, Ser, or Trp;
Xaa at position 111 is Leu, Ile, Arg, Asp, or Met;
Xaa at position 112 is Thr, Val, Gln, Tyr, Glu, His, Ser, or Phe;
Xaa at position 113 is Phe, Ser, Cys, His, Gly, Trp, Tyr, Asp, Lys, Leu, Ile, Val or Asn;
Xaa at position 114 is Tyr, Cys, His, Ser, Trp, Arg, or Leu;
Xaa at position 115 is Leu, Asn, Val, Pro, Arg, Ala, His, Thr, Trp, or Met;
Xaa at position 116 is Lys, Leu, Pro, Thr, Met, Asp, Val, Glu, Arg, Trp, Ser, Asn, His, Ala, Tyr, Phe, Gln, or Ile;
Xaa at position 117 is Thr, Ser, Asn, Ile, Trp, Lys, or Pro;
Xaa at position 118 is Leu, Ser, Pro, Ala, Glu, Cys, Asp, or Tyr;
Xaa at position 119 is Glu, Ser, Lys, Pro, Leu, Thr, Tyr, or Arg;
Xaa at position 120 is Asn, Ala, Pro, Leu, His, Val, or Gln;
Xaa at position 121 is Ala, Ser, Ile, Asn, Pro, Lys, Asp, or Gly;
Xaa at position 122 is Gln, Ser, Met, Trp, Arg, Phe, Pro, His, Ile, Tyr, or Cys;
Xaa at position 123 is Ala, Met, Glu, His, Ser, Pro, Tyr, or Leu,
wherein from 1 to 14 amino acids can optionally be deleted from the N-terminus and/or from 1 to 15 amino acids can optionally be deleted from the C-terminus; and wherein from 1 to 44 of the amino acids designated by Xaa are different from the corresponding amino acids of native (1-133) human interleukin-3 and
L1 is a linker capable of linking R1 to R2 and
additionally said hematopoietic protein can be immediately preceded by (methionine−1), (alanine−1) or (methionine−2, alanine−1).
9. A hematopoietic protein comprising an amino acid sequence of the formula:
R1-L1-R2, R2-L1-R1, R1-R2, or R2-R1
wherein R1 is a polypeptide comprising; a modified human G-CSF amino acid sequence of the formula:
1                                   10 (SEQ ID NO:1) Xaa Xaa Xaa Gly Pro Ala Ser Ser Leu Pro Gln Ser Xaa                         20 Leu Leu Xaa Xaa Xaa Glu Gln Val Xaa Lys Xaa Gln Gly Xaa Gly     30                                      40 Ala Xaa Leu Gln Glu Xaa Leu Xaa Ala Thr Tyr Lys Leu Xaa Xaa                         50 Xaa Glu Xaa Xaa Val Xaa Xaa Gly His Ser Xaa Gly Ile Pro Trp     60                                      70 Ala Pro Leu Ser Ser Xaa Pro Ser Xaa Ala Leu Xaa Leu Ala Gly                         80 Xaa Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu     90                                      100 Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu                         110 Xaa Thr Leu Gln Xaa Asp Val Ala Asp Phe Ala Xaa Thr Ile Trp     120                                     130 Gln Gln Met Glu Xaa Xaa Gly Met Ala Pro Ala Leu Gln Pro Thr                         140 Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Xaa Gln Xaa Xaa Ala     150                                     160 Gly Gly Val Leu Val Ala Ser Xaa Leu Gln Xaa Phe Leu Xaa Xaa                         170 Ser Tyr Arg Val Leu Xaa Xaa Leu Ala Gln Pro
wherein
Xaa at position 1 is Thr, Ser, Arg, Tyr or Gly;
Xaa at position 2 is Pro or Leu;
Xaa at position 3 is Leu, Arg, Tyr or Ser;
Xaa at position 13 is Phe, Ser, His, Thr or Pro;
Xaa at position 16 is Lys, Pro, Ser, Thr or His;
Xaa at position 17 is Cys, Ser, Gly, Ala, Ile, Tyr or Arg;
Xaa at position 18 is Leu, Thr, Pro, His, Ile or Cys;
Xaa at position 22 is Arg, Tyr, Ser, Thr or Ala;
Xaa at position 24 is Ile, Pro, Tyr or Leu;
Xaa at position 27 is Asp, or Gly;
Xaa at position 30 is Ala, Ile, Leu or Gly;
Xaa at position 34 is Lys or Ser;
Xaa at position 36 is Cys or Ser;
Xaa at position 42 is Cys or Ser;
Xaa at position 43 is His, Thr, Gly, Val, Lys, Trp, Ala, Arg, Cys, or Leu;
Xaa at position 44 is Pro, Gly, Arg, Asp, Val, Ala, His, Trp, Gln, or Thr;
Xaa at position 46 is Glu, Arg, Phe, Arg, Ile or Ala;
Xaa at position 47 is Leu or Thr;
Xaa at position 49 is Leu, Phe, Arg or Ser;
Xaa at position 50 is Leu, Ile, His, Pro or Tyr;
Xaa at position 54 is Leu or His;
Xaa at position 64 is Cys or Ser;
Xaa at position 67 is Gln, Lys, Leu or Cys;
Xaa at position 70 is Gln, Pro, Leu, Arg or Ser;
Xaa at position 74 is Cys or Ser;
Xaa at position 104 is Asp, Gly or Val;
Xaa at position 108 is Leu, Ala, Val, Arg, Trp, Gln or Gly;
Xaa at position 115 is Thr, His, Leu or Ala;
Xaa at position 120 is Gln, Gly, Arg, Lys or His
Xaa at position 123 is Glu, Arg, Phe or Thr
Xaa at position 144 is Phe, His, Arg, Pro, Leu, Gln or Glu;
Xaa at position 146 is Arg or Gln;
Xaa at position 147 is Arg or Gln;
Xaa at position 156 is His, Gly or Ser;
Xaa at position 159 is Ser, Arg, Thr, Tyr, Val or Gly;
Xaa at position 162 is Glu, Leu, Gly or Trp;
Xaa at position 163 is Val, Gly, Arg or Ala;
Xaa at position 169 is Arg, Ser, Leu, Arg or Cys;
Xaa at position 170 is His, Arg or Ser,
wherein optionally 1-11 amino acids from the N-terminus and 1-5 from the C-terminus can be deleted from said modified human G-CSF amino acid sequence and
wherein the N-terminus is joined to the C-terminus directly or through a linker capable of joining the N-terminus to the C-terminus and having new C- and N-termini at amino acids:
38-39 62-63 123-124 39-40 63-64 124-125 40-41 64-65 125-126 41-42 65-66 126-127 42-43 66-67 128-129 43-44 67-68 128-129 45-46 68-69 129-130 48-49 69-70 130-131 49-50 70-71 131-132 52-53 71-72 132-133 53-54 91-92 133-134 54-55 92-93 134-135 55-56 93-94 135-136 56-57 94-95 136-137 57-58 95-96 137-138 58-59 96-97 138-139 59-60 97-98 139-140 60-61 98-99 140-141 61-62  99-100 141-142 or 142-143 respectively;
R2 is a polypeptide comprising a modified human c-mpl ligand amino acid sequence of the formula:
SerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeuArgAspSer (SEQ ID NO:256) 1           5              10             15 HisValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuProThrPro 20             25             30             35 ValLeuLeuProAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGluGlu    40             45             50             55 ThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAla       60             65             70             75 AlaArgGlyGlnLeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGly          80             85             90             95 GlnValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnXaaXaaXaa             100            105            110 XaaGlyArgThrThrAlaHisLysAspProAsnAlaIlePheLeuSerPheGlnHis 115            120            125            130 LeuLeuArgGlyLysValArgPheLeuMetLeuValGlyGlySerThrLeuCysVal    135            140            145            150 Arg
wherein
Xaa at position 112 is deleted or Leu, Ala, Val, Ile, Pro, Phe, Trp, or Met;
Xaa at position 113 is deleted or Pro, Phe, Ala, Val, Leu, Ile, Trp, or Met;
Xaa at position 114 is deleted or Pro, Phe, Ala, Val, Leu, Ile, Trp, or Met;
Xaa at position 115 is deleted or Gln, Gly, Ser, Thr, Tyr, or Asn, and
wherein the N-terminus is joined to the C-terminus directly or through a linker (L2) capable of joining the N-terminus to the C-terminus and having new C- and N-termini at amino acids:
26-27 51-52 108-109 27-28 52-53 109-110 28-29 53-54 110-111 29-30 54-55 111-112 30-31 55-56 112-113 32-33 56-57 113-114 33-34 57-58 114-115 34-35 58-59 115-116 36-37 59-60 116-117 37-38 78-79 117-118 38-39 79-80 118-119 40-41 80-81 119-120 41-42 81-82 120-121 42-43 82-83 121-122 43-44 83-84 122-123 44-45 84-85 123-124 46-47 85-86 124-125 47-48 86-87 125-126 48-49 87-88 126-127 50-51 88-89 or  127-128;
wherein L1 is a linker capable of linking R1 to R2 and
additionally said hematopoietic protein can be immediately preceded by (methionine−1), (alanine−1) or (methionine−2, alanine−1).
10. A hematopoietic protein comprising; an amino acid sequence of the formula:
R1—L1—R2, R2—L1—R1, R1—R2, or R2—R1
wherein R1 is a polypeptide comprising a modified human c-mpl ligand amino acid sequence of the formula:
SerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeuArgAspSer (SEQ ID NO:256) 1           5              10             15 HisValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuProThrPro 20             25             30             35 ValLeuLeuProAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGluGlu    40             45             50             55 ThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAla       60             65             70             75 AlaArgGlyGlnLeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGly          80             85             90             95 GlnValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnXaaXaaXaa             100            105            110 XaaGlyArgThrThrAlaHisLysAspProAsnAlaIlePheLeuSerPheGlnHis 115            120            125            130 LeuLeuArgGlyLysValArgPheLeuMetLeuValGlyGlySerThrLeuCysVal    135            140            145            150 Arg 153
wherein
Xaa at position 112 is deleted or Leu, Ala, Val, Ile, Pro, Phe, Trp, or Met;
Xaa at position 113 is deleted or Pro, Phe, Ala, Val, Leu, Ile, Trp, or Met;
Xaa at position 114 is deleted or Pro, Phe, Ala, Val, Leu, Ile, Trp, or Met;
Xaa at position 115 is deleted or Gln, Gly, Ser, Thr, Tyr, or Asn, and
wherein the N-terminus is joined to the C-terminus directly or through a linker (L2) capable of joining the N-terminus to the C-terminus and having new C- and N-termini at amino acids:
26-27 27-28 28-29 29-30 30-31 32-33 33-34 34-35 36-37 37-38 38-39 40-41 41-42 42-43 43-44 44-45 46-47 47-48 48-49 50-51 51-52 52-53 53-54 54-55 55-56 56-57 57-58 58-59 59-60 78-79 79-80 80-81 81-82 82-83 83-84 84-85 85-86 86-87 87-88 88-89 108-109 109-110 110-111 111-112 112-113 113-114 114-115 115-116 116-117 117-118 118-119 119-120 120-121 121-122 122-123 123-124 124-125 125-126 126-127 or 127-128;
wherein R2 is a polypeptide comprising a modified human IL-3 amino acid sequence of the formula:
Ala Pro Met Thr Gln Thr Thr Ser Leu Lys Thr Ser Trp Val Asn (SEQ ID NO:2) 1               5                   10                  15 Cys Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 20                  25                  30 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Asn Xaa Xaa Xaa Xaa Xaa Xaa                 35                  40                  45 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 50                  55                  60 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 65                  70                  75 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 80                  85                  90 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 95                  100                 105 Xaa Phe Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa                 110                 115                 120 Xaa Xaa Xaa Gln Gln Thr Thr Leu Ser Leu Ala Ile Phe                 125                 130
wherein Xaa at position 17 is Ser, Lys, Gly, Asp, Met, Gln, or Arg;
Xaa at position 18 is Asn, His, Leu, Ile, Phe, Arg, or Gln;
Xaa at position 19 is Met, Phe, Ile, Arg, Gly, Ala, or Cys;
Xaa at position 20 is Ile, Cys, Gln, Glu, Arg, Pro, or Ala;
Xaa at position 21 is Asp, Phe, Lys, Arg, Ala, Gly, Glu, Gln, Asn, Thr, Ser or Val;
Xaa at position 22 is Glu, Trp, Pro, Ser, Ala, His, Asp, Asn, Gln, Leu, Val or Gly;
Xaa at position 23 is Ile, Val, Ala, Gly, Trp, Lys, Phe, Leu, Ser, or Arg;
Xaa at position 24 is Ile, Gly, Val, Arg, Ser, Phe, or Leu;
Xaa at position 25 is Thr, His, Gly, Gln, Arg, Pro, or Ala;
Xaa at position 26 is His, Thr, Phe, Gly, Arg, Ala, or Trp;
Xaa at position 27 is Leu, Gly, Arg, Thr, Ser, or Ala;
Xaa at position 28 is Lys, Arg, Leu, Gln, Gly, Pro, Val or Trp;
Xaa at position 29 is Gln, Asn, Leu, Pro, Arg, or Val;
Xaa at position 30 is Pro, His, Thr, Gly, Asp, Gln, Ser, Leu, or Lys;
Xaa at position 31 is Pro, Asp, Gly, Ala, Arg, Leu, or Gln;
Xaa at position 32 is Leu, Val, Arg, Gln, Asn, Gly, Ala, or Glu;
Xaa at position 33 is Pro, Leu, Gln, Ala, Thr, or Glu;
Xaa at position 34 is Leu, Val, Gly, Ser, Lys, Glu, Gln, Thr, Arg, Ala, Phe, Ile or Met;
Xaa at position 35 is Leu, Ala, Gly, Asn, Pro, Gln, or Val;
Xaa at position 36 is Asp, Leu, or Val;
Xaa at position 37 is Phe, Ser, Pro, Trp, or Ile;
Xaa at position 38 is Asn, or Ala;
Xaa at position 40 is Leu, Trp, or Arg;
Xaa at position 41 is Asn, Cys, Arg, Leu, His, Met, or Pro;
Xaa at position 42 is Gly, Asp, Ser, Cys, Asn, Lys, Thr, Leu, Val, Glu, Phe, Tyr, Ile, Met or Ala;
Xaa at position 43 is Glu, Asn, Tyr, Leu, Phe, Asp, Ala, Cys, Gln, Arg, Thr, Gly or Ser;
Xaa at position 44 is Asp, Ser, Leu, Arg, Lys, Thr, Met, Trp, Glu, Asn, Gln, Ala or Pro;
Xaa at position 45 is Gln, Pro, Phe, Val, Met, Leu, Thr, Lys, Trp, Asp, Asn, Arg, Ser, Ala, Ile, Glu or His;
Xaa at position 46 is Asp, Phe, Ser, Thr, Cys, Glu, Asn, Gln, Lys, His, Ala, Tyr, Ile, Val or Gly;
Xaa at position 47 is Ile, Gly, Val, Ser, Arg, Pro, or His;
Xaa at position 48 is Leu, Ser, Cys, Arg, Ile, His, Phe, Glu, Lys, Thr, Ala, Met, Val or Asn;
Xaa at position 49 is Met, Arg, Ala, Gly, Pro, Asn, His, or Asp;
Xaa at position 50 is Glu, Leu, Thr, Asp, Tyr, Lys, Asn, Ser, Ala, Ile, Val, His, Phe, Met or Gln;
Xaa at position 51 is Asn, Arg, Met, Pro, Ser, Thr, or His;
Xaa at position 52 is Asn, His, Arg, Leu, Gly, Ser, or Thr;
Xaa at position 53 is Leu, Thr, Ala, Gly, Glu, Pro, Lys, Ser, or Met;
Xaa at position 54 is Arg, Asp, Ile, Ser, Val, Thr, Gln, Asn, Lys, His, Ala or Leu;
Xaa at position 55 is Arg, Thr, Val, Ser, Leu, or Gly;
Xaa at position 56 is Pro, Gly, Cys, Ser, Gln, Glu, Arg, His, Thr, Ala, Tyr, Phe, Leu, Val or Lys;
Xaa at position 57 is Asn or Gly;
Xaa at position 58 is Leu, Ser, Asp, Arg, Gln, Val, or Cys;
Xaa at position 59 is Glu Tyr, His, Leu, Pro, or Arg;
Xaa at position 60 is Ala, Ser, Pro, Tyr, Asn, or Thr;
Xaa at position 61 is Phe, Asn, Glu, Pro, Lys, Arg, or Ser;
Xaa at position 62 is Asn, His, Val, Arg, Pro, Thr, Asp, or Ile;
Xaa at position 63 is Arg, Tyr, Trp, Lys, Ser, His, Pro, or Val;
Xaa at position 64 is Ala, Asn, Pro, Ser, or Lys;
Xaa at position 65 is Val, Thr, Pro, His, Leu, Phe, or Ser;
Xaa at position 66 is Lys, Ile, Arg, Val, Asn, Glu, or Ser;
Xaa at position 67 is Ser, Ala, Phe, Val, Gly, Asn, Ile, Pro, or His;
Xaa at position 68 is Leu, Val, Trp, Ser, Ile, Phe, Thr, or His;
Xaa at position 69 is Gln, Ala, Pro, Thr, Glu, Arg, Trp, Gly, or Leu;
Xaa at position 70 is Asn, Leu, Val, Trp, Pro, or Ala;
Xaa at position 71 is Ala, Met, Leu, Pro, Arg, Glu, Thr, Gln, Trp, or Asn;
Xaa at position 72 is Ser, Glu, Met, Ala, His, Asn, Arg, or Asp;
Xaa at position 73 is Ala, Glu, Asp, Leu, Ser, Gly, Thr, or Arg;
Xaa at position 74 is Ile, Met, Thr, Pro, Arg, Gly, Ala;
Xaa at position 75 is Glu, Lys, Gly, Asp, Pro, Trp, Arg, Ser, Gln, or Leu;
Xaa at position 76 is Ser, Val, Ala, Asn, Trp, Glu, Pro, Gly, or Asp;
Xaa at position 77 is Ile, Ser, Arg, Thr, or Leu;
Xaa at position 78 is Leu, Ala, Ser, Glu, Phe, Gly, or Arg;
Xaa at position 79 is Lys, Thr, Asn, Met, Arg, Ile, Gly, or Asp;
Xaa at position 80 is Asn, Trp, Val, Gly, Thr, Leu, Glu, or Arg;
Xaa at position 81 is Leu, Gln, Gly, Ala, Trp, Arg, Val, or Lys;
Xaa at position 82 is Leu, Gln, Lys, Trp, Arg, Asp, Glu, Asn, His, Thr, Ser, Ala, Tyr, Phe, Ile, Met or Val;
Xaa at position 83 is Pro, Ala, Thr, Trp, Arg, or Met;
Xaa at position 84 is Cys, Glu, Gly, Arg, Met, or Val;
Xaa at position 85 is Leu, Asn, Val, or Gln;
Xaa at position 86 is Pro, Cys, Arg, Ala, or Lys;
Xaa at position 87 is Leu, Ser, Trp, or Gly;
Xaa at position 88 is Ala, Lys, Arg, Val, or Trp;
Xaa at position 89 is Thr, Asp, Cys, Leu, Val, Glu, His, Asn, or Ser;
Xaa at position 90 is Ala, Pro, Ser, Thr, Gly, Asp, Ile, or Met;
Xaa at position 91 is Ala, Pro, Ser, Thr, Phe, Leu, Asp, or His;
Xaa at position 92 is Pro, Phe, Arg, Ser, Lys, His, Ala, Gly, Ile or Leu;
Xaa at position 93 is Thr, Asp, Ser, Asn, Pro, Ala, Leu, or Arg;
Xaa at position 94 is Arg, Ile, Ser, Glu, Leu, Val, Gln, Lys, His, Ala, or Pro;
Xaa at position 95 is His, Gln, Pro, Arg, Val, Leu, Gly, Thr, Asn, Lys, Ser, Ala, Trp, Phe, Ile, or Tyr;
Xaa at position 96 is Pro, Lys, Tyr, Gly, Ile, or Thr;
Xaa at position 97 is Ile, Val, Lys, Ala, or Asn;
Xaa at position 98 is His, Ile, Asn, Leu, Asp, Ala, Thr, Glu, Gln, Ser, Phe, Met, Val, Lys, Arg, Tyr or Pro;
Xaa at position 99 is Ile, Leu, Arg, Asp, Val, Pro, Gln, Gly, Ser, Phe, or His;
Xaa at position 100 is Lys, Tyr, Leu, His, Arg, Ile, Ser, Gln, or Pro;
Xaa at position 101 is Asp, Pro, Met, Lys, His, Thr, Val, Tyr, Glu, Asn, Ser, Ala, Gly, Ile, Leu, or Gln;
Xaa at position 102 is Gly, Leu, Glu, Lys, Ser, Tyr, or Pro;
Xaa at position 103 is Asp, or Ser;
Xaa at position 104 is Trp, Val, Cys, Tyr, Thr, Met, Pro, Leu, Gln, Lys, Ala, Phe, or Gly;
Xaa at position 105 is Asn, Pro, Ala, Phe, Ser, Trp, Gln, Tyr, Leu, Lys, Ile, Asp, or His;
Xaa at position 106 is Glu, Ser, Ala, Lys, Thr, Ile, Gly, or Pro;
Xaa at position 108 is Arg, Lys, Asp, Leu, Thr, Ile, Gln, His, Ser, Ala or Pro;
Xaa at position 109 is Arg, Thr, Pro, Glu, Tyr, Leu, Ser, or Gly;
Xaa at position 110 is Lys, Ala, Asn, Thr, Leu, Arg, Gln, His, Glu, Ser, or Trp;
Xaa at position 111 is Leu, Ile, Arg, Asp, or Met;
Xaa at position 112 is Thr, Val, Gln, Tyr, Glu, His, Ser, or Phe;
Xaa at position 113 is Phe, Ser, Cys, His, Gly, Trp, Tyr, Asp, Lys, Leu, Ile, Val or Asn;
Xaa at position 114 is Tyr, Cys, His, Ser, Trp, Arg, or Leu;
Xaa at position 115 is Leu, Asn, Val, Pro, Arg, Ala, His, Thr, Trp, or Met;
Xaa at position 116 is Lys, Leu, Pro, Thr, Met, Asp, Val, Glu, Arg, Trp, Ser, Asn, His, Ala, Tyr, Phe, Gln, or Ile;
Xaa at position 117 is Thr, Ser, Asn, Ile, Trp, Lys, or Pro;
Xaa at position 118 is Leu, Ser, Pro, Ala, Glu, Cys, Asp, or Tyr;
Xaa at position 119 is Glu, Ser, Lys, Pro, Leu, Thr, Tyr, or Arg;
Xaa at position 120 is Asn, Ala, Pro, Leu, His, Val, or Gln;
Xaa at position 121 is Ala, Ser, Ile, Asn, Pro, Lys, Asp, or Gly;
Xaa at position 122 is Gln, Ser, Met, Trp, Arg, Phe, Pro, His, Ile, Tyr, or Cys;
Xaa at position 123 is Ala, Met, Glu, His, Ser, Pro, Tyr, or Leu,
wherein from 1 to 14 amino acids can optionally be deleted from the N-terminus and/or from 1 to 15 amino acids can optionally be deleted from the C-terminus of said modified human interleukin-3 amino acid sequence; and wherein from 1 to 44 of the amino acids designated by Xaa are different from the corresponding amino acids of native (1-133) human interleukin-3;
wherein L1 is a linker capable of linking R1 to R2; and
said hematopoietic protein can optionally be immediately preceded by (methionine−1), (alanine−1) or (methionine−2, alanine−1).
11. The hematopoeitic protein of claim 8 or 10 wherein R2 is selected from the group consisting of:
Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys (SEQ ID NO:225) Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Ala Glu Asp Val Asp Ile Leu Met Glu Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln; Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys (SEQ ID NO:226) Arg Pro Pro Asn Pro Leu Leu Asp Pro Asn Asn Leu Asn Ser Glu Asp Met Asp Ile Leu Met Glu Arg Asn Leu Arg Thr Pro Asn Leu Leu Ala Phe Val Arg Ala Val Lys His Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln; Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys (SEQ ID NO:227) Val Pro Pro Ala Pro Leu Leu Asp Ser Asn Asn Leu Asn Ser Glu Asp Met Asp Ile Leu Met Glu Arg Asn Leu Arg Leu Pro Asn Leu Leu Ala Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln; and Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:228) Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln.
12. A hematopoietic protein comprising; an amino acid sequence of the formula:
R1-L1-R2, R2-L1-R1, R1-R2, or R2-R1
wherein R1 is a polypeptide comprising; a modified human c-mpl ligand amino acid sequence of the formula:
SerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeuArgAspSer (SEQ ID NO:256) 1           5              10             15 HisValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuProThrPro 20             25             30             35 ValLeuLeuProAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGluGlu    40             45             50             55 ThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAla       60             65             70             75 AlaArgGlyGlnLeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGly          80             85             90             95 GlnValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnXaaXaaXaa             100            105            110 XaaGlyArgThrThrAlaHisLysAspProAsnAlaIlePheLeuSerPheGlnHis 115            120            125            130 LeuLeuArgGlyLysValArgPheLeuMetLeuValGlyGlySerThrLeuCysVal    135            140            145            150 Arg 153
wherein
Xaa at position 112 is deleted or Leu, Ala, Val, Ile, Pro, Phe, Trp, or Met;
Xaa at position 113 is deleted or Pro, Phe, Ala, Val, Leu, Ile, Trp, or Met;
Xaa at position 114 is deleted or Pro, Phe, Ala, Val, Leu, Ile, Trp, or Met;
Xaa at position 115 is deleted or Gln, Gly, Ser, Thr, Tyr, or Asn; and
wherein the N-terminus is joined to the C-terminus directly or through a linker (L2) capable of joining the N-terminus to the C-terminus and having new C- and N-termini at amino acids:
26-27 27-28 28-29 29-30 30-31 32-33 33-34 34-35 36-37 37-38 38-39 40-41 41-42 42-43 43-44 44-45 46-47 47-48 48-49 50-51 51-52 52-53 53-54 54-55 55-56 56-57 57-58 58-59 59-60 78-79 79-80 80-81 81-82 82-83 83-84 84-85 85-86 86-87 87-88 88-89 108-109 109-110 110-111 111-112 112-113 113-114 114-115 115-116 116-117 117-118 118-119 119-120 120-121 121-122 122-123 123-124 124-125 125-126 126-127 or 127-128 respectively;
wherein R2 is G-CSF or G-CSF Ser17
wherein L1 is a linker capable of linking R1 to R2; and
said hematopoietic protein can optionally be immediately preceded by (methionine−1), (alanine−1) or (methionine−2, alanine−1).
13. The hematopoietic protein as recited in claim 1, 2, 3, 4, 5, 6, 7, 8, 9, 10 or 12 wherein said linker (L2) is selected from the group consisting of;
GlyGlyGlySer; (SEQ ID NO:12) GlyGlyGlySerGlyGlyGlySer; (SEQ ID NO:242) GlyGlyGlySerGlyGlyGlySerGlyGlyGly (SEQ ID NO:243) Ser; SerGlyGlySerGlyGlySer; (SEQ ID NO:244) GluPheGlyAsnMetAla; (SEQ ID NO:245) GluPheGlyGlyAsnMetAla; (SEQ ID NO:246) GluPheGlyGlyAsnGlyGlyAsnMetAla; (SEQ ID NO:247) and GlyGlySerAspMetAlaGly. (SEQ ID NO:248)
14. The hematopoietic protein as recited in claim 11 wherein said linker (L2) is selected from the group consisting of:
GlyGlyGlySer; (SEQ ID NO:12) GlyGlyGlySerGlyGlyGlySer; (SEQ ID NO:242) GlyGlyGlySerGlyGlyGlySerGlyGlyGly (SEQ ID NO:243) Ser; SerGlyGlySerGlyGlySer; (SEQ ID NO:244) GluPheGlyAsnMetAla; (SEQ ID NO:245) GluPheGlyGlyAsnMetAla; (SEQ ID NO:246) GluPheGlyGlyAsnGlyGlyAsnMetAla; (SEQ ID NO:247) and GlyGlySerAspMetAlaGly. (SEQ ID NO:248)
15. The hematopoietic protein as recited in claim 1 wherein said protein is selected from the group consisting of:
Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:166) Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Gly Gly Ser Gly Gly Gly Ser Asn Met Ala Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Ser Gly Gly Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr; Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:167) Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Ser Gly Gly Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr; Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:168) Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Gly Gly Ser Gly Gly Gly Ser Asn Met Ala Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Ser Gly Gly Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser; Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:169) Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Ser Gly Gly Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser; Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:170) Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Gly Gly Ser Gly Gly Gly Ser Asn Met Ala Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Ser Gly Gly Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly; Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:171) Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Ser Gly Gly Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly; Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:172) Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Gly Gly Ser Gly Gly Gly Ser Asn Met Ala Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Ser Gly Gly Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro; Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:173) Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Ser Gly Gly Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro; Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:177) Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Gly Gly Ser Gly Gly Gly Ser Asn Met Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Ser Gly Gly Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala; Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:175) Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Ser Gly Gly Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala; Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:176) Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Gly Gly Ser Gly Gly Gly Ser Asn Met Ala Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Thr Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr; Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:177) Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Thr Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr; Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:179) Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Thr Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser; Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:181) Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Thr Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly; Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:182) Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Gly Gly Ser Gly Gly Gly Ser Asn Met Ala Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Thr Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro; Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:183) Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Thr Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro; Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg (SEQ ID NO:184) Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Gly Gly Ser Gly Gly Gly Ser Asn Met Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Thr Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala; MetAlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAla (SEQ ID NO:194) ProLeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsn LeuArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSer GlyIleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaPro SerArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThr PheTyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGly SerProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGlu SerHisLysSerProAsnMetAlaTyrLysLeuCysHisProGluGluLeuValLeuLeu GlyHisSerLeuGlyIleProTrpAlaProLeuSerSerCysProSerGlnAlaLeuGln LeuAlaGlyCysLeuSerGlnLeuHisSerGlyLeuPheLeuTyrGlnGlyLeuLeuGln AlaLeuGluGlyIleSerProGluLeuGlyProThrLeuAspThrLeuGlnLeuAspVal AlaAspPheAlaThrThrIleTrpGlnGlnMetGluGluLeuGlyMetAlaProAlaLeu GlnProThrGlnGlyAlaMetProAlaPheAlaSerAlaPheGlnArgArgAlaGlyGly ValLeuValAlaSerHisLeuGlnSerPheLeuGluValSerTyrArgValLeuArgHis LeuAlaGlnProGlyGlyGlySerAspMetAlaThrProLeuGlyProAlaSerSerLeu ProGlnSerPheLeuLeuLysSerLeuGluGlnValArgLysIleGlnGlyAspGlyAla AlaLeuGlnGluLysLeuCysAlaThr; MetAlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAla (SEQ ID NO:195) ProLeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsn LeuArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSer GlyIleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaPro SerArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThr PheTyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGly SerProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGlu SerHisLysSerProAsnMetAlaProGluLeuGlyProThrLeuAspThrLeuGlnLeu AspValAlaAspPheAlaThrThrIleTrpGlnGlnMetGluGluLeuGlyMetAlaPro AlaLeuGlnProThrGlnGlyAlaMetProAlaPheAlaSerAlaPheGlnArgArgAla GlyGlyValLeuValAlaSerHisLeuGlnSerPheLeuGluValSerTyrArgValLeu ArgHisLeuAlaGlnProGlyGlyGlySerAspMetAlaThrProLeuGlyProAlaSer SerLeuProGlnSerPheLeuLeuLysSerLeuGluGlnValArgLysIleGlnGlyAsp GlyAlaAlaLeuGlnGluLysLeuCysAlaThrTyrLysLeuCysHisProGluGluLeu ValLeuLeuGlyHisSerLeuGlyIleProTrpAlaProLeuSerSerCysProSerGln AlaLeuGlnLeuAlaGlyCysLeuSerGlnLeuHisSerGlyLeuPheLeuTyrGlnGly LeuLeuGlnAlaLeuGluGlyIleSer; MetAlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAla (SEQ ID NO:196) ProLeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsn LeuArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSer GlyIleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaPro SerArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThr PheTyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGly SerProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGlu SerHisLysSerProAsnMetAlaSerAlaPheGlnArgArgAlaGlyGlyValLeuVal AlaSerHisLeuGlnSerPheLeuGluValSerTyrArgValLeuArgHisLeuAlaGln ProGlyGlyGlySerAspMetAlaThrProLeuGlyProAlaSerSerLeuProGlnSer PheLeuLeuLysSerLeuGluGlnValArgLysIleGlnGlyAspGlyAlaAlaLeuGln GluLysLeuCysAlaThrTyrLysLeuCysHisProGluGluLeuValLeuLeuGlyHis SerLeuGlyIleProTrpAlaProLeuSerSerCysProSerGlnAlaLeuGlnLeuAla GlyCysLeuSerGlnLeuHisSerGlyLeuPheLeuTyrGlnGlyLeuLeuGlnAlaLeu GluGlyIleSerProGluLeuGlyProThrLeuAspThrLeuGlnLeuAspValAlaAsp PheAlaThrThrIleTrpGlnGlnMetGluGluLeuGlyMetAlaProAlaLeuGlnPro ThrGlnGlyAlaMetProAlaPheAla; MetAlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAla (SEQ ID NO:197) ProLeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsn LeuArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSer GlyIleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaPro SerArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThr PheTyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGly SerProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGlu SerHisLysSerProAsnMetAlaMetAlaProAlaLeuGlnProThrGlnGlyAlaMet ProAlaPheAlaSerAlaPheGlnArgArgAlaGlyGlyValLeuValAlaSerHisLeu GlnSerPheLeuGluValSerTyrArgValLeuArgHisLeuAlaGlnProGlyGlyGly SerAspMetAlaThrProLeuGlyProAlaSerSerLeuProGlnSerPheLeuLeuLys SerLeuGluGlnValArgLysIleGlnGlyAspGlyAlaAlaLeuGlnGluLysLeuCys AlaThrTyrLysLeuCysHisProGluGluLeuValLeuLeuGlyHisSerLeuGlyIle ProTrpAlaProLeuSerSerCysProSerGlnAlaLeuGlnLeuAlaGlyCysLeuSer GlnLeuHisSerGlyLeuPheLeuTyrGlnGlyLeuLeuGlnAlaLeuGluGlyIleSer ProGluLeuGlyProThrLeuAspThrLeuGlnLeuAspValAlaAspPheAlaThrThr IleTrpGlnGlnMetGluGluLeuGly; MetAlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAla (SEQ ID NO:198) ProLeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsn LeuArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSer GlyIleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaPro SerArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThr PheTyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGly SerProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGlu SerHisLysSerProAsnMetAlaThrGlnGlyAlaMetProAlaPheAlaSerAlaPhe GlnArgArgAlaGlyGlyValLeuValAlaSerHisLeuGlnSerPheLeuGluValSer TyrArgValLeuArgHisLeuAlaGlnProGlyGlyGlySerAspMetAlaThrProLeu GlyProAlaSerSerLeuProGlnSerPheLeuLeuLysSerLeuGluGlnValArgLys IleGlnGlyAspGlyAlaAlaLeuGlnGluLysLeuCysAlaThrTyrLysLeuCysHis ProGluGluLeuValLeuLeuGlyHisSerLeuGlyIleProTrpAlaProLeuSerSer CysProSerGlnAlaLeuGlnLeuAlaGlyCysLeuSerGlnLeuHisSerGlyLeuPhe LeuTyrGlnGlyLeuLeuGlnAlaLeuGluGlyIleSerProGluLeuGlyProThrLeu AspThrLeuGlnLeuAspValAlaAspPheAlaThrThrIleTrpGlnGlnMetGluGlu LeuGlyMetAlaProAlaLeuGlnPro; Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys (SEQ ID NO:209) Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gly Gln Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Thr Gln Leu Pro Pro Gln Gly Arg Thr Thr Ala His Lys Asp Pro Asn Ala Ile Phe Leu Ser Phe Gln His Leu Leu Arg Gly Lys Val Arg Phe Leu Met Leu Val Gly Gly Ser Thr Leu Cys Val Arg Glu Phe Gly Gly Asn Met Ala Ser Pro Ala Pro Pro Ala Cys Asp Leu Arg Val Leu Ser Lys Leu Leu Arg Asp Ser His Val Leu His Ser Arg Leu Ser Gln Cys Pro Glu Val His Pro Leu Pro Thr Pro Val Leu Leu Pro Ala Val Asp Phe Ser Leu Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln Asp Ile Leu Gly Ala Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Arg Gly Gln Leu; Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys (SEQ ID NO:210) Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Gly Thr Gln Leu Pro Pro Gln Gly Arg Thr Thr Ala His Lys Asp Pro Asn Ala Ile Phe Leu Ser Phe Gln His Leu Leu Arg Gly Lys Val Arg Phe Leu Met Leu Val Gly Gly Ser Thr Leu Cys Val Arg Glu Phe Gly Gly Asn Met Ala Ser Pro Ala Pro Pro Ala Cys Asp Leu Arg Val Leu Ser Lys Leu Leu Arg Asp Ser His Val Leu His Ser Arg Leu Ser Gln Cys Pro Glu Val His Pro Leu Pro Thr Pro Val Leu Leu Pro Ala Val Asp Phe Ser Leu Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln Asp Ile Leu Gly Ala Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Arg Gly Gln Leu Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gly Gln Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu; Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys (SEQ ID NO:211) Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Gly Arg Thr Thr Ala His Lys Asp Pro Asn Ala Ile Phe Leu Ser Phe Gln His Leu Leu Arg Gly Lys Val Arg Phe Leu Met Leu Val Gly Gly Ser Thr Leu Cys Val Arg Glu Phe Gly Gly Asn Met Ala Ser Pro Ala Pro Pro Ala Cys Asp Leu Arg Val Leu Ser Lys Leu Leu Arg Asp Ser His Val Leu His Ser Arg Leu Ser Gln Cys Pro Glu Val His Pro Leu Pro Thr Pro Val Leu Leu Pro Ala Val Asp Phe Ser Leu Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln Asp Ile Leu Gly Ala Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Arg Gly Gln Leu Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gly Gln Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Thr Gln Leu Pro Pro Gln; Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys (SEQ ID NO:212) Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala His Lys Asp Pro Asn Ala Ile Phe Leu Ser Phe Gln His Leu Leu Arg Gly Lys Val Arg Phe Leu Met Leu Val Gly Gly Ser Thr Leu Cys Val Arg Glu Phe Gly Gly Asn Met Ala Ser Pro Ala Pro Pro Ala Cys Asp Leu Arg Val Leu Ser Lys Leu Leu Arg Asp Ser His Val Leu His Ser Arg Leu Ser Gln Cys Pro Glu Val His Pro Leu Pro Thr Pro Val Leu Leu Pro Ala Val Asp Phe Ser Leu Gly Glu Trp Lys Thr Gln Met Glu Glu Thr Lys Ala Gln Asp Ile Leu Gly Ala Val Thr Leu Leu Leu Glu Gly Val Met Ala Ala Arg Gly Gln Leu Gly Pro Thr Cys Leu Ser Ser Leu Leu Gly Gln Leu Ser Gly Gln Val Arg Leu Leu Leu Gly Ala Leu Gln Ser Leu Leu Gly Thr Gln Leu Pro Pro Gln Gly Arg Thr Thr; Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met (SEQ ID NO:186) Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Gly Gly Gly Ser Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg Pro Pro Ala Pro Leu Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Ser Gly Gly Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro; Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys (SEQ ID NO:187) Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Gly Gly Gly Ser Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Ser Gly Gly Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro; Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln (SEQ ID NO:189) Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Gly Gly Gly Ser Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Ser Gly Gly Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro; Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met (SEQ ID NO:190) Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Gly Gly Gly Ser Gly Gly Gly Ser Gly Gly Gly Ser Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg Pro Pro Ala Pro Leu Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Ser Gly Gly Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro; Asn Ala Ser Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys (SEQ ID NO:191) Leu Pro Ser Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr Leu Glu Gln Ala Gln Glu Gln Gln Gly Gly Gly Ser Gly Gly Gly Ser Gly Gly Gly Ser Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu Lys Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Tyr Val Glu Gly Gly Gly Gly Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Ser Gly Gly Ser Gly Gly Ser Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro; MetAlaAsnCysSerAsnMetIleAspGluIleIleThrHisLeuLysGlnProProLeu (SEQ ID NO:199) ProLeuLeuAspPheAsnAsnLeuAsnGlyGluAspGlnAspIleLeuMetAspAsnAsn LeuArgArgProAsnLeuGluAlaPheAsnArgAlaValLysSerLeuGlnAsnAlaSer AlaIleGluSerIleLeuLysAsnLeuLeuProCysLeuProLeuAlaThrAlaAlaPro ThrArgHisProIleHisIleLysAspGlyAspTrpAsnGluPheArgArgLysLeuThr PheTyrLeuLysThrLeuGluAsnAlaGlnAlaGlnGlnTyrValGluGlyGlyGlyGly SerProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGlu SerHisLysSerProAsnMetAlaThrGlnGlyAlaMetProAlaPheAlaSerAlaPhe GlnArgArgAlaGlyGlyValLeuValAlaSerHisLeuGlnSerPheLeuGluValSer TyrArgValLeuArgHisLeuAlaGlnProSerGlyGlySerGlyGlySerGlnSerPhe LeuLeuLysSerLeuGluGlnValArgLysIleGlnGlyAspGlyAlaAlaLeuGlnGlu LysLeuCysAlaThrTyrLysLeuCysHisProGluGluLeuValLeuLeuGlyHisSer LeuGlyIleProTrpAlaProLeuSerSerCysProSerGlnAlaLeuGlnLeuAlaGly CysLeuSerGlnLeuHisSerGlyLeuPheLeuTyrGlnGlyLeuLeuGlnAlaLeuGlu GlyIleSerProGluLeuGlyProThrLeuAspThrLeuGlnLeuAspValAlaAspPhe AlaThrThrIleTrpGlnGlnMetGluGluLeuGlyMetAlaProAlaLeuGlnPro; MetAlaAsnCysSerAsnMetIleAspGluIleIleThrHisLeuLysGlnProProLeu (SEQ ID NO:200) ProLeuLeuAspPheAsnAsnLeuAsnGlyGluAspGlnAspIleLeuMetGluAsnAsn LeuArgArgProAsnLeuGluAlaPheAsnArgAlaValLysSerLeuGlnAsnAlaSer AlaIleGluSerIleLeuLysAsnLeuLeuProCysLeuProLeuAlaThrAlaAlaPro ThrArgHisProIleIleIleArgAspGlyAspTrpAsnGluPheArgArgLysLeuThr PheTyrLeuLysThrLeuGluAsnAlaGlnAlaGlnGlnTyrValGluGlyGlyGlyGly SerProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGlu SerHisLysSerProAsnMetAlaThrGlnGlyAlaMetProAlaPheAlaSerAlaPhe GlnArgArgAlaGlyGlyValLeuValAlaSerHisLeuGlnSerPheLeuGluValSer TyrArgValLeuArgHisLeuAlaGlnProThrProLeuGlyProAlaSerSerLeuPro GlnSerPheLeuLeuLysSerLeuGluGlnValArgLysIleGlnGlyAspGlyAlaAla LeuGlnGluLysLeuCysAlaThrTyrLysLeuCysHisProGluGluLeuValLeuLeu GlyHisSerLeuGlyIleProTrpAlaProLeuSerSerCysProSerGlnAlaLeuGln LeuAlaGlyCysLeuSerGlnLeuHisSerGlyLeuPheLeuTyrGlnGlyLeuLeuGln AlaLeuGluGlyIleSerProGluLeuGlyProThrLeuAspThrLeuGlnLeuAspVal AlaAspPheAlaThrThrIleTrpGlnGlnMetGluGluLeuGlyMetAlaProAlaLeu GlnPro; MetAlaAsnCysSerAsnMetIleAspGluIleIleThrHisLeuLysGlnProProLeu (SEQ ID NO:201) ProLeuLeuAspPheAsnAsnLeuAsnGlyGluAspGlnAspIleLeuMetGluAsnAsn LeuArgArgProAsnLeuGluAlaPheAsnArgAlaValLysSerLeuGlnAsnAlaSer AlaIleGluSerIleLeuLysAsnLeuLeuProCysLeuProLeuAlaThrAlaAlaPro ThrArgHisProIleIleIleArgAspGlyAspTrpAsnGluPheArgArgLysLeuThr PheTyrLeuLysThrLeuGluAsnAlaGlnAlaGlnGlnTyrValGluGlyGlyGlyGly SerProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGlu SerHisLysSerProAsnMetAlaThrGlnGlyAlaMetProAlaPheAlaSerAlaPhe GlnArgArgAlaGlyGlyValLeuValAlaSerHisLeuGlnSerPheLeuGluValSer TyrArgValLeuArgHisLeuAlaGlnProSerGlyGlySerGlyGlySerGlnSerPhe LeuLeuLysSerLeuGluGlnValArgLysIleGlnGlyAspGlyAlaAlaLeuGlnGlu LysLeuCysAlaThrTyrLysLeuCysHisProGluGluLeuValLeuLeuGlyHisSer LeuGlyIleProTrpAlaProLeuSerSerCysProSerGlnAlaLeuGlnLeuAlaGly CysLeuSerGlnLeuHisSerGlyLeuPheLeuTyrGlnGlyLeuLeuGlnAlaLeuGlu GlyIleSerProGluLeuGlyProThrLeuAspThrLeuGlnLeuAspValAlaAspPhe AlaThrThrIleTrpGlnGlnMetGluGluLeuGlyMetAlaProAlaLeuGlnPro; MetAlaAsnCysSerAsnMetIleAspGluIleIleThrHisLeuLysGlnProProLeu (SEQ ID NO:202) ProLeuLeuAspPheAsnAsnLeuAsnGlyGluAspGlnAspIleLeuMetAspAsnAsn LeuArgArgProAsnLeuGluAlaPheAsnArgAlaValLysSerLeuGlnAsnAlaSer AlaIleGluSerIleLeuLysAsnLeuLeuProCysLeuProLeuAlaThrAlaAlaPro ThrArgHisProIleHisIleLysAspGlyAspTrpAsnGluPheArgArgLysLeuThr PheTyrLeuLysThrLeuGluAsnAlaGlnAlaGlnGlnTyrValGluGlyGlyGlyGly SerProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGlu SerHisLysSerProAsnMetAlaThrGlnGlyAlaMetProAlaPheAlaSerAlaPhe GlnArgArgAlaGlyGlyValLeuValAlaSerHisLeuGlnSerPheLeuGluValSer TyrArgValLeuArgHisLeuAlaGlnProThrProLeuGlyProAlaSerSerLeuPro GlnSerPheLeuLeuLysSerLeuGluGlnValArgLysIleGlnGlyAspGlyAlaAla LeuGlnGluLysLeuCysAlaThrTyrLysLeuCysHisProGluGluLeuValLeuLeu GlyHisSerLeuGlyIleProTrpAlaProLeuSerSerCysProSerGlnAlaLeuGln LeuAlaGlyCysLeuSerGlnLeuHisSerGlyLeuPheLeuTyrGlnGlyLeuLeuGln AlaLeuGluGlyIleSerProGluLeuGlyProThrLeuAspThrLeuGlnLeuAspVal AlaAspPheAlaThrThrIleTrpGlnGlnMetGluGluLeuGlyMetAlaProAlaLeu GlnPro; AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:221) LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer HisLysSerProAsnMetGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGly GlnValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeuProProGln GlyArgThrThrAlaHisLysAspProAsnAlaIlePheLeuSerPheGlnHisLeuLeu ArgGlyLysValArgPheLeuMetLeuValGlyGlySerThrLeuCysValArgGluPhe GlyAsnMetAlaSerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeu ArgAspSerHisValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuPro ThrProValLeuLeuProAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGlu GluThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAla AlaArgGlyGlnLeu; AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:222) LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer HisLysSerProAsnMetGlyThrGlnLeuProProGlnGlyArgThrThrAlaHisLys AspProAsnAlaIlePheLeuSerPheGlnHisLeuLeuArgGlyLysValArgPheLeu MetLeuValGlyGlySerThrLeuCysValArgGluPheGlyAsnMetAlaSerProAla ProProAlaCysAspLeuArgValLeuSerLysLeuLeuArgAspSerHisValLeuHis SerArgLeuSerGlnCysProGluValHisProLeuProThrProValLeuLeuProAla ValAspPheSerLeuGlyGluTrpLysThrGlnMetGluGluThrLysAlaGlnAspIle LeuGlyAlaValThrLeuLeuLeuGluGlyValMetAlaAlaArgGlyGlnLeuGlyPro ThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGlnValArgLeuLeuLeuGlyAla LeuGlnSerLeuLeu; AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:223 LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer HisLysSerProAsnMetGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGly GlnValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeuProProGln GlyArgThrThrAlaHisLysAspProAsnAlaIlePheLeuSerPheGlnHisLeuLeu ArgGlyLysValArgPheLeuMetLeuValGlyGlySerThrLeuCysValArgGluPhe GlyGlyAsnGlyGlyAsnMetAlaSerProAlaProProAlaCysAspLeuArgValLeu SerLysLeuLeuArgAspSerHisValLeuHisSerArgLeuSerGlnCysProGluVal HisProLeuProThrProValLeuLeuProAlaValAspPheSerLeuGlyGluTrpLys ThrGlnMetGluGluThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGlu GlyValMetAlaAlaArgGlyGlnLeu; AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO: 234) LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer HisLysSerProAsnMetGlyThrGlnLeuProProGlnGlyArgThrThrAlaHisLys AspProAsnAlaIlePheLeuSerPheGlnHisLeuLeuArgGlyLysValArgPheLeu MetLeuValGlyGlySerThrLeuCysValArgGluPheGlyGlyAsnGlyGlyAsnMet AlaSerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeuArgAspSer HisValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuProThrProVal LeuLeuProAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGluGluThrLys AlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAlaAlaArgGly GlnLeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGlnValArgLeu LeuLeuGlyAlaLeuGlnSerLeuLeu; AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:235) LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer HisLysSerProAsnMetGlyArgThrThrAlaHisLysAspProAsnAlaIlePheLeu SerPheGlnHisLeuLeuArgGlyLysValArgPheLeuMetLeuValGlyGlySerThr LeuCysValArgGluPheGlyGlyAsnGlyGlyAsnMetAlaSerProAlaProProAla CysAspLeuArgValLeuSerLysLeuLeuArgAspSerHisValLeuHisSerArgLeu SerGlnCysProGluValHisProLeuProThrProValLeuLeuProAlaValAspPhe SerLeuGlyGluTrpLysThrGlnMetGluGluThrLysAlaGlnAspIleLeuGlyAla ValThrLeuLeuLeuGluGlyValMetAlaAlaArgGlyGlnLeuGlyProThrCysLeu SerSerLeuLeuGlyGlnLeuSerGlyGlnValArgLeuLeuLeuGlyAlaLeuGlnSer LeuLeuGlyThrGlnLeuProProGln; AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:236) LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer HisLysSerProAsnMetAlaHisLysAspProAsnAlaIlePheLeuSerPheGlnHis LeuLeuArgGlyLysValArgPheLeuMetLeuValGlyGlySerThrLeuCysValArg GluPheGlyGlyAsnGlyGlyAsnMetAlaSerProAlaProProAlaCysAspLeuArg ValLeuSerLysLeuLeuArgAspSerHisValLeuHisSerArgLeuSerGlnCysPro GluValHisProLeuProThrProValLeuLeuProAlaValAspPheSerLeuGlyGlu TrpLysThrGlnMetGluGluThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeu LeuGluGlyValMetAlaAlaArgGlyGlnLeuGlyProThrCysLeuSerSerLeuLeu GlyGlnLeuSerGlyGlnValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThr GlnLeuProProGlnGlyArgThrThr; AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:237) LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer HisLysSerProAsnMetAspProAsnAlaIlePheLeuSerPheGlnHisLeuLeuArg GlyLysValArgPheLeuMetLeuValGlyGlySerThrLeuCysValArgGluPheGly GlyAsnGlyGlyAsnMetAlaSerProAlaProProAlaCysAspLeuArgValLeuSer LysLeuLeuArgAspSerHisValLeuHisSerArgLeuSerGlnCysProGluValHis ProLeuProThrProValLeuLeuProAlaValAspPheSerLeuGlyGluTrpLysThr GlnMetGluGluThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGly ValMetAlaAlaArgGlyGlnLeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeu SerGlyGlnValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeuPro ProGlnGlyArgThrThrAlaHisLys; AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:238) LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer HisLysSerProAsnMetAlaIlePheLeuSerPheGlnHisLeuLeuArgGlyLysVal ArgPheLeuMetLeuValGlyGlySerThrLeuCysValArgGluPheGlyGlyAsnGly GlyAsnMetAlaSerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeu ArgAspSerHisValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuPro ThrProValLeuLeuProAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGlu GluThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAla AlaArgGlyGlnLeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGln ValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeuProProGlnGly ArgThrThrAlaHisLysAspProAsn; AlaAsnCysSerIleMetIleAspGluIleIleHisHisLeuLysArgProProAlaPro (SEQ ID NO:239) LeuLeuAspProAsnAsnLeuAsnAspGluAspValSerIleLeuMetAspArgAsnLeu ArgLeuProAsnLeuGluSerPheValArgAlaValLysAsnLeuGluAsnAlaSerGly IleGluAlaIleLeuArgAsnLeuGlnProCysLeuProSerAlaThrAlaAlaProSer ArgHisProIleIleIleLysAlaGlyAspTrpGlnGluPheArgGluLysLeuThrPhe TyrLeuValThrLeuGluGlnAlaGlnGluGlnGlnTyrValGluGlyGlyGlyGlySer ProGlyGluProSerGlyProIleSerThrIleAsnProSerProProSerLysGluSer HisLysSerProAsnMetAspProAsnAlaIlePheLeuSerPheGlnHisLeuLeuArg GlyLysValArgPheLeuMetLeuValGlyGlySerThrLeuCysValArgGluPheGly GlyAsnMetAlaSerProAlaProProAlaCysAspLeuArgValLeuSerLysLeuLeu ArgAspSerHisValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuPro ThrProValLeuLeuProAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGlu GluThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAla AlaArgGlyGlnLeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGln ValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnGlyArgThrThrAla HisLys; 1 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu (SEQ ID NO:271) 16 Lys Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp 31 Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn 46 Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser 61 Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser 76 Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly 91 Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr 106 Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly 121 Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser 136 Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Leu Gly 151 Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu 166 Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys 181 Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu 196 Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys 211 Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His 226 Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly 241 Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp 256 Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu 271 Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala 286 Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala 301 Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg 316 His Leu Ala Gln Pro Asp Met Ala Thr Pro; 1 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu (SEQ ID NO:272) 16 Lys Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp 31 Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn 46 Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser 61 Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser 76 Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly 31 Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr 106 Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly 121 Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser 136 Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Leu Gly 151 Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu 176 Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys 191 Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu 206 Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys 221 Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His 236 Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly 251 Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp 266 Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu 281 Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala 296 Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala 311 Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg 326 His Leu Ala Gln Pro Asp Met Ala Thr Pro; 1 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu (SEQ ID NO:273) 16 Lys Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp 31 Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn 46 Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser 61 Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser 76 Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly 91 Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr 106 Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly 121 Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser 136 Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Phe Leu 151 Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala 166 Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro 181 Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala 196 Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys 211 Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu 226 Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp 241 Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln 256 Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro Thr Gln 271 Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly 286 Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser 301 Tyr Arg Val Leu Arg His Leu Ala Gln Pro Asp Met Ala Thr Pro 316 Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser; 1 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu (SEQ ID NO:274) 16 Lys Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp 31 Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn 46 Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser 61 Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser 76 Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly 91 Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr 106 Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly 121 Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser 136 Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Glu Gln 151 Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu 166 Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu 181 Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro 196 Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser 211 Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile 226 Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val 241 Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly 256 Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe 271 Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser 286 His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His 301 Leu Ala Gln Pro Asp Met Ala Thr Pro Leu Gly Pro Ala Ser Ser 316 Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu; 1 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu (SEQ ID NO:275) 16 Lys Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp 31 Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn 46 Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser 61 Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser 76 Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly 91 Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr 106 Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly 121 Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser 136 Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Leu Leu 151 Gly His Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro 166 Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser 181 Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile 196 Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val 211 Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly 226 Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe 241 Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser 256 His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His 271 Leu Ala Gln Pro Asp Met Ala Thr Pro Leu Gly Pro Ala Ser Ser 286 Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys 301 Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr 316 Tyr Lys Leu Cys His Pro Glu Glu Leu Val; 1 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu (SEQ ID NO:276) 16 Lys Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp 31 Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn 46 Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser 61 Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser 76 Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly 91 Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr 106 Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly 121 Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser 136 Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Pro Leu 151 Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly Cys Leu Ser 166 Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu Leu Gln Ala 181 Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu Asp Thr Leu 196 Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp Gln Gln Met 211 Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala 226 Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val 241 Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg 256 Val Leu Arg His Leu Ala Gln Pro Asp Met Ala Thr Pro Leu Gly 271 Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu 286 Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys 301 Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu 316 Leu Gly His Ser Leu Gly Ile Pro Trp Ala; 1 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu (SEQ ID NO:277) 16 Lys Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp 31 Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn 46 Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser 61 Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser 76 Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly 91 Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr 106 Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly 121 Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser 136 Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Gln Ala 151 Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe 166 Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu 181 Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe 196 Ala Thr Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro 211 Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala 226 Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln 241 Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln 256 Pro Asp Met Ala Thr Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln 271 Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly 286 Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu 301 Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile 316 Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser; 1 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu (SEQ ID NO:278) 16 Lys Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp 31 Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn 46 Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser 61 Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser 76 Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly 91 Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr 106 Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly 121 Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser 136 Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Leu Gln 151 Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr 166 Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly 181 Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr 196 Thr Ile Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu 211 Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln 226 Arg Arg Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe 241 Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Asp 256 Met Ala Thr Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe 271 Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly 286 Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His 301 Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp 316 Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala; 1 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu (SEQ ID NO:279) 16 Lys Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp 31 Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn 46 Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser 61 Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser 76 Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly 91 Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr 106 Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly 121 Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser 136 Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Leu Ala 151 Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly 166 Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr 181 Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile 196 Trp Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro 211 Thr Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg 226 Ala Gly Gly Val Leu Val Ala Ser His Leu Gln Ser Phe Leu Glu 241 Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Asp Met Ala 256 Thr Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe Leu Leu 271 Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly Ala Ala 286 Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His Pro Glu 301 Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp Ala Pro 316 Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln; 1 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu (SEQ ID NO:280) 16 Lys Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp 31 Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn 46 Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser 61 Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser 76 Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly 91 Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr 106 Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly 121 Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser 136 Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Glu Leu 151 Gly Met Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala 166 Phe Ala Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala 181 Ser His Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg 196 His Leu Ala Gln Pro Asp Met Ala Thr Pro Leu Gly Pro Ala Ser 211 Ser Leu Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg 226 Lys Ile Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala 241 Thr Tyr Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His 256 Ser Leu Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln 271 Ala Leu Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu 286 Phe Leu Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro 301 Glu Leu Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp 316 Phe Ala Thr Thr Ile Trp Gln Gln Met Glu; 1 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu (SEQ ID NO:281) 16 Lys Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp 31 Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn 46 Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser 61 Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser 76 Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly 91 Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr 106 Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly 121 Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser 136 Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Gly Met 151 Ala Pro Ala Leu Gln Pro Thr Gln Gly Ala Met Pro Ala Phe Ala 166 Ser Ala Phe Gln Arg Arg Ala Gly Gly Val Leu Val Ala Ser His 181 Leu Gln Ser Phe Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu 196 Ala Gln Pro Asp Met Ala Thr Pro Leu Gly Pro Ala Ser Ser Leu 211 Pro Gln Ser Phe Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile 226 Gln Gly Asp Gly Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr 241 Lys Leu Cys His Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu 256 Gly Ile Pro Trp Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu 271 Gln Leu Ala Gly Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu 286 Tyr Gln Gly Leu Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu 301 Gly Pro Thr Leu Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala 316 Thr Thr Ile Trp Gln Gln Met Glu Glu Leu; and 1 Met Ala Asn Cys Ser Ile Met Ile Asp Glu Ile Ile His His Leu (SEQ ID NO:282) 16 Lys Arg Pro Pro Ala Pro Leu Leu Asp Pro Asn Asn Leu Asn Asp 31 Glu Asp Val Ser Ile Leu Met Asp Arg Asn Leu Arg Leu Pro Asn 46 Leu Glu Ser Phe Val Arg Ala Val Lys Asn Leu Glu Asn Ala Ser 61 Gly Ile Glu Ala Ile Leu Arg Asn Leu Gln Pro Cys Leu Pro Ser 76 Ala Thr Ala Ala Pro Ser Arg His Pro Ile Ile Ile Lys Ala Gly 91 Asp Trp Gln Glu Phe Arg Glu Lys Leu Thr Phe Tyr Leu Val Thr 106 Leu Glu Gln Ala Gln Glu Gln Gln Tyr Val Glu Gly Gly Gly Gly 121 Ser Pro Gly Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Ser 136 Pro Pro Ser Lys Glu Ser His Lys Ser Pro Asn Met Ala Ser Phe 151 Leu Glu Val Ser Tyr Arg Val Leu Arg His Leu Ala Gln Pro Asp 166 Met Ala Thr Pro Leu Gly Pro Ala Ser Ser Leu Pro Gln Ser Phe 181 Leu Leu Lys Ser Leu Glu Gln Val Arg Lys Ile Gln Gly Asp Gly 196 Ala Ala Leu Gln Glu Lys Leu Cys Ala Thr Tyr Lys Leu Cys His 211 Pro Glu Glu Leu Val Leu Leu Gly His Ser Leu Gly Ile Pro Trp 226 Ala Pro Leu Ser Ser Cys Pro Ser Gln Ala Leu Gln Leu Ala Gly 241 Cys Leu Ser Gln Leu His Ser Gly Leu Phe Leu Tyr Gln Gly Leu 256 Leu Gln Ala Leu Glu Gly Ile Ser Pro Glu Leu Gly Pro Thr Leu 271 Asp Thr Leu Gln Leu Asp Val Ala Asp Phe Ala Thr Thr Ile Trp 286 Gln Gln Met Glu Glu Leu Gly Met Ala Pro Ala Leu Gln Pro Thr 301 Gln Gly Ala Met Pro Ala Phe Ala Ser Ala Phe Gln Arg Arg Ala 316 Gly Gly Val Leu Val Ala Ser His Leu Gln.
16. The hematopoeitic protein as recieted in claim 1 wherein said c-mpl receptor agonist is selected from the group consisiting of:
MetAlaGlyArgThrThrAlaHisLysAspProAsnAlaIlePheLeuSerPheGlnHis (SEQ ID NO: 284) LeuLeuArgGlyLysValArgPheLeuMetLeuValGlyGlySerThrLeuAlaValArg GluPheGlyGlyAsnMetAlaSerProAlaProProAlaAlaAspLeuArgValLeuSer LysLeuLeuArgAspSerHisValLeuHisSerArgLeuSerGlnCysProGluValHis ProLeuProThrProValLeuLeuProAlaValAspPheSerLeuGlyGluTrpLysThr GlnMetGluGluThrLysAlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGly ValMetAlaAlaArgGlyGlnLeuGlyProThrCysLeuSerSerLeuLeuGlyGlnLeu SerGlyGlnValArgLeuLeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeuPro ProGln; and MetAlaGlyProThrCysLeuSerSerLeuLeuGlyGlnLeuSerGlyGlnValArgLeu (SEQ ID NO: 285) LeuLeuGlyAlaLeuGlnSerLeuLeuGlyThrGlnLeuProProGlnGlyArgThrThr AlaHisLysAspProAsnAlaIlePheLeuSerPheGlnHisLeuLeuArgGlyLysVal ArgPheLeuMetLeuValGlyGlySerThrLeuAlaValArgGluPheGlyGlyAsnMet AlaSerProAlaProProAlaAlaAspLeuArgValLeuSerLysLeuLeuArgAspSer HisValLeuHisSerArgLeuSerGlnCysProGluValHisProLeuProThrProVal LeuLeuProAlaValAspPheSerLeuGlyGluTrpLysThrGlnMetGluGluThrLys AlaGlnAspIleLeuGlyAlaValThrLeuLeuLeuGluGlyValMetAlaAlaArgGly GlnLeu
17. The hematopoietic protein of claim 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 or 12 wherein said colony stimulating factor is selected from the group consisting of GM-CSF, G-CSF, G-CSF Ser17, c-mpl ligand (TPO), M-CSF, erythropoietin (EPO), IL-1, IL-4, IL-2, IL-3, IL-5, IL 6, IL-7, IL-8, IL-9, IL-10, IL-11, IL-12, IL-13, IL-15, LIF, flt3/flk2 ligand, human growth hormone, B-cell growth factor, B-cell differentiation factor, eosinophil differentiation factor and stem cell factor (SCF).
18. The hematopoietic protein of claim 17 wherein said colony stimulating factor is selected from the group consisting of G-CSF, G-CSF Ser17 and c-mpl ligand (TPO).
19. A nucleic acid molecule encoding said hematopoietic protein of claim 1.
20. A nucleic acid molecule encoding said hematopoietic protein of claim 2.
21. A nucleic acid molecule encoding said hematopoietic protein of claim 3.
22. A nucleic acid molecule encoding said hematopoietic protein of claim 4.
23. A nucleic acid molecule encoding said hematopoietic protein of claim 5.
24. A nucleic acid molecule encoding said hematopoietic protein of claim 6.
25. A nucleic acid molecule encoding said hematopoietic protein of claim 7.
26. A nucleic acid molecule encoding said hematopoietic protein of claim 8.
27. A nucleic acid molecule encoding said hematopoietic protein of claim 9.
28. A nucleic acid molecule encoding said hematopoietic protein of claim 10.
29. A nucleic acid molecule encoding said hematopoietic protein of claim 11.
30. A nucleic acid molecule encoding said hematopoietic protein of claim 12.
31. A nucleic acid molecule encoding said hematopoietic protein of claim 13.
32. A nucleic acid molecule encoding said hematopoietic protein of claim 14.
33. A nucleic acid molecule encoding said hematopoietic protein of claim 15.
34. A nucleic acid molecule encoding said hematopoietic protein of claim 16.
35. A nucleic acid molecule encoding said hematopoietic protein of claim 17.
36. The nucleic acid molecule according to claim 30 selected from group consisting of:
1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG (SEQ ID NO: 94) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA 151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG GTGGTTCTGG CGGCGGCTCC AACATGGCTT 401 ACAAGCTGTG CCACCCCGAG GAGCTGGTGC TGCTCGGACA CTCTCTGGGC 451 ATCCCCTGGG CTCCCCTGAG CTCCTGCCCC AGCCAGGCCC TGCAGCTGGC 501 AGGCTGCTTG AGCCAACTCC ATAGCGGCCT TTTCCTCTAC CAGGGGCTCC 551 TGCAGGCCCT GGAAGGGATA TCCCCCGAGT TGGGTCCCAC CTTGGACACA 601 CTGCAGCTGG ACCTCCCCGA CTTTGCCACC ACCATCTGGC AGCAGATGGA 651 AGAACTGGGA ATGGCCCCTG CCCTGCAGCC CACCCAGGGT GCCATGCCGG 701 CCTTCGCCTC TGCTTTCCAC CGCCGGGCAG GAGGGGTCCT GGTTGCTAGC 751 CATCTGCAGA GCTTCCTGGA GGTGTCGTAC CGCGTTCTAC GCCACCTTGC 801 GCAGCCCTCT GGCGGCTCTG GCGGCTCTCA GAGCTTCCTG CTCAAGTCTT 851 TAGAGCAAGT GAGAAACATC CAGGGCGATG GCGCAGCGCT CCAGGAGAAG 901 CTGTGTGCCA CCTAATAA; 1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG (SEQ ID NO: 95) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA 151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTGG TTACCCTTGA GCAACCGCAG GAACAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC 401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT GGCTTACAAG 451 CTGTGCCACC CCGAGGAGCT GGTGCTGCTC GGACACTCTC TGGGCATCCC 501 CTGGGCTCCC CTGAGCTCCT GCCCCAGCCA GGCCCTGCAG CTGGCAGGCT 551 GCTTGAGCCA ACTCCATAGC GGCCTTTTCC TCTACCAGGG GCTCCTGCAG 601 GCCCTGCAAG GGATATCCCC CGAGTTGGGT CCCACCTTGG ACACACTGCA 651 GCTGGACGTC GCCGACTTTG CCACCACCAT CTGGCAGCAG ATGGAAGAAC 701 TGGGAATGGC CCCTGCCCTG CAGCCCACCC AGGGTGCCAT GCCGGCCTTC 751 GCCTCTGCTT TCCAGCGCCG GGCAGGAGGG GTCCTGGTTG CTAGCCATCT 801 GCAGAGCTTC CTGGAGGTGT CGTACCGCGT TCTACGCCAC CTTGCGCAGC 851 CCTCTGGCGG CTCTGGCGGC TCTCAGAGCT TCCTGCTCAA GTCTTTAGAG 901 CAAGTGAGAA AGATCCAGGG CGATGGCGCA GCGCTCCAGG AGAAGCTGTG 951 TGCCACCTAA TAA; 1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG (SEQ ID NO: 96) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA 151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG GTGGTTCTGG CGGCGGCTCC AACATGGCTC 401 CCGAGTTGGG TCCCACCTTG GACACACTGC AGCTGGACGT CGCCGACTTT 451 GCCACCACCA TCTGGCAGCA GATGGAAGAA CTGGGAATGG CCCCTGCCCT 501 GCAGCCCACC CAGGGTGCCA TGCCGGCCTT CGCCTCTGCT TTCCAGCGCC 551 GGGCAGGAGG GGTCCTGGTT GCTAGCCATC TGCAGAGCTT CCTGGAGGTG 601 TCGTACCGCG TTCTACGCCA CCTTGCGCAG CCCTCTGGCG GCTCTGGCGG 651 CTCTCAGAGC TTCCTGCTCA AGTCTTTAGA GCAAGTGAGA AAGATCCAGG 701 GCGATGGCGC AGCGCTCCAG GAGAAGCTGT GTGCCACCTA CAAGCTGTGC 751 CACCCCGACG AGCTGGTGCT GCTCGGACAC TCTCTGGGCA TCCCCTGGGC 801 TCCCCTGAGC TCCTGCCCCA GCCAGGCCCT GCAGCTGGCA GGCTGCTTGA 851 GCCAACTCCA TAGCGGCCTT TTCCTCTACC AGGGGCTCCT GCAGGCCCTG 901 GAAGGGATAT CCTAATAA; 1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAC (SEQ ID NO: 97) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGACCCAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA 151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCACGT GACTGGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTGC TTACCCTTGA GCAAGCCCAG GAACAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC 401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT GGCTCCCGAG 451 TTGGGTCCCA CCTTGGACAC ACTGCAGCTG GACGTCGCCG ACTTTGCCAC 501 CACCATCTGG CAGCAGATGG AAGAACTGGG AATGGCCCCT GCCCTGCAGC 551 CCACCCAGGG TGCCATGCCG GCCTTCCCCT CTGCTTTCCA GCGCCGGGCA 601 GGAGGGCTCC TGGTTGCTAG CCATCTGCAG AGCTTCCTGG AGGTGTCGTA 651 CCGCGTTCTA CGCCACCTTG CGCAGCCCTC TGGCGGCTCT GGCGGCTCTC 701 AGAGCTTCCT GCTCAAGTCT TTAGAGCAAG TGAGAAAGAT CCAGGGCGAT 751 GGCGCAGCGC TCCAGGAGAA GCTGTGTGCC ACCTACAAGC TGTCCCACCC 801 CGAGGAGCTG GTGCTGCTCG GACACTCTCT GGGCATCCCC TGGGCTCCCC 851 TGAGCTCCTG CCCCAGCCAG GCCCTGCAGC TGGCAGGCTG CTTGAGCCAA 901 CTCCATAGCG GCCTTTTCCT CTACCAGGGG CTCCTGCAGG CCCTGGAAGG 951 GATATCCTAA TAA; 1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG (SEQ ID NO: 98) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA 151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG GTGGTTCTGG CGGCGGCTCC AACATGGCTA 401 TGGCCCCTGC CCTGCAGCCC ACCCAGGGTG CCATGCCGGC CTTCGCCTCT 451 GCTTTCCAGC GCCGGGCAGG AGGGGTCCTG GTTGCTAGCC ATCTGCAGAG 501 CTTCCTGGAG GTGTCGTACC GCGTTCTACG CCACCTTGCG CAGCCCTCTG 551 GCGGCTCTGG CGGCTCTCAG AGCTTCCTGC TCAAGTCTTT AGAGCAAGTG 601 AGAAAGATCC AGGGCGATGG CGCAGCGCTC CAGGAGAAGC TGTGTGCCAC 651 CTACAAGCTG TGCCACCCCG AGGAGCTGGT GCTGCTCGGA CACTCTCTGG 701 GCATCCCCTG GGCTCCCCTG AGCTCCTGCC CCAGCCAGGC CCTGCAGCTG 751 GCAGGCTGCT TGAGCCAACT CCATAGCGGC CTTTTCCTCT ACCAGGGGCT 801 CCTGCAGGCC CTGGAAGGGA TATCCCCCGA GTTGGGTCCC ACCTTGGACA 851 CACTGCAGCT GGACGTCGCC GACTTTGCCA CCACCATCTG GCAGCAGATG 901 GAAGAACTGG GATAATAA; 1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG (SEQ ID NO: 99) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCCTA 151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC 401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT GGCTATGGCC 451 CCTGCCCTGC AGCCCACCCA GGGTGCCATG CCGGCCTTCG CCTCTGCTTT 501 CCAGCGCCGG GCAGGAGGGG TCCTGGTTGC TAGCCATCTG CAGAGCTTCC 551 TGGAGGTGTC GTACCGCGTT CTACGCCACC TTGCGCAGCC CTCTGGCGGC 601 TCTGGCGGCT CTCAGAGCTT CCTGCTCAAG TCTTTAGAGC AAGTGAGAAA 651 GATCCAGGGC GATGGCGCAG CGCTCCAGGA GAAGCTGTGT GCCACCTACA 701 AGCTGTGCCA CCCCGAGGAG CTGGTGCTGC TCGGACACTC TCTGGGCATC 751 CCCTGGGCTC CCCTGAGCTC CTGCCCCAGC CAGGCCCTGC AGCTGGCAGG 801 CTGCTTGAGC CAACTCCATA GCGGCCTTTT CCTCTACCAG GGGCTCCTGC 851 AGGCCCTGGA AGGGATATCC CCCGAGTTGG GTCCCACCTT GGACACACTG 901 CAGCTGGACG TCGCCGACTT TGCCACCACC ATCTGGCAGC AGATGGAAGA 951 ACTGGGATAA TAA; 1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG (SEQ ID NO: 100) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA 151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG GTGGTTCTGG CGGCGGCTCC AACATGGCTA 401 CCCAGGGTGC CATGCCGGCC TTCGCCTCTG CTTTCCAGCG CCGGGCAGGA 451 GGGGTCCTGG TTGCTAGCCA TCTGCAGAGC TTCCTGGAGG TGTCGTACCG 501 CGTTCTACGC CACCTTGCGC AGCCCTCTGG CGGCTCTGGC GGCTCTCAGA 551 GCTTCCTGCT CAAGTCTTTA GAGCAAGTGA GAAAGATCCA GGGCGATGGC 601 GCAGCGCTCC AGGAGAAGCT GTGTGCCACC TACAAGCTGT GCCACCCCGA 651 GGAGCTGGTG CTGCTCGGAC ACTCTCTGGG CATCCCCTGG GCTCCCCTGA 701 GCTCCTGCCC CAGCCAGGCC CTGCAGCTGG CAGGCTGCTT GAGCCAACTC 751 CATAGCGGCC TTTTCCTCTA CCAGGGGCTC CTGCAGGCCC TGGAAGGGAT 801 ATCCCCCGAG TTGGGTCCCA CCTTGGACAC ACTGCAGCTG GACGTCGCCG 851 ACTTTGCCAC CACCATCTGG CAGCAGATGG AAGAACTGGG AATGGCCCCT 901 GCCCTGCAGC CCTAATAA; 1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG (SEQ ID NO: 101) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA 151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC 401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT GGCTACCCAG 451 GGTGCCATGC CGGCCTTCGC CTCTGCTTTC CAGCGCCGGG CAGGAGGGGT 501 CCTGGTTGCT AGCCATCTGC AGAGCTTCCT GGAGGTGTCG TACCGCGTTC 551 TACGCCACCT TGCGCAGCCC TCTGGCGGCT CTGGCGGCTC TCAGAGCTTC 601 CTGCTCAAGT CTTTAGAGCA AGTGAGAAAG ATCCAGGGCG ATGGCGCAGC 651 GCTCCAGGAG AAGCTGTGTG CCACCTACAA GCTGTGCCAC CCCGAGGAGC 701 TGGTGCTGCT CGGACACTCT CTGCGCATCC CCTGGGCTCC CCTGAGCTCC 751 TGCCCCAGCC AGGCCCTGCA GCTGGCAGGC TGCTTGAGCC AACTCCATAG 801 CGGCCTTTTC CTCTACCAGG GGCTCCTGCA GGCCCTGGAA GGGATATCCC 851 CCGAGTTGGG TCCCACCTTG GACACACTGC AGCTGGACGT CGCCGACTTT 901 GCCACCACCA TCTGGCAGCA GATGGAAGAA CTGGGAATGG CCCCTGCCCT 951 GCAGCCCTAA TAA; 1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG (SEQ ID NO: 102) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA 151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG GTGGTTCTGG CGGCGGCTCC AACATGGCTT 401 CTGCTTTCCA GCGCCGGGCA GGAGGGGTCC TGGTTGCTAG CCATCTGCAG 451 AGCTTCCTGG AGGTGTCGTA CCGCGTTCTA CGCCACCTTG CGCAGCCCTC 501 TGGCGGCTCT GGCGGCTCTC AGAGCTTCCT GCTCAAGTCT TTAGAGCAAG 551 TGAGAAAGAT CCAGGGCGAT GGCGCAGCGC TCCAGGAGAA GCTGTGTGCC 601 ACCTACAAGC TGTGCCACCC CGAGGAGCTG GTGCTGCTCG GACACTCTCT 651 GGGCATCCCC TGGGCTCCCC TGAGCTCCTG CCCCAGCCAG GCCCTGCAGC 701 TGGCAGGCTG CTTGAGCCAA CTCCATAGCG GCCTTTTCCT CTACCAGGGG 751 CTCCTGCAGG CCCTGGAAGG GATATCCCCC GAGTTGGGTC CCACCTTGGA 801 CACACTGCAG CTGGACGTCG CCGACTTTGC CACCACCATC TGGCAGCAGA 851 TGGAAGAACT GGGAATGGCC CCTGCCCTGC AGCCCACCCA GGGTGCCATG 901 CCGGCCTTCG CCTAATAA; 1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG (SEQ ID NO: 107) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA 151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC 401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT GGCTCCCGAG 451 TTGGGTCCCA CCTTGGACAC ACTGCAGCTG GACGTCGCCG ACTTTGCCAC 501 CACCATCTGG CAGCAGATGG AAGAACTGGG AATGGCCCCT GCCCTGCAGC 551 CCACCCAGGG TGCCATGCCG GCCTTCGCCT CTGCTTTCCA GCGCCGGGCA 601 GGAGGGGTCC TGGTTGCTAG CCATCTGCAG AGCTTCCTGG AGGTGTCGTA 651 CCGCGTTCTA CGCCACCTTG CGCAGCCCAC ACCATTGGGC CCTGCCAGCT 701 CCCTGCCCCA GAGCTTCCTG CTCAAGTCTT TAGAGCAAGT GAGAAAGATC 751 CAGGGCGATG GCGCAGCGCT CCAGGAGAAG CTGTGTGCCA CCTACAAGCT 801 GTGCCACCCC GAGGAGCTGG TGCTGCTCGG ACACTCTCTG GGCATCCCCT 851 GGGCTCCCCT GAGCTCCTGC CCCAGCCAGG CCCTGCAGCT GGCAGGCTGC 901 TTGAGCCAAC TCCATAGCGG CCTTTTCCTC TACCAGGGGC TCCTGCAGGC 951 CCTGGAAGGG ATATCCTAAT AA; 1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG (SEQ ID NO: 103) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA 151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC 401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT GGCTTCTGCT 451 TTCCAGCGCC GGGCAGGAGG GGTCCTGGTT GCTAGCCATC TGCAGAGCTT 501 CCTGGAGGTG TCGTACCGCG TTCTACGCCA CCTTGCGCAG CCCTCTGGCG 551 GCTCTGGCGG CTCTCAGAGC TTCCTGCTCA AGTCTTTAGA GCAAGTGAGA 601 AAGATCCAGG GCGATGGCGC AGCGCTCCAG GAGAAGCTGT GTGCCACCTA 651 CAAGCTGTGC CACCCCGAGG AGCTGGTGCT GCTCGGACAC TCTCTGGGCA 701 TCCCCTGGGC TCCCCTGAGC TCCTGCCCCA GCCAGGCCCT GCAGCTGGCA 751 GGCTGCTTGA GCCAACTCCA TAGCGGCCTT TTCCTCTACC AGGGGCTCCT 801 GCAGGCCCTG GAAGGGATAT CCCCCGAGTT GGGTCCCACC TTGGACACAC 851 TGCAGCTGGA CGTCGCCGAC TTTGCCACCA CCATCTGGCA GCAGATGGAA 901 GAACTGGGAA TGGCCCCTGC CCTGCAGCCC ACCCAGGGTG CCATGCCGGC 951 CTTCGCCTAA TAA; 1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG (SEQ ID NO: 104) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA 151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG GTGGTTCTGG CGGCGGCTCC AACATGGCTT 401 ACAAGCTGTG CCACCCCGAG GAGCTGGTGC TGCTCGGACA CTCTCTGGGC 451 ATCCCCTGGG CTCCCCTGAG CTCCTGCCCC AGCCACGCCC TGCAGCTGGC 501 AGGCTGCTTG AGCCAACTCC ATAGCGGCCT TTTCCTCTAC CAGGGGCTCC 551 TGCAGGCCCT GGAAGGGATA TCCCCCGAGT TGCGTCCCAC CTTGGACACA 601 CTGCAGCTGG ACGTCGCCGA CTTTGCCACC ACCATCTGGC AGCAGATGGA 651 AGAACTGGGA ATGGCCCCTG CCCTGCAGCC CACCCAGGGT GCCATGCCGG 701 CCTTCGCCTC TGCTTTCCAG CGCCGGGCAG GAGGGGTCCT GGTTGCTAGC 751 CATCTGCAGA GCTTCCTGGA GGTGTCGTAC CGCGTTCTAC GCCACCTTGC 801 GCAGCCCACA CCATTGGGCC CTCCCAGCTC CCTGCCCCAG AGCTTCCTGC 851 TCAAGTCTTT AGAGCAAGTG AGAAAGATCC AGGGCGATGG CGCAGCGCTC 901 CAGGAGAAGC TGTGTGCCAC CTAATAA; 1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG (SEQ ID NO: 105) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA 151 AGGGCTGTCA ACAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTGG TTACCCTTGA GCAAGCGCAC GAACAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC 401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT CGCTTACAAG 451 CTGTGCCACC COGAGGAGCT GGTGCTGCTC GGACACTCTC TGGGCATCCC 501 CTGGGCTCCC CTGAGCTCCT GCCCCAGCCA GGCCCTGCAG CTGGCAGGCT 551 GCTTGAGCCA ACTCCATAGC GGCCTTTTCC TCTACCAGGG GCTCCTGCAG 601 GCCCTGGAAG GGATATCCCC CGAGTTGGGT CCCACCTTGG ACACACTGCA 651 GCTGGACGTC GCCGACTTTG CCACCACCAT CTGGCAGCAG ATGGAAGAAC 701 TGGGAATGGC CCCTGCCCTG CAGCCCACCC AGGGTGCCAT GCCGGCCTTC 751 GCCTCTGCTT TCCAGCGCCG GGCAGGAGGG GTCCTGGTTG CTAGCCATCT 801 GCAGAGCTTC CTGGAGGTGT CGTACCGCGT TCTACGCCAC CTTGCGCAGC 851 CCACACCATT GGGCCCTGCC AGCTCCCTGC CCCAGAGCTT CCTGCTCAAG 901 TCTTTAGAGC AAGTGAGAAA GATCCAGGGC GATGGCGCAG CGCTCCAGGA 951 GAAGCTGTGT GCCACCTAAT AA; 1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG (SEQ ID NO: 109) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA 151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC 401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT GGCTATGGCC 451 CCTGCCCTGC AGCCCACCCA GGGTGCCATG CCGGCCTTCG CCTCTGCTTT 501 CCAGCGCCCG GCAGGAGGGG TCCTGGTTGC TAGCCATCTG CAGAGCTTCC 551 TGGAGGTGTC GTACCGCGTT CTACGCCACC TTGCGCAGCC CACACCATTG 601 GGCCCTGCCA GCTCCCTGCC CCAGAGCTTC CTGCTCAAGT CTTTAGAGCA 651 AGTGAGAAAG ATCCAGGGCG ATGGCGCAGC GCTCCAGGAG AAGCTGTGTG 701 CCACCTACAA GCTGTGCCAC CCCGAGGAGC TGGTGCTGCT CGGACACTCT 751 CTGGGCATCC CCTGGGCTCC CCTGAGCTCC TGCCCCAGCC AGGCCCTGCA 801 GCTGGCAGGC TGCTTGAGCC AACTCCATAG CGGCCTTTTC CTCTACCAGG 851 GGCTCCTGCA GGCCCTGGAA GGGATATCCC CCGAGTTGGG TCCCACCTTG 901 GACACACTGC AGCTGGACGT CGCCGACTTT GCCACCACCA TCTGGCAGCA 951 GATGGAAGAA CTGGGATAAT AA; 1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG (SEQ ID NO: 110) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA 151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG GTGGTTCTGG CGGCGGCTCC AACATGGCTA 401 CCCAGGGTGC CATGCCGGCC TTCGCCTCTG CTTTCCAGCG CCGGGCAGGA 451 GGGGTCCTGG TTGCTAGCCA TCTGCAGAGC TTCCTGGAGG TGTCGTACCG 501 CGTTCTACGC CACCTTGCGC AGCCCACACC ATTGGGCCCT GCCAGCTCCC 551 TGCCCCAGAG CTTCCTGCTC AAGTCTTTAG AGCAAGTGAG AAAGATCCAG 601 GGCGATGGCG CAGCGCTCCA GGAGAAGCTG TGTGCCACCT ACAAGCTGTG 651 CCACCCCGAG GAGCTGGTGC TGCTCGGACA CTCTCTGGGC ATCCCCTGGG 701 CTCCCCTGAG CTCCTGCCCC AGCCAGGCCC TGCAGCTGGC AGGCTGCTTG 751 AGCCAACTCC ATAGCGGCCT TTTCCTCTAC CAGGGGCTCC TGCAGGCCCT 801 GGAAGGGATA TCCCCCGAGT TGGGTCCCAC CTTGGACACA CTGCAGCTGG 851 ACGTCGCCGA CTTTGCCACC ACCATCTGGC AGCAGATGGA AGAACTGGGA 901 ATGGCCGCTG CCCTGCAGCC CTAATAA; 1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG (SEQ ID NO: 111) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA 151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC 401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT GGCTACCCAG 451 GGTGCCATGC CGGCCTTCGC CTCTGCTTTC CAGCGCCGGG CAGGAGGGGT 501 CCTGGTTGCT AGCCATCTGC AGAGCTTCCT GGAGGTGTCG TACCGCGTTC 551 TACGCCACCT TGCGCAGCCC ACACCATTGG GCCCTGCCAG CTCCCTGCCC 601 CAGAGCTTCC TGCTCAAGTC TTTAGAGCAA GTGAGAAAGA TCCAGGGCGA 651 TGGCGCAGCG CTCCAGGAGA AGCTGTGTGC CACCTACAAG CTGTGCCACC 701 CCGAGGAGCT GGTGCTGCTC GGACACTCTC TGGGCATCCC CTGGGCTCCC 751 CTGAGCTCCT GCCCCAGCCA GGCCCTGCAG CTGCCAGGCT GCTTGAGCCA 801 ACTCCATAGC GGCCTTTTCC TCTACCAGGG GCTCCTGCAG GCCCTGGAAG 851 GGATATCCCC CGAGTTGGGT CCCACCTTCG ACACACTGCA GCTGGACGTC 901 GCCGACTTTG CCACCACCAT CTGGCAGCAG ATGGAAGAAC TGGGAATGGC 951 CCCTGCCCTG CAGCCCTAAT AA; 1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG (SEQ ID NO: 112) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGACCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA 151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG GTGGTTCTGG CGGCGGCTCC AACATGGCTT 401 CTGCTTTCCA GCGCCGGGCA GGAGGGGTCC TGGTTGCTAG CCATCTGCAG 451 AGCTTCCTGG AGGTGTCGTA CCGCGTTCTA CGCCACCTTG CGCAGCCCAC 501 ACCATTGGGC CCTGCCAGCT CCCTGCCCCA GAGCTTCCTG CTCAAGTCTT 551 TAGAGCAAGT GAGAAAGATC CAGGGCGATG GCGCAGCGCT CCAGGAGAAG 601 CTGTGTGCCA CCTACAAGCT GTGCCACCCC GAGGAGCTGG TGCTGCTCGG 651 ACACTCTCTG GGCATCCCCT GGGCTCCCCT GAGCTCCTGC CCCAGCCAGG 701 CCCTGCAGCT GGCAGGCTGC TTGAGCCAAC TCCATAGCGG CCTTTTCCTC 751 TACCAGGGGC TCCTGCAGGC CCTGGAAGGG ATATCCCCCG AGTTGGGTCC 801 CACCTTGGAC ACACTGCAGC TGGACGTCGC CGACTTTGCC ACCACCATCT 851 GGCAGCAGAT GGAAGAACTG GGAATGGCCC CTGCCCTGCA GCCCACCCAC 901 GGTGCCATGC CGGCCTTCGC CTAATAA; 1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG (SEQ ID NO: 155) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA 151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC 401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT GTCTTACAAG 451 CTGTGCCACC CCGAGCAGCT GGTGCTGCTC GGACACTCTC TGGGCATCCC 501 CTGGGCTCCC CTGAGCTCCT GCCCCAGCCA GGCCCTGCAG CTGGCAGGCT 551 GCTTGAGCCA ACTCCATAGC GGCCTTTTCC TCTACCAGGG GCTCCTGCAG 601 GCCCTGGAAG GGATATCCCC CGAGTTGGGT CCCACCTTGG ACACACTGCA 651 GCTGGACGTC GCCGACTTTG CCACCACCAT CTGGCAGCAG ATGGAAGAAC 701 TGGGAATGGC CCCTGCCCTG CAGCCCACCC AGGGTGCCAT GCCGGCCTTC 751 GCCTCTGCTT TCCAGCGCCC GGCAGGAGGG GTCCTGGTTG CTAGCCATCT 801 GCAGAGCTTC CTGGAGGTGT CGTACCGCGT TCTACGCCAC CTTGCGCAGC 851 CCGGCGGCGG CTCTGACATG GCTACACCAT TAGGCCCTGC CAGCTCCCTG 901 CCCCAGAGCT TCCTGCTCAA GTCTTTAGAG CAACTGAGGA AGATCCAGGG 951 CGATGGCGCA GCGCTCCAGG AGAAGCTGTG TGCCACCTAA TAA; 1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG (SEQ ID NO: 156) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA 151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTGG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC 401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT GTCTCCCGAG 451 TTGGGTCCCA CCTTGGACAC ACTGCAGCTG GACGTCGCCG ACTTTGCCAC 501 CACCATCTGG CAGCAGATGG AAGAACTGGG AATGGCCCCT GCCCTCCAGC 551 CCACCCAGGG TGCCATGCCG GCCTTCGCCT CTGCTTTCCA GCGCCGGGCA 601 GGAGGGGTCC TGGTTGCTAG CCATCTGCAG AGCTTCCTGG AGGTGTCGTA 651 CCGCGTTCTA CGCCACCTTG CGCAGCCCGG CGGCGGCTCT GACATGGCTA 701 CACCATTAGG CCCTGCCAGC TCCCTGCCCC AGAGCTTCCT GCTCAAGTCT 751 TTAGAGCAAG TGAGGAAGAT CCAGGGCGAT GGCGCAGCGC TCCAGGAGAA 801 GCTGTGTGCC ACCTACAAGC TGTGCCACCC CGAGGAGCTG GTGCTGCTCG 851 GACACTCTCT GGGCATCCCC TGGGCTCCCC TGAGCTCCTG CCCCAGCCAG 901 GCCCTGCAGC TGGCAGGCTG CTTGAGCCAA CTCCATAGCG GCCTTTTCCT 951 CTACCAGGGG CTCCTGCAGG CCCTGGAAGG GATATCCTAA TAA; 1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG (SEQ ID NO: 157) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA 151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC 401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT GTCTTCTGCT 451 TTCCAGCGCC GGGCAGGAGG GGTCCTGGTT GCTAGCCATC TGCAGAGCTT 501 CCTCGAGGTG TCGTACCGCG TTCTACGCCA CCTTGCCCAG CCCGGCGGCG 551 GCTCTGACAT GGCTACACCA TTAGGCCCTG CCAGCTCCCT GCCCCAGAGC 601 TTCCTGCTCA AGTCTTTAGA GCAAGTGAGG AAGATCCAGG GCGATGGCGC 651 AGCGCTCCAG GAGAAGCTGT GTGCCACCTA CAAGCTGTGC CACCCCGAGG 701 AGCTGGTGCT GCTCGGACAC TCTCTGGGCA TCCCCTGGGC TCCCCTGAGC 751 TCCTGCCCCA GCCAGGCCCT GCAGCTGGCA GGCTGCTTGA GCCAACTCCA 801 TAGCGGCCTT TTCCTCTACC AGGGGCTCCT GCAGGCCCTG GAAGGGATAT 851 CCCCCGAGTT GGGTCCCACC TTGGACACAC TGCAGCTGGA CGTCGCCGAC 901 TTTGCCACCA CCATCTGGCA GCAGATGGAA GAACTGGGAA TGGCCCCTGC 951 CCTGCAGCCC ACCCAGGGTG CCATGCCGGC CTTCGCCTAA TAA; 1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG (SEQ ID NO: 158) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA 151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC 401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT GTCTATGGCC 451 CCTGCCCTGC AGCCCACCCA GGGTGCCATG CCGGCCTTCG CCTCTGCTTT 501 CCAGCGCCGG GCAGGAGGGG TCCTGGTTGC TAGCCATCTG CAGAGCTTCC 551 TGGAGGTGTC GTACCGCGTT CTACGCCACC TTGCGCAGCC CGGCGGCGGC 601 TCTGACATGG CTACACCATT AGGCCCTGCC AGCTCCCTGC CCCAGAGCTT 651 CCTGCTCAAG TCTTTAGAGC AAGTGAGGAA GATCCAGGGC GATGGCGCAG 701 CGCTCCAGGA GAAGCTGTGT GCCACCTACA AGCTGTGCCA CCCCGAGGAG 751 CTGGTGCTGC TCGGACACTC TCTGGGCATC CCCTGGGCTC CCCTGAGCTC 801 CTGCCCCAGC CAGGCCCTGC AGCTGGCAGG CTGCTTGAGC CAACTCCATA 851 GCGGCCTTTT CCTCTACCAG GGGCTCCTGC AGGCCCTGGA AGGGATATCC 901 CCCGAGTTGG GTCCCACCTT GGACACACTG CAGCTGGACG TCGCCGACTT 951 TGCCACCACC ATCTGGCAGC AGATGGAAGA ACTGGGATAA TAA; 1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG (SEQ ID NO: 159) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA 151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC 401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT GTCTACCCAG 451 GGTGCCATGC CGGCCTTCGC CTCTGCTTTC CAGCGCCGGG CAGGAGGGGT 501 CCTGGTTGCT AGCCATCTGC AGAGCTTCCT GGAGGTGTCG TACCGCGTTC 551 TACGCCACCT TGCGCAGCCC GGCGGCGGCT CTGACATGGC TACACCATTA 601 GGCCCTGCCA GCTCCCTGCC CCAGAGCTTC CTGCTCAAGT CTTTAGAGCA 651 AGTGAGGAAG ATCCAGGGCG ATGGCGCAGC GCTCCAGGAG AAGCTGTGTG 701 CCACCTACAA GCTCTGCCAC CCCGAGGAGC TGGTGCTGCT CGGACACTCT 751 CTGGGCATCC CCTGGGCTCC CCTGAGCTCC TGCCCCAGCC AGGCCCTGCA 801 GCTGGCAGGC TGCTTGAGCC AACTCCATAG CGGCCTTTTC CTCTACCAGG 851 GGCTCCTGCA GGCCCTGGAA GGGATATCCC CCGAGTTGGG TCCCACCTTG 901 GACACACTGC AGCTGGACGT CGCCGACTTT GCCACCACCA TCTGGCAGCA 951 GATGGAAGAA CTGGGAATGG CCCCTGCCCT GCAGCCCTAA TAA; GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACCACCTGCACCT (SEQ ID NO: 124) TTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTATCCTGATGGACCGAAACCTT CGACTTCCAAACCTGGAGAGCTTCGTAAGGGCTGTCAAGAACTTAGAAAATGCATCAGGT ATTGAGGCAATTCTTCGTAATCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCT CGACATCCAATCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGGTGGAGGCTCC CCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGTCTCCTCCGTCTAAAGAATCT CATAAATCTCCAAACATGGGACCCACTTGCCTCTCATCCCTCCTGGGGCAGCTTTCTGGA CAGGTCCGTCTCCTCCTTGGGGCCCTGCAGAGCCTCCTTGGAACCCAGCTTCCTCCACAG GGCAGGACCACAGCTCACAAGGATCCCAATGCCATCTTCCTGAGCTTCCAACACCTGCTC CGAGGAAAGGTGCGTTTCCTGATGCTTGTAGGAGGGTCCACCCTCTGCGTCAGGGAATTC GGCGGCAACATGGCGTCTCCGGCGCCGCCTGCTTGTGACCTCCGAGTCCTCAGTAAACTG CTTCGTGACTCCCATGTCCTTCACAGCAGACTGACCCAGTGCCCAGAGGTTCACCCTTTG CCTACACCTGTCCTGCTGCCTGCTGTGGACTTTAGCTTGGGAGAATGGAAAACCCAGATG GAGGAGACCAAGGCACAGGACATTCTGGGAGCAGTGACCCTTCTGCTGGAGGGAGTGATG GCAGCACGGGGACAACTG; GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACCACCTGCACCT (SEQ ID NO: 125) TTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTATCCTGATGGACCGAAACCTT CGACTTCCAAACCTGGAGAGCTTCGTAAGGGCTGTCAAGAACTTAGAAAATGCATCAGGT ATTGAGGCAATTCTTCGTAATCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCT CGACATCCAATCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGGTGGAGGCTCC CCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGTCTCCTCCGTCTAAAGAATCT CATAAATCTCCAAACATGGGAACCCAGCTTCCTCCACAGGGCAGGACCACAGCTCACAAG GATCCCAATGCCATCTTCCTGAGCTTCCAACACCTGCTCCGAGGAAAGGTGCGTTTCCTG ATGCTTGTAGGAGGGTCCACCCTCTGCGTCAGGGAATTCGGCGGCAACATGGCGTCTCCG GCGCCGCCTGCTTGTGACCTCCGAGTCCTCAGTAAACTGCTTCGTGACTCCCATGTCCTT CACAGCAGACTGAGCCAGTGCCCAGAGGTTCACCCTTTGCCTACACCTGTCCTGCTGCCT GCTGTGGACTTTAGCTTGGGAGAATGGAAAACCCAGATGGAGGAGACCAAGGCACAGGAC ATTCTGGGAGCAGTGACCCTTCTGCTGGAGGGAGTGATGGCAGCACGGGGACAACTGGGA CCCACTTGCCTCTCATCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCCTCCTTGGG GCCCTGCAGAGCCTCCTT; GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACCACCTGCACCT (SEQ ID NO: 126) TTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTATCCTGATGGACCGAAACCTT CGACTTCCAAACCTGGAGAGCTTCGTAAGGGCTGTCAAGAACTTAGAAAATGCATCAGGT ATTGAGGCAATTCTTCGTAATCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCT CGACATCCAATCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGGTGGAGGCTCC CCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGTCTCCTCCGTCTAAAGAATCT CATAAATCTCCAAACATGGGCAGGACCACAGCTCACAAGGATCCCAATGCCATCTTCCTG AGCTTCCAACACCTGCTCCGAGGAAAGGTGCGTTTCCTGATGCTTGTAGGAGGGTCCACC CTCTGCGTCAGGGAATTCGCCGGCAACATGGCGTCTCCGGCGCCGCCTGCTTGTGACCTC CGAGTCCTCAGTAAACTGCTTCGTGACTCCCATGTCCTTCACAGCAGACTGAGCCAGTGC CCAGAGGTTCACCCTTTGCCTACACCTGTCCTGCTGCCTGCTGTCGACTTTAGCTTGGGA GAATGGAAAACCCAGATGGAGGAGACCAAGGCACAGGACATTCTGGGAGCAGTGACCCTT CTGCTGGAGGGAGTGATGGCAGCACGGGGACAACTGGGACCCACTTGCCTCTCATCCCTC CTGCGGCAGCTTTCTGGACAGGTCCGTCTCCTCCTTGGGGCCCTGCAGAGCCTCCTTGGA ACCCAGCTTCCTCCACAG; GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACCACCTGCACCT (SEQ ID NO: 127) TTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTATCCTGATGGACCGAAACCTT CGACTTCCAAACCTGGAGAGCTTCGTAAGGGCTGTCAAGATCTTAGAAAATGCATCAGGT ATTGAGGCAATTCTTCGTAATCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCT CGACATCCAATCATCATCAAGGCAGGTGACTGCCAAGAATTCCGGGAAAAACTGACGTTC TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGGTGGAGGCTCC CCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGTCTCCTCCGTCTAAAGAATCT CATAAATCTCCAAACATGGCTCACAAGGATCCCAATGCCATCTTCCTGAGCTTCCAACAC CTGCTCCGAGGAAAGGTGCGTTTCCTGATGCTTGTAGGAGGGTCCACCCTCTGCGTCAGG GAATTCGGCGGCAACATGGCGTCTCCGGCGCCGCCTGCTTGTGACCTCCGAGTCCTCAGT AAACTGCTTCGTGACTCCCATGTCCTTCACAGCAGACTGAGCCAGTGCCCAGAGGTTCAC CCTTTGCCTACACCTGTCCTGCTGCCTGCTGTGGACTTTAGCTTGGGAGAATGGAAAACC CAGATGGAGGAGACCAAGGCACAGGACATTCTGGGAGCAGTGACCCTTCTGCTGGAGGGA GTGATGGCAGCACGGGGACAACTGGGACCCACTTGCCTCTCATCCCTCCTGGGGCAGCTT TCTGGACAGGTCCGTCTCCTCCTTGGGGCCCTGCAGAGCCTCCTTGGAACCCACCTTCCT CCACAGGGCAGGACCACA; GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACCACCTGCACCT (SEQ ID NO: 128) TTGCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTATCCTGATGGACCGAAACCTT CGACTTCCAAACCTGGAGAGCTTCGTAAGGGCTGTCAAGAACTTAGAAAATGCATCAGGT ATTGAGGCAATTCTTCGTAATCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCT CGACATCCAATCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTC TATCTGGTTACCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGGTGGAGGCTCC CCGGGTGAACCGTCTGGTCCAATCTCTACTATCAACCCGTCTCCTCCGTCTAAAGAATCT CATAAATCTCCAAACATGGATCCCAATGCCATCTTCCTGAGCTTCCAACACCTGCTCCGA GGAAAGGTGCGTTTCCTGATGCTTGTAGGAGGGTCCACCCTCTGCGTCAGGGAATTCGGC GGCAACATGGCGTCTCCGGCGCCGCCTGCTTGTGACCTCCGAGTCCTCAGTAAACTGCTT CGTGACTCCCATCTCCTTCACAGCAGACTGAGCCAGTGCCCAGAGGTTCACCCTTTGCCT ACACCTGTCCTGCTGCCTGCTGTGGACTTTAGCTTGGGAGAATGGAAAACCCAGATGGAG GAGACCAAGGCACAGGACATTCTGGGAGCAGTGACCCTTCTGCTGGAGGGAGTGATGGCA GCACGGGGACAACTGGGACCCACTTGCCTCTCATCCCTCCTGGGGCAGCTTTCTGGACAG GTCCGTCTCCTCCTTGGGGCCCTGCAGAGCCTCCTTGGAACCCAGCTTCCTCCACAGGGC AGGACCACAGCTCACAAG; 1 ATGGCTAACT GCTCTAACAT GATCGATGAA ATCATCACCC ACCTGAAGCA (SEQ ID NO: 114) 51 GCCACCGCTG CCGCTGCTGG ACTTCAACAA CCTCAATGGT GAAGACCAAG 101 ATATCCTAAT GGACAATAAC CTTCGTCGTC CAAACCTCGA GGCATTCAAC 151 CGTGCTGTCA AGTCTCTGCA GAATGCATCA GCAATTGAGA GCATTCTTAA 201 AAATCTCCTG CCATGTCTGC CGCTAGCCAC GGCCGCACCC ACGCGACATC 251 CAATCCATAT CAAGGACGGT GACTGGAATG AATTCCGTCG TAAACTGACC 301 TTCTATCTGA AAACCTTGGA GAACGCGCAG GCTCAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC 401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT GGCTACCCAG 451 GGTGCCATGC CGGCCTTCGC CTCTGCTTTC CAGCGCCGGG CAGGAGGGGT 501 CCTGGTTGCT AGCCATCTGC AGAGCTTCCT GGAGGTGTCG TACCGCGTTC 551 TACGCCACCT TGCGCAGCCC TCTGGCGGCT CTGGCGGCTC TCAGAGCTTC 601 CTGCTCAAGT CTTTAGAGCA AGTGAGAAAG ATCCAGGGCG ATGGCGCAGC 651 GCTCCAGGAG AAGCTGTGTG CCACCTACAA GCTGTGCCAC CCCGAGGAGC 701 TGGTGCTGCT CGGACACTCT CTGGGCATCC CCTGGGCTCC CCTGAGCTCC 751 TGCCCCAGCC AGGCCCTGCA GCTGGCAGGC TGCTTGAGCC AACTCCATAG 801 CGGCCTTTTC CTCTACCAGG GGCTCCTGCA GGCCCTGGAA GGGATATCCC 851 CCGAGTTGGG TCCCACCTTG GACACACTGC AGCTGGACGT CGCCGACTTT 901 GCCACCACCA TCTGGCAGCA GATGGAAGAA CTGGGAATGG CCCCTGCCCT 951 GCAGCCCTAA TAA; 1 ATGGCTAACT GCTCTAACAT GATCGATGAA ATCATCACCC ACCTGAAGCA (SEQ ID NO: 115) 51 GCCACCGCTG CCGCTGCTGG ACTTCAACAA CCTCAATGGT GAAGACCAAG 101 ATATCCTGAT GGAAAATAAC CTTCGTCGTC CAAACCTCGA GGCATTCAAC 151 CGTGCTGTCA AGTCTCTGCA GAATGCATCA GCAATTGAGA GCATTCTTAA 201 AAATCTCCTG CCATGTCTGC CCCTGGCCAC GGCCGCACCC ACGCGACATC 251 CAATCATCAT CCGTGACGGT GACTGGAATG AATTCCGTCG TAAACTGACC 301 TTCTATCTGA AAACCTTGGA GAACGCGCAG GCTCAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC 401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT GGCTACCCAG 451 GGTGCCATGC CGGCCTTCGC CTCTGCTTTC CAGCGCCGGG CAGGAGGGGT 501 CCTGGTTGCT AGCCATCTGC AGAGCTTCCT GGAGGTGTCG TACCGCGTTC 551 TACGCCACCT TGCGCAGCCC ACACCATTGG GCCCTGCCAG CTCCCTGCCC 601 CAGAGCTTCC TGCTCAAGTC TTTAGAGCAA GTGAGAAAGA TCCAGGGCGA 651 TGGCGCAGCG CTCCAGGAGA AGCTGTGTGC CACCTACAAG CTGTGCCACC 701 CCGAGGAGCT GGTGCTGCTC GGACACTCTC TGGGCATCCC CTGGGCTCCC 751 CTGAGCTCCT GCCCCAGCCA GGCCCTGCAG CTGGCAGGCT GCTTGAGCCA 801 ACTCCATAGC GGCCTTTTCC TCTACCAGGG GCTCCTGCAG GCCCTGGAAG 851 GGATATCCCC CGAGTTGGGT CCCACCTTGG ACACACTGCA GCTGGACGTC 901 GCCGACTTTG CCACCACCAT CTGGCAGCAG ATGGAAGAAC TGGGAATGGC 951 CCCTGCCCTG CAGCCCTAAT AA; 1 ATGGCTAACT GCTCTAACAT GATCGATGAA ATCATCACCC ACCTGAAGCA (SEQ ID NO: 116) 51 GCCACCGCTG CCGCTGCTGG ACTTCAACAA CCTCAATGGT GAAGACCAAG 101 ATATCCTGAT GGAAAATAAC CTTCGTCGTC CAAACCTCGA GGCATTCAAC 151 CGTGCTGTCA AGTCTCTGCA GAATGCATCA GCAATTGAGA GCATTCTTAA 201 AAATCTCCTG CCATGTCTGC CCCTGGCCAC GGCCGCACCC ACGCGACATC 251 CAATCATCAT CCGTGACGCT GACTGGAATG AATTCCGTCG TAAACTGACC 301 TTCTATCTGA AAACCTTGGA GAACGCGCAG GCTCAACAGT ACGTAGAGGG 351 CGGTGGAGCC TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC 401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT GGCTACCCAG 451 GGTGCCATGC CGGCCTTCGC CTCTGCTTTC CAGCGCCGGG CAGGAGGGGT 501 CCTGGTTGCT AGCCATCTGC AGAGCTTCCT GGAGGTGTCG TACCGCGTTC 551 TACGCCACCT TGCGCAGCCC TCTGGCGGCT CTGGCGGCTC TCAGAGCTTC 601 CTGCTCAAGT CTTTAGAGCA AGTGAGAAAG ATCCAGGGCG ATGGCGCAGC 651 GCTCCAGGAG AAGCTGTGTG CCACCTACAA GCTGTGCCAC CCCGAGGAGC 701 TGGTGCTGCT CGGACACTCT CTGGGCATCC CCTGGGCTCC CCTGAGCTCC 751 TGCCCCAGCC AGGCCCTGCA GCTGGCAGGC TGCTTGAGCC AACTCCATAG 801 CGGCCTTTTC CTCTACCAGG GGCTCCTGCA GGCCCTGGAA GGGATATCCC 851 CCGAGTTGGG TCCCACCTTG GACACACTGC AGCTGGACGT CGCCGACTTT 901 GCCACCACCA TCTGGCAGCA GATGGAAGAA CTGGGAATGG CCCCTGCCCT 951 GCAGCCCTAA TAA; 1 ATGGCTAACT GCTCTAACAT GATCGATGAA ATCATCACCC ACCTGAAGCA (SEQ ID NO: 117) 51 GCCACCGCTG CCGCTGCTGG ACTTCAACAA CCTCAATGGT GAAGACCAAG 101 ATATCCTAAT GGACAATAAC CTTCGTCGTC CAAACCTCGA GGCATTCAAC 151 CGTGCTGTCA AGTCTCTGCA GAATGCATCA GCAATTGAGA GCATTCTTAA 201 AAATCTCCTG CCATGTCTGC CGCTAGCCAC GGCCGCACCC ACGCGACATC 251 CAATCCATAT CAAGGACGGT GACTGGAATG AATTCCGTCG TAAACTGACC 301 TTCTATCTGA AAACCTTGGA GAACGCGCAG GCTCAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC 401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT GGCTACCCAG 451 GGTGCCATGC CGGCCTTCGC CTCTGCTTTC CAGCGCCGGG CAGGAGGGGT 501 CCTGGTTGCT AGCCATCTGC AGAGCTTCCT GGAGGTGTCG TACCGCGTTC 551 TACGCCACCT TGCGCAGCCC ACACCATTGG GCCCTGCCAG CTCCCTGCCC 601 CAGAGCTTCC TGCTCAAGTC TTTAGAGCAA GTGAGAAAGA TCCAGGGCGA 651 TGGCGCAGCG CTCCAGGAGA AGCTGTGTGC CACCTACAAG CTGTGCCACC 701 CCGAGGAGCT GGTGCTGCTC GGACACTCTC TGGGCATCCC CTGGGCTCCC 751 CTGAGCTCCT GCCCCAGCCA GGCCCTGCAG CTGGCAGGCT GCTTGAGCCA 801 ACTCCATAGC GGCCTTTTCC TCTACCAGGG GCTCCTGCAG GCCCTGGAAG 851 GGATATCCCC CGAGTTGGGT CCCACCTTGG ACACACTGCA GCTGGACGTC 901 GCCGACTTTG CCACCACCAT CTGGCAGCAG ATGGAAGAAC TGGGAATGGC 951 CCCTGCCCTG CAGCCCTAAT AA; 1 ATGGCTCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT (SEQ ID NO: 86) 51 GGACCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA 101 AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG TAATCTCCAA 151 CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC CAATCATCAT 201 CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG TTCTATCTGG 251 TTACCCTTGA GCAAGCGCAG GAACAACAGG GTGGTGGCTC TAACTGCTCT 301 ATAATGATCG ATGAAATTAT ACATCACTTA AAGAGACCAC CTGCACCTTT 351 GTACGTAGAG GGCGGTGGAG GCTCCCCGGG TGAACCGTCT GGTCCAATCT 401 CTACTATCAA CCCGTCTCCT CCGTCTAAAG AATCTCATAA ATCTCCAAAC 451 ATGGCTACCC AGGGTGCCAT GCCGGCCTTC GCCTCTGCTT TCCAGCGCCG 501 GGCAGGAGGG GTCCTGGTTG CTAGCCATCT GCAGAGCTTC CTGGAGGTGT 551 CGTACCGCGT TCTACGCCAC CTTGCGCAGC CCTCTGGCGG CTCTGGCGGC 601 TCTCAGAGCT TCCTGCTCAA GTCTTTAGAG CAAGTGAGAA AGATCCAGGG 651 CGATGGCGCA GCGCTCCAGG AGAAGCTGTG TGCCACCTAC AAGCTGTGCC 701 ACCCCGAGGA GCTGGTGCTG CTCGGACACT CTCTGGGCAT CCCCTGGGCT 751 CCCCTGAGCT CCTGCCCCAG CCAGGCCCTG CAGCTGGCAG GCTGCTTGAG 801 CCAACTCCAT AGCGGCCTTT TCCTCTACCA GGGGCTCCTG CAGGCCCTGG 851 AAGGGATATC CCCCGAGTTG GGTCCCACCT TGGACACACT GCAGCTGGAC 901 GTCGCCGACT TTGCCACCAC CATCTGGCAG CAGATGGAAG AACTGGGAAT 951 GGCCCCTGCC CTGCAGCCCT AATAA; 1 ATGGCTAATG CATCAGGTAT TGAGGCAATT CTTCGTAATC TCCAACCATG (SEQ ID NO: 87) 51 TCTGCCCTCT GCCACGGCCG CACCCTCTCG ACATCCAATC ATCATCAAGG 101 CAGGTGACTG GCAAGAATTC CGGGAAAAAC TGACGTTCTA TCTGGTTACC 151 CTTGAGCAAG CGCAGGAACA ACAGGGTGGT GGCTCTAACT GCTCTATAAT 201 GATCGATGAT ATTATACATC ACTTAAAGAG ACCACCTGCA CCTTTGCTGG 251 ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT GGACCGAAAC 301 CTTCGACTTC CAAACCTGGA GAGCTTCGTA AGGGCTGTCA AGAACTTAGA 351 ATACGTAGAG GGCGGTGGAG GCTCCCCGGG TGAACCGTCT GGTCCAATCT 401 CTACTATCAA CCCGTCTCCT CCGTCTAAAG AATCTCATAA ATCTCCAAAC 451 ATGGCTACCC AGGGTGCCAT GCCGGCCTTC GCCTCTGCTT TCCAGCGCCG 501 GGCAGGAGGG GTCCTGGTTG CTAGCCATCT GCAGAGCTTC CTGGAGGTGT 551 CGTACCGCGT TCTACGCCAC CTTGCGCAGC CCTCTGGCGG CTCTGGCGGC 601 TCTCAGAGCT TCCTGCTCAA GTCTTTAGAG CAAGTGAGAA AGATCCAGGG 651 CGATGGCGCA GCGCTCCAGG AGAAGCTGTG TGCCACCTAC AAGCTGTGCC 701 ACCCCGAGGA GCTGGTGCTG CTCGGACACT CTCTGGGCAT CCCCTGGGCT 751 CCCCTGAGCT CCTGCCCCAG CCAGGCCCTG CAGCTGGCAG GCTGCTTGAG 801 CCAACTCCAT AGCGGCCTTT TCCTCTACCA GGGGCTCCTG CAGGCCCTGG 851 AAGGGATATC CCCCGAGTTG GGTCCCACCT TGGACACACT GCAGCTGGAC 901 GTCGCCGACT TTGCCACCAC CATCTGGCAG CAGATGGAAG AACTGGGAAT 951 GGCCCCTGCC CTGCAGCCCT AATAA; 1 ATGGCTGCAC CCTCTCGACA TCCAATCATC ATCAAGGCAG GTGACTGGCA (SEQ ID NO: 88) 51 AGAATTCCGG GAAAAACTGA CGTTCTATCT GGTTACCCTT GAGCAAGCGC 101 AGGAACAACA GGGTGGTGGC TCTAACTGCT CTATAATGAT CGATGAAATT 151 ATACATCACT TAAAGAGACC ACCTGCACCT TTGCTGGACC CGAACAACCT 201 CAATGACGAA GACGTCTCTA TCCTGATGGA CCGAAACCTT CGACTTCCAA 251 ACCTGGAGAG CTTCGTAAGG GCTGTCAAGA ACTTAGAAAA TGCATCAGGT 301 ATTGAGGCAA TTCTTCGTAA TCTCCAACCA TGTCTGCCCT CTGCCACGGC 351 CTACGTAGAG GGCGGTGGAG GCTCCCCGGG TGAACCGTCT GGTCCAATCT 401 CTACTATCAA CCCGTCTCCT CCGTCTAAAG AATCTCATAA ATCTCCAAAC 451 ATGGCTACCC AGGGTGCCAT GCCGGCCTTC GCCTCTGCTT TCCAGCGCCG 501 GGCAGGAGGG GTCCTGGTTG CTAGCCATCT GCAGAGCTTC CTGGAGGTGT 551 CGTACCGCGT TCTACGCCAC CTTGCGCAGC CCTCTGGCGC CTCTGGCGGC 601 TCTCAGAGCT TCCTGCTCAA GTCTTTAGAG CAAGTGAGAA AGATCCAGGG 651 CGATCGCGCA GCGCTCCAGG AGAAGCTGTG TGCCACCTAC AAGCTGTGCC 701 ACCCCGAGGA GCTGGTGCTG CTCGGACACT CTCTGGGCAT CCCCTGGGCT 751 CCCCTGAGCT CCTGCCCCAG CCAGGCCCTG CAGCTGGCAG GCTGCTTGAG 801 CCAACTCCAT AGCGGCCTTT TCCTCTACCA GGGGCTCCTG CAGGCCCTGG 851 AAGGGATATC CCCCCAGTTG GGTCCCACCT TGGACACACT GCAGCTGGAC 901 GTCGCCGACT TTGCCACCAC CATCTGGCAG CAGATGGAAG AACTGGGAAT 951 GGCCCCTGCC CTGCAGCCCT AATAA; 1 ATGGCTCTGC ACCCGAACAA CCTCAATGAC GAAGACGTCT CTATCCTGAT (SEQ ID NO: 90) 51 CGACCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCCTA AGGGCTCTCA 101 AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG TAATCTCCAA 151 CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC CAATCATCAT 201 CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG TTCTATCTGG 251 TTACCCTTGA GCAAGCGCAG GAACAACAGG GTGGTGGCTC TGGCGGTGGC 301 AGCGGCGGCG GTTCTAACTG CTCTATAATG ATCGATGAAA TTATACATCA 351 CTTAAAGAGA CCACCTGCAC CTTTGTACGT AGAGGGCGGT GGAGGCTCCC 401 CGGGTGAACC GTCTGGTCCA ATCTCTACTA TCAACCCGTC TCCTCCGTCT 451 AAAGAATCTC ATAAATCTCC AAACATGGCT ACCCAGGGTG CCATGCCGGC 501 CTTCGCCTCT GCTTTCCAGC GCCGGGCAGG AGGGGTCCTG GTTGCTAGCC 551 ATCTGCAGAG CTTCCTGGAG GTGTCGTACC GCGTTCTACG CCACCTTGCG 601 CAGCCCTCTG GCGGCTCTGG CGGCTCTCAG AGCTTCCTGC TCAAGTCTTT 651 AGAGCAAGTG AGAAAGATCC AGGGCGATGG CGCAGCGCTC CAGGAGAAGC 701 TGTGTGCCAC CTACAAGCTG TGCCACCCCG AGGAGCTGGT GCTGCTCGGA 751 CACTCTCTGG GCATCCCCTG GGCTCCCCTG AGCTCCTGCC CCAGCCAGGC 801 CCTGCAGCTG GCAGGCTGCT TGAGCCAACT CCATAGCGGC CTTTTCCTCT 851 ACCAGGGGCT CCTGCAGGCC CTGGAAGGGA TATCCCCCGA GTTGGGTCCC 901 ACCTTGGACA CACTGCAGCT GGACGTCGCC GACTTTGCCA CCACCATCTG 951 GCAGCAGATG GAAGAACTGG GAATGGCCCC TGCCCTGCAG CCCTAATAA; 1 ATGGCTAATG CATCAGGTAT TGAGGCAATT CTTCGTAATC TCCAACCATG (SEQ ID NO: 91) 51 TCTGCCCTCT GCCACGGCCG CACCCTCTCG ACATCCAATC ATCATCAAGG 101 CAGGTGACTG GCAAGAATTC CGGGAAAAAC TGACGTTCTA TCTGGTTACC 151 CTTGAGCAAG CGCAGGAACA ACAGGGTGGT GGCTCTGGCG GTGGCAGCGG 201 CGGCGGTTCT AACTGCTCTA TAATGATCGA TGAAATTATA CATCACTTAA 251 AGAGACCACC TGCACCTTTG CTGGACCCGA ACAACCTCAA TGACGAAGAC 301 CTCTCTATCC TGATGGACCG AAACCTTCGA CTTCCAAACC TGGAGAGCTT 351 CGTAAGGGCT GTCAAGAACT TAGAATACGT AGAGGGCGGT GGAGGCTCCC 401 CGGGTGAACC GTCTGGTCCA ATCTCTACTA TCAACCCGTC TCCTCCGTCT 451 AAAGAATCTC ATAAATCTCC AAACATGGCT ACCCAGGGTG CCATGCCGGC 501 CTTCGCCTCT GCTTTCCAGC GCCGGGCAGG AGGGGTCCTG GTTGCTACCC 551 ATCTGCAGAG CTTCCTGGAG GTGTCGTACC GCGTTCTACG CCACCTTGCG 601 CAGCCCTCTG GCGGCTCTGG CGGCTCTCAG AGCTTCCTGC TCAAGTCTTT 651 AGAGCAAGTG AGAAAGATCC ACGGCGATGG CGCAGCGCTC CAGGAGAAGC 701 TGTGTGCCAC CTACAAGCTG TGCCACCCCG AGGAGCTGGT GCTGCTCGGA 751 CACTCTCTGG GCATCCCCTG GGCTCCCCTG AGCTCCTGCC CCAGCCAGGC 801 CCTGCAGCTG GCAGGCTGCT TGAGCCAACT CCATAGCGGC CTTTTCCTCT 851 ACCAGGGGCT CCTGCAGGCC CTGGAAGGGA TATCCCCCGA GTTGGGTCCC 901 ACCTTGGACA CACTGCAGCT GGACGTCGCC GACTTTGCCA CCACCATCTG 951 GCAGCAGATG GAAGAACTGG CAATGGCCCC TGCCCTGCAG CCCTAATAA; GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACCACCTGCACCTTT (SEQ ID NO: 136) GCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTATCCTGATGGACCGAAACCTTCGAC TTCCAAACCTGGAGAGCTTCGTAAGGGCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAG CCAATTCTTCGTAATCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCC AATCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTCTATCTGGTTA CCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGGTGGAGGCTCCCCGGGTGAACCG TCTGGTCCAATCTCTACTATCAACCCGTCTCCTCCGTCTAAAGAATCTCATAAATCTCCAAA CATGGGACCCACTTGCCTCTCATCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCCTCC TTGGGGCCCTGCAGAGCCTCCTTGGAACCCAGCTTCCTCCACAGGGCAGGACCACAGCTCAC AAGGATCCCAATGCCATCTTCCTGAGCTTCCAACACCTGCTCCGAGGAAAGGTGCGTTTCCT GATGCTTGTAGGAGGGTCCACCCTCTGCGTCAGGGAATTCGGCAACATGGCGTCTCCCGCTC CGCCTGCTTGTGACCTCCGAGTCCTCAGTAAACTGCTTCGTGACTCCCATGTCCTTCACAGC AGACTGAGCCAGTGCCCAGAGGTTCACCCTTTGCCTACACCTGTCCTGCTGCCTGCTGTGGA CTTTACCTTGGGAGAATGGAAAACCCAGATGGAGGAGACCAAGGCACAGGACATTCTGGGAG CAGTGACCCTTCTGCTGGAGGGAGTGATGGCAGCACGGGGACAACTG; GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACCACCTGCACCTTT (SEQ ID NO: 137) GCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTATCCTGATGGACCGAAACCTTCGAC TTCCAAACCTGGAGAGCTTCGTAAGGGCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAG GCAATTCTTCGTAATCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCC AATCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTCTATCTGGTTA CCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGGTGGAGGCTCCCCGGGTGAACCG TCTGGTCCAATCTCTACTATCAACCCGTCTCCTCCGTCTAAAGAATCTCATAAATCTCCAAA CATGGGAACCCAGCTTCCTCCACAGGGCAGGACCACAGCTCACAAGGATCCCAATGCCATCT TCCTGAGCTTCCAACACCTGCTCCGAGGAAAGGTGCGTTTCCTGATGCTTGTAGGAGGGTCC ACCCTCTGCGTCAGGGAATTCGGCAACATGGCGTCTCCCGCTCCGCCTGCTTGTGACCTCCG AGTCCTCAGTAAACTGCTTCGTGACTCCCATGTCCTTCACAGCAGACTGAGCCAGTGCCCAG AGGTTCACCCTTTGCCTACACCTGTCCTGCTGCCTGCTGTGGACTTTAGCTTGGGAGAATGG AAAACCCAGATGGAGGAGACCAAGGCACAGGACATTCTGGGAGCAGTGACCCTTCTGCTGGA GGGAGTGATGGCAGCACGGGGACAACTGGGACCCACTTGCCTCTCATCCCTCCTGGGGCAGC TTTCTGGACAGGTCCGTCTCCTCCTTGGGGCCCTGCAGAGCCTCCTT; GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACCACCTGCACCTTT (SEQ ID NO: 148) GCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTATCCTGATGGACCGAAACCTTCGAC TTCCAAACCTGGAGAGCTTCGTAAGGGCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAG GCAATTCTTCGTAATCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCC AATCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTCTATCTGGTTA CCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGGTGGAGGCTCCCCGGGTGAACCG TCTGGTCCAATCTCTACTATCAACCCGTCTCCTCCGTCTAAAGAATCTCATAAATCTCCAAA CATGGGACCCACTTGCCTCTCATCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCCTCC TTGGGGCCCTGCAGAGCCTCCTTGGAACCCAGCTTCCTCCACAGGGCAGGACCACACCTCAC AAGGATCCCAATGCCATCTTCCTGAGCTTCCAACACCTGCTCCGAGGAAAGGTGCGTTTCCT GATGCTTGTAGGAGGGTCCACCCTCTGCGTCAGGGAATTCGGCGGCAACGGCGGCAACATGG CGTCCCCAGCGCCGCCTGCTTGTGACCTCCGAGTCCTCAGTAAACTGCTTCGTGACTCCCAT GTCCTTCACAGCAGACTGAGCCAGTGCCCAGAGGTTCACCCTTTGCCTACACCTGTCCTGCT GCCTGCTGTGGACTTTAGCTTGGGAGAATGGAAAACCCAGATGGAGGAGACCAAGGCACAGG ACATTCTGGGAGCAGTGACCCTTCTGCTGGAGGGAGTGATGGCAGCACGGGGACAACTG; GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACCACCTGCACCTTT (SEQ ID NO: 149) GCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTATCCTGATGGACCGAAACCTTCGAC TTCCAAACCTGGACAGCTTCGTAAGGGCTCTCAAGAACTTAGAAAATGCATCAGGTATTGAG GCAATTCTTCGTAATCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCC AATCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTCTATCTGGTTA CCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGGTGGAGGCTCCCCGGGTGAACCG TCTGGTCCAATCTCTACTATCAACCCGTCTCCTCCGTCTAAAGAATCTCATAAATCTCCAAA CATGGGAACCCAGCTTCCTCCACAGGGCAGGACCACAGCTCACAAGGATCCCAATGCCATCT TCCTGAGCTTCCAACACCTGCTCCGAGGAAAGGTGCGTTTCCTGATGCTTGTAGGAGGGTCC ACCCTCTGCGTCAGGGAATTCGGCGGCAACGGCGGCAACATGGCGTCCCCAGCGCCCCCTGC TTGTGACCTCCGAGTCCTCAGTAAACTGCTTCGTGACTCCCATGTCCTTCACAGCAGACTGA GCCAGTGCCCAGAGCTTCACCCTTTGCCTACACCTGTCCTGCTGCCTGCTGTGGACTTTAGC TTGGGAGAATGGAAAACCCAGATGGAGGAGACCAAGGCAGAGGACATTCTGGGAGCAGTGAC CCTTCTGCTGGAGGGAGTGATGGCAGCACGGGGACAACTGGGACCCACTTGCCTCTCATCCC TCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCCTCCTTGGGGCCCTGCAGAGCCTCCTT; GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACCACCTGCACCTTT (SEQ ID NO: 150) GCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTATCCTGATGGACCGAAACCTTCGAC TTCCAAACCTGGAGAGCTTCGTAAGGGCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAG GCAATTCTTCGTAATCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCC AATCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTCTATCTGGTTA CCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGGTGGAGGCTCCCCGGGTGAACCG TCTGGTCCAATCTCTACTATCAACCCGTCTCCTCCGTCTAAAGAATCTCATAAATCTCCAAA CATGGGCAGGACCACAGCTCACAAGGATCCCAATGCCATCTTCCTGAGCTTCCAACACCTGC TCCGAGGAAAGCTGCGTTTCCTGATGCTTGTAGGAGGGTCCACCCTCTGCGTCAGGGAATTC GGCGGCAACGGCGGCAACATGGCGTCCCCAGCGCCGCCTGCTTGTGACCTCCGAGTCCTCAG TAAACTGCTTCGTGACTCCCATGTCCTTCACAGCAGACTGAGCCAGTGCCCAGAGGTTCACC CTTTGCCTACACCTGTCCTGCTGCCTGCTGTGGACTTTAGCTTGGGAGAATGGAAAACCCAG ATGGAGGAGACCAAGGCACAGGACATTCTGGGAGCAGTGACCCTTCTGCTGGAGGGAGTGAT GGCAGCACGGGGACAACTGGGACCCACTTGCCTCTCATCCCTCCTGGGGCAGCTTTCTGGAC AGGTCCGTCTCCTCCTTGGGGCCCTGCAGAGCCTCCTTGGAACCCAGCTTCCTCCACAG; GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACCACCTGCACCTTT (SEQ ID NO: 151) GCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTATCCTGATGGACCGAAACCTTCGAC TTCCAAACCTGGAGAGCTTCGTAAGGGCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAG GCAATTCTTCGTAATCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCC AATCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTCTATCTGGTTA CCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGGTGGAGGCTCCCCGGGTGAACCG TCTGGTCCAATCTCTACTATCAACCCGTCTCCTCCGTCTAAAGAATCTCATAAATCTCCAAA CATGGCTCACAAGGATCCCAATGCCATCTTCCTGAGCTTCCAACACCTGCTCCGAGGAAAGG TGCGTTTCCTGATGCTTGTAGGAGGGTCCACCCTCTGCGTCAGGGAATTCGGCGGCAACGGC GGCAACATGGCGTCCCCAGCGCCGCCTGCTTGTGACCTCCGAGTCCTCAGTAAACTGCTTCG TGACTCCCATGTCCTTCACAGCAGACTGAGCCAGTGCCCAGAGGTTCACCCTTTGCCTACAC CTGTCCTGCTGCCTGCTGTGGACTTTAGCTTGGGAGAATGGAAAACCCAGATGGAGGAGACC AAGGCACAGGACATTCTGGGAGCAGTGACCCTTCTGCTGGAGGGAGTGATGGCAGCACGGGG ACAACTGGGACCCACTTGCCTCTCATCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCC TCCTTGGGGCCCTGCAGAGCCTCCTTGGAACCCAGCTTCCTCCACAGGGCAGGACCACA; GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACCACCTGCACCTTT (SEQ ID NO: 152) GCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTATCGTGATGGACCGAAACCTTCGAC TTCCAAACCTGGAGAGCTTCGTAAGGGCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAG GCAATTCTTCGTAATCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCC AATCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTCTATCTGGTTA CCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGGTGGAGGCTCCCCGGGTGAACCG TCTGGTCCAATCTCTACTATCAACCCGTCTCCTCCGTCTAAAGAATCTCATAAATCTCCAAA CATGGATCCCAATGCCATCTTCCTGAGCTTCCAACACCTGCTCCGAGGAAAGGTGCGTTTCC TGATGCTTGTAGGAGGGTCCACCCTCTGCGTCAGGGAATTCGGCGGCAACGGCGGCAACATG GCGTCCCCAGCGCCGCCTGCTTGTGACCTCCGAGTCCTCAGTAAACTGCTTCGTGACTCCCA TGTCCTTCACAGCAGACTGAGCCAGTGCCCAGAGGTTCACCCTTTGCCTACACCTGTCCTGC TGCCTGCTGTGGACTTTAGCTTGGGAGAATGGAAAACCCAGATGGAGGAGACCAAGGCACAG GACATTCTGGGAGCAGTGACCCTTCTGCTGGAGGGAGTGATGGCAGCACGGGGACAACTGGG ACCCACTTGCCTCTCATCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCCTCCTTGGGG CCCTGCAGAGCCTCCTTGGAACCCAGCTTCCTCCACAGGGCAGGACCACAGCTCACAAG; GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACCACCTGCACCTTT (SEQ ID NO: 153) GCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTATCCTGATGGACCGAAACCTTCGAC TTCCAAACCTGGAGAGCTTCGTAAGGGCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAG GCAATTCTTCGTAATCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCC AATCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTCTATCTGGTTA CCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGGTGGAGGCTCCCCGGGTGAACCG TCTGGTCCAATCTCTACTATCAACCCGTCTCCTCCGTCTAAAGAATCTCATAAATCTCCAAA CATGGCCATCTTCCTGAGCTTCCAACACCTGCTCCGAGGAAAGGTGCGTTTCCTGATGCTTG TAGGAGGGTCCACCCTCTGCGTCAGGGAATTCGGCGGCAACGGCGGCAACATGGCGTCCCCA GCGCCGCCTGCTTGTGACCTCCGAGTCCTCAGTAAACTGCTTCGTGACTCCCATGTCCTTCA CAGCAGACTGAGCCAGTGCCCAGAGGTTCACCCTTTGCCTACACCTGTCCTGCTGCCTGCTG TGGACTTTAGCTTGGGAGAATGGAAAACCCAGATGGAGGAGACCAAGGCACAGGACATTCTG GGAGCAGTGACCCTTCTGCTGGAGGGAGTGATGGCAGCACGGGGACAACTGCGACCCACTTG CCTCTCATCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCCTCCTTGGGGCCCTGCAGA GCCTCCTTGGAACCCAGCTTCCTCCACAGGGCAGGACCACAGCTCACAAGGATCCCAAT; GCTAACTGCTCTATAATGATCGATGAAATTATACATCACTTAAAGAGACCACCTGCACCTTT (SEQ ID NO: 154) GCTGGACCCGAACAACCTCAATGACGAAGACGTCTCTATCCTGATGGACCGAAACCTTCGAC TTCCAAACCTGGAGAGCTTCGTAAGGGCTGTCAAGAACTTAGAAAATGCATCAGGTATTGAG GCAATTCTTCGTAATCTCCAACCATGTCTGCCCTCTGCCACGGCCGCACCCTCTCGACATCC AATCATCATCAAGGCAGGTGACTGGCAAGAATTCCGGGAAAAACTGACGTTCTATCTGGTTA CCCTTGAGCAAGCGCAGGAACAACAGTACGTAGAGGGCGGTGGAGGCTCCCCGGGTGAACCG TCTGGTCCAATCTCTACTATCAACCCGTCTCCTCCGTCTAAAGAATCTCATAAATCTCCAAA CATGGATCCCAATGCCATCTTCCTGAGCTTCCAACACCTGCTCCGAGGAAAGGTGCGTTTCC TGATGCTTGTAGGAGGGTCCACCCTCTGCGTCAGGGAATTCGGCGGCAACATGGCGTCTCCC GCTCCGCCTGCTTGTGACCTCCGAGTCCTCAGTAAACTGCTTCGTGACTCCCATGTCCTTCA CAGCAGACTGAGCCAGTGCCCAGAGGTTCACCCTTTGCCTACACCTGTCCTGCTGCCTGCTG TGGACTTTAGCTTGGGAGAATGGAAAACCCAGATGGAGGAGACCAAGGCACAGGACATTCTG GGAGCAGTGACCCTTCTGCTGGAGGGAGTGATGGCAGCACGGGGACAACTGGGACCCACTTG CCTCTCATCCCTCCTGGGGCAGCTTTCTGGACAGGTCCGTCTCCTCCTTGGGGCCCTGCAGA GCCTCCTTGGAACCCAGGGCAGGACCACAGCTCACAAG; 1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG (SEQ ID NO: 259) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA 151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC 401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT GGCTTTAGGC 451 CCTGCCAGCT CCCTGCCCCA GAGCTTCCTG CTCAAGTCTT TAGAGCAAGT 501 GAGGAAGATC CAGGGCGATG GCGCAGCGCT CCAGGAGAAG CTGTGTGCCA 551 CCTACAAGCT GTGCCACCCC GAGGAGCTGG TGCTGCTCGG ACACTCTCTG 601 GGCATCCCCT GGGCTCCCCT GAGCTCCTGC CCCAGCCAGG CCCTGCAGCT 651 GGCAGGCTGC TTGAGCCAAC TCCATAGCGG CCTTTTCCTC TACCAGGGGC 701 TCCTGCAGGC CCTGGAAGGG ATATCCCCCG AGTTGGGTCC CACCTTGGAC 751 ACACTGCAGC TGGACGTCGC CGACTTTGCC ACCACCATCT GGCAGCAGAT 801 GGAAGAACTG GGAATGGCCC CTGCCCTGCA GCCCACCCAG GGTGCCATGC 851 CGGCCTTCGC CTCTGCTTTC CAGCGCCGGG CAGGAGGGGT CCTGGTTGCT 901 AGCCATCTGC AGAGCTTCCT GGAGGTGTCG TACCGCGTTC TACGCCACCT 951 TGCGCAGCCC GACATGGCTA CACCA; 1 ATGGCTAACT GCTCTATAAT GATCCATGAA ATTATACATC ACTTAAAGAG (SEQ ID NO: 260) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA 151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC 401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT GGCTCAGAGC 451 TTCCTGCTCA AGTCTTTAGA GCAAGTGAGG AAGATCCAGG CCGATGGCGC 501 AGCGCTCCAG GAGAAGCTGT GTGCCACCTA CAAGCTGTGC CACCCCGAGG 551 AGCTGGTGCT GCTCGGACAC TCTCTGGGCA TCCCCTGGGC TCCCCTGAGC 601 TCCTGCCCCA GCCAGGCCCT GCAGCTGGCA GGCTGCTTGA GCCAACTCCA 651 TAGCGGCCTT TTCCTCTACC AGGGGCTCCT GCAGGCCCTG GAAGGGATAT 701 CCCCCGAGTT CGGTCCCACC TTGGACACAC TGCAGCTGGA CGTCGCCGAC 751 TTTGCCACCA CCATCTGGCA GCAGATGGAA GAACTGGGAA TGGCCCCTGC 801 CCTGCAGCCC ACCCAGGGTG CCATGCCGGC CTTCGCCTCT GCTTTCCAGC 851 GCCGGGCAGG AGGGGTCCTG GTTGCTAGCC ATCTGCAGAG CTTCCTGGAG 901 GTGTCGTACC GCGTTCTACG CCACCTTGCG CAGCCCGACA TGGCTACACC 951 ATTAGGCCCT GCCAGCTCCC TGCCC; 1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG (SEQ ID NO: 261) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA 151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC 401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT GGCTTTCCTG 451 CTCAAGTCTT TAGAGCAAGT GAGGAAGATC CAGGGCGATG GCGCAGCGCT 501 CCAGGAGAAG CTGTGTGCCA CCTACAAGCT GTGCCACCCC GAGGAGCTGG 551 TGCTGCTCGG ACACTCTCTG GGCATCCCCT GGGCTCCCCT GAGCTCCTGC 601 CCCAGCCAGG CCCTGCAGCT GGCAGGCTGC TTGAGCCAAC TCCATAGCGG 651 CCTTTTCCTC TACCAGGGCC TCCTGCAGGC CCTGGAAGGG ATATCCCCCG 701 AGTTGGGTCC CACCTTGGAC ACACTGCAGC TGGACGTCGC CGACTTTGCC 751 ACCACCATCT GGCAGCAGAT GGAAGAACTG GGAATGGCCC CTGCCCTGCA 801 GCCCACCCAG GGTGCCATGC CGGCCTTCGC CTCTGCTTTC CAGCGCCGGG 851 CAGGAGGGGT CCTGGTTGCT AGCCATCTGC AGAGCTTCCT GGAGGTGTCG 901 TACCGCGTTC TACGCCACCT TGCGCAGCCC GACATGGCTA CACCATTAGG 951 CCCTGCCAGC TCCCTGCCCC AGAGC; 1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG (SEQ ID NO: 262) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA 151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACACT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC 401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT GGCTGAGCAA 451 GTGAGGAAGA TCCAGGGCGA TGGCGCAGCG CTCCAGGAGA AGCTGTGTGC 501 CACCTACAAG CTGTGCCACC CCGAGGAGCT GGTGCTGCTC GGACACTCTC 551 TGGGCATCCC CTGGGCTCCC CTGAGCTCCT GCCCCAGCCA GGCCCTGCAG 601 CTGGCAGGCT GCTTGAGCCA ACTCCATAGC GGCCTTTTCC TCTACCAGGG 651 GCTCCTGCAG GCCCTGGAAG GGATATCCCC CGAGTTGGGT CCCACCTTGG 701 ACACACTGCA GCTGGACGTC GCCGACTTTG CCACCACCAT CTGGCAGCAG 751 ATGGAAGAAC TGGGAATGGC CCCTGCCCTG CAGCCCACCC AGGGTGCCAT 801 GCCGGCCTTC GCCTCTGCTT TCCAGCGCCG GGCAGGAGGG GTCCTGGTTG 851 CTAGCCATCT GCAGAGCTTC CTGGAGGTGT CGTACCGCGT TCTACGCCAC 901 CTTGCGCAGC CCGACATGGC TACACCATTA GGCCCTGCCA GCTCCCTGCC 951 CCAGAGCTTC CTGCTCAAGT CTTTA; 1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG (SEQ ID NO: 263) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA 151 AGGGCTCTCA AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC 401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT GGCTCTGCTC 451 GGACACTCTC TGGGCATCCC CTGGGCTCCC CTGAGCTCCT GCCCCAGCCA 501 GGCCCTGCAG CTGGCAGGCT GCTTGAGCCA ACTCCATAGC GGCCTTTTCC 551 TCTACCAGGG GCTCCTGCAG GCCCTGGAAG GGATATCCCC CGAGTTGGGT 601 CCCACCTTGG ACACACTGCA GCTGGACGTC GCCGACTTTG CCACCACCAT 651 CTGGCAGCAG ATGGAAGAAC TGGGAATGGC CCCTGCCCTG CAGCCCACCC 701 AGGGTGCCAT GCCGGCCTTC GCCTCTGCTT TCCAGCGCCG GGCAGGAGGG 751 GTCCTGGTTG CTAGCCATCT GCAGAGCTTC CTGGAGGTGT CGTACCGCGT 801 TCTACGCCAC CTTGCGCAGC CCGACATGGC TACACCATTA GGCCCTGCCA 851 GCTCCCTGCC CCAGAGCTTC CTGCTCAAGT CTTTAGAGCA AGTGAGGAAG 901 ATCCAGGGCG ATGGCGCAGC GCTCCAGGAG AAGCTGTGTG CCACCTACAA 951 GCTGTGCCAC CCCGAGGAGC TGGTG; 1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG (SEQ ID NO: 264) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA 151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC 401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT GGCTCCCCTG 451 AGCTCCTGCC CCAGCCAGGC CCTGCAGCTG GCAGGCTGCT TGAGCCAACT 501 CCATAGCGGC CTTTTCCTCT ACCAGGGGCT CCTGCAGGCC CTGGAAGGGA 551 TATCCCCCGA GTTGGGTCCC ACCTTGGACA CACTGCAGCT GGACGTCGCC 601 GACTTTGCCA CCACCATCTG GCAGCAGATG GAAGAACTGG GAATGGCCCC 651 TGCCCTGCAG CCCACCCAGG GTGCCATGCC GGCCTTCGCC TCTGCTTTCC 701 AGCGCCGGGC AGGAGGGGTC CTGGTTGCTA GCCATCTGCA GAGCTTCCTG 751 GAGGTGTCGT ACCGCGTTCT ACGCCACCTT GCGCAGCCCG ACATGGCTAC 801 ACCATTAGGC CCTGCCAGCT CCCTGCCCCA GAGCTTCCTG CTCAAGTCTT 851 TAGAGCAAGT GAGGAAGATC CAGGGCGATG GCGCAGCGCT CCAGGAGAAG 901 CTGTGTGCCA CCTACAAGCT GTGCCACCCC GAGGAGCTGG TGCTGCTCGG 951 ACACTCTCTG GGCATCCCCT GGGCT; 1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG (SEQ ID NO: 265) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA 151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC 401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT GGCTCAGGCC 451 CTGCAGCTGG CAGGCTGCTT GAGCCAACTC CATAGCGGCC TTTTCCTCTA 501 CCAGGGGCTC CTGCAGGCCC TGGAAGGGAT ATCCCCCGAG TTGGGTCCCA 551 CCTTGGACAC ACTGCAGCTG GACGTCGCCG ACTTTGCCAC CACCATCTGG 601 CAGCAGATGG AAGAACTGGG AATGGCCCCT GCCCTGCAGC CCACCCAGGG 651 TGCCATGCCG GCCTTCGCCT CTGCTTTCCA GCGCCGGGCA GGAGGGGTCC 701 TGGTTGCTAG CCATCTGCAG AGCTTCCTGG AGGTGTCGTA CCGCGTTCTA 751 CGCCACCTTG CGCAGCCCGA CATGGCTACA CCATTAGGCC CTGCCAGCTC 801 CCTGCCCCAG AGCTTCCTGC TCAAGTCTTT AGAGCAAGTG AGGAAGATCC 851 AGGGCGATGG CGCAGCCCTC CAGGAGAAGC TGTGTGCCAC CTACAAGCTG 901 TGCCACCCCG AGGAGCTGGT GCTGCTCGGA CACTCTCTGG GCATCCCCTG 951 GGCTCCCCTG AGCTCCTGCC CCAGC; 1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG (SEQ ID NO: 266) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA 151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCAGGT GACTCGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTCG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC 401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT GGCTCTGCAG 451 CTGGCAGGCT GCTTGAGCCA ACTCCATAGC GGCCTTTTCC TCTACCAGGG 501 GCTCCTGCAG GCCCTGGAAG GGATATCCCC CGAGTTGGGT CCCACCTTGG 551 ACACACTGCA GCTGGACGTC GCCGACTTTG CCACCACCAT CTGGCAGCAG 601 ATGGAAGAAC TGGGAATGGC CCCTGCCCTG CAGCCCACCC AGGGTGCCAT 651 GCCGGCCTTC GCCTCTGCTT TCCAGCGCCG GGCAGGAGGG GTCCTGGTTG 701 CTAGCCATCT GCAGAGCTTC CTGGAGGTGT CGTACCGCGT TCTACGCCAC 751 CTTGCGCAGC CCGACATGGC TACACCATTA GGCCCTCCCA GCTCCCTGCC 801 CCAGAGCTTC CTGCTCAAGT CTTTAGAGCA AGTGAGGAAG ATCCAGGGCG 851 ATGGCGCAGC GCTCCAGGAG AAGCTGTGTG CCACCTACAA GCTGTGCCAC 901 CCCGAGGAGC TGGTGCTGCT CGGACACTCT CTGGGCATCC CCTGGGCTCC 951 CCTGAGCTCC TGCCCCAGCC AGGCC; 1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG (SEQ ID NO: 267) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA 151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTGG TTACCCTTGA GCAACCGCAG GAACAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC 401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT GGCTCTGGCA 451 GGCTGCTTGA GCCAACTCCA TAGCGGCCTT TTCCTCTACC AGGGGCTCCT 501 GCAGGCCCTG GAAGGGATAT CCCCCGAGTT GGGTCCCACC TTGGACACAC 551 TGCAGCTGGA CGTCGCCGAC TTTGCCACCA CCATCTGGCA GCAGATGGAA 601 GAACTGGGAA TGGCCCCTGC CCTGCAGCCC ACCCAGGGTG CCATGCCGGC 651 CTTCGCCTCT GCTTTCCAGC GCCGGGCAGG AGGGGTCCTG GTTGCTAGCC 701 ATCTGCAGAG CTTCCTGGAG GTGTCGTACC GCGTTCTACG CCACCTTGCG 751 CAGCCCGACA TGGCTACACC ATTAGGCCCT GCCAGCTCCC TGCCCCAGAG 801 CTTCCTGCTC AAGTCTTTAG AGCAAGTGAG GAAGATCCAG GGCGATGGCG 851 CAGCGCTCCA GGAGAAGCTG TGTGCCACCT ACAAGCTGTG CCACCCCGAG 901 GAGCTGGTGC TGCTCGGACA CTCTCTGGGC ATCCCCTGGG CTCCCCTGAG 951 CTCCTGCCCC AGCCAGGCCC TGCAG; 1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG (SEQ ID NO: 268) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA 151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC 401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT GGCTGAACTG 451 GGAATGGCCC CTGCCCTGCA GCCCACCCAG GGTGCCATGC CGGCCTTCGC 501 CTCTGCTTTC CAGCGCCGGG CAGGAGGGGT CCTGGTTGCT AGCCATCTGC 551 AGAGCTTCCT GGAGGTGTCG TACCGCGTTC TACGCCACCT TGCGCAGCCC 601 GACATGGCTA CACCATTAGG CCCTGCCAGC TCCCTGCCCC AGAGCTTCCT 651 GCTCAAGTCT TTACAGCAAG TGAGGAAGAT CCAGGGCGAT GGCGCAGCGC 701 TCCAGGAGAA GCTGTGTGCC ACCTACAAGC TGTGCCACCC CGAGGAGCTG 751 GTGCTGCTCG GACACTCTCT GGGCATCCCC TGGGCTCCCC TGAGCTCCTG 801 CCCCAGCCAG GCCCTGCAGC TGGCAGGCTG CTTGAGCCAA CTCCATAGCG 851 GCCTTTTCCT CTACCAGGGG CTCCTGCAGG CCCTGGAAGG GATATCCCCC 901 GAGTTGGGTC CCACCTTGGA CACACTGCAG CTGGACGTCG CCGACTTTGC 951 CACCACCATC TGGCAGCAGA TGGAA; 1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG (SEQ ID NO: 269) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA 151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC 401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT GGCTGGAATG 451 GCCCCTGCCC TGCAGCCCAC CCAGGGTGCC ATGCCGGCCT TCGCCTCTGC 501 TTTCCAGCGC CGGGCAGGAG GGGTCCTGGT TGCTAGCCAT CTGCAGAGCT 551 TCCTGGAGGT GTCGTACCGC GTTCTACGCC ACCTTGCGCA GCCCGACATG 601 GCTACACCAT TAGGCCCTGC CAGCTCCCTG CCCCAGAGCT TCCTGCTCAA 651 GTCTTTAGAG CAAGTGAGGA AGATCCAGGG CGATGGCGCA GCGCTCCAGG 701 AGAAGCTGTG TGCCACCTAC AAGCTGTGCC ACCCCGAGGA GCTGGTGCTG 751 CTCGGACACT CTCTGGGCAT CCCCTGGGCT CCCCTGAGCT CCTGCCCCAG 801 CCAGGCCCTG CAGCTGGCAG GCTGCTTGAG CCAACTCCAT AGCGGCCTTT 851 TCCTCTACCA GGGGCTCCTG CAGGCCCTGG AAGGGATATC CCCCGAGTTG 901 GGTCCCACCT TGGACACACT GCAGCTGGAC GTCGCCGACT TTGCCACCAC 951 CATCTGGCAG CAGATGGAAG AACTG; and 1 ATGGCTAACT GCTCTATAAT GATCGATGAA ATTATACATC ACTTAAAGAG (SEQ ID NO: 270) 51 ACCACCTGCA CCTTTGCTGG ACCCGAACAA CCTCAATGAC GAAGACGTCT 101 CTATCCTGAT GGATCGAAAC CTTCGACTTC CAAACCTGGA GAGCTTCGTA 151 AGGGCTGTCA AGAACTTAGA AAATGCATCA GGTATTGAGG CAATTCTTCG 201 TAATCTCCAA CCATGTCTGC CCTCTGCCAC GGCCGCACCC TCTCGACATC 251 CAATCATCAT CAAGGCAGGT GACTGGCAAG AATTCCGGGA AAAACTGACG 301 TTCTATCTGG TTACCCTTGA GCAAGCGCAG GAACAACAGT ACGTAGAGGG 351 CGGTGGAGGC TCCCCGGGTG AACCGTCTGG TCCAATCTCT ACTATCAACC 401 CGTCTCCTCC GTCTAAAGAA TCTCATAAAT CTCCAAACAT GGCTAGCTTC 451 CTGGAGGTGT CGTACCGCGT TCTACGCCAC CTTGCGCAGC CCGACATGGC 501 TACACCATTA GGCCCTGCCA GCTCCCTGCC CCAGAGCTTC CTGCTCAAGT 551 CTTTAGAGCA AGTGAGGAAG ATCCAGGGCG ATGGCGCAGC GCTCCAGGAG 601 AAGCTGTGTG CCACCTACAA GCTGTGCCAC CCCCAGGAGC TGGTGCTGCT 651 CGGACACTCT CTGGGCATCC CCTGGGCTCC CCTGAGCTCC TGCCCCAGCC 701 AGGCCCTCCA GCTGGCAGGC TGCTTGAGCC AACTCCATAG CGGCCTTTTC 751 CTCTACCAGG GGCTCCTGCA GGCCCTGGAA GGGATATCCC CCGAGTTGGG 801 TCCCACCTTG GACACACTGC AGCTGGACGT CGCCGACTTT GCCACCACCA 851 TCTGGCAGCA GATGGAAGAA CTGGGAATGG CCCCTGCCCT GCAGCCCACC 901 CAGGGTGCCA TGCCGGCCTT CGCCTCTGCT TTCCAGCGCC GGGCAGGAGG 951 GGTCCTGGTT GCTAGCCATC TGCAG.
37. The nucleic acid molecule according to claim 34 selected from group consisting of:
1 ATGGCTGGAC CCACTTGCCT CTCATCCCTC CTGGGGCAGC TTTCTGGACA (SEQ ID NO:286) 51 GGTCCGTCTC CTCCTTGGGG CCCTGCAGAG CCTCCTTGGA ACCCAGCTTC 101 CTCCACAGGG CAGGACCACA GCTCACAAGG ATCCCAATGC CATCTTCCTG 151 AGCTTCCAAC ACCTGCTCCG AGGAAAGGTG CGTTTCCTGA TGCTTGTAGG 201 AGGGTCCACC CTCGCCGTCA GGGAATTCGG CGGCAACATG GCGTCTCCGG 251 CGCCGCCTGC TGCTGACCTC CGAGTCCTCA GTAAACTGCT TCGTGACTCC 301 CATGTCCTTC ACAGCAGACT GAGCCAGTGC CCAGAGGTTC ACCCTTTGCC 351 TACACCTGTC CTGCTGCCTG CTGTGGACTT TAGCTTGGGA GAATGGAAAA 401 CCCAGATGGA GGAGACCAAG GCACAGGACA TTCTGGGAGC AGTGACCCTT 451 CTGCTGGAGG GAGTGATGGC AGCACGGGGA CAACTG; and 1 ATGGCTGGCA GGACCACAGC TCACAAGGAT CCCAATGCCA TCTTCCTGAG (SEQ ID NO:287) 51 CTTCCAACAC CTGCTCCGAG GAAAGGTGCG TTTCCTGATG CTTGTAGGAG 101 GGTCCACCCT CGCCGTCAGG GAATTCGGCG GCAACATGGC GTCTCCGGCG 151 CCGCCTGCTG CTGACCTCCG AGTCCTCAGT AAACTGCTTC GTGACTCCCA 201 TGTCCTTCAC AGCAGACTGA GCCAGTGCCC AGAGGTTCAC CCTTTGCCTA 251 CACCTGTCCT GCTGCCTGCT GTGGACTTTA GCTTGGGAGA ATGGAAAACC 301 CAGATGGAGG AGACCAAGGC ACAGGACATT CTGGGAGCAG TGACCCTTCT 351 GCTGGAGGGA GTGATGGCAG CACGGGGACA ACTGGGACCC ACTTGCCTCT 401 CATCCCTCCT GGGGCAGCTT TCTGGACAGG TCCGTCTCCT CCTTGGGGCC 451 CTGCAGAGCC TCCTTGGAAC CCAGCTTCCT CCACAG.
38. A method of producing a hematopoietic protein comprising: growing under suitable nutrient conditions, a host cell transformed or transfected with a replicable vector comprising a nucleic acid molecule of claim 20, 21, 22, 23, 24, 25, 26, 27, 28, 30, 33, 34, 36 or 37 in a manner allowing expression of said hematopoietic protein and recovering said hematopoietic protein.
39. A pharmaceutical composition comprising; the hematopoietic protein according to claim 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 12, 15 or 16 and a pharmaceutically acceptable carrier.
40. A method of stimulating the production of hematopoietic cells in a patient comprising the step of; administering an effective amount of the hematopoietic protein as recited in claim 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 12, 15, or 16 to said patient.
41. A method of stimulating the production of hematopoietic cells in a patient comprising the step of administering an effective amount of the hematopoietic protein as recited in claim 13 to said patient.
42. A method for selective ex vivo expansion of stem cells, comprising the steps of:
(a) separating stem cells from other cells;
(b) culturing said separated stem cells with a selected culture medium-comprising; the hematopoietic protein of claim 1; and
(c) harvesting said cultured cells.
43. A method for treatment of a patient having a hematopoietic disorder, comprising the steps of:
(a) removing stem cells;
(b) separating stem cells from other cells;
(c) culturing said separated stem cells with a selected culture medium comprising; the hematopoietic protein of claim 1;
(d) harvesting said cultured cells; and
(e) transplanting said cultured cells into said patient.
44. A method of human gene therapy, comprising the steps of:
(a) removing stem cells from a patient;
(b) separating said stem cells from other cells;
(c) culturing said separated stem cells with a selected culture medium comprising; the hematopoietic protein of claim 1;
(d) introducing DNA into said cultured cells;
(e) harvesting said transduced cells; and
(f) transplanting said transduced cells into said patient.
45. A method of human gene therapy, comprising the steps of:
(a) removing stem cells from a patient;
(b) separating said stem cells from other cells;
(c) culturing said separated stem cells with a selected culture medium comprising; the hematopoietic protein of claim 1;
(d) introducing DNA into said cultured cells;
(e) harvesting said transduced cells; and
(f) transplanting said transduced cells into said patient.
46. A method of human gene therapy, comprising the steps of:
(a) removing stem cells from a patient;
(b) separating said stem cells from other cells;
(c) culturing said separated stem cells with a selected culture medium comprising; the hematopoietic protein of claim 11;
(d) introducing DNA into said cultured cells;
(e) harvesting said transduced cells; and
(f) transplanting said transduced cells into said patient.
47. A method of human gene therapy, comprising the steps of:
(a) removing stem cells from a patient;
(b) separating said stem cells from other cells;
(c) culturing said separated stem cells with a selected culture medium comprising; the hematopoietic protein of claim 11;
(d) introducing DNA into said cultured cells;
(e) harvesting said transduced cells; and
(f) transplanting said transduced cells into said patient.
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