HEPATITIS C ASSAY UTILIZING RECOMBINANT ANTIGENS TO C-100 REGION

Abstract: The present invention provides unique recombinant antigens representing distinct antigenic regions of the HCV genome which can be used as reagents for the detection of antibodies and antigen in body fluids from individuals exposed to hepatitis C virus (HCV). The present invention also provides an assay for detecting the presence of an antibody to an HCV antigen in a sample by contacting the sample with the recombinant antigens. Preferred assay formats include a screening assay, a confirmatory assay, a competition or neutralization assay and an immunodot assay.

Description: HEPATITIS C ASSAY UTILIZING RECOMBINANT ANTIGENS TO C-100 REGION This is a continuation-in-part application of U.S. Serial No. 07/572,822, filed August 24, 1990 and U.S. Serial No. 07/614,069, filed November 7, 1990, which enjoy common ownership and are incorporated herein by reference. This application also is related to co-filed patent applications entitled "HEPAPTIS C ASSAY UTILIZING RECOMBINANT ANTIGENS TO NS1 REGION" (U.S. Serial No. 748,561) and "HEPATITIS C ASSAY UTILIZING RECOMBINANT ANTIGENS FROM NS5 REGION" (U.S. Serial No. 748,565) which enjoy common ownership and are incorporated herein by reference. This invention relates generally to an assay for identifying the presence in a sample of an antibody which is immunologically reactive with a hepatitis C virus antigen and specifically to an assay for detecting a complex of an antibody and recombinant antigens representing distinct regions of the HCV genome. Recombinant antigens derived from the molecular cloning and expression in a heterologous expression system of the synthetic DNA sequences representing distinct antigenic regions of the HCV genome can be used as reagents for the detection of antibodies and antigen in body fluids from individuals exposed to hepatitis C virus (HCV). BACKGROUND OF THE INVENTION Acute viral hepatitis is clinically diagnosed by a well-defined set of patient symptoms, including jaundice, hepatic tenderness, and an increase in the serum levels of alanine aminotransferase (ALT) and aspartate aminotransferase. Additional serologic immunoassays are generally performed to diagnose the specific type of viral causative agent. Historically, patients presenting clinical hepatitis symptoms and not otherwise infected by hepatitis A, hepatitis B, Epstein-Barr or cytomegalovirus were clinically diagnosed as having non-A non-B hepatitis (NANBH) by default. The disease may result in chronic liver damage. Each of the well-known, immunologically characterized hepatitis-inducing viruses, hepatitis A virus (HAV), hepatitis B virus (HBV), and hepatitis D virus (HDV) belongs to a separate family of viruses and has a distinctive viral organization, protein structure, and mode of replication. Attempts to identify the NANBH virus by virtue of genomic similarity to one of the known hepatitis viruses have failed, suggesting that NANBH has a distinct organization and structure. [Fowler, et al., J. Med. Virol.. 12:205-213 (1983) and Weiner, et al., J. Med. Virol.. 21 :239-247 (1987)]. Progress in developing assays to detect antibodies specific for NANBH has been particularly hampered by difficulties in correctly identifying antigens associated with NANBH. See, for example, Wands, J., et al., U.S. Patent 4,870,076, Wands, et al., Proc. Nat'l. Acad. Sci.. 83:6608-6612 (1986), Ohori, et al., J- Med. Virol.. 12:161-178 (1983), Bradley, et al., Proc. Nat'l. Acad. Sci.. 84:6277- 6281 , (1987), Akatsuka, T., et al., J. Med. Virol. 20:43-56 (1986), Seto, B., et al., U.S. Patent Application Number 07/234,641 (available from U.S. Department of Commerce National Technical Information Service, Springfield, Virginia, No. 89138168), Takahashi, K. f et al., European Patent Application No. 0 293 274, published November 30, 1988, and Seelig, R., et al., in PCT Application PCT/EP88/00123. Recently, another hepatitis-inducing virus has been unequivocally identified as hepatitis C virus (HCV) by Houghton, M., et al., European Patent Application publication number 0 318 216, May 31 , 1989. Related papers describing this virus include Kuo, G., et al., Science, 244:359-361 (1989) and Choo, Q., et. al, Science, 244:362-364 (1989). Houghton, M., et al. reported isolating cDNA sequences from HCV which encode antigens which react immunologically with antibodies present in patients infected with NANBH, thus establishing that HCV is one of the viral agents causing NANBH. The cDNA sequences associated with HCV were isolated from a cDNA library prepared from the RNA obtained from pooled serum from a chimpanzee with chronic HCV infection. The cDNA library contained cDNA sequences of approximate mean size of about 200 base pairs. The cDNA library was screened for encoded epitopes expressed in clones that could bind to antibodies in sera from patients who had previously experienced NANBH. In the European Patent Application, Houghton, M., et al. also described the preparation of several superoxide dismutase fusion polypeptides (SOD) and the use of these SOD fusion polypeptides to develop an HCV screening assay. The most complex SOD fusion polypeptide described in the European Patent Application, designated c100-3, was described as containing 154 amino acids of human SOD at the aminoterminus, 5 amino acid residues derived from the expression of a synthetic DNA adapter containing a restriction site, EcoRI, 363 amino acids derived from the expression of a cloned HCV cDNA fragment, and 5 carboxyl terminal amino acids derived from an MS2 cloning vector nucleotide sequence. The DNA sequence encoding this polypeptide was transformed into yeast cells using a plasmid. The transformed cells were cultured and expressed a 54,000 molecular weight polypeptide which was purified to about 80% purity by differential extraction. Other SOD fusion polypeptides designated SOD-NANB5.-i .-i and SOD- NANBβi were expressed in recombinant bacteria. The E. coli fusion polypeptides were purified by differential extraction and by chromatography using anion and cation exchange columns. The purification procedures were able to produce SOD- NANB5-1 --1 as about 80% pure and SOD-NAN38, as about 50% pure. The recombinant SOD fusion polypeptides described by Houghton, M., et al. were coated on microtiter wells or polystyrene beads and used to assay serum samples. Briefly, coated microtiter wells were incubated with a sample in a diluent. After incubation, the microtiter wells were washed and then developed using either a radioactively labelled sheep anti-human antibody or a mouse antihuman IgG-HRP (horseradish peroxidase) conjugate. These assays were used to detect both post acute phase and chronic phase HCV infection. Due to the preparative methods, assay specificity required adding yeast or E ^ coli extracts to the samples in order to prevent undesired immunological reactions with any yeast or E. coli antibodies present in samples. Ortho Diagnostic Systems Inc. have developed a immunoenzyme assay to detect antibodies to HCV antigens. The Ortho assay procedure is a three-stage test for serum/plasma carried out in a microwell coated with the recombinant yeast/hepatitis C virus SOD fusion polypeptide c100-3. In the first stage, a test specimen is diluted directly in the test well and incubated for a specified length of time. If antibodies to HCV antigens are present in the specimen, antigen-antibody complexes will be formed on the microwell surface. If no antibodies are present, complexes will not be formed and the unbound serum or plasma proteins will be removed in a washing step. In the second stage, anti-human IgG murine monoclonal antibody horseradish peroxidase conjugate is added to the microwell. The conjugate binds specifically to the antibody portion of the antigen-antibody complexes. If antigen-antibody complexes are not present, the unbound conjugate will also be removed by a washing step. In the third stage, an enzyme detection system composed of o- phenylenediamine 2HCI (OPD) and hydrogen peroxide is added to the test well. If bound conjugate is present, the OPD will be oxidized, resulting in a colored end product. After formation of the colored end product, dilute sulfuric acid is added to the microwell to stop the color-forming detection reaction. The intensity of the colored end product is measured with a microwell reader. The assay may be used to screen patient serum and plasma. It is established that HCV may be transmitted by contaminated blood and blood products. In transfused patients, as many as 10% will suffer from post- transfusion hepatitis. Of these, approximately 90% are the result of infections diagnosed as HCV. The prevention of transmission of HCV by blood and blood requires reliable, sensitive and specific diagnosis and prognostic tools to identify HCV carriers as well as contaminated blood and blood products. Thus, there exists a need for an HCV assay which uses reliable and efficient reagents and methods to accurately detect the presence of HCV antibodies in samples. SUMMARY OF THE INVENTION The present invention provides an improved assay for detecting the presence of an antibody to an HCV antigen in a sample by contacting the sample with at least one recombinant protein representing a distinct antigenic region of the HCV genome. Recombinant antigens which are derived from the molecular cloning and expression of synthetic DNA sequences in heterologous hosts are provided. Briefly, synthetic DNA sequences which encode the desired proteins representing distinct antigenic regions of the HCV genome are optimized for expression in E. coli by specific codon selection. Specifically, recombinant proteins representing antigenic regions of the HCV genome, are described. The proteins are expressed as chimeric fusions with E. coli CMP-KDO syπthetase (CKS) gene. The first protein is expressed by plasmid pHCV-62 and identified by SEQ. ID. NO. 11. Note that the term pHCV-62 will also refer to the fusion protein itself and that pHCV-62' will be the designation for the polypeptide using other recombinant or synthetic methodologies. Other recombinant methodologies would include the preparation of pHCV-62', utilizing different expression systems. The methodology for the preparation of synthetic peptides of HCV is described in U.S. Serial No. 456,162, filed December 22, 1989, and 610,180, filed November 7, 1990, which enjoy common ownership and are incorporated herein by reference. The next protein is expressed by plasmid pHCV-63 and is identified by SEQ. ID. NO.12. The fusion protein itself will also be referred to as pHCV-63 and pHCV-63' shall be the designation for the polypeptide identified by SEQ. ID. NO. 12 prepared using other recombinant or synthetic methodologies. SEQ. ID. 13 shall identify the recombinant protein and fusion protein of pHCV-204. The polypeptide pHCV-204' also shall be identified by SEQ. ID. NO. 13. The next protein is expressed by plasmid pHCV-112 and is identified by SEQ. ID. NO.14. The fusion protein itself will also be referred to as pHCV-112 and pHCV-112' shall be the designation for the polypeptide identified by SEQ. ID. NO. 14 prepared using other recombinant or synthetic methodologies. SEQ. ID. 16 shall identify the recombinant protein and fusion protein of pHCV-72. The polypeptide pHCV-72' also shall be identified by SEQ. ID. NO. 16. The next protein is expressed by plasmid pHCV-72 and is identified by SEQ. ID. NO.17. The fusion protein itself will also be referred to as pHCV-72 and pHCV- 72' shall be the designation for the polypeptide identified by SEQ. ID. NO. 17 prepared using other recombinant or synthetic methodologies. SEQ. ID. 18 shall identify the recombinant protein and fusion protein of pHCV-18. The polypeptide pHCV-205' also shall be identified by SEQ. ID. NO. 18. These antigens are used in the inventive immunoassays to detect the presence of HCV antibodies in samples. One assay format according to the invention provides a screening assay for identifying the presence of an antibody that is immunologically reactive with an HCV antigen. Briefly, a fluid sample is incubated with a solid support containing the two commonly bound recombinant proteins selected from the group consisting of pHCV- 62, pHCV-63, pHCV-204, pHCV-112, pHCV-72, pHCV-73 and pHCV-205. Finally, the antibody-antigen complex is detected. Another assay format provides a confirmatory assay for unequivocally identifying the presence of an antibody that is immunologically reactive with an HCV antigen. The confirmatory assay includes synthetic peptides or recombinant antigens representing an epitope contained within the C100 region of the HCV genome, which are the same regions represented by the recombinant proteins described in the screening assay. Recombinant proteins used in the confirmatory assay should have a heterologous source of antigen to that used in the primary screening assay (i.e. should not be an E. coli-derived recombinant antigen or a recombinant antigen composed in part, of CKS sequences). Briefly, specimens repeatedly reactive in the primary screening assay are retested in the confirmatory assay. Aliquots containing identical amounts of specimen are contacted with a synthetic peptide or recombinant antigen individually coated onto a solid support. Finally, the antibody-antigen complex is detected. Synthetic peptides are described in U.S. Serial No. 456,162 entitled "Hepatitis C Assay", filed December 22, 1989, and 610,180, filed November 7, 1990, which enjoy common ownership and are incorporated herein by reference. Another assay format provides a competition assay or neutralization assay directed to the confirmation that positive results are not false by identifying the presence of an antibody that is immunologically reactive with an HCV antigen in a fluid sample where the sample is used to prepare first and second immunologically equivalent aliquots. The first aliquot is contacted with solid support containing a bound polypeptide which contains at least one epitope of an HCV antigen under conditions suitable for complexing with the antibody to form a detectable antibody- polypeptide complex and the second aliquot is first contacted with the same solid support containing bound polypeptide. Another assay format provides an immunodot assay for identifying the presence of an antibody that is immunologically reactive with an HCV antigen by concurrently contacting a sample with recombinant polypeptides each containing distinct epitopes of an HCV antigen under conditions suitable for complexing the antibody with at least one of the polypeptides and detecting the antibody-polypeptide complex by reacting the complex with color producing reagents. The preferred recombinant polypeptides employed include those recombinant polypeptides derived from pHCV-62, pHCV-63, pHCV-72, pHCV-73, pHCV-112, pHCV-204 and pHCV- 205. In all of the assays, the sample is preferably diluted before contacting the polypeptide absorbed on a solid support. Samples may be obtained from different biological samples such as whole blood, serum, plasma, cerebral spinal fluid, and lymphocyte or cell culture supernatants. Solid support materials may include cellulose materials, such as paper and nitrocellulose, natural and synthetic polymeric materials, such as polyacrylamide, polystyrene, and cotton, porous gels such as silica gel, agarose, dextran and gelatin, and inorganic materials such as deactivated alumina, magnesium sulfate and glass. Suitable solid support materials may be used in assays in a variety of well known physical configurations, including microtiter wells, test tubes, beads, strips, membranes, and microparticles. A preferred solid support for a πon-immunodot assay is a polystyrene bead. A preferred solid support for an immunodot assay is nitrocellulose. Suitable methods and reagents for detecting an antibody-antigen complex in an assay of the present invention are commercially available or known in the relevant art. Representative methods may employ detection reagents such as enzymatic, radioisotopic, fluorescent, luminescent, or chemiluminescent reagents. These reagents may be used to prepare hapten-labelled anti-hapten detection systems according to known procedures, for example, a biotin-labelled anti-biotin system may be used to detect an antibody-antigen complex. The present invention also encompasses assay kits including polypeptides which contain at least one epitope of an HCV antigen bound to a solid support as well as needed sample preparation reagents, wash reagents, detection reagents and signal producing reagents. Other aspects and advantages of the invention will be apparent to those skilled in the art upon consideration of the following detailed description which provides illustrations of the invention in its presently preferred embodiments. E. coli strains containing plasmids useful for constructs of the invention have been deposited at the American Type Culture Collection, Rockville, Maryland on August 10, 1990, under the accession Nos. ATCC 68380 (pHCV-23), ATCC 68381 (pHCV-29), ATCC 68382 (pHCV-31 ), ATCC 68383 (pHCV-34) and on November 6, 1990 for E. coli strains containing plasmids useful for constructs under the accession Nos ATCC 68458 (pHCV-50), ATCC 68459 (pHCV-57) ATCC 68460 (pHCV-103), ATCC 68461 (pHCV-102), ATCC 68462 (pHCV-51 ), ATCC 68463 (pHCV-105), ATCC 68464 (pHCV-107), ATCC 68465 (pHCV-104), ATCC 68466 (pHCV-45), ATCC 68467 (pHCV-48), ATCC 68468 (pHCV-49), ATCC 68469 (pHCV-58) and ATCC 68470 (pHCV-101) . E. coli strains containing plasmids useful for constructs of the invention have been deposited at the A.T.C.C. on September 26, 1991 under deposit number ATCC 68692 (pHCV-62), ATCC 68687 (pHCV-63), ATCC 68685 (pHCV-72), ATCC 68684 (pHCV-73), ATCC 68694 (pHCV-204), ATCC 68693 (pHCV-205) and ATCC 68686 (pHCV-112). BRIEF DESCRIPTION OF THE DRAWINGS FIGURE 1 illustrates the HCV genome. FIGURE 2 illustrates the use of recombinant polypeptides to identify the presence of antibodies in a chimpanzee inoculated with HCV. FIGURE 3 illustrates the sensitivity and specificity increase in using the screening assay using pHCV-34 and pHCV-31 antigens. FIGURE 4 illustrates the construction of plasmid pHCV-34. FIGURE 5 illustrates fusion protein pHCV-34. FIGURE 6 illustrates the expression of pHCV-34 proteins in E. coli. FIGURE 7 illustrates the construction of plasmid pHCV-23. FIGURE 8 illustrates the construction of plasmid pHCV-29. FIGURE 9 illustrates the construction of plasmid pHCV-31. FIGURE 10 illustrates the fusion protein pHCV-31. FIGURE 11 illustrates the expression of pHCV-29 in E. coli. FIGURE 12 illustrates the expression of pHCV-23 in E. coli. FIGURE 13 illustrates the expression of pHCV-31 in E. coli. FIGURE 14 illustrates the increased sensitivity using the screening assay utilizing the pHCV-34. FIGURE 15 illustrates the increased specificity with the screening assay utilizing pHCV-34 and pHCV-31. FIGURE 16 illustrates the results in hemodialysis patients using the screening and confirmatory assays. FIGURE 17 illustrates earlier detection of HCV in a hemodialysis patient using the screening assay. FIGURE 18 illustrates the results of the screening assay utilizing pHCV-34 and pHCV-31 on samples from individuals with acute NANBH. FIGURE 19 illustrates the results of the confirmatory assay of the same population group as in Figure 18. FIGURE 20 illustrates the results of the screening and confirmatory assays on individuals infected with chronic NANBH. FIGURE 21 illustrates preferred buffers, pH conditions, and spotting concentrations for the HCV immunodot assay. FIGURE 22 illustrates the results of the HCV immunodot assay. FIGURE 23 illustrates the fusion protein pHCV-45. FIGURE 24 illustrates the expression of pHCV-45 in E. coli. FIGURE 25 illustrates the fusion protein pHCV-48. FIGURE 26 illustrates the expression of pHCV-48 in E. coli. FIGURE 27 illustrates the fusion protein pHCV-51. FIGURE 28 illustrates the expression of pHCV-51 in E. coli. FIGURE 29 illustrates the fusion protein pHCV-50. FIGURE 30 illustrates the expression of pHCV-50 in E. coli. FIGURE 31 illustrates the fusion protein pHCV-49. FIGURE 32 illustrates the expression of pHCV-49 in E. coli. FIGURE 33 illustrates an immunoblot of pHCV-23, pHCV-45, pHCV-48, pHCV-51 , pHCV-50 and pHCV-49. FIGURE 34 illustrates the fusion proteins pHCV-24, pHCV-57, pHCV-58. FIGURE 35 illustrates the expression of pHCV-24, pHCV-57, and pHCV-58 in E. coli. FIGURE 36 illustrates the fusion protein pHCV-105. FIGURE 37 illustrates the expression of pHCV-105 in E. coli. FIGURE 38 illustrates the fusion protein pHCV-103. FIGURE 39 illustrates the fusion protein pHCV-101. FIGURE 40 illustrates the fusion protein pHCV-102. FIGURE 41 illustrates the expression of pHCV-102 in E. coli. FIGURE 42 illustrates the fusion protein pHCV-107. FIGURE 43 illustrates the fusion protein pHCV-104. FIGURE 44A illustrates the expression of pHCV-19 (lane 1), pHCV-54 (lane 2), pHCV-55 (lane 3), pHCV-94 (lane 4), pHCV-95 (lane 6), pHCV-96 (lane 7) and pHCV-97 (lane 8) in E. coli. and FIGURE 44B illustrates an immunoblot of pHCV-19 (lane 1 ), pHCV-54 (lane 2), pHCV-55 (lane 3), pHCV-94 (lane 4), pHCV-95 (lane 6), pHCV-96 (lane 7) and pHCV-97 (lane 8) in E. coli. FIGURE 45A illustrates the expression of pHCV-202 (lanes 1 , 2 and 3) and pHCV-203 (lanes 4, 5 and 6) in E. coli and FIGURE 45B illustrates an immunoblot of pHCV-202 (lanes 1 , 2 and 3) and pHCV-203 (lanes 4, 5 and 6) in E. coli. FIGURE 46A illustrates the amino acid sequence of the recombinant antigen expressed by pHCV-62 (lanes 1 and 2) and pHCV-63 (lanes 3 and 4) and FIGURE 46B illustrates an immunoblot of pHCV-62 (lanes 1 and 2) and pHCV-63 (lanes 3 and 4). FIGURE 47A illustrates the expression of pHCV-204 in E. coli and FIGURE 47B illustrates an immunoblot of pHCV-204 in E. coli. FIGURE 48A illustrates the expression of pHCV-72 (lanes 1 , 2 and 3) and pHCV-73 (lanes 4, 5 and 6) in E. coli and FIGURE 48B illustrates an immunoblot of pHCV-72 (lanes 1 , 2 and 3) and pHCV-73 (lanes 4, 5 and 6) in E. coli. FIGURE 49A illustrates the expression of pHCV-205 in E. coli and FIGURE 49B illustrates an immunoblot of pHCV-205 in E. coli. DETAILED DESCRIPTION OF THE INVENTION The present invention is directed to an assay to detect an antibody to an HCV antigen in a sample. Human serum or plasma is preferably diluted in a sample diluent and incubated with a polystyrene bead coated with a recombinant polypeptide that represents a distinct antigenic region of the HCV genome. If antibodies are present in the sample they will form a complex with the antigenic polypeptide and become affixed to the polystyrene bead. After the complex has formed, unbound materials and reagents are removed by washing the bead and the bead-antigen- antibody complex is reacted with a solution containing horseradish peroxidase labeled goat antibodies directed against human antibodies. This peroxidase enzyme then binds to the antigen-antibody complex already fixed to the bead. In a final reaction the horseradish peroxidase is contacted with o-phenylenediamine and hydrogen peroxide which results in a yellow-orange color. The intensity of the color is proportional to the amount of antibody which initially binds to the antigen fixed to the bead. The preferred recombinant polypeptides having HCV antigenic epitopes were selected from portions of the HCV genome which encoded polypeptides which possessed amino acid sequences similar to other known immunologically reactive agents and which were identified as having some immunological reactivity. (The immunological reactivity of a polypeptide was initially identified by reacting the cellular extract of E. coli clones which had been transformed with cDNA fragments of the HCV genome with HCV infected serum. Polypeptides expressed by clone containing the incorporated cDNA were immunologically reactive with serum known to contain antibody to HCV antigens.) An analysis of a given amino acid sequence, however, only provides rough guides to predicting immunological reactivity. There is no invariably predictable way to ensure immunological activity short of preparing a given amino acid sequence and testing the suspected sequence in an assay. The use of recombinant polypeptides representing distinct antigenic regions of the HCV genome to detect the presence of an antibody to an HCV antigen is illustrated in Figure 2. The course of HCV infection in the chimpanzee, Pan, was followed with one assay using recombinant dOO-3 polypeptide and with another improved assay, using the two recombinant antigens CKS-Core (pHCV-34) (SEQ.ID.NO.22 and 23) and pHCV-33c-BCD (pHCV-31) (SEQ.ID.NO. 24 and 25) expressed by the plasmids pHCV-34 and pHCV-31 , respectively. The assay utilizing the recombinant pHCV-34 and pHCV-31 proteins detected plasma antibody three weeks prior to detection of antibody by the assay using c100-3. A summary of the results of a study which followed the course of HCV infection in Pan and six other chimpanzees using the two assays described above is summarized in Figure 3. Both assays gave negative results before inoculation and both assays detected the presence of antibodies after the animal had been infected with HCV. However, in the comparison of the two assays, the improved screening assay using pHCV-34 and pHCV-31 detected seroconversion to HCV antigens at an earlier or equivalent bleed date in six of the seven chimpanzees. Data from these chimpanzee studies clearly demonstrate that overall detection of HCV antibodies is greatly increased with the assay utilizing the pHCV-34 and pHCV-31 proteins. This test is sufficiently sensitive to detect seroconversion during the acute phase of this disease, as defined as an elevation in ALT levels, in most animals. Equally important is the high degree of specificity of the test as no pre-inoculation specimens were reactive. The polypeptides useful in the practice of this invention are produced using recombinant technologies. The DNA sequences which encode the desired polypeptides are preferably assembled from fragments of the total desired sequence. Synthetic DNA fragments of the HCV genome can be synthesized based on their corresponding amino acid sequences. Once the amino acid sequence is chosen, this is then reverse translated to determine the complementary DNA sequence using codons optimized to facilitate expression in the chosen system. The fragments are generally prepared using well known automated processes and apparatus. After the complete sequence has been prepared the desired sequence is incorporated into an expression vector which is transformed into a host cell. The DNA sequence is then expressed by the host cell to give the desired polypeptide which is harvested from the host cell or from the medium in which the host cell is cultured. When smaller peptides are to be made using recombinant technologies it may be advantageous to prepare a single DNA sequence which encodes several copies of the desired polypeptide in a connected chain. The long chain is then isolated and the chain is cleaved into the shorter, desired sequences. The methodology of polymerase chain reaction (PCR) may also be employed to develop PCR amplified genes from any portion of the HCV genome, which in turn may then be cloned and expressed in a manner similar to the synthetic genes. Vector systems which can be used include plant, bacterial, yeast, insect, and mammalian expression systems. It is preferred that the codons are optimized for expression in the system used. A preferred expression system utilizes a carrier gene for a fusion system where the recombinant HCV proteins are expressed as a fusion protein of an E. coli enzyme, CKS (CTP:CMP-3-deoxy-manno-octulosonate cytidylyl transferase or CMP-KDO synthetase). The CKS method of protein synthesis is disclosed in U.S. Patent Applications Serial Nos. 167,067 and 276,263 filed March 11 , 1988 and November 23, 1988, respectively, by Boiling (EPO 891029282) which enjoy common ownership and are incorporated herein by reference. Other expression systems may be utilized including the lambda PL vector system whose features include a strong lambda pL promoter, a strong three-frame translation terminator rrnBtl, and translation starting at an ATG codon. In the present invention, the amino acid sequences encoding for the recombinant HCV antigens of interest were reverse translated using codons optimized to facilitate high level expression in E. coli. Individual oligonucleotides were synthesized by the method of oligonucleotide directed double-stranded break repair disclosed in U.S. Patent Application Serial No. 883,242, filed July 8, 1986 by Mandecki (EPO 87109357.1) which enjoys common ownership and is incorporated herein by reference. Alternatively, the individual oligonucleotides may be synthesized on the Applied Biosystem 380A DNA synthesizer using methods and reagents recommended by the manufacturer. The DNA sequences of the individual oligonucleotides were confirmed using the Sanger dideoxy chain termination method (Sanger et al., J. Mole. Biol.. 162:729 (1982)). These individual gene fragments were then annealed and ligated together and cloned as EcoRI-BamHI subfragments in the CKS fusion vector pJO200. After subsequent DNA sequence confirmation by the Sanger dideoxy chain termination method, the subfragments were digested with appropriate restriction enzymes, gel purified, ligated and cloned again as an EcoRI-BamHI fragment in the CKS fusion vector pJ0200. The resulting clones were mapped to identify a hybrid gene consisting of the EcoRI-BamHI HCV fragment inserted at the 3' end of the CKS (CMP-KDO synthetase) gene. The resultant fusion proteins, under control of the lac promoter, consist of 239 amino acids of the CKS protein fused to the various regions of HCV. The synthesis, cloning, and characterization of the recombinant polypeptides as well as the preferred formats for assays using these polypeptides are provided in the following examples. Examples 1 and 2 describe the synthesis and cloning of CKS-Core and CKS-33-BCD, respectively. Example 3 describes a screening assay. Example 4 describes a confirmatory assay. Example 5 describes a competition assay. Example 6 describes an immunodot assay. Example 7 describes the synthesis and cloning of HCV CKS-NS5E, CKS-NS5F, CKS-NS5G, CKS-NS5H and CKS-NS51. Example 8 describes the preparation of HCV CKS-C100 vectors. Example 9 describes the preparation of HCV PCR derived expression vectors. Example 10 describes the synthesis scheme, deletion analysis and production and characterization of recombinant antigen HCV pHCV-202, pHCV-204 and pHCV- 205. REAGENTS AND ENZYMES Media such as Luria-Bertani (LB) and Superbroth II (Dri Form) were obtained from Gibco Laboratories Life Technologies, Inc., Madison Wisconsin. Restriction enzymes, Klenow fragment of DNA polymerase I, T4 DNA ligase, T4 polynucleotide kinase, nucleic acid molecular weight standards, M13 sequencing system, X-gal (5-bromo-4-chloro-3-indonyl-β-D-galactoside), IPTG (isopropyl-β-D-thiogalactoside), glycerol, Dithiothreitol, 4-chloro-1 -naphthol were purchased from Boehriπger Mannheim Biochemicals, Indianapolis, Indiana; or New England Biolabs, Inc., Beverly, Massachusetts; or Bethesda Research Laboratories Life Technologies, Inc., Gaithersburg, Maryland. Prestained protein molecular weight standards, acrylamide (crystallized, electrophoretic grade >99%); N-N'-Methylene-bis-acrylamide (BIS); N.N.N'.N',- Tetramethylethylenediamine (TEMED) and sodium dodecylsulfate (SDS) were purchased from BioRad Laboratories, Richmond, California. Lysozyme and ampicillin were obtained from Sigma Chemical Co., St. Louis, Missouri. Horseradish peroxidase (HRPO) labeled secondary antibodies were obtained from Kirkegaard & Perry Laboratories, Inc., Gaithersburg, Maryland. Seaplaque® agarose (low melting agarose) was purchased from FMC Bioproducts, Rockland, Maine. T50E10 contained 50mM Tris, pH 8.0, lOmM EDTA; 1X TG contained 1OOmM Tris, pH 7.5 and 10% glycerol; 2X SDS/PAGE loading buffer consisted of 15% glycerol, 5% SDS, lOOmM Tris base, 1 M β-mercaptoethanol and 0.8% Bromophenol blue dye; TBS container 50 mM Tris, pH 8.0, and 150 mM sodium chloride; Blocking solution consisted of 5% Carnation nonfat dry milk in TBS. HOST CE L CULTURES, P SOURCE? ANP VECTOR? E. coli JM103 cells, pUC8, pUC18, pUC19 and M13 cloning vectors were purchased from Pharmacia LKB Biotechnology, Inc., Piscataway, New Jersey; Competent Epicurean™ coli stains XL1-Blue and JM109 were purchased from Stratagene Cloning Systems, LaJolla, California. RR1 cells were obtained from Coli Genetic Stock Center, Yale University, New Haven, Connecticut; and E. coli CAG456 cells from Dr. Carol Gross, University of Wisconsin, Madison, Wisconsin. Vector pRK248.clts was obtained from Dr. Donald R. Helinski, University of California, San Diego, California. GENERAL METHODS All restriction enzyme digestion were performed according to suppliers' instructions. At least 5 units of enzyme were used per microgram of DNA, and sufficient incubation was allowed to complete digestion of DNA. Standard procedures were used for minicell lysate DNA preparation, phenol-chloroform extraction, ethanol precipitation of DNA, restriction analysis of DNA on agarose, and low melting agarose gel purification of DNA fragments (Maniatis et al., Molecular Cloning. A Laboratory Manual [New York: Cold Spring Harbor, 1982]). Plasmid isolations from E. coli strains used the alkali lysis procedure and cesium chloride- ethidium bromide density gradient method (Maniatis et al., supra). Standard buffers were used for T4 DNA ligase and T4 polynucleotide kinase (Maniatis et al., supra)- EXAMPLE 1. CKS-CORE A. Construction of the Plasmid pJ0200 The cloning vector pJO200 allows the fusion of recombinant proteins to the CKS protein. The plasmid consists of the plasmid pBR322 with a modified lac promoter fused to a KdsB gene fragment (encoding the first 239 of the entire 248 ammo acids of the E coli CMP-KDO synthetase of CKS protein), and a synthetic linker fused to the end of the KdsB gene fragment. The cloning vector pJO200 is a modification of vector pTB210 The synthetic linker includes: multiple restriction sites for insertion of genes; translational stop signals, and the trpA rho- independent transcπptional terminator The CKS method of protein synthesis as well as CKS vectors including pTB210 are disclosed in U.S. Patent Application Serial Nos. 167,067 and 276,263, filed March 1 1 , 1988 and November 23, 1988, respectively, by Boiling (EPO 891029282) which enjoy common ownership, and are herein incorporated by reference. B Preparation of HCV CKS-Core Expression Vector Six individual nucleotides representing ammo acids 1 -150 of the HCV genome were ligated together and cloned as a 466 base pair EcoRI-BamHI fragment into the CKS fusion vector pJO200 as presented in Figure 4. The complete DNA sequence of this plasmid, designated pHCV-34, and the entire ammo acid sequence of the pHCV-34 recombinant antigen produced is presented in SEQ.ID.NO. 22 and 23. The resultant fusion protein HCV CKS-Core, consists of 239 ammo acids of CKS, seven ammo acids contributed by linker DNA sequences, and the first 150 amino acids of HCV as illustrated in Figure 5. The pHCV-34 plasmid and the CKS plasmid pTB210 were transformed into E. coli K-12 strain xL-l (recAI, endAI, gyrA96, thι-1 , hsdRl7, supE44, relAI, lac/F', proAB, laclqZDM15, TN10) cells made competent by the calcium chloride method. In these constructions the expression of the CKS fusion proteins was under the control of the lac promoter and was induced by the addition of IPTG. These plasmids replicated as independent elements, were nonmobilizable and were maintained at approximately 10-30 copies per ceil. C Characterization of Recombinant HCV-Core In order to establish that clone pHCV-34 expressed the unique HCV-CKS Core protein, the pHCV-34/XL-1 culture was grown overnight at 37°C in growth media consisting of yeast extract, trytone, phosphate salts, glucose, and ampicillin. When the culture reached an OD600 of 1.0, IPTG was added to a final concentration of 1 mM to induce expression Samples (1.5 ml) were removed at 1 hour intervals, and cells were pelleted and resuspended to an OD600 of 1.0 in 2X SDS/PAGE loading buffer. Aliquots (15ul) of the prepared samples were separated on duplicate 12.5% SDS/PAGE gels One gel was fixed in a solution of 50% methanol and 10% acetic acid for 20 minutes at room temperature, and then stained with 0.25% Coomassie blue dye in a solution of 50% methanol and 10% acetic acid for 30 minutes. Des taining was carried out using a solution of 10% methanol and 7% acetic acid for 3-4 hours, or until a clear background was obtained. Figure 6 presents the expression of pHCV-34 proteins in E. coli. Molecular weight standards were run in Lane M. Lane 1 contains the plasmid pJ0200-the CKS vector without the HCV sequence. The arrows on the left indicate the mobilities of the molecular weight markers from top to bottom: 110,000; 84,000; 47,000; 33,000; 24,000; and 16,000 daltons. The arrows on the right indicate the mobilities of the recombinant HCV proteins. Lane 2 contains the E. coli lysate containing pHCV-34 expressing CKS-Core (amino acids 1 to 150) prior to induction; and Lane 3 after 3 hours of induction. The results show that the recombinant protein pHCV-34 has an apparent mobility corresponding to a molecular size of 48,000 daltons. This compares acceptably with the predicted molecular mass of 43,750 daltons. Proteins from the second 12.5% SDS/PAGE gel were electrophoretically transferred to nitrocellulose for immunoblotting. The nitrocellulose sheet containing the transferred proteins was incubated with Blocking Solution for one hour and incubated overnight at 4°C with HCV patients' sera diluted in TBS containing E. coli K-12 strain XL-I lysate. The nitrocellulose sheet was washed three times in TBS, then incubated with HRPO-labeled goat anti-human IgG, diluted in TBS containing 10% fetal calf sera. The nitrocellulose was washed three times with TBS and the color was developed in TBS containing 2 mg/ml 4-chloro-1- napthol, 0.02% hydrogen peroxide and 17% methanol. Clone HCV-34 demonstrated a strong immunoreactive band at 48,000 daltons with the HCV patients' sera. Thus, the major protein in the Coomassie stained protein gel was immunoreactive. Normal human serum did not react with any component of pHCV-34. EXAMPLE 2. HCV CKS-33C-BCD A. Preparation of HCV CKS-33c-BCD Expression Vector The construction of this recombinant clone expressing the HCV CKS-33-BCD antigen was carried out in three steps described below. First, a clone expressing the HCV CKS-BCD antigen was constructed, designated pHCV-23. Second, a clone expressing the HCV CKS-33 antigen was constructed, designated pHCV-29. Lastly, the HCV BCD region was excised from pHCV-23 and inserted into pHCV-29 to construct a clone expressing the HCV CKS-33-BCD antigen, designated pHCV-31. To construct the plasmid pHCV-23, thirteen individual oligonucleotides representing amino acids 1676-1931 of the HCV genome were ligated together and cloned as three separate EcoRI-BamHI subfragments into the CKS fusion vector pJO200. After subsequent DNA sequence confirmation, the three subfragments, designated B, C, and D respectively, were digested with the appropriate restriction enzymes, gel purified, ligated together, and cloned as a 781 base pair EcoRI-BamHI fragment in the CKS fusion vector pJO200, as illustrated in Figure 7. The resulting plasmid, designated pHCV-23, expresses the HCV CKS-BCD antigen under control of the lac promoter. The HCV CKS-BCD antigen consists of 239 amino acids of CKS, seven amino acids contributed by linker DNA sequences, 256 amino acids from the HCV NS4 region (amino acids 1676-1931 , and 10 additional amino acids contributed by linker DNA sequences. To construct the plasmid pHCV-29 twelve individual oligonucleotides representing amino acids 1192-1457 of the HCV genome were ligated together and cloned as two separate EcoRI-BamHI subfragments in the CKS fusion vector pJO200. After subsequent DNA sequence confirmation, the two subfragments were digested with the appropriate restriction enzymes, gel purified, ligated together and cloned again as an 816 base pair EcoRI-BamHI fragment in the CKS fusion vector pJO200, as illustrated in Figure 8. The resulting plasmid, designated pHCV-29, expresses the CKS-33 antigen under control of the lac promoter. The HCV CKS-33 antigen consists of 239 amino acids of CKS, eight amino acids contributed by linker DNA sequences, and 266 amino acids from the HCV NS3 region (amino acids 1192- 1 457) . To construct the plasmid pHCV-31 , the 781 base pair EcoRI-BamHI fragment from pHCV-23 representing the HCV-BCD region was linker-adapted to produce a Cla1-BamH1 fragment which was then gel purified and ligated into pHCV- 29 at the Cla1-BamH1 sites as illustrated in Figure 9. The resulting plasmid, designated pHCV-31 , expresses the pHCV-31 antigen under control of the lac promoter. The complete DNA sequence of pHCV-31 and the entire amino acid sequence of the HCV CKS-33-BCD recombinant antigen produced is presented in SEQ.ID.NO. 24 and 25. The HCV CKS-33-BCD antigen consists of 239 amino acids of CKS, eight amino acids contributed by linker DNA sequences, 266 amino acids of the HCV NS3 region (amino acids 1 192-1457), 2 amino acids contributed by linker DNA sequences, 256 amino acids of the HCV NS4 region (amino acids 1676-1931), and 10 additional amino acids contributed by linker DNA sequences. Figure 10 presents a schematic representation of the pHCV-31 antigen. The pHCV-31 plasmid was transformed into E. coli K-12 strain XL-I in a manner similar to the pHCV-34 and CKS-pTB210 plasmids of Example 1. B. Characterization of Recombinant HCV CKS-33-BCD Characterization of pHCV CKS-33-BCD was carried out in a manner similar to pHCV CKS-Core of Example 1. pHCV-23, pHCV SDS/PAGE gels were run for E^ coli lysates containing the plasmids pHCV-29 (Figure 11), pHCV-23 (Figure 12), and pHCV-31 (Figure 13) expressing the recombinant fusion proteins CKS-33c, CKS-BCD, and CKS-33-BCD, respectively. For all three figures, molecular weight standards were run in Lane M, with the arrows on the left indicating mobilities of the molecular weight markers the from top to bottom: 1 10,000; 84,000; 47,000; 33,000; 24,000; and 16,000 daltons. In Figure 11 , Lane 1 contained the E. coli lysate containing pHCV-29 expressing HCV CKS-33C (amino acids 1192 to 1457) prior to induction and lane 2 after 4 hours induction. These results show that the recombinant pHCV-29 fusion protein has an apparent mobility corresponding to a molecular size of 60,000 daltons. This compares acceptably to the predicted molecular mass of 54,911. In Figure 12, Lane 1 contained the E. coli lysate containing pJO200- the CKS vector without the HCV sequence. Lane 2, contained pHCV-20 expressing the HCV CKS-B (amino acids 1676 to 1790). Lane 3, contained the fusion protein pHCV-23 (amino acids 1676-1931 ). These results show that the recombinant pHCV-23 fusion protein has an apparent mobility corresponding to a molecular size of 55,000 daltons. This compares acceptably to the predicted molecular mass of 55,070 daltons. In Figure 13, Lane 1 contained the E. coli lysate containing pJO200 the CKS vector without the HCV sequences. Lane 2 contained pHCV-31 expressing the CKS- 33C-BCD fusion protein (amino acids 1192 to 1447 and 1676 to 1931) prior to induction and lane 3 after 2 hours induction. These results show that the recombinant pHCV-31 (CKS-33c-BCD) fusion protein has an apparent mobility corresponding to a molecular size of 90,000 daltons. This compares acceptably to the predicted molecular mass of 82,995 daltons. An immunoblot was also run on one of the SDS/PAGE gels derived from the pHCV-31/X1-1 culture. Human serum from an HCV exposed individual reacted strongly with the major pHCV-31 band at 90,000 daltons. Normal human serum did not react with any component of the pHCV-31 (CKS-33-BCD) preparations. EXAMPLE 3. SCREENING ASSAY The use of recombinant polypeptides which contain epitopes within cl00-3 as well as epitopes from other antigenic regions from the HCV genome, provide immunological assays which have increased sensitivity and may be more specific than HCV immunological assays using epitopes within c100-3 alone. In the presently preferred screening assay, the procedure uses two E. coli expressed recombinant proteins, CKS-Core (pHCV-34) and CKS-33-BCD (pHCV- 31), representing three distinct regions of the HCV genome. These recombinant polypeptides were prepared following procedures described above. In the screening assay, both recombinant antigens are coated onto the same polystyrene bead. In a modification of the screening assay the polystyrene bead may also be coated with the SOD-fusion polypeptide c100-3. The polystyrene beads are first washed with distilled water and propanol and then incubated with a solution containing recombinant pHCV-31 diluted to 0.5 to 2.0 ug/ml and pHCV-34 diluted to 0.1 to 0.5 ug/ml in 0.1 M NaH2Pθ4.H20 with 0.4M NaCl and 0.0022% Triton X-100, pH 6.5. The beads are incubated in the antigen solution for 2 hours (plus or minus 10 minutes) at 38-42°C, washed in PBS and soaked in 0.1% (w/v) Triton X-100 in PBS for 60 minutes at 38-42°C. The beads are then washed two times in phosphate buffered saline (PBS), overcoated with a solution of 5.0% (w/v) bovine serum albumin (BSA) in PBS for 60 minutes at 38-42°C and washed one time in PBS. Finally, the beads are overcoated with 5% (w/v) sucrose in PBS, and dried under nitrogen or air. The polystyrene beads coated with pHCV-31 and pHCV-34 are used in an antibody capture format. Ten microliters of sample are added to the wells of the reaction tray along with 400 ul of a sample diluent and the recombinant coated bead. The sample diluent consists of 10% (v/v) bovine serum and 20% (v/v) goat serum in 20 mM Tris phosphate buffer containing 0.15% (v/v) Triton X-100, 1%(w/v) BSA, 1% E. coli lysate and 500 ug/ml or less CKS lysate. When the recombinant yeast d 00-3 polypeptide is used, antibodies to yeast antigens which may be present in a sample are reacted with yeast extracts which are added to the sample diluent (typically about 200 ug/ml). The addition of yeast extracts to the sample diluent is used to prevent false positive results. The final material is sterile filtered and filled in plastic bottles, and preserved with 0.1 % sodium azide. After one hour of incubation at 40°C, the beads are washed and 200 ul of conjugate is added to the wells of the reaction tray. The preferred conjugate is goat anti-human IgG horseradish peroxidase conjugate. Concentrated conjugate is titered to determine a working concentration. A twenty-fold concentrate of the working conjugate solution is then prepared by diluting the concentrate in diluent. The 20X concentrate is sterile filtered and stored in plastic bottles. The conjugate diluent includes 10% (v/v) bovine serum, 10% (v/v) goat serum and 0.15% Triton-X100 in 20 mM Tris buffer, pH 7.5 with 0.01% gentamicin sulfate, 0.01% thimerosal and red dye. The conjugate is sterile filtered and filled in plastic bottles. Anti-HCV positive control is prepared from plasma units positive for antibodies to HCV. The pool of units used includes plasma with antibodies reactive to pHCV-31 and pHCV-34. The units are recalcified and heat inactivated at 59-61 °C for 12 hours with constant stirring. The pool is aliquoted and stored at -20°C of at 2-8°C. For each lot of positive control, the stock solution is diluted with negative control containing 0.1% sodium azide as a preservative. The final material is sterile filtered and filled in plastic bottles. Anti-HCV negative control is prepared from recalcified human plasma, negative for antibodies to pHCV-31 and pHCV-34 proteins of HCV. The plasma is also negative for antibodies to human immunodeficiency virus (HIV) and negative for hepatitis B surface antigen (HBsAg). The units are pooled, and 0.1% sodium azide is added as a preservative. The final material is sterile filtered and filled in plastic bottles. After one hour of incubation with the conjugate at 40°C, the beads are washed, exposed to the OPD substrate for thirty minutes at room temperature and the reaction terminated by the addition of 1 N H2SO4. The absorbance is read at 492 nm. In order to maintain acceptable specificity, the cutoff for the assay should be at least 5-7 standard deviations above the absorbance value of the normal population mean. In addition, it has generally been observed that acceptable specificity is obtained when the population mean runs at a sample to cutoff (S/CO) value of 0.25 or less. Consistent with these criteria, a "preclinical" cutoff for the screening assay was selected which clearly separated most of the presumed "true negative" from "true positive" specimens. The cutoff value was calculated as the sum of the positive control mean absorbance value multiplied by 0.25 and the negative control mean absorbance value. The cutoff may be expressed algebraically as: Cutoff value=0.25 PCx + NCx. Testing may be performed by two methods which differ primarily in the degree of automation and the mechanism for reading the resulting color development in the assay. One method is referred to as the manual or Quantum™ method because Quantum or Quantumatic is used to read absorbance at 492 nm. It is also called the manual method because sample pipetting, washing and reagent additions are generally done manually by the technician, using appropriately calibrated pipettes, dispensers and wash instruments. The second method is referred to as the PPC method and utilizes the automated Abbott Commander® system. This system employs a pipetting device referred to as the Sample Management Center (SMC) and a wash/dispense/read device referred to as the Parallel Processing Center (PPC) disclosed in the EPO Publication No. 91114072.1. The optical reader used in the PPC has dual wavelength capabilities that can measure differential absorbeπcies (peak band and side band) from the sample wells. These readings are converted ' into results by the processor's Control Center. Screening Assay Performance 1. Serum/Plasma From Inoculated Chimpanzees As previously described, Table I summarizes the results of a study which followed the course of HCV infection in seven chimpanzees using a screening assay which utilized the c100-3 polypeptide, and the screening assay which utilized pHCV-31 and pHCV-34. Both assays gave negative results before inoculation and both assays detected the presence of antibodies after the animal had been infected with HCV. However, in the comparison of the two assays, the assay utilizing pHCV- 31 and pHCV-34 detected seroconversion to HCV antigens at an earlier or equivalent bleed date in six of the seven chimpanzees. Data from these chimpanzee studies clearly demonstrate that overall detection of HCV antibodies is greatly increased with the assay utilizing the pHCV-31 and pHCV-34 proteins. This test is sufficiently sensitive to detect seroconversion during the acute phase of this disease, as defined as an elevation in ALT levels, in most animals. Equally important is the high degree of specificity of the test as no pre-inoculation specimens were reactive. 2. Non-A. Non-B Panel II (H. Alter. NIH. A panel of highly pedigreed human sera from Dr. H. Alter, NIH, Bethesda, MD., containing infectious HCV sera, negative sera and other disease controls were tested. A total of 44 specimens were present in the panel. Six of seven sera which were "proven infectious" in chimpanzees were positive in both the screening assay using c100-3 as well as in the screening assay utilizing the recombinant proteins pHCV-31 and pHCV-34. These six reactive specimens were obtained from individuals with chronic hepatitis. All six of the reactive specimens were confirmed positive using synthetic peptide sp67. One specimen obtained during the acute phase of NANB post-transfusion hepatitis was non-reactive in both screening assays. In the group labeled "probable infectious" were three samples taken from the same post transfusion hepatitis patient. The first two acute phase samples were negative in both assays, but the third sample was reactive in both assay. The disease control samples and pedigreed negative controls were uniformly negative. All sixteen specimens detected as positive by both screening assays were confirmed by the spll7 confirmatory assay (Figure 14). In addition, specimens 10 and 29 were newly detected in the screening assay utilizing the recombinant pHCV- 31 and pHCV-34 antigens and were reactive by the sp75 confirmatory assay. Specimen 39 was initially reactive in the screening test utilizing pHCV-34 and pHCV-31 , but upon retesting was negative and could not be confirmed by the confirmatory assays. In summary, both screening tests identified 6 of 6 chronic NANBH carriers and 1 of 4 acute NANBH samples. Paired specimens from an implicated donor were non-reactive in the screening test utilizing c100-3 but were reactive in the screening test with pHCV-31 and pHCV-34. Thus, the screening test utilizing the recombinant antigens pHCV-31 and pHCV-34 appears to be more sensitive than the screening assay utilizing c100-3. None of the disease control specimens or pedigreed negative control specimens were reactive in either screening assay. 3. CBER Reference Panel A reference panel for antibody to Hepatitis C was received from the Center for Biologies Evaluation and Research (CBER). This 10 member panel consists of eight reactive samples diluted in normal human sera negative for antibody to HCV and two sera that contain no detectable antibody to HCV. This panel was run on the Ortho first generation HCV EIA assay, the screening assay utilizing c100-3 and the screening assay utilizing pHCV-31 and pHCV-34. The assay results are presented in Figure 15. The screening assay utilizing pHCV-31 and pHCV-34 detected all six of the HCV positive or borderline sample dilutions. The two non-reactive sample dilutions (709 and 710) appear to be diluted well beyond endpoint of antibody detectability for both screening assays. A marked increase was observed in the sample to cutoff values for three of the members on the screening assay utilizing pHCV-31 and pHCV-34 compared to the screening assay utilizing c100-3 or the Ortho first generation test. All repeatably reactive specimens were confirmed. EXAMPLE 4. CONFIRMATORY ASSAY The confirmatory assay provides a means for unequivocally identifying the presence of an antibody that is immunologically reactive with an HCV antigen. The confirmatory assay includes synthetic peptides or recombinant antigens representing major epitopes contained within the three distinct regions of the HCV genome, which are the same regions represented by the two recombinant antigens described in the screening assay. Recombinant proteins used in the confirmatory assay should have a heterologous source of antigen to that used in the primary screening assay (i.e. should not be an E. coli-derived recombinant antigen nor a recombinant antigen composed in part, of CKS sequences). Specimens repeatedly reactive in the primary screening assay are retested in the confirmatory assay. Aliquots containing identical amounts of specimen are contacted with a synthetic peptide or recombinant antigen individually coated onto a polystyrene bead. Seroreactivity for epitopes within the c100-3 region of the HCV genome are confirmed by use of the synthetic peptides sp67 and sp65. The synthetic peptide sp117 can also be used to confirm seroreactivity with the c100-3 region. Seroreactivity for HCV epitopes within the putative core region of HCV are confirmed by the use of the synthetic peptide sp75. In order to confirm seroreactivity for HCV epitopes within the 33c region of HCV, a recombinant antigen expressed as a chimeric protein with superoxide dismutase (SOD) in yeast is used. Finally, the antibody-antigen complex is detected. The assay protocols were similar to those described in Example 3 above. The peptides are each individually coated onto polystyrene beads and used in an antibody capture format similar to that described for the screening assay. Ten microliters of specimen are added to the wells of a reaction tray along with 400 ul of a specimen diluent and a peptide coated bead. After one hour of incubation at 40°C, the beads are washed and 200 ul of conjugate (identical to that described in Example 3) is added to the wells of the reaction tray. After one hour of incubation at 40°C, the beads are washed, exposed to the OPD substrate for 30 minutes at room temperature and the reaction terminated by the addition of 1 N H2SO4. The absorbance is read at 492 nm. The cutoff value for the peptide assay is 4 times the mean of the negative control absorbance value. 1. Panels containing Specimens "At Risk" for HCV Infection. A group of 233 specimens representing 23 hemodialysis patients all with clinically diagnosed NANBH were supplied by Gary Gitnick, M.D. at the University of California, Los Angeles Center for the Health Sciences. These samples which were tested in by the screening assay utilizing c100-3 were subsequently tested in the screening assay which uses pHCV-31 and pHCV-34. A total of 7/23 patients (30.44%) were reactive in the c100-3 screening assay, with a total of 36 repeat reactive specimens. Ten of 23 patients (43.48%) were reactive by the screening assay utilizing pHCV-31 and pHCV-34, with a total of 70 repeatable reactives among the available specimens (Figure 16). Two specimens were unavailable for testing. All of the 36 repeatedly reactive specimens detected in the c100-3 screening assay were confirmed by synthetic peptide confirmatory assays. A total of 34 of these 36 were repeatedly reactive on HCV EIA utilizing pHCV-34 and pHCV-31 : two specimens were not available for testing. Of the 36 specimens additionally detected by the screening assay utilizing pHCV-34 and pHCV-31 , 9 were confirmed by the core peptide confirmatory assay (sp75) and 27 were confirmed by the SOD-33c confirmatory assay. In summary these data indicate that detection of anti-HCV by the screening assay utilizing pHCV-31 and pHCV-34 may occur at an equivalent bleed date or as many as 9 months earlier, when compared to the d 00-3 screening assay. Figure 17 depicts earlier detection by the screening assay utilizing pHCV-34 and pHCV-31 in a hemodialysis patient. 5. Acute/Chronic Non-A. Non-B Hepatitis A population of specimens was identified from individuals diagnosed as having acute or chronic NANBH. Specimens from individuals with acute cases of NANBH were received from Gary Gitnick, M.D. at the University of California, Los Angeles Center for Health Sciences. The diagnosis of acute hepatitis was based on the presence of a cytolytic syndrome (ALT levels greater than 2X the upper normal limit) on at least 2 serum samples for a duration of less than 6 months with or without other biological abnormalities and clinical symptoms. All specimens were also negative for IgM antibodies to Hepatitis A Virus (HAV) and were negative for Hepatitis B surface Ag when tested with commercially available tests. Specimens from cases of chronic NANBH were obtained from two clinical sites. Individuals were diagnosed as having chronic NANBH based on the following criteria: persistently elevated ALT levels, liver biopsy results, and/or the absence of detectable HBsAg. Specimens with biopsy results were further categorized as either chronic active NANBH, chronic persistent NANBH, or chronic NANBH with cirrhosis. These specimens were tested by both the c100-3 screening assay and the screening assay utilizing pHCV-34 and pHCV-31. The latter testing was performed in replicates of two by both the Quantum and PPC methods. Community Acquired NANBH .Acute. The d OO-3 screening assay detected 2 of 10 specimens (20.00%) as repeatedly reactive, both of which were confirmed. The screening assay utilizing pHCV-34 and pHCV-31 detected both of these specimens plus and additional 2 specimens (Figure 18). These 2 specimens were confirmed by sp75 (see Figure 1 9) . Acute Post-Transfusion NANBH The dOO-3 assay detected 4 of 32 specimens (12.50%) as repeatedly reactive, all of which was confirmed. The screening assay utilizing pHCV-34 and pHCV-31 detected 3 out of these 4 specimens (75%) as reactive. The one sample that was missed had an S/CO of 0.95 by the latter screening test. This sample was confirmed by the sp67 peptide (Figure 18). In addition, the screening assay utilizing pHCV-34 and pHCV-31 detected 11 specimens not reactive in the d OO-3 screening assay. Of the 9 specimens available for confirmation, 8 were confirmed by sp75 and 1 could not be confirmed but had an S/CO of 0.90 in the sp65 confirmatory test, (see Figure 19). Chronic NANBH A summary of the results on these populations is shown in Figure 24. Overall, 155 of 164 (94.5%) chronic NANBH samples were detected by the screening test utilizing pHCV-31 and pHCV-34 using either Quantum or PPC. The 155 reactive samples were all confirmed in alternate assays using synthetic peptides based on sequences from either the clOO, 33c or core regions of the HCV genome. In contrast, only 138 of 164 (84.1%) specimens were positive by the clOO-3 assay. All but one of the 138 c100-3 samples were detected as positive by the screening assay utilizing pHCV-31 and pHCV-34. The one discordant specimen was not confirmed by either synthetic or neutralization assays. Conversely, there were 17 confirmed specimens which were positive only by the screening assay utilizing pHCV-34 and pHCV-31 . The results indicate that the screening assay utilizing pHCV-34 and pHCV- 31 is more sensitive than the current test in detecting HCV positive individuals within chronically infected NANBH populations. EXAMPLE 5. COMPETITION ASSAY The recombinant polypeptides containing antigenic HCV epitopes are useful for competition assays. To perform a neutralization assay, a recombinant polypeptide representing epitopes within the c100-3 region such as CKS-BCD (pHCV-23) is solubilized and mixed with a sample diluent to a final concentration of 0.5-50 ug/ml. Ten microliters of specimen or diluted specimen is added to a reaction well followed by 400 ul of the sample diluent containing the recombinant polypeptide and if desired, the mixture may be preincubated for about fifteen minutes to two hours. A bead coated with c100-3 antigen is then added to the reaction well and incubated for one hour at 40°C. After washing, 200 ul of a peroxidase labeled goat anti-human IgG in conjugate diluent is added and incubated for one hour at 40°C. After washing, OPD substrate is added and incubated at room temperature for thirty minutes. The reaction is terminated by the addition of 1 N sulfuric acid and the absorbance read at 492 nm. Samples containing antibodies to the d 00-3 antigen generate a reduced signal caused by the competitive binding of the peptides to these antibodies in solution. The percentage of competitive binding may be calculated by comparing the absorbance value of the sample in the presence of a recombinant polypeptide to the absorbance value of the sample assayed in the absence of a recombinant polypeptide at the same dilution. EXAMPLE 6. IMMUNODOT ASSAY The immunodot assay system uses a panel of purified recombinant polypeptides placed in an array on a nitrocellulose solid support. The prepared solid support is contacted with a sample and captures specific antibodies to HCV antigens. The captured antibodies are detected by a conjugate-specific reaction. Preferably, the conjugate specific reaction is quantified using a reflectance optics assembly within an instrument which has been described in U.S. Patent Applications Serial No. 07/227,408 filed August 2, 1988. The related U.S. Patent Applications Serial Nos. 07/227,272, 07/227,586 and 07/227,590 further describe specific methods and apparatus useful to perform an immunodot assay. The assay has also been described in U.S. Application Serial No. 07/532,489 filed June 6, 1990. Briefly, a nitrocellulose-base test cartridge is treated with multiple antigenic polypeptides. Each polypeptide is contained within a specific reaction zone on the test cartridge. After all the antigenic polypeptides have been placed on the nitrocellulose, excess binding sites on the nitrocellulose are blocked. The test cartridge is then contacted with a sample such that each antigenic polypeptide in each reaction zone will react if the sample contains the appropriate antibody. After reaction, the test cartridge is washed and any antigen-antibody reactions are identified using suitable well known reagents. As described in the patent applications listed above, the entire process is amenable to automation. The specifications of these applications related to the method and apparatus for performing an immunodot assay are incorporated by reference herein. In a preferred immunodot assay, the recombinant polypeptides pHCV-23, pHCV-29, pHCV-34, and clOO-3 were diluted in the preferred buffers, pH conditions, and spotting concentrations as summarized in Figure 21 and applied to a preassembled nitrocellulose test cartridge. After drying the cartridge overnight at room temperature 37°C, the non-specific binding capacity of the nitro-cellulose phase was blocked. The blocking solution contained 1% porcine gelatin, 1% casein enzymatic hydrolysate, 5% Tween-20, 0.1% sodium azide, 0.5 M sodium chloride and 20 mM Tris, pH 7.5. Forty normal donors were assayed by following the method described above. The mean reflectance density value then was determined for each of the recombinant proteins. A cutoff value was calculated as the negative mean plus six standard deviations. Test cartridges were incubated with samples A00642 and 423 (see Figure 22). Sample A00642 was from a convalescent non-A, non-B hepatitis patient, diluted in negative human plasma from 1 :100 to 1 :12800. The other sample, 423, was from a paid plasma donor which tested positive in an assay using a recombinant c100-3 polypeptide, diluted in negative human plasma from 1 :40 to 1 :2560. After sample incubation, sequential incubations with a biotin-conjugated goat anti-human immunoglobulin-specific antibody, an alkaline phosphatase- conjugated rabbit anti-biotin specific antibody, and 5-bromo-4-chloro-3-indolyl phosphate produced a colored product at the site of the reaction. Sample to cutoff values (S/CO) were determined for all HCV recombinant proteins. Those S/CO values greater than or equal to 1.0 were considered reactive. The limiting dilution was defined as the lowest dilution at which the S/CO was greater than or equal to 1.0. As seen in Figure 22, each sample tested positive for all HCV recombinant proteins. The data demonstrate that reactivity for sample A00642 was greatest with pHCV-29, and decreased for the remaining antigens pHCV-23, c100-3, and pHCV-34. Sample 423 most strongly reacted with the recombinant proteins expressing pHCV-29 and pHCV-34, and to a lesser extent with pHCV-23 and c100- 3. EXAMPLE 7 HCV CKS-NS5 EΞXPRESSION VECTORS A. Preparation of HCV CKS-NS5E Eight individual oligonucleotides representing amino acids 1932-2191 of the HCV genome were ligated together and cloned as a 793 base pair EcoRI-BamHI fragment into the CKS fusion vector pJ0200. The resulting plasmid, designated pHCV-45, expresses the HCV CKS-NS5E antigen under control of the lac promoter. The HCV CKS-NS5E antigen consists of 239 amino acids of CKS, nine amino acids contributed by linker DNA sequences, and 260 amino acids from the HCV NS4/NS5 region (amino acids 1932-2191). Figure 23 presents a schematic representation of the recombinant antigen expressed by pHCV-45. SEQ.ID.NO. 26 and 27 presents the DNA and amino acid sequence of the HCV CKS-NS5E recombinant antigen produced by pHCV-45. Figure 27 presents the expression of pHCV-45 proteins in E. coli. Lane 1 contained the E. coli lysate containing pHCV-45 expressing the HCV CKS-NS5E antigen (amino acids 1932-2191) prior to induction and lanes 2 and 3 after 2 and 4 hours post induction, respectively. These results show that the pHCV- 45 fusion protein has an apparent mobility corresponding to a molecular size of 55,000 daltons. This compares acceptably to the predicted molecular mass of 57,597 daltons. B. Preparation of HCV CKS-NS5F Eleven individual oligonucleotides representing amino acids 2188-2481 of the HCV genome were ligated together and cloned as a 895 base pair EcoRI-BamHI fragment into the CKS fusion vector pJ0200. The resulting plasmid, designated pHCV-48, expresses the HCV CKS-NS5F antigen under control of the lac promoter. The HCV CKS-NS5F antigen consists of 239 amino acids of CKS, eight amino acids contributed by linker DNA sequences, and 294 amino acids from the HCV NS5 region (amino acids 2188-2481). Figure 25 presents a schematic representation of the recombinant antigen expressed by pHCV-48. SEQ.ID.NO. 28 and 29 presents the DNA and amino acid sequence of the HCV CKS-NS5F recombinant antigen produced by pHCV-48. Figure 26 presents the expression of pHCV-48 proteins in E. coli. Lane 1 contained the E. coli lysate containing pHCV-48 expressing the HCV CKS-NS5F antigen (amino acids 2188-2481) prior to induction and lanes 2 and 3 after 2 and 4 hours post induction, respectively. These results show that the pHCV-48 fusion protein has an apparent mobility corresponding to a molecular size of 65,000 daltons. This compares acceptably to the predicted molecular mass of 58,985 daltons. C. Preparation of HCV CKS-NS5G Seven individual oligonucleotides representing amino acids 2480-2729 of the HCV genome were ligated together and cloned as a 769 base pair EcoRI-BamHI fragment into the CKS fusion vector pJ0200. The resulting plasmid, designated pHCV-51 , expresses the HCV CKS-NS5G antigen under control of the lac promoter. The HCV CKS-NS5G antigen consists of 239 am o acids of CKS, eight ammo acids contributed by linker DNA sequences, and 250 ammo acids from the HCV NS5 region (ammo acids 2480-2729). Figure 27 presents a schematic representation of the recombinant antigen expressed by pHCV-51 SEQ.ID.NO. 30 and 31 presents the DNA and am o acid sequence of the HCV CKS-NS5G recombinant antigen produced by pHCV-51. Figure 28 presents the expression of pHCV-51 proteins in E. coli. Lane 1 contained the E. coli lysate containing pHCV-51 expressing the HCV CKS-NS5G antigen (ammo acids 2480-2729) prior to induction and lanes 2 and 3 after 2 and 4 hours post induction, respectively These results show that the pHCV-51 fusion protein has an apparent mobility corresponding to a molecular size of 55,000 daltons. This compares acceptably to the predicted molecular mass of 54,720 daltons P. Preparation of HCV CKS-NS5H Six individual oligonucleotides representing ammo acids 2728-2867 of the HCV genome were ligated together and cloned as a 439 base pair EcoRI-BamHI fragment into the CKS fusion vector pJ0200. The resulting plasmid, designated pHCV-50, expresses the HCV CKS-NS5H antigen under control of the lac promoter. The HCV CKS-NS5H antigen consists of 239 ammo acids of CKS, eight ammo acids contributed by linker DNA sequences, and 140 am o acids from the HCV NS5 region (ammo acids 2728-2867) Figure 29 presents a schematic representation of the recombinant antigen expressed by pHCV-50 SEQ. ID NO. 32 and 33 presents the DNA and ammo acid sequence of the HCV CKS-NS5H recombinant antigen produced by pHCV-50 Figure 30 presents the expression of pHCV-50 proteins in E. coli. Lane 1 contained the E. coli lysate containing pHCV-50 expressing the HCV CKS-NS5H antigen (ammo acids 2728-2867) prior to induction and lanes 2 and 3 after 2 and 4 hours post induction, respectively. These results show that the pHCV-50 fusion protein has an apparent mobility corresponding to a molecular size of 45,000 daltons. This compares acceptably to the predicted molecular mass of 42,783 daltons. E Preparation of HCV CKS-NS5I Six individual oligonucleotides representing ammo acids 2866-3011 of the HCV genome were ligated together and cloned as a 460 base pair EcoRI-BamHI fragment into the CKS fusion vector pJ0200 The resulting plasmid, designated pHCV-49, expresses the HCV CKS-NS5I antigen under control of the lac promoter. The HCV CKS-NS5I antigen consists of 239 amino acids of CKS, eight amino acids contributed by linker DNA sequences, and 146 amino acids from the HCV NS5 region (amino acids 2866-3011). Figure 31 presents a schematic representation of the recombinant antigen expressed by pHCV-49. SEQ.ID.NO. 34 and 35 presents the DNA and amino acid sequence of the HCV CKS-NS5I recombinant antigen produced by pHCV-49. Figure 32 presents the expression of pHCV-49 proteins in E. coli. Lane 1 contained the E. coli lysate containing pHCV-49 expressing HCV CKS-NS5I antigen (amino acids 2866-3011) prior to induction and lanes 2 and 3 after 2 and 4 hours post induction, respectively. These results show that the pHCV-49 fusion protein has an apparent mobility corresponding to a molecular size of 42,000 daltons. This compares acceptably to the predicted molecular mass of 43,497 daltons. F. Immunoblot of HCV CKS-NS5 Antigens Induced E. coli lysates containing pHCV-23, pHCV-45, pHCV-48, pHCV-51 , pHCV-50, or pHCV-49 were individually run on preparative SDS/PAGE gels to separate the various HCV CKS-NS5 or HCV CKS-BCD recombinant antigens assay from the majority of other E. coli proteins. Gel slices containing the separated individual HCV CKS-NS5 or HCV CKS-BCD recombinant antigens were then electropheretically transferred to nitrocellulose, and the nitrocellulose sheet cut into strips. Figure 33 presents the results of a Western Blot analysis of various serum or plasma samples using these nitrocellulose strips. The arrows on the right indicate the position of each HCV CKS-BCD or HCV CKS-NS5 recombinant antigen, from top to bottom pHCV-23 (HCV CKS-BCD), pHCV-45 (HCV CKS-NS5E), pHCV- 48 (HCV CKS-NS5F), pHCV-51 (HCV CKS-NS5G), pHCV-50 (HCV CKS-NS5H), pHCV-49 (HCV CKS-NS5I), and pJO200 (CKS). Panel A contained five normal human plasma, panel B contained five normal human sera, panel C contained twenty human sera positive in the Abbott HCV EIA test, panel D contained two mouse sera directed against CKS, and panel E contained two normal mouse sera. Both the HCV CKS-NS5E antigen expressed by pHCV-45 and the HCV CKS-NS5F antigen expressed by pHCV-48 were immunoreactive when screened with human serum samples containing HCV antibodies. EXAMPLE 8 HCV CKS-C100 A. Preparation of HCV CKS-C100 Vectors Eighteen individual oligonucleotides representing amino acids 1569-1931 of the HCV genome were ligated together and cloned as four separate EcoRI-BamHI subfragments into the CKS fusion vector pJ0200. After subsequent DNA sequences confirmation, the four subfragments were digested with the appropriate restriction enzymes, gel purified, ligated together, and cloned as an 1 102 base pair EcoRI- BamHI fragment in the CKS fusion vector pJ0200 The resulting plasmid, designated pHCV-24, expresses the HCV CKS-C100 antigen under control of the lac promoter. The HCV CKS-c100 antigen consists of 239 ammo acids of CKS, eight ammo acids contributed by linker DNA sequences, 363 ammo acids from the HCV NS4 region (ammo acids 1569-1931 ) and 10 additional am o acids contributed by linker DNA sequences The HCV CKS-c100 antigen was expressed at very low levels by pHCV-24. Poor expression levels of this HCV CKS-c100 recombinant antigen were overcome by constructing two additional clones containing deletions in the extreme ammo terminal portion of the HCV c100 region The first of these clones, designated pHCV-57, contains a 23 ammo acid deletion (HCV ammo acids 1575- 1597) and was constructed by deleting a 69 base pair Ddel restriction fragment. The second of these clones, designated pHCV-58, contains a 21 ammo acid deletion (HCV ammo acids 1600-1620) and was constructed by deleting a 63 base pair NlalV-Haelll restriction fragment Figure 34 presents a schematic representation of the recombinant antigens expressed by pHCV-24, pHCV-57, and pHCV-58. SEQ.ID.NO. 36 and 37 presents the DNA and ammo acid sequence of the HCV-C100D1 recombinant antigen produced by pHCV-57. SEQ.ID.NO. 38 and 39 presents the DNA and ammo acid sequence of the HCV-C100D2 recombinant antigen produced by pHCV-58 Figure 35 presents the expression of pHCV-24, pHCV-57, and pHCV-58 proteins in E coli Lane 1 contained the E coli lysate containing pHCV-24 expressing the HCV CKS-c100 antigen (ammo acids 1569-1931) prior to induction and lanes 2 and 3 after 2 and 4 hours post induction, respectively. Lane 4 contained the E. coli lysate containing pHCV-57 expressing the HCV-CKS-C100D1 antigen (ammo acids 1569-1574 and 1598-1931) prior to induction and lanes 5 and 6 after 2 and 4 hours induction, respectively. Lane 7 contained the E. coli lysate containing pHCV-58 expressing the HCV CKS-C100D2 antigen (am o acids 1569-1599 and 1621 -1931) prior to induction, and lanes 8 and 9 after 2 and 4 hours induction, respectively These results show that both the pHCV-57 and pHCV-58 fusion proteins express at significantly higher levels than the pHCV-24 fusion protein and that both the pHCV-57 and pHCV-58 fusion proteins have an apparent mobility corresponding to a molecular size of 65,000 daltons. This compares acceptably to the predicted molecular mass of 64,450 daltons for pHCV- 57 and 64,458 daltons for pHCV-58 EXAMPLE 9 HCV PCR DERIVED EXPRESSION VECTORS A. Preparation of HCV DNA Fragments RNA was extracted from the serum of various chimpanzees or humans infected with HCV by first subjecting the samples to digestion with Proteinase K and SDS for 1 hour at 37° centigrade followed by numerous phenokchloroform extractions. The RNA was then concentrated by several ethanol precipitations and resuspended in water. RNA samples were then reverse transcribed according to supplier's instructions using a specific primer. A second primer was then added and PCR amplification was performed according to supplier's instructions. An aliquot of this PCR reaction was then subjected to an additional round of PCR using nested primers located internal to the first set of primers. In general, these primers also contained restriction endonuclease recognition sequences to be used for subsequent cloning. An aliquot of this second round nested PCR reaction was then subjected to agarose gel electrophoresis and Southern blot analysis to confirm the specificity of the PCR reaction. The remainder of the PCR reaction was then digested with the appropriate restriction enzymes, the HCV DNA fragment of interest gel purified, and ligated to an appropriate cloning vector. This ligation was then transformed into E. coli and single colonies were isolated and plasmid DNA prepared for DNA sequences analysis. The DNA sequences was then evaluated to confirm that the specific HCV coding region of interest was intact. HCV DNA fragments obtained in this manner were then cloned into appropriate vectors for expression analysis. B. Preparation of HCV CKS-NS3 Using the methods detailed above, a 474 base pair DNA fragment from the putative NS3 region of HCV was generated by PCR. This fragment represents HCV amino acids #1473-1629 and was cloned into the CKS expression vector pJ0201 by blunt-end ligation. The resulting clone, designated pHCV-105, expresses the HCV CKS-NS3 antigen under control of the lac promoter. The HCV CKS-NS3 antigen consists of 239 amino acids of CKS, 12 amino acids contributed by linker DNA sequences, 157 amino acids from the HCV NS3 region (amino acids 1473-1629), and 9 additional amino acids contributed by linker DNA sequences. Figure 36 presents a schematic representation of the pHCV-105 antigen. SEQ.ID.NO. 40 and 41 presents the DNA and amino acid sequence of the HCV CKS-NS3 recombinant antigen produced by pHCV-105. Figure 37 presents the expression of pHCV-105 proteins in E. coli. Lane 1 contained the E. coli lysate containing pHCV-105 expressing the HCV CKS-NS3 antigen (amino acids 1472-1629) prior to induction and lanes 2 and 3 after 2 and 4 hours induction, respectively. These results show that the pHCV-105 fusion protein has an apparent mobility corresponding to a molecular mass of 43,000 daltons. This compares acceptably to the predicted molecular mass of 46,454 daltons. C. Preparation of HCV CKS-5'ENV Using the methods detailed above, a 489 base pair DNA fragment from the putative envelope region of HCV was generated by PCR. This fragment represents the HCV amino acids 114-276 and was cloned into the CKS expression vector pJ0202 using EcoRI-BamHI restriction sites. The resulting clone, designated pHCV-103, expresses the HCV CKS-5ΕNV antigen under control of the lac promoter. The HCV CKS-5'ENV antigen consists of 239 amino acids of CKS, 7 amino acids contributed by linker DNA sequences, 163 amino acids from the HCV envelope region (amino acids 1 14-276), and 16 additional amino acids contributed by linker DNA sequences. Figure 38 presents a schematic representation of the pHCV- 103 antigen. SEQ.ID.NO. 42 and 43 presents the DNA and amino acid sequence of the HCV CKS-5ΕNV recombinant antigen produced by pHCV-103. Figure 37 presents the expression of pHCV-103 proteins in E. coli. Lane 1 contained the E. coli lysate containing pHCV-103 expressing the HCV CKS-5ΕNV antigen (amino acids 114- 276) prior to induction and lanes 5 and 6 after 2 and 4 hours induction, respectively. These results show that the pHCV-103 fusion protein has an apparent mobility corresponding to a molecular mass of 47,000 daltons. This compares acceptably to the predicted molecular mass of 46,091 daltons. P. Preparation of HCV CKS-3'ENV Using the methods detailed above, a 621 base pair DNA fragment form the putative envelope region of HCV was generated by PCR. This fragment represents HCV amino acids 263-469 and was cloned into the CKS expression vector pJ0202 using EcoRI restriction sites. The resulting clone, designated pHCV-101 , expresses the HCV CKS-3ΕNV antigen under control of the lac promoter. The HCV CKS- 3'ENV antigen consists of 239 amino acids of CKS, 7 amino acids contributed by linker DNA sequences, 207 amino acids from the HCV envelope region (amino acids 263-469), and 15 additional amino acids contributed by linker DNA sequences. Figure 39 presents a schematic representation of the pHCV-101 antigen. SEQ.ID.NO. 44 and 45 presents the DNA and amino acid sequence of the HCV CKS- 3'ENV recombinant antigen produced by pHCV-101. Figure 37 presents the expression of pHCV-101 proteins in E. coli. Lane 7 contained the E. coli lysate containing pHCV-101 expressing the HCV CKS-3'ENV antigen (amino acids 263- 469) prior to induction and lanes 8 and 9 after 2 and 4 hours induction, respectively. These resulting show that the pHCV-101 fusion protein has an apparent mobility corresponding to a molecular mass of 47,000 daltons. This compares acceptably to the predicted molecular mass of 51 ,181 daltons. E. Preparation of HCV CKS-NS2 Using the methods detailed above, a 636 base pair DNA fragment from the putative NS2 region of HCV was generated by PCR. This fragment represents the HCV amino acids 994-1205 and was cloned into the CKS expression vector pJ0201 using EcoRI restriction sites. The resulting clone, designated pHCV-102, expresses the HCV CKS-NS2 antigen under control of the lac promoter. The HCV CKS-NS2 antigen consists of 239 amino acids of CKS, 7 amino acids contributed by linker DNA sequences, 212 amino acids from the HCV NS2 region (amino acids 994- 1205), and 16 additional amino acids contributed by linker DNA sequences. Figure 40 presents a schematic representation of the pHCV-102 antigen. SEQ.ID.NO. 46 and 47 presents the DNA and amino acid sequence of the HCV CKS-NS2 recombinant antigen produced by pHCV-102. Figure 41 presents the expression of pHCV-102 proteins in E. coli. Lane 1 contained the E. coli lysate containing pHCV-102 expressing the HCV CKS-NS2 antigen (amino acids 994-1205) prior to induction and lanes 2 and 3 after 2 and 4 hours induction, respectively. These results show that the pHCV-102 fusion protein has an apparent mobility corresponding to a molecular mass of 53,000 daltons. This compares acceptably to the predicted molecular mass of 51,213 daltons. F. Preparation of HCV CKS-NS1 Using the methods detailed above, a 654 base pair DNA fragment from the putative NS1 region of HCV was generated by PCR. This fragment represents HCV amino acids 617-834 and was cloned into the CKS expression vector pJ0200 using EcoRI-BamHI restriction sites. The resulting clone, designated pHCV-107, expresses the HCV CKS-NS1 antigen under control of the lac promoter. The HCV CKS-NS1 antigen consists of 239 amino acids of CKS, 10 amino acids contributed by linker DNA sequences, and 218 amino acids from the HCV NS1 region (amino acids 617-834). Figure 42 presents a schematic representation of the pHCV-107 antigen. SEQ.ID.NO. 48 and 49 presents the DNA and amino acid sequence of the HCV CKS-NS1 recombinant antigen produced by pHCV-107. G. Preparation of HCV CKS-ENV Using the methods detailed above, a 1068 base pair DNA fragment from the putative envelope region of HCV was generated by PCR. This fragment represents HCV ammo acids #114-469 and was cloned into the CKS expression vector pJ0202 using EcoRI restriction sites The resulting clone, designated pHCV-104, expresses the HCV CKS-ENV antigen under control of the lac promoter. The HCV CKS-ENV antigen consists of 239 ammo acids of CKS, 7 ammo acids contributed by linker PNA sequences, 356 ammo acids from the HCV envelope region (am o acids 114- 469), and 15 additional ammo acids contributed by linker DNA sequences. Figure 43 presents a schematic representation of the pHCV-104 antigen. SEQ.ID.NO. 50 and 51 presents the DNA and am o acid sequence of the HCV CKS-ENV recombinant antigen produced by pHCV-104 EXAMPLE 10. HCV CKS-C100A A. Construction of HCV CKS-C100A Deletion Clones Example 8 described the construction of a synthetic gene encoding HCV a.a. 1569-1931. Expression of this synthetic gene as a CKS fusion protein in E. coli was at very low levels. In order to define the regιon(s) that were deleterious to the expression of the HCV CKS-C100 antigen in E. coli. the expression levels of four separate subfragments of HCV C100 were examined as fusions to CKS. One such clone, designated pHCV-19 , contained HCV a.a. 1569-1677 and did not express the HCV CKS-C100A protein for which it was designed. Two internal deletions located in the ammo terminal portion of C100 (HCV a.a. 1575-1620) were constructed. The first of these, pHCV-54, was an internal deletion of 23 ammo acids (HCV a.a.1575-1597) using the restriction site Ddel. This deletion expressed well as a CKS fusion in E. coli. SEQ.ID.NO 1 presents the ammo acid sequence of the antigen produced by pHCV-54 . Figure 44A presents the expression of this HCV CKS- CIOOA protein in E. coli Figure 44B presents an immunoblot of the antigen produced by pHCV-54. Lane 2 contained the E. coli lysate from pHCV-54 expressing the HCV CKS-C100A antigen four hours post induction. The second of these deletion clones, pHCV-55, deleted 21 ammo acids (HCV a.a. 1600-1620) and utilized the restriction sites NlalV/Haelll This internal deletion also expressed well in E. coli as a CKS fusion. SEQ.ID.NO. 2 presents the ammo acid sequence of the antigen produced by pHCV-55 Figure 44A presents the expression of this HCV CKS-C100A protein in E. coli Figure 44B presents an immunoblot of the antigen produced by pHCV-55. Lane 3 contained the E coli lysate from pHCV-55 expressing the HCV CKS-C100A antigen four hours post induction. The HCV amino acids deleted in pHCV-55 (HCV a.a. 1600-1620) were sequentially replaced from the carboxy-terminal end using a fragment replacement method. The DNA fragments that were inserted were synthesized as complimentary pairs of single-stranded oligonucleotides. The oligonucleotide pairs were kinased, annealed, and ligated to the remainder of the C100A fragment from pHCV-19 using the restriction enzymes Bsp1286l/Sau96l. The resulting new C-100A fragments were cloned into the CKS fusion expression vector pJO200 and expressed in E. coli. Table 1 summarizes both the HCV amino acids that were manipulated as well as the expression levels of the various HCV CKS-C100A antigens in E. coli. SEQ.ID.NO.3 presents the amino acid sequence of the antigen produced by pHCV-94. Figure 44A presents the expression of this HCV CKS-C100A protein in E. coli. Figure 44B presents an immunoblot of the antigen produced by pHCV-94. Lane 4 contained the E. coli lysate from pHCV-94 expressing the HCV CKS-C100A antigen four hours post induction. SEQ.ID.NO. 4 presents the amino acid sequence of the antigen produced by pHCV-95. Figure 44A presents the expression of the HCV CKS-C100A protein in E. coli. Figure 44B presents an immunoblot of the antigen produced by pHCV-95. Lane 5 contained the E. coli lysate from pHCV-95 expressing the HCV CKS-C100A antigen four hours post induction. SEQ.ID.NO. 5 presents the amino acid sequence of the antigen produced by pHCV-96. Figure 44A presents the expression of this HCV CKS-C100A protein in E. coli. Figure 44B presents an immunoblot of the antigen produced by pHCV-96. Lane 6 contained the E. coli lysate from pHCV-96 expressing the HCV CKS-C100A antigen four hours post induction. SEQ.ID.NO. 6 presents the amino acid sequence of the antigen produced by pHCV-97. Figure 44A presents the expression of this HCV CKS-C100A protein in E. coli. Figure 44B presents an immunoblot of the antigen produced by pHCV-97. Lane 7 contained the E. coli lysate from pHCV-97 expressing the HCV CKS-C100A antigen four hours post induction. SEQ.ID.NO. 7 presents the amino acid sequence of the antigen produced by pHCV-202. Figure 45A presents the expression of this HCV CKS-C100A in E. coli. Figure 45B presents an immunoblot of the antigen produced by pHCV-202. Lanes 1 , 2, and 3 contained the E. coli lysate from pHCV-202 expressing the HCV CKS-C100A antigen before induction and two and four hours post induction, respectively. SEQ.ID.NO 8 presents the amino acid sequence of the antigen produced by pHCV-203. Figure 45A presents the expression of this HCV CKS-C100A protein in E. coli. Figure 45B presents an immunoblot of the antigen produced by pHCV-203. Lanes 1, 2, and 3 contained the E. coli lysate from pHCV- 203 expressing the HCV CKS-C100A antigen before induction and two and four hours post induction, respectively. SEQ.ID.NO. 19 delineates the amino acids that were manipulated in the fragment replacements described above. The results summarized in Table 1 indicated that the deletion of three proline residues at HCV a.a. 1600-1602 (pHCV-96) (SEQ.ID.NO. 5) permitted expresion of the HCV CKS- CI OOA antigen at high levels in E coli Further analysis showed that the deletion of two proline residues at HCV a a 1600-1601 (pHCV-202) also maintained expression of this antigen at high levels However, when only one of these proline residues was deleted (pHCV-203)(SEQ.ID.NO. 8), the expression level of this antigen was reduced to that of pHCV-19, the original HCV CKS-C100A clone. Therefore, the deletion of two prolmes at HCV a.a. 1600-1601 contributes to high level expression of the HCV CKS-C100A antigen in E coli as determined by SDS- PAGE analysis Western blot analysis of these deletion clones indicated a high degree of immunoreactivity when probed with human sera containing antibodies to HCV C100. TABLE 1 +/- = expression detectable by Western blot only +++ = expression level > 10% of total cell protein by coomassie stained gel * indicates the use of alternate codons optimized for E coli expression B Construction of HCV CKS-C100 Expression Clones In order to construct a vector which expressed the various HCV CKS-C100 deletion antigens at high levels in E coli. we replaced the EcoRI/Sall fragment from pHCV-24 with the various corresponding EcoRI/Sall fragments from the deletion clones described above The EcoRI/Sall fragments from pHCV-54 and pHCV-55 were used to replace the EcoRI/Sall fragment of pHCV-24 to create the plasmids pHCV-57 and pHCV-58 as described in Example 8. The HCV CKS-C100 antigens encoded by pHCV-57 and pHCV-58 expressed well in E. coli. The 3' end of these clones were altered by PCR changing the linker associated amino acid sequence from WDPLDCRHAK (SEQ. ID. NO. 9) to VHHKR (SEQ. ID. NO. 10). The resulting plasmids were designated pHCV-62 and pHCV-63, respectively. SEQ.ID.NO. 11 presents the amino acid sequence of the antigen produced by pHCV-62. SEQ.ID.NO. 12 presents the amino acid sequence of the antigen produced by pHCV-63. The HCV CKS-C100 antigens encoded by pHCV-62 and pHCV-63 expressed well in E. coli. Figure 46A presents the expression of these HCV CKS-C100 antigens in E. coli. Figure 46B presents an immunoblot of the antigens produced by pHCV-62 and pHCV-63. Lanes 1 and 2 contained the E. coli lysate from pHCV-62 expressing the HCV CKS-C100 antigen prior to induction and four hours post induction, respectively. Lanes 3 and 4 contained the E. coli lysate from pHCV-63 expressing the HCV CKS-C100 antigen proir to induction and four hours post induction, respectively. The EcoRI/Sall fragment from pHCV-202 was used to replace the EcoRI/Sall fragment of pHCV-63 to create the plasmid pHCV-204. SEQ.ID.NO. 13 presents the amino acid sequence of the antigen produced by pHCV-204. Table 2 summarizes the deletion analysis conducted on the HCV CKS-C100 antigens and their expression levels in E. coli. The expression levels of the HCV CKS-C100 deletion clones corresponded with the expression levels of the HCV CKS-C100A deletion clones from which they were derived. Figure 47A presents the expression of pHCV-204 protein in E. coli. Figure 47B presents an immunoblot of the antigen produced by pHCV-204. Lanes 1 and 2 contained the E. coli lysate from pHCV-204 expressing the HCV CKS-C100 antigen prior to induction and four hours post induction, respectively. TABLE 2 PLASMI D HCV a.a. DELETED EXPRESSION LEVEL HCV-57 1 575- 1 597 + + + pHCV-58 1 600- 1 620 + + + pHCV-62 1 575- 1 597 + + + pHCV-63 1 600 - 1 620 + + + pHCV-204 1 600- 1 601 + + + +/- = expression detectable by Western blot only +++ = expression level > 10% of total cell protein by coomassie stained gel EXAMPLE 11. HCV CKS-C200 Construction of HCV CKS-C200 Expression Clones The construction of a clone which expressed the HCV CKS-C200 antigen (HCV a.a. 1192-1931) at high levels of E. coli required the steps described hereinbelow. First, a clone expressing the HCV CKS-33C antigen (HCV a.a. 1192- 1457) was constructed as described in Example 2, designated pHCV-29. Second, a clone containing the DNA sequence encoding HCV a.a. 1454-1569 was constructed using a PCR methodology as described in Example 9, designated as pHCV-108 (SEQ. ID. NO. 20). This DNA sequence was later cloned as an in-frame fusion to CKS in order to express the HCV CKS-NS3-1 antigen (HCV a.a. 1454-1568), designated pHCV-112 (SEQ. ID. 14). Third, a clone expressing the HCV CKS-C100 deletion antigen (HCV a.a. 1569-1574 and 1598-1931) was constructed, designated pHCV-62 described above. Fourth, the Ncol fragment containing the C100 coding region was excised from pHCV-62 and inserted into the Ncol site of pHCV-108 to create pHCV-68 (SEQ. ID. 15). Lastly, the Clal/BamHI fragment containing the HCV NS3/C100 coding region (HCV a.a. 1454-1574 and 1598-1931) was excised from pHCV-68 and inserted into the Clal/BamHI sites of pHCV-29. The resultant clone, designated pHCV-72, expresses the HCV CKS C200 antigen (HCV a.a. 1192- 1574 and 1598-1931). SEQ.ID.NO. 16 presents the amino acid sequence of the antigen produced by pHCV-72. In a similar manner, the C100 coding region of pHCV-63 was substituted for that of pHCV-62 to generate pHCV-69 (SEQ. ID. 21). The Clal/BamHI fragment containing the HCV NS3/C100 coding region (HCV a.a. 1454-1599 and 1621 -1931) was excised frompHCV-69 and inserted into the Clal/BamHI sites of pHCV-29. The resultant clone, designated pHCV-73, expresses the HCV CKS-C200 antigen (HCV a.a. 1 192-1599 and 1621 -1931 ). SEQ.ID.NO. 17 presents the amino acid sequence of the antigen produced by pHCV-73. Figure 48A presents the expression of these HCV CKS-C200 antigens in E. coli. FIG. 48B presents an immunoblot of the antigen produced from pHCV-73. Lanes 1 , 2, and 3 contained the E. coli lysate from pHCV-72 expressing the HCV CKS-C200 antigen before induction and two and four hours post induction, respectively. Lanes 4, 5, and 6 contained the E. coli lysate from pHCV-73 expressing the HCV CKS-C200 antigen before induction and two and four hours post induction, respectively. A different HCV CKS-C200 construct (HCV a.a. 1192-1599 and 1602-1931) was assembled by first obtaining the HCV C100A region (HCV a.a. 1569-1599 and - 1602-1677) as a Clal/Ncol 352 base pair fragment from pHCV-202. The NS3-1 antigen (HCV a.a. 1454-1568) was obtained as a Clal/Ncol 352 base pair fragment from pHCV-72. The last fragment used was the 792 base pair fragment from pHCV-72 which contained C100 BCD (HCV a.a. 1678-1931). These three fragments were ligated to each other Clal/Ncol/Sall/BamHI and ligated into the vector backbone pHCV-29 Clal/BamHI, which contributed the HCV CKS-33C antigen (HCV a.a. 1192-1453). The HCV CKS-C200 construct, designated pHCV-205, was expressed as a CKS fusion in pJO200 and expressed at high levels as determined by coosmasie stained gel and Western blot analysis. SEQ.ID.NO. 18 presents the amino acid sequence of the antigen produced by pHCV-205. Figure 49A presents the expression of the HCV CKS-C200 antigen in E. coli. Figure 49B presents an immunoblot of the antigen produced by pHCV-205. Lane 1 contained the E. coli lysate from pHCV-205 expressing the HCV CKS-C200 antigen before induction and lane 2 presents two hours post induction. The present invention provides unique antigens corresponding to a distinct antigenic region of the HCV genome which can be utilized as a reagent for the detection and/or confirmation of antibodies and antigen in test samples from individuals exposed to HCV. Although the exact function of the NS4 region is unknown, the antigens described herein are located in the putative immunodominant region of the HCV genome. The recombinant antigens, either alone or in combination, can be used in the assay formats provided herein and exemplified in the Examples. It also is contemplated that these recombinant antigens can be used to develop specific inhibitors of viral replication and used for therapeutic purposes, such as for vaccines. Other applications and modifications of the use of these antigens and the specific embodiments of this invention as set forth herein, will be apparent to those skilled in the art. Accordingly, the invention is intended to be limited only in accordance with the appended claims. SEQUENCE LISTING (1) GENERAL INFORMATION: (i) APPLICANT: DESAI, SURESH M. CASEY, JAMES M. RUPPRECHT, KEVIN R. DEVARE, SUSHIL G. (ii) TITLE OF INVENTION: HEPATITIS C ASSAY UTILIZING RECOMBINANT ANTIGENS TO C-100 REGION (iii) NUMBER OF SEQUENCES: 51 (iv) CORRESPONDENCE ADDRESS: (A) ADDRESSEE: ABBOTT LABORATORIES CHAD377/AP6D (B) STREET: ONE ABBOTT PARK ROAD (C) CITY: ABBOTT PARK (D) STATE: ILLINOIS (E) COUNTRY: USA (F) ZIP: 60064-3500 (v) COMPUTER READABLE FORM: (A) MEDIUM TYPE: Floppy disk (B) COMPUTER: IBM PC compatible (C) OPERATING SYSTEM: PC-DOS/MS-DOS (D) SOFTWARE: Patentln Release #1.0, Version #1.25 (vi) CURRENT APPLICATION DATA: (A) APPLICATION NUMBER: US 07/748,566 (B) FILING DATE: 21 -AUG-1991 (C) CLASSIFICATION: (viii) ATTORNEY/AGENT INFORMATION: (A) NAME: POREMBSKI, PRISCILLA E, (B) REGISTRATION NUMBER: 33,207 (C) REFERENCE/DOCKET NUMBER: 4834.PC.04 (ix) TELECOMMUNICATION INFORMATION: (A) TELEPHONE: 708-937-6365 (B) TELEFAX: 708-937-9556 (2) INFORMATION FOR SEQ ID NO:1 : (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 342 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (xi) SEQUENCE DESCRIPTION: SEQ ID NO:1 : Met Ser Phe Val Val He lie Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 Pro Gly Lys Pro Leu Val Asp lie Asn Gly Lys Pro Met lie Val His 20 25 30 Val Leu GIu Arg Ala Arg Glu Ser Gly Ala Glu Arg He He Val Ala 35 40 45 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val He Val Asn 85 90 95 Val Gin Gly Asp Glu Pro Met He Pro Ala Thr lie He Arg Gin Val 100 105 110 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Val 115 120 125 Pro He His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr lie 145 150 155 160 Pro Trp Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 Asn Phe Leu Arg His Leu Gly He Tyr Gly Tyr Arg Ala Gly Phe lie 180 185 190 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His lie Glu Met 195 200 205 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 Asp Pro Ser Thr Asn Ser Met Asp Ala His Phe Leu Ser Gin Ala Pro 245 250 255 Pro Pro Ser Trp Asp Gin Met Trp Lys Cys Leu He Arg Leu Lys Pro 260 265 270 Thr Leu His Gly Pro Thr Pro Leu Leu Tyr Arg Leu Gly Ala Val Gin 275 280 285 Asn Glu lie Thr Leu Thr His Pro Val Thr Lys Tyr He Met Thr Cys 290 295 300 Met Ser Ala Asp Leu Glu Val Val Thr Ser Thr Trp Val Leu Val Gly 305 310 315 320 Gly Val Leu Ala Ala Leu Ala Ala Tyr Cys Leu Ser Thr Asp Pro Leu 325 330 335 Asp Cys Arg His Ala Lys 340 (2) INFORMATION FOR SEQ ID NO:2: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 344 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: iinear (ii) MOLECULE TYPE: peptide (xi) SEQUENCE DESCRIPTION: SEQ ID NO:2: Met Ser Phe Val Val lie lie Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 Pro Gly Lys Pro Leu Val Asp He Asn Gly Lys Pro Met lie Val His 20 25 30 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg He lie Val Ala 35 40 45 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val lie Val Asn 85 90 95 Val Gin Gly Asp Glu Pro Met lie Pro Ala Thr lie lie Arg Gin Val 100 105 110 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Val 1 15 120 125 Pro lie His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr He 145 150 155 160 Pro Trp Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 Asn Phe Leu Arg His Leu Gly lie Tyr Gly Tyr Arg Ala Gly Phe He 180 185 190 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His lie Glu Met 195 200 205 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 Asp Pro Ser Thr Asn Ser Met Asp Ala His Phe Leu Ser Gin Thr Lys 245 250 255 Gin Ser Gly Glu Asn Leu Pro Tyr Leu Val Ala Tyr Gin Ala Thr Val 260 265 270 Cys Ala Arg Ala Gin Ala Pro Thr Pro Leu Leu Tyr Arg Leu Gly Ala 275 280 285 Val Gin Asn Glu lie Thr Leu Thr His Pro Val Thr Lys Tyr He Met 290 295 300 Thr Cys Met Ser Ala Asp Leu Glu Val Val Thr Ser Thr Trp Val Leu 305 310 315 320 Val Gly Gly Val Leu Ala Ala Leu Ala Ala Tyr Cys Leu Ser Thr Asp 325 330 335 Pro Leu Asp Cys Arg His Ala Lys 340 (2) INFORMATION FOR SEQ ID NO:3: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 352 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (xi) SEQUENCE DESCRIPTION: SEQ ID NO:3: Met Ser Phe Val Val lie He Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 Pro Gly Lys Pro Leu Val Asp He Asn Gly Lys Pro Met lie Val His 20 25 30 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg He He Val Ala 35 40 45 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val lie Val Asn 85 90 95 Val Gin Gly Asp Glu Pro Met lie Pro Ala Thr lie lie Arg Gin Val 100 105 110 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Thr Thr Leu Ala Val 115 120 125 Pro He His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr lie 145 150 155 160 Pro Trp Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 Asn Phe Leu Arg His Leu Gly He Tyr Gly Tyr Arg Ala Gly Phe He 180 185 190 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His He Glu Met 195 200 205 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 Asp Pro Ser Thr Asn Ser Met Asp Ala His Phe Leu Ser Gin Thr Lys 245 250 255 Gin Ser Gly Glu Asn Leu Pro Tyr Leu Val Ala Tyr Gin Ala Thr Val 260 265 270 Cys Ala Arg Ala Gin Ala Arg Leu Lys Pro Thr Leu His Gly Pro Thr 275 280 285 Pro Leu Leu Tyr Arg Leu Gly Ala Val Gin Asn Glu lie Thr Leu Thr 290 295 300 His Pro Val Thr Lys Tyr lie Met Thr Cys Met Ser Ala Asp Leu Glu 305 310 315 320 Val Val Thr Ser Thr Trp Val Leu Val Gly Gly Val Leu Ala Ala Leu 325 330 335 Ala Ala Tyr Cys Leu Ser Thr Asp Pro Leu Asp Cys Arg His Ala Lys 340 345 350 (2) INFORMATION FOR SEQ ID NO:4: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 357 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (xi) SEQUENCE DESCRIPTION: SEQ ID NO:4: Met Ser Phe Val Val He He Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 Pro Gly Lys Pro Leu Val Asp He Asn Gly Lys Pro Met lie Val His 20 25 30 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg lie He Val Ala 35 40 45 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val He Val Asn 85 90 95 Val Gin Gly Asp Glu Pro Met lie Pro Ala Thr He He Arg Gin Val 100 105 110 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Thr Thr Leu Ala Val 115 120 125 Pro He His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr He 145 150 155 160 Pro Trp Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 Asn Phe Leu Arg His Leu Gly He Tyr Gly Tyr Arg Ala Gly Phe lie 180 185 190 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His He Glu Met 195 200 205 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 Asp Pro Ser Thr Asn Ser Met Asp Ala His Phe Leu Ser Gin Thr Lys 245 250 255 Gin Ser Gly Glu Asn Leu Pro Tyr Leu Val Ala Tyr Gin Ala Thr Val 260 265 270 Cys Ala Arg Ala Gin Ala Trp Lys Cys Leu He Arg Leu Lys Pro Thr 275 280 285 Leu His Gly Pro Thr Pro Leu Leu Tyr Arg Leu Gly Ala Val Gin Asn 290 295 300 Glu He Thr Leu Thr His Pro Val Thr Lys Tyr He Met Thr Cys Met 305 310 315 320 Ser Ala Asp Leu Glu Val Val Thr Ser Thr Trp Val Leu Val Gly Gly 325 330 335 Val Leu Ala Ala Leu Ala Ala Tyr Cys Leu Ser Thr Asp Pro Leu Asp 340 345 350 Cys Arg His Ala Lys 355 (2) INFORMATION FOR SEQ ID NO:5: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 362 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (xi) SEQUENCE DESCRIPTION: SEQ ID NO:5: Met Ser Phe Val Val He He Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 Pro Gly Lys Pro Leu Val Asp He Asn Gly Lys Pro Met lie Val His 20 25 30 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg lie He Val Ala 35 40 45 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val He Val Asn 85 90 95 Val Gin Gly Asp Glu Pro Met lie Pro Ala Thr He He Arg Gin Val 100 105 110 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Thr Thr Leu Ala Val 115 120 125 Pro lie His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr He 145 150 155 160 Pro Trp Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 Asn Phe Leu Arg His Leu Gly He Tyr Gly Tyr Arg Ala Gly Phe He 180 185 190 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His He Glu Met 195 200 205 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 Asp Pro Ser Thr Asn Ser Met Asp Ala His Phe Leu Ser Gin Thr Lys 245 250 255 Gin Ser Gly Glu Asn Leu Pro Tyr Leu Val Ala Tyr Gin Ala Thr Val 260 265 270 Cys Ala Arg Ala Gin Ala Ser Trp Asp Gin Met Trp Lys Cys Leu He 275 280 285 Arg Leu Lys Pro Thr Leu His Gly Pro Thr Pro Leu Leu Tyr Arg Leu 290 295 300 Gly Ala Val Gin Asn Glu He Thr Leu Thr His Pro Val Thr Lys Tyr 305 310 315 320 He Met Thr Cys Met Ser Ala Asp Leu Glu Val Val Thr Ser Thr Trp 325 330 335 Val Leu Val Gly Gly Val Leu Ala Ala Leu Ala Ala Tyr Cys Leu Ser 340 345 350 Thr Asp Pro Leu Asp Cys Arg His Ala Lys 355 360 (2) INFORMATION FOR SEQ ID NO:6: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 365 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (xi) SEQUENCE DESCRIPTION: SEQ ID NO:6: Met Ser Phe Val Val He He Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 Pro Gly Lys Pro Leu Val Asp He Asn Gly Lys Pro Met lie Val His 20 25 30 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg He lie Val Ala 35 40 45 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val He Val Asn 85 90 95 Val Gin Gly Asp Glu Pro Met He Pro Ala Thr He lie Arg Gin Val 100 105 110 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Thr Thr Leu Ala Val 115 120 125 Pro lie His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr He 145 150 155 160 Pro Trp Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 Asn Phe Leu Arg His Leu Gly lie Tyr Gly Tyr Arg Ala Gly Phe He 180 185 190 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His He Glu Met 195 200 205 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 Asp Pro Ser Thr Asn Ser Met Asp Ala His Phe Leu Ser Gin Thr Lys 245 250 255 Gin Ser Gly Glu Asn Leu Pro Tyr Leu Val Ala Tyr Gin Ala Thr Val 260 265 270 Cys Ala Arg Ala Gin Ala Pro Pro Pro Ser Trp Asp Gin Met Trp Lys 275 280 285 Cys Leu He Arg Leu Lys Pro Thr Leu His Gly Pro Thr Pro Leu Leu 290 295 300 Tyr Arg Leu Gly Ala Val Gin Asn Glu lie Thr Leu Thr His Pro Val 305 310 315 320 Thr Lys Tyr He Met Thr Cys Met Ser Ala Asp Leu Glu Val Val Thr 325 330 335 Ser Thr Trp Val Leu Val Gly Gly Val Leu Ala Ala Leu Ala Ala Tyr 340 345 350 Cys Leu Ser Thr Asp Pro Leu Asp Cys Arg His Ala Lys 355 360 365 (2) INFORMATION FOR SEQ ID NO:7: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 363 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (xi) SEQUENCE DESCRIPTION: SEQ ID NO:7: Met Ser Phe Val Val He He Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 Pro Gly Lys Pro Leu Val Asp lie Asn Gly Lys Pro Met He Val His 20 25 30 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg He lie Val Ala 35 40 45 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val lie Val Asn 85 90 95 Val Gin Gly Asp Glu Pro Met He Pro Ala Thr lie lie Arg Gin Val 100 105 110 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Thr Thr Leu Ala Val 115 120 125 Pro lie His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr He 145 150 155 160 Pro Trp Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 Asn Phe Leu Arg His Leu Gly He Tyr Gly Tyr Arg Aia Gly Phe He 180 185 190 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His He Glu Met 195 200 205 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys lie His Val Aia 210 215 220 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 Asp Pro Ser Thr Asn Ser Met Asp Ala His Phe Leu Ser Gin Thr Lys 245 250 255 Gin Ser Gly Glu Asn Leu Pro Tyr Leu Val Ala Tyr Gin Ala Thr Val 260 265 270 Cys Ala Arg Ala Gin Ala Pro Ser Trp Asp Gin Met Trp Lys Cys Leu 275 280 285 lie Arg Leu Lys Pro Thr Leu His Gly Pro Thr Pro Leu Leu Tyr Arg 290 295 300 Leu Gly Ala Val Gin Asn Glu He Thr Leu Thr His Pro Val Thr Lys 305 310 315 320 Tyr He Met Thr Cys Met Ser Ala Asp Leu Glu Val Val Thr Ser Thr 325 330 335 Trp Val Leu Val Gly Gly Val Leu Ala Ala Leu Ala Ala Tyr Cys Leu 340 345 350 Ser Thr Asp Pro Leu Asp Cys Arg His Ala Lys 355 360 (2) INFORMATION FOR SEQ ID NO:8: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 364 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (xi) SEQUENCE DESCRIPTION: SEQ ID NO:8: Met Ser Phe Val Val He He Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 Pro Gly Lys Pro Leu Val Asp lie Asn Gly Lys Pro Met He Val His 20 25 30 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg He He Val Ala 35 40 45 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val He Val Asn 85 90 95 Val Gin Gly Asp Glu Pro Met He Pro Ala Thr lie He Arg Gin Val 100 105 110 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Thr Thr Leu Ala Val 115 120 125 Pro lie His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr lie 145 150 155 160 Pro Trp Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 Asn Phe Leu Arg His Leu Gly He Tyr Gly Tyr Arg Ala Gly Phe He 180 185 190 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His He Glu Met 195 200 205 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 Asp Pro Ser Thr Asn Ser Met Asp Ala His Phe Leu Ser Gin Thr Lys 245 250 255 Gin Ser Gly Glu Asn Leu Pro Tyr Leu Val Ala Tyr Gin Aia Thr Val 260 265 270 Cys Ala Arg Ala Gin Ala Pro Pro Ser Tφ Asp Gin Met Tφ Lys Cys 275 280 285 Leu He Arg Leu Lys Pro Thr Leu His Gly Pro Thr Pro Leu Leu Tyr 290 295 300 Arg Leu Gly Ala Val Gin Asn Glu lie Thr Leu Thr His Pro Val Thr 305 310 315 320 Lys Tyr He Met Thr Cys Met Ser Ala Asp Leu Glu Val Val Thr Ser 325 330 335 Thr Trp Val Leu Val Gly Gly Val Leu Ala Ala Leu Ala Ala Tyr Cys 340 345 350 Leu Ser Thr Asp Pro Leu Asp Cys Arg His Ala Lys 355 360 (2) INFORMATION FOR SEQ ID NO:9: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 10 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (xi) SEQUENCE DESCRIPTION: SEQ ID NO:9: Trp Asp Pro Leu Asp Cys Arg His Ala Lys 1 5 10 (2) INFORMATION FOR SEQ ID NO:10: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 5 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (xi) SEQUENCE DESCRIPTION: SEQ ID NO:10: Val His His Lys Arg 1 5 (2) INFORMATION FOR SEQ ID NO:11 : (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 592 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (xi) SEQUENCE DESCRIPTION: SEQ ID NO:11 : Met Ser Phe Val Val He He Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 Pro Gly Lys Pro Leu Val Asp lie Asn Gly Lys Pro Met He Val His 20 25 30 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg He He Val Ala 35 40 45 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val He Val Asn 85 90 95 Val Gin Gly Asp Glu Pro Met lie Pro Ala Thr He He Arg Gin Val 100 105 110 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Val 115 120 125 Pro He His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr He 145 150 155 160 Pro Trp Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 Asn Phe Leu Arg His Leu Gly He Tyr Gly Tyr Arg Ala Gly Phe He 180 185 190 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His He Glu Met 195 200 205 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 Asp Pro Ser Thr Asn Ser Met Asp Ala His Phe Leu Ser Gin Ala Pro 245 250 255 Pro Pro Ser Trp Asp Gin Met Tφ Lys Cys Leu lie Arg Leu Lys Pro 260 265 270 Thr Leu His Gly Pro Thr Pro Leu Leu Tyr Arg Leu Gly Ala Val Gin 275 280 285 Asn Glu lie Thr Leu Thr His Pro Val Thr Lys Tyr lie Met Thr Cys 290 295 300 Met Ser Ala Asp Leu Glu Val Val Thr Ser Thr Trp Val Leu Val Gly 305 310 315 320 Gly Val Leu Ala Ala Leu Ala Ala Tyr Cys Leu Ser Thr Gly Cys Val 325 330 335 Val lie Val Gly Arg Val Val Leu Ser Gly Lys Pro Ala He lie Pro 340 345 350 Asp Arg Glu Val Leu Tyr Arg Glu Phe Asp Glu Met Glu Glu Cys Ser 355 360 365 Gin His Leu Pro Tyr He Glu Gin Gly Met Met Leu Ala Glu Gin Phe 370 375 380 Lys Gin Lys Aia Leu Gly Leu Leu Gin Thr Ala Ser Arg Gin Ala Glu 385 390 395 400 Val He Ala Pro Ala Val Gin Thr Asn Trp Gin Lys Leu Glu Thr Phe 405 410 415 Trp Ala Lys His Met Tφ Asn Phe lie Ser Gly He Gin Tyr Leu Ala 420 425 430 Gly Leu Ser Thr Leu Pro Gly Asn Pro Ala He Ala Ser Leu Met Ala 435 440 445 Phe Thr Ala Ala Val Thr Ser Pro Leu Thr Thr Ser Gin Thr Leu Leu 450 455 460 Phe Asn He Leu Gly Gly Tφ Val Ala Ala Gin Leu Ala Ala Pro Gly 465 470 475 480 Ala Ala Thr Ala Phe Val Gly Ala Gly Leu Ala Gly Ala Ala lie Gly 485 490 495 Ser Val Gly Leu Gly Lys Val Leu He Asp He Leu Ala Gly Tyr Gly 500 505 510 Ala Gly Val Ala Gly Ala Leu Val Ala Phe Lys He Met Ser Gly Glu 515 520 525 Val Pro Ser Thr Glu Asp Leu Val Asn Leu Leu Pro Ala lie Leu Ser 530 535 540 Pro Gly Ala Leu Val Val Gly Val Val Cys Ala Ala He Leu Arg Arg 545 550 555 560 His Val Gly Pro Gly Glu Gly Ala Val Gin Tφ Met Asn Arg Leu He 565 570 575 Ala Phe Ala Ser Arg Gly Asn His Val Ser Pro Val His His Lys Arg 580 585 590 (2) INFORMATION FOR SEQ ID NO:12: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 594 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (xi) SEQUENCE DESCRIPTION: SEQ ID NO:12: Met Ser Phe Val Val He He Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 Pro Gly Lys Pro Leu Val Asp He Asn Gly Lys Pro Met He Val His 20 25 30 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg He He Val Ala 35 40 45 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val lie Val Asn 85 90 95 Val Gin Gly Asp Glu Pro Met He Pro Ala Thr lie He Arg Gin Val 100 105 110 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Val 115 120 125 Pro lie His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr lie 145 150 155 160 Pro Trp Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 Asn Phe Leu Arg His Leu Gly lie Tyr Gly Tyr Arg Ala Gly Phe He 180 185 190 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His lie Glu Met 195 200 205 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 Asp Pro Ser Thr Asn Ser Met Asp Ala His Phe Leu Ser Gin Thr Lys 245 250 255 Gin Ser Gly Glu Asn Leu Pro Tyr Leu Val Ala Tyr Gin Ala Thr Val 260 265 270 Cys Ala Arg Ala Gin Ala Pro Thr Pro Leu Leu Tyr Arg Leu Gly Ala 275 280 285 Val Gin Asn Glu He Thr Leu Thr His Pro Val Thr Lys Tyr lie Met 290 295 300 Thr Cys Met Ser Ala Asp Leu Glu Val Val Thr Ser Thr Trp Val Leu 305 310 315 320 Val Gly Gly Val Leu Ala Ala Leu Ala Ala Tyr Cys Leu Ser Thr Gly 325 330 335 Cys Val Val lie Val Gly Arg Val Val Leu Ser Gly Lys Pro Ala lie 340 345 350 He Pro Asp Arg Glu Val Leu Tyr Arg Glu Phe Asp Glu Met Glu Glu 355 360 365 Cys Ser Gin His Leu Pro Tyr lie Glu Gin Gly Met Met Leu Ala Glu 370 375 380 Gin Phe Lys Gin Lys Ala Leu Gly Leu Leu Gin Thr Ala Ser Arg Gin 385 390 395 400 Ala Glu Val He Ala Pro Ala Val Gin Thr Asn Trp Gin Lys Leu Glu 405 410 415 Thr Phe Trp Ala Lys His Met Trp Asn Phe He Ser Gly He Gin Tyr 420 425 430 Leu Ala Gly Leu Ser Thr Leu Pro Gly Asn Pro Ala He Ala Ser Leu 435 440 445 Met Ala Phe Thr Ala Ala Val Thr Ser Pro Leu Thr Thr Ser Gin Thr 450 455 460 Leu Leu Phe Asn He Leu Gly Gly Trp Val Ala Ala Gin Leu Ala Ala 465 470 475 480 Pro Gly Ala Ala Thr Ala Phe Val Gly Ala Gly Leu Ala Gly Ala Ala 485 490 495 He Gly Ser Val Gly Leu Gly Lys Val Leu He Asp lie Leu Ala Gly 500 505 510 Tyr Gly Ala Gly Val Ala Gly Ala Leu Val Ala Phe Lys He Met Ser 515 520 525 Gly Glu Val Pro Ser Thr Glu Asp Leu Val Asn Leu Leu Pro Ala lie 530 535 540 Leu Ser Pro Gly Ala Leu Val Val Gly Val Val Cys Ala Ala He Leu 545 550 555 560 Arg Arg His Val Gly Pro Gly Glu Gly Ala Val Gin Trp Met Asn Arg 565 570 575 Leu lie Ala Phe Ala Ser Arg Gly Asn His Val Ser Pro Val His His 580 585 590 Lys Arg (2) INFORMATION FOR SEQ ID NO:13: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 613 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (xi) SEQUENCE DESCRIPTION: SEQ ID NO:13: Met Ser Phe Val Val He He Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 Pro Gly Lys Pro Leu Val Asp He Asn Gly Lys Pro Met He Val His 20 25 30 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg He He Val Ala 35 40 45 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val lie Val Asn 85 90 95 Val Gin Gly Asp Glu Pro Met lie Pro Ala Thr He lie Arg Gin Val 100 105 110 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Aia Val 115 120 125 Pro He His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr He 145 150 155 160 Pro Trp Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 Asn Phe Leu Arg His Leu Gly lie Tyr Gly Tyr Arg Ala Gly Phe He 180 185 190 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His He Glu Met 195 200 205 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 Asp Pro Ser Thr Asn Ser Met Asp Ala His Phe Leu Ser Gin Thr Lys 245 250 255 Gin Ser Gly Glu Asn Leu Pro Tyr Leu Val Ala Tyr Gin Ala Thr Val 260 265 270 Cys Ala Arg Ala Gin Ala Pro Ser Trp Asp Gin Met Trp Lys Cys Leu 275 280 285 lie Arg Leu Lys Pro Thr Leu His Gly Pro Thr Pro Leu Leu Tyr Arg 290 295 300 Leu Gly Ala Val Gin Asn Glu lie Thr Leu Thr His Pro Val Thr Lys 305 310 315 320 Tyr He Met Thr Cys Met Ser Ala Asp Leu Glu Val Val Thr Ser Thr 325 330 335 Trp Val Leu Val Gly Gly Val Leu Ala Ala Leu Ala Ala Tyr Cys Leu 340 345 350 Ser Thr Gly Cys Val Val He Val Gly Arg Val Val Leu Ser Gly Lys 355 360 365 Pro Ala He He Pro Asp Arg Glu Val Leu Tyr Arg Glu Phe Asp Glu 370 375 380 Met Glu Glu Cys Ser Gin His Leu Pro Tyr He Glu Gin Gly Met Met 385 390 395 400 Leu Ala Glu Gin Phe Lys Gin Lys Ala Leu Gly Leu Leu Gin Thr Ala 405 410 415 Ser Arg Gin Ala Glu Val He Ala Pro Ala Val Gin Thr Asn Trp Gin 420 425 430 Lys Leu Glu Thr Phe Trp Ala Lys His Met Trp Asn Phe He Ser Gly 435 440 445 He Gin Tyr Leu Ala Gly Leu Ser Thr Leu Pro Gly Asn Pro Ala He 450 455 460 Ala Ser Leu Met Ala Phe Thr Ala Ala Val Thr Ser Pro Leu Thr Thr 465 470 475 480 Ser Gin Thr Leu Leu Phe Asn He Leu Gly Gly Trp Val Ala Ala Gin 485 490 495 Leu Ala Ala Pro Gly Ala Ala Thr Ala Phe Val Gly Ala Gly Leu Ala 500 505 510 Gly Ala Ala He Gly Ser Val Gly Leu Gly Lys Val Leu He Asp He 515 520 525 Leu Ala Gly Tyr Gly Ala Gly Val Aia Gly Ala Leu Val Ala Phe Lys 530 535 540 lie Met Ser Gly Glu Val Pro Ser Thr Glu Asp Leu Val Asn Leu Leu 545 550 555 560 Pro Ala He Leu Ser Pro Gly Ala Leu Val Val Gly Val Val Cys Ala 565 570 575 Ala He Leu Arg Arg His Val Gly Pro Gly Glu Gly Ala Val Gin Trp 580 585 590 Met Asn Arg Leu He Ala Phe Ala Ser Arg Gly Asn His Val Ser Pro 595 600 605 Val His His Lys Arg 610 (2) INFORMATION FOR SEQ ID NO:14: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 375 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (xi) SEQUENCE DESCRIPTION: SEQ ID NO:14: Met Ser Phe Val Val He He Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 Pro Gly Lys Pro Leu Val Asp He Asn Gly Lys Pro Met lie Val His 20 25 30 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg lie lie Val Ala 35 40 45 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val He Val Asn 85 90 95 Val Gin Gly Asp Glu Pro Met lie Pro Ala Thr lie lie Arg Gin Val 100 105 110 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Val 115 120 125 Pro He His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr He 145 150 155 160 Pro Trp Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 Asn Phe Leu Arg His Leu Gly lie Tyr Gly Tyr Arg Ala Gly Phe He 180 185 190 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His lie Glu Met 195 200 205 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 Asp Pro Ser Thr Glu Phe Val He Asp Cys Asn Thr Cys Val Thr Gin 245 250 255 Thr Val Asp Phe Ser Leu Asp Pro Thr Phe Thr He Glu Thr Thr Thr 260 265 270 Leu Pro Gin Asp Ala Val Ser Arg Thr Gin Arg Arg Gly Arg Thr Gly 275 280 285 Arg Gly Lys Pro Gly He Tyr Arg Phe Val Ala Pro Gly Glu Arg Pro 290 295 300 Ser Gly Met Phe Asp Ser Ser Val Leu Cys Glu Cys Tyr Asp Ala Gly 305 310 315 320 Cys Ala Trp Tyr Glu Leu Thr Pro Ala Glu Thr Thr Val Arg Leu Arg 325 330 335 Ala Tyr Met Asn Thr Pro Gly Leu Pro Val Cys Gin Asp His Leu Glu 340 345 350 Phe Trp Glu Gly Val Phe Thr Gly Leu Thr His He Ala Met Asp Pro 355 360 365 Leu Asp Cys Arg His Ala Lys 370 375 (2) INFORMATION FOR SEQ ID NO: 15: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1414 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:15: GAATTCGTGATCGATTGCAATACGTGTGTC ACCCAGACAGTCX_V\CTTCAG CCTTGACCCT 60 ACCTTCttCCATTGAGAC C^CGCT^^ 120 TCCGGCATGTTTGACTCGJCCGTCXΠ " CTGC GAGTGCTATGACGC^ 240 G^GCΓΓTACACCCGCCGAGACCACAGTTAGGCTACGAGCΓΓΓAC^^ 300 CCCGTGTGCC AAGATCATCTTGAATTTTGG GAGGGCGTCTTTACAGGCCT CACTCATATA 360 TGCCTCATCC GTCTGAAACC GACCCTGCAC GGCCCGACCC CGCTGCTGTA CCX3TCTGGGT 480 GCTGTTCAGAACGAMTCACCCTGACXCAC cXGG^ 540 TCTGCTGATCTAG GTTGTTACCTCTACCTGGGTΓCTGGTTGGTGGTGTTCTGGCT 600 CTGGCTGCTT ACTGCCTGTC GACCGGTTGC GTTGTTATCX3TTGGT 3TGTTGrrrCTGTCT 660 GGTA CCGGCCATTATCθ GGAC _TrGMGTTCTGTACC 720 G TGCTCTCAGCACCTGCCGTACATCG CAGGGTATGATGCTGGCT^ 780 CAG*WVGCTCTGGGm_TOCT 840 GTTCAGACCAACTGGCAGMACTCGAGA(XTTCTGGGCTAMCACATGTGGM 900 TCTGGTATCCAGTA<_X GGCTGGTCTGTCTACX^ 960 TTGATGGCTTTCACCGCTGC TGTTACCTCT CCGCTGACCA CCTCTCAGAC CCTGCTGTTC 1020 MCATTCTGGGTGGTTGGGTTGCTGCTC^GCTGGCTGCTCCGGGTGCT 1080 GTTGGTGCTG GTCTGGCTGG TGCTGCTATC GGTTCTGTAG GCCTGGGTAA AGTTCTGATC 1140 GACATTCTGGCTGGTTACGGTGCTGGTGTTGCTGGAGCTCTGGTTGCπiTCAA^ 1200 TCTGGTGAAGTTCCGTCTACCGAAGATCTG GπMCCTGCTGCCGGCTATCCTGTCTCCG 1260 GGTGCTCTGGTTGTTGGTGTTGfrTTGCGCTG^ 1320 GAAGGTGCTG TTCAGTGGAT GAACCGTCTG ATCGCTTTCG CTTCTCGTGG TAACCACGTT 1380 TCTCCGGTTC ACCACAAACG TTAACCATGG ATCC 1414 (2) INFORMATION FOR SEQ ID NO:16: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 971 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (xi) SEQUENCE DESCRIPTION: SEQ ID NO:16: Met Ser Phe Val Val He He Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 Pro Gly Lys Pro Leu Val Asp lie Asn Gly Lys Pro Met He Val His 20 25 30 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg He He Val Ala 35 40 45 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val lie Val Asn 85 90 95 Val Gin Gly Asp Glu Pro Met He Pro Ala Thr lie He Arg Gin Val 100 105 110 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Val 115 120 125 Pro lie His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr He 145 150 155 160 Pro Trp Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 Asn Phe Leu Arg His Leu Gly lie Tyr Gly Tyr Arg Ala Gly Phe He 180 185 190 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His He Glu Met 195 200 205 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys lie His Val Ala 210 215 220 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 Asp Pro Ser Thr Asn Ser Met Ala Val Asp Phe He Pro Val Glu Asn 245 250 255 Leu Glu Thr Thr Met Arg Ser Pro Val Phe Thr Asp Asn Ser Ser Pro 260 265 270 Pro Val Val Pro Gin Ser Phe Gin Val Ala His Leu His Ala Pro Thr 275 280 285 Gly Ser Gly Lys Ser Thr Lys Val Pro Ala Ala Tyr Ala Ala Gin Gly 290 295 300 Tyr Lys Val Leu Val Leu Asn Pro Ser Val Ala Ala Thr Leu Gly Phe 305 310 315 320 Gly Ala Tyr Met Ser Lys Ala His Gly lie Asp Pro Asn lie Arg Thr 325 330 335 Gly Val Arg Thr lie Thr Thr Gly Ser Pro lie Thr Tyr Ser Thr Tyr 340 345 350 Gly Lys Phe Leu Ala Asp Gly Gly Cys Ser Gly Gly Ala Tyr Asp He 355 360 365 lie lie Cys Asp Glu Cys His Ser Thr Asp Ala Thr Ser lie Leu Gly 370 375 380 lie Gly Thr Val Leu Asp Gin Ala Glu Thr Ala Gly Ala Arg Leu Val 385 390 395 400 Val Leu Ala Thr Ala Thr Pro Pro Gly Ser Val Thr Val Pro His Pro 405 410 415 Asn He Glu Glu Val Ala Leu Ser Thr Thr Gly Glu He Pro Phe Tyr 420 425 430 Gly Lys Ala lie Pro Leu Glu Val He Lys Gly Gly Arg His Leu He 435 440 445 Phe Cys His Ser Lys Lys Lys Cys Asp Glu Leu Ala Ala Lys Leu Val 450 455 460 Ala Leu Gly lie Asn Ala Val Ala Tyr Tyr Arg Gly Leu Asp Val Ser 465 470 475 480 Val He Pro Thr Ser Gly Asp Val Val Val Val Ala Thr Asp Ala Leu 485 490 495 Met Thr Gly Tyr Thr Gly Asp Phe Asp Ser Val He Asp Cys Asn Thr 500 505 510 Cys Val Thr Gin Thr Val Asp Phe Ser Leu Asp Pro Thr Phe Thr He 515 520 525 Glu Thr Thr Thr Leu Pro Gin Asp Ala Val Ser Arg Thr Gin Arg Arg 530 535 540 Gly Arg Thr Gly Arg Gly Lys Pro Gly lie Tyr Arg Phe Val Ala Pro 545 550 555 560 Gly Glu Arg Pro Ser Gly Met Phe Asp Ser Ser Val Leu Cys Glu Cys 565 570 575 Tyr Asp Ala Gly Cys Ala Trp Tyr Glu Leu Thr Pro Aia Glu Thr Thr 580 585 590 Val Arg Leu Arg Ala Tyr Met Asn Thr Pro Gly Leu Pro Val Cys Gin 595 600 605 Asp His Leu Glu Phe Trp Glu Gly Val Phe Thr Gly Leu Thr His lie 610 615 620 Ala Met Asp Ala His Phe Leu Ser Gin Ala Pro Pro Pro Ser Trp Asp 625 630 635 640 Gin Met Trp Lys Cys Leu He Arg Leu Lys Pro Thr Leu His Gly Pro 645 650 655 Thr Pro Leu Leu Tyr Arg Leu Gly Ala Val Gin Asn Glu He Thr Leu 660 665 670 Thr His Pro Val Thr Lys Tyr He Met Thr Cys Met Ser Ala Asp Leu 675 680 685 Glu Val Val Thr Ser Thr Trp Val Leu Val Gly Gly Val Leu Ala Ala 690 695 700 Leu Ala Ala Tyr Cys Leu Ser Thr Gly Cys Val Val He Val Gly Arg 705 710 715 720 Val Val Leu Ser Gly Lys Pro Ala He He Pro Asp Arg Glu Val Leu 725 730 735 Tyr Arg Glu Phe Asp Glu Met Glu Glu Cys Ser Gin His Leu Pro Tyr 740 745 750 lie Glu Gin Gly Met Met Leu Ala Glu Gin Phe Lys Gin Lys Ala Leu 755 760 765 Gly Leu Leu Gin Thr Ala Ser Arg Gin Ala Glu Val He Ala Pro Ala 770 775 780 Val Gin Thr Asn Trp Gin Lys Leu Glu Thr Phe Trp Ala Lys His Met 785 790 795 800 Tφ Asn Phe He Ser Gly lie Gin Tyr Leu Ala Gly Leu Ser Thr Leu 805 810 815 Pro Gly Asn Pro Ala He Ala Ser Leu Met Ala Phe Thr Aia Ala Val 820 825 830 Thr Ser Pro Leu Thr Thr Ser Gin Thr Leu Leu Phe Asn lie Leu Gly 835 840 845 Gly Trp Val Ala Ala Gin Leu Ala Ala Pro Gly Ala Ala Thr Ala Phe 850 855 860 Val Gly Ala Gly Leu Ala Gly Aia Ala He Gly Ser Val Gly Leu Gly 865 870 875 880 Lys Val Leu He Asp He Leu Ala Gly Tyr Gly Ala Gly Val Ala Gly 885 890 895 Ala Leu Val Ala Phe Lys lie Met Ser Gly Glu Val Pro Ser Thr Glu 900 905 910 Asp Leu Val Asn Leu Leu Pro Ala lie Leu Ser Pro Gly Ala Leu Val 915 920 925 Val Gly Val Val Cys Ala Ala He Leu Arg Arg His Val Gly Pro Gly 930 935 940 Glu Gly Ala Val Gin Tφ Met Asn Arg Leu He Ala Phe Ala Ser Arg 945 950 955 960 Gly Asn His Val Ser Pro Val His His Lys Arg 965 970 (2) INFORMATION FOR SEQ ID NO: 17: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 973 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (xi) SEQUENCE DESCRIPTION: SEQ ID NO:17: Met Ser Phe Val Val He He Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 Pro Gly Lys Pro Leu Val Asp He Asn Gly Lys Pro Met He Val His 20 25 30 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg He He Val Ala 35 40 45 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val He Val Asn 85 90 95 Val Gin Gly Asp Glu Pro Met He Pro Ala Thr lie lie Arg Gin Val 100 105 110 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Val 115 120 125 Pro He His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr He 145 150 155 160 Pro Trp Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 Asn Phe Leu Arg His Leu Gly He Tyr Gly Tyr Arg Ala Gly Phe He 180 185 190 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His He Glu Met 195 200 205 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 Asp Pro Ser Thr Asn Ser Met Ala Val Asp Phe He Pro Val Glu Asn 245 250 255 Leu Glu Thr Thr Met Arg Ser Pro Val Phe Thr Asp Asn Ser Ser Pro 260 265 270 Pro Val Val Pro Gin Ser Phe Gin Val Ala His Leu His Ala Pro Thr 275 280 285 Gly Ser Gly Lys Ser Thr Lys Val Pro Ala Ala Tyr Ala Ala Gin Gly 290 295 300 Tyr Lys Val Leu Val Leu Asn Pro Ser Val Ala Ala Thr Leu Gly Phe 305 310 315 320 Gly Ala Tyr Met Ser Lys Ala His Gly He Asp Pro Asn He Arg Thr 325 330 335 Gly Val Arg Thr lie Thr Thr Gly Ser Pro He Thr Tyr Ser Thr Tyr 340 345 350 Gly Lys Phe Leu Ala Asp Gly Gly Cys Ser Gly Gly Ala Tyr Asp He 355 360 365 He He Cys Asp Glu Cys His Ser Thr Asp Ala Thr Ser lie Leu Gly 370 375 380 lie Gly Thr Val Leu Asp Gin Ala Glu Thr Ala Gly Ala Arg Leu Val 385 390 395 400 Val Leu Ala Thr Ala Thr Pro Pro Gly Ser Val Thr Val Pro His Pro 405 410 415 Asn He Glu Glu Val Ala Leu Ser Thr Thr Gly Glu He Pro Phe Tyr 420 425 430 Gly Lys Aia lie Pro Leu Glu Val He Lys Gly Gly Arg His Leu He 435 440 445 Phe Cys His Ser Lys Lys Lys Cys Asp Glu Leu Ala Ala Lys Leu Val 450 455 460 Ala Leu Gly He Asn Ala Val Ala Tyr Tyr Arg Gly Leu Asp Val Ser 465 470 475 480 Val lie Pro Thr Ser Gly Asp Val Val Val Val Ala Thr Asp Ala Leu 485 490 495 Met Thr Gly Tyr Thr Gly Asp Phe Asp Ser Val lie Asp Cys Asn Thr 500 505 510 Cys Val Thr Gin Thr Val Asp Phe Ser Leu Asp Pro Thr Phe Thr He 515 520 525 Glu Thr Thr Thr Leu Pro Gin Asp Ala Val Ser Arg Thr Gin Arg Arg 530 535 540 Gly Arg Thr Gly Arg Gly Lys Pro Gly He Tyr Arg Phe Val Ala Pro 545 550 555 560 Gly Glu Arg Pro Ser Gly Met Phe Asp Ser Ser Val Leu Cys Glu Cys 565 570 575 Tyr Asp Ala Gly Cys Ala Trp Tyr Glu Leu Thr Pro Ala Glu Thr Thr 580 585 590 Val Arg Leu Arg Ala Tyr Met Asn Thr Pro Gly Leu Pro Val Cys Gin 595 600 605 Asp His Leu Glu Phe Trp Glu Gly Val Phe Thr Gly Leu Thr His lie 610 615 620 Ala Met Asp Ala His Phe Leu Ser Gin Thr Lys Gin Ser Gly Glu Asn 625 630 635 640 Leu Pro Tyr Leu Val Ala Tyr Gin Ala Thr Val Cys Ala Arg Ala Gin 645 650 655 Ala Pro Thr Pro Leu Leu Tyr Arg Leu Gly Ala Val Gin Asn Glu lie 660 665 670 Thr Leu Thr His Pro Val Thr Lys Tyr lie Met Thr Cys Met Ser Ala 675 680 685 Asp Leu Glu Val Val Thr Ser Thr Trp Val Leu Val Gly Gly Val Leu 690 695 700 Ala Ala Leu Ala Ala Tyr Cys Leu Ser Thr Gly Cys Val Val lie Val 705 710 715 720 Gly Arg Val Val Leu Ser Gly Lys Pro Ala lie He Pro Asp Arg Glu 725 730 735 Val Leu Tyr Arg Glu Phe Asp Glu Met Glu Glu Cys Ser Gin His Leu 740 745 750 Pro Tyr He Glu Gin Gly Met Met Leu Ala Glu Gin Phe Lys Gin Lys 755 760 765 Ala Leu Gly Leu Leu Gin Thr Ala Ser Arg Gin Ala Glu Val He Ala 770 775 780 Pro Ala Val Gin Thr Asn Trp Gin Lys Leu Glu Thr Phe Trp Ala Lys 785 790 795 800 His Met Trp Asn Phe He Ser Gly He Gin Tyr Leu Ala Gly Leu Ser 805 810 815 Thr Leu Pro Gly Asn Pro Ala lie Ala Ser Leu Met Ala Phe Thr Ala 820 825 830 Ala Val Thr Ser Pro Leu Thr Thr Ser Gin Thr Leu Leu Phe Asn He 835 840 845 Leu Gly Gly Trp Val Ala Ala Gin Leu Ala Ala Pro Gly Ala Ala Thr 850 855 860 Ala Phe Val Gly Ala Gly Leu Ala Gly Ala Ala He Gly Ser Val Gly 865 870 875 880 Leu Gly Lys Val Leu He Asp lie Leu Ala Gly Tyr Gly Ala Gly Val 885 890 895 Ala Gly Ala Leu Val Ala Phe Lys lie Met Ser Gly Glu Val Pro Ser 900 905 910 Thr Glu Asp Leu Val Asn Leu Leu Pro Ala He Leu Ser Pro Gly Ala 915 920 925 Leu Val Val Gly Val Val Cys Ala Ala He Leu Arg Arg His Val Gly 930 935 940 Pro Gly Glu Gly Ala Val Gin Trp Met Asn Arg Leu He Ala Phe Ala 945 950 955 960 Ser Arg Gly Asn His Val Ser Pro Val His His Lys Arg 965 970 (2) INFORMATION FOR SEQ ID NO: 18: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 992 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (xi) SEQUENCE DESCRIPTION: SEQ ID NO:18: Met Ser Phe Val Val He He Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 Pro Gly Lys Pro Leu Val Asp He Asn Gly Lys Pro Met lie Val His 20 25 30 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg He He Val Ala 35 40 45 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val lie Val Asn 85 90 95 Val Gin Gly Asp Glu Pro Met lie Pro Ala Thr He He Arg Gin Val 100 105 1 10 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Val 115 120 125 Pro He His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr He 145 150 155 160 Pro Trp Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 Asn Phe Leu Arg His Leu Gly lie Tyr Gly Tyr Arg Ala Gly Phe He 180 185 190 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His He Glu Met 195 200 205 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 Asp Pro Ser Thr Asn Ser Met Ala Val Asp Phe He Pro Val Glu Asn 245 250 255 Leu Glu Thr Thr Met Arg Ser Pro Val Phe Thr Asp Asn Ser Ser Pro 260 265 270 Pro Val Val Pro Gin Ser Phe Gin Val Ala His Leu His Ala Pro Thr 275 280 285 Gly Ser Gly Lys Ser Thr Lys Val Pro Ala Ala Tyr Ala Ala Gin Gly 290 295 300 Tyr Lys Val Leu Val Leu Asn Pro Ser Val Ala Ala Thr Leu Gly Phe 305 310 315 320 Gly Ala Tyr Met Ser Lys Ala His Gly lie Asp Pro Asn He Arg Thr 325 330 335 Gly Val Arg Thr He Thr Thr Gly Ser Pro He Thr Tyr Ser Thr Tyr 340 345 350 Gly Lys Phe Leu Ala Asp Gly Gly Cys Ser Gly Gly Ala Tyr Asp He 355 360 365 He He Cys Asp Glu Cys His Ser Thr Asp Ala Thr Ser lie Leu Gly 370 375 380 He Gly Thr Val Leu Asp Gin Ala Glu Thr Aia Gly Ala Arg Leu Val 385 390 395 400 Val Leu Ala Thr Ala Thr Pro Pro Gly Ser Val Thr Val Pro His Pro 405 410 415 Asn He Glu Glu Val Ala Leu Ser Thr Thr Gly Glu lie Pro Phe Tyr 420 425 430 Gly Lys Ala He Pro Leu Glu Val He Lys Gly Gly Arg His Leu lie 435 440 445 Phe Cys His Ser Lys Lys Lys Cys Asp Glu Leu Ala Ala Lys Leu Val 450 455 460 Ala Leu Gly lie Asn Ala Val Ala Tyr Tyr Arg Gly Leu Asp Val Ser 465 470 475 480 Val He Pro Thr Ser Gly Asp Val Val Val Val Ala Thr Asp Ala Leu 485 490 495 Met Thr Gly Tyr Thr Gly Asp Phe Asp Ser Val lie Asp Cys Asn Thr 500 505 510 Cys Val Thr Gin Thr Val Asp Phe Ser Leu Asp Pro Thr Phe Thr He 515 520 525 Glu Thr Thr Thr Leu Pro Gin Asp Ala Val Ser Arg Thr Gin Arg Arg 530 535 540 Gly Arg Thr Gly Arg Gly Lys Pro Gly lie Tyr Arg Phe Val Ala Pro 545 550 555 560 Gly Glu Arg Pro Ser Gly Met Phe Asp Ser Ser Val Leu Cys Glu Cys 565 570 575 Tyr Asp Ala Gly Cys Ala Trp Tyr Glu Leu Thr Pro Ala Glu Thr Thr 580 585 590 Val Arg Leu Arg Ala Tyr Met Asn Thr Pro Gly Leu Pro Val Cys Gin 595 600 605 Asp His Leu Glu Phe Trp Glu Gly Val Phe Thr Gly Leu Thr His lie 610 615 620 Ala Met Asp Ala His Phe Leu Ser Gin Thr Lys Gin Ser Gly Glu Asn 625 630 635 640 Leu Pro Tyr Leu Val Ala Tyr Gin Ala Thr Val Cys Ala Arg Ala Gin 645 650 655 Ala Pro Ser Tφ Asp Gin Met Trp Lys Cys Leu lie Arg Leu Lys Pro 660 665 670 Thr Leu His Gly Pro Thr Pro Leu Leu Tyr Arg Leu Gly Ala Val Gin 675 680 685 Asn Glu lie Thr Leu Thr His Pro Val Thr Lys Tyr He Met Thr Cys 690 695 700 Met Ser Ala Asp Leu Glu Val Val Thr Ser Thr Trp Val Leu Val Gly 705 710 715 720 Gly Val Leu Ala Ala Leu Ala Ala Tyr Cys Leu Ser Thr Gly Cys Val 725 730 735 Val He Val Gly Arg Val Val Leu Ser Gly Lys Pro Ala He He Pro 740 745 750 Asp Arg Glu Val Leu Tyr Arg Glu Phe Asp Glu Met Glu Glu Cys Ser 755 760 765 Gin His Leu Pro Tyr He Glu Gin Gly Met Met Leu Ala Glu Gin Phe 770 775 780 Lys Gin Lys Ala Leu Gly Leu Leu Gin Thr Ala Ser Arg Gin Ala Glu 785 790 795 800 Val lie Ala Pro Ala Val Gin Thr Asn Trp Gin Lys Leu Glu Thr Phe 805 810 815 Trp Ala Lys His Met Tφ Asn Phe lie Ser Gly He Gin Tyr Leu Ala 820 825 830 Gly Leu Ser Thr Leu Pro Gly Asn Pro Ala lie Ala Ser Leu Met Ala 835 840 845 Phe Thr Ala Ala Val Thr Ser Pro Leu Thr Thr Ser Gin Thr Leu Leu 850 855 860 Phe Asn lie Leu Gly Gly Tφ Val Ala Ala Gin Leu Ala Ala Pro Gly 865 870 875 880 Aia Ala Thr Ala Phe Val Gly Ala Gly Leu Ala Gly Ala Ala lie Gly 885 890 895 Ser Val Gly Leu Gly Lys Val Leu He Asp He Leu Ala Gly Tyr Gly 900 905 910 Ala Gly Val Ala Gly Ala Leu Val Ala Phe Lys He Met Ser Gly Glu 915 920 925 Val Pro Ser Thr Glu Asp Leu Val Asn Leu Leu Pro Ala He Leu Ser 930 935 940 Pro Gly Ala Leu Val Val Gly Val Val Cys Ala Ala He Leu Arg Arg 945 950 955 960 His Val Gly Pro Gly Glu Gly Ala Val Gin Trp Met Asn Arg Leu lie 965 970 975 Ala Phe Ala Ser Arg Gly Asn His Val Ser Pro Val His His Lys Arg 980 985 990 (2) INFORMATION FOR SEQ ID NO:19: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (xi) SEQUENCE DESCRIPTION: SEQ ID NO:19: Pro Pro Pro Ser Tyr Asp Gin Met Tφ Lys Cys Leu He Arg Leu Lys 1 5 10 15 Pro Thr Leu His Giy 20 (2) INFORMATION FOR SEQ ID NO:20: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 382 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO.20: CTCCACTCTA TGAATTCGTG ATCGATTGCA ATACGTGTGT CACCCAGACA GTCGACTTCA 60 GCCTTGACCCTACCTTCACCATTGAGAC CCACGCTTrc 120 CTCAQOG DGQGQCΛQGAlCT 180 GGGAGOGCCCπCCCGCATGTTTGACTCGTCCGTCXπ^ 240 GTGCTTGGTATGAGCnTACACCCGCCGAGAC^^ 300 CTra3GGGCTTCCCGTGTGCC GATCATCTT^ 360 TCACTCATATAGCCATGGAT CC 382 (2) INFORMATION FOR SEQ ID NO:21: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1420 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:21: GAATTCGTGATCGATTGCAATACGTGTGTC ACCCAGACAGTCGACTTCAG CCTTGACCCT 60 ACCπTCΑCCATTGAGACMC ( ^ 3C rCCCCAGGATGCTGT^ 120 TC _-CATGTTTGACTCXTO 240 G^GCΠTACACCCGCCGAGACCACAGTTAGG CTACGAGCΠTACATG ^^ 300 CCCGTGTGCC AAGATCATCTTGAATTTTGG GAGGGCGTCTTTACAGGCCT CACTCATATA 360 GCCATGGACG CTCACTTCCT GTCTCAGACC AAACAGTCTG GTGAAAACCTTCCGTACCTG 420 GTTGCΠACCAGGCTACO_Π " TTGCGCTCGTGCTCAGGCCCCG^ 480 CTGGGTOCTCT7OAGAA _X3A 540 TGCATGTCTG CTGATCTAGA AGTTGTTACCTCTACCTGGGTTCTGGTTGGTGGTGTTCTG 600 GCTGCTCTGG CTGCTTACTG CCTGTCGACC GGTTGCG^ 660 CTGTCTGGTAMCCGGCCATTATCCXXX_^ 720 ATGGAAGAATGCTCTCAQCACC GT^ 780 TTCA CAGAMGCTCTGGGTCTGCTGCAGACXX_CTTCT^ 840 OX_X-X_TGΠCAGΑCCMCTGGC^^ 900 TTCATCTCTG GTATCCAGTACCTGGCTGGTCTGTCTACCCTGCCGGGTMCCCGGCTATC 960 GCAAGCΠTGATGGCTTTCAC ( ^GCTGCTGTTACCTCTCCGCTGACX-AC^ 1020 CTGTTC ^CATTCTGGCTGGTTGGGTTGCTGCT 1080 GCTTTCGTTGGTGCTGGTCTGGCTGGTGCTGCTATCGGΠCTGTAGGCCTGGGTAMGΠ 1140 CTGATCXIV\CATTCTGGCTGGTTACGGTGCTGGTGΓΓGCTGG^GCTCT 1200 ATCATGTCTG GTTGAAGTTCC GTCTACCGAA GATCTGGTTA ACCTGCTGCC GGCTATCCTG 1260 TCTCCGGGTG CTCTGGTTCTTGGTGTTGTTTGCGCTGCTATCCTGCGTCGTCACGTTGGC 1320 CCGGGTGAAG GTGCTGTTCAGTGGATGAAC CGTCTGATCG CTRTCGCTTCTCGTGGTAAC 1380 CACGTTTCTC CGGTTCACCA CAAACGTTAA CCATGGATCC 1420 (2) INFORMATION FOR SEQ ID NO:22: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4481 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: circular (ii) MOLECULE TYPE: DNA (genomic) (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 130..1317 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:22: GAATTAATTC CCATTAATGTGAGTTAGCTC ACTCATTAGG CACCCCAGGCTTTACACTTT 60 ATGTTCCGGCTCGTATTTTGTGTGGAATTGT^ 120 GAGGTTTAAATG AGTTTTGTG GTC ATTATTCCCGCG CGCTAC GCGTCG 168 Met Ser Phe Val Val lie lie Pro Ala Arg Tyr Ala Ser 1 5 10 ACGCGTCTGCCCGGTAAACCATTGGTTGATATTAACGGCAAACCCATG 216 Thr Arg Leu Pro Gly Lys Pro Leu Val Asp He Asn Gly Lys Pro Met 15 20 25 ATTGTTCATGTTCTTGMCGCGCGCGTGAATCAGGTGCCGAG CGCATC 264 He Val His Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg lie 30 35 40 45 ATCGTGGCAACCGATCATGAGGATGTTGCCCGCGCCGTTGAAGCCGCT 312 He Val Ala Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala 50 55 60 GGC GGT GAA GTA TGT ATG ACG CGC GCC GAT CAT CAG TCA GGA ACA GAA 360 Gly Gly Glu Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu 65 70 75 CGTCTGGCGGAAGTTGTCGAAAAATGC GCATTCAGCGACGACACGGTG 408 Arg Leu Aia Glu Val Val Glu Lys Cys Aia Phe Ser Asp Asp Thr Val 80 85 90 ATC GTT AAT GTG CAG GGT GAT GAA CCG ATG ATC CCT GCG ACA ATC ATT 456 He Val Asn Val Gin Gly Asp Glu Pro Met lie Pro Ala Thr lie lie 95 100 105 CGT CAG GTTGCTGATAACCTCGCTCAG CGT CAG GTG GGTATGGCG ACT 504 Arg Gin Val Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr 110 115 120 125 CTGGCGGTG X.AATCCACMTG03GMGMGCX3TTTAACCCGAATGCG 552 Leu Ala Val Pro He His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala 130 135 140 GTG AAA GTG GTT CTC GAC GCT GAA GGG TAT GCA CTG TAC TTC TCT CGC 600 Val Lys Val Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg 145 150 155 GCCACC ATTCCTTGG GATCGTGATCGTTTTGCAGAA GGCCTTGAAACC 648 Ala Thr He Pro Tφ Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr 160 165 170 GTT GGC GAT AAC TTC CTG CGT CAT CTT GGT ATT TAT GGC TAC CGT GCA 696 Val Gly Asp Asn Phe Leu Arg His Leu Gly He Tyr Gly Tyr Arg Ala 175 180 185 GGCTTTATC CGTCGTTAC GTCAACTGG CAG CCAAGTCCGTTA GAACAC 744 Gly Phe He Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His 190 195 200 205 ATC GAA ATG TTA GAG CAG CTT CGT GTT CTG TGG TAC GGC GAA AAA ATC 792 lie Glu Met Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys lie 210 215 220 CATGTTGCTGTTGCTCAG GAAGTTCCTGGCACAGGTGTGGATACC CCT 840 His Val Ala Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro 225 230 235 GAAGATCTCGAC CCGTCGACGAATTCCATGTCTACCAACCCGAAA CCG 888 Glu Asp Leu Asp Pro Ser Thr Asn Ser Met Ser Thr Asn Pro Lys Pro 240 245 250 CAG AAA AAA AAC AAA CGT AAC ACC AAC CGT CGT CCG CAG GAC GTT AAA 936 Gin Lys Lys Asn Lys Arg Asn Thr Asn Arg Arg Pro Gin Asp Val Lys 255 260 265 TTC CCG GGT GGT GGT CAG ATC GTT GGT GGT GTTTAC CTG CTG CCG CGT 984 Phe Pro Gly Gly Gly Gin lie Val Gly Gly Val Tyr Leu Leu Pro Arg 270 275 280 285 CGTGGTCCGCGTCTGGGTGTTCGTGCTACGCGTAAAACCTCTGAACGT 1032 Arg Gly Pro Arg Leu Gly Val Arg Ala Thr Arg Lys Thr Ser Glu Arg 290 295 300 TCTCAGC∞CXSTGGGCGTCGTCAGCCGATCCCGAAAGCTCGTCGTCCG 1080 Ser Gin Pro Arg Gly Arg Arg Gin Pro lie Pro Lys Ala Arg Arg Pro 305 310 315 GAAGGTCGTACCTGGGCTCAGCCGGGTTACCCGTGGCCGCTGTACGGT 1128 Glu Gly Arg Thr Trp Ala Gin Pro Gly Tyr Pro Trp Pro Leu Tyr Gly 320 325 330 AAC GAA GGTTGC GGTTGG GCT GGTTGG CTG CTG TCT CCG CGTGGATCT 1176 Asn Glu Gly Cys Gly Tφ Ala Gly Trp Leu Leu Ser Pro Arg Gly Ser 335 340 345 CGTCXX3TCTTGGGGTCCGA∞GACCXX3CX3TCGTCGTTCTCGTAACCTT 1224 Arg Pro Ser Trp Gly Pro Thr Asp Pro Arg Arg Arg Ser Arg Asn Leu 350 355 360 365 GGT AAA GTT ATC GAT ACC CTG ACC TGC GGTTTC GCT GAC CTG ATG GGT 1272 Gly Lys Val He Asp Thr Leu Thr Cys Gly Phe Ala Asp Leu Met Gly 370 375 380 TACATACCGCTGGTTGGAGCTCCGCTGGGTGGTGCTGCTCGTGCT 1317 Tyr He Pro Leu Val Gly Ala Pro Leu Gly Gly Ala Ala Arg Ala 385 390 395 T CCCATGGATCCTCTAGACTGCAGGCATGCTMGTMGTAGATCTTGAGCGCGπ 1377 GCTGAAATGC GCTAATTTCA CTTCACGΛCA CTTCAGCCAATTTTGGGAGG AGTGTCGTAC 1437 CGTTACGATTTTCCTCMTTTTTCTTTTCAACMTTGATCTCATTCAGGTGACATCTTTT 1497 ATATTGGCGCTCATTATG AGCAGTAGCTTITATGAGGGTMTCTGMTGGAAC^ 1557 CGTGCCX3AATTAAGCCATTT ACTGGGCGAA AAACTCAGTC GTATTGAGTG CGTCAATGAA 1617 AMGCGGΛTACGGCGTTCTGGGCTTTGTATGACAGCCAGGGAMCCCM 1677 GC GMGCTTAGCCCGCCTMTGAGCGGGCI 1 1 1 1 1 1 ICGACGCGAGGCTGGATGGCCT 1737 TCCCXATTATGATTCCTTCTCGCTTCCGGCX3GC_ΛTCGGGAT 1797 TGTCCAGGCAG<_flAGATGACGACCATC^^ 1857 CCAGCCTMCπCGATCACTGKlWCCGCTGATCGTCACGGCGATTTAT 1917 GCΛCATQGMOGGGfTTGGCATQGAT^ 1977 CGTTGCGTCGCGGTGCATGGAGCCGGGCCACXTCXIVkCCT 20S7 CGCTMCX3GATTCAOCACTCCMGMTTGGAGCCMTC TT 2097 TGCGCAM∞ CCCπGGCAGMGATATC 2157 GCGGCGCATCTCGGGCAGCGTTGGCTO^^ 2217 GTTGAGGACX. CGGCTAGGCTGGCGGGGTTGCCTTACTGCTTAGCAG TGM 2277 ACGCG^GCGAACGTGAAGCGACTGCTGCTGCWW\CGTCTGCGACCTG^^ 2337 MTGGTCTTCGGTTTCCGTGTTTCGTA GTCTGGA CGCGGMGTCAGCGC^ 2397 CATTATGTTC CGGATCTGCATCGCAGGATG CTGCTGGCTACCCTGTGGAACACCTACATC 2457 TGTATTAACGAAQαΞK rCTTCCGCT 2517 GGCTGCGGCGAGCGCTATCAGCT ^CTC^AGGCGCT 2577 GGGATMCGCAGGAMGAACATCTGAGC MGGCX^GCAAMGGCC^ 2637 AC_ _X_XX_πTGCTXXXX_ππ 2697 GACGCTC \GTC^GAGGTGG O_W\ACCA3AC^ 2757 CTOGAACΞ CCCTO-ΠGCXΞC^ 2817 CCΓΓTCTCCCTTCGGG GC GJGGCGCTTTCTCMTGCTCACGCTGT^ 2877 CGCTGTAGCTCGTTCGCTCCMGCTGGGCTGTCTGCACGAA^ 2937 GCTGCGCCTT ATCCGGTAAC TATCGTCTTG AGTCCAACCC GGTAAGACAC GACTTATCGC 2997 CACTGGC^GCAGO^CTGGTMC^GGATTAGCAGAGCGAGCTATCTAGG^ 3057 AGTTCTTGAAGTGCTGGCCTAACTACGGCTACACTAGAAG GACAGTATTTGGTATCTGCG 3117 CTCTGCTG GCC \GTTACCTTCGGAAAMGAGTTGCTAGCTCTTGATCCGGCA 3177 CCACCGCTGGTAGCGGTGGT 1 1 I I I IGTTTGCMGCAGCAGATTACX_ 3CAGAAAAAAAG 3237 GATCTC GAAGATCCΓΓTGATCTTTTCTACGGGGTCTGACGCTC^^ 3297 CACGTTAAGG GATTTTGGTC ATGAGATTAT CAAAAAGGAT CTTCACCTAG ATCCTTTTAA 3357 ATTAAAAATG AAGTTTTAAA TCAATCTAAA GTATATATGA GTAAACTTGG TCTGACAGTT 3417 ACCAATGCTT AATCAGTGAG GCACCTATCT CAGCGATCTG TCTATTTCGTTCATCCATAG 3477 ΠGCCTGACTCCCCGTCCTGTAGATMCTACGAT^^ 3537 GTGCTGC TGATACXXACGAGACCCACGCTCAC^^ 3597 AGCCAGCCGGMGGGCCGAGCGCAG CTGGTCCTGCMCTTT^^ 3657 CTATTAATTG TTGCCGGGAA GCTAGAGTAA GTAGTTCGCC AGTTAATAGTTTGCGCAACG 3717 TTGTTGCCATTGCTACAGGC ATCGTGGTGT CACGCTCGTC GTTTGGTATG GCTTCATTCA 3777 GCTCCGGTTCCC CXSATCAAGGCGAGTTACATGATCCCCCATGπGTGC 3837 πAGCTCCπCGGTCCTCCGATCGπGTCAG ^ 3897 TGGTTATGGCAGCACTGCATMTTCTCTTACTGTCATG∞^ 3957 T(_ttCTGGTGAGTACTC <λCCMGTCA^ 4017 TCATTGGA ACGπCTTCGGGGCGAAMCTCTC GGATCTTACCGCTGπ 4137 GTTCGATGTAACCCACTCGTGCAOXMCTGAT^^ 4197 TTTCTOGGTGAGCAAAMCAGG GGCA ATGCCGC \AAMGG^ 4257 GGAAATGTTG AATACTCATA CTCTTCCTTTTTCAATATTATTGAAGCATTTATCAGGGTT 4317 ATTGTCTC AT GAGCGGATAC ATATTTGAAT GTATTTAGAA AAATAAACAA ATAGGGGTTC 4377 CXI XSCACATTTCCCCGAAAA GTGCCACCTG ACGTCTAAGA AACCATTATT ATCATGACAT 4437 TAACCTATAA AAATAGGCGT ATCACGAGGC CCTTTCGTCTTCAA 4481 (2) INFORMATION FOR SEQ ID NO:23: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 396 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:23: Met Ser Phe Val Val He He Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 Pro Gly Lys Pro Leu Val Asp lie Asn Gly Lys Pro Met He Val His 20 25 30 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg He He Val Ala 35 40 45 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val He Val Asn 85 90 95 Val Gin Gly Asp Glu Pro Met He Pro Ala Thr He We Arg Gin Val 100 105 1 10 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Val 115 120 125 Pro He His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr He 145 150 155 160 Pro Tφ Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 Asn Phe Leu Arg His Leu Gly lie Tyr Gly Tyr Arg Ala Gly Phe He 180 185 190 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His He Glu Met 195 200 205 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 Asp Pro Ser Thr Asn Ser Met Ser Thr Asn Pro Lys Pro Gin Lys Lys 245 250 255 Asn Lys Arg Asn Thr Asn Arg Arg Pro Gin Asp Val Lys Phe Pro Gly 260 265 270 Gly Gly Gin lie Val Gly Gly Val Tyr Leu Leu Pro Arg Arg Gly Pro 275 280 285 Arg Leu Gly Val Arg Ala Thr Arg Lys Thr Ser Glu Arg Ser Gin Pro 290 295 300 Arg Gly Arg Arg Gin Pro He Pro Lys Ala Arg Arg Pro Glu Gly Arg 305 310 315 320 Thr Trp Ala Gin Pro Gly Tyr Pro Trp Pro Leu Tyr Gly Asn Glu Gly 325 330 335 Cys Gly Trp Ala Gly Trp Leu Leu Ser Pro Arg Gly Ser Arg Pro Ser 340 345 350 Tφ Gly Pro Thr Asp Pro Arg Arg Arg Ser Arg Asn Leu Gly Lys Val 355 360 365 He Asp Thr Leu Thr Cys Gly Phe Ala Asp Leu Met Gly Tyr We Pro 370 375 380 Leu Val Gly Ala Pro Leu Gly Gly Ala Ala Arg Ala 385 390 395 (2) INFORMATION FOR SEQ ID NO:24: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 5600 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: circular (ii) MOLECULE TYPE: DNA (genomic) (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 130..2472 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:3: GAATTAATTC CCATTAATGTGAGTTAGCTC ACTCATTAGG CACCCCAGGCTTTACACTTT 60 ATGTTCCGGCTCGTATTTTGTGTGGAATTGTGAGCGGATAACMTTGGGCATCCAG^ 120 GAGGTTTAA ATG AGT TTT GTG GTC ATT ATT CCC GCG CGC TAC GCG TCG 168 Met Ser Phe Val Val lie He Pro Ala Arg Tyr Ala Ser 1 5 10 ACGCX3TCTGCCCGGTAAACCATTGGTTGATATTAACGGCAAACCCATG 216 Thr Arg Leu Pro Gly Lys Pro Leu Val Asp lie Asn Gly Lys Pro Met 15 20 25 ATTGTTCATGTTCTTGAACGCGCGCGTGAATCAGGTGCCGAGCGCATC 264 He Val His Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg He 30 35 40 45 ATCGTGGCAACCGATCATGAGGATGTTGCCCGCGCCGTTGAAGCCGCT 312 lie Val Ala Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala 50 55 60 GGC GGT GAA GTATGT ATG ACG CGC GCC GAT CAT CAGTCA GGA ACA GAA 360 Gly Gly Glu Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu 65 70 75 CGTCTGGCGGAAGTTGTCGAAAAATGCGCATTCAGCGACGACACGGTG 408 Arg Leu Ala Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val 80 85 90 ATC GTTAATGTGCAGGGTGATGAACCGATGATCCCTGCGACAATCATT 456 lie Val Asn Val Gin Gly Asp Glu Pro Met He Pro Ala Thr He He 95 100 105 CGT CAG GTT GCT GAT AAC CTCGCTCAG CGT CAG GTG GGT ATG GCG ACT 504 Arg Gin Val Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr 110 115 120 125 CTGGCG GTGCCAATCCACMTGCGGMGMG _.TTTAACCCGAATGCG 552 Leu Ala Val Pro He His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala 130 135 140 GTG AAA GTG GTT CTC GAC GCT GAA GGG TAT GCA CTG TAC TTC TCT CGC 600 Val Lys Val Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg 145 150 155 GCC ACC ATTCCTTGG GAT CGT GAT CGT TTT GCA GAA GGC CTT GAA ACC 648 Ala Thr He Pro Tφ Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr 160 165 170 GTTGGC GATAACTTC CTG CGTCATCTT GGTATTTATGGCTAC CGTGCA 696 Val Gly Asp Asn Phe Leu Arg His Leu Gly He Tyr Gly Tyr Arg Ala 175 180 185 GGC TTT ATC CGT CGTTAC GTC AAC TGG CAG CCA AGT CCG TTA GAA CAC 744 Gly Phe He Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His 190 195 200 205 ATC GAA ATG TTA GAG CAG CTT CGT GTT CTG TGG TAC GGC GAA AAA ATC 792 He Glu Met Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He 210 215 220 CAT GTT GCT GTT GCT CAG GAA GTT CCT GGC ACA GGT GTG GAT ACC CCT 840 His Val Ala Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro 225 230 235 GAA GAT CTC GAC CCG TCG ACG AAT TOO ATG GCT GTT GAC TTT ATC CCG 888 Glu Asp Leu Asp Pro Ser Thr Asn Ser Met Ala Val Asp Phe He Pro 240 245 250 GTT GAA AAT CTC GAG ACT ACT ATG CGT TCT CCG GTT TTC ACT GAC AAC 936 Val Glu Asn Leu Glu Thr Thr Met Arg Ser Pro Val Phe Thr Asp Asn 255 260 265 TCTTCT CCG CCG GTT GTT CCG CAG TCTTTC CAG GTT GCT CAC CTG CAT 984 Ser Ser Pro Pro Val Val Pro Gin Ser Phe Gin Val Ala His Leu His 270 275 280 285 GCT CCG ACT GGTTCT GGT AAA TCT ACT AM GTT CCA GCT GCTTAC GCT 1032 Ala Pro Thr Gly Ser Gly Lys Ser Thr Lys Val Pro Ala Ala Tyr Ala 290 295 300 GCT CAG GGT TAC AAA GTT CTG GTT CTG AAC CCG TCT GTT GCT GCT ACT 1080 Ala Gin Gly Tyr Lys Val Leu Val Leu Asn Pro Ser Val Ala Ala Thr 305 310 315 CTG GGT TTC GGC GCC TAC ATG TCT AAA GCT CAC GGT ATC GAC CCG AAC 1128 Leu Gly Phe Gly Ala Tyr Met Ser Lys Ala His Gly lie Asp Pro Asn 320 325 330 ATT CGT ACT GGT GTA CGT ACT ATC ACT ACT GGT TCT CCG ATC ACT TAC 1176 He Arg Thr Gly Val Arg Thr He Thr Thr Gly Ser Pro He Thr Tyr 335 340 345 TCT ACTTAC GGT AAA TTC CTG GCT GAC GGT GGTTGC TCT GGT GGT GCT 1224 Ser Thr Tyr Gly Lys Phe Leu Ala Asp Gly Gly Cys Ser Gly Gly Ala 350 355 360 365 TAC GAT ATC ATC ATC TGC GAC GAA TGC CAC TCT ACT GAC GCTACTTCT 1272 Tyr Asp lie He He Cys Asp Glu Cys His Ser Thr Asp Ala Thr Ser 370 375 380 ATC CTG GGT ATC GGT ACC GTT CTG GAC CAG GCT GAA ACT GCA GGT GCT 1320 He Leu Gly He Gly Thr Val Leu Asp Gin Ala Glu Thr Ala Gly Ala 385 390 395 CGT CTG GTT GTT CTG GCT ACT GCT ACT CCG CCG GGT TCT GTT ACT GTT 1368 Arg Leu Val Val Leu Ala Thr Ala Thr Pro Pro Gly Ser Val Thr Val 400 405 410 CCG CAC CCG AAC ATC GAA GAA GTT GCT CTG TCG ACT ACT GGT GAA ATC 1416 Pro His Pro Asn He Glu Glu Val Ala Leu Ser Thr Thr Gly Glu He 415 420 425 CCGTTCTACGGTAAAGCTATCCCGCTCGAG GTTATCAAAGGTGGTCGT 1464 Pro Phe Tyr Gly Lys Ala lie Pro Leu Glu Val He Lys Gly Gly Arg 430 435 440 445 CACCTG ATTTTCTGC CACTCTAAA AAA AAATGC GAC GAA CTG GCT GCT 1512 His Leu He Phe Cys His Ser Lys Lys Lys Cys Asp Glu Leu Ala Ala 450 455 460 AAG CTTGTTGCTCTG GGTATCAACGCTGTTGCTTACTAC CGTGGTCTG 1560 Lys Leu Val Ala Leu Gly He Asn Ala Val Ala Tyr Tyr Arg Gly Leu 465 470 475 GAC GTTTCTGTTATC CCG ACT TCT GGT GAC GTT GTT GTT GTG GCC ACT 1608 Asp Val Ser Val He Pro Thr Ser Gly Asp Val Val Val Val Ala Thr 480 485 490 GAC GCT CTG ATG ACT GGT TAC ACT GGT GAC TTC GAC TCT GTT ATC GAT 1656 Asp Ala Leu Met Thr Gly Tyr Thr Gly Asp Phe Asp Ser Val He Asp 495 500 505 TGC AAC ACTTGC AATTCG TCG ACC GGTTGC GTT GTT ATC GTT GGT CGT 1704 Cys Asn Thr Cys Asn Ser Ser Thr Gly Cys Val Val He Val Gly Arg 510 515 520 525 GTTGTTCTGTCTGGTAAACCG GCCATTATC CCG GAC CGTGAAGTTCTG 1752 Val Val Leu Ser Gly Lys Pro Ala He He Pro Asp Arg Glu Val Leu 530 535 540 TACCGTGAGTTCGACGAAATGGAAGAATGCTCTCAG CACCTGCCGTAC 1800 Tyr Arg Glu Phe Asp Glu Met Glu Glu Cys Ser Gin His Leu Pro Tyr 545 550 555 ATC GAA CAG GGT ATG ATG CTG GCT GAA CAG TTC AAA CAG AAA GCT CTG 1848 lie Glu Gin Gly Met Met Leu Ala Glu Gin Phe Lys Gin Lys Ala Leu 560 565 570 GGT CTG CTG CAG ACC GCTTCT CGT CAG GCT GAA GTT ATC GCT CCG GCT 1896 Gly Leu Leu Gin Thr Ala Ser Arg Gin Ala Glu Val lie Ala Pro Ala 575 580 585 GTT CAG ACC AAC TGG CAG AAA CTC GAG ACC TTC TGG GCT AAA CAC ATG 1944 Val Gin Thr Asn Trp Gin Lys Leu Glu Thr Phe Trp Ala Lys His Met 590 595 600 605 TGG AAC TTC ATC TCT GGT ATC CAG TAC CTG GCT GGT CTG TCT ACC CTG 1992 Tφ Asn Phe lie Ser Gly We Gin Tyr Leu Ala Gly Leu Ser Thr Leu 610 615 620 CCGGGTAACCCG GCTATCGCAAGCTTGATGGCTTTCACCGCTGCTGTT 2040 Pro Gly Asn Pro Ala He Ala Ser Leu Met Ala Phe Thr Ala Ala Val 625 630 635 ACC TCT CCG CTG ACC ACC TCT CAG ACC CTG CTG TTC AAC ATT CTG GGT 2088 Thr Ser Pro Leu Thr Thr Ser Gin Thr Leu Leu Phe Asn He Leu Gly 640 645 650 GGTTGG GTT GCT GCT CAG CTG GCT GCT CCG GGT GCT GCT ACC GCTTTC 2136 Gly Tφ Val Ala Ala Gin Leu Ala Ala Pro Gly Ala Ala Thr Ala Phe 655 660 665 GTT GGT GCT GGT CTG GCT GGT GCT GCT ATC GGT TCT GTA GGC CTG GGT 2184 Val Gly Ala Gly Leu Ala Gly Ala Ala He Gly Ser Val Gly Leu Gly 670 675 680 685 AAAGTTCTGATCGACATTCTGGCTGGTTACGGTGCTGGTGTTGCTGGA 2232 Lys Val Leu He Asp lie Leu Ala Gly Tyr Gly Ala Gly Val Ala Gly 690 695 700 GCTCTGGTTGCTTTCAAAATCATGTCTGGTGAAGTTCCGTCTACC GAA 2280 Ala Leu Val Ala Phe Lys He Met Ser Gly Glu Val Pro Ser Thr Glu 705 710 715 GAT CTG GTT AAC CTG CTG CCG GCT ATC CTG TCT CCG GGT GCT CTG GTT 2328 Asp Leu Val Asn Leu Leu Pro Ala He Leu Ser Pro Gly Ala Leu Val 720 725 730 GTT GGT GTT GTTTGC GCT GCT ATC CTG CGT CGT CAC GTT GGC CCG GGT 2376 Val Gly Val Val Cys Ala Ala We Leu Arg Arg His Val Gly Pro Gly 735 740 745 GAA GGT GCT GTT CAG TGG ATG AAC CGT CTG ATC GCTTTC GCTTCT CGT 2424 Glu Gly Ala Val Gin Trp Met Asn Arg Leu lie Ala Phe Ala Ser Arg 750 755 760 765 GGTAACCAC GTTTCTCCATGG GAT CCT CTA GAC TGC AGG CAT GCT AAG 2472 Gly Asn His Val Ser Pro Tφ Asp Pro Leu Asp Cys Arg His Ala Lys 770 775 780 TMGTAGATCTTGAGCX_KX3TTCGCGCTGAA ATGCGCTAATTTCACTTCAC GACACTTCAG 2532 CCAATTTTGG GAGGAGTGTC GTACCGTTAC GATTTTCCTC AATΠTTCTTTTCAACAATT 2592 GATCTCATTC AGGTGACATCTTTTATATTG GCGCTCATTATGAAAGCAGTAGCTTTTATG 2652 AGGCTMTCTGAATGGMO\GCTGCGTGCCGAATTMG∞^ 2712 AGTCGTATTG AGTGCGTCAATGAAAAAGCG GATACGGCGTTCTGGGCTTTGTATGAGAGC 2772 CAGGGAMCCCMTGCXX3TTMTGGCW\GAAGCTTAGCCCGCCTMTGA^ 2832 TTTCGAO_XX3AG<_K GGATGGCCTTCXXX_ATTATGAπ 2892 GGATGOXGCGπGCΑGGOCATGCTOTCC^ 2952 TTCMGGATCGCTCGCGGCTCTTACCAGCCTMCTTCGATCACTGGACCG 3012 CCCTATACCTTGTCTGCCTCCCCGCX3TTGCCTCGCX__ΒTGCA 3132 CCTGMTGGAAGCCGGCGGCACCTCGCTMCGGATTCACX- ACTCC^ 3192 TC TT(_*TTGCGGAGAACTGTGMTGCGCAM 3252 GMOCGC)CATCTCCAGCAGCCGCACGCGGCGC^^ 3312 GGTGCGCATGATCCTGCTCCTCTCGTTGAGGACCCGGCTAGGCTGGO^ 3372 TGGTTAGCAGMTGMTCACCGATACGCGAGCX ^CCTGAAG ( OGA 3432 GTCTGCGACCTGAGC CMCATG TGCTCT^^ 3492 MCGCGGMGTCAGCGCCCTGCACCATTATGTTCCGGATCTGC^^ 3552 GCTA(XCTGTGGMCACCTACATCTGTATTMCGMGC^ 3612 CTGACTCGCTG£X_CTΑ3CTCGΠCGGCTGC 3672 TMTACGGΓΓTATCX.ACΛGMTCΛGGGGATAACGCAGGAMGMCATGTGAGC^ 3732 AGCAAMGQCCAGGMCC(JrAAAMGGCCG∞ιTTGCT 3792 CCCCTGACGAGCATCACAAAMTCGACGCTCMCTCAGAGCTG^ 3852 TATAMGATACX^AGGCGTTTCCCfXTGG GCTCCCTO^ 3912 TGCCGCTTACCX_K_^TACCTGTCCG XTTTCTCα^ 3972 GCTCACGCTGTAGGTATCTC AGTTCGGTGT AGGTCGTTCG CTCCAAGCTG GGCTGTGTGC 4032 ACGMCCCCCCGTTCAGCCCGACCGCTGCGCCTTATCCGGTM 4092 ACCCGGTAAG ACACGACTTATCGCCACTGG CAGCAGCCAC TGGTAACAGG ATTAGCAGAG 4152 CGAGGTATGT AGGCGGTGCT ACAG^GTTCTTGAAGTGGTG GCCTAACTAC GGCTACACTA 4212 GMGGACAGTATTTGGTATCTGCGCTCTGCTGMGCX^CTTACCTTCGGAAAMG^ 4272 GTAGCTCTTGATCCGGCAMCAMCCACXGCTGGTAGCGGTGG I I I I I 1 1 GTTTGCAAGC 4332 AGCAGATTAC GCGCAGAAAA AAAGGATCTC AAGAAGATCC TTTGATCTTTTCTACGGGGT 4392 CTGACGCTCACTGGMCG CTCACGTTMGGGATTTTGGTCAT^ 4452 GGATCTTCAC CTAGATCCTTTTAAATTAAA AATGAAGTTTTAAATCAATCTAAAGTATAT 4512 ATGAGTAAAC TTGGTCTGAC AGTTACCAAT GCTTAATCAG TGAGGCACCT ATCTCAGCGA 4572 TCTGTCTATT TCGTTCATCC ATAGTTGCCT GACTCCCCGT CGTGTAGATA ACTACGATAC 4632 GGGAGGGCΠACCATCTGGCCCCACTGCTGCMTGATACCGCGAGACC^ 4692 ΣITXAGATTTATCAGCMTAM ( XAGCCAGCCGGAAGGG^ 4752 CAACTTTATC CGCCTCCATC CAGTCTATTA ATTGTTGCCG GGAAGCTAGAGTAAGTAGTT 4812 ΑXXAGTTAATAGTTTGCGC AACGTTGTTG CCATTGCTAC AGGCATCGTG GTGTCACGCT 4872 CGTCGTTTGG TATGGCTTCATTCAGCTCCG GTTCCCAACG ATCAAGGCGA GTTACATGAT 4932 <XCCX^TGΠTGTGCAAAAMG _X_^TTAGCTCCΓΓCGGTCCTCC^ 4992 AGTTGGCCGC AGTGTTATCA CTCATGGTTA TGGCAGCACT GCATAATTCT CTTACTGTCA 5052 TGCCATCCGT AAGATGCTTT TCTGTGACTG GTGAGTACTC AACCAAGTCA TTCTGAGAAT 5112 ACTCTATGCGGCGACCGAGTTGCTCΠTGCCCGGCGTCMCACGGGATM^ 5172 ATAGCAGMCTTTAAAAGTG CTCATCATTG GAAAACGTTCTTCGGGGCGA AAACTCTCAA 5232 GGATCTTACCGCTGTTGAGATCCAGTTCGATGT^^ 5292 CV\GCATCTΓΓTACTTTCACCAGCGTTTCTGGGTGAGCAMMCAGGMGGC^ 5352 CAAAAAAGGG AATAAGGGCG ACACGGAAAT GTTGAATACT CATACTCTTC CI I I I ICAAT 5412 ATTATTGAAG CATTTATCAG GGTTATTGTC TCATGAGCGG ATACATATTT GAATGTATTT 5472 AAGAAACCATTATTATCATG ACATTAACCT ATAAAAATAG GCGTATCACG AGGCCCTTTC 5592 GTCTTCAA 5600 (2) INFORMATION FOR SEQ ID NO:25: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 781 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:25: Met Ser Phe Val Val He He Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 Pro Gly Lys Pro Leu Val Asp He Asn Gly Lys Pro Met He Val His 20 25 30 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg lie lie Val Ala 35 40 45 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val He Val Asn 85 90 95 Val Gin Gly Asp Glu Pro Met lie Pro Ala Thr He He Arg Gin Val 100 105 110 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Val 115 120 125 Pro He His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr He 145 150 155 160 Pro Tφ Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 Asn Phe Leu Arg His Leu Gly He Tyr Gly Tyr Arg Ala Gly Phe He 180 185 190 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His He Glu Met 195 200 205 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 . Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 Asp Pro Ser Thr Asn Ser Met Ala Val Asp Phe He Pro Val Glu Asn 245 250 255 Leu Glu Thr Thr Met Arg Ser Pro Val Phe Thr Asp Asn Ser Ser Pro 260 265 270 Pro Val Val Pro Gin Ser Phe Gin Val Ala His Leu His Ala Pro Thr 275 280 285 Gly Ser Gly Lys Ser Thr Lys Val Pro Ala Ala Tyr Ala Ala Gin Gly 290 295 300 Tyr Lys Val Leu Val Leu Asn Pro Ser Val Ala Ala Thr Leu Gly Phe 305 310 315 320 Gly Ala Tyr Met Ser Lys Ala His Gly lie Asp Pro Asn He Arg Thr 325 330 335 Gly Val Arg Thr He Thr Thr Gly Ser Pro lie Thr Tyr Ser Thr Tyr 340 345 350 Gly Lys Phe Leu Ala Asp Gly Gly Cys Ser Gly Gly Ala Tyr Asp He 355 360 365 He He Cys Asp Glu Cys His Ser Thr Asp Ala Thr Ser He Leu Gly 370 375 380 He Gly Thr Val Leu Asp Gin Ala Glu Thr Ala Gly Ala Arg Leu Val 385 390 395 400 Val Leu Ala Thr Ala Thr Pro Pro Gly Ser Val Thr Val Pro His Pro 405 410 415 Asn He Glu Glu Val Ala Leu Ser Thr Thr Gly Glu lie Pro Phe Tyr 420 425 430 Gly Lys Ala He Pro Leu Glu Val lie Lys Gly Gly Arg His Leu lie 435 440 445 Phe Cys His Ser Lys Lys Lys Cys Asp Glu Leu Ala Ala Lys Leu Val 450 455 460 Ala Leu Gly lie Asn Ala Val Ala Tyr Tyr Arg Gly Leu Asp Val Ser 465 470 475 480 Val He Pro Thr Ser Gly Asp Val Val Val Val Ala Thr Asp Ala Leu 485 490 495 Met Thr Gly Tyr Thr Gly Asp Phe Asp Ser Val He Asp Cys Asn Thr 500 505 510 Cys Asn Ser Ser Thr Gly Cys Val Val We Val Gly Arg Val Val Leu 515 520 525 Ser Gly Lys Pro Ala lie He Pro Asp Arg Glu Val Leu Tyr Arg Glu 530 535 540 Phe Asp Glu Met Glu Glu Cys Ser Gin His Leu Pro Tyr He Glu Gin 545 550 555 560 Gly Met Met Leu Ala Glu Gin Phe Lys Gin Lys Ala Leu Gly Leu Leu 565 570 575 Gin Thr Ala Ser Arg Gin Ala Glu Val lie Ala Pro Ala Val Gin Thr 580 585 590 Asn Trp Gin Lys Leu Glu Thr Phe Trp Ala Lys His Met Trp Asn Phe 595 600 605 He Ser Gly He Gin Tyr Leu Ala Gly Leu Ser Thr Leu Pro Gly Asn 610 615 620 Pro Ala He Ala Ser Leu Met Ala Phe Thr Ala Ala Val Thr Ser Pro 625 630 635 640 Leu Thr Thr Ser Gin Thr Leu Leu Phe Asn He Leu Gly Gly Trp Val 645 650 655 Ala Ala Gin Leu Ala Ala Pro Gly Ala Ala Thr Ala Phe Val Gly Ala 660 665 670 Gly Leu Ala Gly Ala Ala He Gly Ser Val Gly Leu Gly Lys Val Leu 675 680 685 He Asp He Leu Ala Gly Tyr Gly Ala Gly Val Ala Gly Ala Leu Val 690 695 700 Ala Phe Lys He Met Ser Gly Glu Val Pro Ser Thr Glu Asp Leu Val 705 710 715 720 Asn Leu Leu Pro Ala He Leu Ser Pro Gly Ala Leu Val Val Gly Val 725 730 735 Val Cys Ala Ala He Leu Arg Arg His Val Gly Pro Gly Glu Gly Ala 740 745 750 Val Gin Trp Met Asn Arg Leu He Ala Phe Ala Ser Arg Gly Asn His 755 760 765 Val Ser Pro Trp Asp Pro Leu Asp Cys Arg His Ala Lys 770 775 780 (2) INFORMATION FOR SEQ ID NO:26: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1548 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: circular (ii) MOLECULE TYPE: DNA (genomic) (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 1..1548 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:26: ATGAGTTTTGTGGTCATTATTCCCGCG CGCTACGCGTCGACGCGTCTG 48 Met Ser Phe Val Val He lie Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 CCC GGT AAA CCA TTG GTT GAT ATT AAC GGC AAA CCC ATG ATT GTT CAT 96 Pro Gly Lys Pro Leu Val Asp lie Asn Gly Lys Pro Met He Val His 20 25 30 GTTCTTG CGCG∞CGTGAATCAGGTGCCGAGCGCATCATCGTGGCA 144 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg He He Val Ala 35 40 45 ACC GAT CAT GAG GAT GTT GCC CGC GCC GTT GAA GCC GCT GGC GGT GAA 192 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 GTATGT ATG ACG CGC GCC GAT CAT CAG TCA GGA ACA GAA CGT CTG GCG 240 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 GAAGTTGTCGAAAAATGC GCATTC AGC GAC GACACG GTGATCGTTAAT 288 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val We Val Asn 85 90 95 GTG CAG GGT GAT GAA CCG ATG ATC CCT GCG ACA ATC ATT CGT CAG GTT 336 Val Gin Gly Asp Glu Pro Met lie Pro Ala Thr lie We Arg Gin Val 100 105 1 10 GCT GAT AAC CTC GCT CAG CGT CAG GTG GGT ATG GCG ACT CTG GCG GTG 384 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Val 115 120 125 CCA ATC CAC AAT GCG GAA GAA GCG TTT AAC CCG AAT GCG GTG AAA GTG 432 Pro He His Asn Ala Glu Glu Aia Phe Asn Pro Asn Ala Val Lys Val 130 135 140 GTT CTC GAC GCT GAA GGG TAT GCA CTG TAC TTC TCT CGC GCC ACC ATT 480 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr He 145 150 155 160 CX TGG GATCGTGAT STTTTGCAGAA GGC CTTGAAACCGTTGGC GAT 528 Pro Tφ Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 AAC TTC CTG CGT CAT CTT GGT ATT TAT GGC TAC CGT GCA GGC TTT ATC 576 Asn Phe Leu Arg His Leu Gly lie Tyr Gly Tyr Arg Aia Gly Phe He 180 185 190 CGTCGTTAC GTC AACTGG CAG GCA AGT CCG TTA GAA CAC ATC GAA ATG 624 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His He Glu Met 195 200 205 TTA GAG CAG CTT CGT GTT CTG TGG TAC GGC GAA AAA ATC CAT GTT GCT 672 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 GTT GCT CAG GAA GTT CCT GGC ACA GGT GTG GAT ACC CCT GAA GAT CTC 720 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 GAC CCGTCG ACG AATTCC CCA TGG ACC CAC TAC GTT CCG GAA TCT GAC 768 Asp Pro Ser Thr Asn Ser Pro Trp Thr His Tyr Val Pro Glu Ser Asp 245 250 255 GCT GCT GCT CGA GTT ACC GCT ATC CTG TCT TCT CTG ACC GTT ACC CAG 816 Aia Ala Ala Arg Val Thr Ala He Leu Ser Ser Leu Thr Val Thr Gin 260 265 270 CTTCTGCGTCGTCTGCACCAGTGGATCTCTTCTGAATGCACCACCCCG 864 Leu Leu Arg Arg Leu His Gin Trp lie Ser Ser Glu Cys Thr Thr Pro 275 280 285 TGC TCT GGTTCTTGG CTG CGT GAC ATC TGG GAC TGG ATC TGC GAA GTT 912 Cys Ser Gly Ser Trp Leu Arg Asp lie Trp Asp Trp lie Cys Glu Val 290 295 300 CTG TCT GAC TTC AAA ACC TGG CTG AAA GCT AAA CTG ATG CCG CAG CTG 960 Leu Ser Asp Phe Lys Thr Trp Leu Lys Ala Lys Leu Met Pro Gin Leu 305 310 315 320 CCG GGT ATC CCG TTC GTTTCTTGC CAG CGTGGTTAC AAA GGTGTTTGG 1008 Pro Gly lie Pro Phe Val Ser Cys Gin Arg Gly Tyr Lys Gly Val Trp 325 330 335 CGT GTT GAC GGT ATC ATG CAC ACC GGTTGC CAC TGC GGT GCT GAA ATC 1056 Arg Val Asp Gly lie Met His Thr Arg Cys His Cys Gly Ala Glu lie 340 345 350 ACC GGT CAC GTT AAA AAC GGT ACC ATG CGT ATC GTT GGT CCG CGT ACC 1104 Thr Gly His Val Lys Asn Gly Thr Met Arg He Val Gly Pro Arg Thr 355 360 365 TGCCGTAACATGTGGTCTGGCACCTTC CCG ATC AACGCTTACACC ACC 1152 Cys Arg Asn Met Trp Ser Gly Thr Phe Pro He Asn Ala Tyr Thr Thr 370 375 380 GGTCGGTGCAGCCCGCTGCCGGCTCCGAACTACACCTTCGCTCTGTGG 1200 Gly Pro Cys Thr Pro Leu Pro Ala Pro Asn Tyr Thr Phe Ala Leu Trp 385 390 395 400 CGT GTTTCT GCT GAA GAA TAC GTT GAA ATC CGT CAG GTT GGT GAC TTC 1248 Arg Val Ser Ala Glu Glu Tyr Val Glu lie Arg Gin Val Gly Asp Phe 405 410 415 CAC TAC GTT ACC GGT ATG ACC ACC GAC AAC CTG AAA TGC CCG TGC CAG 1296 His Tyr Val Thr Gly Met Thr Thr Asp Asn Leu Lys Cys Pro Cys Gin 420 425 430 GTT CCG TCT CCG GAG TTC TTC ACC GAA CTG GAC GGT GTT CGT CTG CAC 1344 Val Pro Ser Pro Glu Phe Phe Thr Glu Leu Asp Gly Val Arg Leu His 435 440 445 CGTTTC GCTCCG CCGTGCAAACCG CTG CTG CGTGAA GAAGTTTCTTTC 1392 Arg Phe Ala Pro Pro Cys Lys Pro Leu Leu Arg Glu Glu Val Ser Phe 450 455 460 CGTGTTGGTCTG CACGAATACCCGGTTGGTTCTCAGCTGCCGTGCGAA 1440 Arg Val Gly Leu His Glu Tyr Pro Val Gly Ser Gin Leu Pro Cys Glu 465 470 475 480 GCG GAACCGGACGTTGCTGTTCTGACCTCTATGCTGACCGACCCGTCT 1488 Pro Glu Pro Asp Val Ala Val Leu Thr Ser Met Leu Thr Asp Pro Ser 485 490 495 CAC ATC ACC GCT GAA GCT GCT GGT CGT CGA CTG GAT CCT CTA GAC TGC 1536 His He Thr Ala Glu Ala Ala Gly Arg Arg Leu Asp Pro Leu Asp Cys 500 505 510 AGG CAT GCT AAG 1548 Arg His Ala Lys 515 (2) INFORMATION FOR SEQ ID NO:27: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 516 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:27: Met Ser Phe Val Val We lie Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 Pro Gly Lys Pro Leu Val Asp lie Asn Gly Lys Pro Met He Val His 20 25 30 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg lie lie Val Ala 35 40 45 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val He Val Asn 85 90 95 Val Gin Gly Asp Glu Pro Met He Pro Ala Thr He He Arg Gin Val 100 105 1 10 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Val 115 120 125 Pro He His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr He 145 150 155 160 Pro Tφ Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 Asn Phe Leu Arg His Leu Gly lie Tyr Gly Tyr Arg Ala Gly Phe He 180 185 190 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His He Glu Met 195 200 205 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 Asp Pro Ser Thr Asn Ser Pro Trp Thr His Tyr Val Pro Glu Ser Asp 245 250 255 Ala Ala Ala Arg Val Thr Ala lie Leu Ser Ser Leu Thr Val Thr Gin 260 265 270 Leu Leu Arg Arg Leu His Gin Trp lie Ser Ser Glu Cys Thr Thr Pro 275 280 285 Cys Ser Gly Ser Trp Leu Arg Asp He Trp Asp Trp He Cys Glu Val 290 295 300 Leu Ser Asp Phe Lys Thr Trp Leu Lys Ala Lys Leu Met Pro Gin Leu 305 310 315 320 Pro Gly He Pro Phe Val Ser Cys Gin Arg Gly Tyr Lys Gly Val Trp 325 330 335 Arg Val Asp Gly He Met His Thr Arg Cys His Cys Gly Ala Glu He 340 345 350 Thr Gly His Val Lys Asn Gly Thr Met Arg He Val Gly Pro Arg Thr 355 360 365 Cys Arg Asn Met Trp Ser Gly Thr Phe Pro He Asn Ala Tyr Thr Thr 370 375 380 Gly Pro Cys Thr Pro Leu Pro Ala Pro Asn Tyr Thr Phe Ala Leu Trp 385 390 395 400 Arg Val Ser Ala Glu Glu Tyr Val Glu We Arg Gin Val Gly Asp Phe 405 410 415 His Tyr Val Thr Gly Met Thr Thr Asp Asn Leu Lys Cys Pro Cys Gin 420 425 430 Val Pro Ser Pro Glu Phe Phe Thr Glu Leu Asp Gly Val Arg Leu His 435 440 445 Arg Phe Ala Pro Pro Cys Lys Pro Leu Leu Arg Glu Glu Val Ser Phe 450 455 460 Arg Val Gly Leu His Glu Tyr Pro Val Gly Ser Gin Leu Pro Cys Glu 465 470 475 480 Pro Glu Pro Asp Val Ala Val Leu Thr Ser Met Leu Thr Asp Pro Ser 485 490 495 His He Thr Ala Glu Ala Ala Gly Arg Arg Leu Asp Pro Leu Asp Cys 500 505 510 Arg His Ala Lys 515 (2) INFORMATION FOR SEQ ID NO:28: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1623 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: circular (ii) MOLECULE TYPE: DNA (genomic) (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 1..1623 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:7: ATGAGTTTTGTGGTCATTATTCCC GCG CGC TAC GCG TCG AGG CGT CTG 48 Met Ser Phe Val Val lie lie Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 CCC GGT AAA CCA TTG GTT GAT ATT AAC GGC AAA CCC ATG ATT GTT CAT 96 Pro Gly Lys Pro Leu Val Asp lie Asn Gly Lys Pro Met We Val His 20 25 30 GTT CTT GAA CGC GCG CGT GAA TCA GGT GCC GAG CGC ATC ATC GTG GCA 144 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg lie He Val Ala 35 40 45 ACCGATCATGAGGATGTTGCC CGCGCCGTTGAAGCCGCTGGCGGTGAA 192 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 GTATGTATGACG CGCGGCGATCATCAGTCAGGAACAGAACGTCTGGCG 240 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 GAA GTT GTC GAA AAA TGC GCA TTC AGC GAC GAC ACG GTG ATC GTT AAT 288 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val lie Val Asn 85 90 95 GTG CAG GGT GAT GAA CCG ATG ATC CCT GCG ACA ATC ATT CGT CAG GTT 336 Val Gin Gly Asp Glu Pro Met lie Pro Ala Thr He He Arg Gin Val 100 105 1 10 GCTGATAACCTCGCTCAGCGTCAGGTGGGTATGGCGACTCTGGCG GTG 384 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Val 115 120 125 CCAATCCACMTGCG GMGMGCGTTTAACCCGAATGCGGTGAAAGTG 432 Pro lie His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 GTTCTCGAC GCTGAAGGGTATGCACTGTACTTCTCTCGC GCCACCATT 480 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr He 145 150 155 160 CCTTGGGATCGTGATCGTTTTGCAGAAGGCCTTGAAAGCGTTGGC GAT 528 Pro Tφ Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 AAC TTC CTG CGT CAT CTT GGT ATT TAT GGC TAC CGT GCA GGC TTT ATC 576 Asn Phe Leu Arg His Leu Gly He Tyr Gly Tyr Arg Ala Gly Phe He 180 185 190 CGTCGTTACGTC AACTGG CAG CCA AGT CCG TTA GAA CAC ATC GAA ATG 624 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His He Glu Met 195 200 205 TTA GAG CAG CTT CGT GTT CTG TGG TAC GGC GAA AAA ATC CAT GTT GCT 672 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys We His Val Ala 210 215 220 GTT GCT CAG GAA GTT CCT GGC ACA GGT GTG GAT ACC CCT GAA GAT CTC 720 Val Ala Gin Giu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 GAC XBTCGACGMTTCTATGCGTCGACTGGCTCGTGGTTCTCOGCCG 768 Asp Pro Ser Thr Asn Ser Met Arg Arg Leu Ala Arg Gly Ser Pro Pro 245 250 255 TCT GTT GCT TCT TCT TCT GCT TCT CAA CTG TCT GCT CCG TCT CTG AAA 816 Ser Val Ala Ser Ser Ser Ala Ser Gin Leu Ser Ala Pro Ser Leu Lys 260 265 270 GCTACCTGCACC GCTAAC CAC GACTCTCCGGACGCTGAACTGATC GAA 864 Ala Thr Cys Thr Ala Asn His Asp Ser Pro Asp Ala Glu Leu We Glu 275 280 285 GCTAAC CTG CTGTGGCGTCAG GAAATG GGTGGTAACATCACCCGTGTT 912 Ala Asn Leu Leu Trp Arg Gin Glu Met Gly Gly Asn lie Thr Arg Val 290 295 300 GAA TCT GAA AAC AAA GTT GTT ATC CTG GAC TCTTTC GAC CCG CTG GTT 960 Glu Ser Glu Asn Lys Val Val He Leu Asp Ser Phe Asp Pro Leu Val 305 310 315 320 GCT GAA GAA GAC GAA CGT GAG ATC TCT GTT CCG GCT GAA ATC CTG CGT 1008 Ala Glu Glu Asp Glu Arg Glu We Ser Val Pro Ala Glu We Leu Arg 325 330 335 AAATCTCGTCGTTTC GCT CAG GCT CTG CCG GTT TGG GCT CGT CCG GAC 1056 Lys Ser Arg Arg Phe Ala Gin Ala Leu Pro Val Tφ Ala Arg Pro Asp 340 345 350 TAC AACCCG CCG CTG GTT GAA ACC TGG AAA AAA CCG GAC TAC GAA CCG 1104 Tyr Asn Pro Pro Leu Val Glu Thr Trp Lys Lys Pro Asp Tyr Glu Pro 355 360 365 CCG GTT GTT CAC GGTTGC CCG CTG CCG CCG CCG AAATCT CCG CCG GTT 1152 Pro Val Val His Gly Cys Pro Leu Pro Pro Pro Lys Ser Pro Pro Val 370 375 380 CCG CCG CCG CGTAAAAAA CGTACC GTTGTTCTGACCGAATCTACC CTG 1200 Pro Pro Pro Arg Lys Lys Arg Thr Val Val Leu Thr Glu Ser Thr Leu 385 390 395 400 TCT ACC GCT CTG GCT GAA CTG GCT ACC CGTTCTTTC GGTTCTTCTTCT 1248 Ser Thr Ala Leu Ala Glu Leu Ala Thr Arg Ser Phe Gly Ser Ser Ser 405 410 415 ACC TCG GGT ATC ACC GGT GAC AAC ACC ACC ACC TCTTCT GAA CCG GCT 1296 Thr Ser Gly He Thr Gly Asp Asn Thr Thr Thr Ser Ser Glu Pro Ala 420 425 430 CCG TCT GGTTGC CCG CCG GAC TCT GAC GCTGAATCTTACTCTTCT ATG 1344 Pro Ser Gly Cys Pro Pro Asp Ser Asp Ala Glu Ser Tyr Ser Ser Met 435 440 445 CCGCCG CTG GMGGTGAACCG GGTGAC CCGGATCTGTCTGAC GGTTCT 1392 Pro Pro Leu Glu Gly Glu Pro Gly Asp Pro Asp Leu Ser Asp Gly Ser 450 455 460 TGGTCTACC GTTTCTTCTGAAGCTAAC GCTGAAGAC GTTGTTTGCTGC 1440 Tφ Ser Thr Val Ser Ser Glu Ala Asn Ala Glu Asp Val Val Cys Cys 465 470 475 480 TCTATGTCTTACTCTTGG ACC GGT GCT CTG GTT ACT CCG TGC GCT GCT 1488 Ser Met Ser Tyr Ser Trp Thr Gly Ala Leu Val Thr Pro Cys Ala Ala 485 490 495 GAAGAACAGAAACTGCCGATCAACGCTCTGTCTAACTCTCTG CTG CGT 1536 Glu Glu Gin Lys Leu Pro He Asn Ala Leu Ser Asn Ser Leu Leu Arg 500 505 510 CAC CAC AAC CTG GTTTAC TCT ACC ACC TCT CGTTCT GCTTGC CAG CGT 1584 His His Asn Leu Val Tyr Ser Thr Thr Ser Arg Ser Ala Cys Gin Arg 515 520 525 CAG AAA AAA GTT ACC TTC GAC CGT CTG CAA GTT CTA GAC 1623 Gin Lys Lys Val Thr Phe Asp Arg Leu Gin Val Leu Asp 530 535 540 (2) INFORMATION FOR SEQ ID NO:29: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 541 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:29: Met Ser Phe Val Val He lie Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 Pro Gly Lys Pro Leu Val Asp He Asn Gly Lys Pro Met He Val His 20 25 30 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg He lie Val Ala 35 40 45 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 Glu Val Val Glu Lys Cys Aia Phe Ser Asp Asp Thr Val We Val Asn 85 90 95 Val Gin Gly Asp Glu Pro Met lie Pro Ala Thr We He Arg Gin Val 100 105 110 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Val 115 120 125 Pro lie His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr lie 145 150 155 160 Pro Tφ Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 Asn Phe Leu Arg His Leu Gly lie Tyr Gly Tyr Arg Ala Gly Phe lie 180 185 190 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His He Glu Met 195 200 205 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 Asp Pro Ser Thr Asn Ser Met Arg Arg Leu Ala Arg Gly Ser Pro Pro 245 250 255 Ser Val Ala Ser Ser Ser Ala Ser Gin Leu Ser Ala Pro Ser Leu Lys 260 265 270 Ala Thr Cys Thr Ala Asn His Asp Ser Pro Asp Ala Glu Leu We Glu 275 280 285 Ala Asn Leu Leu Trp Arg Gin Glu Met Gly Gly Asn He Thr Arg Val 290 295 300 Glu Ser Glu Asn Lys Val Val He Leu Asp Ser Phe Asp Pro Leu Val 305 310 315 320 Ala Glu Glu Asp Glu Arg Glu He Ser Val Pro Ala Glu He Leu Arg 325 330 335 Lys Ser Arg Arg Phe Ala Gin Ala Leu Pro Val Tφ Ala Arg Pro Asp 340 345 350 Tyr Asn Pro Pro Leu Val Glu Thr Trp Lys Lys Pro Asp Tyr Glu Pro 355 360 365 Pro Val Val His Gly Cys Pro Leu Pro Pro Pro Lys Ser Pro Pro Val 370 375 380 Pro Pro Pro Arg Lys Lys Arg Thr Val Val Leu Thr Glu Ser Thr Leu 385 390 395 400 Ser Thr Ala Leu Ala Glu Leu Ala Thr Arg Ser Phe Gly Ser Ser Ser 405 410 415 Thr Ser Gly lie Thr Gly Asp Asn Thr Thr Thr Ser Ser Glu Pro Ala 420 425 430 Pro Ser Gly Cys Pro Pro Asp Ser Asp Ala Glu Ser Tyr Ser Ser Met 435 440 445 Pro Pro Leu Glu Gly Glu Pro Gly Asp Pro Asp Leu Ser Asp Gly Ser 450 455 460 Trp Ser Thr Val Ser Ser Glu Ala Asn Ala Glu Asp Val Val Cys Cys 465 470 475 480 Ser Met Ser Tyr Ser Trp Thr Gly Ala Leu Val Thr Pro Cys Ala Ala 485 490 495 Glu Glu Gin Lys Leu Pro We Asn Ala Leu Ser Asn Ser Leu Leu Arg 500 505 510 His His Asn Leu Val Tyr Ser Thr Thr Ser Arg Ser Ala Cys Gin Arg 515 520 525 Gin Lys Lys Val Thr Phe Asp Arg Leu Gin Val Leu Asp 530 535 540 (2) INFORMATION FOR SEQ ID NO:30: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1488 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: circular (ii) MOLECULE TYPE: DNA (genomic) (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 1..1488 (xi) SEQUENCE DESCRIPTION: SEQ ID NO.30: ATG AGTTTTGTG GTC ATT ATT CCC GCG CGC TAC GCGTCG ACG CGT CTG 48 Met Ser Phe Val Val lie He Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 CCCGGTAAACCATTG GTTGATATTAAC GGCAAACCCATGATTGTTCAT 96 Pro Gly Lys Pro Leu Val Asp lie Asn Gly Lys Pro Met He Val His 20 25 30 GTTCTTGAACGCGCGCGTGAATCAGGTGCCGAG CGCATCATCGTGGCA 144 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg lie lie Val Ala 35 40 45 ACX- GATCATGAGGATGTTGCC<OGCGCCGTTGMGCC GCTGGCGGTGAA 192 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 GTA TGT ATG ACG CGC GCC GAT CAT CAG TCA GGA ACA GAA CGT CTG GCG 240 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 GAA GTT GTC GAA AAA TGC GCA TTC AGC GAC GAC ACG GTG ATC GTT AAT 288 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val He Val Asn 85 90 95 GTG CAG GGT GAT GAA CCG ATG ATC CCT GCG ACA ATC ATT CGT CAG GTT 336 Val Gin Gly Asp Glu Pro Met He Pro Ala Thr lie He Arg Gin Val 100 105 110 GCT GAT AAC CTC GCT CAG CGT CAG GTG GGT ATG GCG ACT CTG GCG GTG 384 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Val 115 120 125 CCA ATC CAC AAT GCG GAA GAA GCG TTT AAC CCG AAT GCG GTG AAA GTG 432 Pro lie His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 GTT CTC GAC GCT GAA GGG TAT GCA CTG TAC TTC TCT CGC GCC ACC ATT 480 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr lie 145 150 155 160 CCTTGGGATCGTGATCGTTTTGCAGAAGGC CTTGAAACCGTTGGC GAT 528 Pro Tφ Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 AAC TTC CTG CGT CAT CTT GGT ATT TAT GGC TAC CGT GCA GGC TTT ATC 576 Asn Phe Leu Arg His Leu Gly lie Tyr Gly Tyr Arg Ala Gly Phe lie 180 185 190 CGT CGTTAC GTC AAC TGG CAG CCA AGT CCG TTA GAA CAC ATC GAA ATG 624 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His He Glu Met 195 200 205 TTA GAG CAG CTT CGT GTT CTG TGG TAC GGC GAA AAA ATC CAT GTT GCT 672 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 GTT GCT CAG GAA GTT CCT GGC ACA GGT GTG GAT ACC CCT GAA GAT CTC 720 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 GAC CCG TCG ACG AATTCT CTA GAC TCC CAC TAC CAG GAC GTT CTG AAA 768 Asp Pro Ser Thr Asn Ser Leu Asp Ser His Tyr Gin Asp Val Leu Lys 245 250 255 GAA GTT AAA GCT GCT GCTTCT AAA GTT AAA GCT AAC CTG CTG TCT GTT 816 Glu Val Lys Ala Ala Ala Ser Lys Val Lys Ala Asn Leu Leu Ser Val 260 265 270 GAA GAA GCA TGC TCT CTG ACC CCG CCG CAC TCT GCT AAA TCT AAA TTC 864 Glu Glu Ala Cys Ser Leu Thr Pro Pro His Ser Ala Lys Ser Lys Phe 275 280 285 GGTTACGGTGCTAAAGAC GTTCGTTGC CAC GCT CGT AAA GCT GTT ACC 912 Gly Tyr Gly Ala Lys Asp Val Arg Cys His Ala Arg Lys Ala Val Thr 290 295 300 CACATCAACTCTGTTTGGAAAGATCTG CTG GAAGACAACGTTACC CCG 960 His He Asn Ser Val Trp Lys Asp Leu Leu Glu Asp Asn Val Thr Pro 305 310 315 320 ATCGACACCACCATCATG GCTAAAAACGAAGTTTTCTGCGTTCAG CCG 1008 He Asp Thr Thr lie Met Ala Lys Asn Glu Val Phe Cys Val Gin Pro 325 330 335 GAAAAAGGTGGTCGTAAACCG GCTCGTCTGATCGTTTTCCCGGACCTG 1056 Glu Lys Gly Gly Arg Lys Pro Ala Arg Leu He Val Phe Pro Asp Leu 340 345 350 GGTGTTCGTGTTTGCGAAAAAATGGCTCTGTAC GAC GTTGTTACCAAA 1104 Gly Val Arg Val Cys Glu Lys Met Ala Leu Tyr Asp Val Val Thr Lys 355 360 365 CTG CCG CTG GCT GTT ATG GGTTCTTCTTAC GGTTTC CAG TAC TCT CCG 1152 Leu Pro Leu Ala Val Met Gly Ser Ser Tyr Gly Phe Gin Tyr Ser Pro 370 375 380 GGT CAG CGT GTT GAG TTC CTG GTT CAG GCTTGG AAA TCT AAA AAAACC 1200 Gly Gin Arg Val Glu Phe Leu Val Gin Ala Trp Lys Ser Lys Lys Thr 385 390 395 400 CCG ATG GGTTTC TCTTAC GAC ACC CGTTGC TTC GAC TCT ACC GTT ACC 1248 Pro Met Gly Phe Ser Tyr Asp Thr Arg Cys Phe Asp Ser Thr Val Thr 405 410 415 GAATCTGACATTCGTACCGAAGAAGCTATCTAC CAGTGCTGCGACCTG 1296 Glu Ser Asp He Arg Thr Glu Glu Ala He Tyr Gin Cys Cys Asp Leu 420 425 430 GAC CCGCAG GCTCGTGTTGCTATCAAATCTCTGACCGAACGTCTGTAC 1344 Asp Pro Gin Ala Arg Val Ala He Lys Ser Leu Thr Glu Arg Leu Tyr 435 440 445 GTT GGT GGT CCG CTG ACC AAC TCT CGG GGT GAA AAC TGC GGTTACCGT 1392 Val Gly Gly Pro Leu Thr Asn Ser Arg Gly Glu Asn Cys Gly Tyr Arg 450 455 460 CGTTGCCGTGCTTCTGGTGTTCTGACCACCTCTTGCGGTAACACC CTG 1440 Arg Cys Arg Ala Ser Gly Val Leu Thr Thr Ser Cys Gly Asn Thr Leu 465 470 475 480 ACC TGC TAC ATC AAA GCT CGT GCT GCTTGC CGT GCT GCT GGT CTG CAG 1488 Thr Cys Tyr He Lys Ala Arg Ala Ala Cys Arg Ala Ala Gly Leu Gin 485 490 495 (2) INFORMATION FOR SEQ ID NO:31 : (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 496 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:31 : Met Ser Phe Val Val He lie Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 Pro Gly Lys Pro Leu Val Asp lie Asn Gly Lys Pro Met We Val His 20 25 30 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg lie He Val Ala 35 40 45 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val He Val Asn 85 90 95 Val Gin Gly Asp Glu Pro Met lie Pro Ala Thr We lie Arg Gin Val 100 105 110 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Val 115 120 125 Pro He His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr lie 145 150 155 160 Pro Tφ Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 Asn Phe Leu Arg His Leu Gly lie Tyr Gly Tyr Arg Ala Gly Phe He 180 185 190 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His He Glu Met 195 200 205 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 Asp Pro Ser Thr Asn Ser Leu Asp Ser His Tyr Gin Asp Val Leu Lys 245 250 255 Glu Val Lys Ala Ala Ala Ser Lys Val Lys Ala Asn Leu Leu Ser Val 260 265 270 Glu Glu Ala Cys Ser Leu Thr Pro Pro His Ser Ala Lys Ser Lys Phe 275 280 285 Gly Tyr Gly Ala Lys Asp Val Arg Cys His Ala Arg Lys Ala Val Thr 290 295 300 His lie Asn Ser Val Trp Lys Asp Leu Leu Glu Asp Asn Val Thr Pro 305 310 315 320 He Asp Thr Thr lie Met Ala Lys Asn Glu Val Phe Cys Val Gin Pro 325 330 335 Glu Lys Gly Gly Arg Lys Pro Ala Arg Leu He Val Phe Pro Asp Leu 340 345 350 Gly Val Arg Val Cys Glu Lys Met Ala Leu Tyr Asp Val Val Thr Lys 355 360 365 Leu Pro Leu Ala Val Met Gly Ser Ser Tyr Gly Phe Gin Tyr Ser Pro 370 375 380 Gly Gin Arg Val Glu Phe Leu Val Gin Ala Trp Lys Ser Lys Lys Thr 385 390 395 400 Pro Met Gly Phe Ser Tyr Asp Thr Arg Cys Phe Asp Ser Thr Val Thr 405 410 415 Glu Ser Asp lie Arg Thr Glu Glu Ala lie Tyr Gin Cys Cys Asp Leu 420 425 430 Asp Pro Gin Ala Arg Val Ala lie Lys Ser Leu Thr Glu Arg Leu Tyr 435 440 445 Val Gly Gly Pro Leu Thr Asn Ser Arg Gly Glu Asn Cys Gly Tyr Arg 450 455 460 Arg Cys Arg Ala Ser Gly Val Leu Thr Thr Ser Cys Gly Asn Thr Leu 465 470 475 480 Thr Cys Tyr lie Lys Aia Arg Ala Ala Cys Arg Ala Ala Gly Leu Gin 485 490 495 (2) INFORMATION FOR SEQ ID NO:32: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1161 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: circular (ii) MOLECULE TYPE: DNA (genomic) (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 1..1161 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:32: ATG AGTTTTGTG GTC ATT ATT CCC GCG CGC TAC GCGTCG ACG CGT CTG 48 Met Ser Phe Val Val We He Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 CCCGGTAAACCATTG GTTGATATTAAC GGCAAACCCATGATTGTTCAT 96 Pro Gly Lys Pro Leu Val Asp lie Asn Gly Lys Pro Met He Val His 20 25 30 GTT CTT GAA CGC GCG CGT GAA TCA GGT GCC GAG CGC ATC ATC GTG GCA 144 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg lie lie Val Ala 35 40 45 ACCGATCATGAGGATGTTGCCCGCGCCGTTGAAGCCGCTGGCGGTGAA 192 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 GTATGT ATG ACG CGC GCC GAT CAT CAG TCA GGA ACA GAA CGT CTG GCG 240 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 GAA GTT GTC GAA AAA TGC GCA TTC AGC GAC GAC ACG GTG ATC GTT AAT 288 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val He Val Asn 85 90 95 GTG CAG GGT GAT GAA CCG ATG ATC CCT GCG ACA ATC ATT CGT CAG GTT 336 Val Gin Gly Asp Glu Pro Met lie Pro Ala Thr lie He Arg Gin Val 100 105 110 GCTGATAACCTCGCTCAG CGTCAGGTG GGTATG GCGACTCTG GCG GTG 384 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Val 115 120 125 CCA ATC CAC AAT GCG GAA GAA GCG TTT AAC CCG AAT GCG GTG AAA GTG 432 Pro He His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 GTT CTC GAC GCT GAA GGG TAT GCA CTG TAC TTC TCT CGC GCC ACC ATT 480 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr He 145 150 155 160 CCTTGG GATCGTGATCGTTTTGCAGAAGGC CTTGAAACCGTTGGC GAT 528 Pro Tφ Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 AACTTCCTG CGTCATCTTGGTATTTATGGCTAC CGTGCAGGCTTTATC 576 Asn Phe Leu Arg His Leu Gly He Tyr Gly Tyr Arg Ala Gly Phe lie 180 185 190 CGTGGTTAC GTC AAC TGG CAG CCA AGT CCG TTA GAA CAC ATC GAA ATG 624 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His He Glu Met 195 200 205 TTAGAGCAG CTTCGTGTTCTGTGGTACGGCGAAAAAATC CATGTTGCT 672 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 GTT GCT CAG GAA GTT CCT GGC ACA GGT GTG GAT ACC CCT GAA GAT CTC 720 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 GACCCGTCGACGAATTGCATGCTGCAGGACTGCACCATGCTG GTTTGC 768 Asp Pro Ser Thr Asn Cys Met Leu Gin Asp Cys Thr Met Leu Val Cys 245 250 255 GGTGACGACCTGGTTGTTATCTGCGAATCTGCTGGTGTTCAGGAAGAC 816 Gly Asp Asp Leu Val Val lie Cys Glu Ser Ala Gly Val Gin Glu Asp 260 265 270 GCT GCTTCT CTG CGT GCTTTC ACC GAA GCT ATG ACC CGTTACTCTGCT 864 Ala Ala Ser Leu Arg Ala Phe Thr Glu Ala Met Thr Arg Tyr Ser Ala 275 280 285 CCCCCGGGTGACCXX3CCGCAGCCGGAATACGACCTGGAACTGATCACC 912 Pro Pro Gly Asp Pro Pro Gin Pro Glu Tyr Asp Leu Glu Leu lie Thr 290 295 300 TCTTGC TCTTCT AAC GTTTCT GTT GCT CAC GAC GGT GCT GGT AAA CGT 960 Ser Cys Ser Ser Asn Val Ser Val Ala His Asp Gly Ala Gly Lys Arg 305 310 315 320 GTTTAC TAC CTG ACC CGT GAC CCG ACC ACC CCG CTG GCT CGT GCT GCT 1008 Val Tyr Tyr Leu Thr Arg Asp Pro Thr Thr Pro Leu Ala Arg Ala Ala 325 330 335 TGG GAAACC GCT CGT CAC ACC CCG GTAAACTCTTGG CTG GGT AAC ATC 1056 Trp Glu Thr Ala Arg His Thr Pro Val Asn Ser Trp Leu Gly Asn He 340 345 350 ATCATGTTCGCTCCGACCCTGTGG GCCCGTATGATCCTGATGACCCAC 1104 He Met Phe Ala Pro Thr Leu Trp Ala Arg Met lie Leu Met Thr His 355 360 365 TTCTTCTCTGTTCTGATCGCTCGTGAC CAG CTG GAACAG GCTCTG GAC 1152 Phe Phe Ser Val Leu lie Ala Arg Asp Gin Leu Glu Gin Ala Leu Asp 370 375 380 TGC GAG ATC 1161 Cys Glu He 385 (2) INFORMATION FOR SEQ ID NO:33: (0 SEQUENCE CHARACTERISTICS: (A) LENGTH: 387 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:12: Met Ser Phe Val Val He lie Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 Pro Gly Lys Pro Leu Val Asp lie Asn Gly Lys Pro Met We Val His 20 25 30 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg lie lie Val Ala 35 40 45 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val He Val Asn 85 90 95 Val Gin Gly Asp Glu Pro Met lie Pro Ala Thr He We Arg Gin Val 100 105 1 10 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Val 115 120 125 Pro lie His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr He 145 150 155 160 Pro Tφ Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 Asn Phe Leu Arg His Leu Gly He Tyr Gly Tyr Arg Ala Gly Phe He 180 185 190 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His lie Glu Met 195 200 205 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 Asp Pro Ser Thr Asn Cys Met Leu Gin Asp Cys Thr Met Leu Val Cys 245 250 255 Gly Asp Asp Leu Val Val He Cys Glu Ser Ala Gly Val Gin Glu Asp 260 265 270 Ala Ala Ser Leu Arg Ala Phe Thr Glu Ala Met Thr Arg Tyr Ser Ala 275 280 285 Pro Pro Gly Asp Pro Pro Gin Pro Glu Tyr Asp Leu Glu Leu He Thr 290 295 300 Ser Cys Ser Ser Asn Val Ser Val Ala His Asp Gly Ala Gly Lys Arg 305 310 315 320 Val Tyr Tyr Leu Thr Arg Asp Pro Thr Thr Pro Leu Ala Arg Ala Ala 325 330 335 Trp Glu Thr Ala Arg His Thr Pro Val Asn Ser Trp Leu Gly Asn He 340 345 350 He Met Phe Ala Pro Thr Leu Trp Ala Arg Met He Leu Met Thr His 355 360 365 Phe Phe Ser Val Leu He Ala Arg Asp Gin Leu Glu Gin Ala Leu Asp 370 375 380 Cys Glu He 385 (2) INFORMATION FOR SEQ ID NO:34: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1179 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: circular (ii) MOLECULE TYPE: DNA (genomic) (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 1..1179 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:34: ATG AGTTTTGTG GTC ATT ATT CCC GCG CGC TAC GCGTCG ACG CGT CTG 48 Met Ser Phe Val Val He lie Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 CCCGGTAAACCATTG GTTGATATTAACGGCAAACCCATGATTGTTCAT 96 Pro Gly Lys Pro Leu Val Asp He Asn Gly Lys Pro Met He Val His 20 25 30 GTT CTT GAA CGC GCG CGT GAA TCA GGT GCC GAG CGC ATC ATC GTG GCA 144 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg lie lie Val Ala 35 40 45 ACC GAT CAT GAG GAT GTT GCC CGC GCC GTT GAA GCC GCT GGC GGT GAA 192 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 GTA TGT ATG ACG CGC GCC GAT CAT CAG TCA GGA ACA GAA CGT CTG GCG 240 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 GAAGTTGTCGAAAAATGC GCATTCAGCGAC GACACG GTGATCGTTAAT 288 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val lie Val Asn 85 90 95 GTGCAG GGTGATGAACCGATGATC CCTGCGACAATCATTCGTCAGGTT 336 Val Gin Gly Asp Glu Pro Met He Pro Ala Thr We lie Arg Gin Val 100 105 110 GCTGATAACCTCGCTCAGCGTCAG GTG GGTATG GCGACTCTGGCGGTG 384 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Val 115 120 125 CCA ATC CAC AAT GCG GAA GAA GCG TTT AAC CCG AAT GCG GTG AAA GTG 432 Pro He His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 GTT CTC GAC GCT GAA GGG TAT GCA CTG TAC TTC TCT CGC GCC ACC ATT 480 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr lie 145 150 155 160 (XTTGGGATCGTGATCX3TTTTGCAGMGGCCTTGAAACC GTTGGC GAT 528 Pro Tφ Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 AAC TTC CTG CGT CAT CTT GGT ATTTAT GGC TAC CGT GCA GGC TTT ATC 576 Asn Phe Leu Arg His Leu Gly lie Tyr Gly Tyr Arg Ala Gly Phe He 180 185 190 CGT CGT TAC GTC AAC TGG CAG CCA AGT CCG TTA GAA CAC ATC GAA ATG 624 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His He Glu Met 195 200 205 TTA GAG CAG CTT CGT GTT CTG TGG TAC GGC GAA AAA ATC CAT GTT GCT 672 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 GTTGCTCAGGAAGTTCCTGGCACAGGTGTGGATACCCCTGAAGATCTC 720 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 GAC CCG TCG ACG AATTCC ATG GAG ATC TAC GGT GCTTGC TAC TCT ATC 768 Asp Pro Ser Thr Asn Ser Met Glu He Tyr Gly Ala Cys Tyr Ser He 245 250 255 GAACCGCTGGACCTGCα3CCGATCATTCAGCGTCTGCACGGTCTGTCT 816 Glu Pro Leu Asp Leu Pro Pro He He Gin Arg Leu His Gly Leu Ser 260 265 270 GCTTTC TCT CTG CACTCTTAC TCC CCG GGT GAA ATC AAC CGT GTT GCT 864 Ala Phe Ser Leu His Ser Tyr Ser Pro Gly Glu He Asn Arg Val Ala 275 280 285 GCTTGC CTG CGT AAA CTG GGT GTT CCG CCG CTG CGTGCTTGG CGT CAC 912 Ala Cys Leu Arg Lys Leu Gly Val Pro Pro Leu Arg Ala Trp Arg His 290 295 300 CGTGCTCGTTCTGπCGTGCTCGTCTGCTGGCTCGTGGTGGCCGTGCT 960 Arg Ala Arg Ser Val Arg Ala Arg Leu Leu Ala Arg Gly Gly Arg Ala 305 310 315 320 GCTATCTGCGGTAAATACCTGTTCAACTGGGCTGTTCGTACCAAACTG 1008 Ala He Cys Gly Lys Tyr Leu Phe Asn Trp Ala Val Arg Thr Lys Leu 325 330 335 AAACTGACCCCGATCGCTGCTGCTGGTCAGCTGGACCTGTCTGGTTGG 1056 Lys Leu Thr Pro He Ala Ala Ala Gly Gin Leu Asp Leu Ser Gly Tφ 340 345 350 TTCACCGCTGGTTACTCTGGTGGTGACATCTACCACTCTGTTTCTCAC 1104 Phe Thr Ala Gly Tyr Ser Gly Gly Asp He Tyr His Ser Val Ser His 355 360 365 GCTCGTCCGCGTTGGATCTGGTTCTGCCTGCTGCTGCTGGCTGCTGGT 1152 Ala Arg Pro Arg Trp He Trp Phe Cys Leu Leu Leu Leu Ala Ala Gly 370 375 380 GTT GGT ATC TAC CTG CTG CCG AAC CGT 1179 Val Gly lie Tyr Leu Leu Pro Asn Arg 385 390 (2) INFORMATION FOR SEQ ID NO:35: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 393 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:35: Met Ser Phe Val Val He lie Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 Pro Gly Lys Pro Leu Val Asp lie Asn Gly Lys Pro Met We Val Hi . 20 25 30 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg lie lie Val Ala 35 40 45 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Aia Ala Gly Gly Glu 50 55 60 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Aι_ 65 70 75 80 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val He Val Asr 85 90 95 Val Gin Gly Asp Glu Pro Met lie Pro Aia Thr We We Arg Gin Val 100 105 110 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Va 115 120 125 Pro He His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Va 130 135 140 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr lie 145 150 155 160 Pro Tφ Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Aε 165 170 175 Asn Phe Leu Arg His Leu Gly lie Tyr Gly Tyr Arg Ala Gly Phe h- 180 185 190 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His He Glu M- 195 200 205 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ate 210 215 220 Val Ala Gin Glu Val Pro Gly Thr Gly Vai Asp Thr Pro Glu Asp Le 225 230 235 240 Asp Pro Ser Thr Asn Ser Met Glu We Tyr Gly Ala Cys Tyr Ser ι* 245 250 255 Glu Pro Leu Asp Leu Pro Pro lie lie Gin Arg Leu His Gly Leu Se 260 265 270 Ala Phe Ser Leu His Ser Tyr Ser Pro Gly Glu lie Asn Arg Val Aι 275 280 285 Ala Cys Leu Arg Lys Leu Gly Val Pro Pro Leu Arg Ala Tφ Arg H 290 295 300 Arg Ala Arg Ser Val Arg Ala Arg Leu Leu Ala Arg Gly Gly Arg Aι. 305 310 315 320 Ala lie Cys Gly Lys Tyr Leu Phe Asn Trp Ala Val Arg Thr Lys Leu 325 330 335 Lys Leu Thr Pro He Ala Ala Ala Gly Gin Leu Asp Leu Ser Gly Tφ 340 345 350 Phe Thr Ala Gly Tyr Ser Gly Gly Asp He Tyr His Ser Val Ser His 355 360 365 Ala Arg Pro Arg Trp He Trp Phe Cys Leu Leu Leu Leu Ala Ala Gly 370 375 380 Val Gly He Tyr Leu Leu Pro Asn Arg 385 390 (2) INFORMATION FOR SEQ ID NO:36: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1791 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: circular (ii) MOLECULE TYPE: DNA (genomic) (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 1..1791 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:36: ATG AGTTTTGTG GTC ATT ATT CCC GCG CGC TAC GCGTCG ACG CGT CTG 48 Met Ser Phe Val Val He He Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 CCC GGTAAACCATTG GTTGATATTAAC GGCAAACCCATGATTGTTCAT 96 Pro Gly Lys Pro Leu Val Asp He Asn Gly Lys Pro Met He Val His 20 25 30 GTTCTTGAACGCGCGCGTGAATCAGGTGCCGAG CGCATCATCGTGGCA 144 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg lie lie Val Ala 35 40 45 ACCGATCATGAGGATGTTGCX- CGCGCCGTTGAAGCCGCTGGCGGTGAA 192 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Aia Ala Gly Gly Glu 50 55 60 GTATGTATGACGCGCGCCGATCATCAGTCAGGAACAGAACGTCTGGCG 240 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 GAAGTTGTCGAAAAATGC GCATTCAGC GACGACACG GTGATCGTTAAT 288 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val We Val Asn 85 90 95 GTG CAG GGT GAT GAA CCG ATG ATC CCT GCG ACA ATC ATT CGT CAG GTT 336 Val Gin Gly Asp Glu Pro Met lie Pro Ala Thr lie We Arg Gin Val 100 105 110 GCT GAT AAC CTC GCT CAG CGT CAG GTG GGT ATG GCG ACT CTG GCG GTG 384 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Val 115 120 125 CX AATC CACMTG(^ GMGM GC_GT1T C CCGAATGCG GTGAAA GTG 432 Pro He His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 GTT CTC GAC GCT GAA GGG TAT GCA CTG TAC TTC TCT CGC GCC ACC ATT 480 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr lie 145 150 155 160 CCTTG aGATCGTGATCGTTTTGCAGMGGCCTTGAAACCGTTGGC GAT 528 Pro Tφ Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 AAC TTC CTG CGT CAT CTT GGT ATT TAT GGC TAC CGT GCA GGC TTT ATC 576 Asn Phe Leu Arg His Leu Gly lie Tyr Gly Tyr Arg Ala Gly Phe lie 180 185 190 CGT CGTTAC GTC AAC TGG CAG CCA AGT CCG TTA GAA CAC ATC GAA ATG 624 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His He Glu Met 195 200 205 TTA GAG CAG CTT CGT GTT CTG TGG TAC GGC GAA AAA ATC CAT GTT GCT 672 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 GTT GCT CAG GAA GTT CCT GGC ACA GGT GTG GAT ACC CCT GAA GAT CTC 720 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 GACCCGTCGACGAATTCCATG GACGCTCACTTC CTGTCTCAGGCGCCG 768 Asp Pro Ser Thr Asn Ser Met Asp Ala His Phe Leu Ser Gin Ala Pro 245 250 255 CCG CCG TCTTGG GAT CAG ATG TGG AAA TGC CTG ATC CGT CTG AAA CCG 816 Pro Pro Ser Tφ Asp Gin Met Trp Lys Cys Leu lie Arg Leu Lys Pro 260 265 270 ACCCTGCACGGCCCGACCCCGCTGCTGTACCGTCTGGGTGCTGTTCAG 854 Thr Leu His Gly Pro Thr Pro Leu Leu Tyr Arg Leu Gly Ala Val Gin 275 280 285 AAC GAA ATC ACC CTG ACC CAC CCG GTT ACC AAA TAC ATC ATG ACC TGC 912 Asn Glu He Thr Leu Thr His Pro Val Thr Lys Tyr lie Met Thr Cys 290 295 300 ATG TCT GCT GAT CTA GAA GTT GTT ACC TCT ACC TGG GTT CTG GTT GGT 960 Met Ser Ala Asp Leu Glu Val Val Thr Ser Thr Trp Val Leu Val Gly 305 310 315 320 GGT GTT CTG GCT GCT CTG GCT GCTTAC TGC CTG TCG ACC GGTTGC GTT 1008 Gly Val Leu Ala Ala Leu Ala Ala Tyr Cys Leu Ser Thr Gly Cys Val 325 330 335 GTTATCGTTGGTCGTGTTGTTCTGTCTGGTAAACCGGCCATTATCCCG 1056 Val He Val Gly Arg Val Val Leu Ser Gly Lys Pro Ala He He Pro 340 345 350 GAC CGT GAA GTT CTG TAC CGT GAG TTC GAC GAA ATG GAA GAA TGC TCT 1104 Asp Arg Glu Val Leu Tyr Arg Glu Phe Asp Glu Met Glu Glu Cys Ser 355 360 365 CAG CAC CTG CCG TAC ATC GAA CAG GGT ATG ATG CTG GCT GAA CAG TTC 1152 Gin His Leu Pro Tyr He Glu Gin Gly Met Met Leu Ala Glu Gin Phe 370 375 380 AAACAGAAAGCTCTGGGTCTGCTGCAGACCGCTTCTCGTCAGGCTGAA 1200 Lys Gin Lys Ala Leu Gly Leu Leu Gin Thr Ala Ser Arg Gin Ala Glu 385 390 395 400 GTTATCGCTCCGGCTGTTCAGACCAACTGGCAGAAACTCGAGACCTTC 1248 Val lie Ala Pro Ala Val Gin Thr Asn Trp Gin Lys Leu Glu Thr Phe 405 410 415 TGG GCT AAA CAC ATG TGG AAC TTC ATC TCT GGT ATC CAG TAC CTG GCT 1296 Trp Ala Lys His Met Trp Asn Phe He Ser Gly He Gin Tyr Leu Ala 420 425 430 GGT CTG TCT ACC CTG CCG GGT AAC CCG GCT ATC GCA AGC TTG ATG GCT 1344 Gly Leu Ser Thr Leu Pro Gly Asn Pro Ala lie Ala Ser Leu Met Ala 435 440 445 TTCACCGCTGCTGTTACCTCTCCGCTGACCACCTCTCAGACCCTGCTG 1392 Phe Thr Ala Ala Val Thr Ser Pro Leu Thr Thr Ser Gin Thr Leu Leu 450 455 460 TTC AAC ATT CTG GGT GGTTGG GTT GCT GCT CAG CTG GCT GCT CCG GGT 1440 Phe Asn He Leu Gly Gly Trp Val Ala Ala Gin Leu Ala Ala Pro Gly 465 470 475 480 GCTGCTACCGCTTTCGTTGGTGCTGGTCTGGCTGGTGCTGCTATCGGT 1488 Ala Ala Thr Ala Phe Val Gly Ala Gly Leu Ala Gly Ala Ala He Gly 485 490 495 TCT GTA GGC CTG GGT AAA GTT CTG ATC GAC ATT CTG GCT GGTTAC GGT 1536 Ser Val Gly Leu Gly Lys Val Leu lie Asp He Leu Ala Gly Tyr Gly 500 505 510 GCTGGTGTTGCTGGAGCTCTGGTTGCTTTCAAAATCATGTCTGGTGAA 1584 Ala Gly Val Ala Gly Ala Leu Val Ala Phe Lys He Met Ser Gly Glu 515 520 525 GTTCCGTCTACCGAAGATCTG GπAACCTG CTGCCGGCTATC CTGTCT 1632 Val Pro Ser Thr Glu Asp Leu Val Asn Leu Leu Pro Ala He Leu Ser 530 535 540 CCG GGT GCT CTG GTT GTT GGT GTT GTT TGC GCT GCT ATC CTG CGT CGT 1680 Pro Gly Ala Leu Val Val Gly Val Val Cys Ala Ala He Leu Arg Arg 545 550 555 560 CACGTTGGCCCGGGTGAAGGTGCTGTTCAGTGGATGAACCGTCTGATC 1728 His Val Gly Pro Gly Glu Gly Ala Val Gin Trp Met Asn Arg Leu He 565 570 575 GCT TTC GCT TCT CGT GGT AAC CAC GTT TCT CCA TGG GAT CCT CTA GAC 1776 Ala Phe Ala Ser Arg Gly Asn His Val Ser Pro Tφ Asp Pro Leu Asp 580 585 590 TGC AGG CAT GCT AAG 1791 Cys Arg His Ala Lys 595 (2) INFORMATION FOR SEQ ID NO:37: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 597 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:37: Met Ser Phe Val Val He lie Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 Pro Gly Lys Pro Leu Val Asp lie Asn Gly Lys Pro Met He Val His 20 25 30 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg lie lie Val Ala 35 40 45 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val He Val Asn 85 90 95 Val Gin Gly Asp Glu Pro Met lie Pro Ala Thr We We Arg Gin Val 100 105 110 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Val 115 120 125 Pro He His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr He 145 150 155 160 Pro Trp Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 Asn Phe Leu Arg His Leu Gly He Tyr Gly Tyr Arg Ala Gly Phe He 180 185 190 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His He Glu Met 195 200 205 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 Asp Pro Ser Thr Asn Ser Met Asp Ala His Phe Leu Ser Gin Ala Pro 245 250 255 Pro Pro Ser Trp Asp Gin Met Trp Lys Cys Leu He Arg Leu Lys Pro 260 265 270 Thr Leu His Gly Pro Thr Pro Leu Leu Tyr Arg Leu Gly Ala Val Gin 275 280 285 Asn Glu lie Thr Leu Thr His Pro Val Thr Lys Tyr lie Met Thr Cys 290 295 300 Met Ser Ala Asp Leu Glu Val Val Thr Ser Thr Trp Val Leu Val Gly 305 310 315 320 Gly Val Leu Ala Ala Leu Ala Ala Tyr Cys Leu Ser Thr Gly Cys Val 325 330 335 Val He Val Gly Arg Val Val Leu Ser Gly Lys Pro Ala He He Pro 340 345 350 Asp Arg Glu Val Leu Tyr Arg Glu Phe Asp Glu Met Glu Glu Cys Ser 355 360 365 Gin His Leu Pro Tyr He Glu Gin Gly Met Met Leu Ala Glu Gin Phe 370 375 380 Lys Gin Lys Ala Leu Gly Leu Leu Gin Thr Ala Ser Arg Gin Ala Glu 385 390 395 400 Val He Ala Pro Aia Val Gin Thr Asn Trp Gin Lys Leu Glu Thr Phe 405 410 415 Trp Ala Lys His Met Trp Asn Phe lie Ser Gly He Gin Tyr Leu Ala 420 425 430 Gly Leu Ser Thr Leu Pro Gly Asn Pro Ala lie Ala Ser Leu Met Ala 435 440 445 Phe Thr Ala Ala Val Thr Ser Pro Leu Thr Thr Ser Gin Thr Leu Leu 450 455 460 Phe Asn He Leu Gly Gly Tφ Val Ala Ala Gin Leu Ala Ala Pro Gly 465 470 475 480 Ala Ala Thr Ala Phe Val Gly Ala Gly Leu Ala Gly Ala Ala He Gly 485 490 495 Ser Val Gly Leu Gly Lys Val Leu He Asp lie Leu Ala Gly Tyr Gly 500 505 510 Ala Gly Val Ala Gly Ala Leu Val Ala Phe Lys He Met Ser Gly Glu 515 520 525 Val Pro Ser Thr Glu Asp Leu Val Asn Leu Leu Pro Ala He Leu Ser 530 535 540 Pro Gly Ala Leu Val Val Gly Val Val Cys Ala Ala He Leu Arg Arg 545 550 555 560 His Val Gly Pro Gly Glu Gly Ala Val Gin Trp Met Asn Arg Leu He 565 570 575 Ala Phe Ala Ser Arg Gly Asn His Val Ser Pro Trp Asp Pro Leu Asp 580 585 590 Cys Arg His Ala Lys 595 (2) INFORMATION FOR SEQ ID NO:38: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1797 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: circular (ii) MOLECULE TYPE: DNA (genomic) (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 1..1797 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:38: ATG AGTTTT GTG GTC ATT ATT CCC GCG CGC TAC GCG TCG ACG CGT CTG 48 Met Ser Phe Val Val He He Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 CCC GGTAAACCATTGGTTGATATTAAC GGCAAACCCATGATTGTTCAT 96 Pro Gly Lys Pro Leu Val Asp He Asn Gly Lys Pro Met He Val His 20 25 30 GTTCTTGMCGCGCGCGTGAATCAGGTGCCGAGCGCATCATCGTGGCA 144 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg lie lie Val Ala 35 40 45 ACCGATC^TGAGGATGTTGCCCGCGCCGTTGAAGCCGCTGGCGGTGAA 192 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 GTATGTATGACGCGCGCCGATCATCAGTCAGGAACAGAACGTCTGGCG 240 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 GAA GTT GTC GAA AAA TGC GCA TTC AGC GAC GAC ACG GTG ATC GTT AAT 288 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val He Val Asn 85 90 95 GTG CAG GGT GAT GAA CCG ATG ATC CCT GCG ACA ATC ATT CGT CAG GTT 336 Val Gin Gly Asp Glu Pro Met He Pro Ala Thr He He Arg Gin Val 100 105 1 10 GCTGATAACCTCGCTCAG CGTCAGGTGGGTATGGCGACTCTGGCGGTG 384 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Val 115 120 125 CCAATCCACMTGCG GMG GCX3TTTAACCCGAATGCGGTGAAAGTG 432 Pro He His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 GTT CTC GAC GCT GAA GGG TAT GCA CTG TAC TTC TCT CGC GCC ACC ATT 480 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr He 145 150 155 160 CCTTGGGATCGTGATCGTTTTGCAGAAGGC CπGAAACCGTTGGC GAT 528 Pro Trp Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 AAC TTC CTG CGT CAT CTT GGT ATTTAT GGC TAC CGT GCA GGC TTT ATC 576 Asn Phe Leu Arg His Leu Gly He Tyr Gly Tyr Arg Ala Gly Phe lie 180 185 190 CGT CGTTAC GTC AAC TGG CAG CCA AGT CCG TTA GAA CAC ATC GAA ATG 624 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His He Glu Met 195 200 205 TTA GAG CAG CTT CGT GTT CTG TGG TAC GGC GAA AAA ATC CAT GTT GCT 672 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 GTTGCTCAGGAAGTTCCTGGCACA GGTGTGGATACCCCTGAA GATCTC 720 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 GAC CCGTCGACGAATTCCATGGAC GCTCACTTCCTGTCTCAGACCAAA 768 Asp Pro Ser Thr Asn Ser Met Asp Ala His Phe Leu Ser Gin Thr Lys 245 250 255 CAG TCT GGT GAA AAC CTT CCG TAC CTG GTT GCTTAC CAG GCT ACC GTT 816 Gin Ser Gly Glu Asn Leu Pro Tyr Leu Val Ala Tyr Gin Ala Thr Val 260 265 270 TGCGCTCGTGCTCAG GCCCCGACC CCGCTG CTGTACCGTCTGGGTGCT 864 Cys Ala Arg Ala Gin Ala Pro Thr Pro Leu Leu Tyr Arg Leu Gly Ala 275 280 285 GTT CAG AAC GAA ATC ACC CTG ACC CAC CCG GTT ACC AAA TAC ATC ATG 912 Val Gin Asn Glu He Thr Leu Thr His Pro Val Thr Lys Tyr He Met 290 295 300 ACC TGC ATG TCT GCT GAT CTA GAA GTT GTT ACC TCT ACC TGG GTT CTG 960 Thr Cys Met Ser Ala Asp Leu Glu Val Val Thr Ser Thr Tφ Val Leu 305 310 315 320 GTT GGT GGT GTT CTG GCT GCT CTG GCT GCTTAC TGC CTG TCG ACC GGT 1008 Val Gly Gly Val Leu Ala Ala Leu Ala Ala Tyr Cys Leu Ser Thr Gly 325 330 335 TGCGTTGTTATC GTTGGTCGTGTTGTTCTGTCTGGTAAA CCG GCCATT 1056 Cys Val Val We Val Gly Arg Val Val Leu Ser Gly Lys Pro Ala lie 340 345 350 ATC CCG GAC CGT GAA GTT CTG TAC CGT GAG TTC GAC GAA ATG GAA GAA 1104 He Pro Asp Arg Glu Val Leu Tyr Arg Glu Phe Asp Glu Met Glu Glu 355 360 365 TGC TCT CAG CAC CTG CCG TAC ATC GAA CAG GGT ATG ATG CTG GCT GAA 1152 Cys Ser Gin His Leu Pro Tyr lie Glu Gin Gly Met Met Leu Ala Glu 370 375 380 CAG TTC AAA CAG AAA GCT CTG GGT CTG CTG CAG ACC GCTTCT CGT CAG 1200 Gin Phe Lys Gin Lys Ala Leu Gly Leu Leu Gin Thr Ala Ser Arg Gin 385 390 395 400 GCT GAA GTT ATC GCT CCG GCT GTT CAG ACC AAC TGG CAG AAA CTC GAG 1248 Ala Glu Val We Ala Pro Ala Val Gin Thr Asn Trp Gin Lys Leu Glu 405 410 415 ACC TTC TGG GCT AAA CAC ATG TGG AAC TTC ATC TCT GGT ATC CAG TAC 1296 Thr Phe Tφ Ala Lys His Met Trp Asn Phe lie Ser Gly lie Gin Tyr 420 425 430 CTG GCT GGT CTG TCT ACC CTG CCG GGT AAC CCG GCT ATC GCAAGCTTG 1344 Leu Ala Gly Leu Ser Thr Leu Pro Gly Asn Pro Ala lie Ala Ser Leu 435 440 445 ATGGCTTTCACCGCTGCTGTTACCTCTCCG CTGACCACCTCTCAGACC 1392 Met Ala Phe Thr Ala Ala Val Thr Ser Pro Leu Thr Thr Ser Gin Thr 450 455 460 CTG CTG TTC AAC ATT CTG GGT GGTTGG GTT GCT GCT CAG CTG GCT GCT 1440 Leu Leu Phe Asn We Leu Gly Gly Trp Val Ala Ala Gin Leu Ala Ala 465 470 475 480 CCGGGTGCTGCTACCGCTTTCGTTGGTGCTGGTCTG GCTGGTGCTGCT 1488 Pro Gly Ala Ala Thr Ala Phe Val Gly Ala Gly Leu Ala Gly Ala Ala 485 490 495 ATC GGT TCT GTA GGC CTG GGT AAA GTT CTG ATC GAC ATT CTG GCT GGT 1536 He Gly Ser Val Gly Leu Gly Lys Val Leu lie Asp He Leu Ala Gly 500 505 510 TAC GGT GCT GGT GTT GCT GGA GCT CTG GTT GCTTTC AAA ATC ATG TCT 1584 Tyr Gly Ala Gly Val Ala Gly Ala Leu Val Ala Phe Lys He Met Ser 515 520 525 GGTGAAGTTCCGTCTACCGAAGATCTG GTTAAC CTG CTGCCGGCTATC 1632 Gly Glu Val Pro Ser Thr Glu Asp Leu Val Asn Leu Leu Pro Ala He 530 535 540 CTGTCTCCG GGTGCTCTG GTTGTTGGTGTTGTTTGCGCTGCTATC CTG 1680 Leu Ser Pro Gly Ala Leu Val Val Gly Val Val Cys Ala Ala lie Leu 545 550 555 560 CGTCGTCACGTTGGCCCGGGTGAAGGTGCTGTTCAGTGGATGAACCGT 1728 Arg Arg His Val Gly Pro Gly Glu Gly Ala Val Gin Trp Met Asn Arg 565 570 575 CTG ATCGCTTTC GCT TCT CGT GGT AAC CAC GTTTCT CCA TGG GAT CCT 1776 Leu He Ala Phe Ala Ser Arg Gly Asn His Val Ser Pro Trp Asp Pro 580 585 590 CTA GAC TGC AGG CAT GCT AAG 1797 Leu Asp Cys Arg His Ala Lys 595 (2) INFORMATION FOR SEQ ID NO:39: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 599 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:39: Met Ser Phe Val Val He lie Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 Pro Gly Lys Pro Leu Val Asp lie Asn Gly Lys Pro Met We Val His 20 25 30 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg lie lie Val Ala 35 40 45 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val lie Val Asn 85 90 95 Val Gin Gly Asp Glu Pro Met lie Pro Ala Thr He He Arg Gin Val 100 105 1 10 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Val 115 120 125 Pro He His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr He 145 150 155 160 Pro Tφ Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 Asn Phe Leu Arg His Leu Gly lie Tyr Gly Tyr Arg Ala Gly Phe He 180 185 190 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His We Glu Met 195 200 205 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 Vai Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 Asp Pro Ser Thr Asn Ser Met Asp Ala His Phe Leu Ser Gin Thr Lys 245 250 255 Gin Ser Gly Glu Asn Leu Pro Tyr Leu Val Ala Tyr Gin Ala Thr Val 260 265 270 Cys Ala Arg Ala Gin Ala Pro Thr Pro Leu Leu Tyr Arg Leu Gly Ala 275 280 285 Val Gin Asn Glu He Thr Leu Thr His Pro Val Thr Lys Tyr He Met 290 295 300 Thr Cys Met Ser Ala Asp Leu Glu Val Val Thr Ser Thr Trp Val Leu 305 310 315 320 Val Gly Gly Val Leu Ala Ala Leu Ala Ala Tyr Cys Leu Ser Thr Gly 325 330 335 Cys Val Val He Val Gly Arg Val Val Leu Ser Gly Lys Pro Ala He 340 345 350 He Pro Asp Arg Glu Val Leu Tyr Arg Glu Phe Asp Glu Met Glu Glu 355 360 365 Cys Ser Gin His Leu Pro Tyr He Glu Gin Gly Met Met Leu Ala Glu 370 375 380 Gin Phe Lys Gin Lys Ala Leu Gly Leu Leu Gin Thr Ala Ser Arg Gin 385 390 395 400 Ala Glu Val He Ala Pro Ala Val Gin Thr Asn Trp Gin Lys Leu Glu 405 410 415 Thr Phe Tφ Ala Lys His Met Trp Asn Phe He Ser Gly He Gin Tyr 420 425 430 Leu Ala Gly Leu Ser Thr Leu Pro Gly Asn Pro Ala He Ala Ser Leu 435 440 445 Met Ala Phe Thr Ala Ala Val Thr Ser Pro Leu Thr Thr Ser Gin Thr 450 455 460 Leu Leu Phe Asn lie Leu Gly Gly Trp Val Ala Ala Gin Leu Ala Ala 465 470 475 480 Pro Gly Ala Ala Thr Ala Phe Val Gly Ala Gly Leu Aia Gly Ala Ala 485 490 495 He Gly Ser Val Gly Leu Gly Lys Val Leu He Asp He Leu Ala Gly 500 505 510 Tyr Gly Ala Gly Val Ala Gly Ala Leu Val Ala Phe Lys He Met Ser 515 520 525 Gly Glu Val Pro Ser Thr Glu Asp Leu Val Asn Leu Leu Pro Aia He 530 535 540 Leu Ser Pro Gly Ala Leu Val Val Gly Val Val Cys Ala Ala He Leu 545 550 555 560 Arg Arg His Val Gly Pro Gly Glu Gly Ala Val Gin Trp Met Asn Arg 565 570 575 Leu He Ala Phe Ala Ser Arg Gly Asn His Val Ser Pro Trp Asp Pro 580 585 590 Leu Asp Cys Arg His Ala Lys 595 (2) INFORMATION FOR SEQ ID NO.40: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1251 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: circular (ii) MOLECULE TYPE: DNA (genomic) (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 1..1251 (xi) SEQUENCE DESCRIPTION: SEQ ID NO.40: ATG AGTTTT GTG GTC ATT ATT CCC GCG CGC TAC GCG TCG ACG CGT CTG 48 Met Ser Phe Val Val We lie Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 CCC GGT AAA CCA TTG GTT GAT ATT AAC GGC AAA CCC ATG ATT GTT CAT 96 Pro Gly Lys Pro Leu Val Asp lie Asn Gly Lys Pro Met He Val His 20 25 30 GTT CTT GAA CGC GCG CGT GAA TCA GGT GCC GAG CGC ATC ATC GTG GCA 144 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg lie lie Val Ala 35 40 45 ACCGATCATGAGGATGTTGCC CGCGCCGTTGAAGCC GCTGGCGGTGAA 192 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 GTATGTATGACGCGCGCCGATCATCAGTCAGGAACAGAACGTCTGGCG 240 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 GAA GTT GTC GAA AAA TGC GCA TTC AGC GAC GAC ACG GTG ATC GTT AAT 288 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val lie Val Asn 85 90 95 GTG CAG GGT GAT GAA CCG ATG ATC CCT GCG ACA ATC ATT CGT CAG GTT 336 Val Gin Gly Asp Glu Pro Met lie Pro Ala Thr lie lie Arg Gin Val 100 105 1 10 GCT GAT AAC CTC GCT CAG CGT CAG GTG GGT ATG GCG ACT CTG GCG GTG 384 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Val 115 120 125 CCAATCCACMTGCG GMGMG STTTAAC CCGAATGCG GTGAAA GTG 432 Pro We His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 GTTCTC GAC GCTGAAGGGTATGCACTGTACTTCTCTCGC GCCACCATT 480 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr He 145 150 155 160 CCTTGGGATαSTGATCGTTTTGCAGAAGGCCTTGAAACCGTTGGC GAT 528 Pro Tφ Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 AAC TTC CTG CGTCATCTTGGTATTTATGGCTAC CGT GCA GGC TTT ATC 576 Asn Phe Leu Arg His Leu Gly He Tyr Gly Tyr Arg Ala Gly Phe lie 180 185 190 CGTGGTTAC GTC AAC TGG CAG CCA AGT CCG TTA GAA CAC ATC GAA ATG 624 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His lie Glu Met 195 200 205 TTA GAG CAG CTT CGT GTT CTG TGG TAC GGC GAA AAA ATC CAT GTT GCT 672 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 GTTGCTCAGGAAGTTCCTGGCACAGGTGTGGATACC CCTGAAGATCTC 720 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 GAC CCG TCG ACT CGA ATT CGA GCT CGG TAC CCT GAG ACA ATC ACG CTT 768 Asp Pro Ser Thr Arg He Arg Ala Arg Tyr Pro Glu Thr He Thr Leu 245 250 255 CCC ( ^GGATGCTGTCTCCCGCACCCAGCCTCGGGGCAGGACTGGCAGG 816 Pro Gin Asp Ala Val Ser Arg Thr Gin Arg Arg Gly Arg Thr Gly Arg 260 265 270 GGGMGCCAGGCATCTACAGATTTGTGGCACCGGGGGAGCGCCCTTCC 864 Gly Lys Pro Gly He Tyr Arg Phe Val Ala Pro Gly Glu Arg Pro Ser 275 280 285 GGC ATG TTC GACTCGTCCGTC CTC TGC GAG TGC TAT GAC GCG GGC TGG 912 Gly Met Phe Asp Ser Ser Val Leu Cys Glu Cys Tyr Asp Ala Gly Trp 290 295 300 CCTTGG TAT GAG CTC ACA CCC GCC GAG ACC ACA GTT AGG CTA CGA GCG 960 Pro Trp Tyr Glu Leu Thr Pro Ala Glu Thr Thr Val Arg Leu Arg Ala 305 310 315 320 TAC ATG AAC ACC CCG GGA CTC CCC GTG TGC CAA GAC CAT CTT GAA TTT 1008 Tyr Met Asn Thr Pro Gly Leu Pro Val Cys Gin Asp His Leu Glu Phe 325 330 335 TGG GAG GGC GTC TTC ACG GGT CTC ACC CAT ATA GAC GCC CAC TTT CTA 1056 Tφ Glu Gly Val Phe Thr Gly Leu Thr His lie Asp Ala His Phe Leu 340 345 350 TCC CAG ACA AAG CAG AGT GGG GAA AAC CTT CCT TAC CTG GTA GCG TAC 1104 Ser Gin Thr Lys Gin Ser Gly Glu Asn Leu Pro Tyr Leu Val Ala Tyr 355 360 365 CMGCCACCGTGTGCGCTAGAGCTCAAGCCCCTCCCCCATCGTGGGAC 1152 Gin Ala Thr Val Cys Ala Arg Ala Gin Ala Pro Pro Pro Ser Trp Asp 370 375 380 CAG ATG TGG AAG TGC TTG ATC CGC CTC AAG CCT ACC CTT CAT GGG CCG 1200 Gin Met Tφ Lys Cys Leu lie Arg Leu Lys Pro Thr Leu His Gly Pro 385 390 395 400 ACC CCC CTG CTA TAC AGA CTG GGC GGG GGATCCTCT AGA CTG CAG GCA 1248 Thr Pro Leu Leu Tyr Arg Leu Gly Gly Gly Ser Ser Arg Leu Gin Ala 405 410 415 TGC 1251 Cys (2) INFORMATION FOR SEQ ID NO:41 : (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 417 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:41 : Met Ser Phe Val Val He lie Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 Pro Gly Lys Pro Leu Val Asp lie Asn Gly Lys Pro Met lie Val His 20 25 30 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg lie lie Val Ala 35 40 45 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val He Val Asn 85 90 95 Val Gin Gly Asp Glu Pro Met lie Pro Ala Thr lie He Arg Gin Val 100 105 110 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Val 1 15 120 125 Pro He His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr He 145 150 155 160 Pro Trp Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 Asn Phe Leu Arg His Leu Gly lie Tyr Gly Tyr Arg Ala Gly Phe He 180 185 190 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His He Glu Met 195 200 205 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 Asp Pro Ser Thr Arg He Arg Ala Arg Tyr Pro Glu Thr He Thr Leu 245 250 255 Pro Gin Asp Ala Val Ser Arg Thr Gin Arg Arg Gly Arg Thr Gly Arg 260 265 270 Gly Lys Pro Gly He Tyr Arg Phe Val Ala Pro Gly Glu Arg Pro Ser 275 280 285 Gly Met Phe Asp Ser Ser Val Leu Cys Glu Cys Tyr Asp Ala Gly Trp 290 295 300 Pro Trp Tyr Glu Leu Thr Pro Ala Glu Thr Thr Val Arg Leu Arg Ala 305 310 315 320 Tyr Met Asn Thr Pro Gly Leu Pro Val Cys Gin Asp His Leu Glu Phe 325 330 335 Tφ Glu Gly Val Phe Thr Gly Leu Thr His lie Asp Ala His Phe Leu 340 345 350 Ser Gin Thr Lys Gin Ser Gly Glu Asn Leu Pro Tyr Leu Val Ala Tyr 355 360 365 Gin Ala Thr Val Cys Ala Arg Ala Gin Ala Pro Pro Pro Ser Trp Asp 370 375 380 Gin Met Trp Lys Cys Leu lie Arg Leu Lys Pro Thr Leu His Gly Pro 385 390 395 400 Thr Pro Leu Leu Tyr Arg Leu Gly Gly Gly Ser Ser Arg Leu Gin Ala 405 410 415 Cys (2) INFORMATION FOR SEQ ID NO:42: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1275 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: circular (ii) MOLECULE TYPE: DNA (genomic) (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 1..1275 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:42: ATG AGTTTTGTG GTC ATT ATT CCC GCG CGC TAC GCGTCG ACG CGT CTG 48 Met Ser Phe Val Val He He Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 CCC GGT AAA CCA TTG GTT GAT ATT AAC GGC AAA CCC ATG ATT GTT CAT 96 Pro Gly Lys Pro Leu Val Asp He Asn Gly Lys Pro Met We Val His 20 25 30 GΠTCΓΓTGM CGC G(_X_5CGTGAATCAGGTGCCGAG CGCATCATC GTG GCA 144 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg lie lie Val Ala 35 40 45 ACC GAT CAT GAG GAT GTT GCC CGC GCC GTT GAA GCC GCT GGC GGT GAA 192 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 GTATGT ATG ACG CGC GCC GAT CAT CAG TCA GGA ACA GAA CGT CTG GCG 240 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 GAA GTT GTC GAA AAA TGC GCA TTC AGC GAC GAC ACG GTG ATC GTT AAT 288 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val He Val Asn 85 90 95 GTG CAG GGT GAT GAA CCG ATG ATC CCT GCG ACA ATC ATT CGT CAG GTT 336 Val Gin Gly Asp Glu Pro Met He Pro Ala Thr He He Arg Gin Val 100 105 1 10 GCTGATAACCTCGCTCAG CGTCAG GTG GGTATG GCGACTCTGGCG GTG 384 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Val 115 120 125 CCA ATC CAC AAT GCG GAA GAA GCG TTT AAC CCG AAT GCG GTG AAA GTG 432 Pro He His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 GTT CTC GAC GCT GAA GGG TAT GCA CTG TAC TTC TCT CGC GCC ACC ATT 480 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr lie 145 150 155 160 CCTTGGGATCGTGATCGTTTTGCAGAAGGCCTTGAAACCGTTGGCGAT 528 Pro Tφ Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 AAC TTC CTG CGT CAT CTT GGT ATTTAT GGC TAC CGT GCA GGC TTT ATC 576 Asn Phe Leu Arg His Leu Gly He Tyr Gly Tyr Arg Ala Gly Phe He 180 185 190 CGT CGT TAC GTC AAC TGG CAG CCA AGT CCG TTA GAA CAC ATC GAA ATG 624 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His He Glu Met 195 200 205 TTA GAG CAG CTT CGT GTT CTG TGG TAC GGC GAA AAA ATC CAT GTT GCT 672 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 GTT GCT CAG GAA GTT CCT GGC ACA GGT GTG GAT ACC CCT GAA GAT CTC 720 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 GAC CCG TCG ACT CGA ATT CGT AGG TCG CGC AATTTG GGTAAG GTC ATC 768 Asp Pro Ser Thr Arg He Arg Arg Ser Arg Asn Leu Gly Lys Val He 245 250 255 GACACCCTCACGTGCGGCTTCGCCGACCTCATGGGGTATATTCCGCTC 816 Asp Thr Leu Thr Cys Gly Phe Ala Asp Leu Met Gly Tyr He Pro Leu 260 265 270 GTCGGCGCCCCTCTTG _V\GGCGCTGCCAGGGCCCTGGGCCATGGCGTC 864 Val Gly Ala Pro Leu Gly Gly Ala Ala Arg Ala Leu Gly His Gly Val 275 280 285 CGGGTTCTGGAAGACGGCGTGMCTATGCGACAGGGAATCTTCCTGGT 912 Arg Val Leu Glu Asp Gly Val Asn Tyr Ala Thr Gly Asn Leu Pro Gly 290 295 300 TGC TCT TTC TCT ATC TTC CTT CTG GCC CTG CTC TCT TGC CTG ACC GTG 960 Cys Ser Phe Ser He Phe Leu Leu Ala Leu Leu Ser Cys Leu Thr Val 305 310 315 320 CCC GCA TCA GCC TAC CAA GTA CGC AAC TCC TCG GGC CTTTAC CAT GTC 1008 Pro Ala Ser Ala Tyr Gin Val Arg Asn Ser Ser Gly Leu Tyr His Val 325 330 335 ACCMTGATTGCCCCAACTCGAGTATTGTGTACGAGACGGCCGATGCC 1056 Thr Asn Asp Cys Pro Asn Ser Ser lie Val Tyr Glu Thr Ala Asp Ala 340 345 350 ATCCTGCACACTCCGGGGTGCGTCCCTTGCGTTCGTGAGGGCAACGCC 1104 He Leu His Thr Pro Gly Cys Val Pro Cys Val Arg Glu Gly Asn Ala 355 360 365 TCG AGA TGTTGG GTG GCG GTG GCC CCC ACA GTG GCC ACC AGG GAT GGA 1152 Ser Arg Cys Trp Val Ala Val Ala Pro Thr Val Ala Thr Arg Asp Gly 370 375 380 AAA CTC CCC GCA ACG CAG CTT CGA CGT CAC ATT GAT CTG CTT GTC GGG 1200 Lys Leu Pro Ala Thr Gin Leu Arg Arg His He Asp Leu Leu Val Gly 385 390 395 400 AGC GCC ACC CTC TGTTCG GCC CTC TAC TTA AGG AGC TCG GTA CCC GGG 1248 Ser Ala Thr Leu Cys Ser Ala Leu Tyr Leu Arg Ser Ser Val Pro Gly 405 410 415 GAT CCT CTA GAC TGC AGG CAT GCT AAG 1275 Asp Pro Leu Asp Cys Arg His Ala Lys 420 425 (2) INFORMATION FOR SEQ ID NO:43: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 425 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:43: Met Ser Phe Val Val He lie Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 Pro Gly Lys Pro Leu Val Asp lie Asn Gly Lys Pro Met lie Val His 20 25 30 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg lie lie Val Ala 35 40 45 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val He Val Asn 85 90 95 Val Gin Gly Asp Glu Pro Met lie Pro Ala Thr We lie Arg Gin Val 100 105 1 10 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Val 115 120 125 Pro lie His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr We 145 150 155 160 Pro Trp Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 Asn Phe Leu Arg His Leu Gly lie Tyr Gly Tyr Arg Ala Gly Phe lie 180 185 190 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His He Glu Met 195 200 205 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 Asp Pro Ser Thr Arg He Arg Arg Ser Arg Asn Leu Gly Lys Val He 245 250 255 Asp Thr Leu Thr Cys Gly Phe Ala Asp Leu Met Gly Tyr lie Pro Leu 260 265 270 Val Gly Ala Pro Leu Gly Gly Ala Ala Arg Ala Leu Gly His Gly Val 275 280 285 Arg Val Leu Glu Asp Gly Val Asn Tyr Ala Thr Gly Asn Leu Pro Gly 290 295 300 Cys Ser Phe Ser lie Phe Leu Leu Ala Leu Leu Ser Cys Leu Thr Val 305 310 315 320 Pro Ala Ser Ala Tyr Gin Val Arg Asn Ser Ser Gly Leu Tyr His Val 325 330 335 Thr Asn Asp Cys Pro Asn Ser Ser He Val Tyr Glu Thr Ala Asp Aia 340 345 350 He Leu His Thr Pro Gly Cys Val Pro Cys Val Arg Glu Gly Asn Ala 355 360 365 Ser Arg Cys Trp Val Ala Val Ala Pro Thr Val Ala Thr Arg Asp Gly 370 375 380 Lys Leu Pro Ala Thr Gin Leu Arg Arg His He Asp Leu Leu Val Gly 385 390 395 400 Ser Ala Thr Leu Cys Ser Ala Leu Tyr Leu Arg Ser Ser Val Pro Gly 405 410 415 Asp Pro Leu Asp Cys Arg His Ala Lys 420 425 (2) INFORMATION FOR SEQ ID NO:44: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1401 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: circular (ii) MOLECULE TYPE: DNA (genomic) (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 1..1401 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:44: ATGAGTTTTGTGGTCATTATTCCC GCG CGCTAC GCGTCGACGCGTCTG 48 Met Ser Phe Val Val We lie Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 CCC GGTAAA CCATTG GTTGATATTAAC GGCAAACCCATGATTGTTCAT 96 Pro Gly Lys Pro Leu Val Asp lie Asn Gly Lys Pro Met We Val His 20 25 30 GTT CTT GAA CGC GCG CGT GAA TCA GGT GCC GAG CGC ATC ATC GTG GCA 144 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg lie lie Val Ala 35 40 45 ACC GAT CAT GAG GAT GTT GCC CGC GCC GTT GAA GCC GCT GGC GGT GAA 192 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 GTA TGT ATG ACG CGC GCC GAT CAT CAG TCA GGA ACA GAA CGT CTG GCG 240 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 GAA GTT GTC GAA AAA TGC GCA TTC AGC GAC GAC ACG GTG ATC GTT AAT 288 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val We Val Asn 85 90 95 GTGCAGGGTGATGAACCGATGATCCCTGCGACAATCATTCGTCAGGTT 336 Val Gin Gly Asp Glu Pro Met lie Pro Ala Thr lie He Arg Gin Val 100 105 1 10 GCT GAT AAC CTC GCT CAG CGT CAG GTG GGT ATG GCG ACT CTG GCG GTG 384 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Val 115 120 125 CCA ATC CAC AAT GCG GAA GAA GCG TTT AAC CCG AAT GCG GTG AAA GTG 432 Pro He His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 GTT CTC GAC GCT GAA GGG TAT GCA CTG TAC TTC TCT CGC GCC ACC ATT 480 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr He 145 150 155 160 CCTTGG GAT CGT GAT CGTTTT GCA GAA GGC CTT GAA ACC GTT GGC GAT 528 Pro Tφ Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 AAC TTC CTG CGT CAT CTT GGT ATTTAT GGC TAC CGT GCA GGC TTT ATC 576 Asn Phe Leu Arg His Leu Gly He Tyr Gly Tyr Arg Ala Gly Phe He 180 185 190 CGT CGT TAC GTC AAC TGG CAG CCA AGT CCG TTA GAA CAC ATC GAA ATG 624 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His He Glu Met 195 200 205 TTA GAG CAG CTT CGT GTT CTG TGG TAC GGC GAA AAA ATC CAT GTT GCT 672 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 GTTGCTCAGGAAGTTCCTGGCACAGGTGTGGATACCCCTGAAGATCTC 720 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 GACCCGTCGACTCGAATTCTGCTTGTCGGGAGCGCCACCCTCTGCTCG 768 Asp Pro Ser Thr Arg He Leu Leu Val Gly Ser Ala Thr Leu Cys Ser 245 250 255 GCC CTC TAT GTG GGG GAC TTG TGC GGG TCT GTC TTT CTT GTC GGT CAA 816 Ala Leu Tyr Val Gly Asp Leu Cys Gly Ser Val Phe Leu Val Gly Gin 260 265 270 CTGTTCACTTTCTCCCCCAGG CAG CACTGGACAACG CAAGACTGCAAC 864 Leu Phe Thr Phe Ser Pro Arg Gin His Trp Thr Thr Gin Asp Cys Asn 275 280 285 TGTTCTATCTAC CCC GGC CAC GTA ACG GGT CAC CGC ATG GCA TGG GAT 912 Cys Ser He Tyr Pro Gly His Val Thr Gly His Arg Met Ala Trp Asp 290 295 300 ATG ATG ATG AAC TGG TCC CCT ACG ACA GCG CTG GTA GTA GCT CAG CTG 960 Met Met Met Asn Trp Ser Pro Thr Thr Ala Leu Val Val Ala Gin Leu 305 310 315 320 CTCAGGGTCCCG CAAGCCATCπGGACATGATCGCTGGTGCCCACTGG 1008 Leu Arg Val Pro Gin Ala He Leu Asp Met He Ala Gly Ala His Trp 325 330 335 GGA GTC CTA GCG GGC ATA GCG TATTTC TCC ATG GTG GGG AAC TGG GCG 1056 Gly Val Leu Ala Gly lie Ala Tyr Phe Ser Met Val Gly Asn Trp Ala 340 345 350 MG GTCCTG GTAGTG CTG CTGCTATTTGCCGGCGTTGACGCGGAAACC 1104 Lys Val Leu Val Val Leu Leu Leu Phe Ala Gly Val Asp Ala Glu Thr 355 360 365 CACGTCACCGGGGGAAGTGCCGGCCACATTACGGCTGGGCTTGTTCGT 1152 His Val Thr Gly Gly Ser Ala Gly His We Thr Ala Gly Leu Val Arg 370 375 380 CTC CTTTCA CCA GGC GCC AAG CAG AAC ATC CAA CTG ATC AAC ACC AAC 1200 Leu Leu Ser Pro Gly Ala Lys Gin Asn He Gin Leu lie Asn Thr Asn 385 390 395 400 GGC AGT TGG CAC ATC AAT AGC ACG GCC TTG AAC TGC AAT GAA AGC CTT 1248 Gly Ser Trp His lie Asn Ser Thr Ala Leu Asn Cys Asn Glu Ser Leu 405 410 415 AAC ACC GGC TGG TTA GCA GGG CTC TTC TAT CAC CAC AAA TTC AAC TCT 1296 Asn Thr Gly Trp Leu Ala Gly Leu Phe Tyr His His Lys Phe Asn Ser 420 425 430 TCAGGCTGTCCTGAGAGG GTTGCCAGCTGC CGTCGCCTTACCGATTTT 1344 Ser Gly Cys Pro Glu Arg Val Ala Ser Cys Arg Arg Leu Thr Asp Phe 435 440 445 GACCAGGGCTGGGAATTC GAG CTCGGTACC CGG GGATCCTCTAGACTG 1392 Asp Gin Gly Tφ Glu Phe Glu Leu Gly Thr Arg Gly Ser Ser Arg Leu 450 455 460 CAG GCA TGC 1401 Gin Ala Cys 465 (2) INFORMATION FOR SEQ ID NO:45: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 467 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:45: Met Ser Phe Val Val He He Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 Pro Gly Lys Pro Leu Val Asp lie Asn Gly Lys Pro Met lie Val His 20 25 30 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg lie lie Val Ala 35 40 45 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val He Val Asn 85 90 95 Val Gin Gly Asp Glu Pro Met He Pro Ala Thr He He Arg Gin Val 100 105 1 10 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Val 115 120 125 Pro He His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr lie 145 150 155 160 Pro Tφ Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 Asn Phe Leu Arg His Leu Gly lie Tyr Gly Tyr Arg Ala Gly Phe He 180 185 190 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His We Glu Met 195 200 205 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 Asp Pro Ser Thr Arg He Leu Leu Val Gly Ser Ala Thr Leu Cys Ser 245 250 255 Ala Leu Tyr Val Gly Asp Leu Cys Gly Ser Val Phe Leu Val Gly Gin 260 265 270 Leu Phe Thr Phe Ser Pro Arg Gin His Trp Thr Thr Gin Asp Cys Asn 275 280 285 Cys Ser He Tyr Pro Gly His Val Thr Gly His Arg Met Ala Trp Asp 290 295 300 Met Met Met Asn Trp Ser Pro Thr Thr Ala Leu Val Val Ala Gin Leu 305 310 315 320 Leu Arg Val Pro Gin Ala lie Leu Asp Met He Ala Gly Ala His Trp 325 330 335 Gly Val Leu Ala Gly lie Ala Tyr Phe Ser Met Val Gly Asn Trp Ala 340 345 350 Lys Val Leu Val Val Leu Leu Leu Phe Ala Gly Val Asp Ala Glu Thr 355 360 365 His Val Thr Gly Gly Ser Ala Gly His He Thr Ala Gly Leu Val Arg 370 375 380 Leu Leu Ser Pro Gly Ala Lys Gin Asn We Gin Leu He Asn Thr Asn 385 390 395 400 Gly Ser Trp His He Asn Ser Thr Ala Leu Asn Cys Asn Glu Ser Leu 405 410 415 Asn Thr Gly Trp Leu Ala Gly Leu Phe Tyr His His Lys Phe Asn Ser 420 425 430 Ser Gly Cys Pro Glu Arg Val Ala Ser Cys Arg Arg Leu Thr Asp Phe 435 440 445 Asp Gin Gly Trp Glu Phe Glu Leu Gly Thr Arg Gly Ser Ser Arg Leu 450 455 460 Gin Ala Cys 465 (2) INFORMATION FOR SEQ ID NO:46: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1422 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: circular (ii) MOLECULE TYPE: DNA (genomic) (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 1..1422 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:46: ATG AGTTTTGTG GTC ATT ATT CCC GCG CGC TAC GCGTCG ACG CGT CTG 48 Met Ser Phe Val Val He lie Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 CCC GGT AAA CCA TTG GTT GAT ATT AAC GGC AAA CCC ATG ATT GTT CAT 96 Pro Gly Lys Pro Leu Val Asp He Asn Gly Lys Pro Met He Val His 20 25 30 GTT CTT GAA CGC GCG CGT GAA TCA GGT GCC GAG CGC ATC ATC GTG GCA 144 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg lie lie Val Ala 35 40 45 AC-CGATCATGAGGATGTTGCCCGCGCCGTTGAAGCCGCT03CGGTGAA 192 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 GTATGTATGACGCGCGCCGATCATCAGTCAGGAACAGAACGTCTG GCG 240 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 GAA GTT GTC GAA AAA TGC GCA TTC AGC GAC GAC ACG GTG ATC GTT AAT 288 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val He Val Asn 85 90 95 GTGCAG GGT GAT GAA CCG ATGATCCCTGCG ACAATC ATTCGTCAGGTT 336 Val Gin Gly Asp Glu Pro Met He Pro Ala Thr He He Arg Gin Val 100 105 110 GCTGATAACCTCGCTCAG CGT CAG GTG GGT ATG GCG ACT CTG GCG GTG 384 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Val 115 120 125 CCAATCCACMTGCG GAAGAAGOGTTTAACCCGAATGCGGTGAAAGTG 432 Pro He His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 GTTCTCGAC GCTGAAGGGTATGCACTGTACTTCTCTCGC GCCACCATT 480 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr lie 145 150 155 160 CCTTGGGATCGTGATCGTTTTGCAGAAGGC CTTGAAACCGTTGGC GAT 528 Pro Tφ Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 AAC TTC CTG CGT CAT CTT GGT ATTTAT GGC TAC CGT GCA GGC TTT ATC 576 Asn Phe Leu Arg His Leu Gly lie Tyr Gly Tyr Arg Ala Gly Phe He 180 185 190 CGTCGTTAC GTCAACTGG CAGCCAAGTCCGTTAGAACACATCGAAATG 624 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His He Glu Met 195 200 205 TTA GAG CAG CTT CGT GTT CTG TGG TAC GGC GAA AAA ATC CAT GTT GCT 672 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys lie His Val Ala 210 215 220 GTTGCTCAGGAAGTTCCTGGCACAGGTGTGGATACCCCTGAAGATCTC 720 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 GAC CCGTCG ACCGAATTCGGTGAC ATC ATC AAC GGC TTG CCC GTC TCC 768 Asp Pro Ser Thr Glu Phe Gly Asp He He Asn Gly Leu Pro Val Ser 245 250 255 GCC CGT AGG GGC CAG GAG ATA CTG CTC GGA CCA GCC GAC GGA ATG GTC 816 Ala Arg Arg Gly Gin Glu lie Leu Leu Gly Pro Ala Asp Gly Met Val 260 265 270 TCCAAGGGGTGGAGGTTGCTG GCGCCCATCACGGCGTACGCCCAGCAG 864 Ser Lys Gly Trp Arg Leu Leu Ala Pro He Thr Ala Tyr Ala Gin Gin 275 280 285 ACAAGGGGCCTCCTAGGGTGTATAATCACCAGCCTGACTGGCCGGGAC 912 Thr Arg Gly Leu Leu Gly Cys He He Thr Ser Leu Thr Gly Arg Asp 290 295 300 AAA AAC CAA GCG GAG GGT GAG GTC CAG ATT GTG TCA ACT GCT GCC CAA 960 Lys Asn Gin Ala Glu Gly Glu Val Gin We Val Ser Thr Ala Ala Gin 305 310 315 320 ACT TTC CTG GCA ACG TGC ATC AAT GGG GTA TGC TGG ACT GTC TAC CAT 1008 Thr Phe Leu Ala Thr Cys lie Asn Gly Val Cys Trp Thr Val Tyr His 325 330 335 GGG GCC GGA ACG AGG ACC CTC GCA TCA CCC AAG GGT CCT GTT ATC CAG 1056 Gly Ala Gly Thr Arg Thr Leu Ala Ser Pro Lys Gly Pro Val lie Gin 340 345 350 ATG TAT ACC AAT GTA GAC CAA GAC CTT GTG GGC TGG CCC GCT CCT CAA 1104 Met Tyr Thr Asn Val Asp Gin Asp Leu Val Gly Trp Pro Ala Pro Gin 355 360 365 GGTGCCCGCTCATTGACACCCTGCACCTGC GGCTCCTCG GACCTTTAC 1152 Gly Ala Arg Ser Leu Thr Pro Cys Thr Cys Gly Ser Ser Asp Leu Tyr 370 375 380 CTG GTT ACG AGG CAC GCC GAT GTC ATT CCC GTG CGC CGG CGG GGT GAT 1200 Leu Val Thr Arg His Ala Asp Val He Pro Val Arg Arg Arg Gly Asp 385 390 395 400 AGC AGG GGC AGC CTG CTTTCG CCC CGG CCC ATT TCT TAT TTG AAA GGC 1248 Ser Arg Gly Ser Leu Leu Ser Pro Arg Pro lie Ser Tyr Leu Lys Gly 405 410 415 TCC TCG GGG GGT CCG CTG TTG TGC CCC GCG GGA CAC GCC GTG GGC ATA 1296 Ser Ser Gly Gly Pro Leu Leu Cys Pro Ala Gly His Ala Val Gly He 420 425 430 TTC AGG GCC GCG GTG TGT ACC CGT GGA GTG GCT AAG GCG GTG GAC TTT 1344 Phe Arg Ala Ala Val Cys Thr Arg Gly Val Ala Lys Ala Val Asp Phe 435 440 445 GTC CCC GTG GAG AAC CTC GAG ACA ACC ATG AATTCG AGC TCG GTA CCC 1392 Val Pro Val Glu Asn Leu Glu Thr Thr Met Asn Ser Ser Ser Val Pro 450 455 460 GGG GAT CCT CTA GAC TGC AGG CAT GCT AAG 1422 Gly Asp Pro Leu Asp Cys Arg His Ala Lys 465 470 (2) INFORMATION FOR SEQ ID NO:47: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 474 ammo acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:47: Met Ser Phe Val Val He He Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 Pro Gly Lys Pro Leu Val Asp He Asn Gly Lys Pro Met He Val His 20 25 30 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg lie lie Val Ala 35 40 45 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val He Val Asn 85 90 95 Val Gin Gly Asp Glu Pro Met He Pro Ala Thr He He Arg Gin Val 100 105 110 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Val 115 120 125 Pro He His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr He 145 150 155 160 Pro Trp Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 Asn Phe Leu Arg His Leu Gly He Tyr Gly Tyr Arg Ala Gly Phe He 180 185 190 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His lie Glu Met 195 200 205 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Aia 210 215 220 Val Aia Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 Asp Pro Ser Thr Glu Phe Gly Asp He He Asn Gly Leu Pro Val Ser 245 250 255 Ala Arg Arg Gly Gin Glu He Leu Leu Gly Pro Ala Asp Gly Met Val 260 265 270 Ser Lys Gly Trp Arg Leu Leu Ala Pro He Thr Ala Tyr Ala Gin Gin 275 280 285 Thr Arg Gly Leu Leu Gly Cys He We Thr Ser Leu Thr Gly Arg Asp 290 295 300 Lys Asn Gin Ala Glu Gly Glu Val Gin He Val Ser Thr Ala Ala Gin 305 310 315 320 Thr Phe Leu Ala Thr Cys We Asn Gly Val Cys Trp Thr Val Tyr His 325 330 335 Gly Ala Gly Thr Arg Thr Leu Ala Ser Pro Lys Gly Pro Val lie Gin 340 345 350 Met Tyr Thr Asn Val Asp Gin Asp Leu Val Gly Trp Pro Ala Pro Gin 355 360 365 Gly Ala Arg Ser Leu Thr Pro Cys Thr Cys Gly Ser Ser Asp Leu Tyr 370 375 380 Leu Val Thr Arg His Ala Asp Val We Pro Val Arg Arg Arg Gly Asp 385 390 395 400 Ser Arg Gly Ser Leu Leu Ser Pro Arg Pro We Ser Tyr Leu Lys Gly 405 410 415 Ser Ser Gly Gly Pro Leu Leu Cys Pro Ala Gly His Ala Val Gly He 420 425 430 Phe Arg Ala Ala Val Cys Thr Arg Gly Val Ala Lys Ala Val Asp Phe 435 440 445 Val Pro Val Glu Asn Leu Glu Thr Thr Met Asn Ser Ser Ser Val Pro 450 455 460 Gly Asp Pro Leu Asp Cys Arg His Ala Lys 465 470 (2) INFORMATION FOR SEQ ID N0:48: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1401 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: circular (ii) MOLECULE TYPE: DNA (genomic) (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 1..1401 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:48: ATGAGTTTTGTGGTCATTATTCCC GCG CGCTAC GCGTCGACG CGTCTG 48 Met Ser Phe Val Val lie He Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 CCCGGTAAACCATTG GTTGATATTAAC GGCAAACCCATGATTGTTCAT 96 Pro Gly Lys Pro Leu Val Asp lie Asn Gly Lys Pro Met He Val His 20 25 30 GTTCTTGAACGCGCGCGTGAATCAGGTGCCGAGCGCATCATCGTGGCA 144 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg lie lie Val Ala 35 40 45 ACXΪGATCATGAGGATGπGlXCGCGCCGTTG GCCGCTGGCGGTGAA 192 Thr Asp His Glu Asp Val Ala Arg Aia Val Glu Ala Ala Gly Gly Glu 50 55 60 GTATGTATGACGCGCGCCGATCATCAGTCAGGAACAGAACGTCTGGCG 240 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 GAAGTTGTCGAAAAATGC GCATTCAGCGACGACACG GTGATCGTTAAT 288 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val He Val Asn 85 90 95 GTG CAG GGT GAT GAA CCG ATG ATC CCT GCG ACA ATC ATT CGT CAG GTT 336 Val Gin Gly Asp Glu Pro Met He Pro Ala Thr He He Arg Gin Val 100 105 1 10 GCT GAT AAC CTC GCT CAG CGT CAG GTG GGT ATG ACG ACT CTG GCG GTG 384 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Thr Thr Leu Ala Val 115 120 125 CCA ATC CAC AAT GCG GAA GAA GCG TTT AAC CCG AAT GCG GTG AAA GTG 432 Pro He His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 GTT CTC GAC GCT GAA GGG TAT GCA CTG TAC TTC TCT CGC GCC ACC ATT 480 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr He 145 150 155 160 CCTTGGGATCGTGATCGTT1TGCAGMGGCCTTGAAACCGTTGGC GAT 528 Pro Tφ Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 AAC TTC CTG CGT CAT CTT GGT ATT TAT GGC TAC CGT GCA GGC TTT ATC 576 Asn Phe Leu Arg His Leu Gly lie Tyr Gly Tyr Arg Ala Gly Phe He 180 185 190 CGT CGT TAC GTC AAC TGG CAG CCA AGT CCG TTA GAA CAC ATC GAA ATG 624 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His He Glu Met 195 200 205 TTA GAG CAG CTT CGT GTT CTG TGG TAC GGC GAA AAA ATC CAT GTT GCT 672 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 GTT GCT CAG GAA GTT CCT GGC ACA GGT GTG GAT ACC CCT GAA GAT CTC 720 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 GAC CCG TCG ACG AAT TCC ACC ATG GGG CATTAT CCTTGT ACC ATC AAC 768 Asp Pro Ser Thr Asn Ser Thr Met Gly His Tyr Pro Cys Thr He Asn 245 250 255 TACACCCTGTTCAAAGTCAGGATGTACGTG GGAGGGGTCGAGCACAGG 816 Tyr Thr Leu Phe Lys Val Arg Met Tyr Val Gly Gly Val Glu His Arg 260 265 270 CTGGMGTTGCTTGCAACTGGACGCGGGGCGAACGTTGTGATCTGGAC 864 Leu Glu Val Ala Cys Asn Tφ Thr Arg Gly Glu Arg Cys Asp Leu Asp 275 280 285 GAC AGG GAC AGG TCC GAG CTC AGC CCG CTG CTG CTG TCC ACC ACT CAG 912 Asp Arg Asp Arg Ser Glu Leu Ser Pro Leu Leu Leu Ser Thr Thr Gin 290 295 300 TGG CAG GTC CTT CCG TGTTCC TTC ACG ACC TTG CCA GCC TTG ACC ACC 960 Trp Gin Val Leu Pro Cys Ser Phe Thr Thr Leu Pro Ala Leu Thr Thr 305 310 315 320 GGC CTC ATC CAC CTC CAC CAG AAC ATC GTG GAC GTG CAA TAC TTG TAC 1008 Gly Leu He His Leu His Gin Asn lie Val Asp Val Gin Tyr Leu Tyr 325 330 335 GGGGTGGGGTCAAGCATTGTGTCCTGG GCCATCAAGTGGGAGTAC GTC 1056 Gly Val Gly Ser Ser We Val Ser Tφ Ala He Lys Tφ Glu Tyr Val 340 345 350 ATC CTC TTG TTT CTC CTG CTT GCA GAC GCG CGC ATC TGC TCC TGC TTG 1104 He Leu Leu Phe Leu Leu Leu Ala Asp Ala Arg We Cys Ser Cys Leu 355 360 365 TGG ATG ATG TTA CTC ATA TCC CAA GCG GAG GCA GCC TTG GAA AAC CTT 1152 Tφ Met Met Leu Leu He Ser Gin Ala Glu Ala Ala Leu Glu Asn Leu 370 375 380 GTG TTA CTC AAT GCG GCG TCT CTG GCC GGG ACG CAC GGT CTT GTG TCC 1200 Val Leu Leu Asn Ala Ala Ser Leu Ala Gly Thr His Gly Leu Val Ser 385 390 395 400 TTC CTC GTG TTTTTC TGC TTT GCA TGG TAT CTG AAG GGT AAG TGG GTG 1248 Phe Leu Val Phe Phe Cys Phe Ala Tφ Tyr Leu Lys Gly Lys Tφ Val 405 410 415 CCC GGA GTG GCC TAC GCC TTC TAC GGG ATG TGG CCTTTC CTC CTG CTC 1296 Pro Gly Val Ala Tyr Ala Phe Tyr Gly Met Trp Pro Phe Leu Leu Leu 420 425 430 CTGTTAGCGTTG CCCCAACGG GCATACGCG CTGGACACG GAGATGGCC 1344 Leu Leu Ala Leu Pro Gin Arg Ala Tyr Ala Leu Asp Thr Glu Met Ala 435 440 445 GCG TCG TGT GGC GGC GTT GTT CTT GTC GGG TTA ATG GCG CTG ACT CTG 1392 Ala Ser Cys Gly Gly Val Val Leu Val Gly Leu Met Ala Leu Thr Leu 450 455 460 TCA CCA TAT 1401 Ser Pro Tyr 465 (2) INFORMATION FOR SEQ ID NO:49: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 467 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:49: Met Ser Phe Val Val We He Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 Pro Gly Lys Pro Leu Val Asp He Asn Gly Lys Pro Met He Val His 20 25 30 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg He lie Val Ala 35 40 45 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val He Val Asn 85 90 95 Val Gin Gly Asp Glu Pro Met He Pro Ala Thr He He Arg Gin Val 100 105 110 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Thr Thr Leu Ala Val 115 120 125 Pro He His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr He 145 150 155 160 Pro Trp Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 Asn Phe Leu Arg His Leu Gly lie Tyr Gly Tyr Arg Ala Gly Phe He 180 185 190 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His lie Glu Met 195 200 205 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys We His Val Aia 210 215 220 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 Asp Pro Ser Thr Asn Ser Thr Met Gly His Tyr Pro Cys Thr We Asn 245 250 255 Tyr Thr Leu Phe Lys Val Arg Met Tyr Val Gly Gly Val Glu His Arg 260 265 270 Leu Glu Val Ala Cys Asn Tφ Thr Arg Gly Glu Arg Cys Asp Leu Asp 275 280 285 Asp Arg Asp Arg Ser Glu Leu Ser Pro Leu Leu Leu Ser Thr Thr Gin 290 295 300 Trp Gin Val Leu Pro Cys Ser Phe Thr Thr Leu Pro Ala Leu Thr Thr 305 310 315 320 Gly Leu He His Leu His Gin Asn lie Val Asp Val Gin Tyr Leu Tyr 325 330 335 Gly Val Gly Ser Ser lie Val Ser Tφ Ala We Lys Tφ Glu Tyr Val 340 345 350 He Leu Leu Phe Leu Leu Leu Ala Asp Ala Arg We Cys Ser Cys Leu 355 360 365 Tφ Met Met Leu Leu lie Ser Gin Ala Glu Ala Ala Leu Glu Asn Leu 370 375 380 Val Leu Leu Asn Ala Aia Ser Leu Ala Gly Thr His Gly Leu Val Ser 385 390 395 400 Phe Leu Val Phe Phe Cys Phe Ala Tφ Tyr Leu Lys Gly Lys Tφ Val 405 410 415 Pro Gly Val Ala Tyr Ala Phe Tyr Gly Met Trp Pro Phe Leu Leu Leu 420 425 430 Leu Leu Ala Leu Pro Gin Arg Ala Tyr Ala Leu Asp Thr Glu Met Ala 435 440 445 Ala Ser Cys Gly Gly Val Val Leu Val Gly Leu Met Ala Leu Thr Leu 450 455 460 Ser Pro Tyr 465 (2) INFORMATION FOR SEQ ID NO:50: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1851 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: circular (ii) MOLECULE TYPE: DNA (genomic) (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 1..1851 (xi) SEQUENCE DESCRIPTION: SEQ ID NO.50: ATG AGTTTTGTG GTC ATT ATT CCC GCG CGC TAC GCGTCG ACG CGT CTG 48 Met Ser Phe Val Val lie lie Pro Ala Arg Tyr Aia Ser Thr Arg Leu 1 5 10 15 CCCGGTAAACCATTGGTTGATATTAACGGCAAACCCATGATTGTTCAT 96 Pro Gly Lys Pro Leu Val Asp He Asn Gly Lys Pro Met He Val His 20 25 30 GTTCTTGAACGCGCGCGTGAATCAGGTGCCGAGCGCATCATCGTGGCA 144 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg lie He Val Ala 35 40 45 ACCGATCATGAGGATGTTGCCCGCGCCGTTGAAGCCGCTGGCGGTGAA 192 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 GTATGTATGACGCGCGCCGATCATCAGTCAGGAACAGAACGTCTGGCG 240 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 GAAGTTGTCGAAAAATGC GCATTCAGCGACGACACG GTGATCGTTAAT 288 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val He Val Asn 85 90 95 GTG CAG GGT GAT GAA CCG ATG ATC CCT GCG ACA ATC ATT CGT CAG GTT 336 Val Gin Gly Asp Glu Pro Met lie Pro Ala Thr He He Arg Gin Val 100 105 1 10 GCT GAT AAC CTC GCT CAG CGT CAG GTG GGT ATG GCG ACT CTG GCG GTG 384 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Val 115 120 125 CCAATCCACMTGCG GMGAAGCGTTTAACCCGAATGCGGTGAAAGTG 432 Pro He His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 GTT CTC GAC GCT GAA GGG TAT GCA CTG TAC TTC TCT CGC GCC ACC ATT 480 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr lie 145 150 155 160 CCT TGG GAT CGT GAT CGT TTT GCA GAA GGC CTT GAA ACC GTT GGC GAT 528 Pro Tφ Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 AAC TTC CTG CGT CAT CTT GGT ATT TAT GGC TAC CGT GCA GGC TTT ATC 576 Asn Phe Leu Arg His Leu Gly lie Tyr Gly Tyr Arg Ala Gly Phe He 180 185 190 CGT CGTTAC GTC AAC TGG CAG CCA AGT CCG TTA GAA CAC ATC GAA ATG 624 Arg Arg Tyr Val Asn Trp Gin Pro Ser Pro Leu Glu His We Glu Met 195 200 205 TTA GAG CAG CTT CGT GTT CTG TGG TAC GGC GAA AAA ATC CAT GTT GCT 672 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 GTT GCT CAG GAA GTT CCT GGC ACA GGT GTG GAT ACC CCT GAA GAT CTC 720 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 GACCCGTCGACTCGAATTCGTAGGTCG CGCAATTTG GGTAAG GTCATC 768 Asp Pro Ser Thr Arg lie Arg Arg Ser Arg Asn Leu Gly Lys Val He 245 250 255 GAT ACC CTC ACG TGC GGC TTC GCC GAC CTC ATG GGG TAC ATT CCG CTC 816 Asp Thr Leu Thr Cys Gly Phe Ala Asp Leu Met Gly Tyr lie Pro Leu 260 265 270 GTC GGC GCC CCT CTT GGA GGC GCT GCC AGG GCC CTG GCG CAT GGC GTC 864 Val Gly Ala Pro Leu Gly Gly Ala Ala Arg Ala Leu Ala His Gly Val 275 280 285 CGG GTT CTG GAA GAC GGC GTG AAC TAT GCA ACA GGG AAC CTT CCC GGT 912 Arg Val Leu Glu Asp Gly Val Asn Tyr Ala Thr Gly Asn Leu Pro Gly 290 295 300 TGC TCT TTC TCT ATC TTC CTT CTG GCC CTG CTC TCT TGC CTG ACT GTG 960 Cys Ser Phe Ser He Phe Leu Leu Ala Leu Leu Ser Cys Leu Thr Val 305 310 315 320 CCC GCG TCA TCC TAC CAA GTA CGC AAC TCC TCG GGC CTT TAT CAT GTC 1008 Pro Ala Ser Ser Tyr Gin Val Arg Asn Ser Ser Gly Leu Tyr His Val 325 330 335 ACCAATGATTGCCCCAACTCG AGCATTGTGTAC GAGACG GCC GATACC 1056 Thr Asn Asp Cys Pro Asn Ser Ser lie Val Tyr Glu Thr Ala Asp Thr 340 345 350 ATCCTACACTCTCCG GGGTGCGTC CCTTGC GTTCGC GAGGGCAACACC 1104 He Leu His Ser Pro Gly Cys Val Pro Cys Val Arg Glu Gly Asn Thr 355 360 365 TCG AAA TGTTGG GTG GCG GTG GCC CCC ACA GTG GCC ACC AGG GAC GGC 1152 Ser Lys Cys Trp Val Ala Val Ala Pro Thr Val Ala Thr Arg Asp Gly 370 375 380 AAACTCCCCTCAACGCAG CTTCGACGTCACATC GATCTGCTCGTCGGG 1200 Lys Leu Pro Ser Thr Gin Leu Arg Arg His He Asp Leu Leu Val Gly 385 390 395 400 AGCGCCACCCTCTGCTCG GCCCTCTATGTGGGG GACTTGTGCGGGTCT 1248 Ser Ala Thr Leu Cys Ser Ala Leu Tyr Val Gly Asp Leu Cys Gly Ser 405 410 415 GTC TTT CTT GTC AGT CAA CTG TTC ACC TTC TCC CCT AGG CGC CAT TGG 1296 Val Phe Leu Val Ser Gin Leu Phe Thr Phe Ser Pro Arg Arg His Trp 420 425 430 ACA ACG CAAGACTGC AACTGTTCT ATCTAC CCC GGC CAT ATA ACG GGT 1344 Thr Thr Gin Asp Cys Asn Cys Ser He Tyr Pro Gly His He Thr Gly 435 440 445 CAC CGC ATG GCATGG GAT ATG ATG ATG AAC TGG TCC CCT ACA ACG GCG 1392 His Arg Met Ala Trp Asp Met Met Met Asn Tφ Ser Pro Thr Thr Aia 450 455 460 CTG GTA GTA GCT CAG CTG CTC AGG GTC CCA CAA GCC ATC TTG GAC ATG 1440 Leu Val Val Ala Gin Leu Leu Arg Val Pro Gin Ala He Leu Asp Met 465 470 475 480 ATC GCA GGT GCC CAC TGG GGA GTC CTA GCG GGC ATA GCG TATTTC TCC 1488 lie Ala Gly Ala His Trp Gly Val Leu Ala Gly He Ala Tyr Phe Ser 485 490 495 ATG GTG GGG AAC TGG GCG AAG GTC CTG GTA GTG CTG TTG CTG TTT TCC 1536 Met Val Gly Asn Trp Ala Lys Val Leu Val Val Leu Leu Leu Phe Ser 500 505 510 GGCGTCGATGCGGCAACCTACACCACCGGGGGGAGCGTTGCTAGGACC 1584 Gly Val Asp Ala Ala Thr Tyr Thr Thr Gly Gly Ser Val Ala Arg Thr 515 520 525 ACG CATGGATTCTCCAGCTTATTCAGTCAAGGC GCCAAG CAGAACATC 1632 Thr His Gly Phe Ser Ser Leu Phe Ser Gin Gly Ala Lys Gin Asn He 530 535 540 CAG CTG ATT AAC ACC AAC GGC AGTTGG CAC ATC AAT CGC ACG GCC TTG 1680 Gin Leu He Asn Thr Asn Gly Ser Trp His He Asn Arg Thr Ala Leu 545 550 555 560 AACTGTAATGCGAGC CTCGACACTGGCTGGGTAGCG GGG CTCTTCTAT 1728 Asn Cys Asn Ala Ser Leu Asp Thr Gly Trp Val Ala Gly Leu Phe Tyr 565 570 575 TAC CACAAATTC AACTCTTCAGGCTGCCCTGAG AGG ATG GCC AGCTGT 1776 Tyr His Lys Phe Asn Ser Ser Gly Cys Pro Glu Arg Met Ala Ser Cys 580 585 590 AGA OX. CΓΓΓGCX; GATTTT GAC CAG GGC TGG GMTTC GAG CTC GGTACC 1824 Arg Pro Leu Ala Asp Phe Asp Gin Gly Trp Glu Phe Glu Leu Gly Thr 595 600 605 CGG GGA TCC TCT AGA CTG CAG GCA TGC 1851 Arg Gly Ser Ser Arg Leu Gin Ala Cys 610 615 (2) INFORMATION FOR SEQ ID NO:51 : (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 617 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:30: Met Ser Phe Val Val lie lie Pro Ala Arg Tyr Ala Ser Thr Arg Leu 1 5 10 15 Pro Gly Lys Pro Leu Val Asp lie Asn Gly Lys Pro Met lie Val His 20 25 30 Val Leu Glu Arg Ala Arg Glu Ser Gly Ala Glu Arg lie He Val Ala 35 40 45 Thr Asp His Glu Asp Val Ala Arg Ala Val Glu Ala Ala Gly Gly Glu 50 55 60 Val Cys Met Thr Arg Ala Asp His Gin Ser Gly Thr Glu Arg Leu Ala 65 70 75 80 Glu Val Val Glu Lys Cys Ala Phe Ser Asp Asp Thr Val He Val Asn 85 90 95 Val Gin Gly Asp Glu Pro Met He Pro Ala Thr We We Arg Gin Val 100 105 1 10 Ala Asp Asn Leu Ala Gin Arg Gin Val Gly Met Ala Thr Leu Ala Val 115 120 125 Pro He His Asn Ala Glu Glu Ala Phe Asn Pro Asn Ala Val Lys Val 130 135 140 Val Leu Asp Ala Glu Gly Tyr Ala Leu Tyr Phe Ser Arg Ala Thr He 145 150 155 160 Pro Tφ Asp Arg Asp Arg Phe Ala Glu Gly Leu Glu Thr Val Gly Asp 165 170 175 sn Phe Leu Arg His Leu Gly He Tyr Gly Tyr Arg Ala Gly Phe He 180 185 190 Arg Arg Tyr Val Asn Trp Gin Pro -Ser Pro Leu Glu His He Glu Met 195 200 205 Leu Glu Gin Leu Arg Val Leu Trp Tyr Gly Glu Lys He His Val Ala 210 215 220 Val Ala Gin Glu Val Pro Gly Thr Gly Val Asp Thr Pro Glu Asp Leu 225 230 235 240 Asp Pro Ser Thr Arg He Arg Arg Ser Arg Asn Leu Gly Lys Val lie 245 250 255 Asp Thr Leu Thr Cys Gly Phe Ala Asp Leu Met Gly Tyr He Pro Leu 260 265 270 Val Gly Ala Pro Leu Gly Gly Ala Ala Arg Ala Leu Ala His Gly Val 275 280 285 Arg Val Leu Glu Asp Gly Val Asn Tyr Ala Thr Gly Asn Leu Pro Gly 290 295 300 Cys Ser Phe Ser lie Phe Leu Leu Ala Leu Leu Ser Cys Leu Thr Val 305 310 315 320 Pro Ala Ser Ser Tyr Gin Val Arg Asn Ser Ser Gly Leu Tyr His Val 325 330 335 Thr Asn Asp Cys Pro Asn Ser Ser lie Val Tyr Glu Thr Ala Asp Thr 340 345 350 He Leu His Ser Pro Gly Cys Val Pro Cys Val Arg Glu Gly Asn Thr 355 360 365 Ser Lys Cys Trp Val Ala Val Ala Pro Thr Val Ala Thr Arg Asp Gly 370 375 380 Lys Leu Pro Ser Thr Gin Leu Arg Arg His He Asp Leu Leu Val Gly 385 390 395 400 Ser Ala Thr Leu Cys Ser Ala Leu Tyr Val Gly Asp Leu Cys Gly Ser 405 410 415 Val Phe Leu Val Ser Gin Leu Phe Thr Phe Ser Pro Arg Arg His Trp 420 425 430 Thr Thr Gin Asp Cys Asn Cys Ser He Tyr Pro Gly His lie Thr Gly 435 440 445 His Arg Met Ala Trp Asp Met Met Met Asn Tφ Ser Pro Thr Thr Ala 450 455 460 Leu Val Val Ala Gin Leu Leu Arg Val Pro Gin Ala He Leu Asp Met 465 470 475 480 We Ala Gly Ala His Tφ Gly Val Leu Ala Gly lie Ala Tyr Phe Ser 485 490 495 Met Val Gly Asn Trp Ala Lys Val Leu Val Val Leu Leu Leu Phe Ser 500 505 510 Gly Val Asp Ala Ala Thr Tyr Thr Thr Gly Gly Ser Val Ala Arg Thr 515 520 525 Thr His Gly Phe Ser Ser Leu Phe Ser Gin Gly Ala Lys Gin Asn He 530 535 540 Gin Leu He Asn Thr Asn Gly Ser Trp His He Asn Arg Thr Ala Leu 545 550 555 560 Asn Cys Asn Ala Ser Leu Asp Thr Gly Trp Val Ala Gly Leu Phe Tyr 565 570 575 Tyr His Lys Phe Asn Ser Ser Gly Cys Pro Glu Arg Met Ala Ser Cys 580 585 590 Arg Pro Leu Ala Asp Phe Asp Gin Gly Trp Glu Phe Glu Leu Gly Thr 595 600 605 Arg Gly Ser Ser Arg Leu Gin Ala Cys 610 615

Claims: CLAIMS 1 . A recombinant fusion protein having SEQ. ID. NO. 11. 2. A recombinant fusion protein having SEQ. ID. NO. 12. 3. A recombinant fusion protein having SEQ. ID. NO. 13. 4. A recombinant fusion protein having SEQ. ID. NO. 14. 5. A recombinant fusion protein having SEQ. ID. NO. 16. 6. A recombinant fusion protein having SEQ. ID. NO. 17. 7. A recombinant fusion protein having SEQ. ID. NO. 18. 8. A polypeptide having SEQ. ID. NO. 11. 9. A polypeptide having SEQ. ID. NO. 12. 10. A polypeptide having SEQ. ID. NO. 13. 1 1 . A polypeptide having SEQ. ID. NO. 14. 12. A polypeptide having SEQ. ID. NO. 16. 13. A polypeptide having SEQ. ID. NO. 17. 14. A polypeptide having SEQ. ID. NO. 18. 15. An assay for identifying the presence of an antibody immunologically reactive with an HCV antigen in a fluid sample comprising: contacting the sample with at least one polypeptide selected from the group consisting of recombinant proteins having SEQ. ID. NO. 11, SEQ. ID. NO. 12, SEQ. ID. NO. 13, SEQ. ID. NO. 14, SEQ. ID. NO. 16, SEQ. ID. NO. 17, SEQ. ID. NO. 18, polypeptides having SEQ. ID. NO. 11, SEQ. ID. NO. 12, SEQ. ID. NO. 13, SEQ. ID. NO. 14, SEQ. ID. NO. 16 SEQ. ID. NO. 17 and SEQ. ID. NO. 18 under conditions suitable for complexing the antibody with the polypeptide; and detecting the antibody- poiypeptide complex. 1 6. In a confirmatory assay for identifying the presence of an antibody in a fluid sample immunologically reactive with an HCV antigen wherein the sample is used to prepare first and second immunologically equivalent aliquots and the first aliquot is contacted with at least one polypeptide selected from the group consisting of recombinant proteins having SEQ. ID. NO. 11, SEQ. ID. NO. 12, SEQ. ID. NO. 13, SEQ. ID. NO. 14, SEQ. ID. NO. 16, SEQ. ID. NO. 17, SEQ. ID. NO. 18, polypeptides having SEQ. ID. NO. 11, SEQ. ID. NO. 12, SEQ. ID. NO. 13, SEQ. ID. NO. 14, SEQ. ID. NO. 16, SEQ. ID. NO. 17 and SEQ. ID. NO. 18 under conditions suitable for complexing the antibody with the polypeptide and wherein the first antibody- antigen complex is detected, and: contacting the second aliquot with a polypeptide selected from the group consisting of recombinant proteins SEQ. ID. NO. 11 , SEQ. ID. NO. 12, SEQ. ID. NO. 13, SEQ. ID. NO. 14, SEQ. ID. NO. 16, SEQ. ID. NO. 17, SEQ. ID. NO. 18, polypeptides having SEQ. ID. NO. 11 , SEQ. ID. NO. 12, SEQ. ID. NO. 13, SEQ. ID. NO. 14, SEQ.ID. NO. 16, SEQ. ID. NO. 17 and SEQ. ID. NO. 18 under conditions suitable to form a second antibody-antigen complex; and detecting the second antibody-antigen complex; wherein the polypeptide selected in the first aliquot is not the same as the polypeptide selected in the second aliquot. 1 7. in an immunodot assay for identifying the presence of an antibody immunologically reactive with an HCV antigen in a fluid sample wherein the sample is concurrently contacted with at least two polypeptides separately bound to distinct regions of the solid support, each containing distinct epitopes of an HCV antigen under conditions suitable for complexing the antibody with the polypeptide; and detecting the antibody-polypeptide complex, and wherein said polypeptides are selected from the group consisting of recombinant proteins having SEQ. ID. NO. 1 1 , SEQ. ID,. NO. 12, SEQ. ID. NO. 13, SEQ. ID. NO. 14, SEQ. ID. NO. 16.SEQ. ID. NO. 17, SEQ. ID. NO. 18, polypeptides having SEQ. ID. NO. 11 , SEQ. ID. NO. 12, SEQ. ID. NO. 13, SEQ. ID. NO. 14, SEQ. ID. NO. 16. SEQ. ID. NO. 17 and SEQ. ID. NO. 18. 1 8. In a competition assay for identifying the presence of an antibody immunologically reactive with an HCV antigen in a fluid sample wherein the sample is used to prepare first and second immunologically equivalent aliquots wherein the first aliquot is contacted with a polypeptide bound to a solid support under conditions suitable for complexing the antibody with the polypeptide to form a detectable antibody-polypeptide complex, and wherein the second aliquot is first contacted with unbound polypeptide and then contacted with said bound polypeptide wherein the polypeptide is selected from the group consisting of recombinant proteins SEQ. ID. NO. 1 1 , SEQ. ID. NO. 12., SEQ. ID.NO. 13, SEQ. ID. NO. 14, SEQ. ID. NO 16, SEQ. ID. NO. 17, SEQ. ID. NO. 18, polypeptides having SEQ. ID. NO. 11 , SEQ. ID. NO. 12, SEQ. ID. NO. 13, SEQ. ID. NO. 14, SEQ. ID. NO. 16, SEQ. ID. NO. 17 and SEQ. ID. NO. 18. 1 9. In a competition assay for identifying the presence of an antibody immunologically reactive with an HCV antigen in a fluid sample wherein the sample is used to prepare first and second immunologically equivalent aliquots wherein the first aliquot is contacted with a polypeptide bound to a solid support under conditions suitable for complexing the antibody with the polypeptide to form a detectable antibody-polypeptide complex and wherein the second aliquot is first contacted with unbound polypeptide and then contacted with said bound polypeptide wherein the polypeptide is selected from the group consisting of recombinant proteins SEQ. ID. NO. 1 1 , SEQ. ID. NO. 12, SEQ. ID. NO. 13, SEQ. ID. NO. 14, SEQ. ID. NO. 16, SEQ. ID. NO. 17, SEQ. ID. NO. 18, polypeptides SEQ. ID. NO. 11., SEQ. ID. NO. 12, SEQ. ID. NO. 13, SEQ. ID. NO. 14, SEQ. ID. NO. 16, SEQ. ID. NO. 17 and SEQ. ID. NO. 18; wherein the second aliquot is contacted with unbound and bound polypeptide simultaneously. 20. In a neutralization assay for identifying the presence of an antibody immunologically reactive with an HCV antigen in a fluid sample wherein the sample is used to prepare first and second immunologically equivalent aliquots wherein the first aliquot is contacted with a polypeptide bound to a solid support under conditions suitable for complexing the antibody with the polypeptide to form a detectable antibody-polypeptide complex wherein the bound polypeptide is selected from the group consisting of recombinant proteins SEQ. ID. NO. 11 , SEQ. ID. NO. 12, SEQ. ID. NO. 13, SEQ. ID. NO. 14, SEQ. ID. NO. 16, SEQ. ID. NO. 17, SEQ. ID. NO. 18, polypeptides SEQ. ID. NO. 11., SEQ. ID. NO. 12, SEQ. ID. NO. 13, SEQ. ID. NO. 14, SEQ. ID. NO. 16, SEQ. ID. NO. 17 and SEQ. ID. NO. 18 ; and wherein the second aliquot is first contacted with unbound polypeptide and then contacted with said bound polypeptide wherein the unbound polypeptide is selected from the group consisting of recombinant proteins SEQ. ID. NO. 11 , SEQ. ID. NO. 12, SEQ. ID. NO. 13, SEQ. ID. NO. 14, SEQ. ID. NO. 16, SEQ. ID. NO. 17, SEQ. ID. NO. 18, polypeptides SEQ. ID. NO. 11., SEQ. ID. NO. 12, SEQ. ID. NO. 13, SEQ. ID. NO. 14, SEQ. ID. NO. 16, SEQ. ID. NO. 17 and SEQ. ID. NO. 18 and wherein the bound polypeptide selected is not the same as the same as the unbound polypeptide selected. 21 . In a neutralization assay for identifying the presence of an antibody immunologically reactive with an HCV antigen in a fluid sample wherein the sample is used to prepare first and second immunologically equivalent aliquots wherein the first aliquot is contacted with a polypeptide bound to a solid support under conditions suitable for complexing the antibody with the polypeptide to form a detectable antibody-polypeptide complex wherein the bound polypeptide is selected from the group consisting of recombinant proteins SEQ. ID. NO. 11, SEQ. ID. NO. 12, SEQ. ID. NO. 13, SEQ. ID. NO. 14, SEQ. ID. NO. 16, SEQ. ID. NO. 17, SEQ. ID. NO. 18, polypeptides SEQ. ID. NO. 11., SEQ. ID. NO. 12, SEQ. ID. NO. 13, SEQ. ID. NO. 14, SEQ. ID. NO. 16, SEQ. ID. NO. 17 and SEQ. ID. NO. 18; and wherein the second aliquot is first contacted with unbound polypeptide and then contacted with said bound polypeptide wherein the unbound polypeptide is selected from the group consisting of recombinant proteins SEQ. ID. NO. 11 , SEQ. ID. NO. 12, SEQ. ID. NO. 13, SEQ. ID. NO. 14, SEQ. ID. NO. 16, SEQ. ID. NO. 17, SEQ. ID. NO. 18, polypeptides SEQ. ID. NO. 11., SEQ. ID. NO. 12, SEQ. ID. NO. 13, SEQ. ID. NO. 14, SEQ. ID. NO. 16, SEQ. ID. NO. 17 and SEQ. ID. NO. 18; and wherein the bound polypeptide selected is not the same as the unbound polypeptide selected; and wherein the second aliquot is contacted with unbound and bound polypeptide simultaneously. 22. An immunoassay kit comprising: a polypeptide containing at least one HCV antigen selected from the group consisting of recombinant proteins SEQ. ID. NO. 11, SEQ. ID. NO. 12, SEQ. ID. NO. 13, SEQ. ID. NO. 14, SEQ. ID. NO. 16, SEQ. ID. NO. 17, SEQ. ID. NO. 18, polypeptides SEQ. ID. NO. 11., SEQ. ID. NO. 12, SEQ. ID. NO. 13, SEQ. ID. NO. 14, SEQ. ID. NO. 16, SEQ. ID. NO. 17 and SEQ. ID. NO. 18; one or more sample preparation reagents; and one or more detection and signal producing reagents. 23. A kit of claim 22 wherein the polypeptides are bound to a solid support.

Inventors: CASEY JAMES M, DESAI SURESH M, DEVARE SUSHIL G, RUPPRECHT KEVIN R, CASEY, JAMES, M., DESAI, SURESH, M., DEVARE, SUSHIL, G., RUPPRECHT, KEVIN, R.
Applicants: ABBOTT LAB, ABBOTT LABORATORIES
Application year: 1992
Main classification: C12Q1
IPC codes: C07K14, C07K16, C07K19, C12N15, C12P21, C12R1, G01N33