FIELD OF THE INVENTION The present invention relates to human Erythropoietin (EPO) receptor agonists. These EPO receptor agonists retain one or more activities of native EPO and may also show improved hematopoietic cell-stimulating activity and/or an improved activity profile which may include reduction of undesirable biological activities associated with native EPO and/or have improved physical properties which may include increased solubility, stability and refold efficiency.

BACKGROUND OF THE INVENTION 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.

Erythropoietin is a naturally-occurring glycoprotein hormone with a molecular weight that was first reported to be approximately 39,000 daltons (T.

Miyaki et al., J. Biol. Chem. 252:5558-5564 (1977)).

The mature hormone is 166 amino acids long and the "prepro" form of the hormone, with its leader peptide, is 193 amino acids long (F. Lin, U.S. Patent No.

4,703,008). The mature hormone has a molecular weight, calculated from its amino acid sequence, of 18,399 daltons (K. Jacobs et al., Nature 313:806-810 (1985); J. K. Browne et al., Cold Spring Harbor Symp. Quant.

Biol. 5:1693-702 (1986).

The first mutant erythropoietins (i.e., erythropoietin analogs), prepared by making amino acid substitutions and deletions, have demonstrated reduced or unimproved activity. As described in U.S. Patent NO.

4,703,008, replacement of the tyrosine residues at positions 15, 40 and 145 with phenylalanine residues, replacement of the cysteine residue at position 7 with an histidine, substitution of the proline at position 2 with an asparagine, deletion of residues 2-6, deletion of residues 163-166, and deletion of residues 27-55 does not result in an apparent increase in biological activity. The Cys-to-His mutation eliminates biological activity. A series of mutant erythropoietins with a single amino acid substitution at asparagine residues 24, 38 or 83 show severely reduced activity (substitution at position 24) or exhibit rapid intracellular degradation and apparent lack of secretion (substitution at residue 38 or 183). Elimination of the O-linked glycosylation site at serinel26 results in rapid degradation or lack of secretion of the erythropoietin analog (S. Dube et al., J. Biol. Chem.

33:17516-17521 (1988). These authors conclude that glycosylation sites at residues 38, 83 and 126 are required for proper secretion and that glycosylation sites located at residues 24 and 38 may be involved in the biological activity of mature erythropoietin.

Deglycosylated erythropoietin is fully active in in vitro bioassays (M. S. Dorsdal et al., Endocrinology 116:2293-2299 (1985); U.S. Patent No. 4,703,008; E.

Tsuda et al., Eur J. Biochem. 266:20434-20439 (1991).

However, glycosylation of erythropoietin is widely accepted to play a critical role in the in vivo activity of the hormone (P. H.. Lowy et al., Nature 185:102-105 (1960); E. Goldwasser and C. K. H.. Kung, Ann. N.Y.

Acad. Science 149:49-53 (1968); W. A. Lukowsky and R.

H.. Painter, Can. J. Biochem. :909-917 (1972); D.W.

Briggs et al., Amer. J. Phys. 201:1385-1388 (1974); J.C.

Schooley, Exp. Hematol. 13:994-998; N. Imai et al., Eur.

J. Biochem. 194:457-462 (1990); M.S. Dordal et al., Endocrinology 116:2293-2299 (1985); E. Tsuda et al., Eur. J. Biochem. 188:405-411 (1990); U.S. Patent No.

4,703,008; J.K. Brown et al., Cold Spring Harbor Symposia on Quant. Biol. 51:693-702 (1986); and K.

Yamaguchi et al., J. Biol. Chem. 266:20434-20439 (1991).

The lack if in vivo biological activity of deglycosylated analogs of erythropoietin is attributed to a rapid clearance of the deglycosylated hormone from the circulation of treated animals. This view is supported by direct comparison of the plasma half-life of glycosylated and deglycosylated erythropoietin (J.C.

Spivak and B.B. Hoyans, Blood 73:90-99 (1989), and M.N.

Fukuda, et al., Blood 73:84-89 (1989).

Oligonucleotide-directed mutagenesis of erythropoietin glycosylation sites has effectively probed the function of glycosylation but has failed, as yet, to provide insight into an effective strategy for significantly improving the characteristics of the hormone for therapeutic applications.

A series of single amino acid substitution or deletion mutants have been constructed, involving amino acid residues 15, 24, 49, 76, 78, 83, 143, 145, 160, 162, 163, 164, 165 and 166. In these mutants are altered the carboxy terminus, the glycosylation sites, and the tyrosine residues of erythropoietin. The mutants have been administered to animals while monitoring hemoglobin, hematocrit and reticulocyte levels (EP No. 0 409 113). While many of these mutants retain in vivo biological activity, none show a significant increase in their ability to raise hemoglobin, hematocrit or

reticulocyte (the immediate precursor of an erythrocyte) levels when compared to native erythropoietin.

Another set of mutants has been constructed to probe the function of residues 99-119 (domain 1) and residues 111-129 (domain 2) (Y. Chern et al., Eur. J.

Biochem. 202:225-230 (1991)). The domain 1 mutants are rapidly degraded and inactive in an in vitro bioassay while the domain 2 mutants, at best, retain in vitro activity. These mutants also show no enhanced in vivo biological activity as compared to wild-type, human erythropoietin. These authors conclude that residues 99- 119 play a critical role in the structure of erythropoietin.

The human erythropoietin molecule contains two disulfide bridges, one linking the cysteine residues at positions 7 and 161, and a second connecting cysteines at positions 29 and 33 (P.H. Lai et al., J. Biol. Chem.

261:3116-3121 (1986)). Oligonucleotide-directed mutagenesis has been used to probe the function of the disulfide bridge linking cysteines 29 and 33 in human erythropoietin. The cysteine at position 33 has been converted to a proline residue, which, mimics the structure of murine erythropoietin at this residue. The resulting mutant has greatly reduced in vitro activity.

The loss of activity is so severe that the authors conclude that the disulfide bridge between residues 29 and 33 is essential for erythropoietin function (F.K.

Lin, Molecular and Cellular Aspects of Erythropoietin and Erythropoiesis, pp. 23-36, ed. I.N. Rich, Springer- Verlag, Berlin (1987)).

U.S. Patent No. 4,703,008 by Lin, F-K. (hereinafter referred to as "the '008 patent") speculates about a wide variety of modifications of EPO, including addition, deletion, and substitution analogs of EPO.

The '008 patent does not indicate that any of the suggested modifications would increase biological activity per se, although it is stated that deletion of glycosylation sites might increase the activity of EPO produced in yeast (See the '008 patent at column 37, lines 25-28). Also, the '008 patent speculates that EPO analogs which have one or more tyrosine residues replaced with phenylalanine may exhibit an increased or decreased receptor binding affinity.

Australian Patent Application No. AU-A-59145/90 by Fibi, M et al. also discusses a number of modified EPO proteins (EPO muteins) . It is generally speculated that the alteration of amino acids 10-55, 70-85, and 130-166 of EPO. In particular, additions of positively charged basic amino acids in the carboxyl terminal region are purported to increase the biological activity of EPO.

U.S. Patent No. 4,835,260 by Shoemaker, C.B.

discusses modified EPO proteins with amino acid substitutions of the methionine at position 54 and asparagine at position 38. Such EPO muteins are thought to have improved stability but are not proposed to exhibit any increase in biological activity relative to wild type EPO.

WO 91/05867 discloses analogs of human erythropoietin having a greater number of sites for carbohydrate attachment than human erythropoietin, such as EPO (Asn9), EPO (Asn125, Serf2), EPO (Thr12) , and EPO (Pro124, Thr125) WO 94 /24160 discloses erythropoietin muteins which have enhanced activity, specifically amino acid substitutions at positions 20, 49, 73, 140, 143, 146, 147 and 154.

WO 94/25055 discloses erythropoietin analogs, including EPO (X33, Cys139, des-Arg'66) and EPO (Cys139, des- Arg166) Rearrangement of Protein Seauences 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, 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., 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, 1996). 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, 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), -sheet (interleukin-l; 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 reductase Buchwalder et al., Biochemistry 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 p-glucanse Hahn et al., Proc. Natl. Acad. Sci.

U.S.A. 91:10417-10421 (1994)

aspartate transcarbamoylase Yang & Schachman, Proc. Natl. Acad.

Sci. U.S.A. 90:11980-11984 (1993) phosphoribosyl anthranilate isomerase Luger et al., Science 243:206-210 (1989); Luger et al., Prot. Eng.

3:249-258 (1990) pepsin/pepsinogen Lin et al., Protein Science 4:159- 166 (1995) glyceraldehyde-3- phosphate dehydro- genase Vignais et al., Protein Science 4:994-1000 (1995) ornithine decarboxylase Li & Coffino, Mol. Cell. Biol.

13:2377-2383 (1993) yeast phosphoglycerate dehydrogenase Ritco-Vonsovici et al., Biochemistry 34:16543-16551 (1995) Enzyme Inhibitor basic pancreatic trypsin inhibitor Goldenberg & Creighton, J. Mol.

Biol. 165:407-413 (1983) Cytokines interleukin-lD 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 domain Viguera, et al., J.

Mol. Biol. 247:670-681 (1995) Transmembrane Protein omp A Koebnik & Framer, J. Mol. Biol.

250:617-626 (1995) Chimeric Protein interleukin-4- Ps e udomonas exotoxin fusion molecule Kreitman et al., Proc. Natl. Acad.

Sci. U.S.A. 91:6889-6893 (1994).

The results of these studies have been highly variable. In many cases substantially lower activity, solubility or thermodynamic stability were observed (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 T1, Bacillus -glucanase, interleukin-l , 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., 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 -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, 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.

Summarv of the Invention The modified human EPO receptor agonists of the present invention can be represented by the Formula: 1 2 X -(L)a-X wherein; a is 0 or 1; 1 X is a peptide comprising an amino acid sequence corresponding to the sequence of residues n+l through J; X is a peptide comprising an amino acid sequence corresponding to the sequence of residues 1 through n; n is an integer ranging from 1 to J-l; and L is a linker.

In the formula above the constituent amino acids residues of human EPO are numbered sequentially 1 through J from the amino to the carboxyl terminus. A pair of adjacent amino acids within this protein may be numbered n and n+l respectively where n is an integer ranging from 1 to J-1. The residue n+l becomes the new N-terminus of the new EPO receptor agonist and the residue n becomes the new C-terminus of the new EPO receptor agonist.

The present invention relates to novel EPO receptor agonists polypeptides comprising a modified EPO amino acid sequence of the following formula: AlaProProArgLeuIleCysAspSerArgValLeuGluArgTyrLeuLeuGluAlaLys 10 20 GluAlaGluAsnIleThrThrGlyCysAlaGluHisCysSerLeuAsnGluAsnIleThr 30 40 ValProAspThrLysValAsnPheTyrAlaTrpLysArgMetGluValGlyGlnGlnAla

50 60 ValGluValTrpGlnGlyLeuAlaLeuLeuSerGluAlaValLeuArgGlyGlnAlaLeu 70 80 LeuValAsnSerSerGlnProTrpGluProLeuGlnLeuHisValAspLysAlaValSer 90 100 GlyLeuArgSerLeuThrThrLeuLeuArgAlaLeuGlyAlaGlnLysGluAlaIleSer 110 120 ProProAspAlaAlaSerAlaAlaProLeuArgThrIleThrAlaAspThrPheArgLys 130 140 LeuPheArgvalTyrSerAsnPheLeuArgGlyLysLeuLysLeuTyrThrGlyGluAla 150 160 CysArgThrGlyAspArg 166 wherein optionally 1-6 amino acids from the N-terminus and 1-5 from the C-terminus can be deleted from said EPO receptor agonists polypeptide; 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; 23-24 48-49 111-112 24-25 50-51 112-113 25-26 51-52 113-114 26-27 52-53 114-115 27-28 53-54 115-116 28-29 54-55 116-117 29-30 55-56 117-118 30-31 56-57 118-119 31-32 57-58 119-120 32-33 77-78 120-121 33-34 78-79 121-122 34-35 79-80 122-123 35-36 80-81 123-124 36-37 81-82 124-125 37-38 82-83 125-126 38-39 84-85 126-127 40-41 85-86 127-128 41-42 86-87 128-129 43-44 87-88 129-130 44-45 88-89 131-132 45-46 108-109 respectively; and 46-47 109-110 47-48 110-111

said EPO receptor agonist polypeptide may optionally be immediately preceded by (methionine") , (alaninel) or (methionine2, alanine~l).

The more preferred breakpoints at which new C- terminus and N-terminus can be made are; 23-24, 24-25, 25-26, 27-28, 28-29, 29-30, 30-31, 31-32, 32-33, 33-34, 34-35, 35-36, 36-37, 37-38, 38-39, 40-41, 41-42, 42-43, 52-53, 53-54, 54-55, 55-56, 77-78, 78-79, 79-80, 80-81, 81-82, 82-83, 83-84, 84-85, 85-86, 86-87, 87-88, 88-89, 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, 127-128, 128-129, 129-130, 130-131, and 131-132.

The most preferred breakpoints at which new C- terminus and N-terminus can be made are; 23-24, 24-25, 31-32, 32-33, 37-38, 38-39, 82-83, 83-84,85-86, 86-87, 87-88, 125-126, 126-127, and 131-132.

The most preferred breakpoints include glycosylationn sites, non-nuetralizing antibodies, proteolyte cleavage sites.

The EPO receptor agonists of the present invention may contain amino acid substitutions, such as those <BR> <BR> <BR> disclosed in WO 94/24160 or one or more of the<BR> <BR> 24 83 126 glycosylation sites at Asn , Asn , and Asn are changed to other amino acids such as but not limited to Asp or Glu, deletions and/or insertions. It is also intended that the EPO receptor agonists of the present invention may also have amino acid deletions at either/or both the N- and C- termini of the original protein and or deletions from the new N- and/or C- termini of the sequence rearranged proteins in the formulas shown above.

A preferred embodiment of the present invention the linker (L) joining the N-terminus to the C-terminus is a polypeptide selected from the group consisting of: GlyGlyGlySer SEQ ID NO:123; GlyGlyGlySerGlyGlyGlySer SEQ ID NO:124; GlyGlyGlySerGlyGlyGlySerGlyGlyGlySer SEQ ID NO: 125; SerGlyGlySerGlyGlySer SEQ ID NO:126; GluPheGlyAsnMet SEQ ID NO:127; GluPheGlyGlyAsnMet SEQ ID NO:128; GluPheGlyGlyAsnGlyGlyAsnMet SEQ ID NO:129; and GlyGlySerAspMetAlaGly SEQ ID NO:130.

The present invention also encompasses recombinant human EPO receptor agonists co-administered or sequentially with one or more additional colony stimulating factors (CSF) including, cytokines, lymphokines, interleukins, hematopoietic growth factors which include but are not limited to GM-CSF, G-CSF, c- mpl ligand (also known as TPO or MGDF), M-CSF, 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, human growth hormone, B- cell growth factor, B-cell differentiation factor, eosinophil differentiation factor and stem cell factor (SCF) also known as steel factor or c-kit ligand (herein collectively referred to as "factors"). These co- administered mixtures may be characterized by having the usual activity of both of the peptides or the mixture may be further characterized by having a biological or physiological activity greater than simply the additive function of the presence of the EPO receptor agonists or the second colony stimulating factor alone. The co- administration may also provide an enhanced effect on the activity or an activity different from that expected by the presence of the EPO or the second colony stimulating factor. The co-administration may also have an improved activity profile which may include reduction

of undesirable biological activities associated with native human EPO. In addition to the list above, IL-3 variants taught in WO 94/12639 and WO 94/12638 fusion protein taught in WO 95/21197, and WO 95/21254 G-CSF receptor agonists disclosed in WO 97/12977, c-mpl receptor agonists disclosed in WO 97/12978, IL-3 receptor agonists disclosed in WO 97/12979 and multi- functional receptor agonists taught in WO 97/12985 can be co-administered with the polypeptides of the present invention. As used herein "IL-3 variants" refer to IL-3 variants taught in WO 94/12639 and WO 94/12638. As used herein "fusion proteins" refer to fusion protein taught in WO 95/21197, and WO 95/21254. As used herein "G-CSF receptor agonists" refer to G-CSF receptor agonists disclosed in WO 97/12978. As used herein "c-mpl receptor agonists" refer to c-mpl receptor agonists disclosed in WO 97/12978. As used herein "IL-3 receptor agonists" refer to IL-3 receptor agonists disclosed in WO 97/12979. As used herein "multi-functional receptor agonists11 refer to multi-functional receptor agonists taught in WO 97/12985.

In addition, it is envisioned that in vitro uses would include the ability to stimulate bone marrow and blood cell activation and growth before the expanded cells are infused into patients.

It is also envisioned that uses of EPO receptor agonists of the present invention would include blood banking applications, where the EPO receptor agonists are given to a patent to increase the number of red blood cells and blood products removed from the patient, prior to some medical procedure, and the blood products stored and transfused back into the patient after the medical procedure. Additionally, it is envisioned that uses of EPO receptor agonists would include giving the EPO receptor agonists to a blood donor prior to blood donation to increase the number of red blood cells, thereby allowing the donor to safely give more blood.

Brief Description of the Figures Figure 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.

Figure 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 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.

Figure 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 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.

Figure 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 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.

Figure 5 shows a DNA sequence encoding human mature EPO based on the sequence of Lin et al. (PNAS 82:7580- 7584, 1985).

Detailed Description of the Invention Receptor agonists of the present invention may be useful in the treatment of diseases characterized by decreased levels of red blood cells of the hematopoietic system.

A EPO receptor agonist may be useful in the treatment or prevention of anemia. 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 phenytoin or carbamazepine, antithyroids such as propylthiouracil and methimazole and diuretics. EPO receptor agonists 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 present peptide may be useful in treating such hematopoietic deficiency.

Another aspect of the present invention provides plasmid DNA vectors for use in the method of expression of these novel EPO 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 host cells capable of expressing the EPO receptor agonists include expression vectors comprising nucleotide sequences coding for the EPO 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 modified EPO 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 capable of directing the replication and expression thereof in selected host cells.

As another aspect of the present invention, there is provided a method for producing the novel family of human EPO 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 the novel EPO receptor agonist polypeptide. Suitable cells or cell lines may include various strains of bacteria such as E. coli, yeast, mammalian cells, or insect cells may be utilized as host cells in the method of the present invention.

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 EPO 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.

Administration will be in accordance with a dosage regimen that will be readily ascertained by the skilled,

based on in vivo specific activity of the analog in comparison with human erythropoietin and based on what is now known in the art concerning the administration of human erythropoietin for inducing erythropoiesis and treating various conditions, such as anemia, in humans, including anemia in patients suffering from renal failure. Dosage of an analog of the invention may vary somewhat from individual to individual, depending on the particular analog and its specific in vivo activity, the route of administration, the medical condition, age, weight or sex of the patient, the patient's sensitivities to the analog or components of vehicle, and other factors which the attending physician will be capable of readily taking into account. With regard to therapeutic uses of analogs of the invention, reference is made to U.S. Patent Nos. 4,703,008 and 4,835,260; see also the chapter on (recombinant) [des-Arg6'jhuman erythropoietin at pages 591-595 of the Physicians' Desk Commercially available preparations of recombinant [des- Arg;""] human erythropoietin have 2,000, 3,000, 4,000 or 10,000 units of the glycohormone per mL in preservative- free aqueous solution with 2.5 mg/mL human serum albumin, 5.8 mg/mL sodium citrate, 5.8 mg/mL NaCl, and 0.06 mg/mL citric acid, pH 6.9 (+/-0.3).

Recombinantly produced EPO has proven especially useful for the treatment of patients suffering from impaired red blood cell production (Physicians Desk Reference (PDR). 1993 edition, pp 602-605). Recombinant EPO has proven effective in treating anemia associated with chronic renal failure and HIV-Infected individuals suffering from lowered endogenous EPO levels related to therapy with Zidovudine (AZT) (See PDR, 1993 edition, at page 6002).

Modifications of the EPO protein which would improve its utility as a tool for diagnosis or treatment

of blood disorders are certainly desirable. In particular, modified forms of EPO exhibiting enhanced biological activity would be more effective and efficient than native EPO in the therapy setting when it is necessary to administer EPO to the patient, enabling administration less frequently and/or at a lower dose.

Administration of reduced amounts of EPO would also presumably reduce the risk of adverse effects associated with EPO treatment, such as hypertension, seizures, headaches, etc. (See PDR, 1993 edition, at pp. 603-604).

The EPO receptor agonists of the present invention may also have improved stability and hence increased half- life which would allow for the production of a non- glycosylated form of EPO in a bacterial expression system at a much lower cost. Due it's increased half- life this non-glycosylated form of EPO would have an increased in vivo activity compared de-glycosylated EPO.

The therapeutic method and compositions may also include co-administration with other hematopoietic factors. A non-exclusive list of other appropriate hematopoietins, colony stimulating factors (CSFs) 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, IL-1, IL-4, IL-2, IL-3, IL-5, IL 6, IL-7, IL-8, IL-9, IL-10, IL-1l, IL-12, IL- 13, IL-15, LIF, human growth hormone, B-cell growth factor, B-cell differentiation factor, eosinophil differentiation factor and stem cell factor (SCF) also known as steel factor or c-kit ligand (herein collectively referred to as "factors"), or combinations thereof. In addition to the list above, IL-3 variants taught in WO 94/12639 and WO 94/12638 fusion protein taught in WO 95/21197, and WO 95/21254 G-CSF receptor agonists disclosed in WO 97/12977, c-mpl receptor agonists disclosed in WO 97/12978, IL-3 receptor

agonists disclosed in WO 97/12979 and multi-functional receptor agonists taught in WO 97/12985 can be co- administered with the polypeptides of the present invention.

The EPO 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.

The EPO receptor agonists of the present invention may also be useful in the ex vivo expansion of hematopoietic progenitors. Colony stimulating factors (CSFs) , such as G-CSF, have been administered alone, co- administered with other CSFs, or in combination with bone marrow transplants subsequent to high dose chemotherapy to treat the anemia, neutropenia and thrombocytopenia which are often the result of such treatment.

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 EPO receptor agonist of the present invention.

Determination of the Linker The length of the amino acid sequence of the linker 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, Mol. Immunol. 20: 483- 489, 1983; Kyte & Doolittle, J. Mol. Biol. 157:105-132, 1982; solvent exposed surface area, Lee & Richards, J.

Mol. Biol. 55:379-400, 1971) and the ability to adopt the necessary conformation without deranging the configuration of the EPO receptor agonist (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 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 3.8Å 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" cassette approach mentioned above; or optionally a combination of the original sequence and new sequence having the appropriate total length may be used.

Determination of the Amino and Carboxvl Termini of EPO Recestor Aaonists Sequences of EPO receptor agonists 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 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, 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 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.

Materials and Methods Recombinant DNA 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, MA) or Boehringer Mannheim (Indianapolis, IN).

Transformation of E. coli strains E. coli strains, such as DH5ccTM (Life Technologies, Gaithersburg, MD) and TG1 (Amersham Corp., Arlington Heights, IL) are used for transformation of ligation reactions and are the source of plasmid DNA for transfecting mammalian cells. E. coli strains, such as MON105 and JM101, can be used for expressing the EPO receptor agonist of the present invention in the cytoplasm or periplasmic space.

MON105 ATCC#55204: F-, lamda-,IN(rrnD, rrE)1, rpoD+, rpoH358 DH5aTM: F-, phi80dlacZdeltaM15, delta(lacZYA-argF)U169, deoR, recAl, endAl, hsdR17(rk-,mk+), phoA, supE44lamda-, thi-l, gyrA96, relAl TG1: delta(lac-pro), supE, thi-l, hsdD5/F' (traD36, proA+B+, lacIq, lacZdeltaM15) DH5ccTM 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 MON105 are rendered competent to take up DNA using a CaCl 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, NY). The cells are collected by centrifugation and resuspended in one-fifth culture volume of CaCl solution (50 mM CaCl2, 10 mM Tris-Cl, pH7.4) and are held at 40C 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 0.2mL of these cells, and the samples are held at 40C for 1 hour. The samples are shifted to 420C for two minutes and lmL of LB is added prior to shaking the samples at 370C 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 37oC. Single colonies are picked, grown in LB supplemented with appropriate antibiotic for 6-16 hours at 37"C with shaking. Colonies are picked and inoculated into LB plus appropriate antibiotic (100 ug/mL ampicillin or 75 ug/mL spectinomycin) and are grown at 370C while shaking. Before harvesting the cultures, 1 ul of cells are analyzed by PCR for the presence of a EPO receptor agonist gene. The PCR is carried out using a combination of primers that anneal to the EPO receptor agonist gene and/or vector. After the PCR is complete, loading dye is added to the sample followed by electrophoresis as described earlier. A gene has been ligated to the vector when a PCR product of the expected size is observed.

Methods for creation of aenes with new N-terminus/C- terminus Method I. Creation of genes with new N-terminus/C- terminus which contain a linker region.

Genes with new N-terminus/C-terminus which contain a linker region 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 Figure 2.

In the first step, the 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 that connects the C-terminal and N-terminal ends of the original protein. In the second step, the 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 enzyme recognition sites which allow cloning of the new gene into expression plasmids. Typical PCR conditions are one cycle 950C melting for two minutes; 25 cycles 940C denaturation for one minute, 500C annealing for one minute and 720C extension for one minute; plus one cycle 720C 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 lx PCR buffer, 200 uM dGTP, 200 uM dATP, 200 uM dTTP, 200 uM dCTP, 2.5 units AmpliTaq DNA polymerase and 2 mM NgCl2. PCR reactions are performed in a Model 480 DNA thermal cycler (Perkin Elmer Corporation, Norwalk, CT).

"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 700C 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 950C melting for two minutes; 25 cycles 940C denaturation for one minute, 600C annealing for one minute and 720C extension for one minute; plus one cycle 720C 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 lx 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).

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 Figure 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 the original 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 950C melting for two minutes; 25 cycles 940C denaturation for one minute, 500C annealing for 45 seconds and 720C 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 lx 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, CT). PCR reaction products are purified using a Wizard PCR Preps kit (Promega).

The primers are designed to include appropriate restriction enzyme recognition sites which allow for the cloning of the new gene into expression vectors.

Typically "Fragment Start" is designed to create a 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 500C 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 E. coli strain DHSa 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 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 Figure 4.

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 950C melting for two minutes; 25 cycles 940C denaturation for one minute, 500C annealing for one minute and 720C extension for one minute; plus one cycle 720C extension for seven minutes. A Perkin Elmer GeneAmp PCR Core Reagents kit (Perkin Elmer Corporation, Norwalk, CT) is used. A 100 ul reaction contains 100 pmole of each primer and one ug of template DNA; and lx 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, CT). PCR reactions are purified using a Wizard PCR Preps kit (Promega).

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, WI), the Qiagen QIAwell Plasmid isolation kits (Chatsworth, CA) or Qiagen Plasmid Midi kit. These kits follow the same general procedure for plasmid DNA isolation. Briefly, cells are pelleted by centrifugation (5000 x g), plasmid DNA released with sequential NaOH/acid treatment, and cellular debris is removed by centrifugation (10000 x 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 370C 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 dHZO 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 PRISMM DyeDeoxyrM terminator sequencing chemistry (Applied Biosystems Division of Perkin Elmer Corporation, Lincoln City, CA) 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, CT)

following the recommended amplification conditions.

Samples are purified to remove excess dye terminators with Centri-Sep'M spin columns (Princeton Separations, Adelphia, NJ) 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, MI).

Expression of EPO receptor aaonists in mammalian cells Mammalian Cell Transfection/Production of Conditioned Media 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 2mM (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, CA).

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-VPl6. 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-VPl6 cells are seeded into a 60 millimeter (mm) tissue culture dish at 3 X 105 cells per dish 24 hours

prior to transfection. Cells are transfected for 16 hours in 3 mL of "OPTIMEN1,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. 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 EPO recestor aqonists in E. coli E. coli strain MON105 or JM101 harboring the plasmid of interest are grown at 370C in M9 plus casamino acids medium with shaking in a air incubator Model G25 from New Brunswick Scientific (Edison, New Jersey). Growth is monitored at OD600 until it reaches a value of 1, at which time nalidixic acid (10 milligrams/mL) in 0.1 N NaOH is added to a final concentration of 50 ug/mL. The cultures are then shaken at 370C 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 x g) to pellet the cells.

Additional strategies for achieving high-level expression of genes in E. coli can be found in Savvas, C.M. (Microbiological Reviews 60;512-538, 1996).

Inclusion Bodv sresaration, Extraction, Refoldinq, Dialvsis, DEAE Chromatoqrashv, and Characterization of the EPO receotor aqonists which accumulate as inclusion bodies in E. coli.

Isolation of Inclusion Bodies: 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-HC1), pH 8.0 + 1 mM ethylenediaminetetraacetic acid (DATA)). 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-HC1, 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.

The extraction solution is transferred to a beaker containing 70 mL of 5mM Tris-HCl, pH 9.5 and 2.3 M urea and gently stirred while exposed to air at 40C 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 (0.46x25 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.

Purification: Following the refold, 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 40C for 2 hours and then centrifuged for 20 minutes at 12,000 x g to pellet any insoluble protein.

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 l0mM Tris-HC1, 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 x g) to pellet any insoluble protein following dialysis.

A Bio-Rad Bio-Scale DEAE2 column (7 x 52 mm) is used for ion exchange chromatography. The column is equilibrated in a buffer containing l0mM Tris-HCl, pH 8.0. The protein is eluted using a 0-to-500 mM sodium chloride (NaCl) gradient, in equilibration buffer, over 45 column volumes. A flow rate of 1 mL per minute is used throughout the run. Column fractions (2 mL per fraction) are collected across the gradient and analyzed by RP HPLC on a Vydac (Hesperia, Ca.) C18 column (0.46 x 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/Por 3 membrane with a MWCO of 3,500 daltons.

Finally, the sample is sterile filtered using a 0.22um syringe filter (uStar LB syringe filter, Costar, Cambridge, Ma.), and stored at 40C.

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.

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, CA (1990).

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.

Methvlcellulose Assav 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) Methods 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 1X 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 x g for 30 min. The mononuclear cell band is removed and washed two times in 1X PBS and once with 1% BSA PBS (CellPro Co., Bothel, WA).

Mononuclear cells are counted and CD34+ cells are selected using the Ceprate LC (CD34) Kit (CellPro Co., Bothel, WA) 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 X 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, CA.) is added

to the culture media. 3,000-10,000 CD34+ cells are added per dish. EPO 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 .001 nM to 10 nM. Cultures are resuspended using a 3cc 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 370C, 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 40x 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.

Human Cord Blood Hematopoietic Growth Factor Assavs 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., 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 burst forming colonies (BFU-E) activity.

Methods 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, CA); and CD34+ selection using a CellPro (Bothell, WA) 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 1x104 cells in lml of 0.9% methylcellulose containing medium without additional growth factors (Methocult H4230 from Stem Cell Technologies, Vancouver, BC.). After culturing for 7-9 days, colonies containing >30 cells are counted.

Transfected cell lines: Cell lines, such as BHK or the murine pro B cell line Baf/3, can be transfected with a colony stimulating factor receptor, such as the human EPO receptor which the cell line does not have. These transfected cell lines can be used to determine the cell proliferative activity and/or receptor binding.

EXAMPLE 1 Genes encoding the sequence rearranged EPO ligands can be constructed by any one of the methods described herein or by other recombinant methods known to those

skilled in the art. For the purpose of this example, the site of permutation is between residues 131(Arg) and 132(Thr) of EPO. This is a site which is susceptible to proteolytic cleavage, thereby indicating surface exposure with a relatively high degree of flexibility.

In this example a new N-terminus and a new C-terminus is created without a linker joining the original termini.

This is done, as described in Method II, in 2 steps of PCR and a blunt end ligation.

In the first PCR step, using a vector containing the DNA sequence of SEQ ID NO:120 as the template, and the primers "new start" and "blunt start", a DNA fragment is created which encodes the new N-terminus. This fragment is termed "fragment start". The sequence underlined in the new start primer is the NcoI restriction site.

New start primer = gcgcgcCCATGGACAATCACTGCTGAC SEQ ID NO:131 Blunt start primer = TCTGTCCCCTGTCCT SEQ ID NO:132 In the second PCR step, using a vector containing the DNA sequence of SEQ ID NO:120 as the template, and the primers "new stop" and "blunt stop" create a DNA fragment which encodes the new C-terminus. This fragment is termed "fragment stop". The sequence underlined in the new stop primer is the HindIII restriction site.

New stop primer = gcgcgcAAGCTTATTATCGGAGTGGAGCAGCTGAGGCCGCATC SEQ ID NO:133 Blunt end primer = GCCCCACCACGCCTCATCTGT SEQ ID NO:134

In the ligation step, the two fragments created in the two PCR reactions are ligated together, digested with NcoI and HindIII and cloned into an expression vector.

The clones are screened by restiction analysis and DNA sequenced to confirm the proper sequence. The primers can be designed to create restriction sites other than NcoI and HindIII to clone into other expression vectors.

EXAMPLE 2 The sequence rearranged EPO receptor agonists of the present invention can be assayed for bioactivity by the methods described herein or by other assays know to those skilled in the art.

Additional techniques for the construction of the variant genes, recombinant protein expression , protein purification, protein characterization, biological activity determination can be found in WO 94/12639, WO 94/12638, WO 95/20976, WO 95/21197, WO 95/20977, WO 95/21254 which are hereby incorporated by reference in their entirety.

All references, patents or applications cited herein are incorporated by reference in their entirety as if written herein.

Various other examples will be apparent to the person skilled in the art after reading the present disclosure without departing from the spirit and scope of the invention. It is intended that all such other examples be included within the scope of the appended claims.

SEQUENCE LISTING (1) GENERAL INFORMATION (i) APPLICANT: G. D. Searle and Company (ii) TITLE OF THE INVENTION: Novel Erythropoietin Receptor Agonists (iii) NUMBER OF SEQUENCES: 134 (iv) CORRESPONDENCE ADDRESS: (A) ADDRESSEE: G. D. Searle & Co.

(B) STREET: P.O. Box 5110 (C) CITY: Chicago (D) STATE: IL (E) COUNTRY: U. S. A.

(F) ZIP: 60680 (v) COMPUTER READABLE FORM: (A) MEDIUM TYPE: Diskette (B) COMPUTER: IBM Compatible (C) OPERATING SYSTEM: DOS (D) SOFTWARE: FastSEQ for Windows Version 2.0 (vi) CURRENT APPLICATION DATA: (A) APPLICATION NUMBER: (B) FILING DATE: 21-OCT-1997 (C) CLASSIFICATION: (vii) PRIOR APPLICATION DATA: (A) APPLICATION NUMBER: 60/034,044 (B) FILING DATE: 25-OCT-1996 (viii) ATTORNEY/AGENT INFORMATION: (A) NAME: Bennett, Dennis A (B) REGISTRATION NUMBER: 34,547 (C) REFERENCE/DOCKET NUMBER: 2991/1 (ix) TELECOMMUNICATION INFORMATION: (A) TELEPHONE: 314-737-6986 (B) TELEFAX: 314-737-6972 (C) TELEX: (2) INFORMATION FOR SEQ ID NO:1: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:1: Asn Ile Thr Thr Gly Cys Ala Glu His Cys Ser Leu Asn Glu Asn Ile 15 10 15 Thr Val Pro Asp Thr Lys Val Asn Phe Tyr Ala Trp Lys Arg Met Glu 20 25 30 Val Gly Gln Gln Ala Val Glu Val Trp Gln Gly Leu Ala Leu Leu Ser 35 40 45 Glu Ala Val Leu Arg Gly Gln Ala Leu Leu Val Asn Ser Ser Gln Pro 50 55 60 Trp Glu Pro Leu Gln Leu His Val Asp Lys Ala Val Ser Gly Leu Arg 65 70 75 80 Ser Leu Thr Thr Leu Leu Arg Ala Leu Gly Ala Gln Lys Glu Ala Ile 85 90 95 Ser Pro Pro Asp Ala Ala Ser Ala Ala Pro Leu Arg Thr Ile Thr Ala 100 105 110 Asp Thr Phe Arg Lys Leu Phe Arg Val Tyr Ser Asn Phe Leu Arg Gly 115 120 125 Lys Leu Lys Leu Tyr Thr Gly Glu Ala Cys Arg Thr Gly Asp Arg Gly 130 135 140 Gly Gly Ser Ala Pro Pro Arg Leu Ile Cys Asp Ser Arg Val Leu Glu 145 150 155 160 Arg Tyr Leu Leu Glu Ala Lys Glu Ala Gln 165 170 (2) INFORMATION FOR SEQ ID NO:2: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:2: Ile Thr Thr Gly Cys Ala Glu His Cys Ser Leu Asn Glu Asn Ile Thr 1 5 10 15 Val Pro Asp Thr Lys Val Asn Phe Tyr Ala Trp Lys Arg Met Glu Val 20 25 30 Gly Gln Gln Ala Val Glu Val Trp Gln Gly Leu Ala Leu Leu Ser Glu 35 40 45 Ala Val Leu Arg Gly Gln Ala Leu Leu Val Asn Ser Ser Gln Pro Trp 50 55 60 Glu Pro Leu Gln Leu His Val Asp Lys Ala Val Ser Gly Leu Arg Ser 65 70 75 80 Leu Thr Thr Leu Leu Arg Ala Leu Gly Ala Gln Lys Glu Ala Ile Ser 85 90 95 Pro Pro Asp Ala Ala Ser Ala Ala Pro Leu Arg Thr Ile Thr Ala Asp 100 105 110 Thr Phe Arg Lys Leu Phe Arg Val Tyr Ser Asn Phe Leu Arg Gly Lys 115 120 125 Leu Lys Leu Tyr Thr Gly Glu Ala Cys Arg Thr Gly Asp Arg Gly Gly 130 135 140 Gly Ser Ala Pro Pro Arg Leu Ile Cys Asp Ser Arg Val Leu Glu Arg 145 150 155 160 Tyr Leu Leu Glu Ala Lys Glu Ala Glu Asn 165 170 (2) INFORMATION FOR SEQ ID NO:3: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:3: Thr Thr Gly Cys Ala Glu His Cys Ser Leu Asn Glu Asn Ile Thr Val 1 5 10 15 Pro Asp Thr Lys Val Asn Phe Tyr Ala Trp Lys Arg Met Glu Val Gly 20 25 30 Gln Gln Ala Val Glu Val Trp Gln Gly Leu Ala Leu Leu Ser Glu Ala 35 40 45 Val Leu Arg Gly Gln Ala Leu Leu Val Asn Ser Ser Gln Pro Trp Glu 50 55 60 Pro Leu Gln Leu His Val Asp Lys Ala Val Ser Gly Leu Arg Ser Leu 65 70 75 80 Thr Thr Leu Leu Arg Ala Leu Gly Ala Gln Lys Glu Ala Ile Ser Pro 85 90 95 Pro Asp Ala Ala Ser Ala Ala Pro Leu Arg Thr Ile Thr Ala Asp Thr 100 105 110 Phe Arg Lys Leu Phe Arg Val Tyr Ser Asn Phe Leu Arg Gly Lys Leu 115 120 125 Lys Leu Tyr Thr Gly Glu Ala Cys Arg Thr Gly Asp Arg Gly Gly Gly 130 135 140 Ser Ala Pro Pro Arg Leu Ile Cys Asp Ser Arg Val Leu Glu Arg Tyr 145 150 155 160 Leu Leu Glu Ala Lys Glu Ala Glu Asn Ile 165 170 (2) INFORMATION FOR SEQ ID NO:4: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:4: Thr Gly Cys Ala Glu His Cys Ser Leu Asn Glu Asn Ile Thr Val Pro 1 5 10 15 Asp Thr Lys Val Asn Phe Tyr Ala Trp Lys Arg Met Glu Val Gly Gln 20 25 30 Gln Ala Val Glu Val Trp Gln Gly Leu Ala Leu Leu Ser Glu Ala Val 35 40 45 Leu Arg Gly Gln Ala Leu Leu Val Asn Ser Ser Gln Pro Trp Glu Pro 50 55 60 Leu Gln Leu His Val Asp Lys Ala Val Ser Gly Leu Arg Ser Leu Thr 65 70 75 80 Thr Leu Leu Arg Ala Leu Gly Ala Gln Lys Glu Ala Ile Ser Pro Pro 85 90 95 Asp Ala Ala Ser Ala Ala Pro Leu Arg Thr Ile Thr Ala Asp Thr Phe 100 105 110 Arg Lys Leu Phe Arg Val Tyr Ser Asn Phe Leu Arg Gly Lys Leu Lys 115 120 125 Leu Tyr Thr Gly Glu Ala Cys Arg Thr Gly Asp Arg Gly Gly Gly Ser 130 135 140 Ala Pro Pro Arg Leu Ile Cys Asp Ser Arg Val Leu Glu Arg Tyr Leu 145 150 155 160 Leu Glu Ala Lys Glu Ala Glu Asn Ile Thr 165 170 (2) INFORMATION FOR SEQ ID NO:5: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170.amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:5: Gly Cys Ala Glu His Cys Ser Leu Asn Glu Asn Ile Thr Val Pro Asp 1 5 10 15 Thr Lys Val Asn Phe Tyr Ala Trp Lys Arg Met Glu Val Gly Gln Gln 20 25 30 Ala Val Glu Val Trp Gln Gly Leu Ala Leu Leu Ser Glu Ala Val Leu 35 40 45 Arg Gly Gln Ala Leu Leu Val Asn Ser Ser Gln Pro Trp Glu Pro Leu 50 55 60 Gln Leu His Val Asp Lys Ala Val Ser Gly Leu Arg Ser Leu Thr Thr 65 70 75 80 Leu Leu Arg Ala Leu Gly Ala Gln Lys Glu Ala Ile Ser Pro Pro Asp 85 90 95 Ala Ala Ser Ala Ala Pro Leu Arg Thr Ile Thr Ala Asp Thr Phe Arg 100 105 110 Lys Leu Phe Arg Val Tyr Ser Asn Phe Leu Arg Gly Lys Leu Lys Leu 115 120 125 Tyr Thr Gly Glu Ala Cys Arg Thr Gly Asp Arg Gly Gly Gly Ser Ala 130 135 140 Pro Pro Arg Leu Ile Cys Asp Ser Arg Val Leu Glu Arg Tyr Leu Leu 145 150 155 160 Glu Ala Lys Glu Ala Glu Asn Ile Thr Thr 165 170 (2) INFORMATION FOR SEQ ID NO:6: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:6: Cys Ala Glu His Cys Ser Leu Asn Glu Asn Ile Thr Val Pro Asp Thr 1 5 10 15 Lys Val Asn Phe Tyr Ala Trp Lys Arg Met Glu Val Gly Gln Gln Ala 20 25 30 Val Glu Val Trp Gln Gly Leu Ala Leu Leu Ser Glu Ala Val Leu Arg 35 40 45 Gly Gln Ala Leu Leu Val Asn Ser Ser Gln Pro Trp Glu Pro Leu Gln 50 55 60 Leu His Val Asp Lys Ala Val Ser Gly Leu Arg Ser Leu Thr Thr Leu 65 70 75 80 Leu Arg Ala Leu Gly Ala Gln Lys Glu Ala Ile Ser Pro Pro Asp Ala 85 90 95 Ala Ser Ala Ala Pro Leu Arg Thr Ile Thr Ala Asp Thr Phe Arg Lys 100 105 110 Leu Phe Arg Val Tyr Ser Asn Phe Leu Arg Gly Lys Leu Lys Leu Tyr 115 120 125 Thr Gly Glu Ala Cys Arg Thr Gly Asp Arg Gly Gly Gly Ser Ala Pro 130 135 140 Pro Arg Leu Ile Cys Asp Ser Arg Val Leu Glu Arg Tyr Leu Leu Glu 145 150 155 160 Ala Lys Glu Ala Glu Asn Ile Thr Thr Gly 165 170 (2) INFORMATION FOR SEQ ID NO:7: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:7: Ala Glu His Cys Ser Leu Asn Glu Asn Ile Thr Val Pro Asp Thr Lys 1 5 10 15 Val Asn Phe Tyr Ala Trp Lys Arg Met Glu Val Gly Gln Gln Ala Val 20 25 30 Glu Val Trp Gln Gly Leu Ala Leu Leu Ser Glu Ala Val Leu Arg Gly 35 40 45 Gln Ala Leu Leu Val Asn Ser Ser Gln Pro Trp Glu Pro Leu Gln Leu 50 55 60 His Val Asp Lys Ala Val Ser Gly Leu Arg Ser Leu Thr Thr Leu Leu 65 70 75 80 Arg Ala Leu Gly Ala Gln Lys Glu Ala Ile Ser Pro Pro Asp Ala Ala 85 90 95 Ser Ala Ala Pro Leu Arg Thr Ile Thr Ala Asp Thr Phe Arg Lys Leu 100 105 110 Phe Arg Val Tyr Ser Asn Phe Leu Arg Gly Lys Leu Lys Leu Tyr Thr 115 120 125 Gly Glu Ala Cys Arg Thr Gly Asp Arg Gly Gly Gly Ser Ala Pro Pro 130 135 140 Arg Leu Ile Cys Asp Ser Arg Val Leu Glu Arg Tyr Leu Leu Glu Ala 145 150 155 160 Lys Glu Ala Glu Asn Ile Thr Thr Gly Cys 165 170 (2) INFORMATION FOR SEQ ID NO:8: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:8: Glu His Cys Ser Leu Asn Glu Asn Ile Thr Val Pro Asp Thr Lys Val 1 5 10 15 Asn Phe Tyr Ala Trp Lys Arg Met Glu Val Gly Gln Gln Ala Val Glu 20 25 30 Val Trp Gln Gly Leu Ala Leu Leu Ser Glu Ala Val Leu Arg Gly Gln 35 40 45 Ala Leu Leu Val Asn Ser Ser Gln Pro Trp Glu Pro Leu Gln Leu His 50 55 60 Val Asp Lys Ala Val Ser Gly Leu Arg Ser Leu Thr Thr Leu Leu Arg 65 70 75 80 Ala Leu Gly Ala Gln Lys Glu Ala Ile Ser Pro Pro Asp Ala Ala Ser 85 90 95 Ala Ala Pro Leu Arg Thr Ile Thr Ala Asp Thr Phe Arg Lys Leu Phe 100 105 110 Arg Val Tyr Ser Asn Phe Leu Arg Gly Lys Leu Lys Leu Tyr Thr Gly 115 120 125 Glu Ala Cys Arg Thr Gly Asp Arg Gly Gly Gly Ser Ala Pro Pro Arg 130 135 140 Leu Ile Cys Asp Ser Arg Val Leu Glu Arg Tyr Leu Leu Glu Ala Lys 145 150 155 160 Glu Ala Glu Asn Ile Thr Thr Gly Cys Ala 165 170 (2) INFORMATION FOR SEQ ID NO:9: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:9: His Cys Ser Leu Asn Glu Asn Ile Thr Val Pro Asp Thr Lys Val Asn 1 5 10 15 Phe Tyr Ala Trp Lys Arg Met Glu Val Gly Gln Gln Ala Val Glu Val 20 25 30 Trp Gln Gly Leu Ala Leu Leu Ser Glu Ala Val Leu Arg Gly Gln Ala 35 40 45 Leu Leu Val Asn Ser Ser Gln Pro Trp Glu Pro Leu Gln Leu His Val 50 55 60 Asp Lys Ala Val Ser Gly Leu Arg Ser Leu Thr Thr Leu Leu Arg Ala 65 70 75 80 Leu Gly Ala Gln Lys Glu Ala Ile Ser Pro Pro Asp Ala Ala Ser Ala 85 90 95 Ala Pro Leu Arg Thr Ile Thr Ala Asp Thr Phe Arg Lys Leu Phe Arg 100 105 110 Val Tyr Ser Asn Phe Leu Arg Gly Lys Leu Lys Leu Tyr Thr Gly Glu 115 120 125 Ala Cys Arg Thr Gly Asp Arg Gly Gly Gly Ser Ala Pro Pro Arg Leu 130 135 140 Ile Cys Asp Ser Arg Val Leu Glu Arg Tyr Leu Leu Glu Ala Lys Glu 145 150 155 160 Ala Glu Asn Ile Thr Thr Gly Cys Ala Glu 165 170 (2) INFORMATION FOR SEQ ID NO:10: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:10: Cys Ser Leu Asn Glu Asn Ile Thr Val Pro Asp Thr Lys Val Asn Phe 1 5 10 15 Tyr Ala Trp Lys Arg Met Glu Val Gly Gln Gln Ala Val Glu Val Trp 20 25 30 Gln Gly Leu Ala Leu Leu Ser Glu Ala Val Leu Arg Gly Gln Ala Leu 35 40 45 Leu Val Asn Ser Ser Gln Pro Trp Glu Pro Leu Gln Leu His Val Asp 50 55 60 Lys Ala Val Ser Gly Leu Arg Ser Leu Thr Thr Leu Leu Arg Ala Leu 65 70 75 80 Gly Ala Gln Lys Glu Ala Ile Ser Pro Pro Asp Ala Ala Ser Ala Ala 85 90 95 Pro Leu Arg Thr Ile Thr Ala Asp Thr Phe Arg Lys Leu Phe Arg Val 100 105 110 Tyr Ser Asn Phe Leu Arg Gly Lys Leu Lys Leu Tyr Thr Gly Glu Ala 115 120 125 Cys Arg Thr Gly Asp Arg Gly Gly Gly Ser Ala Pro Pro Arg Leu Ile 130 135 140 Cys Asp Ser Arg Val Leu Glu Arg Tyr Leu Leu Glu Ala Lys Glu Ala 145 150 155 160 Glu Asn Ile Thr Thr Gly Cys Ala Glu His 165 170 (2) INFORMATION FOR SEQ ID NO:ll: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:ll: Ser Leu Asn Glu Asn Ile Thr Val Pro Asp Thr Lys Val Asn Phe Tyr 1 5 10 15 Ala Trp Lys Arg Met Glu Val Gly Gln Gln Ala Val Glu Val Trp Gln 20 25 30 Gly Leu Ala Leu Leu Ser Glu Ala Val Leu Arg Gly Gln Ala Leu Leu 35 40 45 Val Asn Ser Ser Gln Pro Trp Glu Pro Leu Gln Leu His Val Asp Lys 50 55 60 Ala Val Ser Gly Leu Arg Ser Leu Thr Thr Leu Leu Arg Ala Leu Gly 65 70 75 80 Ala Gln Lys Glu Ala Ile Ser Pro Pro Asp Ala Ala Ser Ala Ala Pro 85 90 95 Leu Arg Thr Ile Thr Ala Asp Thr Phe Arg Lys Leu Phe Arg Val Tyr 100 105 110 Ser Asn Phe Leu Arg Gly Lys Leu Lys Leu Tyr Thr Gly Glu Ala Cys 115 120 125 Arg Thr Gly Asp Arg Gly Gly Gly Ser Ala Pro Pro Arg Leu Ile Cys 130 135 140 Asp Ser Arg Val Leu Glu Arg Tyr Leu Leu Glu Ala Lys Glu Ala Glu 145 150 155 160 Asn Ile Thr Thr Gly Cys Ala Glu His Cys 165 170 (2) INFORMATION FOR SEQ ID NO:12: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:12: Leu Asn Glu Asn Ile Thr Val Pro Asp Thr Lys Val Asn Phe Tyr Ala 1 5 10 15 Trp Lys Arg Met Glu Val Gly Gln Gln Ala Val Glu Val Trp Gln Gly 20 25 30 Leu Ala Leu Leu Ser Glu Ala Val Leu Arg Gly Gln Ala Leu Leu Val 35 40 45 Asn Ser Ser Gln Pro Trp Glu Pro Leu Gln Leu His Val Asp Lys Ala 50 55 60 Val Ser Gly Leu Arg Ser Leu Thr Thr Leu Leu Arg Ala Leu Gly Ala 65 70 75 80 Gln Lys Glu Ala Ile Ser Pro Pro Asp Ala Ala Ser Ala Ala Pro Leu 85 90 95 Arg Thr Ile Thr Ala Asp Thr Phe Arg Lys Leu Phe Arg Val Tyr Ser 100 105 110 Asn Phe Leu Arg Gly Lys Leu Lys Leu Tyr Thr Gly Glu Ala Cys Arg 115 120 125 Thr Giy Asp Arg Gly Gly Gly Ser Ala Pro Pro Arg Leu Ile Cys Asp 130 135 140 Ser Arg Val Leu Glu Arg Tyr Leu Leu Glu Ala Lys Glu Ala Glu Asn 145 150 155 160 Ile Thr Thr Gly Cys Ala Glu His Cys Ser 165 170 (2) INFORMATION FOR SEQ ID NO:13: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:13: Asn Glu Asn Ile Thr Val Pro Asp Thr Lys Val Asn Phe Tyr Ala Trp 1 5 10 15 Lys Arg Met Glu Val Gly Gln Gln Ala Val Glu Val Trp Gln Gly Leu 20 25 30 Ala Leu Leu Ser Glu Ala Val Leu Arg Gly Gln Ala Leu Leu Val Asn 35 40 45 Ser Ser Gln Pro Trp Glu Pro Leu Gln Leu His Val Asp Lys Ala Val 50 55 60 Ser Gly Leu Arg Ser Leu Thr Thr Leu Leu Arg Ala Leu Gly Ala Gln 65 70 75 80 Lys Glu Ala Ile Ser Pro Pro Asp Ala Ala Ser Ala Ala Pro Leu Arg 85 90 95 Thr Ile Thr Ala Asp Thr Phe Arg Lys Leu Phe Arg Val Tyr Ser Asn 100 105 110 Phe Leu Arg Gly Lys Leu Lys Leu Tyr Thr Gly Glu Ala Cys Arg Thr 115 120 125 Gly Asp Arg Gly Gly Gly Ser Ala Pro Pro Arg Leu Ile Cys Asp Ser 130 135 140 Arg Val Leu Glu Arg Tyr Leu Leu Glu Ala Lys Glu Ala Glu Asn Ile 145 150 155 160 Thr Thr Gly Cys Ala Glu His Cys Ser Leu 165 170 (2) INFORMATION FOR SEQ ID NO:14: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:14: Glu Asn Ile Thr Val Pro Asp Thr Lys Val Asn Phe Tyr Ala Trp Lys 1 5 10 15 Arg Met Glu Val Gly Gln Gln Ala Val Glu Val Trp Gln Gly Leu Ala 20 25 30 Leu Leu Ser Glu Ala Val Leu Arg Gly Gln Ala Leu Leu Val Asn Ser 35 40 45 Ser Gln Pro Trp Glu Pro Leu Gln Leu His Val Asp Lys Ala Val Ser 50 55 60 Gly Leu Arg Ser Leu Thr Thr Leu Leu Arg Ala Leu Gly Ala Gln Lys 65 70 75 80 Glu Ala Ile Ser Pro Pro Asp Ala Ala Ser Ala Ala Pro Leu Arg Thr 85 90 95 Ile Thr Ala Asp Thr Phe Arg Lys Leu Phe Arg Val Tyr Ser Asn Phe 100 105 110 Leu Arg Gly Lys Leu Lys Leu Tyr Thr Gly Glu Ala Cys Arg Thr Gly 115 120 125 Asp Arg Gly Gly Gly Ser Ala Pro Pro Arg Leu Ile Cys Asp Ser Arg 130 135 140 Val Leu Glu Arg Tyr Leu Leu Glu Ala Lys Glu Ala Glu Asn Ile Thr 145 150 155 160 Thr Gly Cys Ala Glu His Cys Ser Leu Asn 165 170 (2) INFORMATION FOR SEQ ID NO:15: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:15: Asn Ile Thr Val Pro Asp Thr Lys Val Asn Phe Tyr Ala Trp Lys Arg 1 5 10 15 Met Glu Val Gly Gln Gln Ala Val Glu Val Trp Gln Gly Leu Ala Leu 20 25 30 Leu Ser Glu Ala Val Leu Arg Gly Gln Ala Leu Leu Val Asn Ser Ser 35 40 45 Gln Pro Trp Glu Pro Leu Gln Leu His Val Asp Lys Ala Val Ser Gly 50 55 60 Leu Arg Ser Leu Thr Thr Leu Leu Arg Ala Leu Gly Ala Gln Lys Glu 65 70 75 80 Ala Ile Ser Pro Pro Asp Ala Ala Ser Ala Ala Pro Leu Arg Thr Ile 85 90 95 Thr Ala Asp Thr Phe Arg Lys Leu Phe Arg Val Tyr Ser Asn Phe Leu 100 105 110 Arg Gly Lys Leu Lys Leu Tyr Thr Gly Glu Ala Cys Arg Thr Gly Asp 115 120 125 Arg Gly Gly Gly Ser Ala Pro Pro Arg Leu Ile Cys Asp Ser Arg Val 130 135 140 Leu Glu Arg Tyr Leu Leu Glu Ala Lys Glu Ala Glu Asn Ile Thr Thr 145 150 155 160 Gly Cys Ala Glu His Cys Ser Leu Asn Glu 165 170 (2) INFORMATION FOR SEQ ID NO:16: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (Ci STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:16: Ile Thr Val Pro Asp Thr Lys Val Asn Phe Tyr Ala Trp Lys Arg Met 1 5 10 15 Glu Val Gly Gln Gln Ala Val Glu Val Trp Gln Gly Leu Ala Leu Leu 20 25 30 Ser Glu Ala Val Leu Arg Gly Gln Ala Leu Leu Val Asn Ser Ser Gln 35 40 45 Pro Trp Glu Pro Leu Gln Leu His Val Asp Lys Ala Val Ser Gly Leu 50 55 60 Arg Ser Leu Thr Thr Leu Leu Arg Ala Leu Gly Ala Gln Lys Glu Ala 65 70 75 80 Ile Ser Pro Pro Asp Ala Ala Ser Ala Ala Pro Leu Arg Thr Ile Thr 85 90 95 Ala Asp Thr Phe Arg Lys Leu Phe Arg Val Tyr Ser Asn Phe Leu Arg 100 105 110 Gly Lys Leu Lys Leu Tyr Thr Gly Glu Ala Cys Arg Thr Gly Asp Arg 115 120 125 Gly Gly Gly Ser Ala Pro Pro Arg Leu Ile Cys Asp Ser Arg Val Leu 130 135 140 Glu Arg Tyr Leu Leu Glu Ala Lys Glu Ala Glu Asn Ile Thr Thr Gly 145 150 155 160 Cys Ala Glu His Cys Ser Leu Asn Glu Asn 165 170 (2) INFORMATION FOR SEQ ID NO:17: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:17: Val Pro Asp Thr Lys Val Asn Phe Tyr Ala Trp Lys Arg Met Glu Val 1 5 10 15 Gly Gln Gln Ala Val Glu Val Trp Gln Gly Leu Ala Leu Leu Ser Glu 20 25 30 Ala Val Leu Arg Gly Gln Ala Leu Leu Val Asn Ser Ser Gln Pro Trp 35 40 45 Glu Pro Leu Gln Leu His Val Asp Lys Ala Val Ser Gly Leu Arg Ser 50 55 60 Leu Thr Thr Leu Leu Arg Ala Leu Gly Ala Gln Lys Glu Ala Ile Ser 65 70 75 80 Pro Pro Asp Ala Ala Ser Ala Ala Pro Leu Arg Thr Ile Thr Ala Asp 85 90 95 Thr Phe Arg Lys Leu Phe Arg Val Tyr Ser Asn Phe Leu Arg Gly Lys 100 105 110 Leu Lys Leu Tyr Thr Gly Glu Ala Cys Arg Thr Gly Asp Arg Gly Gly 115 120 125 Gly Ser Ala Pro Pro Arg Leu Ile Cys Asp Ser Arg Val Leu Glu Arg 130 135 140 Tyr Leu Leu Glu Ala Lys Glu Ala Glu Asn Ile Thr Thr Gly Cys Ala 145 150 155 160 Glu His Cys Ser Leu Asn Glu Asn Ile Thr 165 170 (2) INFORMATION FOR SEQ ID NO:18: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:18: Pro Asp Thr Lys Val Asn Phe Tyr Ala Trp Lys Arg Met Glu Val Gly 1 5 10 15 Gln Gln Ala Val Glu Val Trp Gln Gly Leu Ala Leu Leu Ser Glu Ala 20 25 30 Val Leu Arg Gly Gln Ala Leu Leu Val Asn Ser Ser Gln Pro Trp Glu 35 40 45 Pro Leu Gln Leu His Val Asp Lys Ala Val Ser Gly Leu Arg Ser Leu 50 55 60 Thr Thr Leu Leu Arg Ala Leu Gly Ala Gln Lys Glu Ala Ile Ser Pro 65 70 75 80 Pro Asp Ala Ala Ser Ala Ala Pro Leu Arg Thr Ile Thr Ala Asp Thr 85 90 95 Phe Arg Lys Leu Phe Arg Val Tyr Ser Asn Phe Leu Arg Gly Lys Leu 100 105 110 Lys Leu Tyr Thr Gly Glu Ala Cys Arg Thr Gly Asp Arg Gly Gly Gly 115 120 125 Ser Ala Pro Pro Arg Leu Ile Cys Asp Ser Arg Val Leu Glu Arg Tyr 130 135 140 Leu Leu Glu Ala Lys Glu Ala Glu Asn Ile Thr Thr Gly Cys Ala Glu 145 150 155 160 His Cys Ser Leu Asn Glu Asn Ile Thr Val 165 170 (2) INFORMATION FOR SEQ ID NO:19: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:19: Asp Thr Lys Val Asn Phe Tyr Ala Trp Lys Arg Met Glu Val Gly Gln 1 5 10 15 Gln Ala Val Glu Val Trp Gln Gly Leu Ala Leu Leu Ser Glu Ala Val 20 25 30 Leu Arg Gly Gln Ala Leu Leu Val Asn Ser Ser Gln Pro Trp Glu Pro 35 40 45 Leu Gln Leu His Val Asp Lys Ala Val Ser Gly Leu Arg Ser Leu Thr 50 55 60 Thr Leu Leu Arg Ala Leu Gly Ala Gln Lys Glu Ala Ile Ser Pro Pro 65 70 75 80 Asp Ala Ala Ser Ala Ala Pro Leu Arg Thr Ile Thr Ala Asp Thr Phe 85 90 95 Arg Lys Leu Phe Arg Val Tyr Ser Asn Phe Leu Arg Gly Lys Leu Lys 100 105 110 Leu Tyr Thr Gly Glu Ala Cys Arg Thr Gly Asp Arg Gly Gly Gly Ser 115 120 125 Ala Pro Pro Arg Leu Ile Cys Asp Ser Arg Val Leu Glu Arg Tyr Leu 130 135 140 Leu Glu Ala Lys Glu Ala Glu Asn Ile Thr Thr Gly Cys Ala Glu His 145 150 155 160 Cys Ser Leu Asn Glu Asn Ile Thr Val Pro 165 170 (2) INFORMATION FOR SEQ ID NO:20: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:20: Arg Met Glu Val Gly Gln Gln Ala Val Glu Val Trp Gln Gly Leu Ala 1 5 10 15 Leu Leu Ser Glu Ala Val Leu Arg Gly Gln Ala Leu Leu Val Asn Ser 20 25 30 Ser Gln Pro Trp Glu Pro Leu Gln Leu His Val Asp Lys Ala Val Ser 35 40 45 Gly Leu Arg Ser Leu Thr Thr Leu Leu Arg Ala Leu Gly Ala Gln Lys 50 55 60 Glu Ala Ile Ser Pro Pro Asp Ala Ala Ser Ala Ala Pro Leu Arg Thr 65 70 75 80 Ile Thr Ala Asp Thr Phe Arg Lys Leu Phe Arg Val Tyr Ser Asn Phe 85 90 95 Leu Arg Gly Lys Leu Lys Leu Tyr Thr Gly Glu Ala Cys Arg Thr Gly 100 105 110 Asp Arg Gly Gly Gly Ser Ala Pro Pro Arg Leu Ile Cys Asp Ser Arg 115 120 125 Val Leu Glu Arg Tyr Leu Leu Glu Ala Lys Glu Ala Glu Asn Ile Thr 130 135 140 Thr Gly Cys Ala Glu His Cys Ser Leu Asn Glu Asn Ile Thr Val Pro 145 150 155 160 Asp Thr Lys Val Asn Phe Tyr Ala Trp Lys 165 170 (2) INFORMATION FOR SEQ ID NO:21: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:21: Met Glu Val Gly Gln Gln Ala Val Glu Val Trp Gln Gly Leu Ala Leu 1 5 10 15 Leu Ser Glu Ala Val Leu Arg Gly Gln Ala Leu Leu Val Asn Ser Ser 20 25 30 Gln Pro Trp Glu Pro Leu Gln Leu His Val Asp Lys Ala Val Ser Gly 35 40 45 Leu Arg Ser Leu Thr Thr Leu Leu Arg Ala Leu Gly Ala Gln Lys Glu 50 55 60 Ala Ile Ser Pro Pro Asp Ala Ala Ser Ala Ala Pro Leu Arg Thr Ile 65 70 75 80 Thr Ala Asp Thr Phe Arg Lys Leu Phe Arg Val Tyr Ser Asn Phe Leu 85 90 95 Arg Gly Lys Leu Lys Leu Tyr Thr Gly Glu Ala Cys Arg Thr Gly Asp 100 105 110 Arg Gly Gly Gly Ser Ala Pro Pro Arg Leu Ile Cys Asp Ser Arg Val 115 120 125 Leu Glu Arg Tyr Leu Leu Glu Ala Lys Glo Ala Glu Asn Ile Thr Thr 130 135 140 Gly Cys Ala Glu His Cys Ser Leu Asn Glu Asn Ile Thr Val Pro Asp 145 150 155 160 Thr Lys Val Asn Phe Tyr Ala Trp Lys Arg 165 170 (2) INFORMATION FOR SEQ ID NO:22: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:22: Glu Val Gly Gln Gln Ala Val Glu Val Trp Gln Gly Leu Ala Leu Leu 1 5 10 15 Ser Glu Ala Val Leu Arg Gly Gln Ala Leu Leu Val Asn Ser Ser Gln 20 25 30 Pro Trp Glu Pro Leu Gln Leu His Val Asp Lys Ala Val Ser Gly Leu 35 40 45 Arg Ser Leu Thr Thr Leu Leu Arg Ala Leu Gly Ala Gln Lys Glu Ala 50 55 60 Ile Ser Pro Pro Asp Ala Ala Ser Ala Ala Pro Leu Arg Thr Ile Thr 65 70 75 80 Ala Asp Thr Phe Arg Lys Leu Phe Arg Val Tyr Ser Asn Phe Leu Arg 85 90 95 Gly Lys Leu Lys Leu Tyr Thr Gly Glu Ala Cys Arg Thr Gly Asp Arg 100 105 110 Gly Gly Gly Ser Ala Pro Pro Arg Leu Ile Cys Asp Ser Arg Val Leu 115 120 125 Glu Arg Tyr Leu Leu Glu Ala Lys Glu Ala Glu Asn Ile Thr Thr Gly 130 135 140 Cys Ala Glu His Cys Ser Leu Asn Glu Asn Ile Thr Val Pro Asp Thr 145 150 155 160 Lys Val Asn Phe Tyr Ala Trp Lys Arg Met 165 170 (2) INFORMATION FOR SEQ ID NO:23: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:23: Val Gly Gln Gln Ala Val Glu Val Trp Gln Gly Leu Ala Leu Leu Ser 1 5 10 15 Glu Ala Val Leu Arg Gly Gln Ala Leu Leu Val Asn Ser Ser Gln Pro 20 25 30 Trp Glu Pro Leu Gln Leu His Val Asp Lys Ala Val Ser Gly Leu Arg 35 40 45 Ser Leu Thr Thr Leu Leu Arg Ala Leu Gly Ala Gln Lys Glu Ala Ile 50 55 60 Ser Pro Pro Asp Ala Ala Ser Ala Ala Pro Leu Arg Thr Ile Thr Ala 65 70 75 80 Asp Thr Phe Arg Lys Leu Phe Arg Val Tyr Ser Asn Phe Leu Arg Gly 85 90 95 Lys Leu Lys Leu Tyr Thr Gly Glu Ala Cys Arg Thr Gly Asp Arg Gly 100 105 110 Gly Gly Ser Ala Pro Pro Arg Leu Ile Cys Asp Ser Arg Val Leu Glu 115 120 125 Arg Tyr Leu Leu Glu Ala Lys Glu Ala Glu Asn Ile Thr Thr Gly Cys 130 135 140 Ala Glu His Cys Ser Leu Asn Glu Asn Ile Thr Val Pro Asp Thr Lys 145 150 155 160 Val Asn Phe Tyr Ala Trp Lys Arg Met Glu 165 170 (2) INFORMATION FOR SEQ ID NO:24: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:24: Gln Ala Leu Leu Val Asn Ser Ser Gln Pro Trp Glu Pro Leu Gln Leu 1 5 10 15 His Val Asp Lys Ala Val Ser Gly Leu Arg Ser Leu Thr Thr Leu Leu 20 25 30 Arg Ala Le Gly Ala Gln Lys Glu Ala Ile Ser Pro Pro Asp Ala Ala 35 40 45 Ser Ala Ala Pro Leu Arg Thr Ile Thr Ala Asp Thr Phe Arg Lys Leu 50 55 60 Phe Arg Val Tyr Ser Asn Phe Leu Arg Gly Lys Leu Lys Leu Tyr Thr 65 70 75 80 Gly Glu Ala Cys Arg Thr Gly Asp Arg Gly Gly Gly Ser Ala Pro Pro 85 90 95 Arg Leu Ile Cys Asp Ser Arg Val Leu Glu Arg Tyr Leu Leu Glu Ala 100 105 110 Lys Glu Ala Glu Asn Ile Thr Thr Gly Cys Ala Glu His Cys Ser Leu 115 120 125 Asn Glu Asn Ile Thr Val Pro Asp Thr Lys Val Asn Phe Tyr Ala Trp 130 135 140 Lys Arg Met Glu Val Gly Gln Gln Ala Val Glu Val Trp Gln Gly Leu 145 150 155 160 Ala Leu Leu Ser Glu Ala Val Leu Arg Gly 165 170 (2) INFORMATION FOR SEQ ID NO:25: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:25: Ala Leu Leu Val Asn Ser Ser Gln Pro Trp Glu Pro Leu Gln Leu His 1 5 10 15 Val Asp Lys Ala Val Ser Gly Leu Arg Ser Leu Thr Thr Leu Leu Arg 20 25 30 Ala Leu Gly Ala Gln Lys Glu Ala Ile Ser Pro Pro Asp Ala Ala Ser 35 40 45 Ala Ala Pro Leu Arg Thr Ile Thr Ala Asp Thr Phe Arg Lys Leu Phe 50 55 60 Arg Val Tyr Ser Asn Phe Leu Arg Gly Lys Leu Lys Leu Tyr Thr Gly 65 70 75 80 Glu Ala Cys Arg Thr Gly Asp Arg Gly Gly Gly Ser Ala Pro Pro Arg 85 90 95 Leu Ile Cys Asp Ser Arg Val Leu Glu Arg Tyr Leu Leu Glu Ala Lys 100 105 110 Glu Ala Glu Asn Ile Thr Thr Gly Cys Ala Glu His Cys Ser Leu Asn 115 120 125 Glu Asn Ile Thr Val Pro Asp Thr Lys Val Asn Phe Tyr Ala Trp Lys 130 135 140 Arg Met Glu Val Gly Gln Gln Ala Val Glu Val Trp Gln Gly Leu Ala 145 150 155 160 Leu Leu Ser Glu Ala Val Leu Arg Gly Gln 165 170 (2) INFORMATION FOR SEQ ID NO:26: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:26: Leu Leu Val Asn Ser Ser Gln Pro Trp Glu Pro Leu Gln Leu His Val 1 5 10 15 Asp Lys Ala Val Ser Gly Leu Arg Ser Leu Thr Thr Leu Leu Arg Ala 20 25 30 Leu Gly Ala Gln Lys Glu Ala Ile Ser Pro Pro Asp Ala Ala Ser Ala 35 40 45 Ala Pro Leu Arg Thr Ile Thr Ala Asp Thr Phe Arg Lys Leu Phe Arg 50 55 60 Val Tyr Ser Asn Phe Leu Arg Gly Lys Leu Lys Leu Tyr Thr Gly Glu 65 70 75 80 Ala Cys Arg Thr Gly Asp Arg Gly Gly Gly Ser Ala Pro Pro Arg Leu 85 90 95 Ile Cys Asp Ser Arg Val Leu Glu Arg Tyr Leu Leu Glu Ala Lys Glu 100 105 110 Ala Glu Asn Ile Thr Thr Gly Cys Ala Glu His Cys Ser Leu Asn Glu 115 120 125 Asn Ile Thr Val Pro Asp Thr Lys Val Asn Phe Tyr Ala Trp Lys Arg 130 135 140 Met Glu Val Gly Gln Gln Ala Val Glu Val Trp Gln Gly Leu Ala Leu 145 150 155 160 Leu Ser Glu Ala Val Leu Arg Gly Gln Ala 165 170 (2) INFORMATION FOR SEQ ID NO:27: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:27: Leu Val Asn Ser Ser Gln Pro Trp Glu Pro Leu Gln Leu His Val Asp 1 5 10 15 Lys Ala Val Ser Gly Leu Arg Ser Leu Thr Thr Leu Leu Arg Ala Leu 20 25 30 Gly Ala Gln Lys Glu Ala Ile Ser Pro Pro Asp Ala Ala Ser Ala Ala 35 40 45 Pro Leu Arg Thr Ile Thr Ala Asp Thr Phe Arg Lys Leu Phe Arg Val 50 55 60 Tyr Ser Asn Phe Leu Arg Gly Lys Leu Lys Leu Tyr Thr Gly Glu Ala 65 70 75 80 Cys Arg Thr Gly Asp Arg Gly Gly Gly Ser Ala Pro Pro Arg Leu Ile 85 90 95 Cys Asp Ser Arg Val Leu Glu Arg Tyr Leu Leu Glu Ala Lys Glu Ala 100 105 110 Glu Asn Ile Thr Thr Gly Cys Ala Glu His Cys Ser Leu Asn Glu Asn 115 120 125 Ile Thr Val Pro Asp Thr Lys Val Asn Phe Tyr Ala Trp Lys Arg Met 130 135 140 Glu Val Gly Gln Gln Ala Val Glu Val Trp Gln Gly Leu Ala Leu Leu 145 150 155 160 Ser Glu Ala Val Leu Arg Gly Gln Ala Leu 165 170 (2) INFORMATION FOR SEQ ID NO:28: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (li) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:28: Val Asn Ser Ser Gln Pro Trp Glu Pro Leu Gln Leu His Val Asp Lys 1 5 10 15 Ala Val Ser Gly Leu Arg Ser Leu Thr Thr Leu Leu Arg Ala Leu Gly 20 25 30 Ala Gln Lys Glu Ala Ile Ser Pro Pro Asp Ala Ala Ser Ala Ala Pro 35 40 45 Leu Arg Thr Ile Thr Ala Asp Thr Phe Arg Lys Leu Phe Arg Val Tyr 50 55 60 Ser Asn Phe Leu Arg Gly Lys Leu Lys Leu Tyr Thr Gly Glu Ala Cys 65 70 75 80 Arg Thr Gly Asp Arg Gly Gly Gly Ser Ala Pro Pro Arg Leu Ile Cys 85 90 95 Asp Ser Arg Val Leu Glu Arg Tyr Leu Leu Glu Ala Lys Glu Ala Glu 100 105 110 Asn Ile Thr Thr Gly Cys Ala Glu His Cys Ser Leu Asn Glu Asn Ile 115 120 125 Thr Val Pro Asp Thr Lys Val Asn Phe Tyr Ala Trp Lys Arg Met Glu 130 135 140 Val Gly Gln Gln Ala Val Glu Val Trp Gln Gly Leu Ala Leu Leu Ser 145 150 155 160 Glu Ala Val Leu Arg Gly Gln Ala Leu Leu 165 170 (2) INFORMATION FOR SEQ ID NO:29: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:29: Asn Ser Ser Gln Pro Trp Glu Pro Leu Gln Leu His Val Asp Lys Ala 1 5 10 15 Val Ser Gly Leu Arg Ser Leu Thr Thr Leu Leu Arg Ala Leu Gly Ala 20 25 30 Gln Lys Glu Ala Ile Ser Pro Pro Asp Ala Ala Ser Ala Ala Pro Leu 35 40 45 Arg Thr Ile Thr Ala Asp Thr Phe Arg Lys Leu Phe Arg Val Tyr Ser 50 55 60 Asn Phe Leu Arg Gly Lys Leu Lys Leu Tyr Thr Gly Glu Ala Cys Arg 65 70 75 80 Thr Gly Asp Arg Gly Gly Gly Ser Ala Pro Pro Arg Leu Ile Cys Asp 85 90 95 Ser Arg Val Leu Glu Arg Tyr Leu Leu Glu Ala Lys Glu Ala Glu Asn 100 105 110 Ile Thr Thr Gly Cys Ala Glu His Cys Ser Leu Asn Glu Asn Ile Thr 115 120 125 Val Pro Asp Thr Lys Val Asn Phe Tyr Ala Trp Lys Arg Met Glu Val 130 135 140 Gly Gln Gln Ala Val Glu Val Trp Gln Gly Leu Ala Leu Leu Ser Glu 145 150 155 160 Ala Val Leu Arg Gly Gln Ala Leu Leu Val 165 170 (2) INFORMATION FOR SEQ ID NO:30: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SQ ID NO:30: Ser Ser Gln Pro Trp Glu Pro Leu Gln Leu His Val Asp Lys Ala Val 1 5 10 15 Ser Gly Leu Arg Ser Leu Thr Thr Leu Leo Arg Ala Leu Gly Ala Gln 20 25 30 Lys Glu Ala Ile Ser Pro Pro Asp Ala Ala Ser Ala Ala Pro Leu Arg 35 40 45 Thr Ile Thr Ala Asp Thr Phe Arg Lys Leu Phe Arg Val Tyr Ser Asn 50 55 60 Phe Leu Arg Gly Lys Leu Lys Leu Tyr Thr Gly Glu Ala Cys Arg Thr 65 70 75 80 Gly Asp Arg Gly Gly Gly Ser Ala Pro Pro Arg Leu Ile Cys Asp Ser 85 90 95 Arg Val Leu Glu Arg Tyr Leu Leu Glu Ala Lys Glu Ala Glu Asn Ile 100 105 110 Thr Thr Gly Cys Ala Glu His Cys Ser Leu Asn Glu Asn Ile Thr Val 115 120 125 Pro Asp Thr Lys Val Asn Phe Tyr Ala Trp Lys Arg Met Glu Val Gly 130 135 140 Gln Gln Ala Val Glu Val Trp Gln Gly Leu Ala Leu Leu Ser Glu Ala 145 150 155 160 Val Leu Arg Gly Gln Ala Leu Leu Val Asn 165 170 (2) INFORMATION FOR SEQ ID NO:31: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:31: Ser Gln Pro Trp Glu Pro Leu Gln Leu His Val Asp Lys Ala Val Ser 1 5 10 15 Gly Leu Arg Ser Leu Thr Thr Leu Leu Arg Ala Leu Gly Ala Gln Lys 20 25 30 Glu Ala Ile Ser Pro Pro Asp Ala Ala Ser Ala Ala Pro Leu Arg Thr 35 40 45 Ile Thr Ala Asp Thr Phe Arg Lys Leu Phe Arg Val Tyr Ser Asn Phe 50 55 60 Leu Arg Gly Lys Leu Lys Leu Tyr Thr Gly Glu Ala Cys Arg Thr Gly 65 70 75 80 Asp Arg Gly Gly Gly Ser Ala Pro Pro Arg Leu Ile Cys Asp Ser Arg 85 90 95 Val Leu Glu Arg Tyr Leu Leu Glu Ala Lys Glu Ala Glu Asn Ile Thr 100 105 110 Thr Gly Cys Ala Glu His Cys Ser Leu Asn Glu Asn Ile Thr Val Pro 115 120 125 Asp Thr Lys Val Asn Phe Tyr Ala Trp Lys Arg Met Glu Val Gly Gln 130 135 140 Gln Ala Val Glu Val Trp Gln Gly Leu Ala Leu Leu Ser Glu Ala Val 145 150 155 160 Leu Arg Gly Gln Ala Leu Leu Val Asn Ser 165 170 (2) INFORMATION FOR SEQ ID NO:32: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:32: Gln Pro Trp Glu Pro Leu Gln Leu His Val Asp Lys Ala Val Ser Gly 1 5 10 15 Leu Arg Ser Leu Thr Thr Leu Leu Arg Ala Leu Gly Ala Gln Lys Glu 20 25 30 Ala Ile Ser Pro Pro Asp Ala Ala Ser Ala Ala Pro Leo Arg Thr Ile 35 40 45 Thr Ala Asp Thr Phe Arg Lys Leu Phe Arg Val Tyr Ser Asn Phe Leu 50 55 60 Arg Gly Lys Leu Lys Leu Tyr Thr Gly Glu Ala Cys Arg Thr Gly Asp 65 70 75 80 Arg Gly Gly Gly Ser Ala Pro Pro Arg Leu Ile Cys Asp Ser Arg Val 85 90 95 Leu Glu Arg Tyr Leu Leu Glu Ala Lys Glu Ala Glu Asn Ile Thr Thr 100 105 110 Gly Cys Ala Glu His Cys Ser Leu Asn Glu Asn Ile Thr Val Pro Asp 115 120 125 Thr Lys Val Asn Phe Tyr Ala Trp Lys Arg Met Glu Val Gly Gln Gln 130 135 140 Ala Val Glu Val Trp Gln Gly Leu Ala Leu Leu Ser Glu Ala Val Leu 145 150 155 160 Arg Gly Gln Ala Leu Leu Val Asn Ser Ser 165 170 (2) INFORMATION FOR SEQ ID NO:33: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:33: Pro Trp Glu Pro Leu Gln Leu His Val Asp Lys Ala Val Ser Gly Leu 1 5 10 15 Arg Ser Leu Thr Thr Leu Leu Arg Ala Leu Gly Ala Gln Lys Glu Ala 20 25 30 Ile Ser Pro Pro Asp Ala Ala Ser Ala Ala Pro Leu Arg Thr Ile Thr 35 40 45 Ala Asp Thr Phe Arg Lys Leu Phe Arg Val Tyr Ser Asn Phe Leu Arg 50 55 60 Gly Lys Leu Lys Leu Tyr Thr Gly Glu Ala Cys Arg Thr Gly Asp Arg 65 70 75 80 Gly Gly Gly Ser Ala Pro Pro Arg Leu Ile Cys Asp Ser Arg Val Leu 85 90 95 Glu Arg Tyr Leu Leu Glu Ala Lys Glu Ala Glu Asn Ile Thr Thr Gly 100 105 110 Cys Ala Glu His Cys Ser Leu Asn Glu Asn Ile Thr Val Pro Asp Thr 115 120 125 Lys Val Asn Phe Tyr Ala Trp Lys Arg Met Glu Val Gly Gln Gln Ala 130 135 140 Val Glu Val Trp Gln Gly Leu Ala Leu Leu Ser Glu Ala Val Leu Arg 145 150 155 160 Gly Gln Ala Leu Leu Val Asn Ser Ser Gln 165 170 (2) INFORMATION FOR SEQ ID NO:34: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:34: Trp Glu Pro Leu Gln Leu His Val Asp Lys Ala Val Ser Gly Leu Arg 1 5 10 15 Ser Leu Thr Thr Leu Leu Arg Ala Leu Gly Ala Gln Lys Glu Ala Ile 20 25 30 Ser Pro Pro Asp Ala Ala Ser Ala Ala Pro Leu Arg Thr Ile Thr Ala 35 40 45 Asp Thr Phe Arg Lys Leu Phe Arg Val Tyr Ser Asn Phe Leu Arg Gly 50 55 60 Lys Leu Lys Leu Tyr Thr Gly Glu Ala Cys Arg Thr Gly Asp Arg Gly 65 70 75 80 Gly Gly Ser Ala Pro Pro Arg Leu Ile Cys Asp Ser Arg Val Leu Glu 85 90 95 Arg Tyr Leu Leu Glu Ala Lys Glu Ala Glu Asn Ile Thr Thr Gly Cys 100 105 110 Ala Glu His Cys Ser Leu Asn Glu Asn Ile Thr Val Pro Asp Thr Lys 115 120 125 Val Asn Phe Tyr Ala Trp Lys Arg Met Glu Val Gly Gln Gln Ala Val 130 135 140 Glu Val Trp Gln Gly Leu Ala Leu Leu Ser Glu Ala Val Leu Arg Gly 145 150 155 160 Gln Ala Leu Leu Val Asn Ser Ser Gln Pro 165 170 (2) INFORMATION FOR SEQ ID NO:35: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:35: Glu Pro Leu Gln Leu His Val Asp Lys Ala Val Ser Gly Leu Arg Ser 1 5 10 15 Leu Thr Thr Leu Leu Arg Ala Leu Gly Ala Gln Lys Glu Ala Ile Ser 20 25 30 Pro Pro Asp Ala Ala Ser Ala Ala Pro Leu Arg Thr Ile Thr Ala Asp 35 40 45 Thr Phe Arg Lys Leu Phe Arg Val Tyr Ser Asn Phe Leu Arg Gly Lys 50 55 60 Leu Lys Leu Tyr Thr Gly Glu Ala Cys Arg Thr Gly Asp Arg Gly Gly 65 70 75 80 Gly Ser Ala Pro Pro Arg Leu Ile Cys Asp Ser Arg Val Leu Glu Arg 85 90 95 Tyr Leu Leu Glu Ala Lys Glu Ala Glu Asn Ile Thr Thr Gly Cys Ala 100 105 110 Glu His Cys Ser Leu Asn Glu Asn Ile Thr Val Pro Asp Thr Lys Val 115 120 125 Asn Phe Tyr Ala Trp Lys Arg Met Glu Val Gly Gln Gln Ala Val Glu 130 135 140 Val Trp Gln Gly Leu Ala Leu Leu Ser Glu Ala Val Leu Arg Gly Gln 145 150 155 160 Ala Leu Leu Val Asn Ser Ser Gln Pro Trp 165 170 (2) INFORMATION FOR SEQ ID NO:36: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:36: Leu Arg Ala Leu Gly Ala Gln Lys Glu Ala Ile Ser Pro Pro Asp Ala 1 5 10 15 Ala Ser Ala Ala Pro Leu Arg Thr Ile Thr Ala Asp Thr Phe Arg Lys 20 25 30 Leu Phe Arg Val Tyr Ser Asn Phe Leu Arg Gly Lys Leu Lys Leu Tyr 35 40 45 Thr Gly Glu Ala Cys Arg Thr Gly Asp Arg Gly Gly Gly Ser Ala Pro 50 55 60 Pro Arg Leu Ile Cys Asp Ser Arg Val Leu Glu Arg Tyr Leu Leu Glu 65 70 75 80 Ala Lys Glu Ala Glu Asn Ile Thr Thr Gly Cys Ala Glu His Cys Ser 85 90 95 Leu Asn Glu Asn Ile Thr Val Pro Asp Thr Lys Val Asn Phe Tyr Ala 100 105 110 Trp Lys Arg Met Glu Val Gly Gln Gln Ala Val Glu Val Trp Gln Gly 115 120 125 Leu Ala Leu Leu Ser Glu Ala Val Leu Arg Gly Gln Ala Leu Leu Val 130 135 140 Asn Ser Ser Gln Pro Trp Glu Pro Leu Gln Leu His Val Asp Lys Ala 145 150 155 160 Val Ser Gly Leu Arg Ser Leu Thr Thr Leu 165 170 (2) INFORMATION FOR SEQ ID NO:37: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:37: Arg Ala Leu Gly Ala Gln Lys Glu Ala Ile Ser Pro Pro Asp Ala Ala 1 5 10 15 Ser Ala Ala Pro Leu Arg Thr Ile Thr Ala Asp Thr Phe Arg Lys Leu 20 25 30 Phe Arg Val Tyr Ser Asn Phe Leu Arg Gly Lys Leu Lys Leu Tyr Thr 35 40 45 Gly Glu Ala Cys Arg Thr Gly Asp Arg Gly Gly Gly Ser Ala Pro Pro 50 55 60 Arg Leu Ile Cys Asp Ser Arg Val Leu Glu Arg Tyr Leu Leu Glu Ala 65 70 75 80 Lys Glu Ala Glu Asn Ile Thr Thr Gly Cys Ala Glu His Cys Ser Leu 85 90 95 Asn Glu Asn Ile Thr Val Pro Asp Thr Lys Val Asn Phe Tyr Ala Trp 100 105 110 Lys Arg Met Glu Val Gly Gln Gln Ala Val Glu Val Trp Gln Gly Leu 115 120 125 Ala Leu Leu Ser Glu Ala Val Leu Arg Gly Gln Ala Leu Leu Val Asn 130 135 140 Ser Ser Gln Pro Trp Glu Pro Leu Gln Leu His Val Asp Lys Ala Val 145 150 155 160 Ser Gly Leu Arg Ser Leu Thr Thr Leu Leu 165 170 (2) INFORMATION FOR SEQ ID NO:38: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:38: Ala Leu Gly Ala Gln Lys Glu Ala Ile Ser Pro Pro Asp Ala Ala Ser 1 5 10 15 Ala Ala Pro Leu Arg Thr Ile Thr Ala Asp Thr Phe Arg Lys Leu Phe 20 25 30 Arg Val Tyr Ser Asn Phe Leu Arg Gly Lys Leu Lys Leu Tyr Thr Gly 35 40 45 Glu Ala Cys Arg Thr Gly Asp Arg Gly Gly Gly Ser Ala Pro Pro Arg 50 55 60 Leu Ile Cys Asp Ser Arg Val Leu Glu Arg Tyr Leu Leu Glu Ala Lys 65 70 75 80 Glu Ala Glu Asn Ile Thr Thr Gly Cys Ala Glu His Cys Ser Leu Asn 85 90 95 Glu Asn Ile Thr Val Pro Asp Thr Lys Val Asn Phe Tyr Ala Trp Lys 100 105 110 Arg Met Glu Val Gly Gln Gln Ala Val Glu Val Trp Gln Gly Leu Ala 115 120 125 Leu Leu Ser Glu Ala Val Leu Arg Gly Gln Ala Leu Leu Val Asn Ser 130 135 140 Ser Gln Pro Trp Glu Pro Leu Gln Leu His Val Asp Lys Ala Val Ser 145 150 155 160 Gly Leu Arg Ser Leu Thr Thr Leu Leu Arg 165 170 (2) INFORMATION FOR SEQ ID NO:39: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:39: Leu Gly Ala Gln Lys Glu Ala Ile Ser Pro Pro Asp Ala Ala Ser Ala 1 5 10 15 Ala Pro Leu Arg Thr Ile Thr Ala Asp Thr Phe Arg Lys Leu Phe Arg 20 25 30 Val Tyr Ser Asn Phe Leu Arg Gly Lys Leu Lys Leu Tyr Thr Gly Glu 35 40 45 Ala Cys Arg Thr Gly Asp Arg Gly Gly Gly Ser Ala Pro Pro Arg Leu 50 55 60 Ile Cys Asp Ser Arg Val Leu Glu Arg Tyr Leu Leu Glu Ala Lys Glu 65 70 75 80 Ala Glu Asn Ile Thr Thr Gly Cys Ala Glu His Cys Ser Leu Asn Glu 85 90 95 Asn Ile Thr Val Pro Asp Thr Lys Val Asn Phe Tyr Ala Trp Lys Arg 100 105 110 Met Glu Val Gly Gln Gln Ala Val Glu Val Trp Gln Gly Leu Ala Leu 115 120 125 Leu Ser Glu Ala Val Leu Arg Gly Gln Ala Leu Leu Val Asn Ser Ser 130 135 140 Gln Pro Trp Glu Pro Leu Gln Leu His Val Asp Lys Ala Val Ser Gly 145 150 155 160 Leu Arg Ser Leu Thr Thr Leu Leu Arg Ala 165 170 (2) INFORMATION FOR SEQ ID NO:40: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:40: Gly Ala Gln Lys Glu Ala Ile Ser Pro Pro Asp Ala Ala Ser Ala Ala 1 5 10 15 Pro Leu Arg Thr Ile Thr Ala Asp Thr Phe Arg Lys Leu Phe Arg Val 20 25 30 Tyr Ser Asn Phe Leu Arg Gly Lys Leu Lys Leu Tyr Thr Gly Glu Ala 35 40 45 Cys Arg Thr Gly Asp Arg Gly Gly Gly Ser Ala Pro Pro Arg Leu Ile 50 55 60 Cys Asp Ser Arg Val Leu Glu Arg Tyr Leu Leu Glu Ala Lys Glu Ala 65 70 75 80 Glu Asn Ile Thr Thr Gly Cys Ala Glu His Cys Ser Leu Asn Glu Asn 85 90 95 Ile Thr Val Pro Asp Thr Lys Val Asn Phe Tyr Ala Trp Lys Arg Met 100 105 110 Glu Val Gly Gln Gln Ala Val Glu Val Trp Gln Gly Leu Ala Leu Leu 115 120 125 Ser Glu Ala Val Leu Arg Gly Gln Ala Leu Leu Val Asn Ser Ser Gln 130 135 140 Pro Trp Glu Pro Leu Gln Leu His Val Asp Lys Ala Val Ser Gly Leu 145 150 155 160 Arg Ser Leu Thr Thr Leu Leu Arg Ala Leu 165 170 (2) INFORMATION FOR SEQ ID NO:41: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:41: Ala Gln Lys Glu Ala Ile Ser Pro Pro Asp Ala Ala Ser Ala Ala Pro 1 5 10 15 Leu Arg Thr Ile Thr Ala Asp Thr Phe Arg Lys Le Phe Arg Val Tyr 20 25 30 Ser Asn Phe Leu Arg Gly Lys Leu Lys Leu Tyr Thr Gly Glu Ala Cys 35 40 45 Arg Thr Gly Asp Arg Gly Gly Gly Ser Ala Pro Pro Arg Leu Ile Cys 50 55 60 Asp Ser Arg Val Leu Glu Arg Tyr Leu Leu Glu Ala Lys Glu Ala Glu 65 70 75 80 Asn Ile Thr Thr Gly Cys Ala Glu His Cys Ser Leu Asn Glu Asn Ile 85 90 95 Thr Val Pro Asp Thr Lys Val Asn Phe Tyr Ala Trp Lys Arg Met Glu 100 105 110 Val Gly Gln Gln Ala Val Glu Val Trp Gln Gly Leu Ala Leu Leu Ser 115 120 125 Glu Ala Val Leu Arg Gly Gln Ala Leu Leu Val Asn Ser Ser Gln Pro 130 135 140 Trp Glu Pro Leu Gln Leu His Val Asp Lys Ala Val Ser Gly Leu Arg 145 150 155 160 Ser Leu Thr Thr Leu Leu Arg Ala Leu Gly 165 170 (2) INFORMATION FOR SEQ ID NO:42: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:42: Gln Lys Glu Ala Ile Ser Pro Pro Asp Ala Ala Ser Ala Ala Pro Leu 1 5 10 15 Arg Thr Ile Thr Ala Asp Thr Phe Arg Lys Leu Phe Arg Val Tyr Ser 20 25 30 Asn Phe Leu Arg Gly Lys Leu Lys Leu Tyr Thr Gly Glu Ala Cys Arg 35 40 45 Thr Gly Asp Arg Gly Gly Gly Ser Ala Pro Pro Arg Leu Ile Cys Asp 50 55 60 Ser Arg Val Leu Glu Arg Tyr Leu Leu Glu Ala Lys Glu Ala Glu Asn 65 70 75 80 Ile Thr Thr Gly Cys Ala Glu His Cys Ser Leu Asn Glu Asn Ile Thr 85 90 95 Val Pro Asp Thr Lys Val Asn Phe Tyr Ala Trp Lys Arg Met Glu Val 100 105 110 Gly Gln Gln Ala Val Glu Val Trp Gln Gly Leu Ala Leu Leu Ser Glu 115 120 125 Ala Val Leu Arg Gly Gln Ala Leu Leu Val Asn Ser Ser Gln Pro Trp 130 135 140 Glu Pro Leu Gln Leu His Val Asp Lys Ala Val Ser Gly Leu Arg Ser 145 150 155 160 Leu Thr Thr Leu Leu Arg Ala Leu Gly Ala 165 170 (2) INFORMATION FOR SEQ ID NO:43: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:43: Lys Glu Ala Ile Ser Pro Pro Asp Ala Ala Ser Ala Ala Pro Leu Arg 1 5 10 15 Thr Ile Thr Ala Asp Thr Phe Arg Lys Leu Phe Arg Val Tyr Ser Asn 20 25 30 Phe Leu Arg Gly Lys Leu Lys Leu Tyr Thr Gly Glu Ala Cys Arg Thr 35 40 45 Gly Asp Arg Gly Gly Gly Ser Ala Pro Pro Arg Leu Ile Cys Asp Ser 50 55 60 Arg Val Leu Glu Arg Tyr Leu Leu Glu Ala Lys Glu Ala Glu Asn Ile 65 70 1 75 80 Thr Thr Gly Cys Ala Glu His Cys Ser Leu Asn Glu Asn Ile Thr Val 85 90 95 Pro Asp Thr Lys Val Asn Phe Tyr Ala Trp Lys Arg Met Glu Val Gly 100 105 110 Gln Gln Ala Val Glu Val Trp Gln Gly Leu Ala Leu Leu Ser Glu Ala 115 120 125 Val Leu Arg Gly Gln Ala Leu Leu Val Asn Ser Ser Gln Pro Trp Glu 130 135 140 Pro Leu Gln Leu His Val Asp Lys Ala Val Ser Gly Leu Arg Ser Leu 145 150 155 160 Thr Thr Leu Leu Arg Ala Leu Gly Ala Gln 165 170 (2) INFORMATION FOR SEQ ID NO:44: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:44: Glu Ala Ile Ser Pro Pro Asp Ala Ala Ser Ala Ala Pro Leu Arg Thr 1 5 10 15 Ile Thr Ala Asp Thr Phe Arg Lys Leu Phe Arg Val Tyr Ser Asn Phe 20 25 30 Leu Arg Gly Lys Leu Lys Leu Tyr Thr Gly Glu Ala Cys Arg Thr Gly 35 40 45 Asp Arg Gly Gly Gly Ser Ala Pro Pro Arg Leu Ile Cys Asp Ser Arg 50 55 60 Val Leu Glu Arg Tyr Leu Leu Glu Ala Lys Glu Ala Glu Asn Ile Thr 65 70 75 80 Thr Gly Cys Ala Glu His Cys Ser Leu Asn Glu Asn Ile Thr Val Pro 85 90 95 Asp Thr Lys Val Asn Phe Tyr Ala Trp Lys Arg Met Glu Val Gly Gln 100 105 110 Gln Ala Val Glu Val Trp Gln Gly Leu Ala Leu Leu Ser Glu Ala Val 115 120 125 Leu Arg Gly Gln Ala Leu Leu Val Asn Ser Ser Gln Pro Trp Glu Pro 130 135 140 Leu Gln Leu His Val Asp Lys Ala Val Ser Gly Leu Arg Ser Leu Thr 145 150 155 160 Thr Leu Leu Arg Ala Leu Gly Ala Gln Lys 165 170 (2) INFORMATION FOR SEQ ID NO:45: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:5: Ala Ile Ser Pro Pro Asp Ala Ala Ser Ala Ala Pro Leu Arg Thr Ile 1 5 10 15 Thr Ala Asp Thr Phe Arg Lys Leu Phe Arg Val Tyr Ser Asn Phe Leu 20 25 30 Arg Gly Lys Leu Lys Leu Tyr Thr Gly Glu Ala Cys Arg Thr Gly Asp 35 40 45 Arg Gly Gly Gly Ser Ala Pro Pro Arg Leu Ile Cys Asp Ser Arg Val 50 55 60 Leu Glu Arg Tyr Leu Leu Glu Ala Lys Glu Ala Glu Asn Ile Thr Thr 65 70 75 80 Gly Cys Ala Glu His Cys Ser Leu Asn Glu Asn Ile Thr Val Pro Asp 85 90 95 Thr Lys Val Asn Phe Tyr Ala Trp Lys Arg Met Glu Val Gly Gln Gln 100 105 110 Ala Val Glu Val Trp Gln Gly Leu Ala Leu Leu Ser Glu Ala Val Leu 115 120 125 Arg Gly Gln Ala Leu Leu Val Asn Ser Ser Gln Pro Trp Glu Pro Leu 130 135 140 Gln Leu His Val Asp Lys Ala Val Ser Gly Leu Arg Ser Leu Thr Thr 145 150 155 160 Leu Leu Arg Ala Leu Gly Ala Gln Lys Glu 165 170 (2) INFORMATION FOR SEQ ID NO:46: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:46: Ile Ser Pro Pro Asp Ala Ala Ser Ala Ala Pro Leu Arg Thr Ile Thr 1 5 10 15 Ala Asp Thr Phe Arg Lys Leu Phe Arg Val Tyr Ser Asn Phe Leu Arg 20 25 30 Gly Lys Le Lys Leu Tyr Thr Gly Glu Ala Cys Arg Thr Gly Asp Arg 35 40 45 Gly Gly Gly Ser Ala Pro Pro Arg Leu Ile Cys Asp Ser Arg Val Leu 50 55 60 Glu Arg Tyr Leu Leu Glu Ala Lys Glu Ala Glu Asn Ile Thr Thr Gly 65 70 75 80 Cys Ala Glu His Cys Ser Leu Asn Glu Asn Ile Thr Val Pro Asp Thr 85 90 95 Lys Val Asn Phe Tyr Ala Trp Lys Arg Met Glu Val Gly Gln Gln Ala 100 105 110 Val Glu Val Trp Gln Gly Leu Ala Leu Leu Ser Glu Ala Val Leu Arg 115 120 125 Gly Gln Ala Leu Leu Val Asn Ser Ser Gln Pro Trp Glu Pro Leu Gln 130 135 140 Leu His Val Asp Lys Ala Val Ser Gly Leu Arg Ser Leu Thr Thr Leu 145 150 155 160 Leu Arg Ala Leu Gly Ala Gln Lys Glu Ala 165 170 (2) INFORMATION FOR SEQ ID NO:47: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:47: Ser Pro Pro Asp Ala Ala Ser Ala Ala Pro Leu Arg Thr Ile Thr Ala 1 5 10 15 Asp Thr Phe Arg Lys Leu Phe Arg Val Tyr Ser Asn Phe Leu Arg Gly 20 25 30 Lys Leu Lys Leu Tyr Thr Gly Glu Ala Cys Arg Thr Gly Asp Arg Gly 35 40 45 Gly Gly Ser Ala Pro Pro Arg Leu Ile Cys Asp Ser Arg Val Leu Glu 50 55 60 Arg Tyr Leu Leu Glu Ala Lys Glu Ala Glu Asn Ile Thr Thr Gly Cys 65 70 75 80 Ala Glu His Cys Ser Leu Asn Glu Asn Ile Thr Val Pro Asp Thr Lys 85 90 95 Val Asn Phe Tyr Ala Trp Lys Arg Met Glu Val Gly Gln Gln Ala Val 100 105 110 Glu Val Trp Gln Gly Leu Ala Leu Leu Ser Glu Ala Val Leu Arg Gly 115 120 125 Gln Ala Leu Leu Val Asn Ser Ser Gln Pro Trp Glu Pro Leu Gln Leu 130 135 140 His Val Asp Lys Ala Val Ser Gly Leu Arg Ser Leu Thr Thr Leu Leu 145 150 155 160 Arg Ala Leu Gly Ala Gln Lys Glu Ala Ile 165 170 (2) INFORMATION FOR SEQ ID NO:48: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:48: Pro Pro Asp Ala Ala Ser Ala Ala Pro Leu Arg Thr Ile Thr Ala Asp 1 5 10 15 Thr Phe Arg Lys Leu Phe Arg Val Tyr Ser Asn Phe Leu Arg Gly Lys 20 25 30 Leu Lys Leu Tyr Thr Gly Glu Ala Cys Arg Thr Gly Asp Arg Gly Gly 35 40 45 Gly Ser Ala Pro Pro Arg Leu Ile Cys Asp Ser Arg Val Leu Glu Arg 50 55 60 Tyr Leu Leu Glu Ala Lys Glu Ala Glu Asn Ile Thr Thr Gly Cys Ala 65 70 75 80 Glu His Cys Ser Leu Asn Glu Asn Ile Thr Val Pro Asp Thr Lys Val 85 90 95 Asn Phe Tyr Ala Trp Lys Arg Met Glu Val Gly Gln Gln Ala Val Glu 100 105 110 Val Trp Gln Gly Leu Ala Leu Leu Ser Glu Ala Val Leu Arg Gly Gln 115 120 125 Ala Leu Leu Val Asn Ser Ser Gln Pro Trp Glu Pro Leu Gln Leu His 130 135 140 Val Asp Lys Ala Val Ser Gly Leu Arg Ser Leu Thr Thr Leu Leu Arg 145 150 155 160 Ala Lao Gly Ala Gln Lys Glu Ala Ile Ser 165 170 (2) INFORMATION FOR SEQ ID NO:49: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:49: Pro Asp Ala Ala Ser Ala Ala Pro Leu Arg Thr Ile Thr Ala Asp Thr 1 5 10 15 Phe Arg Lys Leu Phe Arg Val Tyr Ser Asn Phe Leu Arg Gly Lys Leu 20 25 30 Lys Leu Tyr Thr Gly Glu Ala Cys Arg Thr Gly Asp Arg Gly Gly Gly 35 40 45 Ser Ala Pro Pro Arg Leu Ile Cys Asp Ser Arg Val Leu Glu Arg Tyr 50 55 60 Leu Leu Glu Ala Lys Glu Ala Glu Asn Ile Thr Thr Gly Cys Ala Glu 65 70 75 80 His Cys Ser Leu Asn Glu Asn Ile Thr Val Pro Asp Thr Lys Val Asn 85 90 95 Phe Tyr Ala Trp Lys Arg Met Glu Val Gly Gln Gln Ala Val Glu Val 100 105 110 Trp Gln Gly Leu Ala Leu Leu Ser Glu Ala Val Leu Arg Gly Gln Ala 115 120 125 Leu Leu Val Asn Ser Ser Gln Pro Trp Glu Pro Leu Gln Leu His Val 130 135 140 Asp Lys Ala Val Ser Gly Leu Arg Ser Leu Thr Thr Leu Leu Arg Ala 145 150 155 160 Leu Gly Ala Gln Lys Glu Ala Ile Ser Pro 165 170 (2) INFORMATION FOR SEQ ID NO:50: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:50: Asp Ala Ala Ser Ala Ala Pro Leu Arg Thr Ile Thr Ala Asp Thr Phe 1 5 10 15 Arg Lys Leu Phe Arg Val Tyr Ser Asn Phe Leu Arg Gly Lys Leu Lys 20 25 30 Leu Tyr Thr Gly Glu Ala Cys Arg Thr Gly Asp Arg Gly Gly Gly Ser 35 40 45 Ala Pro Pro Arg Leu Ile Cys Asp Ser Arg Val Leu Glu Arg Tyr Leu 50 55 60 Leu Glu Ala Lys Glu Ala Glu Asn Ile Thr Thr Gly Cys Ala Glu His 65 70 75 80 Cys Ser Leu Asn Glu Asn Ile Thr Val Pro Asp Thr Lys Val Asn Phe 85 90 95 Tyr Ala Trp Lys Arg Met Glu Val Gly Gln Gln Ala Val Glu Val Trp 100 105 110 Gln Gly Leu Ala Leu Leu Ser Glu Ala Val Leu Arg Gly Gln Ala Leu 115 120 125 Leu Val Asn Ser Ser Gln Pro Trp Glu Pro Leu Gln Leu His Val Asp 130 135 140 Lys Ala Val Ser Gly Leu Arg Ser Leu Thr Thr Leu Leu Arg Ala Leu 145 150 155 160 Gly Ala Gln Lys Glu Ala Ile Ser Pro Pro 165 170 (2) INFORMATION FOR SEQ ID NO:51: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:51: Ala Ala Ser Ala Ala Pro Leu Arg Thr Ile Thr Ala Asp Thr Phe Arg 1 5 10 15 Lys Leu Phe Arg Val Tyr Ser Asn Phe Leu Arg Gly Lys Leu Lys Leu 20 25 30 Tyr Thr Gly Glu Ala Cys Arg Thr Gly Asp Arg Gly Gly Gly Ser Ala 35 40 45 Pro Pro Arg Leu Ile Cys Asp Ser Arg Val Leu Glu Arg Tyr Leu Leu 50 55 60 Glu Ala Lys Glu Ala Glu Asn Ile Thr Thr Gly Cys Ala Glu His Cys 65 70 75 80 Ser Leu Asn Glu Asn Ile Thr Val Pro Asp Thr Lys Val Asn Phe Tyr 85 90 95 Ala Trp Lys Arg Met Glu Val Gly Gln Gln Ala Val Glu Val Trp Gln 100 105 110 Gly Leu Ala Leu Leu Ser Glu Ala Val Leu Arg Gly Gln Ala Leu Leu 115 120 125 Val Asn Ser Ser Gln Pro Trp Glu Pro Leu Gln Leu His Val Asp Lys 130 135 140 Ala Val Ser Gly Leu Arg Ser Leu Thr Thr Leu Leu Arg Ala Leu Gly 145 150 155 160 Ala Gln Lys Glu Ala Ile Ser Pro Pro Asp 165 170 (2) INFORMATION FOR SEQ ID NO:52: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:52: Ala Ser Ala Ala Pro Leu Arg Thr Ile Thr Ala Asp Thr Phe Arg Lys 1 5 10 15 Leu Phe Arg Val Tyr Ser Asn Phe Leu Arg Gly Lys Leu Lys Leu Tyr 20 25 30 Thr Gly Glu Ala Cys Arg Thr Gly Asp Arg Gly Gly Gly Ser Ala Pro 35 40 45 Pro Arg Leu Ile Cys Asp Ser Arg Val Leu Glu Arg Tyr Leu Leu Glu 50 55 60 Ala Lys Glu Ala Glu Asn Ile Thr Thr Gly Cys Ala Glu His Cys Ser 65 70 75 80 Leu Asn Glu Asn Ile Thr Val Pro Asp Thr Lys Val Asn Phe Tyr Ala 85 90 95 Trp Lys Arg Met Glu Val Gly Gln Gln Ala Val Glu Val Trp Gln Gly 100 105 110 Leu Ala Leu Leu Ser Glu Ala Val Leu Arg Gly Gln Ala Leu Leu Val 115 120 125 Asn Ser Ser Gln Pro Trp Glu Pro Leu Gln Leu His Val Asp Lys Ala 130 135 140 Val Ser Gly Leu Arg Ser Leu Thr Thr Leu Leu Arg Ala Leu Gly Ala 145 150 155 160 Gln Lys Glu Ala Ile Ser Pro Pro Asp Ala 165 170 (2) INFORMATION FOR SEQ ID NO:53: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:53: Ser Ala Ala Pro Leu Arg Thr Ile Thr Ala Asp Thr Phe Arg Lys Leu 1 5 10 15 Phe Arg Val Tyr Ser Asn Phe Leu Arg Gly Lys Leu Lys Leu Tyr Thr 20 25 30 Gly Glu Ala Cys Arg Thr Gly Asp Arg Gly Gly Gly Ser Ala Pro Pro 35 40 45 Arg Leu Ile Cys Asp Ser Arg Val Leu Glu Arg Tyr Leu Leu Glu Ala 50 55 60 Lys Glu Ala Glu Asn Ile Thr Thr Gly Cys Ala Glu His Cys Ser Leu 65 70 75 80 Asn Glu Asn Ile Thr Val Pro Asp Thr Lys Val Asn Phe Tyr Ala Trp 85 90 95 Lys Arg Met Glu Val Gly Gln Gln Ala Val Glu Val Trp Gln Gly Leu 100 105 110 Ala Leu Leu Ser Glu Ala Val Leu Arg Gly Gln Ala Leu Leu Val Asn 115 120 125 Ser Ser Gln Pro Trp Glu Pro Leu Gln Leu His Val Asp Lys Ala Val 130 135 140 Ser Gly Leu Arg Ser Leu Thr Thr Leu Leu Arg Ala Leu Gly Ala Gln 145 150 155 160 Lys Glu Ala Ile Ser Pro Pro Asp Ala Ala 165 170 (2) INFORMATION FOR SEQ ID NO:54: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:54: Ala Ala Pro Leu Arg Thr Ile Thr Ala Asp Thr Phe Arg Lys Leu Phe 1 5 10 15 Arg Val Tyr Ser Asn Phe Le Arg Gly Lys Leu Lys Leu Tyr Thr Gly 20 25 30 Glu Ala Cys Arg Thr Gly Asp Arg Gly Gly Gly Ser Ala Pro Pro Arg 35 40 45 Leu Ile Cys Asp Ser Arg Val Leu Glu Arg Tyr Leu Leu Glu Ala Lys 50 55 60 Glu Ala Glu Asn Ile Thr Thr Gly Cys Ala Glu His Cys Ser Leu Asn 65 70 75 80 Glu Asn Ile Thr Val Pro Asp Thr Lys Val Asn Phe Tyr Ala Trp Lys 85 90 95 Arg Met Glu Val Gly Gln Gln Ala Val Glu Val Trp Gln Gly Leu Ala 100 105 110 Leu Leu Ser Glu Ala Val Leu Arg Gly Gln Ala Leu Leu Val Asn Ser 115 120 125 Ser Gln Pro Trp Glu Pro Leu Gln Leu His Val Asp Lys Ala Val Ser 130 135 140 Gly Leu Arg Ser Leu Thr Thr Leu Leu Arg Ala Leu Gly Ala Gln Lys 145 150 155 160 Glu Ala Ile Ser Pro Pro Asp Ala Ala Ser 165 170 (2) INFORMATION FOR SEQ ID NO:55: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:55: Ala Pro Leu Arg Thr Ile Thr Ala Asp Thr Phe Arg Lys Leu Phe Arg 1 5 10 15 Val Tyr Ser Asn Phe Leu Arg Gly Lys Leu Lys Leu Tyr Thr Gly Glu 20 25 30 Ala Cys Arg Thr Gly Asp Arg Gly Gly Gly Ser Ala Pro Pro Arg Leu 35 40 45 Ile Cys Asp Ser Arg Val Leu Glu Arg Tyr Leu Leu Glu Ala Lys Glu 50 55 60 Ala Glu Asn Ile Thr Thr Gly Cys Ala Glu His Cys Ser Leu Asn Glu 65 70 75 80 Asn Ile Thr Val Pro Asp Thr Lys Val Asn Phe Tyr Ala Trp Lys Arg 85 90 95 Met Glu Val Gly Gln Gln Ala Val Glu Val Trp Gln Gly Leu Ala Leu 100 105 110 Leu Ser Glu Ala Val Leu Arg Gly Gln Ala Leu Leu Val Asn Ser Ser 115 120 125 Gln Pro Trp Glu Pro Leu Gln Leu His Val Asp Lys Ala Val Ser Gly 130 135 140 Leu Arg Ser Leu Thr Thr Leu Leu Arg Ala Leu Gly Ala Gln Lys Glu 145 150 155 160 Ala Ile Ser Pro Pro Asp Ala Ala Ser Ala 165 170 (2) INFORMATION FOR SEQ ID NO:56: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:56: Pro Leu Arg Thr Ile Thr Ala Asp Thr Phe Arg Lys Leu Phe Arg Val 1 5 10 15 Tyr Ser Asn Phe Leu Arg Gly Lys Leu Lys Leu Tyr Thr Gly Glu Ala 20 25 30 Cys Arg Thr Gly Asp Arg Gly Gly Gly Ser Ala Pro Pro Arg Leu Ile 35 40 45 Cys Asp Ser Arg Val Leu Glu Arg Tyr Leu Leu Glu Ala Lys Glu Ala 50 55 60 Glu Asn Ile Thr Thr Gly Cys Ala Glu His Cys Ser Leu Asn Glu Asn 65 70 75 80 Ile Thr Val Pro Asp Thr Lys Val Asn Phe Tyr Ala Trp Lys Arg Met 85 90 95 Glu Val Gly Gln Gln Ala Val Glu Val Trp Gln Gly Leu Ala Leu Leu 100 105 110 Ser Glu Ala Val Leu Arg Gly Gln Ala Leu Leu Val Asn Ser Ser Gln 115 120 125 r Pro Trp Glu Pro Leu Gln Leu His Val Asp Lys Ala Val Ser Gly Leu 130 135 140 Arg Ser Leu Thr Thr Leu Leu Arg Ala Leu Gly Ala Gln Lys Glu Ala 145 150 155 160 Ile Ser Pro Pro Asp Ala Ala Ser Ala Ala 165 170 (2) INFORMATION FOR SEQ ID NO:57: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 171 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:57: Leu Arg Thr Ile Thr Ala Asp Thr Phe Arg Lys Leu Phe Arg Val Tyr 1 5 10 15 Ser Asn Phe Leu Arg Gly Lys Leu Lys Leu Tyr Thr Gly Glu Ala Cys 20 25 30 Arg Thr Gly Asp Arg Gly Gly Gly Ser Ala Pro Pro Arg Leu Ile Cys 35 40 45 Asp Ser Arg Val Leu Glu Arg Tyr Leu Leu Glu Ala Lys Glu Ala Glu 50 55 60 Asn Ile Thr Thr Gly Cys Ala Glu His Cys Ser Leu Asn Glu Asn Ile 65 70 75 80 Thr Val Pro Asp Thr Lys Val Asn Phe Tyr Ala Trp Lys Arg Met Glu 85 90 95 Val Gly Gln Gln Ala Val Glu Val Trp Gln Gly Leu Ala Leu Leu Ser 100 105 110 Glu Ala Val Leu Arg Gly Gln Ala Leu Leu Val Asn Ser Ser Gln Pro 115 120 125 Trp Glu Pro Leu Gln Leu His Val Asp Lys Ala Val Ser Gly Leu Arg 130 135 140 Ser Leu Thr Thr Leu Leu Arg Ala Leu Gly Ala Gln Ala Lys Glu Ala 145 150 155 160 Ile Ser Pro Pro Asp Ala Ala Ser Ala Ala Pro 165 170 (2) INFORMATION FOR SEQ ID NO:58: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:58: Arg Thr Ile Thr Ala Asp Thr Phe Arg Lys Leu Phe Arg Val Tyr Ser 1 5 10 15 Asn Phe Leu Arg Gly Lys Leu Lys Leu Tyr Thr Gly Glu Ala Cys Arg 20 25 30 Thr Gly Asp Arg Gly Gly Gly Ser Ala Pro Pro Arg Leu Ile Cys Asp 35 40 45 Ser Arg Val Leu Glu Arg Tyr Leu Leu Glu Ala Lys Glu Ala Glu Asn 50 55 60 Ile Thr Thr Gly Cys Ala Glu His Cys Ser Leu Asn Glu Asn Ile Thr 65 70 75 80 Val Pro Asp Thr Lys Val Asn Phe Tyr Ala Trp Lys Arg Met Glu Val 85 90 95 Gly Gln Gln Ala Val Glu Val Trp Gln Gly Leu Ala Leu Leu Ser Glu 100 105 110 Ala Val Leu Arg Gly Gln Ala Leu Leu Val Asn Ser Ser Gln Pro Trp 115 120 125 Glu Pro Leu Gln Leu His Val Asp Lys Ala Val Ser Gly Leu Arg Ser 130 135 140 Leu Thr Thr Leu Leu Arg Ala Leu Gly Ala Gln Lys Glu Ala Ile Ser 145 150 155 160 Pro Pro Asp Ala Ala Ser Ala Ala Pro Leu 165 170 (2) INFORMATION FOR SEQ ID NO:59: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:59: Thr Ile Thr Ala Asp Thr Phe Arg Lys Leu Phe Arg Val Tyr Ser Asn 1 5 10 15 Phe Leu Arg Gly Lys Leu Lys Leu Tyr Thr Gly Glu Ala Cys Arg Thr 20 25 30 Gly Asp Arg Gly Gly Gly Ser Ala Pro Pro Arg Leu Ile Cys Asp Ser 35 40 45 Arg Val Leu Glu Arg Tyr Leu Leu Glu Ala Lys Glu Ala Glu Asn Ile 50 55 60 Thr Thr Gly Cys Ala Glu His Cys Ser Leu Asn Glu Asn Ile Thr Val 65 70 75 80 Pro Asp Thr Lys Val Asn Phe Tyr Ala Trp Lys Arg Met Glu Val Gly 85 90 95 Gln Gln Ala Val Glu Val Trp Gln Gly Leu Ala Leu Leu Ser Glu Ala 100 105 110 Val Leu Arg Gly Gln Ala Leu Leu Val Asn Ser Ser Gln Pro Trp Glu 115 120 125 Pro Leu Gln Leu His Val Asp Lys Ala Val Ser Gly Leu Arg Ser Leu 130 135 140 Thr Thr Leu Leu Arg Ala Leu Gly Ala Gln Lys Glu Ala Ile Ser Pro 145 150 155 160 Pro Asp Ala Ala Ser Ala Ala Pro Leu Arg 165 170 (2) INFORMATION FOR SEQ ID NO:60: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 512 base pairs (B) TYPE: nucleic acid (Cj STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:60: AATATCACGA CGGGCTGTGC TGAACACTGC AGCTTGAATG AGAATATCAC TGTCCCAGAC 60 ACCAAAGTTA ATTTCTATGC CTGGAAGAGG ATGGAGGTCG GGCAGCAGGC CGTAGAAGTC 120 TGGCAGGGCC TGGCCCTGCT GTCGGAAGCT GTCCTGCGGG GCCAGGCCCT GTTGGTCAAC 180 TCTTCCCAGC CGTGGGAGCC CCTGCAGCTG CATGTGGATA AAGCCGTCAG TGGCCTTCGC 240 AGCCTCACCA CTCTGCTTCG GGCTCTGGGA GCCCAGAAGG AAGCCATCTC CCCTCCAGAT 300 GCGGCCTCAG CTGCTCCACT CCGAACAATC ACTGCTGACA CTTTCCGCAA ACTCTTCCGA 360 GTCTACTCCA ATTTCCTCCG GGGAAAGCTG AAGCTGTACA CAGGGGAGGC CTGCAGGACA 420 GGGGACAGAT GAGGCGGCGG CTCCCCCCAC CACGCCTCAT CTGTGACAGC CGAGTCCTGG 480 AGAGGTACCT CTTGGAGGCC AAGGAGGCCG AG 512 (2) INFORMATION FOR SEQ ID NO:61: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 512 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:61: ATCACGACGG GCTGTGCTGA ACACTGCAGC TTGAATGAGA ATATCACTGT CCCAGACACC 60 AAAGTTAATT TCTATGCCTG GAAGAGGATG GAGGTCGGGC AGCAGGCCGT AGAAGTCTGG 120 CAGGGCCTGG CCCTGCTGTC GGAAGCTGTC CTGCGGGGCC AGGCCCTGTT GGTCAACTCT 180 TCCCAGCCGT GGGAGCCCCT GCAGCTGCAT GTGGATAAAG CCGTCAGTGG CCTTCGCAGC 240 CTCACCACTC TGCTTCGGGC TCTGGGAGCC CAGAAGGAAG CCATCTCCCC TCCAGATGCG 300 GCCTCAGCTG CTCCACTCCG AACAATCACT GCTGACACTT TCCGCAAACT CTTCCGAGTC 360 TACTCCAATT TCCTCCGGGG AAAGCTGAAG CTGTACACAG GGGAGGCCTG CAGGACAGGG 420 GACAGATGAG GCGGCGGCTC CCCCCACCAC GCCTCATCTG TGACAGCCGA GTCCTGGAGA 480 GGTACCTCTT GGAGGCCAAG GAGGCCGAGA AT 512 (2) INFORMATION FOR SEQ ID NO:62: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 512 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:62: ACGACGGGCT GTGCTGAACA CTGCAGCTTG AATGAGAATA TCACTGTCCC AGACACCAAA 60 GTTAATTTCT ATGCCTGGAA GAGGATGGAG GTCGGGCAGC AGGCCGTAGA AGTCTGGCAG 120 GGCCTGGCCC TGCTGTCGGA AGCTGTCCTG CGGGGCCAGG CCCTGTTGGT CAACTCTTCC 180 CAGCCGTGGG AGCCCCTGCA GCTGCATGTG GATAAAGCCG TCAGTGGCCT TCGCAGCCTC 240 ACCACTCTGC TTCGGGCTCT GGGAGCCCAG AAGGAAGCCA TCTCCCCTCC AGATGCGGCC 300 TCAGCTGCTC CACTCCGAAC AATCACTGCT GACACTTTCC GCAAACTCTT CCGAGTCTAC 360 TCCAATTTCC TCCGGGGAAA GCTGAAGCTG TACACAGGGG AGGCCTGCAG GACAGGGGAC 420 AGATGAGGCG GCGGCTCCCC CCACCACGCC TCATCTGTGA CAGCCGAGTC CTGGAGAGGT 480 ACCTCTTGGA GGCCAAGGAG GCCGAGAATA TC 512 (2) INFORMATION FOR SEQ ID NO:63: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 512 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:63: ACGGGCTGTG CTGAACACTG CAGCTTGAAT GAGAATATCA CTGTCCCAGA CACCAAAGTT 60 AATTTCTATG CCTGGAAGAG GATGGAGGTC GGGCAGCAGG CCGTAGAAGT CTGGCAGGGC 120 CTGGCCCTGC TGTCGGAAGC TGTCCTGCGG GGCCAGGCCC TGTTGGTCAA CTCTTCCCAG 180 CCGTGGGAGC CCCTGCAGCT GCATGTGGAT AAAGCCGTCA GTGGCCTTCG CAGCCTCACC 240 ACTCTGCTTC GGGCTCTGGG AGCCCAGAAG GAAGCCATCT CCCCTCCAGA TGCGGCCTCA 300 GCTGCTCCAC TCCGAACAAT CACTGCTGAC ACTTTCCGCA AACTCTTCCG AGTCTACTCC 360 AATTTCCTCC GGGGAAAGCT GAAGCTGTAC ACAGGGGAGG CCTGCAGGAC AGGGGACAGA 420 TGAGGCGGCG GCTCCCCCCA CCACGCCTCA TCTGTGACAG CCGAGTCCTG GAGAGGTACC 480 TCTTGGAGGC CAAGGAGGCC GAGAATATCA CG 512 (2) INFORMATION FOR SEQ ID NO:64: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 512 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:64: GGCTGTGCTG AACACTGCAG CTTGAATGAG AATATCACTG TCCCAGACAC CAAAGTTAAT 60 TTCTATGCCT GGAAGAGGAT GGAGGTCGGG CAGCAGGCCG TAGAAGTCTG GCAGGGCCTG 120 GCCCTGCTGT CGGAAGCTGT CCTGCGGGGC CAGGCCCTGT TGGTCAACTC TTCCCAGCCG 180 TGGGAGCCCC TGCAGCTGCA TGTGGATAAA GCCGTCAGTG GCCTTCGCAG CCTCACCACT 240 CTGCTTCGGG CTCTGGGAGC CCAGAAGGAA GCCATCTCCC CTCCAGATGC GGCCTCAGCT 300 GCTCCACTCC GAACAATCAC TGCTGACACT TTCCGCAAAC TCTTCCGAGT CTACTCCAAT 360 TTCCTCCGGG GAAAGCTGAA GCTGTACACA GGGGAGGCCT GCAGGACAGG GGACAGATGA 420 GGCGGCGGCT CCCCCCACCA CGCCTCATCT GTGACAGCCG AGTCCTGGAG AGGTACCTCT 480 TGGAGGCCAA GGAGGCCGAG AATATCACGA CG 512 (2) INFORMATION FOR SEQ ID NO:65: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 512 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:65: TGTGCTGAAC ACTGCAGCTT GAATGAGAAT ATCACTGTCC CAGACACCAA AGTTAATTTC 60 TATGCCTGGA AGAGGATGGA GGTCGGGCAG CAGGCCGTAG AAGTCTGGCA GGGCCTGGCC 120 CTGCTGTCGG AAGCTGTCCT GCGGGGCCAG GCCCTGTTGG TCAACTCTTC CCAGCCGTGG 180 GAGCCCCTGC AGCTGCATGT GGATAAAGCC GTCAGTGGCC TTCGCAGCCT CACCACTCTG 240 CTTCGGGCTC TGGGAGCCCA GAAGGAAGCC ATCTCCCCTC CAGATGCGGC CTCAGCTGCT 300 CCACTCCGAA CAATCACTGC TGACACTTTC CGCAAACTCT TCCGAGTCTA CTCCAATTTC 360 CTCCGGGGAA AGCTGAAGCT GTACACAGGG GAGGCCTGCA GGACAGGGGA CAGATGAGGC 420 GGCGGCTCCC CCCACCACGC CTCATCTGTG ACAGCCGAGT CCTGGAGAGG TACCTCTTGG 480 AGGCCAAGGA GGCCGAGAAT ATCACGACGG GC 512 (2) INFORMATION FOR SEQ ID NO:66: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 512 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:66: GCTGAACACT GCAGCTTGAA TGAGAATATC ACTGTCCCAG ACACCAAAGT TAATTTCTAT 60 GCCTGGAAGA GGATGGAGGT CGGGCAGCAG GCCGTAGAAG TCTGGCAGGG CCTGGCCCTG 120 CTGTCGGAAG CTGTCCTGCG GGGCCAGGCC CTGTTGGTCA ACTCTTCCCA GCCGTGGGAG 180 CCCCTGCAGC TGCATGTGGA TAAAGCCGTC AGTGGCCTTC GCAGCCTCAC CACTCTGCTT 240 CGGGCTCTGG GAGCCCAGAA GGAAGCCATC TCCCCTCCAG ATGCGGCCTC AGCTGCTCCA 300 CTCCGAACAA TCACTGCTGA CACTTTCCGC AAACTCTTCC GAGTCTACTC CAATTTCCTC 360 CGGGGAAAGC TGAAGCTGTA CACAGGGGAG GCCTGCAGGA CAGGGGACAG ATGAGGCGGC 420 GGCTCCCCCC ACCACGCCTC ATCTGTGACA GCCGAGTCCT GGAGAGGTAC CTCTTGGAGG 480 CCAAGGAGGC CGAGAATATC ACGACGGGCT GT 512 (2) INFORMATION FOR SEQ ID NO:67: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 512 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:67: GAACACTGCA GCTTGAATGA GAATATCACT GTCCCAGACA CCAAAGTTAA TTTCTATGCC 60 TGGAAGAGGA TGGAGGTCGG GCAGCAGGCC GTAGAAGTCT GGCAGGGCCT GGCCCTGCTG 120 TCGGAAGCTG TCCTGCGGGG CCAGGCCCTG TTGGTCAACT CTTCCCAGCC GTGGGAGCCC 180 CTGCAGCTGC ATGTGGATAA AGCCGTCAGT GGCCTTCGCA GCCTCACCAC TCTGCTTCGG 240 GCTCTGGGAG CCCAGAAGGA AGCCATCTCC CCTCCAGATG CGGCCTCAGC TGCTCCACTC 300 CGAACAATCA CTGCTGACAC TTTCCGCAAA CTCTTCCGAG TCTACTCCAA TTTCCTCCGG 360 GGAAAGCTGA AGCTGTACAC AGGGGAGGCC TGCAGGACAG GGGACAGATG AGGCGGCGGC 420 TCCCCCCACC ACGCCTCATC TGTGACAGCC GAGTCCTGGA GAGGTACCTC TTGGAGGCCA 480 AGGAGGCCGA GAATATCACG ACGGGCTGTG CT 512 (2) INFORMATION FOR SEQ ID NO:68: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 512 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:68: CACTGCAGCT TGAATGAGAA TATCACTGTC CCAGACACCA AAGTTAATTT CTATGCCTGG 60 AAGAGGATGG AGGTCGGGCA GCAGGCCGTA GAAGTCTGGC AGGGCCTGGC CCTGCTGTCG 120 GAAGCTGTCC TGCGGGGCCA GGCCCTGTTG GTCAACTCTT CCCAGCCGTG GGAGCCCCTG 180 CAGCTGCATG TGGATAAAGC CGTCAGTGGC CTTCGCAGCC TCACCACTCT GCTTCGGGCT 240 CTGGGAGCCC AGAAGGAAGC CATCTCCCCT CCAGATGCGG CCTCAGCTGC TCCACTCCGA 300 ACAATCACTG CTGACACTTT CCGCAAACTC TTCCGAGTCT ACTCCAATTT CCTCCGGGGA 360 AAGCTGAAGC TGTACACAGG GGAGGCCTGC AGGACAGGGG ACAGATGAGG CGGCGGCTCC 420 CCCCACCACG CCTCATCTGT GACAGCCGAG TCCTGGAGAG GTACCTCTTG GAGGCCAAGG 480 AGGCCGAGAA TATCACGACG GGCTGTGCTG AA 512 (2) INFORMATION FOR SEQ ID NO:69: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 512 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:69: TGCAGCTTGA ATGAGAATAT CACTGTCCCA GACACCAAAG TTAATTTCTA TGCCTGGAAG 60 AGGATGGAGG TCGGGCAGCA GGCCGTAGAA GTCTGGCAGG GCCTGGCCCT GCTGTCGGAA 120 GCTGTCCTGC GGGGCCAGGC CCTGTTGGTC AACTCTTCCC AGCCGTGGGA GCCCCTGCAG 180 CTGCATGTGG ATAAAGCCGT CAGTGGCCTT CGCAGCCTCA CCACTCTGCT TCGGGCTCTG 240 GGAGCCCAGA AGGAAGCCAT CTCCCCTCCA GATGCGGCCT CAGCTGCTCC ACTCCGAACA 300 ATCACTGCTG ACACTTTCCG CAAACTCTTC CGAGTCTACT CCAATTTCCT CCGGGGAAAG 360 CTGAAGCTGT ACACAGGGGA GGCCTGCAGG ACAGGGGACA GATGAGGCGG CGGCTCCCCC 420 CACCACGCCT CATCTGTGAC AGCCGAGTCC TGGAGAGGTA CCTCTTGGAG GCCAAGGAGG 480 CCGAGAATAT CACGACGGGC TGTGCTGAAC AC 512 (2) INFORMATION FOR SEQ ID NO:70: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 512 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:70: AGCTTGAATG AGAATATCAC TGTCCCAGAC ACCAAAGTTA ATTTCTATGC CTGGAAGAGG 60 ATGGAGGTCG GGCAGCAGGC CGTAGAAGTC TGGCAGGGCC TGGCCCTGCT GTCGGAAGCT 120 GTCCTGCGGG GCCAGGCCCT GTTGGTCAAC TCTTCCCAGC CGTGGGAGCC CCTGCAGCTG 180 CATGTGGATA AAGCCGTCAG TGGCCTTCGC AGCCTCACCA CTCTGCTTCG GGCTCTGGGA 240 GCCCAGAAGG AAGCCATCTC CCCTCCAGAT GCGGCCTCAG CTGCTCCACT CCGAACAATC 300 ACTGCTGACA CTTTCCGCAA ACTCTTCCGA GTCTACTCCA ATTTCCTCCG GGGAAAGCTG 360 AAGCTGTACA CAGGGGAGGC CTGCAGGACA GGGGACAGAT GAGGCGGCGG CTCCCCCCAC 420 CACGCCTCAT CTGTGACAGC CGAGTCCTGG AGAGGTACCT CTTGGAGGCC AAGGAGGCCG 480 AGAATATCAC GACGGGCTGT GCTGAACACT GC 512 (2) INFORMATION FOR SEQ ID NO:71: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 512 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:71: TTGAATGAGA ATATCACTGT CCCAGACACC AAAGTTAATT TCTATGCCTG GAAGAGGATG 60 GAGGTCGGGC AGCAGGCCGT AGAAGTCTGG CAGGGCCTGG CCCTGCTGTC GGAAGCTGTC 120 CTGCGGGGCC AGGCCCTGTT GGTCAACTCT TCCCAGCCGT GGGAGCCCCT GCAGCTGCAT 180 GTGGATAAAG CCGTCAGTGG CCTTCGCAGC CTCACCACTC TGCTTCGGGC TCTGGGAGCC 240 CAGAAGGAAG CCATCTCCCC TCCAGATGCG GCCTCAGCTG CTCCACTCCG AACAATCACT 300 GCTGACACTT TCCGCAAACT CTTCCGAGTC TACTCCAATT TCCTCCGGGG AAAGCTGAAG 360 CTGTACACAG GGGAGGCCTG CAGGACAGGG GACAGATGAG GCGGCGGCTC CCCCCACCAC 420 GCCTCATCTG TGACAGCCGA GTCCTGGAGA GGTACCTCTT GGAGGCCAAG GAGGCCGAGA 480 ATATCACGAC GGGCTGTGCT GAACACTGCA GC 512 (2) INFORMATION FOR SEQ ID NO:72: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 512 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:72: AATGAGAATA TCACTGTCCC AGACACCAAA GTTAATTTCT ATGCCTGGAA GAGGATGGAG 60 GTCGGGCAGC AGGCCGTAGA AGTCTGGCAG GGCCTGGCCC TGCTGTCGGA AGCTGTCCTG 120 CGGGGCCAGG CCCTGTTGGT CAACTCTTCC CAGCCGTGGG AGCCCCTGCA GCTGCATGTG 180 GATAAAGCCG TCAGTGGCCT TCGCAGCCTC ACCACTCTGC TTCGGGCTCT GGGAGCCCAG 240 AAGGAAGCCA TCTCCCCTCC AGATGCGGCC TCAGCTGCTC CACTCCGAAC AATCACTGCT 300 GACACTTTCC GCAAACTCTT CCGAGTCTAC TCCAATTTCC TCCGGGGAAA GCTGAAGCTG 360 TACACAGGGG AGGCCTGCAG GACAGGGGAC AGATGAGGCG GCGGCTCCCC CCACCACGCC 420 TCATCTGTGA CAGCCGAGTC CTGGAGAGGT ACCTCTTGGA GGCCAAGGAG GCCGAGAATA 480 TCACGACGGG CTGTGCTGAA CACTGCAGCT TG 512 (2) INFORMATION FOR SEQ ID NO:73.

(i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 512 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:73: GAGAATATCA CTGTCCCAGA CACCAAAGTT AATTTCTATG CCTGGAAGAG GATGGAGGTC 60 GGGCAGCAGG CCGTAGAAGT CTGGCAGGGC CTGGCCCTGC TGTCGGAAGC TGTCCTGCGG 120 GGCCAGGCCC TGTTGGTCAA CTCTTCCCAG CCGTGGGAGC CCCTGCAGCT GCATGTGGAT 180 AAAGCCGTCA GTGGCCTTCG CAGCCTCACC ACTCTGCTTC GGGCTCTGGG AGCCCAGAAG 240 GAAGCCATCT CCCCTCCAGA TGCGGCCTCA GCTGCTCCAC TCCGAACAAT CACTGCTGAC 300 ACTTTCCGCA AACTCTTCCG AGTCTACTCC AATTTCCTCC GGGGAAAGCT GAAGCTGTAC 360 ACAGGGGAGG CCTGCAGGAC AGGGGACAGA TGAGGCGGCG GCTCCCCCCA CCACGCCTCA 420 TCTGTGACAG CCGAGTCCTG GAGAGGTACC TCTTGGAGGC CAAGGAGGCC GAGAATATCA 480 CGACGGGCTG TGCTGAACAC TGCAGCTTGA AT 512 (2) INFORMATION FOR SEQ ID NO:74: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 512 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:74: AATATCACTG TCCCAGACAC CAAAGTTAAT TTCTATGCCT GGAAGAGGAT GGAGGTCGGG 60 CAGCAGGCCG TAGAAGTCTG GCAGGGCCTG GCCCTGCTGT CGGAAGCTGT CCTGCGGGGC 120 CAGGCCCTGT TGGTCAACTC TTCCCAGCCG TGGGAGCCCC TGCAGCTGCA TGTGGATAAA 180 GCCGTCAGTG GCCTTCGCAG CCTCACCACT CTGCTTCGGG CTCTGGGAGC CCAGAAGGAA 240 GCCATCTCCC CTCCAGATGC GGCCTCAGCT GCTCCACTCC GAACAATCAC TGCTGACACT 300 TTCCGCAAAC TCTTCCGAGT CTACTCCAAT TTCCTCCGGG GAAAGCTGAA GCTGTACACA 360 GGGGAGGCCT GCAGGACAGG GGACAGATGA GGCGGCGGCT CCCCCCACCA CGCCTCATCT 420 GTGACAGCCG AGTCCTGGAG AGGTACCTCT TGGAGGCCAA GGAGGCCGAG AATATCACGA 480 CGGGCTGTGC TGAACACTGC AGCTTGAATG AG 512 (2) INFORMATION FOR SEQ ID NO:75: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 512 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:75: ATCACTGTCC CAGACACCAA AGTTAATTTC TATGCCTGGA AGAGGATGGA GGTCGGGCAG 60 CAGGCCGTAG AAGTCTGGCA GGGCCTGGCC CTGCTGTCGG AAGCTGTCCT GCGGGGCCAG 120 GCCCTGTTGG TCAACTCTTC CCAGCCGTGG GAGCCCCTGC AGCTGCATGT GGATAAAGCC 180 GTCAGTGGCC TTCGCAGCCT CACCACTCTG CTTCGGGCTC TGGGAGCCCA GAAGGAAGCC 240 ATCTCCCCTC CAGATGCGGC CTCAGCTGCT CCACTCCGAA CAATCACTGC TGACACTTTC 300 CGCAAACTCT TCCGAGTCTA CTCCAATTTC CTCCGGGGAA AGCTGAAGCT GTACACAGGG 360 GAGGCCTGCA GGACAGGGGA CAGATGAGGC GGCGGCTCCC CCCACCACGC CTCATCTGTG 420 ACAGCCGAGT CCTGGAGAGG TACCTCTTGG AGGCCAAGGA GGCCGAGAAT ATCACGACGG 480 GCTGTGCTGA ACACTGCAGC TTGAATGAGA AT 512 (2) INFORMATION FOR SEQ ID NO:76: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:76: ACTGTCCCAG ACACCAAAGT TAATTTCTAT GCCTGGAAGA GGATGGAGGT CGGGCAGCAG 60 GCCGTAGAAG TCTGGCAGGG CCTGGCCCTG CTGTCGGAAG CTGTCCTGCG GGGCCAGGCC 120 CTGTTGGTCA ACTCTTCCCA GCCGTGGGAG CCCCTGCAGC TGCATGTGGA TAAAGCCGTC 180 AGTGGCCTTC GCAGCCTCAC CACTCTGCTT CGGGCTCTGG GAGCCCAGAA GGAAGCCATC 240 TCCCCTCCAG ATGCGGCCTC AGCTGCTCCA CTCCGAACAA TCACTGCTGA CACTTTCCGC 300 AAACTCTTCC GAGTCTACTC CAATTTCCTC CGGGGAAAGC TGAAGCTGTA CACAGGGGAG 360 GCCTGCAGGA CAGGGGACAG ATGAGGCGGC GGCTCCCCCC ACCACGCCTC ATCTGTGACA 420 GCCGAGTCCT GGAGAGGTAC CTCTTGGAGG CCAAGGAGGC CGAGAATATC ACGACGGGCT 480 GTGCTGAACA CTGCAGCTTG AATGAGAATA ATC 513 (2) INFORMATION FOR SEQ ID NO:77: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:77: GTCCCAGACA CCAAAGTTAA TTTCTATGCC TGGAAGAGGA TGGAGGTCGG GCAGCAGGCC 60 GTAGAAGTCT GGCAGGGCCT GGCCCTGCTG TCGGAAGCTG TCCTGCGGGG CCAGGCCCTG 120 TTGGTCAACT CTTCCCAGCC GTGGGAGCCC CTGCAGCTGC ATGTGGATAA AGCCGTCAGT 180 GGCCTTCGCA GCCTCACCAC TCTGCTTCGG GCTCTGGGAG CCCAGAAGGA AGCCATCTCC 240 CCTCCAGATG CGGCCTCAGC TGCTCCACTC CGAACAATCA CTGCTGACAC TTTCCGCAAA 300 CTCTTCCGAG TCTACTCCAA TTTCCTCCGG GGAAAGCTGA AGCTGTACAC AGGGGAGGCC 360 TGCAGGACAG GGGACAGATG AGGCGGCGGC TCCCCCCACC ACGCCTCATC TGTGACAGCC 420 GAGTCCTGGA GAGGTACCTC TTGGAGGCCA AGGAGGCCGA GAATATCACG ACGGGCTGTG 480 CTGAACACTG CAGCTGAAT GAGAATAATC ACT 513 (2) INFORMATION FOR SEQ ID NO:78: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:78: CCAGACACCA AAGTTAATTT CTATGCCTGG AAGAGGATGG AGGTCGGGCA GCAGGCCGTA 60 GAAGTCTGGC AGGGCCTGGC CCTGCTGTCG GAAGCTGTCC TGCGGGGCCA GGCCCTGTTG 120 GTCAACTCTT CCCAGCCGTG GGAGCCCCTG CAGCTGCATG TGGATAAAGC CGTCAGTGGC 180 CTTCGCAGCC TCACCACTCT GCTTCGGGCT CTGGGAGCCC AGAAGGAAGC CATCTCCCCT 240 CCAGATGCGG CCTCAGCTGC TCCACTCCGA ACAATCACTG CTGACACTTT CCGCAAACTC 300 TTCCGAGTCT ACTCCAATTT CCTCCGGGGA AAGCTGAAGC TGTACACAGG GGAGGCCTGC 360 AGGACAGGGG ACAGATGAGG CGGCGGCTCC CCCCACCACG CCTCATCTGT GACAGCCGAG 420 TCCTGGAGAG GTACCTCTTG GAGGCCAAGG AGGCCGAGAA TATCACGACG GGCTGTGCTG 480 AACACTGCAG CTTGAATGAG AATAATCACT GTC 513 (2) INFORMATION FOR SEQ ID NO:79: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:79: GACACCAAAG TTAATTTCTA TGCCTGGAAG AGGATGGAGG TCGGGCAGCA GGCCGTAGAA 60 GTCTGGCAGG GCCTGGCCCT GCTGTCGGAA GCTGTCCTGC GGGGCCAGGC CCTGTTGGTC 120 AACTCTTCCC AGCCGTGGGA GCCCCTGCAG CTGCATGTGG ATAAAGCCGT CAGTGGCCTT 180 CGCAGCCTCA CCACTCTGCT TCGGGCTCTG GGAGCCCAGA AGGAAGCCAT CTCCCCTCCA 240 GATGCGGCCT CAGCTGCTCC ACTCCGAACA ATCACTGCTG ACACTTTCCG CAAACTCTTC 300 CGAGTCTACT CCAATTTCCT CCGGGGAAAG CTGAAGCTGT ACACAGGGGA GGCCTGCAGG 360 ACAGGGGACA GATGAGGCGG CGGCTCCCCC CACCACGCCT CATCTGTGAC AGCCGAGTCC 420 TGGAGAGGTA CCTCTTGGAG GCCAAGGAGG CCGAGAATAT CACGACGGGC TGTGCTGAAC 480 ACTGCAGCTT GAATGAGAAT AATCACTGTC CCA 513 (2) INFORMATION FOR SEQ ID NO:80: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:80: AGGATGGAGG TCGGGCAGCA GGCCGTAGAA GTCTGGCAGG GCCTGGCCCT GCTGTCGGAA 60 GCTGTCCTGC GGGGCCAGGC CCTGTTGGTC AACTCTTCCC AGCCGTGGGA GCCCCTGCAG 120 CTGCATGTGG ATAAAGCCGT CAGTGGCCTT CGCAGCCTCA CCACTCTGCT TCGGGCTCTG 180 GGAGCCCAGA AGGAAGCCAT CTCCCCTCCA GATGCGGCCT CAGCTGCTCC ACTCCGAACA 240 ATCACTGCTG ACACTTTCCG CAAACTCTTC CGAGTCTACT CCAATTTCCT CCGGGGAAAG 300 CTGAAGCTGT ACACAGGGGA GGCCTGCAGG ACAGGGGACA GATGAGGCGG CGGCTCCCCC 360 CACCACGCCT CATCTGTGAC AGCCGAGTCC TGGAGAGGTA CCTCTTGGAG GCCAAGGAGG 420 CCGAGAATAT CACGACGGGC TGTGCTGAAC ACTGCAGCTT GAATGAGAAT AATCACTGTC 480 CCAGACACCA AAGTTAATTT CTATGCCTGG AAG 513 (2) INFORMATION FOR SEQ ID NO:81: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:81: ATGGAGGTCG GGCAGCAGGC CGTAGAAGTC TGGCAGGGCC TGGCCCTGCT GTCGGAAGCT 60 GTCCTGCGGG GCCAGGCCCT GTTGGTCAAC TCTTCCCAGC CGTGGGAGCC CCTGCAGCTG 120 CATGTGGATA AAGCCGTCAG TGGCCTTCGC AGCCTCACCA CTCTGCTTCG GGCTCTGGGA 180 GCCCAGAAGG AAGCCATCTC CCCTCCAGAT GCGGCCTCAG CTGCTCCACT CCGAACAATC 240 ACTGCTGACA CTTTCCGCAA ACTCTTCCGA GTCTACTCCA ATTTCCTCCG GGGAAAGCTG 300 AAGCTGTACA CAGGGGAGGC CTGCAGGACA GGGGACAGAT GAGGCGGCGG CTCCCCCCAC 360 CACGCCTCAT CTGTGACAGC CGAGTCCTGG AGAGGTACCT CTTGGAGGCC AAGGAGGCCG 420 AGAATATCAC GACGGGCTGT GCTGAACACT GCAGCTTGAA TGAGAATAAT CACTGTCCCA 480 GACACCAAAG TTAATTTCTA TGCCTGGAAG AGG 513 (2) INFORMATION FOR SEQ ID NO:82: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:82: GAGGTCGGGC AGCAGGCCGT AGAAGTCTGG CAGGGCCTGG CCCTGCTGTC GGAAGCTGTC 60 CTGCGGGGCC AGGCCCTGTT GGTCAACTCT TCCCAGCCGT GGGAGCCCCT GCAGCTGCAT 120 GTGGATAAAG CCGTCAGTGG CCTTCGCAGC CTCACCACTC TGCTTCGGGC TCTGGGAGCC 180 CAGAAGGAAG CCATCTCCCC TCCAGATGCG GCCTCAGCTG CTCCACTCCG AACAATCACT 240 GCTGACACTT TCCGCAAACT CTTCCGAGTC TACTCCAATT TCCTCCGGGG AAAGCTGAAG 300 CTGTACACAG GGGAGGCCTG CAGGACAGGG GACAGATGAG GCGGCGGCTC CCCCCACCAC 360 GCCTCATCTG TGACAGCCGA GTCCTGGAGA GGTACCTCTT GGAGGCCAAG GAGGCCGAGA 420 ATATCACGAC GGGCTGTGCT GAACACTGCA GCTTGAATGA GAATAATCAC TGTCCCAGAC 480 ACCAAAGTTA ATTTCTATGC CTGGAAGAGG ATG 513 (2) INFORMATION FOR SEQ ID NO:83: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:83: GTCGGGCAGC AGGCCGTAGA AGTCTGGCAG GGCCTGGCCC TGCTGTCGGA AGCTGTCCTG 60 CGGGGCCAGG CCCTGTTGGT CAACTCTTCC CAGCCGTGGG AGCCCCTGCA GCTGCATGTG 120 GATAAAGCCG TCAGTGGCCT TCGCAGCCTC ACCACTCTGC TTCGGGCTCT GGGAGCCCAG 180 AAGGAAGCCA TCTCCCCTCC AGATGCGGCC TCAGCTGCTC CACTCCGAAC AATCACTGCT 240 GACACTTTCC GCAAACTCTT CCGAGTCTAC TCCAATTTCC TCCGGGGAAA GCTGAAGCTG 300 TACACAGGGG AGGCCTGCAG GACAGGGGAC AGATGAGGCG GCGGCTCCCC CCACCACGCC 360 TCATCTGTGA CAGCCGAGTC CTGGAGAGGT ACCTCTTGGA GGCCAAGGAG GCCGAGAATA 420 TCACGACGGG CTGTGCTGAA CACTGCAGCT TGAATGAGAA TAATCACTGT CCCAGACACC 480 AAAGTTAATT TCTATGCCTG GAAGAGGATG GAG 513 (2) INFORMATION FOR SEQ ID NO:84: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:84: CAGGCCCTGT TGGTCAACTC TTCCCAGCCG TGGGAGCCCC TGCAGCTGCA TGTGGATAAA 60 GCCGTCAGTG GCCTTCGCAG CCTCACCACT CTGCTTCGGG CTCTGGGAGC CCAGAAGGAA 120 GCCATCTCCC CTCCAGATGC GGCCTCAGCT GCTCCACTCC GAACAATCAC TGCTGACACT 180 TTCCGCAAAC TCTTCCGAGT CTACTCCAAT TTCCTCCGGG GAAAGCTGAA GCTGTACACA 240 GGGGAGGCCT GCAGGACAGG GGACAGATGA GGCGGCGGCT CCCCCCACCA CGCCTCATCT 300 GTGACAGCCG AGTCCTGGAG AGGTACCTCT TGGAGGCCAA GGAGGCCGAG AATATCACGA 360 CGGGCTGTGC TGAACACTGC AGCTTGAATG AGAATAATCA CTGTCCCAGA CACCAAAGTT 420 AATTTCTATG CCTGGAAGAG GATGGAGGTC GGGCAGCAGG CCGTAGAAGT CTGGCAGGGC 480 CTGGCCCTGC TGTCGGAAGC TGTCCTGCGG GGC 513 (2) INFORMATION FOR SEQ ID NO:85: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:85: GCCCTGTTGG TCAACTCTTC CCAGCCGTGG GAGCCCCTGC AGCTGCATGT GGATAAAGCC 60 GTCAGTGGCC TTCGCAGCCT CACCACTCTG CTTCGGGCTC TGGGAGCCCA GAAGGAAGCC 120 ATCTCCCCTC CAGATGCGGC CTCAGCTGCT CCACTCCGAA CAATCACTGC TGACACTTTC 180 CGCAAACTCT TCCGAGTCTA CTCCAATTTC CTCCGGGGAA AGCTGAAGCT GTACACAGGG 240 GAGGCCTGCA GGACAGGGGA CAGATGAGGC GGCGGCTCCC CCCACCACGC CTCATCTGTG 300 ACAGCCGAGT CCTGGAGAGG TACCTCTTGG AGGCCAAGGA GGCCGAGAAT ATCACGACGG 360 GCTGTGCTGA ACACTGCAGC TTGAATGAGA ATAATCACTG TCCCAGACAC CAAAGTTAAT 420 TTCTATGCCT GGAAGAGGAT GGAGGTCGGG CAGCAGGCCG TAGAAGTCTG GCAGGGCCTG 480 GCCCTGCTGT CGGAAGCTGT CCTGCGGGGC CAG 513 (2) INFORMATION FOR SEQ ID NO:86: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:86: CTGTTGGTCA ACTCTTCCCA GCCGTGGGAG CCCCTGCAGC TGCATGTGGA TAAAGCCGTC 60 AGTGGCCTTC GCAGCCTCAC CACTCTGCTT CGGGCTCTGG GAGCCCAGAA GGAAGCCATC 120 TCCCCTCCAG ATGCGGCCTC AGCTGCTCCA CTCCGAACAA TCACTGCTGA CACTTTCCGC 180 AAACTCTTCC GAGTCTACTC CAATTTCCTC CGGGGAAAGC TGAAGCTGTA CACAGGGGAG 240 GCCTGCAGGA CAGGGGACAG ATGAGGCGGC GGCTCCCCCC ACCACGCCTC ATCTGTGACA 300 GCCGAGTCCT GGAGAGGTAC CTCTTGGAGG CCAAGGAGGC CGAGAATATC ACGACGGGCT 360 GTGCTGAACA CTGCAGCTTG AATGAGAATA ATCACTGTCC CAGACACCAA AGTTAATTTC 420 TATGCCTGGA AGAGGATGGA GGTCGGGCAG CAGGCCGTAG AAGTCTGGCA GGGCCTGGCC 480 CTGCTGTCGG AAGCTGTCCT GCGGGGCCAG GCC 513 (2) INFORMATION FOR SEQ ID NO:87: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:87: TTGGTCAACT CTTCCCAGCC GTGGGAGCCC CTGCAGCTGC ATGTGGATAA AGCCGTCAGT 60 GGCCTTCGCA GCCTCACCAC TCTGCTTCGG GCTCTGGGAG CCCAGAAGGA AGCCATCTCC 120 CCTCCAGATG CGGCCTCAGC TGCTCCACTC CGAACAATCA CTGCTGACAC TTTCCGCAAA 180 CTCTTCCGAG TCTACTCCAA TTTCCTCCGG GGAAAGCTGA AGCTGTACAC AGGGGAGGCC 240 TGCAGGACAG GGGACAGATG AGGCGGCGGC TCCCCCCACC ACGCCTCATC TGTGACAGCC 300 GAGTCCTGGA GAGGTACCTC TTGGAGGCCA AGGAGGCCGA GAATATCACG ACGGGCTGTG 360 CTGAACACTG CAGCTTGAAT GAGAATAATC ACTGTCCCAG ACACCAAAGT TAATTTCTAT 420 GCCTGGAAGA GGATGGAGGT CGGGCAGCAG GCCGTAGAAG TCTGGCAGGG CCTGGCCCTG 480 CTGTCGGAAG CTGTCCTGCG GGGCCAGGCC CTG 513 (2) INFORMATION FOR SEQ ID NO:88: )i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:88: GTCAACTCTT CCCAGCCGTG GGAGCCCCTG CAGCTGCATG TGGATAAAGC CGTCAGTGGC 60 CTTCGCAGCC TCACCACTCT GCTTCGGGCT CTGGGAGCCC AGAAGGAAGC CATCTCCCCT 120 CCAGATGCGG CCTCAGCTGC TCCACTCCGA ACAATCACTG CTGACACTTT CCGCAAACTC 180 TTCCGAGTCT ACTCCAATTT CCTCCGGGGA AAGCTGAAGC TGTACACAGG GGAGGCCTGC 240 AGGACAGGGG ACAGATGAGG CGGCGGCTCC CCCCACCACG CCTCATCTGT GACAGCCGAG 300 TCCTGGAGAG GTACCTCTTG GAGGCCAAGG AGGCCGAGAA TATCACGACG GGCTGTGCTG 360 AACACTGCAG CTTGAATGAG AATAATCACT GTCCCAGACA CCAAAGTTAA TTTCTATGCC 420 TGGAAGAGGA TGGAGGTCGG GCAGCAGGCC GTAGAAGTCT GGCAGGGCCT GGCCCTGCTG 480 TCGGAAGCTG TCCTGCGGGG CCAGGCCCTG TTG 513 (2) INFORMATION FOR SEQ ID NO:89: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:89: AACTCTTCCC AGCCGTGGGA GCCCCTGCAG CTGCATGTGG ATAAAGCCGT CAGTGGCCTT 60 CGCAGCCTCA CCACTCTGCT TCGGGCTCTG GGAGCCCAGA AGGAAGCCAT CTCCCCTCCA 120 GATGCGGCCT CAGCTGCTCC ACTCCGAACA ATCACTGCTG ACACTTTCCG CAAACTCTTC 180 CGAGTCTACT CCAATTTCCT CCGGGGAAAG CTGAAGCTGT ACACAGGGGA GGCCTGCAGG 240 ACAGGGGACA GATGAGGCGG CGGCTCCCCC CACCACGCCT CATCTGTGAC AGCCGAGTCC 300 TGGAGAGGTA CCTCTTGGAG GCCAAGGAGG CCGAGAATAT CACGACGGGC TGTGCTGAAC 360 ACTGCAGCTT GAATGAGAAT AATCACTGTC CCAGACACCA AAGTTAATTT CTATGCCTGG 420 AAGAGGATGG AGGTCGGGCA GCAGGCCGTA GAAGTCTGGC AGGGCCTGGC CCTGCTGTCG 480 GAAGCTGTCC TGCGGGGCCA GGCCCTGTTG GTC 513 (2) INFORMATION FOR SEQ ID NO:90: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:90: TCTTCCCAGC CGTGGGAGCC CCTGCAGCTG CATGTGGATA AAGCCGTCAG TGGCCTTCGC 60 AGCCTCACCA CTCTGCTTCG GGCTCTGGGA GCCCAGAAGG AAGCCATCTC CCCTCCAGAT 120 GCGGCCTCAG CTGCTCCACT CCGAACAATC ACTGCTGACA CTTTCCGCAA ACTCTTCCGA 180 GTCTACTCCA ATTTCCTCCG GGGAAAGCTG AAGCTGTACA CAGGGGAGGC CTGCAGGACA 240 GGGGACAGAT GAGGCGGCGG CTCCCCCCAC CACGCCTCAT CTGTGACAGC CGAGTCCTGG 300 AGAGGTACCT CTTGGAGGCC AAGGAGGCCG AGAATATCAC GACGGGCTGT GCTGAACACT 360 GCAGCTTGAA TGAGAATAAT CACTGTCCCA GACACCAAAG TTAATTTCTA TGCCTGGAAG 420 AGGATGGAGG TCGGGCAGCA GGCCGTAGAA GTCTGGCAGG GCCTGGCCCT GCTGTCGGAA 480 GCTGTCCTGC GGGGCCAGGC CCTGTTGGTC AAC 513 (2) INFORMATION FOR SEQ ID NO:91: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:91: TCCCAGCCGT GGGAGCCCCT GCAGCTGCAT GTGGATAAAG CCGTCAGTGG CCTTCGCAGC 60 CTCACCACTC TGCTTCGGGC TCTGGGAGCC CAGAAGGAAG CCATCTCCCC TCCAGATGCG 120 GCCTCAGCTG CTCCACTCCG AACAATCACT GCTGACACTT TCCGCAAACT CTTCCGAGTC 180 TACTCCAATT TCCTCCGGGG AAAGCTGAAG CTGTACACAG GGGAGGCCTG CAGGACAGGG 240 GACAGATGAG GCGGCGGCTC CCCCCACCAC GCCTCATCTG TGACAGCCGA GTCCTGGAGA 300 GGTACCTCTT GGAGGCCAAG GAGGCCGAGA ATATCACGAC GGGCTGTGCT GAACACTGCA 360 GCTTGAATGA GAATAATCAC TGTCCCAGAC ACCAAAGTTA ATTTCTATGC CTGGAAGAGG 420 ATGGAGGTCG GGCAGCAGGC CGTAGAAGTC TGGCAGGGCC TGGCCCTGCT GTCGGAAGCT 480 GTCCTGCGGG GCCAGGCCCT GTTGGTCAAC TCT 513 (2) INFORMATION FOR SEQ ID NO:92: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:92: CAGCCGTGGG AGCCCCTGCA GCTGCATGTG GATAAAGCCG TCAGTGGCCT TCGCAGCCTC 60 ACCACTCTGC TTCGGGCTCT GGGAGCCCAG AAGGAAGCCA TCTCCCCTCC AGATGCGGCC 120 TCAGCTGCTC CACTCCGAAC AATCACTGCT GACACTTTCC GCAAACTCTT CCGAGTCTAC 180 TCCAATTTCC TCCGGGGAAA GCTGAAGCTG TACACAGGGG AGGCCTGCAG GACAGGGGAC 240 AGATGAGGCG GCGGCTCCCC CCACCACGCC TCATCTGTGA CAGCCGAGTC CTGGAGAGGT 300 ACCTCTTGGA GGCCAAGGAG GCCGAGAATA TCACGACGGG CTGTGCTGAA CACTGCAGCT 360 TGAATGAGAA TAATCACTGT CCCAGACACC AAAGTTAATT TCTATGCCTG GAAGAGGATG 420 GAGGTCGGGC AGCAGGCCGT AGAAGTCTGG CAGGGCCTGG CCCTGCTGTC GGAAGCTGTC 480 CTGCGGGGCC AGGCCCTGTT GGTCAACTCT TCC 513 (2) INFORMATION FOR SEQ ID NO:93: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:93: CCGTGGGAGC CCCTGCAGCT GCATGTGGAT AAAGCCGTCA GTGGCCTTCG CAGCCTCACC 60 ACTCTGCTTC GGGCTCTGGG AGCCCAGAAG GAAGCCATCT CCCCTCCAGA TGCGGCCTCA 120 GCTGCTCCAC TCCGAACAAT CACTGCTGAC ACTTTCCGCA AACTCTTCCG AGTCTACTCC 180 AATTTCCTCC GGGGAAAGCT GAAGCTGTAC ACAGGGGAGG CCTGCAGGAC AGGGGACAGA 240 TGAGGCGGCG GCTCCCCCCA CCACGCCTCA TCTGTGACAG CCGAGTCCTG GAGAGGTACC 300 TCTTGGAGGC CAAGGAGGCC GAGAATATCA CGACGGGCTG TGCTGAACAC TGCAGCTTGA 360 ATGAGAATAA TCACTGTCCC AGACACCAAA GTTAATTTCT ATGCCTGGAA GAGGATGGAG 420 GTCGGGCAGC AGGCCGTAGA AGTCTGGCAG GGCCTGGCCC TGCTGTCGGA AGCTGTCCTG 480 CGGGGCCAGG CCCTGTTGGT CAACTCTTCC CAG 513 (2) INFORMATION FOR SEQ ID NO:94: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (c) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:94: TGGGAGCCCC TGCAGCTGCA TGTGGATAAA GCCGTCAGTG GCCTTCGCAG CCTCACCACT 60 CTGCTTCGGG CTCTGGGAGC CCAGAAGGAA GCCATCTCCC CTCCAGATGC GGCCTCAGCT 120 GCTCCACTCC GAACAATCAC TGCTGACACT TTCCGCAAAC TCTTCCGAGT CTACTCCAAT 180 TTCCTCCGGG GAAAGCTGAA GCTGTACACA GGGGAGGCCT GCAGGACAGG GGACAGATGA 240 GGCGGCGGCT CCCCCCACCA CGCCTCATCT GTGACAGCCG AGTCCTGGAG AGGTACCTCT 300 TGGAGGCCAA GGAGGCCGAG AATATCACGA CGGGCTGTGC TGAACACTGC AGCTTGAATG 360 AGAATAATCA CTGTCCCAGA CACCAAAGTT AATTTCTATG CCTGGAAGAG GATGGAGGTC 420 GGGCAGCAGG CCGTAGAAGT CTGGCAGGGC CTGGCCCTGC TGTCGGAAGC TGTCCTGCGG 480 GGCCAGGCCC TGTTGGTCAA CTCTTCCCAG CCG 513 (2) INFORMATION FOR SEQ ID NO:95: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:95: GAGCCCCTGC AGCTGCATGT GGATAAAGCC GTCAGTGGCC TTCGCAGCCT CACCACTCTG 60 CTTCGGGCTC TGGGAGCCCA GAAGGAAGCC ATCTCCCCTC CAGATGCGGC CTCAGCTGCT 120 CCACTCCGAA CAATCACTGC TGACACTTTC CGCAAACTCT TCCGAGTCTA CTCCAATTTC 180 CTCCGGGGAA AGCTGAAGCT GTACACAGGG GAGGCCTGCA GGACAGGGGA CAGATGAGGC 240 GGCGGCTCCC CCCACCACGC CTCATCTGTG ACAGCCGAGT CCTGGAGAGG TACCTCTTGG 300 AGGCCAAGGA GGCCGAGAAT ATCACGACGG GCTGTGCTGA ACACTGCAGC TTGAATGAGA 360 ATAATCACTG TCCCAGACAC CAAAGTTAAT TTCTATGCCT GGAAGAGGAT GGAGGTCGGG 420 CAGCAGGCCG TAGAAGTCTG GCAGGGCCTG GCCCTGCTGT CGGAAGCTGT CCTGCGGGGC 480 CAGGCCCTGT TGGTCAACTC TTCCCAGCCG TGG 513 (2) INFORMATION FOR SEQ ID NO:96: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:96: CTTCGGGCTC TGGGAGCCCA GAAGGAAGCC ATCTCCCCTC CAGATGCGGC CTCAGCTGCT 60 CCACTCCGAA CAATCACTGC TGACACTTTC CGCAAACTCT TCCGAGTCTA CTCCAATTTC 120 CTCCGGGGAA AGCTGAAGCT GTACACAGGG GAGGCCTGCA GGACAGGGGA CAGATGAGGC 180 GGCGGCTCCC CCCACCACGC CTCATCTGTG ACAGCCGAGT CCTGGAGAGG TACCTCTTGG 240 AGGCCAAGGA GGCCGAGAAT ATCACGACGG GCTGTGCTGA ACACTGCAGC TTGAATGAGA 300 ATAATCACTG TCCCAGACAC CAAAGTTAAT TTCTATGCCT GGAAGAGGAT GGAGGTCGGG 360 CAGCAGGCCG TAGAAGTCTG GCAGGGCCTG GCCCTGCTGT CGGAAGCTGT CCTGCGGGGC 420 CAGGCCCTGT TGGTCAACTC TTCCCAGCCG TGGGAGCCCC TGCAGCTGCA TGTGGATAAA 480 GCCGTCAGTG GCCTTCGCAG CCTCACCACT CTG 513 (2) INFORMATION FOR SEQ ID NO:97: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:97: CGGGCTCTGG GAGCCCAGAA GGAAGCCATC TCCCCTCCAG ATGCGGCCTC AGCTGCTCCA 60 CTCCGAACAA TCACTGCTGA CACTTTCCGC AAACTCTTCC GAGTCTACTC CAATTTCCTC 120 CGGGGAAAGC TGAAGCTGTA CACAGGGGAG GCCTGCAGGA CAGGGGACAG ATGAGGCGGC 180 GGCTCCCCCC ACCACGCCTC ATCTGTGACA GCCGAGTCCT GGAGAGGTAC CTCTTGGAGG 240 CCAAGGAGGC CGAGAATATC ACGACGGGCT GTGCTGAACA CTGCAGCTTG AATGAGAATA 300 ATCACTGTCC CAGACACCAA AGTTAATTTC TATGCCTGGA AGAGGATGGA GGTCGGGCAG 360 CAGGCCGTAG AAGTCTGGCA GGGCCTGGCC CTGCTGTCGG AAGCTGTCCT GCGGGGCCAG 420 GCCCTGTTGG TCAACTCTTC CCAGCCGTGG GAGCCCCTGC AGCTGCATGT GGATAAAGCC 480 GTCAGTGGCC TTCGCAGCCT CACCACTCTG CTT 513 (2) INFORMATION FOR SEQ ID NO:98: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:98: GCTCTGGGAG CCCAGAAGGA AGCCATCTCC CCTCCAGATG CGGCCTCAGC TGCTCCACTC 60 CGAACAATCA CTGCTGACAC TTTCCGCAAA CTCTTCCGAG TCTACTCCAA TTTCCTCCGG 120 GGAAAGCTGA AGCTGTACAC AGGGGAGGCC TGCAGGACAG GGGACAGATG AGGCGGCGGC 180 TCCCCCCACC ACGCCTCATC TGTGACAGCC GAGTCCTGGA GAGGTACCTC TTGGAGGCCA 240 AGGAGGCCGA GAATATCACG ACGGGCTGTG CTGAACACTG CAGCTTGAAT GAGAATAATC 300 ACTGTCCCAG ACACCAAAGT TAATTTCTAT GCCTGGAAGA GGATGGAGGT CGGGCAGCAG 360 GCCGTAGAAG TCTGGCAGGG CCTGGCCCTG CTGTCGGAAG CTGTCCTGCG GGGCCAGGCC 420 CTGTTGGTCA ACTCTTCCCA GCCGTGGGAG CCCCTGCAGC TGCATGTGGA TAAAGCCGTC 480 AGTGGCCTTC GCAGCCTCAC CACTCTGCTT CGG 513 (2) INFORMATION FOR SEQ ID NO:99: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:99: CTGGGAGCCC AGAAGGAAGC CATCTCCCCT CCAGATGCGG CCTCAGCTGC TCCACTCCGA 60 ACAATCACTG CTGACACTTT CCGCAAACTC TTCCGAGTCT ACTCCAATTT CCTCCGGGGA 120 AAGCTGAAGC TGTACACAGG GGAGGCCTGC AGGACAGGGG ACAGATGAGG CGGCGGCTCC 180 CCCCACCACG CCTCATCTGT GACAGCCGAG TCCTGGAGAG GTACCTCTTG GAGGCCAAGG 240 AGGCCGAGAA TATCACGACG GGCTGTGCTG AACACTGCAG CTTGAATGAG AATAATCACT 300 GTCCCAGACA CCAAAGTTAA TTTCTATGCC TGGAAGAGGA TGGAGGTCGG GCAGCAGGCC 360 GTAGAAGTCT GGCAGGGCCT GGCCCTGCTG TCGGAAGCTG TCCTGCGGGG CCAGGCCCTG 420 TTGGTCAACT CTTCCCAGCC GTGGGAGCCC CTGCAGCTGC ATGTGGATAA AGCCGTCAGT 480 GGCCTTCGCA GCCTCACCAC TCTGCTTCGG GTC 513 (2) INFORMATION FOR SEQ ID NO:100: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:100: GGAGCCCAGA AGGAAGCCAT CTCCCCTCCA GATGCGGCCT CAGCTGCTCC ACTCCGAACA 60 ATCACTGCTG ACACTTTCCG CAAACTCTTC CGAGTCTACT CCAATTTCCT CCGGGGAAAG 120 CTGAAGCTGT ACACAGGGGA GGCCTGCAGG ACAGGGGACA GATGAGGCGG CGGCTCCCCC 180 CACCACGCCT CATCTGTGAC AGCCGAGTCC TGGAGAGGTA CCTCTTGGAG GCCAAGGAGG 240 CCGAGAATAT CACGACGGGC TGTGCTGAAC ACTGCAGCTT GAATGAGAAT AATCACTGTC 300 CCAGACACCA AAGTTAATTT CTATGCCTGG AAGAGGATGG AGGTCGGGCA GCAGGCCGTA 360 GAAGTCTGGC AGGGCCTGGC CCTGCTGTCG GAAGCTGTCC TGCGGGGCCA GGCCCTGTTG 420 GTCAACTCTT CCCAGCCGTG GGAGCCCCTG CAGCTGCATG TGGATAAAGC CGTCAGTGGC 480 CTTCGCAGCC TCACCACTCT GCTTCGGGCT CTG 513 (2) INFORMATION FOR SEQ ID NO:101: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:101: GCCCAGAAGG AAGCCATCTC CCCTCCAGAT GCGGCCTCAG CTGCTCCACT CCGAACAATC 60 ACTGCTGACA CTTTCCGCAA ACTCTTCCGA GTCTACTCCA ATTTCCTCCG GGGAAAGCTG 120 AAGCTGTACA CAGGGGAGGC CTGCAGGACA GGGGACAGAT GAGGCGGCGG CTCCCCCCAC 180 CACGCCTCAT CTGTGACAGC CGAGTCCTGG AGAGGTACCT CTTGGAGGCC AAGGAGGCCG 240 AGAATATCAC GACGGGCTGT GCTGAACACT GCAGCTTGAA TGAGAATAAT CACTGTCCCA 300 GACACCAAAG TTAATTTCTA TGCCTGGAAG AGGATGGAGG TCGGGCAGCA GGCCGTAGAA 360 GTCTGGCAGG GCCTGGCCCT GCTGTCGGAA GCTGTCCTGC GGGGCCAGGC CCTGTTGGTC 420 AACTCTTCCC AGCCGTGGGA GCCCCTGCAG CTGCATGTGG ATAAAGCCGT CAGTGGCCTT 480 CGCAGCCTCA CCACTCTGCT TCGGGCTCTG GGA 513 (2) INFORMATION FOR SEQ ID NO:102: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:102: CAGAAGGAAG CCATCTCCCC TCCAGATGCG GCCTCAGCTG CTCCACTCCG AACAATCACT 60 GCTGACACTT TCCGCAAACT CTTCCGAGTC TACTCCAATT TCCTCCGGGG AAAGCTGAAG 120 CTGTACACAG GGGAGGCCTG CAGGACAGGG GACAGATGAG GCGGCGGCTC CCCCCACCAC 180 GCCTCATCTG TGACAGCCGA GTCCTGGAGA GGTACCTCTT GGAGGCCAAG GAGGCCGAGA 240 ATATCACGAC GGGCTGTGCT GAACACTGCA GCTTGAATGA GAATAATCAC TGTCCCAGAC 300 ACCAAAGTTA ATTTCTATGC CTGGAAGAGG ATGGAGGTCG GGCAGCAGGC CGTAGAAGTC 360 TGGCAGGGCC TGGCCCTGCT GTCGGAAGCT GTCCTGCGGG GCCAGGCCCT GTTGGTCAAC 420 TCTTCCCAGC CGTGGGAGCC CCTGCAGCTG CATGTGGATA AAGCCGTCAG TGGCCTTCGC 480 AGCCTCACCA CTCTGCTTCG GGCTCTGGGA GCC 513 (2) INFORMATION FOR SEQ ID NO:103: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:103: AAGGAAGCCA TCTCCCCTCC AGATGCGGCC TCAGCTGCTC CACTCCGAAC AATCACTGCT 60 GACACTTTCC GCAAACTCTT CCGAGTCTAC TCCAATTTCC TCCGGGGAAA GCTGAAGCTG 120 TACACAGGGG AGGCCTGCAG GACAGGGGAC AGATGAGGCG GCGGCTCCCC CCACCACGCC 180 TCATCTGTGA CAGCCGAGTC CTGGAGAGGT ACCTCTTGGA GGCCAAGGAG GCCGAGAATA 240 TCACGACGGG CTGTGCTGAA CACTGCAGCT TGAATGAGAA TAATCACTGT CCCAGACACC 300 AAAGTTAATT TCTATGCCTG GAAGAGGATG GAGGTCGGGC AGCAGGCCGT AGAAGTCTGG 360 CAGGGCCTGG CCCTGCTGTC GGAAGCTGTC CTGCGGGGCC AGGCCCTGTT GGTCAACTCT 420 TCCCAGCCGT GGGAGCCCCT GCAGCTGCAT GTGGATAAAG CCGTCAGTGG CCTTCGCAGC 480 CTCACCACTC TGCTTCGGGC TCTGGGAGCC CAG 513 (2) INFORMATION FOR SEQ ID NO:104: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:104: GAAGCCATCT CCCCTCCAGA TGCGGCCTCA GCTGCTCCAC TCCGAACAAT CACTGCTGAC 60 ACTTTCCGCA AACTCTTCCG AGTCTACTCC AATTTCCTCC GGGGAAAGCT GAAGCTGTAC 120 ACAGGGGAGG CCTGCAGGAC AGGGGACAGA TGAGGCGGCG GCTCCCCCCA CCACGCCTCA 180 TCTGTGACAG CCGAGTCCTG GAGAGGTACC TCTTGGAGGC CAAGGAGGCC GAGAATATCA 240 CGACGGGCTG TGCTGAACAC TGCAGCTTGA ATGAGAATAA TCACTGTCCC AGACACCAAA 300 GTTAATTTCT ATGCCTGGAA GAGGATGGAG GTCGGGCAGC AGGCCGTAGA AGTCTGGCAG 360 GGCCTGGCCC TGCTGTCGGA AGCTGTCCTG CGGGGCCAGG CCCTGTTGGT CAACTCTTCC 420 CAGCCGTGGG AGCCCCTGCA GCTGCATGTG GATAAAGCCG TCAGTGGCCT TCGCAGCCTC 480 ACCACTCTGC TTCGGGCTCT GGGAGCCCAG AAG 513 (2) INFORMATION FOR SEQ ID NO:105: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:105: GCCATCTCCC CTCCAGATGC GGCCTCAGCT GCTCCACTCC GAACAATCAC TGCTGACACT 60 TTCCGCAAAC TCTTCCGAGT CTACTCCAAT TTCCTCCGGG GAAAGCTGAA GCTGTACACA 120 GGGGAGGCCT GCAGGACAGG GGACAGATGA GGCGGCGGCT CCCCCCACCA CGCCTCATCT 180 GTGACAGCCG AGTCCTGGAG AGGTACCTCT TGGAGGCCAA GGAGGCCGAG AATATCACGA 240 CGGGCTGTGC TGAACACTGC AGCTTGAATG AGAATAATCA CTGTCCCAGA CACCAAAGTT 300 AATTTCTATG CCTGGAAGAG GATGGAGGTC GGGCAGCAGG CCGTAGAAGT CTGGCAGGGC 360 CTGGCCCTGC TGTCGGAAGC TGTCCTGCGG GGCCAGGCCC TGTTGGTCAA CTCTTCCCAG 420 CCGTGGGAGC CCCTGCAGCT GCATGTGGAT AAAGCCGTCA GTGGCCTTCG CAGCCTCACC 480 ACTCTGCTTC GGGCTCTGGG AGCCCAGAAG GAA 513 (2) INFORMATION FOR SEQ ID NO:106: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:106: ATCTCCCCTC CAGATGCGGC CTCAGCTGCT CCACTCCGAA CAATCACTGC TGACACTTTC 60 CGCAAACTCT TCCGAGTCTA CTCCAATTTC CTCCGGGGAA AGCTGAAGCT GTACACAGGG 120 GAGGCCTGCA GGACAGGGGA CAGATGAGGC GGCGGCTCCC CCCACCACGC CTCATCTGTG 180 ACAGCCGAGT CCTGGAGAGG TACCTCTTGG AGGCCAAGGA GGCCGAGAAT ATCACGACGG 240 GCTGTGCTGA ACACTGCAGC TTGAATGAGA ATAATCACTG TCCCAGACAC CAAAGTTAAT 300 TTCTATGCCT GGAAGAGGAT GGAGGTCGGG CAGCAGGCCG TAGAAGTCTG GCAGGGCCTG 360 GCCCTGCTGT CGGAAGCTGT CCTGCGGGGC CAGGCCCTGT TGGTCAACTC TTCCCAGCCG 420 TGGGAGCCCC TGCAGCTGCA TGTGGATAAA GCCGTCAGTG GCCTTCGCAG CCTCACCACT 480 CTGCTTCGGG CTCTGGGAGC CCAGAAGGAA GCC 513 (2) INFORMATION FOR SEQ ID NO:107: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:107: TCCCCTCCAG ATGCGGCCTC AGCTGCTCCA CTCCGAACAA TCACTGCTGA CACTTTCCGC 60 AAACTCTTCC GAGTCTACTC CAATTTCCTC CGGGGAAAGC TGAAGCTGTA CACAGGGGAG 120 GCCTGCAGGA CAGGGGACAG ATGAGGCGGC GGCTCCCCCC ACCACGCCTC ATCTGTGACA 180 GCCGAGTCCT GGAGAGGTAC CTCTTGGAGG CCAAGGAGGC CGAGAATATC ACGACGGGCT 240 GTGCTGAACA CTGCAGCTTG AATGAGAATA ATCACTGTCC CAGACACCAA AGTTAATTTC 300 TATGCCTGGA AGAGGATGGA GGTCGGGCAG CAGGCCGTAG AAGTCTGGCA GGGCCTGGCC 360 CTGCTGTCGG AAGCTGTCCT GCGGGGCCAG GCCCTGTTGG TCAACTCTTC CCAGCCGTGG 420 GAGCCCCTGC AGCTGCATGT GGATAAAGCC GTCAGTGGCC TTCGCAGCCT CACCACTCTG 480 CTTCGGGCTC TGGGAGCCCA GAAGGAAGCC ATC 513 (2) INFORMATION FOR SEQ ID NO:108: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:108: CCTCCAGATG CGGCCTCAGC TGCTCCACTC CGAACAATCA CTGCTGACAC TTTCCGCAAA 60 CTCTTCCGAG TCTACTCCAA TTTCCTCCGG GGAAAGCTGA AGCTGTACAC AGGGGAGGCC 120 TGCAGGACAG GGGACAGATG AGGCGGCGGC TCCCCCCACC ACGCCTCATC TGTGACAGCC 180 GAGTCCTGGA GAGGTACCTC TTGGAGGCCA AGGAGGCCGA GAATATCACG ACGGGCTGTG 240 CTGAACACTG CAGCTTGAAT GAGAATAATC ACTGTCCCAG ACACCAAAGT TAATTTCTAT 300 GCCTGGAAGA GGATGGAGGT CGGGCAGCAG GCCGTAGAAG TCTGGCAGGG CCTGGCCCTG 360 CTGTCGGAAG CTGTCCTGCG GGGCCAGGCC CTGTTGGTCA ACTCTTCCCA GCCGTGGGAG 420 CCCCTGCAGC TGCATGTGGA TAAAGCCGTC AGTGGCCTTC GCAGCCTCAC CACTCTGCTT 480 CGGGCTCTGG GAGCCCAGAA GGAAGCCATC TCC 513 (2) INFORMATION FOR SEQ ID NO:109: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:109: CCAGATGCGG CCTCAGCTGC TCCACTCCGA ACAATCACTG CTGACACTTT CCGCAAACTC 60 TTCCGAGTCT ACTCCAATTT CCTCCGGGGA AAGCTGAAGC TGTACACAGG GGAGGCCTGC 120 AGGACAGGGG ACAGATGAGG CGGCGGCTCC CCCCACCACG CCTCATCTGT GACAGCCGAG 180 TCCTGGAGAG GTACCTCTTG GAGGCCAAGG AGGCCGAGAA TATCACGACG GGCTGTGCTG 240 AACACTGCAG CTTGAATGAG AATAATCACT GTCCCAGACA CCAAAGTTAA TTTCTATGCC 300 TGGAAGAGGA TGGAGGTCGG GCAGCAGGCC GTAGAAGTCT GGCAGGGCCT GGCCCTGCTG 360 TCGGAAGCTG TCCTGCGGGG CCAGGCCCTG TTGGTCAACT CTTCCCAGCC GTGGGAGCCC 420 CTGCAGCTGC ATGTGGATAA AGCCGTCAGT GGCCTTCGCA GCCTCACCAC TCTGCTTCGG 480 GCTCTGGGAG CCCAGAAGGA AGCCATCTCC CCT 513 (2) INFORMATION FOR SEQ ID NO:110: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:110: GATGCGGCCT CAGCTGCTCC ACTCCGAACA ATCACTGCTG ACACTTTCCG CAAACTCTTC 60 CGAGTCTACT CCAATTTCCT CCGGGGAAAG CTGAAGCTGT ACACAGGGGA GGCCTGCAGG 120 ACAGGGGACA GATGAGGCGG CGGCTCCCCC CACCACGCCT CATCTGTGAC AGCCGAGTCC 180 TGGAGAGGTA CCTCTTGGAG GCCAAGGAGG CCGAGAATAT CACGACGGGC TGTGCTGAAC 240 ACTGCAGCTT GAATGAGAAT AATCACTGTC CCAGACACCA AAGTTAATTT CTATGCCTGG 300 AAGAGGATGG AGGTCGGGCA GCAGGCCGTA GAAGTCTGGC AGGGCCTGGC CCTGCTGTCG 360 GAAGCTGTCC TGCGGGGCCA GGCCCTGTTG GTCAACTCTT CCCAGCCGTG GGAGCCCCTG 420 CAGCTGCATG TGGATAAAGC CGTCAGTGGC CTTCGCAGCC TCACCACTCT GCTTCGGGCT 480 CTGGGAGCCC AGAAGGAAGC CATCTCCCCT CCA 513 (2) INFORMATION FOR SEQ ID NO:lll: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:ll1: GCGGCCTCAG CTGCTCCACT CCGAACAATC ACTGCTGACA CTTTCCGCAA ACTCTTCCGA 60 GTCTACTCCA ATTTCCTCCG GGGAAAGCTG AAGCTGTACA CAGGGGAGGC CTGCAGGACA 120 GGGGACAGAT GAGGCGGCGG CTCCCCCCAC CACGCCTCAT CTGTGACAGC CGAGTCCTGG 180 AGAGGTACCT CTTGGAGGCC AAGGAGGCCG AGAATATCAC GACGGGCTGT GCTGAACACT 240 GCAGCTTGAA TGAGAATAAT CACTGTCCCA GACACCAAAG TTAATTTCTA TGCCTGGAAG 300 AGGATGGAGG TCGGGCAGCA GGCCGTAGAA GTCTGGCAGG GCCTGGCCCT GCTGTCGGAA 360 GCTGTCCTGC GGGGCCAGGC CCTGTTGGTC AACTCTTCCC AGCCGTGGGA GCCCCTGCAG 420 CTGCATGTGG ATAAAGCCGT CAGTGGCCTT CGCAGCCTCA CCACTCTGCT TCGGGCTCTG 480 GGAGCCCAGA AGGAAGCCAT CTCCCCTCCA GAT 513 (2) INFORMATION FOR SEQ ID NO:112: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:112: GCCTCAGCTG CTCCACTCCG AACAATCACT GCTGACACTT TCCGCAAACT CTTCCGAGTC 60 TACTCCAATT TCCTCCGGGG AAAGCTGAAG CTGTACACAG GGGAGGCCTG CAGGACAGGG 120 GACAGATGAG GCGGCGGCTC CCCCCACCAC GCCTCATCTG TGACAGCCGA GTCCTGGAGA 180 GGTACCTCTT GGAGGCCAAG GAGGCCGAGA ATATCACGAC GGGCTGTGCT GAACACTGCA 240 GCTTGAATGA GAATAATCAC TGTCCCAGAC ACCAAAGTTA ATTTCTATGC CTGGAAGAGG 300 ATGGAGGTCG GGCAGCAGGC CGTAGAAGTC TGGCAGGGCC TGGCCCTGCT GTCGGAAGCT 360 GTCCTGCGGG GCCAGGCCCT GTTGGTCAAC TCTTCCCAGC CGTGGGAGCC CCTGCAGCTG 420 CATGTGGATA AAGCCGTCAG TGGCCTTCGC AGCCTCACCA CTCTGCTTCG GGCTCTGGGA 480 GCCCAGAAGG AAGCCATCTC CCCTCCAGAT GCG 513 (2) INFORMATION FOR SEQ ID NO:113: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:113: TCAGCTGCTC CACTCCGAAC AATCACTGCT GACACTTTCC GCAAACTCTT CCGAGTCTAC 60 TCCAATTTCC TCCGGGGAAA GCTGAAGCTG TACACAGGGG AGGCCTGCAG GACAGGGGAC 120 AGATGAGGCG GCGGCTCCCC CCACCACGCC TCATCTGTGA CAGCCGAGTC CTGGAGAGGT 180 ACCTCTTGGA GGCCAAGGAG GCCGAGAATA TCACGACGGG CTGTGCTGAA CACTGCAGCT 240 TGAATGAGAA TAATCACTGT CCCAGACACC AAAGTTAATT TCTATGCCTG GAAGAGGATG 300 GAGGTCGGGC AGCAGGCCGT AGAAGTCTGG CAGGGCCTGG CCCTGCTGTC GGAAGCTGTC 360 CTGCGGGGCC AGGCCCTGTT GGTCAACTCT TCCCAGCCGT GGGAGCCCCT GCAGCTGCAT 420 GTGGATAAAG CCGTCAGTGG CCTTCGCAGC CTCACCACTC TGCTTCGGGC TCTGGGAGCC 480 CAGAAGGAAG CCATCTCCCC TCCAGATGCG GCC 513 (2) INFORMATION FOR SEQ ID NO:114: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:114: GCTGCTCCAC TCCGAACAAT CACTGCTGAC ACTTTCCGCA AACTCTTCCG AGTCTACTCC 60 AATTTCCTCC GGGGAAAGCT GAAGCTGTAC ACAGGGGAGG CCTGCAGGAC AGGGGACAGA 120 TGAGGCGGCG GCTCCCCCCA CCACGCCTCA TCTGTGACAG CCGAGTCCTG GAGAGGTACC 180 TCTTGGAGGC CAAGGAGGCC GAGAATATCA CGACGGGCTG TGCTGAACAC TGCAGCTTGA 240 ATGAGAATAA TCACTGTCCC AGACACCAAA GTTAATTTCT ATGCCTGGAA GAGGATGGAG 300 GTCGGGCAGC AGGCCGTAGA AGTCTGGCAG GGCCTGGCCC TGCTGTCGGA AGCTGTCCTG 360 CGGGGCCAGG CCCTGTTGGT CAACTCTTCC CAGCCGTGGG AGCCCCTGCA GCTGCATGTG 420 GATAAAGCCG TCAGTGGCCT TCGCAGCCTC ACCACTCTGC TTCGGGCTCT GGGAGCCCAG 480 AAGGAAGCCA TCTCCCCTCC AGATGCGGCC TCA 513 (2) INFORMATION FOR SEQ ID NO:115: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:115: GCTCCACTCC GAACAATCAC TGCTGACACT TTCCGCAAAC TCTTCCGAGT CTACTCCAAT 60 TTCCTCCGGG GAAAGCTGAA GCTGTACACA GGGGAGGCCT GCAGGACAGG GGACAGATGA 120 GGCGGCGGCT CCCCCCACCA CGCCTCATCT GTGACAGCCG AGTCCTGGAG AGGTACCTCT 180 TGGAGGCCAA GGAGGCCGAG AATATCACGA CGGGCTGTGC TGAACACTGC AGCTTGAATG 240 AGAATAATCA CTGTCCCAGA CACCAAAGTT AATTTCTATG CCTGGAAGAG GATGGAGGTC 300 GGGCAGCAGG CCGTAGAAGT CTGGCAGGGC CTGGCCCTGC TGTCGGAAGC TGTCCTGCGG 360 GGCCAGGCCC TGTTGGTCAA CTCTTCCCAG CCGTGGGAGC CCCTGCAGCT GCATGTGGAT 420 AAAGCCGTCA GTGGCCTTCG CAGCCTCACC ACTCTGCTTC GGGCTCTGGG AGCCCAGAAG 480 GAAGCCATCT CCCCTCCAGA TGCGGCCTCA GCT 513 (2) INFORMATION FOR SEQ ID NO:116: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:116: CCACTCCGAA CAATCACTGC TGACACTTTC CGCAAACTCT TCCGAGTCTA CTCCAATTTC 60 CTCCGGGGAA AGCTGAAGCT GTACACAGGG GAGGCCTGCA GGACAGGGGA CAGATGAGGC 120 GGCGGCTCCC CCCACCACGC CTCATCTGTG ACAGCCGAGT CCTGGAGAGG TACCTCTTGG 180 AGGCCAAGGA GGCCGAGAAT ATCACGACGG GCTGTGCTGA ACACTGCAGC TTGAATGAGA 240 ATAATCACTG TCCCAGACAC CAAAGTTAAT TTCTATGCCT GGAAGAGGAT GGAGGTCGGG 300 CAGCAGGCCG TAGAAGTCTG GCAGGGCCTG GCCCTGCTGT CGGAAGCTGT CCTGCGGGGC 360 CAGGCCCTGT TGGTCAACTC TTCCCAGCCG TGGGAGCCCC TGCAGCTGCA TGTGGATAAA 420 GCCGTCAGTG GCCTTCGCAG CCTCACCACT CTGCTTCGGG CTCTGGGAGC CCAGAAGGAA 480 GCCATCTCCC CTCCAGATGC GGCCTCAGCT GCT 513 (2) INFORMATION FOR SEQ ID NO:117: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:117: CTCCGAACAA TCACTGCTGA CACTTTCCGC AAACTCTTCC GAGTCTACTC CAATTTCCTC 60 CGGGGAAAGC TGAAGCTGTA CACAGGGGAG GCCTGCAGGA CAGGGGACAG ATGAGGCGGC 120 GGCTCCCCCC ACCACGCCTC ATCTGTGACA GCCGAGTCCT GGAGAGGTAC CTCTTGGAGG 180 CCAAGGAGGC CGAGAATATC ACGACGGGCT GTGCTGAACA CTGCAGCTTG AATGAGAATA 240 ATCACTGTCC CAGACACCAA AGTTAATTTC TATGCCTGGA AGAGGATGGA GGTCGGGCAG 300 CAGGCCGTAG AAGTCTGGCA GGGCCTGGCC CTGCTGTCGG AAGCTGTCCT GCGGGGCCAG 360 GCCCTGTTGG TCAACTCTTC CCAGCCGTGG GAGCCCCTGC AGCTGCATGT GGATAAAGCC 420 GTCAGTGGCC TTCGCAGCCT CACCACTCTG CTTCGGGCTC TGGGAGCCCA GAAGGAAGCC 480 ATCTCCCCTC CAGATGCGGC CTCAGCTGCT CCA 513 (2) INFORMATION FOR SEQ ID NO:118: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:118: CGAACAATCA CTGCTGACAC TTTCCGCAAA CTCTTCCGAG TCTACTCCAA TTTCCTCCGG 60 GGAAAGCTGA AGCTGTACAC AGGGGAGGCC TGCAGGACAG GGGACAGATG AGGCGGCGGC 120 TCCCCCCACC ACGCCTCATC TGTGACAGCC GAGTCCTGGA GAGGTACCTC TTGGAGGCCA 180 AGGAGGCCGA GAATATCACG ACGGGCTGTG CTGAACACTG CAGCTTGAAT GAGAATAATC 240 ACTGTCCCAG ACACCAAAGT TAATTTCTAT GCCTGGAAGA GGATGGAGGT CGGGCAGCAG 300 GCCGTAGAAG TCTGGCAGGG CCTGGCCCTG CTGTCGGAAG CTGTCCTGCG GGGCCAGGCC 360 CTGTTGGTCA ACTCTTCCCA GCCGTGGGAG CCCCTGCAGC TGCATGTGGA TAAAGCCGTC 420 AGTGGCCTTC GCAGCCTCAC CACTCTGCTT CGGGCTCTGG GAGCCCAGAA GGAAGCCATC 480 TCCCCTCCAG ATGCGGCCTC AGCTGCTCCA CTC 513 (2) INFORMATION FOR SEQ ID NO:119: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 513 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:119: ACAATCACTG CTGACACTTT CCGCAAACTC TTCCGAGTCT ACTCCAATTT CCTCCGGGGA 60 AAGCTGAAGC TGTACACAGG GGAGGCCTGC AGGACAGGGG ACAGATGAGG CGGCGGCTCC 120 CCCCACCACG CCTCATCTGT GACAGCCGAG TCCTGGAGAG GTACCTCTTG GAGGCCAAGG 180 AGGCCGAGAA TATCACGACG GGCTGTGCTG AACACTGCAG CTTGAATGAG AATAATCACT 240 GTCCCAGACA CCAAAGTTAA TTTCTATGCC TGGAAGAGGA TGGAGGTCGG GCAGCAGGCC 300 GTAGAAGTCT GGCAGGGCCT GGCCCTGCTG TCGGAAGCTG TCCTGCGGGG CCAGGCCCTG 360 TTGGTCAACT CTTCCCAGCC GTGGGAGCCC CTGCAGCTGC ATGTGGATAA AGCCGTCAGT 420 GGCCTTCGCA GCCTCACCAC TCTGCTTCGG GCTCTGGGAG CCCAGAAGGA AGCCATCTCC 480 CCTCCAGATG CGGCCTCAGC TGCTCCACTC CGA 513 (2) INFORMATION FOR SEQ ID NO:120: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 501 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:120: GCCCCACCAC GCCTCATCTG TGACAGCCGA GTCCTGGAGA GGTACCTCTT GGAGGCCAAG 60 GAGGCCGAGA ATATCACGAC GGGCTGTGCT GAACACTGCA GCTTGAATGA GAATATCACT 120 GTCCCAGACA CCAAAGTTAA TTTCTATGCC TGGAAGAGGA TGGAGGTCGG GCAGCAGGCC 180 GTAGAAGTCT GGCAGGGCCT GGCCCTGCTG TCGGAAGCTG TCCTGCGGGG CCAGGCCCTG 240 TTGGTCAACT CTTCCCAGCC GTGGGAGCCC CTGCAGCTGC ATGTGGATAA AGCCGTCAGT 300 GGCCTTCGCA GCCTCACCAC TCTGCTTCGG GCTCTGGGAG CCCAGAAGGA AGCCATCTCC 360 CCTCCAGATG CGGCCTCAGC TGCTCCACTC CGAACAATCA CTGCTGACAC TTTCCGCAAA 420 CTCTTCCGAG TCTACTCCAA TTTCCTCCGG GGAAAGCTGA AGCTGTACAC AGGGGAGGCC 480 TGCAGGACAG GGGACAGATG A 501 (2) INFORMATION FOR SEQ ID NO:121: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 166 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:121: Ala Pro Pro Arg Leu Ile Cys Asp Ser Arg Val Leu Glu Arg Tyr Leu 1 5 10 15 Leu Glu Ala Lys Glu Ala Glu Asn Ile Thr Thr Gly Cys Ala Glu His 20 25 30 Cys Ser Leu Asn Glu Asn Ile Thr Val Pro Asp Thr Lys Val Asn Phe 35 40 45 Tyr Ala Trp Lys Arg Met Glu Val Gly Gln Gln Ala Val Glu Val Trp 50 55 60 Gln Gly Leu Ala Leu Leu Ser Glu Ala Val Leu Arg Gly Gln Ala Leu 65 70 75 80 Leu Val Asn Ser Ser Gln Pro Trp Glu Pro Leu Gln Leu His Val Asp 85 90 95 Lys Ala Val Ser Gly Leu Arg Ser Leu Thr Thr Leu Leu Arg Ala Leu 100 105 110 Gly Ala Gln Lys Glu Ala Ile Ser Pro Pro Asp Ala Ala Ser Ala Ala 115 120 125 Pro Leu Arg Thr Ile Thr Ala Asp Thr Phe Arg Lys Leu Phe Arg Val 130 135 140 Tyr Ser Asn Phe Leu Arg Gly Lys Leu Lys Leu Tyr Thr Gly Glu Ala 145 150 155 160 Cys Arg Thr Gly Asp Arg 165 (2) INFORMATION FOR SEQ ID NO:122: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 170 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:122: Thr Val Pro Asp Thr Lys Val Asn Phe Tyr Ala Trp Lys Arg Met Glu 1 5 10 15 Val Gly Gln Gln Ala Val Glu Val Trp Gln Gly Leu Ala Leu Leu Ser 20 25 30 Glu Ala Val Leu Arg Gly Gln Ala Leu Leu Val Asn Ser Ser Gln Pro 35 40 45 Trp Glu Pro Leu Gln Leu His Val Asp Lys Ala Val Ser Gly Leu Arg 50 55 60 Ser Leu Thr Thr Leu Leu Arg Ala Leu Gly Ala Gln Lys Glu Ala Ile 65 70 75 80 Ser Pro Pro Asp Ala Ala Ser Ala Ala Pro Leu Arg Thr Ile Thr Ala 85 90 95 Asp Thr Phe Arg Lys Leu Phe Arg Val Tyr Ser Asn Phe Leu Arg Gly 100 105 110 Lys Leu Lys Leu Tyr Thr Gly Glu Ala Cys Arg Thr Gly Asp Arg Gly 115 120 125 Gly Gly Ser Ala Pro Pro Arg Leu Ile Cys Asp Ser Arg Val Leu Glu 130 135 140 Arg Tyr Leu Leu Glu Ala Lys Glu Ala Glu Asn Ile Thr Thr Gly Cys 145 150 155 160 Ala Glu His Cys Ser Leu Asn Glu Asn Ile 165 170 (2) INFORMATION FOR SEQ ID NO:123: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:123: Gly Gly Gly Ser (2) INFORMATION FOR SEQ ID NO:124: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:124: Gly Gly Gly Ser Gly Gly Gly Ser 15 (2) INFORMATION FOR SEQ ID NO:125: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 12 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:125: Gly Gly Gly Ser Gly Gly Gly Ser Gly Gly Gly Ser 15 10 (2) INFORMATION FOR SEQ ID NO:126: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 7 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:126: Ser Gly Gly Ser Gly Gly Ser 15 (2) INFORMATION FOR SEQ ID NO:127: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 5 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:127: Glu Phe Gly Asn Met 15 (2) INFORMATION FOR SEQ ID NO:128: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 6 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:128: Glu Phe Gly Gly Asn Met 15 (2) INFORMATION FOR SEQ ID NO:129: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:129: Glu Phe Gly Gly Asn Gly Gly Asn Met 15 (2) INFORMATION FOR SEQ ID NO:130: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 7 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: None (xi) SEQUENCE DESCRIPTION: SEQ ID NO:130: Gly Gly Ser Asp Met Ala Gly 15 (2) INFORMATION FOR SEQ ID NO:131: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 27 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:131: GCGCGCCCAT GGACAATCAC TGCTGAC 27 (2) INFORMATION FOR SEQ ID NO:132: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 15 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:132: TCTGTCCCCT GTCCT 15 (2) INFORMATION FOR SEQ ID NO:133: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 43 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:133: GCGCGCAAGC TTATTATCGG AGTGGAGCAG CTGAGGCCGC ATC 43 (2) INFORMATION FOR SEQ ID NO:134: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO:134: GCCCCACCAC GCCTCATCTG T 21