CELL CYCLE CHECKPOINT PIK-RELATED KINASE MATERIALS AND METHODS

Abstract: The present invention generally relates to genes encoding cell cycle checkpoint phosphatidylinositol kinase (PIK)-related proteins essential to DNA damage responses in cells. These PIK-related kinases are required in regulatory pathways that arrest the cell cycle following DNA damage to allow DNA repair prior to mitosis or initiation of DNA replication. More particularly, the invention provides a novel human cell cycle checkpoint PIK-related kinase, MCCS1, and polynucleotide sequences encoding the MCSS1. Assays for identifying modulators of MCCS1 useful as, for example, chemotherapy and radiation adjuvants, are also provided by the invention. Further, assays for identifying modulators of the cell cycle checkpoint phosphatidylinositol kinase (PIK)-related protein identified as ATM are provided.

Description: CELL CYCLE CHECKPOINT PIK-RELATED KINASE MATERIALS AND METHODS FIELD OF THE INVENTION The present invention generally relates to genes encoding cell-cycle checkpoint phosphatidylinositol kinase (PΙK)-related genes and proteins essential to DNA damage responses in cells. The checkpoint kinases play a role in the surveillance of DNA damage that occurs as a result of replication errors, DNA mismatches, radiation treatment, or chemotherapeutic drugs. These kinases are required in regulatory pathways that lead to cell cycle arrest following DNA damage, giving the cell notice and time to correct lesions prior to the initiation of DNA replication. More particularly, the invention relates to a novel human PIK-related kinase, Mammalian Cell Cycle Surveillance 1 (MCCS1), polynucleotides encoding the PIK-related kinase, and methods for assaying and modulating the enzymatic activity of the kinase and related kinases. BACKGROUND The process of eukaryotic cell growth and division is the somatic or mitotic cell cycle which consists of four phases, the G, phase, the S phase, the G 2 phase, and the M phase. The G,, S, and G 2 phases are collectively referred to as interphase of the cell cycle. The cell cycle is structurally and functionally conserved in its basic process and mode of regulation across all eukaryotic species. During the G, (gap) phase, biosynthetic activities of the cell progress at a high rate. The S (synthesis) phase begins when DNA synthesis starts and ends when the DNA content of the nucleus of the cell has been replicated and two identical sets of chromosomes are formed. The cell then enters the G 2 (gap) phase which continues until mitosis starts. In mitosis, the chromosomes pair and separate and two new nuclei foπn, and in cytokinesis the cell itself splits into two daughter cells each receiving one nucleus containing one of the two sets of chromosomes. Mitosis and cytokinesis together form the M (mitosis) phase of the cell cycle. Cytokinesis terminates the M phase and marks the beginning of interphase of the next cell cycle. The sequence in which the events in the cell cycle proceed is tightly regulated such that the initiation of one cell cycle event is dependent on the completion of the prior cell cycle event. This allows fidelity in the duplication and segregation of genetic material from one generation of cells to the next. The term "cell cycle checkpoints" refers to the proteins, signals, processes, and feedback controls that integrate discontinuous events during cellular replication, in order to maintain essential dependencies within the cell cycle. The present invention specifically relates to the cell cycle checkpoint that ensures that mitosis is delayed until the completion of DNA synthesis and/or the accurate repair of DNA damage occurs. Failure of cell cycle checkpoints predisposes individuals to or directly causes many disease states such as cancer, ataxia telangiectasia, embryo abnormalities, and various immunological defects associated with aberrant B and T cell development. The latter are associated with pathological states such as lupus, arthritis and autoimmune diseases. Intense research efforts have therefore focused on identifying cell cycle checkpoints and the proteins essential for the function of the checkpoints. Genetic analysis in the yeasts Schizosaccharomyces pombe and Saccharomyces cerevisiae has identified a number of genes important for cell cycle arrest and DNA repair responses to ionizing radiation (TR). For a review, see Carr and Hoekstra, Trends in Cell Biology, 5: 32-40 (1995). One such gene, identified in both yeasts, is required for a DNA damage checkpoint which arrests the cell cycle at the G2 phase, as well as a related checkpoint which monitors the completion of DNA synthesis and arrests the cell cycle at the S phase. The gene is named rad3+ in 5. pombe [Seaton et al. , Gene, 119: 83-89 (1992)], MEC1IESR1 in S. cerevisiae [Kato et al. , Nuc. Acids. Res. , 22(15): 3104-3112 (1994)], and is hereinafter referred to as rad3+. Cells having mutations in rad3+ fail to either sense or appropriately respond to DNA damage and subsequently lose viability more rapidly than wild type cells after exposure to clastogenic agents or events (e.g. , IR, DNA damaging agents, and mutations affecting chromosomal integrity). See Weinert et al. , GENES & DEVELOPMENT, 8: 652-665 (1994) and Al-Khodairy et al. , EMBO J . , 11(4): 1343- 1350 (1992). This sensitivity to IR (radiosensitivity) can be caused by defects in checkpoint responses or defects in direct DNA repair reactions. The product of the rad3 + gene is an approximately 270 kD protein that falls into a growing family of high molecular weight PIK-related kinases. See Hunter, Cell, 83: 1-4 (1995) for a discussion of this family of kinases. The primary structures of the catalytic domains found in members of this gene family are closely related to well characterized phosphatidylinositol kinases. This structural relationship initially suggested that these PIK-related kinases might be capable of phosphorylating lipids. When the substrate specificity of the PIK-related kinases is examined, however, these enzymes appear to function as protein kinases and have yet to be demonstrated to phosphorylate phosphatidylinositides. Hartley et al. , Cell, 82: 849856 (1995) reports that purified preparations highly active in protein kinase assays failed to show lipid kinase activity. Additional PIK-related kinases identified include: the TEL1 gene product from S. cerevisiae which affects telomere length [Greenwell et al. , Cell, 82: 823-829 (1995)], and Mei41 + gene product from Drosophila melanogaster which is important for a G2 checkpoint and meiotic development [Hari et al. , Cell, 82: 815-821 (1995)], the DNA-PK gene product from mouse which is important in immunoglobulin rearrangements and processing of DNA double strand breaks, and the FRAP gene product which is important in the Gl/S transition [Brown, E. et al. , Nature, 377: 441-446 (1995)]. Mutations in the DNA-PK gene can result in the Severe Combined Immunodeficiency Syndrome (SCID) defect (Hartley et al. , supra). In humans, less is known about the molecular components required for checkpoint function. One component of the mammalian checkpoint machinery has been identified through the analysis of the human disease syndrome ataxia- telangiectasia (AT). Patients with AT show a diverse set of clinical symptoms, including predisposition to a variety of tumor types. Fibroblasts from AT patients are radiosensitive and fail to undergo cell cycle arrest following treatment with IR leading to a phenomenon termed radioresistant DNA synthesis. This is reminiscent of the S. pombe rad3 defect where cells fail to sense or respond appropriately to DNA damage. Interestingly, the locus responsible for AT, the Ataxia-Telangiectasia Mutated (ATM) gene, was recently described in Savitsky et al , Science, 268: 1749-1753 (1995) and the partial cDNA encodes a protein with amino acid similarity to the rad3+ gene. Savitsky et al. , Human Molecular Genetics, 4(11)..-2025-2032 (1995) describes isolation of a cDNA encoding full length ATM. The increased radiosensitivity of rad3+ yeast mutants and of mammalian cells lacking functional ATM suggests that these proteins may comprise a family of checkpoint proteins. Kuerbitz et al. , Proc. Natl. Acad. Sci. USA, 89: 7492-7495 (1992) establishes that the tumor suppressor p53 is required for a Gl checkpoint and cell cycle arrest observed following DNA damage. Irradiation of cells results in increased levels of p53 leading to the transcriptional activation of p53 responsive genes. One such p53-induced target is the product of the WAF1 gene (also called p21 , CIP1 , and sdil). WAF1 is a member of an expanding class of cell cycle regulators termed cyclin-dependent kinase inhibitory proteins. The activities of cyclin-dependent kinases control transit through the cell cycle. Transcriptional activation of WAF1 thus provides a direct link between DNA damage-dependent induction of p53 and the inhibition of kinases essential for cell cycle progression. See Elledge and Harper, Current Opinion in Cell Biology, 6: 847-852 (1994). Mutations in the p53 gene are one of the most common genetic alterations in human cancers. For example, Baker et al. . Science, 244:217-221 (1989) reports that approximately 70% of human colorectal carcinomas contain deletions or mutant copies of the p53 gene. In addition, Fearon et al. , Cell, 61: 759-767 (1990) reports that breast, lung, bladder and brain tumors have been associated with loss of chromosome 17p, the region to which the p53 gene localizes. At present there is relatively little known about the molecular components of the G2 checkpoints in mammalian cells. Caffeine is a chemical entity which abrogates G2 checkpoint control. Russell et al , Cancer Res., 55: 1639-1642 (1995) and Powell et al , Cancer Res. , 55: 1643-1648 (1995) report that analysis of cell lines which differ only by the presence or absence of functional p53 demonstrated preferential caffeine-enhanced sensitization to IR in those cells lacking the p53- dependent Gl checkpoint. Thus, the conversion of potentially lethal damage into lethal damage is greater in cells lacking the Gl and G2 checkpoints in comparison to cells containing an intact Gl checkpoint. While certain cells undergo DNA damage-dependent cell cycle arrest, other cells appear to respond to DNA damage by initiating an intrinsic suicide program termed apoptosis or programmed cell death. The factors determining which process occurs are not fully understood. Recent work has demonstrated an important role for p53 both in the regulation of Gl cell cycle transitions and apoptosis. Symonds et al , Cell, 78: 703-711 (1994) describe p53-dependent apoptosis as suppressing tumor growth and progression in vivo. High doses of radiation and chemotherapy are used to treat tumor cells in order to damage DNA so severely that the cells will die. However, even though tumor cells having mutations in the p53 gene are defective in a Gl checkpoint, they can still repair DNA damaged induced by radiation or chemotherapy. The present invention contemplates, for example, that inhibition of the G2 checkpoint in tumor cells should lead to a state in which tumor cells are incapable of repairing DNA damage therefore sensitizing the tumor cells to DNA damaging agents. Normal cells, containing intact Gl and G2 checkpoints, should still be able to repair DNA damage in the presence of a G2 checkpoint-specific inhibitor. Thus, treatment of tumors with a G2 checkpoint-specific inhibitor followed by radiation or chemotherapy should increase the efficacy of cell killing and thereby decrease the required doses of toxic DNA-damaging agents. There thus exists a need in the art for identification of the mammalian proteins that are involved in the cell cycle checkpoints in order to develop therapies for the human disease states associated with defective cell cycle checkpoints and for the isolation of the genes encoding those proteins which in themselves may be useful as therapeutics or which would enable the development of therapeutically useful modulators of the proteins encoded by the genes. SUMMARY OF THE INVENTION The present invention provides novel human PIK-related kinases essential for a cell cycle checkpoint that responds in the G2 phase of the cell cycle to both damaged and unreplicated DNA. In one of its aspects, the present invention provides purified and isolated polynucleotides (e.g. , DNAs and RNAs, both coding and non-coding strands thereof) encoding the cell cycle checkpoint PIK-related kinase MCCSl and polynucleotides encoding other cell cycle checkpoint PIK-related kinases that exhibit about 50, about 60, or about 65% nucleotide identity to the MCCSl polynucleotide region encoding the MCCSl kinase domain (MCCSlα nucleotides 6579 to 7562 of SEQ ID NO: 30 or MCCS 1/3 nucleotides 6457 to 7440 of SEQ ID NO: 32). Alternatively, the MCCSl -like PIK-related kinases exhibit about 40% , about 45 % , or about 50% amino acid identity to the MCCSl kinase domain (MCCSlα amino acids 2083 to 2410 of SEQ ID NO: 31 or MCCS 1/3 amino acids 2152 to 2480 of SEQ ID NO: 33). Polynucleotides contemplated by the invention include genomic DNAs, RNAs, cDNAs and wholly or partially chemically synthesized DNAs. Preferred polynucleotides of the invention comprise the MCCSlα DNA sequence set out in SEQ ID NO: 30, the partial MCCS1/3 DNA sequence set out in SEQ ID NO: 3, the full length MCCS 1 3 DNA sequence set out in SEQ ID NO: 32, and DNA sequences which hybridize to the noncoding strands thereof under stringent conditions or which would hybridize but for the redundancy of the genetic code. Exemplary stringent hybridization conditions are as follows: hybridization at 65 °C in 3X SSC, 20mM NaPO 4 pH 6.8 and washing at 65 'C in 0.2X SSC. It is understood by those of skill in the art that variation in these conditions occurs based on the length and GC nucleotide base content of the sequences to be hybridized. Formulas standard in the art are appropriate for determining exact hybridization conditions. See Sambrook et al , 9.47-9.51 in Molecular Cloning, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York (1989). The MCCSlα DNA of SEQ ID NO: 30 was deposited with the American Type Culture Collection (ATCC), 12301 Parklawn Drive, Rockville, Maryland 20852, on November 3, 1995 as an insert in plasmid pBSHFB/HT2-27 in E. coli DH5α and was assigned ATCC Accession No. 69951. The MCCS 1 / 3 DNA of SEQ ID NO: 32, was deposited with the ATCC on November 7, 1995 as an insert in plasmid 517 in E. coli DH5α and was assigned ATCC Accession No. 69950. The DNA sequence information provided by the present invention makes possible the identification and isolation of DNAs encoding related molecules by well-known techniques such as DNA/DNA hybridization as described above and polymerase chain reaction (PCR) cloning. As one series of examples, knowledge of the sequence of a cDNA encoding MCCS l makes possible the isolation by DNA/DNA hybridization of genomic DNA sequences encoding the kinase and expression control regulatory sequences such as promoters, operators and the like. Similarly, knowledge of a partial cDNA sequence encoding MCCS1/3 make isolation of a complete cDNA possible. DNA/DNA hybridization procedures carried out with DNA sequences of the invention under stringent conditions are likewise expected to allow the isolation of DNAs encoding allelic variants of the PIK-related kinase; non- human species enzymes homologous to the PIK-related kinase; and other structurally related proteins sharing one or more of the enzymatic activities, or abilities to interact with members or regulators, of the cell cycle checkpoint pathway in which MCCSl participates. Polynucleotides of the invention when detectably labelled are also useful in hybridization assays to detect the capacity of cells to synthesize MCCSl . The DNA sequence information provided by the present invention also makes possible the development, by homologous recombination or "knockout" strategies [see, Capecchi, Science, 244: 1288-1292 (1989)], of rodents that fail to express functional MCCSl or that express a variant of MCCSl . Such rodents are useful as models for studying the activities of MCCSl and MCCSl modulators in vivo. Polynucleotides of the invention may also be the basis for diagnostic methods useful for identifying a genetic alteration(s) in the MCCSl locus that underlies a disease state or states. Also made available by the invention are anti-sense polynucleotides relevant to regulating expression of MCCSl by those cells which ordinarily express the same. The invention also provides autonomously repbcating recombinant constructions such as plasmid and viral DNA vectors incorporating polynucleotides of the invention, especially vectors in which the polynucleotides are functionally linked to an endogenous or heterologous expression control DNA sequence and a transcription terminator. According to another aspect of the invention, host cells, especially unicellular host cells such as procaryotic and eukaryotic cells, are stably transformed or transfected with DNAs of the invention in a manner allowing expression of the PIK-related kinase therein. Host cells of the invention are conspicuously useful in methods for the large scale production of MCCSl wherein the cells are grown in a suitable culture medium and the desired enzymes are isolated from the cells or from the medium in which the cells are grown. MCCSl products having part or all of the amino acid sequence set out in SEQ ID NO: 31 , SEQ ID NO: 4, or SEQ ID NO: 33 are contemplated. Use of mammalian host cells is expected to provide for such post-translational modifications (e.g. , myristoylation, glycosylation, truncation, lipidation and tyrosine, serine or threonine phosphorylation) as may be needed to confer optimal biological activity on recombinant expression products of the invention. The enzyme products of the invention may be full length polypeptides, fragments or variants. Variants comprise MCCSl products wherein one or more of the specified (i.e. , naturally encoded) amino acids is deleted or replaced or wherein one or more nonspecified amino acids are added: (1) without loss of the kinase activity specific to MCCSl ; or (2) with disablement of the kinase activity specific to MCCSl ; or (3) with disablement of the ability to interact with members or regulators of the cell cycle checkpoint pathway. Substrates of MCCSl and proteins which interact with MCCSl may be identified by various assays. Substrates of MCCSl may be identified by incorporating test compounds in assays for kinase activity. MCCSl kinase is resuspended in kinase buffer and incubated either in the presence or absence of the test compound (e.g. , casein, histone HI , or appropriate substrate peptide). Moles of phosphate transferred by the kinase to the test compound are measured by autoradiography or scintillation counting. Transfer of phosphate to the test compound is indicative that the test compound is a substrate of the kinase. Interacting proteins may be identified by the following assays. A first assay contemplated by the invention is a two-hybrid screen. The two-hybrid system was developed in yeast [Chien et al. , Proc. Natl. Acad. Sci. USA, 88: 9578-9582 (1991)] and is based on functional in vivo reconstitution of a transcription factor which activates a reporter gene. Specifically, a polynucleotide encoding a protein that interacts with MCCSl is isolated by: transforming or transfecting appropriate host cells with a DNA construct comprising a reporter gene under the control of a promoter regulated by a transcription factor having a DNA binding domain and an activating domain; expressing in the host cells a first hybrid DNA sequence encoding a first fusion of part or all of MCCS 1 and either the DNA binding domain or the activating domain of the transcription factor; expressing in the host cells a library of second hybrid DNA sequences encoding second fusions of part or all of putative MCCS 1 binding proteins and the DNA binding domain or activating domain of the transcription factor which is not incoφorated in the first fusion; detecting binding of an MCCSl interacting protein to MCCSl in a particular host cell by detecting the production of reporter gene product in the host cell; and isolating second hybrid DNA sequences encoding the interacting protein from the particular host cell. Presently preferred for use in the assay are a lexA promoter to drive expression of the reporter gene, the lacZ reporter gene, a transcription factor comprising the lexA DNA binding domain and the GAL4 transactivation domain, and yeast host cells. Other assays for identifying proteins that interact with MCCSl may involve immobilizing MCCSl or a test protein, detectably labelling the nonimmobilized binding partner, incubating the binding partners together and determining the amount of label bound. Bound label indicates that the test protein interacts with MCCSl . Another type of assay for identifying MCCSl interacting proteins involves immobilizing MCCSl or a fragment thereof on a solid support coated (or impregnated with) a fluorescent agent, labelling a test protein with a compound capable of exciting the fluorescent agent, contacting the immobilized MCCSl with the labelled test protein, detecting light emission by the fluorescent agent, and identifying interacting proteins as test proteins which result in the emission of light by the fluorescent agent. Alternatively, the putative interacting protein may be immobilized and MCCS l may be labelled in the assay. Also comprehended by the present invention are antibody products (e.g. , monoclonal and polyclonal antibodies, single chain antibodies, chimeric antibodies, CDR-grafted antibodies and the like) and other binding proteins (such as those identified in the assays above) which are specific for the MCCS 1 kinases of the invention. Binding proteins can be developed using isolated natural or recombinant enzymes. The binding proteins are useful, in turn, for purifying recombinant and naturally occurring enzymes and identifying cells producing such enzymes. Specifically illistrating monoclonal antibodies of the invention are the monoclonal antibodies produced by hybridoma cell lines 224C and 224F which were deposited with the American Type Culture Collection (ATCC), 12301 Parklawn Drive, Rockville, MD 20852 on November 7, 1996 and assigned ATCC Accession Nos. HB 12233 and HB 12234, respectively. Assays for the detection and quantification of proteins in cells and in fluids may involve a single antibody substance or multiple antibody substances in a "sandwich" assay format. The binding proteins are also manifestly useful in modulating (i.e. , blocking, inhibiting, or stimulating) enzyme/ substrate or enzyme/ regulator interactions. Anti-idiotypic antibodies specific for PIK-related kinase binding proteins are also contemplated. The invention contemplates that mutations in the MCCSl gene that result in loss of normal function of the MCCSl gene product underlie human disease states in which failure of the G 2 cell cycle checkpoint is involved. Gene therapy to restore MCCSl activity would thus be indicated in treating those disease states (for example, testicular cancer). Delivery of a functional MCCSl gene to appropriate cells is effected in vivo or ex vivo by use of viral vectors (e.g. , adenovirus, adeno- associated virus, or a retrovirus) or ex vivo by use of physical DNA transfer methods (e.g. , liposomes or chemical treatments). For reviews of gene therapy technology see Fried ann, Science, 244: 1275-1281 (1989); Verma, Scientific American: 68-84 (1990); and Miller, Nature, 357: 455-460 (1992). Alternatively, it is contemplated that in other human disease states preventing the expression of or inhibiting the activity of MCCSl will be useful in treating the disease states. It is contemplated that antisense therapy or gene therapy could be applied to negatively regulate the expression of MCCSl . Antisense nucleic acids (preferably 10 to 20 base pair oligonucleotides) capable of specifically binding to MCCSl expression control sequences or MCCSl RNA are introduced into cells (e.g. , by a viral vector or colloidal dispersion system such as a liposome). The antisense nucleic acid binds to the MCCSl target sequence in the cell and prevents transcription or translation of the target sequence. Phosphothioate and methylphosphate antisense oligonucleotides are specifically contemplated for therapeutic use by the invention. The antisense oligonucleotides may be further modified by poly-L-lysine, transferrin polylysine, or cholesterol moieties at their 5' end. Moreover, for example, if a particular form of cancer results from a mutation in a gene other than MCCSl such as the p53 gene, an agent which inhibits the transcription or the enzymatic activity of MCCSl and thus the G 2 cell cycle checkpoint may be used to render cancerous cells more sensitive to chemotherapy or radiation therapy. The therapeutic value of such an agent lies in the fact that current radiation therapy or chemotherapy in most cases does nothing to overcome the ability of the p53 mutant cancerous cell to sense and correct the DNA damage imposed as a result of the treatment. As a result, a cancer cell can simply repair the DNA damage. Modulating agents of the invention may therefore be chemotherapy and radiation adjuvants or may be directly active as chemotherapeutic drugs themselves. Agents that modulate MCCSl kinase activity may be identified by incubating a test compound with MCCSl immunopurified from cells naturally expressing the PIK-related kinase, with MCCS l obtained from recombinant procaryotic or eukaryotic host cells expressing the enzyme, or with purified MCCSl , and then determining the effect of the test compound on MCCSl activity. The activity of the PIK-related kinase can be measured by determining the moles of 32 P-phosphate transferred by the kinase from gamma- 32 P-ATP to either itself (autophosphorylation) or to an exogenous substrate such as a lipid or protein. The amount of phosphate incoφorated into the substrate is measured by scintillation counting or autoradiography. An increase in the moles of phosphate transferred to the substrate in presence of the test compound compared to the moles of phosphate transferred to the substrate in the absence of the test compound indicates that the test compound is an activator of said MCCSl kinase. Conversely, a decrease in the moles of phosphate transferred to the substrate in presence of the test compound compared to the moles of phosphate transferred to the substrate in the absence of the test compound indicates that the modulator is an inhibitor of said MCCSl kinase. In another aspect, agents that modulate both MCCSl and ATM or modulate one of the enzymes are also contemplated. Agents which modulate MCCSl are screened in a kinase assay as described above in which ATM is the phosphorylating enzyme. In a presently preferred assay, a MCCSl -specific antibody linked to agarose beads is incubated with a cell lysate prepared from host cells expressing the kinase. The beads are washed to remove proteins binding nonspecifically to the beads and the beads are then resuspended in kinase buffer. The reaction is initiated by the addition of gamma- 2 P-ATP and an appropriate exogenous substrate such as lipid or peptide. The activity of the kinase is measured by determining the moles of 32 P- phosphate transferred either to the kinase itself or the added substrate. In a preferred embodiment the host cells lack endogenous MCCSl and/or ATM kinase activity. The selectivity of a compound that modulates the kinase activity of MCCSl can be evaluated by comparing its activity on MCCSl to its activity on other known PIK- related kinases. The combination of the recombinant MCCSl products of the invention with other recombinant PIK-related kinase products in a series of independent assays provides a system for developing selective modulators of MCCSl . Furthermore, combinatorial libraries, peptide and peptide mimetics, defined chemical entities, oligonucleotides, and natural product libraries may be screened for activity as modulators in assays such as those described below. For example, an assay for identifying modulators of MCCSl kinase activity involves incubating an MCCSl kinase preparation in kinase buffer with gamma- 32 P-ATP and an exogenous kinase substrate, both in the presence and absence of a test compound, and measuring the moles of phosphate transferred to the substrate. An increase in the moles of phosphate transferred to the substrate in presence of the test compound compared to the moles of phosphate transferred to the substrate in the absence of the test compound indicates that the test compound is an activator of said MCCSl kinase. Conversely, a decrease in the moles of phosphate transferred to the substrate in presence of the test compound compared to the moles of phosphate transferred to the substrate in the absence of the test compound indicates that the modulator is an inhibitor of said MCCS 1 kinase. Moreover, assays for identifying compounds that modulate interaction of MCCS 1 with other proteins may involve: transforming or transfecting appropriate host cells with a DNA construct comprising a reporter gene under the control of a promoter regulated by a transcription factor having a DNA-binding domain and an activating domain; expressing in the host cells a first hybrid DNA sequence encoding a first fusion of part or all of MCCS 1 and the DNA binding domain or the activating domain of the transcription factor; expressing in the host cells a second hybrid DNA sequence encoding part or all of a protein that interacts with MCCSl and the DNA binding domain or activating domain of the transcription factor which is not incoφorated in the first fusion; evaluating the effect of a test compound on the interaction between MCCSl and the interacting protein by detecting binding of the interacting protein to MCCSl in a particular host cell by measuring the production of reporter gene product in the host cell in the presence or absence of the test compound; and identifying modulating compounds as those test compounds altering production of the reported gene product in comparison to production of the reporter gene product in the absence of the modulating compound. Presently preferred for use in the assay are a lexA promoter to drive expression of the reporter gene, the lacZ reporter gene, a transcription factor comprising the lexA DNA binding domain and the GAL4 transactivation domain, and yeast host cells. Another type of assay for identifying compounds that modulate the interaction between MCCSl and an interacting protein involves immobilizing MCCS 1 or a natural MCCSl interacting protein, detectably labelling the nonimmobilized binding partner, incubating the binding partners together and determining the effect of a test compound on the amount of label bound wherein a reduction in the label bound in the present of the test compound compared to the amount of label bound in the absence of the test compound indicates that the test agent is an inhibitor of MCCSl interaction with protein. Conversely, an increase in the bound in the presence of the test compound compared to the amount label bound in the absence of the compound indicates that the putative modulator is an activator of MCCSl interaction with the protein. Yet another method contemplated by the invention for identifying compounds that modulate the binding between MCCSl and an interacting protein involves immobilizing MCCSl or a fragment thereof on a solid support coated (or impregnated with) a fluorescent agent, labelling the interacting protein with a compound capable of exciting the fluorescent agent, contacting the immobilized MCCS 1 with the labelled interacting protein in the presence and absence of a test compound, detecting light emission by the fluorescent agent, and identifying modulating compounds as those test compounds that affect the emission of light by the flourescent agent in comparison to the emission of light by the fluorescent agent in the absence of the test compound. Alternatively, the MCCSl interacting protein may be immobilized and MCCSl may be labelled in the assay. The present invention further provides a cell-based complementation assay for identifying compounds which modulate the activity of MCCSl or ATM. The assay involves complementation of a phenotypic trait associated with a genetic alteration in the cell. For example, the genetic alteration identified as esrl-1 results in cellular sensitivity to DNA damage in yeast cells [Kato et al , Nuc. Acids. Res. , 22(15): 3104-3112 (1994)]. esrl-1 cells fail to either sense or appropriately response to DNA damage after exposure to DNA damaging agents such as ionizing radiation or clastogenic agents. The phenotypic trait of the genetically altered cell is complemented by transforming and expressing MCCSl or ATM in the cell. The transformed cells are exposed to DNA damaging treatment (e.g. ionizing radiation) in the presence and absence of a test compound and sensitivity of the cells to DNA damage is measured. Agents that affect the cell sensitivity to DNA damaging activity of MCCS l and/or ATM are identified as modulators. Modulators of MCCS l may affect its kinase activity, its localization in the cell, and/or its interaction with members of the cell cycle checkpoint pathway. MCCSl modulators may be formulated in compositions comprising pharmaceutically acceptable carriers. Such compositions may additionally include chemotherapeutic agents. Dosage amounts indicated would be sufficient to result in modulation of MCCSl activity in vivo. Selective modulators may include, for example, polypeptides or peptides which specifically bind to MCCSl or MCCSl nucleic acid, oligonucleotides which specifically bind to the PIK-related kinase or PIK-related kinase nucleic acid, and/or other non-peptide compounds (e.g. , isolated or synthetic organic molecules) which specifically react with MCCSl or MCCSl nucleic acid. Mutant forms of MCCSl which affect the enzymatic activity or cellular localization of wild-type MCCSl are also contemplated by the invention. Presently preferred regions of the PIK-related kinases which are targets for the development of selective modulators include, for example, the following four regions: the MCCSlα amino terminal effector domain (amino acids 1 to 1081 of SEQ ID NO: 31), the MCCS 1/3 a ino terminal effector domain (amino acids 1 to 1150 of SEQ ID NO: 33), the MCCSlα rad3+ domain (amino acids 1082 to 2082 of SEQ ID NO: 31), the MCCS1/3 rad3+ domain (amino acids 1 151 to 2151 of SEQ ID NO: 33), the MCCS lα PIK domain (amino acids 2083 to 2410 of SEQ ID NO: 31), and the MCCS 1/3 PIK domain (amino acids 2152 to 2480 of SEQ ID NO: 33). DET AILED DESCRIPTION The present invention is illustrated by the following examples. Example 1 details the isolation of cDNAs encoding MCCSl kinases. Example 2 describes mapping of the human MCCSl gene to human chromosome 3. The recombinant expression of MCCSl in E. coli and insect cells is respectively described in Examples 3 and 4. Example 4 also presents assays for measuring MCCSl kinase activity. Example 5 describes the production of MCCS 1 -specific polyclonal and monoclonal antibodies. Example 6 reports the immunoprecipitation of MCCS 1 kinase associated activity from mouse testes. Example 7 examines the expression of MCCS 1 mRNA in various human tissues and cancer cell lines. Example 8 describes analyses of MCCSl mRNA and protein expression in mouse testes. Example 9 describes analyses of MCCSl protein expression in meiotic cells. Assays for substrates and interacting proteins of MCCSl are described in Example 10. Example 1 1 describes modulators and assays for modulators of the kinase activity of MCCS 1. Example 12 describes the cell-based complementation assay for identifying modulators of MCCS 1 and/or ATM and Example 13 describes the kinase activity of ATM. Example 1 cDNAs encoding the PIK-related kinase MCCSl were isolated by a series of PCR reactions. An alignment of the amino acid sequences of S. pombe rad3+ (Hari et al. , supra) and S. cerevisiae MEC1 (Kato et al. , supra) was the basis for design of seven degenerate oligonucleotides that encoded (or were complementary to) the regions of highest homology/lowest degeneracy between the sequences and contained convenient restriction sites to facilitate cloning of amplification products. The oligonucleotides were then used in a PCR-based assay to isolate a related human sequence. Initially, PCR amplifications were performed on cDNA preparations from rat T-cells, human peripheral blood mononuclear cells (PBMC), and S. cerevisiae genomic DNA. Five oligonucleotide pairs were used (oDH15a/oDH16, oDH15b/oDH16, oDH17a/oDH16, oDH15a/oDH17b, and oDH15b/oDH17b) for the primary amplifications. The sequences of the oligonucleotide primers included inosines and are set out below in IUPAC nomenclature for degenerate nucleotide positions. oDH15a (SEQ ID NO: 5) 5' GCA GAC GGA TCC GGI WCI GAY GGI AAY HTI TAY 3' oDH15b (SEQ ID NO: 6) 5 ' GCA GAC GGA TCC GGI WCI GAY GGI AAY 3 ' oDH16 (SEQ ID NO: 7) 5' GCA GAC GAA TTC RCA RTY RAA RTC IAC RTG 3' oDH17a (SEQ ID NO: 8) 5' GCA GAC GGA TCC AAR TTY CCI CCI RTI YTI TAY SAR TGG TT 3 ' oDH17b (SEQ ID NO: 9) 5' GCA GAC GAA TCC AAC CAY TSR TAI ARI AYI GGI GGR AAY TT 3 ' PCR was performed on reaction mixtures of IX PCR buffer (Perkin Elmer Cetus, Emeryville, California), 2-3/ M oDH primers, 1.5mM MgCl 2 , 200μM dNTPs, and 0.5 μl Amplitaq polymerase. The reaction was performed in a Perkin-Elmer Cetus Thermocycler Model 480 under the following conditions: denaturation at 94 ° C for 1 minute, annealing at 64 " C for 2 minutes, and elongation at 72 °C for 1 minute for 3 cycles. The procedure was then repeated using 60 °C annealing temperature for 3 cycles, 56 °C annealing for 3 cycles, and finished with denaturation at 94 °C for 1 minute, annealing at 54 ° C (2 minutes, and elongation at 72 * C for 1 minute for 30 cycles. PCR products were separated on 2 or 4% Tris Acetate EDTA (TAE) agarose gels, stained with ethidium bromide, and DNA products were visualized by UV fluorescence. From the primary amplifications of yeast genomic DNA, rat T-cell cDNA, and human PBMC cDNA, only a single reaction with yeast genomic DNA (oDH17a/oDH16) gave a visible amplification product, resulting in a product that was the expected size for the region of the S. cerevisiae MECl gene between these primers. Further analysis of the oDH17a/oDH16 amplifications that utilized rat T- cell and PBMC cDNA was therefore performed. To remove oligonucleotides and "primer dimers" that might interfere with subsequent PCR, primary reactions were purified prior to reamplification. A "nested" PCR strategy was employed, and amplifications were repeated with primer pairs oDH18a/oDH16 and oDH18b/oDH16 under reaction conditions described above with cycle times of denaturation of 94°C for 1 minute, annealing at 55 C for 1 minute, and elongation at 72' C for 30 seconds for 30 cycles. The sequences of the oDH18a and oDH18b oligonucleotide primers included inosines and are set out below in IUPAC nomenclature for degenerate nucleotide positions. oDH18a (SEQ ID NO: 10) 5' GCA GAC GGA TCC YΗ GGI YTI GGI GAY CGI CA 3' oDH18b (SEQ ID NO: 1 1) 5' GCA GAC GGA TCC YΗ GGI YTI GGI GAY AGR CA 3' An approximately 90 base pair (bp) product (the expected size amplification product for these primers) was seen in the reamplifications of the yeast genomic and human PBMC cDNA primary reactions. No 90 bp product was seen in the reamplification of the primary reaction on rat T-cell cDNA and this reaction was not analyzed further. In addition to the approximately 90 bp product, several other non- specific bands were also present, though significantly fewer than were observed when the primary reactions were reamplified with oDH17a/oDH16. While the approximately 90 bp product was present in both the oDH18a/oDH16 and oDH18b/oDH16 reamplifications of the yeast genomic DNA primary reactions, only the oDH18a/oDH16 reaction yielded the appropriate size fragment during reamplification of the human PMBC cDNA primary reaction. This was presumed to reflect codon usage in the human gene (compare primers oDH18a and oDHl 8b). The approximately 90 bp product from the oDH18a/oDH16 reamplification of the human PMBC cDNA primary reaction was gel purified and subcloned into the pBluescript SKπ+ cloning vector (Stratagene, La Jolla, California) and sequenced. Analysis of the sequence encoded by the 90 bp product indicated that the deduced amino acid sequence was similar to both S. cerevisiae MECl and S. pombe rad3+, but was not identical to either. To identify a larger region of coding sequence and extend the sequence comparison, a non-degenerate oligonucleotide, oDH23 5' GACGCAGAATTCACCAGTCAAAGAATCAAAGAG 3' (SEQ ID NO: 12), was synthesized for use in additional amplification reactions. Reamplification of the purified PBMC cDNA primary reaction with oDH17a/oDH23 led to the production of an amplification product of 174 bp. This fragment was then purified, subcloned and sequenced as described above. Computer analysis of the conceptual translation product confirmed its relationship (similar but not identical) to MECl and rad3+ . This PCR fragment was then used as a probe to screen a plasmid library containing macrophage cDNA using the following hybridization conditions: incubation of nitrocellulose filters with radiolabelled probes in 3X SSC, 5X Denhardt's, 0.1 % sarcosyl, 20mM NaPO 4 pH 6.8, 100 ug/ml single stranded salmon speπn DNA, for 18 to 24 hours at 65 °C. Washes were done 3 times in 0.2X SSC, 0.1 % SDS at 65 °C for 30 minutes (with changes of wash buffer). Four positive clones were isolated, and the nucleotide sequence of each was determined. Computer analysis of the four sequences demonstrated that they were overlapping clones derived from a locus with homology to the rad3+ gene from S. pombe. Clone 517 (ATCC 69950) contained a 2.8 kbp insert and its DNA and deduced amino acid sequence are set out in SEQ ID NOs: 3 and 4, respectively. The clone contained an open reading frame encoding an amino terminal truncated protein product of 870 amino acids which were 39% identical to the COOH-terminus of rad3+ . The protein product of the cDNA insert was named MCCS 1/3. The sequence of clone 517 was used to design the oligonucleotides, mo3 5'-CTACAGAGCCAAGGAG-3' (SEQ ID NO: 13) and mo6 5'- TCGAGCTATGCTACTAGTGGGC-3' (SEQ ID NO: 14), which were used to generate a probe using a gel purified EcoRI fragment derived from clone 517 as a template. The PCR conditions were as follows: 50 ng DNA fragment, IX PCR buffer (Perkin-Elmer Cetus), 1.5mM MgCl 2 , 200/χM dATP, dGTP, and TTP, l M dCTP, 50μCi α 32 P-dCTP, lOng/ml each oligonucleotide, 1U AmpliTaq (Perkin-Elmer Cetus). The reaction was performed in a Perkin-Elmer Cetus Thermocycler Model 480 for an initial denaturing cycle at 94 ° C for 4 minutes followed by 20 cycles of 94°C for 15 seconds, 60°C for 15 seconds, 72 ° C for 30 seconds. Unincoφorated nucleotides were removed using a Stratagene Nuc-trap Push Column. Since Northern blot analyses showed that the expression of the mRNA corresponding to clone 517 was highest in testis, one million clones from a human testis cDNA library (Stratagene #939202) were screened with the PCR-generated probe and eleven clones were obtained. The two longest clones, HT2 and HT9, were chosen for analysis. HT2 contained a 4.7 Kb insert (corresponding to nucleotide 2974 of SEQ ID NO: 30 and extending further downstream than SEQ ID NO: 1) and HT9 contained a 5485 bp insert (corresponding to nucleotides 2152 to 7624 of SEQ ID NO: 30). Nucleotide sequence analysis revealed that in the region common to both cDNA clones there was a single base pair insertion of a T at nucleotide 3233 in HT9. This nucleotide insertion causes the predicted amino acid reading frame to shift and then terminate and is believed to be an error introduced by reverse transcriptase in clone HT9. In order to isolate a clone containing an additional 2.5 Kb, one million clones from each of three additional cDNA libraries were screened: a human fetal brain cDNA library (Stratagene #93206), a human heart cDNA library (Stratagene # 936207), and a human aorta cDNA library (Clontech Laboratories #HL1 136a, Palo Alto, California). The sequence of the most 5' region of HT9 was utilized to design and synthesize two oligonucleotides, oHT9-l 5'-CCTAGTCCAGTAAAACTTGC-3' (SEQ ID NO: 15) and oHT9-4 S'-TTTGCGGCCCTTCCAATATC-S' (SEQ ID NO: 16) which were used to generate a 317 bp PCR probe under conditions described for generating the probe above. While no positive clones were isolated from the heart or aorta cDNA libraries, two positive clones were obtained from the fetal brain library. One of these clones, HFB2, included a cDNA 4.5 Kb insert which included approximately 2300 bp of additional sequence. The HFB2 insert corresponds to nucleotides 1 to 3194 of SEQ ID NO: 30. A composite cDNA encoding MCCSlα was constructed from clones HFB2, HT9 and HT2. The three clones were joined together by digesting HFB2 with the restriction enzymes Kpnl and Sail to generate a fragment to comprise the 5 ' end of the composite clone, digesting HT9 with Kpnl and NotI to generate a fragment to comprise the 3' end of the composite clone, and then ligating isolated fragments to the vector pBS SK " (Stratagene) that had been digested with Sail and NotI. The region of the HT9 fragment containing the one nucleotide insertion was replaced with an EcoRV fragment containing nucleotides 3174 to 5282 of clone HT2. The final plasmid containing a 7621 bp insert was named pBSHFB2HT2-27 (ATCC 69951). The DNA and deduced amino acid sequence of the insert are presented in SEQ ID NOs: 1 and 2, respectively. The coding domain of the cDNA initiates with an ATG at nucleotide 333 and ends with a termination codon at nucleotide 7560 predicting a coding sequence of 2409 amino acids and protein of 265 kD. The protein product of the cDNA insert was named MCCSlα. Subsequent sequence analysis of the insert in plasmid pBSHFB2HT2-27 (ATCC 69951) revealed sequencing errors in SEQ ID NO: 1. Corrected DNA and deduced amino acid sequences of the insert are set out in SEQ ID NOs: 23 and 24, respectively. Even further sequence anaysis of insert in plasmid pBSHFB2HT2-27 revealed sequencing error in SEQ ID NO: 23. At nucleotide position 6317 (SEQ ID NO: 23) a "G" was erroneously included and between positions 6338 and 6339 the sequence was missing an "A" . The corrected sequences of MCCSlα are provided in SEQ ID NOs: 30 and 31. Comparison of the predicted amino acid sequence of MCCSl with the partial amino acid sequence of MCCS1/3 predicted from clone 517 revealed the presence of a seventy amino acid deletion in the MCCSlα product. The MCCS 1/3 clone 517 amino acid sequence corresponds to MCCSlα amino acids 161 1 to 2410 of SEQ ID NO: 31. The seventy amino acid deletion in MCCSlα (i.e. , where the seventy amino acids would be inserted to generate a product identical to MCCS 1/3) occurs between amino acids 2065 and 2066 in SEQ ID NO: 31 , seventeen amino acids upstream from the kinase domain. Since both clones maintain an open reading frame, cDNA clone pBSHFB2HT2-27 was apparently generated from alternatively spliced mRNA. The carboxyl terminal domains containing the kinase domains are identical in MCCSlα (amino acids 2083 to 2410 of SEQ ID NO: 31) and MCCS1 / 3 clone (amino acids 543 to 870 of SEQ ID NO: 4). A composite clone containing the complete coding sequence of MCCS 1 / 3 (with the seventy amino acid insert) is presented in SEQ ID NO: 32. The amino acid sequence deduced from the clone is presented in SEQ ID NO: 33. This clone is constructed by replacing the sequence between the BSTXI site, which cleaves after nucleotide 3229, and the NotI site in the polylinker sequence at the 3' end of pBSHFB2HT2-27 (SEQ ID NO: 1) with the sequence contained in HT2 between the BstXI site and the NotI site at the 3' end of HT2. Thus this clone contains sequences that are identical to MCCSlα nucleotides 1 to 5159 of SEQ ID NO: 1 (encoding amino acids 1 to 1609 of SEQ ID NO: 2) linked to sequences that are identical to clone 517 nucleotides 1 to 2610 of SEQ ID NO: 3 (encoding amino acids 1 to 870 of SEQ ID NO: 4). As noted above, subsequent sequence analysis revealed errors in nucleotides 1 to 5159 of SEQ ID NO: 1. Corrected MCCS Iβ DNA and deduced amino acid sequences that include the same corrections that appear in MCCSlα SEQ ID NOs: 23 and 24 are set out in SEQ ID NOs: 25 and 26. The SEQ ID NO: 25 clone represents a cDNA encoding a full length MCCS 1/3 kinase. Further sequences for MCCS1/3 including corrections of errors identified in resequencing the MCCSlα clone are presented in SEQ ID NOs: 32 and 33. The MCCSl products can be divided into three regions based on similarity to other PIK-related kinases: an amino terminal domain (MCCS let amino acids 1 to 1081 of SEQ ID NO: 31 and MCCS 1/3 amino acids 1 to 1150 of SEQ ID NO: 33), a region with similarity to rad3+ (MCCS let amino acids 1082 to 2082 of SEQ ID NO: 31 and MCSS 1/3 amino acids 1151 to 2151 of SEQ ID NO: 33) and a PIK domain (MCCSlα amino acids 2083 to 2410 of SEQ ID NO: 31 and MCCS1/3 amino acids 2152 to 2480 of SEQ ID NO: 33) including a kinase domain. The amino terminal region and rad3+ region are regulatory domains that modulate the kinase activity of the enzyme and are involved in interactions with associated proteins. Results of comparisons of the nucleotide and amino acid sequence of MCCS let and MCCSl ,3 to the sequences of other PIK-related and non-PIK-related kinases are shown in Table 1. Specifically, the 3' end of MCCS let (nucleotides 6579 to 7562 of SEQ ID NO: 30 encoding the kinase domain), the 3' end of MCCS 1/3 (nucleotides 1627 to 2379 of SEQ ID NO: 32 encoding the kinase domain), the rad3+ domain of MCCS let (nucleotides 3576 to 6578 of SEQ ID NO: 30), and the rad3+ domain of MCCS 1/3 (clone 517 nucleotides 1 to 1626 of SEQ ID NO: 3) were compared to the analogous region in human ATM [Savitsky et al , supra], human DNA-PK [Huntley et al , Cell, 82: 849-856 (1995)], human FRAP [Brown et al , supra], human pi 10 [Hu et al . Mol. Cell. Biol , 13(12): 7677-7688 (1993)], S. cerevisiae MECl [Weinert et al , Genes Dev. , 8(6): 652-665 (1994), S. pombe rad3+ [Seaton et al , supra and Hari et al. , Cell, 82: 815-821 (1995)] and an cAMP- dependent protein kinase (PKA) [Beebe et al , Mol. Endocήnol , 4(3): 465-475 (1990)]. Percent identity of nucleotides is shown in the top line, percent identity of amino acids is shown in the middle line, and percent similarity of amino acids (i.e. , including identical amino acids and conservative variations in amino acids) is shown in the bottom line for each kinase in Table 1. Conservative variation as used herein denotes biologically similar residues. Examples of conservative variations include the substitution of one hydrophobic residue such as isoleucine, valine, leucine or methionine for another, or the substitution of one polar residue for another, such as the substitution of arginine for lysine, glutamic for aspartic acids, or glutamine for asparagine, and the like. In the Table, "ND" indicates a value was not determined either because the nucleotide sequence encoding the kinase (i.e. , rad3+) was not publically available or because the kinase (i.e. , FRAP, pi 10/3, or PKA) lacks the particular domain being compared. Table Protein Kinase MCCS let/MCCS 1/3 Kinase Domain S. pombe rad3+ ND 56 72 S. cerevisiae 51 MECl 45 63 Human ATM 50 38 60 Human DNA-PK 43 29 53 Human FRAP 45 37 61 Human pi 103 45 24 54 Human PKA 39 16 39 Example 2 The MCCSl gene was mapped to chromosome 3 by a PCR-based assay. Human/rodent somatic cell hybrids containing various human chromosome panels available from the NIGMS Human Genetic Mutant Cell Repository [Drwinga et al , Genomics, 16: 31 1-314 (1993)] were used as templates. Two oligonucleotide primers oDH23 (SEQ ID NO: 12) and oDH26 5' TGGTTTCTGAGAACATTCCCTGA 3' (SEQ ID NO: 19) based on the MCCS let cDNA sequence were utilized to amplify a portion of the gene. The primers generate 237 bp PCR products. PCR conditions consisted of 50 ng genomic DNA, 0.5 μg of each primer, 200 μM dNTPs, 1.5mM MgCl 2 , IX PCR buffer (Perkin Elmer-Cetus), and 1 unit of Amplitaq polymerase (Perkin-Elmer Cetus) in a 25 μl reaction volume. The samples were denatured for 4 minutes and then cycled 35 times with denaturing, annealing, and extension times of 45 seconds, 30 seconds, and 45 seconds, respectively, in a Model 480 Cetus Thermocycler. Five μl of the resulting PCR product was electrophoresed on a 3 % agarose gel and stained with ethidium bromide. DNA corresponding to the human/rodent chromosome 3 hybrid yielded a positive amplification product. In a second set of amplification reactions, the same oligonucleotide primers were used to sublocalize the MCCS l gene to a specific region on chromosome 3. The templates for these amplifications consisted of DNA samples from patients with chromosome 3 truncations [Leach et al. , Genomics, 24: 549-556 (1994)]. Amplifications were performed as described in the foregoing paragraph. The pattern of positive amplification products narrowed the localization to the interval between q21 and q25.1. Example 3 Polynucleotides encoding carboxyl terminal portions of the PIK-related kinase MCCS 1/3 were expressed by recombinant techniques in E. coli. Two E. coli expression plasmids were constructed that expressed either the COOH-terminal 423 or 571 amino acid residues of the kinase in the Pinpoint fusion protein expression/purification system (Promega, Madison, Wisconsin). Briefly, DNA sequences encoding the COOH-terminal portion of the kinase (nucleotides 1339 to 2630 or nucleotides 898 to 2630 of SEQ ID NO: 3) were fused in frame to the COOH-terminus of a 13 kD peptide derived from the transcarboxylase complex from propionibacterium shermanii. This region undergoes biotination in E. coli, and thus provides a means for monitoring expression and purification of the fusion proteins. Expression was driven from the tac promoter in pinpoint Xa3. Fusion protein expression was induced with O. lmM IPTG and confirmed using streptavidin alkaline phosphatase in a pseudo-Western format as described by the manufacturer. Example 4 Recombinant versions of MCCSl may also expressed in yeast or in SF9 insect cells using a baculovirus expression system. The FRAP kinase has been expressed, purified and is enzymatically active after expression in the baculovirus system [Brown et al. , supra] . The coding region of MCCSl is fused at the amino terminus to a heterologous peptide sequence, such as the FLAG tag MDYKDDDDK (SEQ ID NO: 20) or a six-histidine tag, and reconstructed into the appropriate vectors. Once expressed in insect cells, a monoclonal antibody that recognizes the FLAG tag (Eastman Kodak, Rochester, New York) is used to purify large quantities of the FLAG-PIK-related kinase fusion protein. Infected insect cells are incubated for 48 hours and lysed in lysis buffer (25mM 2-glycerolphosphate, 50mM sodium phosphate pH 7.2, 0.5 % Triton-X 100, 2mM EDTA, 2mM EGTA, 25 mM sodium fluoride, lOOμM sodium vanadate, ImM PMSF, lμg/ l leupeptin, lμg/ l pepstatin, ImM benzamidine, and 2mM DTT). Expressed FLAG fusion proteins are purified over a column containing anti-FLAG antibody M2 affinity resin (Eastman Kodak). The column is washed with 20 column volumes of lysis buffer, then 5 column volumes of 0.5M lithium chloride, 50mM Tris pH 7.6, I M DTT, and then eluted either with 0. IM glycine pH 3.0 followed by immediate neutralization or by competitive elution with the FLAG peptide. For six-histidine tagged proteins, Ni-NTA agarose (Qiagen) is used for protein purification. Shortly after the filing of parent application U.S.S.N. 08/558,666, a gene identified as ATR was described by Antony M. Carr and co-workers (personal communications). ATR appears to encode the same or a closely related protein to MCCS 1 based on a comparison of amino acid sequences between ATR and MCCS 1. The DNA and deduced amino acid sequences of ATR are presented in SEQ ID NOs: 28 and 29, respectively. The sequence differences between ATR and MCCS1 / 3 are as follows. ATR includes an additional 98 amino acid residues at the N-terminus. At nucleotide position 1284 (SEQ ID NO: 32) there is a conservative base change from "A" in MCCS1 / 3 to "T" in ATR and at nucleotide position 4176, there is an additional conservative base change from "C" in MCCS1/3 to "T" in ATR. The FLAG tag was fused at the amino-terminus of a truncated ATR molecule which lacked the first sixty-six ATR amino acids. The FLAG tag was a d d ed b y P C R a s fo l l o w s . Th e o l i g o s FLA G - A T R (5'-CGGGATCCGCCATGGACTACAAGGACGATGACAAGATGTTGCTTGATTTC-3 ). And HFB24 (5'CTTAAGCCGCATGAGCACACCGTC-3') were used in the following PCR reaction: lOOng of pcDNAATR (obtained from Antony M. Carr) as template; IX PCR buffer (Perkin-Elmer Cetus); 1.5 mM MgCl 2 , 200μM each of dATP, dGTP, dCTP, and TTP, 10 ng/μl of each primer; 1U AmpliTaq (Perkin- Elmer Cetus). The reaction was denatured at 94 °C for 4 minutes followed by 30 cycles of 94°C for 30 seconds, 60°C for 30 seconds and 72°C for 30 seconds. The resulting approximately 800 bp PCR product was digested with BamHI and Nhel and was ligated to the lOkb fragment of the mammalian ATR expression plasmid, pcDNAATR digested with BamHI and BstXI along with the remainder of the ATR coding sequences contained on a 2.5 kb BstXI to Nhel fragment. Sequence analysis confirmed the addition of the FLAG tag. The insert contained within this plasmid was then used to construct a baculovirus expression plasmid that would express the FLAG tagged ATR truncate. The 5' end of ATR contained on a BamHI to BstXI fragment and the 3' end of ATR contained on a BstXI to Sail fragment derived from pBTM ATR were ligated to the baculovirus expression vector, pFB (Gibco/BRL) that had been digested with BamHI and Sail. This plasmid was designated pFMBCCS/3FLAG. The full coding region of ATR was fused at the amino terminus to the six h i stidine tag by PCR. Oligonucleotides MC CS όhi s (5'-CGGGATCCAGCATGCATCACCATCACCATCACATGGGGGAACATGGGC-3') and FφlR ("5'-CATGACCACTGGCCATTCCACACG-3') were used in a PCR reaction to add the six histidine tag to sequences encoding the amino-terminus of ATR. PCR conditions were as follows: 100 ng of PstA 12ATR (obtained from Antony M. Carr) was used as template; IX PCR buffer (Perkin-Elmer Cetus); 1.5 mM MgCl 2 , 200μM each of dATP, dGTP, dCTP, and TTP, 10 ng/μl of each primer; 1U AmpliTaq (Perkine-Elmer Cetus). The reaction was denatured at 94 °C for 4 minutes followed by 25 cycles of 94°C for 30 seconds, 60°C for 30 seconds and 72 °C for 30 seconds. The approximately 800 bp PCR product was digested with BamHI and MscI and ligated to two other fragments: a lOkb fragment from pcDNAATR digested with BamHI and BstXI and an approximately 3 kb MscI to BstXI fragment containing the remainder of the ATR coding sequence. The addition of the six histidine tag was verified by sequence analysis. The resulting plasmid encoding a six-histidine tagged full length ATR molecule was designated pcDNAόhis ATR. To construct a baculovirus expression plasmid that expressed the entire coding sequence of ATR, the 1.2 kb BamHI to Agel fragment from pFBMCCSβFLAG was ligated to the BamHI to Agel fragment from ρcDNA6his ATR. The resulting plasmid, designated pFB/HisX6MCCS-l plasmid was transformed into the E.coli strain, DH5ct (Gibco/BRL) for screening of recombinants. This plasmid was purified by using the Promega "Wizard" mini-prep kit, then transformed into E. coli ctSF9 cells (Invitrogen) using the Cellfectin protocol described by Gibco/BRL. Forty eight hours after transfection, the SF9 cell pellet and baculovirus produced by the transfected cells were harvested. The virus was stored at 4°C in Grace's Complete media containing 10% FBS, Pennicillin-Streptomycin, and Gentamicin. This viral prep was used to make a high liter (P2) virus stock. The P2 virus stock was used to infect a 50 ml culture of SF9 cells. The cells were collected 48 hours after infection and centrifuged at low speed to pellet the cells without lysis. The cell pellet was stored at -20°C for 24 hours before lysis. The cells were lysed in 5 ml of lysis buffer (50 mM Tris, pH 8.0; 500 mM NaCl; 1 % NP40; 100 μm PMSF). Expression of ATR was confirmed by immunoblot using the polyclonal antibody anti-AgDH2 as a probe. The FBHisXό ATR baculovirus produced an approximately 300 kDa protein that was immunoreactive with anti-AgDH2 antibodies and comigrated with a protein in a mouse testes cell extract. The P2 virus stock was also used to infect a 2 liter culture of SF9 cells. The cells were collected 48 hours after infection, centrifuged at low speed to pellet the cells without lysis and stored at -20°C. A cell pellet from 150 is of this culture was lysed in 7.5 ml of lysis buffer (50mM NaPO, pH7.2; 0.5 % NP-40; lOmM imidazole, 25mM NaF, 100μM Na 3 VO 4 ; 0.5mM AEBSF; 1 μg/ml leupeptin; lμg/ml pepstatin A) and incubated on ice for 15 minutes. The lysate was then centrifuged for 30 minutes at 10,000 x g. The supernatant was removed and any DNA in the lysate resulting from broken nuclei was sheared by aspirating through an 20 gauge needle. Particulate matter was then removed by filtering through a 0.8 micron filter followed by a 0.2 micron filter. This cleared lysate was adjusted to contain 5 mM /3-mercaptoethanol and 0.4 M NaCl . A 1 ml Ni-NTA-agarose column (Qiagen) was equilibrated in Buffer A (0.4 M NaCl ; 5 M /3-mercaptoethanol; 0.1 % Triton X- 100; 50 mM NaPO 4 10 mM imidazole; 25 mM NaF, 100 μM Na 3 VO 4 ; 0.5 M AEBSF; 1 μg/ml leupeptin; 1 μg/ml pepstatin A) prior to loading the cleared lysate. The sample was loaded at a flow rate of 0.25 ml/minute, washed 5 ml of Buffer A and then eluted in 10 ml of a gradient of 50 to 500 mM imidazole in Buffer A. One half ml fractions were collected and was assayed for kinase activity as follows. Five μl of each fraction was incubated in kinase buffer, 10 μCi 32 PγATP, 10 μM ATP, and 5 μg of substrate PHAS-1 (Stratagene) and incubated at 37 °C for 20 minutes. The reaction was then spotted onto phosphocellulose spin columns and centrifuged at 2500x g, washed twice with 0.5 ml of 75 mM phosphoric acid and once with 0.5 ml absolute ethanol. The phosphocellulose disks were then transferred to scintillation vials and the counts per minutes incoφorated into the PHAS-1 proteins were recorded. Fractions 4 through 9 were found to contain activity toward PHAS-1 and immunoblot analysis confirmed that ATR was also present in the same fractions. MCCS1 encoding plasmid DNA was transformed into an esrl-1 diploid yeast strain (Mata leu2-l his4-4 canl ura3 cyh2 ade6ade2 esrl-1/MATa Ieu2-27his4 trpl met2 ade2 esrl-1), and cells were grown to mid-log phase in either galactose or glucose containing medium. Cells were pelleted, washed and all steps performed at 4°C. Cell pastes were resuspended in buffer (20 mM Tris at pH 8.0, 300 mM NaCl, 10% glycerol, 0.1 mM PMSF, 0.25 mg/ml pepstatin, leupeptin, and aprotinin) and lysed in a French Press or using glass beads. Lysis was verified by microscopy following a low-speed (10K) spin and a high-speed spin (100K), and the supernatant was loaded onto a 1.5 ml Ni-NTA agarose (Qiagen, Inc., Chatsworth, CA) column prewashed in lx buffer. The column was washed with six column volumes of buffer. The column was eluted stepwise with 8 ml of 10 mM, 50 mM, 100 mM, and 250 mM imidazole in buffer. Fractions were collected and Western analysis was performed using 15 μl of each elution peak. Kinase activity was measured as described above. Example 5 Polyclonal and monoclonal antibodies specific for MCCSl were generated by standard techniques in the art. Two different bacterial expression plasmids, pGEX 1 -MEC and pGEX3- MEC, were constructed for the recombinant production of portions of the MCCSl polypeptide as fusions to the COOH-terminus of glutathione S-transferase (GST). Both plasmids were used for the generation of antigens AgDH-2 and AgDH-3, from pGEXl-MEC and pGEX3-MEC respectively for use in a standard immunization protocol. pGEXl-MEC contains an EcoRI fragment encoding amino acid residues 566 to 870 of SEQ ID NO: 4 fused to GST in the pGEXl vector (Pharmacia Biotech, Milwaukee, Wisconsin); pGEX3-MEC contains an Eco Rl fragment encoding amino acid residues 118 to 567 of SEQ ID NO: 4 fused to GST in the pGEX3 vector (Pharmacia Biotech). Induction of the pGEX tac promoter with 0. ImM IPTG led to high level expression of each fusion protein in an insoluble form (inclusion bodies). Following lysis of induced cultures with a French pressure cell, AgDH-2 and AgDH- 3 extracts were centrifuged through a 35 % sucrose solution containing 0.1M NaCl, 0.01M Tris pH7.5, and O.OOIM EDTA (STE). Pellets were then washed twice and resuspended in STE. For the generation of polyclonal antisera in rabbits, AgDH-2 and AgDH-3 were further purified using preparative SDS polyacrylamide gel electrophoresis and electroelution of each antigen from gel slices. Primary immunization of female New Zealand White rabbits was with 200 μg of each antigen mixed with complete Freund's adjuvant injected at multiple sites subcutaneously. Subsequent immunizations were with 100 μg antigen mixed with incomplete Freund's adjuvant at approximately 21 day intervals, and test bleeds were taken after immunizations 3, 4 and 5. Western blot analysis of extracts of human testis tissue demonstrates antibody reactivity against an approximately 270 kD protein in immune but not preimmune antisera. In addition, the immune sera showed reactivity against the MCCS l pinpoint fusion proteins described in Example 3, providing evidence of the generation of MCCSl -specific antibodies. The MCCSl -specific antibodies were purified as follows. Inclusion body preparations of AgDH-2 and AgDH-3 were coupled to cyanogen bromide (CNBr)-activated Sepharose (Pharmacia, Alameda, CA). Two mg of antigen were solubilized in 1 % SDS (4.5 ml final volume) and dialyzed overnight against Coupling Buffer (0. IM NaHCO 3 /0.1 % SDS). 0.5 ml of 5M NaCl were added to each antigen preparation prior to incubation with the CNBr Sepharose. 0.4 gm of freeze-dried CNBr Sepharose (per antigen) were resuspended in 1 mM HCl and washed in a scintered glass funnel with 250 ml 1 mM HCl added in several aliquots over 15 minutes. The HCl-washed CNBr Sepharose was then removed to a 15 ml snap cap tube and washed twice with 5 ml of Coupling Buffer. Dialyzed antigen preps were added to the washed Sepharose and then incubated at room temperature for 1.5 hours on a slowly rotating wheel. The Sepharose was washed once with 5 ml of Coupling Buffer, once with 10 ml of 0.1M Tris pH8.0, and then incubated in 10 ml 0.1M Tris 8.0 for 2 hours at room temperature to block any remaining reactive groups on the resin. Coupling efficiency was 60-80% as judged by SDS-PAGE analysis. The antigen columns were then washed with 15 ml of 6M Guanidine HCl (to remove uncoupled antigen), 25 ml of Buffer A (50mM Tris pH 7.4), 15 ml of Buffer B (4.5M MgCl 2 /lmg/ml BSA/50mM Tris 7.4), and then 50 ml of Buffer A. Thirty ml of rabbit serum from immunized animals (rabbit 4747 immunized with AgDH-3 and rabbit 4779 immunized with AgDH-2) were passed over the appropriate antigen column over the course of 3 hours. The columns were then washed with 20 ml of Buffer A, 40 ml of IM Guanidine HCl, and then equilibrated with an additional 20 ml of Buffer A. Anti-AgDH-3 or Anti-AgDH-2 antibodies were then eluted off the antigen columns with 10 ml of Buffer B. One ml fractions were collected, IgG- containing fractions were pooled and dialyzed against 1 L of phosphate buffered saline (PBS) for 3 hours, and then overnight against 1 L of PBS containing 35 % glycerol. Antipeptide antibodies were generated against the human ATM protein by coupling a 15-amino-acid peptide (residues 1359-1373) to Keyhole Limpet Hemocyanin-using EDC as described by the manufacturer (Pierce), followed by injection of the coupled immunogen into rabbits. The antibodies were first precipitated from the serum (#6076) with an equal volume of saturated ammonium chloride followed by resuspension and dialysis against PBS. Affinity purification was carried out using a peptide column prepared by coupling the antigenic peptide to CNBr-activated Sepharose (Pharmacia) as described by the manufacturer. The antibodies were then bound to the peptide column and washed with 2 m KC1-PBS. Elution was carried out with 20 ml S m Nal (in 1 mM sodium thiosulfate), which was dialyzed immediately against PBS. To generate monoclonal antibodies, female Balb/c mice were immunized with 50 ug AgDH-2 or AgDH-3. Additional mice were immunized with 25 to 50 ug AgDH-2 or AgDH-3 that had been combined with an equal molar ratio of mAb 61F3B, a monoclonal antibody with specific reactivity to GST. A third group of mice were immunized with SDS polyacrylamide gel slices containing AgDH-2 or AgDH-3. The immunogen for each group of mice was prepared in complete Freund's adjuvant, with subsequent boosts (25 ug antigen in incomplete Freund's) at about 21 day intervals. Cell lines producing monoclonal antibodies were isolated as follows. Briefly a single cell suspension was formed by grinding immunized mouse spleen in serum free RPMI 1640, supplemented with 2mM L- glutamine, ImM sodium pyruvate, 100 units/ml penicillin, and 100 μg/ml streptomycin (RPMI) (Gibco, Canada). The cell suspension was filtered through sterile 70-mesh Nitex cell strainer (Becton Dickinson, Parsippany, New Jersey), and washed twice by centrifuging at 200 g for 5 minutes and resuspending the pellet in 20 ml serum free RPMI. Thymocytes taken from three naive Balb/c mice were prepared in this manner. NS-1 myeloma cells kept in log phase in RPMI with 11 % fetal bovine serum (FBS) (Hyclone Laboratories, Inc. , Logan, Utah) for three days prior to fusion, were centrifuged at 200 g for 5 minutes, and the pellet was washed twice as described in the foregoing paragraph. After washing, each cell suspension was brought to a final volume of 10 ml in serum free RPMI, and 10 μl was diluted 10: 100. Twenty μl of each dilution was removed, mixed with 20 μl 0.4% trypan blue stain in 0.85 % saline (Gibco), loaded onto a hemacytometer and counted. Two x 10 8 spleen cells were combined with 4 x 10 7 NS-1 cells, centrifuged, and the supernatant was aspirated. The cell pellet was dislodged by tapping the tube and 2 ml of 37° C PEG 1500 (50% in 75 mM Hepes, pH 8.0) (Boehringer Mannheim) was added with stirring over the course of 1 minute, followed by adding 14 ml of serum free RPMI over 7 minutes. An additional 16 ml RPMI was added and the cells were centrifuged at 200 g for 10 minutes. After discarding the supernatant, the pellet was resuspended in 200 ml RPMI containing 15 % FBS, 100 μM sodium hypoxanthine, 0.4μM aminopterin, 16μM thymidine (HAT) (Gibco), 25 units/ml IL-6 (Mallinckrodt, Folcrost, Pennsylvania), and 1.5 x IO 6 thymocytes/ml. The suspension was dispensed into ten 96-well flat bottom tissue culture plates at 200 μl/well. Cells in plates were fed 3 to 4 times between fusing and screening by aspirating approximately half the medium from each well with an 18 G needle and replenishing plating medium described above except containing 10 units/ml IL-6 and lacking thymocytes. Fusions were screened when cell growth reached 60-80% confluency (day 7 to 9) by ELISA on AgDH2 versus AgDH3. Immunlon 4 plates (Dynatech, Cambridge, MA) were coated at 4 ° C overnight with 100 ng/well protein in 30mM carbonate buffer, pH 9.6. Plates were blocked with 100 μg/well 0.5 % fish skin gelatin in PBS for one hour at 37 ° C, washed 3 times with PBS, 0.05 % Tween 20 (PBST) and 50 μl culture supernatant is added. After incubation at 37° C for 30 minutes, and washing as described above, 50 μl of horseradish peroxidase conjugated goat anti-mouse IgG(fc) (Jackson ImmunoResearch, West Grove, PA) diluted 1 : 10,000 in PBST was added. Plates were incubated as above, washed 4 times with PBST and 100 μl substrate consisting of 100 μg/ml of tetramethylbenzidine and 0.15 μl/ml H 2 O 2 in lOO M sodium acetate, pH 5.5, was added. The color reaction was stopped in 5-10 minutes with the addition of 50 μl of 15 % H 2 SO 4 . A 490 was read on a plate reader. Fifty three pools of hybridomas that were positive in an ELISA were screened for the ability to immunoblot or immunoprecipitate MCCS from a mouse testes cell lysate. Immunoblot analysis using the mouse testes extract is described in Example 6. Immunoprecipitations was performed as follows. A six percent SDS polyacrylamide gel was run and transferred to Immobilon-PVDF in 192 mM glycine, 25 mM Tris base, 0.1 % SDS, 20% methanol, then blocked for 1 hour in 5 % powdered nonfat milk, 20 mM Tris ph 7.5, 100 mM NaCl 0.1 % Tween 20, and cut into the appropriate number of strips. The primary antibody (well supernatant) was diluted in the above block solution and incubated for one hour at room temperature, washed four times in block minus milk, incubated in goat anti-mouse IgG (H+L) HRP (BioRad #170-6516), washed again in block solution minus milk, transfered to NEN Renaissance ECL reagent and developed for 5 minutes. Immunoprecipitation was performed as follows. Fifty μl of hybridoma supernatant was incubated for one hour on ice with 300 μg of testes cell lysate prepared as described in Example 6. Thirty μl of a 50% slurry of protein A agarose (Pierce, Rockford, IL), prebound to a rabbit anti-mouse bridging antibody (5 μg/reaction) (Pierce) was added and incubated at 4°C with rocking. The immune complexes were washed three times in lysis buffer and the antigen/antibody complex eluted by boiling in SDS sample buffer (2% SDS, 20 mM Tris pH 6.8, 20% glycerol, 0.001 % bromphenol blue). The resulting supernatant was separated on a 6% SDS polyacrylamide gel and transferred to Immobilon-PVDF (Millipore) and an immunoblot was performed using affinity purified rabbit anti-Ag DH2 polyclonal antiserum. Four hybridomas were cloned and characterized in immunoblots, immunoprecipitations and in immunoprecipitation/kinase assays as described in Example 6. The four hybridoma cell lines were designated 224B, 224C (ATCC HB 12233), 224F (ATCC HB 12234) and 224G. All four monoclonal antibodies recognized MCCS l by immunoblot and immunoprecipitation. Example 6 MCCSl associated protein kinase activity was immunoprecipitated using the MCCSl -specific polyclonal antibodies described in Example 5. Extracts were made from fresh testes tissue isolated from Balb/c mice. Minced testes were homogenized on ice with 10-15 strokes of a tight fitting dounce homogenizer in Lysis Buffer (50 mM NaPO4, pH 7.2; 0.5 % TritonX-100; 2 mM EDTA; 2 mM EGTA; 25 mM NaF; 25 mM 2-glycerophosphate; 1 mM phenylmethylsulfonyl fluoride [PMSF]; 1 μg/ml leupeptin; 1 μg/ml pepstatin A; 2 mM DTT) and incubated on ice for 30 minutes. The lysate was centrifuged at 13,000xg φm for 10 minutes at 4° C in a TL-100 table-top ultracentrifuge (Beck an) to remove unbroken cells and other insoluble material. Aliquots of cell lysate were snap frozen in liquid N 2 and stored at -70 ° C. Five hundred ug of testes extract was incubated with either 5 ug of affinity purified anti-AgDH-2 polyclonal antibody or 5 ug purified rabbit IgG (Zymed, So. San Francisco, CA) in 1 ml of Lysis buffer for one hour on ice in microcentrifuge tubes. Thirty μl of protein A sepharose beads (Repligen, Cambridge, MA) (washed in Lysis buffer) were added to the extracts, and then incubated for an additional 30 minutes at 4 ° C on a rocking platform. The immune complex/Protein A sepharose beads were washed four times with 1 ml of Lysis buffer, one time with 1 ml Kinase Buffer (25 mM Hepes pH 7.7; 50 mM KCl; 10 mM MgCl 2 ; 0.1 % NP-40; 2 % glycerol; 1 mM DTT), and then incubated in 20 ul Kinase Buffer with 10 μCi ATP [50 Ci/mmol]) for 20 minutes at 37° C. The kinase reactions were stopped with 20 μl 2X SDS sample buffer and heated to 100° C prior to separation on 6% polyacrylamide gels. Gels were fixed in 20% methanol/7% Acetic acid, and then dried onto Whatman 3MM paper prior to autoradiography. While little or no phosphorylation was evident in control immunoprecipitations, immunoprecipitations using anti-AgDH-2 antibody contained two major phosphorylated bands at approximately 300 kD and approximately 180 kD. In addition, there were several minor phosphorylation products, including one which comigrated with the MCCSl protein itself as demonstrated by Western blot analysis (see Example 8 for Western blot description.) Phosphoaminoacid analysis of the approximately 300 kD protein identified the presence of phosphoserine residues. Addition of 5 ug of AgDH-2 (but not AgDH-3) dramatically reduced or eliminated the MCCSl -associated kinase activity found in the immunoprecipitates. Example 7 The expression pattern of MCCSl in various human tissues was examined by Northern blot hybridization. Nylon membranes containing 2 μg of size-fractionated poly A + RNA from a variety of human tissue sources were obtained from Clontech Laboratories, Inc. , and the hybridization protocol supplied by the manufacturer was followed precisely, except that the final wash was performed at 55 ° C, rather than 50° C, to minimize the possibility of cross-hybridization to related sequences. The 32 P- labelled DNA hybridization probe used was generated by PCR. A DNA encoding the COOH- terminal 30% of MCCS lα was used as a template to amplify a 1.3 kb fragment in the presence of 32 P-dCTP using primers 279-3 5 'TGGATGATGACAGCTGTGTC 3 ' (SEQ ID NO: 21) and 279-6 5'TGTAGTCGCTGCTCAATGTC3' (SEQ ID NO: 22). Results of the Northern blots show that MCCSl is expressed as an approximately 9 kb mRNA in a wide variety of human tissues. Testis tissue contains the highest level of MCCSl mRNA, though the transcript is also expressed in small intestine, ovary, prostate, thymus, spleen, heart, peripheral blood lymphocytes, colon, brain, placenta, skeletal muscle, kidney and pancreas. Expression of MCCSl mRNA in human cancer cell lines was also examined using a human cancer cell line RNA blot obtained from Clonetech. The RNA blot contained RNA from the cell lines HL-60 (promyelocytic leukemia), HeLa (cervical carcinoma), K-562 (chronic myelogenous leukemia), MOLT-4 (lymphoblastic leukemia), Raji (Burkitt's lymphoma), SW480 (colorectal adenocarcinoma), A549 (lung carcinoma), and G361 (melanoma). Northern blot analysis was performed as directed by the manufacturer with hybridization being carried out at 65 °C using a 2.0kb Kpnl-Sall fragment of the MCCSl partial clone HFB2. Expression was observed in the HL-60, HeLa, K-562, Raji, SW480, and G361 cell lines with the highest level of expression occurring in the G361 cell line. Detectable but low levels of expression were observed in the MOLT-4 and A549 cell lines. Example 8 The expression of MCCSl mRNA and protein in normal and irradiated mouse testes and in mouse embryos was examined by in situ hybridization, immunostaining and/or immunoblotting. In situ Hybridization Normal and irradiated mouse testes were harvested from male Balb/c mice. The tissues were sectioned at 6μm thickness, picked up on Superfrost Plus ® (VWR Scientific) slides and allowed to air-dry at room temperature overnight. Sections were stored at -70° C if not immediately used. The tissue sections were fixed in 4% paraformaldehyde (Sigma) in PBS for 20 minutes at 4° C, dehydrated (70% , 95 % , 100% ethanol) for 1 minute at 4° C in each grade, then allowed to air dry for 30 minutes at room temperature. The slides were acetylated in a solution of 0.25 % (v/v) acetic anhydride (Sigma)/0. IM triethanolamine pH 8.0 for 10 minutes at room temperature with stirring, rinsed in 0.2X SSC for 10 minutes at room temperature with stirring, and dehydrated and air dried as described above. The tissues were hybridized in situ with digoxigenin-labeled single- stranded mRNA generated from murine MCCSl DNA by in vitro RNA transcription incoφorating digoxigen-UTP (Boehringer Mannheim). The labeled riboprobes (see sequence in SEQ ID NO: 27) (lμg/section) and diethylpyrocarbonate (depc) -treated water were added to hybridization buffer with a final concentration of 50% formamide, 0.3 M NaCl, 20 mM Tris pH 7.5, 10% dextran sulfate, IX Denhardt's solution, 100 mM dithiothreitol (DTT) and 5 mM EDTA, and 20 μl of the solution was applied to each section and covered with a sterile, RNase-free 22 x 22 cover slip. The mRNA in both the section and the probe solution was denatured by heating the slides to 85 ° C for 10 minutes in an oven. Hybridization was carried out overnight (12-16 hours) at 50° C. After hybridization, sections were washed for 1 hour at room temperature in 4X SSC/ 10 mM DTT, then for 30 minutes at 50 ° C in 50% formamide/2X SSC/ 10 mM DTT, 30 minutes at 37 ° C in a solution of 500 mM NaCl, 10 mM Tris-HCl , 1 mM EDTA, pH 7.5 (NTE buffer), 30 minutes at 37° C in a bath of 10 μg/mL RNase A (Boehringer Mannheim) in NTE buffer, 15 minutes at 37 ° C in NTE buffer, 15 minutes at room temperature in 2X SSC, 15 minutes at room temperature in 0.1X SSC, and 2 minutes at room temperature in 100 M Tris- HCl , 150 mM NaCl, pH 7.5 (Buffer 1). To detect the labeled riboprobes, the sections were blocked for 30 minutes at room temperature in a solution of 5 % normal sheep serum (Harlan Bioproducts for Science, Indianapolis, IN) and 0.3 % Triton X- 100 (Sigma) in Buffer 1 with gentle stirring, after which 150 μl/section of sheep ctDigoxigenin-gold conjugate (Goldmark Biologicals, Philipburg, Pa) was applied to the tissues and incubated for 2 hours at room temperature. The slides were then washed three times for 5 minutes in Buffer 1 , five times for 3 minutes in sterile deionized water, the excess liquid blotted off the slide and 2 drops each of silver enhancing and initiating solution (Goldmark Biologicals) applied to each section. The chemical reaction was allowed to proceed for 23 minutes at room temperature, then the sections were rinsed thoroughly in sterile deionized water, counterstained in Nuclear Fast Red (Vector), rinsed again in sterile deionized water, air dried overnight at room temperature and mounted with Cytoseal 60 (VWR). In both normal and irradiated mouse testes signal was observed in the cytoplasm of spermatogonia and spermatocytes. The expression level in irradiated testis was not increased over that seen in normal testis. Immunostaining Testis tissue from normal male Balb/c mice was sectioned at 6 μ thickness, picked up on Superfrost Plus ® (VWR Scientific) slides and allowed to air- dry at room temperature overnight. Sections were stored at -70° C if not immediately used. The sections were fixed in cold (4° C) acetone for 10 minutes at room temperature; once the slides were removed from the acetone the reagent was allowed to evaporate from the sections. Each tissue section was blocked with 150 μl of a solution of 30% normal rat serum (Harlan Bioproducts), 5 % normal goat serum (Vector Laboratories) and 1 % bovine serum albumin (BSA) (Sigma) in IX TBS for 30 minutes at room temperature. After blocking, the solution was gently blotted from the sections and anti-AgDH-3 and anti-AgDH-2 polyclonal antibodies and preimmune sera from the same rabbits were diluted 1 :50 and 1 : 100 in the blocking solution and 100 μl applied to each tissue section and incubated for 30 minutes at 37 ° C. The antibody solution was blotted gently from the sections and unbound antibody removed from the sections by washing the slides 3 times for 5 minutes each in IX TBS. The excess TBS was blotted from the slide and 100 μl of the biotinylated goat anti-rabbit antibody contained in the Elite Rabbit IgG Vectastain ABC kit (Vector), prepared according to the product insert, were applied to each section and incubated for 15 minutes at 37° C. After incubation, the slides were washed 2 times in IX TBS for 5 minutes in each wash. Next, 100 μl of streptavidin-gold conjugate (Goldmark Biologicals) diluted 1 : 100 in a solution containing 5 % normal rat serum and 1 % BSA was applied to each section and incubated for 1 hour at room temperature. The slides were then washed 3 times in IX TBS for 5 minutes each wash, and 100 μl of 1 % glutaraldehyde (Sigma) in TBS buffer was applied to the slides for 5 minutes at room temperature. The slides were then washed 3 times for 5 minutes each in TBS, then 4 times in sterile deionized water for 3 minutes each. The excess liquid was blotted from each slide and 2 drops each of silver enhancing and initiating solution (Goldmark Biologicals) were applied to each section. The chemical reaction was allowed to proceed for 13 minutes at room temperature, then the sections were rinsed thoroughly in sterile deionized water, counterstained in Nuclear Fast Red (Vector), rinsed again in sterile deionized water, air dried overnight at room temperature and mounted with Cytoseal 60 (VWR). Signal was detected in the spermatogonia and primary spermatocytes with both of the polyclonal antibodies, but not with the preimmune sera from the same animals. Immunoblotting Freshly obtained mouse testicles were minced with razor blades in cold PBS, and a cell suspension was generated using a loose fitting dounce homogenizer. This cell suspension was then boiled with an equal volume of 2X SDS sample buffer. Fifty ug aliquots of each extract were separated on 6% polyacrylamide gels, transferred onto Immobilon membranes (Millipore, Bedford, MA) and analyzed for anti-MCCS 1 -reactivity using the affinity purified antibodies in Example 5, and HRP- conjugated goat anti-rabbit secondary antibody and the Renaissance Enhanced Chemiluminescence kit (Dupont/NEN, Boston, MA). Extracts prepared from fresh mouse testis contain a high molecular weight species (about 294 kD) that was recognized by both affinity-purified antiserum. No reactivity against this protein was seen with either of the preimmune sera. Importantly, the signal obtained from each affinity purified sera was specifically blocked after pre-incubation of the antibody with the corresponding immunogen. In summary, high levels of MCCSl mRNA and protein are detected in mouse testis in the spermatogonia and primary spermatocytes, cells that are in the early stages of meiosis. This suggests that MCCSl plays an important role in meiotic cell division. Meiosis is a specialized form of cell division that produces germ cells in higher eukaryotes. There are two major characteristics of meiosis that distinguish it from mitosis. Whereas mitotic cell division results in genetically identical cells containing two of each chromosome, meiotic cell division results in cells containing one of each chromosome. Early in meiosis, during the "reduction division" process, sister chromatids pair and undergo reciprocal recombination at some regions. During this process, these cells are exposed to DNA strand breaks. It is likely that the cellular response to the DNA strand breaks during meiosis is similar to the cellular response found in non-germ cells in response to IR-induced DNA damage. This inteφretation is further substantiated by studies that demonstrate the MECl is upregulated 10 to 20 fold during sporulation, indicating an important role for MCCSl during meiosis in addition to its role in DNA repair. Example 9 In order to identify the cells within the developing mouse testis that express MCCSl , Western blot analysis of MCCSl expression within populations of meiotic cells was performed. Extracts of purified pachytene spermatocytes, round spermatids, condensing sper atids, and epididymal sperm cells were examined for MCCSl expression as described above in Example 8. Pachytene spermatocytes, round, and condensing spermatids were prepared from decapsulated testes of adult mice by sequential dissociation with collagenase and trypsin-DNase 1. The cells were separated into discrete populations by sedimentation velocity at unit gravity in 2-4% BSA gradients in Enriched Krebs Ringer Bicarbonate Medium (EKRB). The pachytene spermatocyte and round spermatid populations were each at least 85 % pure, while the condensing spermatid population was about 40-50% pure (contaminated primarily with enucleated residual bodies and some round spermatids). Sperm were obtained from the cauda epididymides. Purified populations of spermatogenic cells were dissolved directly in SDS-sample buffer containing 40 mM DTT, heated to 100 ° C for 5 minutes, and the amount of protein in each sample determined by the Amido-Black procedure. The highest levels of MCCSl protein were found in pachytene spermatocytes, with the level dropping significantly in round spermatids. MCCSl protein levels were barely detectable lower in the condensing spermatid population, and this may reflect the presence of round spermatids in the preparation (see above). No MCCSl protein was detected in epididymal sperm. The Western analysis thus corroborates the immunocytochemical data, and suggests a role for MCCS 1 in meiotic cells. Example 10 Substrates of MCCSl and proteins that interact with MCCSl (for example, members of the cell cycle checkpoint pathway and proteins that localize MCCSl in cells) may be identified by various assays. A. Identification of Substrates Substrates of MCCS l may be identified by incoφorating test compounds in assays for kinase activity. MCCSl kinase is resuspended in 20 μl kinase buffer (25mM Hepes pH7.4, 25mM KCl, lOmM MgC12, ImM DTT, 2 % glycerol, 0.1 % NP40, 0.5mM ATP, 10 uCI gamma 32 P-ATP) and incubated for 30 minutes, either in the presence or absence of 4 μg test compound (e.g. , casein, histone HI , or appropriate substrate peptide). Reactions are separated on 12 % PAGE gels and dried onto Whatman paper prior to autoradiography. Moles of phosphate transferred by the kinase to the test compound are measured by autoradiography or scintillation counting. Transfer of phosphate indicates that the test compound is a substrate of the kinase. The protein PHAS-1 has been identified as an in vitro substrate of ATR (Example 4). PHAS-I is a heat and acid-stable protein that phosphorylated at several sites in vivo in response to insulin and growth factors. PHAS-1 binds to the mRNA cap binding factor, EIF-4E, and prevents translation of capped mRNAs. Phosphorylation of PHAS-1 at a specific serine residue results in dissociation of PHAS-1 form EIF-4E and thus releasing the inhibition of translation of capped mRNAs. This mechanism allows for a rapid synthesis of protein in response to a particular stimulus. PHAS-1 may be phosphorylated by several protein kinases in vivo including a protein kinase that is sensitive to rapamycin. Since the rapamycin- sensitive protein kinase, FRAP, is related to ATR, it would be reasonable to assume that there might be an overlap in substrate specificity between FRAP and ATR and that PHAS-1 is a substrate for both of these protein kinases in vitro. To test this hypothesis, ATR that was immunoprecipitated from a mouse testes cell extract or His- tagged ATR purified from baculovirus-infected SF9 cells (Example 4) was incubated with 10 μg PHAS-1 (Stratagene) in kinase buffer (25 mM Hepes pH 7.4, 25 mM KCl , 10 mM MgCl 2 , 1 mM DTT, 0.1 % NP-40), 10 μM ATP and 10 μCi 32 P ATP for 20 minutes at 37 C C. Since phosphorylated PHAS-1 was known to bind to phosphocellulose paper, the reaction was spotted onto phosphocellulose spin columns and centrifuged at 2500 x g, washed twice with 0.5 ml of 75 mM phosphoric acid and once with 0.5 ml absolute ethanol. The phosphocellulose disks were then transferred to scintillation vials and the counts per minutes incoφorated into the PHAS-1 proteins were recorded. ATR readily phosphorylated PHAS-1 whereas negative controls showed little or no PHAS-1 phosphorylation. To map which residue is phosphorylated, the following peptides representing PHAS-1 sequences containing serine and threonine residues were synthesized. Peptide PH-1 MSGGSSCQTPSRAIPATRR (SEQ ID NO: 36) Peptide PH-2 GDYSTTPGGTLFSTTPGGTRR (SEQ ID NO: 37) Peptide PH-3 ECRNSPVTKTRR (SEQ ID NO: 38) Peptide PH-4 GVTSPSSDEPRR (SEQ ID NO: 39) Peptide PH-5 MEASQSHLRR (SEQ ID NO: 40) Peptide PH-6 RRNSPEDKRAGG (SEQ ID NO: 41) Peptide PH-7 GEESQFEMDIRR (SEQ ID NO: 42) These peptides are tested in the same kinase reaction to determine which peptide(s) is (are) phosphorylated by ATR. The peptide(s) are then used as substrate for ATR or MCCSl in assays such as described in Example 11 to identify modulators. The same kinase reaction was also used to determine if proteins such as histone HI (Upstate Biotechnology, Inc., Waltham, NY) and myelin basic protein (Gibco BRL, Gaithersburg, MD) which are known to be substrates of other protein kinases are substrates of MCCSl and ATR. No phosphorylation of histone HI or myelin basic protein was observed under the conditions of the assay. Moreover, a peptide from p53 known to be a substrate of DNA-PK was also not phosphorylated in the assay. B. Identification of Interacting Proteins Interacting proteins may be identified by the following assays. A first assay contemplated by the invention is a two-hybrid screen. The two-hybrid system was developed in yeast [Chien et al. , Proc. Natl. Acad. Sci. USA, 88: 9578-9582 (1991)] and is based on functional in vivo reconstitution of a transcription factor which activates a reporter gene. Specifically, a polynucleotide encoding a protein that interacts with MCCS l is isolated by: transforming or transfecting appropriate host cells with a DNA construct comprising a reporter gene under the control of a promoter regulated by a transcription factor having a DNA binding domain and an activating domain; expressing in the host cells a first hybrid DNA sequence encoding a first fusion of part or all of MCCS 1 and either the DNA binding domain or the activating domain of the transcription factor; expressing in the host cells a library of second hybrid DNA sequences encoding second fusions of part or all of putative MCCSl binding proteins and the DNA binding domain or activating domain of the transcription factor which is not incoφorated in the first fusion; detecting binding of an MCCSl interacting protein to MCCSl in a particular host cell by detecting the production of reporter gene product in the host cell; and isolating second hybrid DNA sequences encoding the interacting protein from the particular host cell. Presently preferred for use in the assay are a lexA promoter to drive expression of the reporter gene, the lacZ reporter gene, a transcription factor comprising the lexA DNA binding domain and the GAL4 transactivation domain, and yeast host cells. Other assays for identifying proteins that interact with MCCSl may involve immobilizing MCCSl or a test protein, detectably labelling the nonimmobilized binding partner, incubating the binding partners together and determining the amount of label bound. Bound label indicates that the test protein interacts with MCCSl . Another type of assay for identifying MCCSl interacting proteins involves immobilizing MCCSl or a fragment thereof on a solid support coated (or impregnated with) a fluorescent agent, labelling a test protein with a compound capable of exciting the fluorescent agent, contacting the immobilized MCCSl with the labelled test protein, detecting light emission by the fluorescent agent, and identifying interacting proteins as test proteins which result in the emission of light by the florescent agent. Alternatively, the putative interacting protein may be immobilized and MCCSl may be labelled in the assay. Example 11 Modulators of MCCSl include MCCSl variants and other molecules. The modulators may affect MCCSl kinase activity, its localization in the cell, and/or its interaction with members of the cell cycle checkpoint pathway. Presently preferred regions of MCCSl which are targets for mutation or the development of selective modulators include the following four regions: the MCCS 1 et amino terminal effector domain (amino acids 1 to 1081 of SEQ ID NO: 31), the MCCS 1/3 amino terminal effector domain (amino acids 1 to 1150 of SEQ ID NO: 33), the MCCSlct rad3+ domain (amino acids 1082 to 2082 of SEQ ID NO: 31), the MCCS1/3 rad3+ domain (amino acids 1151 to 2151 of SEQ ID NO: 33), the MCCSlct PIK domain (amino acids 2083 to 2410 of SEQ ID NO: 31), and the MCCS1/3 PIK domain (amino acids 2152 to 2480 of SEQ ID NO: 33). MCCSl variants having mutations in the kinase domain may be useful as a radiosensitizing agents. Mutations specifically contemplated by the invention are, replacement of the MCCS let aspartic acid at amino acid 2241 , the asparagine at 2246, and the aspartic acid at 2260 of SEQ ID NO: 31 with alanine or methionine, and the corresponding mutations in MCCS 1/3. Analogous mutations in the rad3+ gene resulted in yeast hypersensitive to radiation. In addition, mutations in the kinase domain of ATM are found in patients with AT, a disease that causes radiation sensitivity. Furthermore, combinatorial libraries, peptide and peptide mimetics, defined chemical entities, oligonucleotides, and natural product libraries may be screened for activity as modulators in assays such as those described below. For example, an assay for identifying modulators of MCCSl kinase activity involves incubating an MCCSl kinase preparation in kinase buffer with gamma- 3 P-ATP and an exogenous kinase substrate, both in the presence and absence of a test compound, and measuring the moles of phosphate transferred to the substrate. For example, 2 μl of the 50 mM imidazole elution pool is added to kinase buffer. (See Example 6.) The reactions are incubated at 37°C for 20 min and samples are analyzed by SDS-PAGE prior to autoradiography or Western analysis. An increase in the moles of phosphate transferred to the substrate in presence of the test compound compared to the moles of phosphate transferred to the substrate in the absence of the test compound indicates that the test compound is an activator of said MCCSl kinase. Conversely, a decrease in the moles of phosphate transferred to the substrate in presence of the test compound compared to the moles of phosphate transferred to the substrate in the absence of the test compound indicates that the modulator is an inhibitor of said MCCSl kinase. Moreover, assays for identifying compounds that modulate interaction of MCCS 1 with other proteins may involve: transforming or transferring appropriate host cells with a DNA construct comprising a reporter gene under the control of a promoter regulated by a transcription factor having a DNA-binding domain and an activating domain; expressing in the host cells a first hybrid DNA sequence encoding a first fusion of part or all of MCCSl and the DNA binding domain or the activating domain of the transcription factor; expressing in the host cells a second hybrid DNA sequence encoding part or all of a protein that interacts with MCCSl and the DNA binding domain or activating domain of the transcription factor which is not incoφorated in the first fusion; evaluating the effect of a test compound on the interaction between MCCS 1 and the interacting protein by detecting binding of the interacting protein to MCCSl in a particular host cell by measuring the production of reporter gene product in the host cell in the presence or absence of the test compound; and identifying modulating compounds as those test compounds altering production of the reported gene product in comparison to production of the reporter gene product in the absence of the modulating compound. Presently preferred for use in the assay are a lexA promoter to drive expression of the reporter gene, the lacZ reporter gene, a transcription factor comprising the lexA DNA binding domain and the GAL4 transactivation domain, and yeast host cells. Another type of assay for identifying compounds that modulate the interaction between MCCSl and an interacting protein involves immobilizing MCCSl or a natural MCCSl interacting protein, detectably labelling the nonim mobilized binding partner, incubating the binding partners together and determining the effect of a test compound on the amount of label bound wherein a reduction in the label bound in the present of the test compound compared to the amount of label bound in the absence of the test compound indicates that the test agent is an inhibitor of MCCSl interaction with protein. Conversely, an increase in the bound in the presence of the test compound compared to the amount label bound in the absence of the compound indicates that the putative modulator is an activator of MCCSl interaction with the protein. Yet another method contemplated by the invention for identifying compounds that modulate the binding between MCCSl and an interacting protein involves immobilizing MCCS 1 or a fragment thereof on a solid support coated (or impregnated with) a fluorescent agent, labelling the interacting protein with a compound capable of exciting the fluorescent agent, contacting the immobilized MCCSl with the labelled interacting protein in the presence and absence of a test compound, detecting light emission by the fluorescent agent, and identifying modulating compounds as those test compounds that affect the emission of light by the florescent agent in comparison to the emission of light by the fluorescent agent in the absence of the test compound. Alternatively, the MCCSl interacting protein may be immobilized and MCCSl may be labelled in the assay. Example 12 Cell based complementation assays for identifying modulators of MCCSl or ATM are described below. In one type of assay, host cells (for example, esrl-1 yeast cells) are transformed with MCCSl -encoding DNA as is described in Example 4. The esrl-1 yeast strain is normally sensitive to treatment with ultraviolet (UV) light, but esrl-1 yeast cells expressing MCCSl or ATR are no longer sensitive to treatment with UV light. The transformed yeast cells are exposed to test compounds and the effect of the test compounds on UV sensitivity of the transformed host cell is determined. Test compounds that are inhibitors of MCCSl or ATR activity restore UV sensitivity to the MCCSl transformed esrl-1 cells. Alternatively, esrl-1 tell double mutant yeast cells are used as host cells instead of esrl-1 yeast cells. The TEL1 gene is homologous to ATM and the TEL1 mutation is described in Morrow, et al , Cell, #2:831-840 (1995). The invention also specifically contemplates that the esrl-1 or esrl-1 tell double mutant yeast host cells may be transformed with ATM-encoding DNA (SEQ ID NO: 34). In an alternative embodiment, the assays include clastogenic agents or events instead of treatment with UV light (e.g. , IR, hydroxyurea, or DNA damaging agents). Appropriate host cells for use in such embodiments would be those that are sensitive to the alternative clastogenic agents or events. Another type of complementation assay involves the use of mammalian host cells such as cell lines derived from cells of AT patients. As described above for yeast cells, the mammalian cells are transfected with DNA encoding MCCS l , ATR, or ATM and then exposed to test compounds. Test compounds that are inhibitors of MCCSl , ATR, or ATM activity will restore the phenotype of the untransformed host cell (e.g. , sensitivity to IR). The above assays can be used to identify compounds that inhibit activity of MCCSl , ATR, and ATM or compounds that inhibit activity of only one of the enzymes. In an alternative type of assay, the yeast or mammalian host cells are transformed with DNA encoding chimeric polypeptides including various combinations of MCCSl and ATM domains. MCCSl and ATM show structural similarities, and chimeric polypeptides which comprise portions of MCCSl and ATM are useful in elucidating active sites and binding domains of both MCCSl and ATM. Polynucleotides encoding the chimeras can be prepared by standard molecular biology techniques known to the skilled worker and as exemplified herein. The chimeric polypeptides are expressed in host cells and modulators of the chimeras can be identified by the assays disclosed herein. Example 13 MCCSl and ATM are both involved in meiosis I checkpoints. Since MCCSl is demonstrated herein to have kinase activity, assays were performed to determine if ATM possessed kinase activity. To determine the kinase activity of ATM, ATM was immunoprecipitated from MRC-5 fibroblasts (ATCC #171 -CCL) with polyclonal antisera, 6076. MRC-5 cells are human lung embryonal diploid fibroblasts. MRC-5 cells were obtained from the ATCC at passage 19 and maintained in Minimal Essential Medium supplemented with 10% fetal bovine serum, 100 units/ml penicillin, 100 mg/ml streptomycin, and 100 mM MEM non-essential amino acids. Media and media supplements were obtained through Gibco Life Technologies. Cell lines were maintained in a water- saturated 37 C C incubator with 5 % C. MRC-5 cell extracts were prepared by lysis of a 10cm plate of log- phase cells in 0.5 ml of Lysis Buffer I (50 M NaPO 4 , pH 7.2; 0.5 % TritonX-100; 2 M EDTA; 2 mM EGTA; 25 mM NaF; 25 mM 2-glycerophosphate; 1 mM phenylmethylsulfonyl fluoride [PMSF]; 1 μg/ml leupeptin 1 μg/ml pepstatin A; 2 mM DTT) on ice. Cells were scraped from plates using a rubber spatula then sonicated in a cup horn sonicator (Sonifier 250, Branson Ultrasonics Coφ. , Danbury, CT) at 100% output for 90 seconds. Lysates were then clarified in a 4°C microfuge for 2 minutes. Preclearing was done by adding 10 μg purified rabbit IgG (Zymed) and 30 μl Protein A Agarose slurry (Pierce) followed by incubation at 4°C for 60 minutes while rocking. To the precleared lysates, 10 μg of affinity purified 6076 antisera (or 10 μg 6076 pre-blocked with 0.04 mg P45 peptide for 30 min.) was added and incubated on ice for 60 minutes. Immunoprecipitates were collected by addition of 30 μl Protein A agarose slurry and incubated with rocking at 4°C for 30 minutes followed by four washes in Lysis Buffer I. Kinase reactions were carried out by washing the immunoprecipitations once with kinase buffer (25 μM Hepes pH 7.7; 50 mM KCl; 10 mM MgCl 2 ; 0.1 % NP-40; 2 % glycerol; 1 mM DTT), followed by incubation in 20 μl of Kinase Buffer containing 10 μM ATP + 10μCi γ 32 P-ATP [50 Ci/mmol] for 20 minutes at 37°C. Reactions were stopped by the addition of 20 μl 2X SDS sample buffer and boiled for 5 minutes prior to separation on 6% SDS polyacrylamide gels. The gels were dried and exposed to x-ray film (Kodak, XAR-5) at -80°C overnight. 10 cm plates of log-phase MRC-5 cells were washed once with PBS then incubated in Dulbeco's Modified Eagle Medium (minus methionine) containing 2 % dialyzed fetal bovine serum for 30 minutes. Cells were labeled by adding 200 μCi 35 S-methionine (1000 Ci/mmol TRAN 35 S-LABEL, ICN Radiochemicals) for 2 hours. Labeled cells were then washed once with PBS and frozen at -80°C prior to immunoprecipitation. The incubation of the immunoprecipitated complexes in kinase buffer produced a phosphorylated product with a molecular weight of approximately 350,000 that co-migrated with ATM in polyacrylamide gels. Similar results were obtained for ATR immune complexes immunoprecipitated with anti-AgDH-2 (MCCSl) polyclonal antisera of Example 5. ATR and ATM thus appear to be able to self-phosphorylate or associate with a protein kinase. To determine the role of ATR and ATM in meiosis, immunostaining techniques on surface spreads of mouse spermatocytes were utilized to localize ATR and ATM to meiotic chromosomes. Antibodies recognizing ATR and ATM were utilized with mouse antibodies against Corl . Corl is a component of axial/lateral elements of synapsing chromosomes [Dobson et al , J. Cell Sci. , 107:2749-2760 (1994)]. Corl chromosomal staining appears when the axial elements begin to form between the sister chromatids of each homolog in leptonema of meiotic prophase, prior to the initiation of synapsis. As homologous bivalents synapse, the axial elements from the two homologs align and a central element forms between them, completing the structure called the synaptonemal complex (SC). When short stretches of Corl begin to appear prior to any evidence of synapsis, neither ATR nor ATM is detectable. As homologs start synapsis, both proteins were seen at pairing forks; however, the location and behavior of the two proteins differed markedly. In normal zygotene nuclei, the stage during which homologs synapse, ATR was present in small amounts and transiently at discrete foci along the asynapsed (unpaired) axes. As homologs synapse, ATR disappeared from these locations. However, at regions delayed in synapsis, often seen near the proximal ends of autosomal bivalents, there was an accumulation of ATR foci along the unsynapsed axes. ATR was detected at similar locations on the two axial elements. In nuclei where an entire autosome fails to find its homologous pairing partner, ATR foci were detected along the entire lengths of these asynapsed axis. In males, where the X chromosome has no homolog, ATR foci were localized along the unpaired axis. ATM was also visualized as foci and was first detected during zygonema as homologs synapse, but ATM localization was different than ATR. ATM was first observed along synapsed axes when homologous autosomal axial elements come into contact. However, during mid-pachynema, after autosomal synapsis has been completed, ATM foci appeared on the X chromosome axis. ATM localization persisted on fully synapsed bivalents into pachynema, a substage that lasts 3 days in mouse oocytes and 6 days in mouse spermatocytes. During pachynema, the number of foci drops gradually, stabilizing briefly in mid-pachynema before eventually disappearing mid-to late pachynema. Thus, ATR and ATM protein kinases play important and complementary roles at distinct stages in meiosis I. The involvement of ATR appears to be transient during early meiotic prophase while the role of ATM appears to be more prolonged. However, both ATR and ATM coordinate the various events of meiotic prophase by performing similar checkpoint functions. The foregoing illustrative examples relate to presently preferred embodiments of the invention and numerous modifications and variations thereof are expected to occur to those skilled in the art. Thus only such limitations as appear in the appended claims should be placed upon the scope of the present invention. SEQUENCE LISTING (1) GENERAL INFORMATION: (i) APPLICANT: ICOS Corporation (ii) TITLE OF INVENTION: Cell Cycle Checkpoint PIK-Related Kinase Materials and Methods (iii) NUMBER OF SEQUENCES: 42 (iv) CORRESPONDENCE ADDRESS: (A) ADDRESSEE: Marshall, O'Toole, Gerstein, Murray & Borun (B) STREET: 6300 Sears Tower, 233 S. Wacker Dr. (C) CITY: Chicago (D) STATE: Illinois (E) COUNTRY: USA (F) ZIP: 60606 (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 #1.30 (vi) CURRENT APPLICATION DATA: (A) APPLICATION NUMBER: (B) FILING DATE: (C) CLASSIFICATION: (viii) ATTORNEY/AGENT INFORMATION: (A) NAME: Noland, Greta E. (B) REGISTRATION NUMBER: 35,302 (C) REFERENCE/DOCKET NUMBER: 27866/33607 (ix) TELECOMMUNICATION INFORMATION: (A) TELEPHONE: (312) 474-6300 (B) TELEFAX: (312) 474-0448 (C) TELEX: 25-3856 (2) INFORMATION FOR SEQ ID NO: 1 : (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 7621 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA (vii) IMMEDIATE SOURCE: (B) CLONE: pBSHFB2HT -27 (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 333..7559 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:l: CTTGTGAAGA GAATGTTTTA CACTCTTGTT AGTGAAGTTT ATTCTTTAAA AGTCAATCGT 60 CAAGGATTTA GCAAATGAAT TAGCACTTCG GATATACTTG TTTATTTAAT ATCTTTTTTG 120 TTTATTTCAA AGAATTCAGT AATTGGATCA TAACGAGACT TCTGCGGATT GCAGCAACTC 180 CCTCCTGTCA TTTGTTACAC AAGAAAATCT GTGAAGTCAT CTGTTCATTA TTATTTCTTT 240 TTAAAAGCAA GAGTCCTGCT ATTTTTGGGG TACTCACAAA AGAATTATTA CAACTTTTTG 300 AAGACTTGGT TTACCTCCAT AGAAGAAATG TG ATG GGT CAT GCT GTG GAA TGG 353 Met Gly His Ala Val Glu Trp 1 5 CCA GTG GTC ATG AGC CGA TTT TTA AGT CAA TTA GAT GAA CAC ATG GGA 401 Pro Val Val Met Ser Arg Phe Leu Ser Gin Leu Asp Glu His Met Gly 10 15 20 TAT TTA CAA TCA GCT CCT TTG CAG TTG ATG AGT ATG CAA AAA TTA GAA 449 Tyr Leu Gin Ser Ala Pro Leu Gin Leu Met Ser Met Gin Lys Leu Glu 25 30 35 TTT ATT GAA GTC ACT TTA TTA ACG GTT CTT ACT CGT ATT ATT GCA ATT 497 Phe He Glu Val Thr Leu Leu Thr Val Leu Thr Arg He He Ala He 40 45 50 55 GTG TTT TTT AGA AGG CAA GAA CTC TTA CTT TGG CAG ATA GGT TGT GTT 5 5 Val Phe Phe Arg Arg Gin Glu Leu Leu Leu Trp Gin He Gly Cys Val 60 65 70 CTG CTA GAG TAT GGT AGT CCA AAA ATT AAA TCC CTA GCA ATT AGC TTT 593 Leu Leu Glu Tyr Gly Ser Pro Lys He Lys Ser Leu Ala He Ser Phe 75 80 85 TTA ACA GAA CTT TTT CAG CTT GGA GGA CTA CCA GCA CAA CCA GCT AGC 641 Leu Thr Glu Leu Phe Gin Leu Gly Gly Leu Pro Ala Gin Pro Ala Ser 90 95 100 ACT TTT TTC AGC TCA TTT TTG GAA TTA TTA AAA CAC CTT GTA GAA ATG 689 Thr Phe Phe Ser Ser Phe Leu Glu Leu Leu Lys His Leu Val Glu Met 105 110 115 GAT ACT GAC CAA TTG AAA CTC TAT GAA GAG CCA TTA TCA AAG CTG ATA 737 Asp Thr Asp Gin Leu Lys Leu Tyr Glu Glu Pro Leu Ser Lys Leu He 120 125 130 135 AAG ACA CTA TTT CCC TTT GAA GCA GAA GCT TAT AGA AAT ATT GAA CCT 785 Lys Thr Leu Phe Pro Phe Glu Ala Glu Ala Tyr Arg Asn He Glu Pro 140 145 150 GTC TAT TTA AAT ATG CTG CTG GAA AAA CTC TGT GTC ATG TTT GAA GAC 833 Val Tyr Leu Asn Met Leu Leu Glu Lys Leu Cys Val Met Phe Glu Asp 155 160 165 GGT GTG CTC ATG CGG CTT AAG TCT GAT TTG CTA AAA GCA GCT TTG TGC 881 Gly Val Leu Met Arg Leu Lys Ser Asp Leu Leu Lys Ala Ala Leu Cys 170 175 180 CAT TTA CTG CAG TAT TTC CTT AAA TTT GTG CCA GCT GGG TAT GAA TCT 929 His Leu Leu Gin Tyr Phe Leu Lys Phe Val Pro Ala Gly Tyr Glu Ser 185 190 195 GCT TTA CAA GTC AGG AAG GTC TAT GTG AGA AAT ATT TGT AAA GCT CTT 977 Ala Leu Gin Val Arg Lys Val Tyr Val Arg Asn He Cys Lys Ala Leu 200 205 210 215 TTG GAT GTG CTT GGA ATT GAG GTA GAT GCA GAG TAC TTG TTG GGC CCA 1025 Leu Asp Val Leu Gly He Glu Val Asp Ala Glu Tyr Leu Leu Gly Pro 220 225 230 CTT TAT GCA GCT TTG AAA ATG GAA AGT ATG GAA ATC ATT GAG GAG ATT 1073 Leu Tyr Ala Ala Leu Lys Met Glu Ser Met Glu He He Glu Glu He 235 240 245 CAA TGC CAA ACT CAA CAG GAA AAC CTC AGC AGT AAT AGT GAT GGA ATA 1121 Gin Cys Gin Thr Gin Gin Glu Asn Leu Ser Ser Asn Ser Asp Gly He 250 255 260 TCA CCC AAA AGG CGT CGT CTC AGC TCG TCT CTA AAC CCT TCT AAA AGA 1169 Ser Pro Lys Arg Arg Arg Leu Ser Ser Ser Leu Asn Pro Ser Lys Arg 265 270 275 GCA CCA AAA CAG ACT GAG GAA ATT AAA CAT GTG GAC ATG AAC CAA AAG 1217 Ala Pro Lys Gin Thr Glu Glu He Lys His Val Asp Met Asn Gin Lys 280 285 290 295 AGC ATA TTA TGG AGT GCA CTG AAA CAG AAA GCT GAA TCC CTT CAG ATT 1265 Ser He Leu Trp Ser Ala Leu Lys Gin Lys Ala Glu Ser Leu Gin He 300 305 310 TCC CTT GAA TAC AGT GGC CTA AAG AAT CCT GTT ATT GAG ATG TTA GAA 1313 Ser Leu Glu Tyr Ser Gly Leu Lys Asn Pro Val He Glu Met Leu Glu 315 320 325 GGA ATT GCT GTT GTC TTA CAA CTG ACT GCT CTG TGT ACT GTT CAT TGT 1361 Gly He Ala Val Val Leu Gin Leu Thr Ala Leu Cys Thr Val His Cys 330 335 340 TCT CAT CAA AAC ATG AAC TGC CGT ACT TTC AAG GAC TGT CAA CAT AAA 1409 Ser His Gin Asn Met Asn Cys Arg Thr Phe Lys Asp Cys Gin His Lys 345 350 355 TCC AAG AAG AAA CCT TCT GTA GTG ATA ACT TGG ATG TCA TTG GAT TTT 1457 Ser Lys Lys Lys Pro Ser Val Val He Thr Trp Met Ser Leu Asp Phe 360 365 370 375 TAC ACA ACA GTG CTT AAG AGC TGT AGA AGG TTG TTA GAA TCT GTT CAG 1505 Tyr Thr Thr Val Leu Lys Ser Cys Arg Arg Leu Leu Glu Ser Val Gin 380 385 390 AAA CGG ACT GGA GGC AAC ATT GAT AAG GTG GTG AAA ATT TAT GAT GCT 1553 Lys Arg Thr Gly Gly Asn He Asp Lys Val Val Lys He Tyr Asp Ala 395 400 405 TTG ATT TAT ATG CAA GTA AAC AGT TCA TTT GAA GAT CAT ATC CTG GAA 1601 Leu He Tyr Met Gin Val Asn Ser Ser Phe Glu Asp His He Leu Glu 410 415 420 GAT TTA TGT GGA ATG CTC TCA CTT CCA TGG ATT TAT TCC CAT TCT GAT 1649 Asp Leu Cys Gly Met Leu Ser Leu Pro Trp He Tyr Ser His Ser Asp 425 430 435 GAT GGC TGT TTA AAG TTG ACC ACA TTT GCC GCT AAT CTT CTA ACA TTA 1697 Asp Gly Cys Leu Lys Leu Thr Thr Phe Ala Ala Asn Leu Leu Thr Leu 440 445 450 455 AGC TGT AGG ATT TCA GAT AGC TAT TCA CCA CAG GCA CAA TCA CGA TGT 1745 Ser Cys Arg He Ser Asp Ser Tyr Ser Pro Gin Ala Gin Ser Arg Cys 460 465 470 GTG TTT CTT CTG ACT CTG TTT CCA AGA AGA ATA TTC CTT GAG TGG AGA 1793 Val Phe Leu Leu Thr Leu Phe Pro Arg Arg He Phe Leu Glu Trp Arg 475 480 485 ACA GCA GTT TAC AAC TGG GCC CTG CAG AGC TCC CAT GAA GTA ATC CGG 18 1 Thr Ala Val Tyr Asn Trp Ala Leu Gin Ser Ser His Glu Val He Arg 490 495 500 GCT AGT TGT GTT AGT GGA TTT TTT ATC TTA TTG CAG CAG CAG AAT TCT 1889 Ala Ser Cys Val Ser Gly Phe Phe He Leu Leu Gin Gin Gin Asn Ser 505 510 515 TGT AAC AGA GTT CCC AAG ATT CTT ATA GAT AAA GTC AAA GAT GAT TCT 1937 Cys Asn Arg Val Pro Lys He Leu He Asp Lys Val Lys Asp Asp Ser 520 525 530 535 GAC ATT GTC AAG AAA GAA TTT GCT TCT ATA CTT GGT CAA CTT GTC TGT 1985 Asp He Val Lys Lys Glu Phe Ala Ser He Leu Gly Gin Leu Val Cys 540 545 550 ACT CTT CAC GGC ATG TTT TAT CTG ACA AGT TCT TTA ACA GAA CCT TTC 2033 Thr Leu His Gly Met Phe Tyr Leu Thr Ser Ser Leu Thr Glu Pro Phe 555 560 565 TCT GAA CAC GGA CAT GTG GAC CTC TTC TGT AGG AAC TTG AAA GCC ACT 2081 Ser Glu His Gly His Val Asp Leu Phe Cys Arg Asn Leu Lys Ala Thr 570 575 580 TCT CAA CAT GAA TGT TCA TCT TCT CAA CTA AAA GCT TCT GTC TGC AAG 2129 Ser Gin His Glu Cys Ser Ser Ser Gin Leu Lys Ala Ser Val Cys Lys 585 590 595 CCA TTC CTT TTC CTA CTG AAA AAA AAA ATA CCT AGT CCA GTA AAA CTT 2177 Pro Phe Leu Phe Leu Leu Lys Lys Lys He Pro Ser Pro Val Lys Leu 600 605 610 615 GCT TTC ATA GAT AAT CTA CAT CAT CTT TGT AAG CAT CTT GAT TTT AGA 2225 Ala Phe He Asp Asn Leu His His Leu Cys Lys His Leu Asp Phe Arg 620 625 630 GAA GAT GAA ACA GAT GTA AAA GCA GTT CTT GGA ACT TTA TTA AAT TTA 2273 Glu Asp Glu Thr Asp Val Lys Ala Val Leu Gly Thr Leu Leu Asn Leu 635 640 645 ATG GAA GAT CCA GAC AAA GAT GTT AGA GTG GCT TTT AGT GGA AAT ATC 2321 Met Glu Asp Pro Asp Lys Asp Val Arg Val Ala Phe Ser Gly Asn He 650 655 660 AAG CAC ATA TTG GAA TCC TTG GAC TCT GAA GAT GGA TTT ATA AAG GAG 2369 Lys His He Leu Glu Ser Leu Asp Ser Glu Asp Gly Phe He Lys Glu 665 670 675 CTT TTT GTC TTA AGA ATG AAG GAA GCA TAT ACA CAT GCC CAA ATA TCA 2417 Leu Phe Val Leu Arg Met Lys Glu Ala Tyr Thr His Ala Gin He Ser 680 685 690 695 AGA AAT AAT GAG CTG AAG GAT ACC TTG ATT CTT ACA ACA GGG GAT ATT 2465 Arg Asn Asn Glu Leu Lys Asp Thr Leu He Leu Thr Thr Gly Asp He 700 705 710 GGA AGG GCC GCA AAA GGA GAT TTG GTA CCA TTT GCA CTC TTA CAC TTA 2513 Gly Arg Ala Ala Lys Gly Asp Leu Val Pro Phe Ala Leu Leu His Leu 715 720 725 TTG CAT TGT TTG TTA TCC AAG TCA GCA TCT GTC TCT GGA GCA GCA TAC 2561 Leu His Cys Leu Leu Ser Lys Ser Ala Ser Val Ser Gly Ala Ala Tyr 730 735 740 ACA GAA ATT AGA GCT CTG GTT GCA GCT AAA AGT GTT AAA CTG CAA AGT 2609 Thr Glu He Arg Ala Leu Val Ala Ala Lys Ser Val Lys Leu Gin Ser 745 750 755 TTT TTC AGC CAG TAT AAG AAA CCC ATC TGT CAG TTT TTG GTA GAA TCC 2657 Phe Phe Ser Gin Tyr Lys Lys Pro He Cys Gin Phe Leu Val Glu Ser 760 765 770 775 CTT CAC TCT AGT CAG ATG ACA GCA CTT CCG AAT ACT CCA TGC CAG AAT 2705 Leu His Ser Ser Gin Met Thr Ala Leu Pro Asn Thr Pro Cys Gin Asn 780 785 790 GCT GAC GTG CGA AAA CAA GAT GTG GCT CAC CAG AGA GAA ATG GCT TTA 2753 Ala Asp Val Arg Lys Gin Asp Val Ala His Gin Arg Glu Met Ala Leu 795 800 805 AAT ACG TTG TCT GAA ATT GCC AAC GTT TTC GAC TTT CCT GAT CTT AAT 2801 Asn Thr Leu Ser Glu He Ala Asn Val Phe Asp Phe Pro Asp Leu Asn 810 815 820 CGT TTT CTT ACT AGG ACA TTA CAA GTT CTA CTA CCT GAT CTT GCT GCC 2849 Arg Phe Leu Thr Arg Thr Leu Gin Val Leu Leu Pro Asp Leu Ala Ala 825 830 835 AAA GCA AGC CCT GCA GCT TCT GCT CTC ATT CGA ACT TTA GGA AAA CAA 2897 Lys Ala Ser Pro Ala Ala Ser Ala Leu He Arg Thr Leu Gly Lys Gin 840 845 850 855 TTA AAT GTC AAT CGT AGA GAG ATT TTA ATA AAC AAC TTC AAA TAT ATT 2945 Leu Asn Val Asn Arg Arg Glu He Leu He Asn Asn Phe Lys Tyr He 860 865 870 TTT TCT CAT TTG GTC TGT TCT TGT TCC AAA GAT GAA TTA GAA CGT GCC 2993 Phe Ser His Leu Val Cys Ser Cys Ser Lys Asp Glu Leu Glu Arg Ala 875 880 885 CTT CAT TAT CTG AAG AAT GAA ACA GAA ATT GAA CTG GGG AGC CTG TTG 3041 Leu His Tyr Leu Lys Asn Glu Thr Glu He Glu Leu Gly Ser Leu Leu 890 895 900 AGA CAA GAT TTC CAA GGA TTG CAT AAT GAA TTA TTG CTG CGT ATT GGA 3089 Arg Gin Asp Phe Gin Gly Leu His Asn Glu Leu Leu Leu Arg He Gly 905 910 915 GAA CAC TAT CAA CAG GTT TTT AAT GGT TTG TCA ATA CTT GCC TCA TTT 3137 Glu His Tyr Gin Gin Val Phe Asn Gly Leu Ser He Leu Ala Ser Phe 920 925 930 935 GCA TCC AGT GAT GAT CCA TAT CAG GGC CCG AGA GAT ATC ATA TCA CCT 3185 Ala Ser Ser Asp Asp Pro Tyr Gin Gly Pro Arg Asp He He Ser Pro 940 945 950 GAA CTG ATG GCT GAT TAT TTA CAA CCC AAA TTG TTG GGC ATT TTG GCT 3233 Glu Leu Met Ala Asp Tyr Leu Gin Pro Lys Leu Leu Gly He Leu Ala 955 960 965 TTT TTT AAC ATG CAG TTA CTG AGC TCT AGT GTT GGC ATT GAA GAT AAG 3281 Phe Phe Asn Met Gin Leu Leu Ser Ser Ser Val Gly He Glu Asp Lys 970 975 980 AAA ATG GCC TTG AAC AGT TTG ATG TCT TTG ATG AAG TTA ATG GGA CCC 3329 Lys Met Ala Leu Asn Ser Leu Met Ser Leu Met Lys Leu Met Gly Pro 985 990 995 AAA CAT GTC AGT TCT GTG AGG GTG AAG ATG ATG ACC ACA CTG AGA ACT 3377 Lys His Val Ser Ser Val Arg Val Lys Met Met Thr Thr Leu Arg Thr 1000 1005 1010 1015 GGC CTT CGA TTC AAG GAT GAT TTT CCT GAA TTG TGT TGC AGA GCT TGG 3425 Gly Leu Arg Phe Lys Asp Asp Phe Pro Glu Leu Cys Cys Arg Ala Trp 1020 1025 1030 GAC TGC TTT GTT CGC TGC CTG GAT CAT GCT TGT CTG GGC TCC CTT CTC 3473 Asp Cys Phe Val Arg Cys Leu Asp His Ala Cys Leu Gly Ser Leu Leu 1035 1040 1045 AGT CAT GTA ATA GTA GCT TTG TTA CCT CTT ATA CAC ATC CAG CCT AAA 3521 Ser His Val He Val Ala Leu Leu Pro Leu He His He Gin Pro Lys 1050 1055 1060 GAA ACT GCA GCT ATC TTC CAC TAC CTC ATA ATT GAA AAC AGG GAT GCT 3569 Glu Thr Ala Ala He Phe His Tyr Leu He He Glu Asn Arg Asp Ala 1065 1070 1075 GTG CAA GAT TTT CTT CAT GAA ATA TAT TTT TTA CCT GAT CAT CCA GAA 3617 Val Gin Asp Phe Leu His Glu He Tyr Phe Leu Pro Asp His Pro Glu 1080 1085 1090 1095 TTA AAA AAG ATA AAA GCC GTT CTC CAG GAA TAC AGA AAG GAG ACC TCT 3665 Leu Lys Lys He Lys Ala Val Leu Gin Glu Tyr Arg Lys Glu Thr Ser 1100 1105 1110 GAG AGC ACT GAT CTT CAG ACA ACT CTT CAG CTC TCT ATG AAG GCC ATT 3713 Glu Ser Thr Asp Leu Gin Thr Thr Leu Gin Leu Ser Met Lys Ala He 1115 1120 1125 CAA CAT GAA AAT GTC GAT GTT CGT ATT CAT GCT CTT ACA AGC TTG AAG 3761 Gin His Glu Asn Val Asp Val Arg He His Ala Leu Thr Ser Leu Lys 1130 1135 1140 GAA ACC TTG TAT AAA AAT CAG GAA AAA CTG ATA AAG TAT GCA ACA GAC 3809 Glu Thr Leu Tyr Lys Asn Gin Glu Lys Leu He Lys Tyr Ala Thr Asp 1145 1150 1155 AGT GAA ACA GTA GAA CCT ATT ATC TCA CAG TTG GTG ACA GTG CTT TTG 3857 Ser Glu Thr Val Glu Pro He He Ser Gin Leu Val Thr Val Leu Leu 1160 1165 1170 1175 AAA GGT TGC CAA GAT GCA AAC TCT CAA GCT CGG TTG CTC TGT GGG GAA 3905 Lys Gly Cys Gin Asp Ala Asn Ser Gin Ala Arg Leu Leu Cys Gly Glu 1180 1185 1190 TGT TTA GGG GAA TTG GGG GCG ATA GAT CCA GGT CGA TTA GAT TTC TCA 3953 Cys Leu Gly Glu Leu Gly Ala He Asp Pro Gly Arg Leu Asp Phe Ser 1195 1200 1205 ACA ACT GAA ACT CAA GGA AAA GAT TTT ACA TTT GTG ACT GGA GTA GAA 4001 Thr Thr Glu Thr Gin Gly Lys Asp Phe Thr Phe Val Thr Gly Val Glu 1210 1215 1220 GAT TCA AGC TTT GCC TAT GGA TTA TTG ATG GAG CTA ACA AGA GCT TAC 4049 Asp Ser Ser Phe Ala Tyr Gly Leu Leu Met Glu Leu Thr Arg Ala Tyr 1225 1230 1235 CTT GCG TAT GCT GAT AAT AGC CGA GCT CCA GAT TCA GCT GCC TAT GCC 4097 Leu Ala Tyr Ala Asp Asn Ser Arg Ala Pro Asp Ser Ala Ala Tyr Ala 1240 1245 1250 1255 ATT CAG GAG TTG CTT TCT ATT TAT GAC TGT AGA GAG ATG GAG ACC AAC 4145 He Gin Glu Leu Leu Ser He Tyr Asp Cys Arg Glu Met Glu Thr Asn 1260 1265 1270 GGC CCA GGT CAC CAA TTG TGG AGG AGA TTT CCT GAG CAT GTT CGG GAA 4193 Gly Pro Gly His Gin Leu Trp Arg Arg Phe Pro Glu His Val Arg Glu 1275 1280 1285 ATA CTA GAA CCT CAT CTA AAT ACC AGA TAC AAG AGT TCT CAG AAG TCA 4241 He Leu Glu Pro His Leu Asn Thr Arg Tyr Lys Ser Ser Gin Lys Ser 1290 1295 1300 ACC GAT TGG TCT GGA GTA AAG AAG CCA ATT TAC TTA AGT AAA TTG GGT 4289 Thr Asp Trp Ser Gly Val Lys Lys Pro He Tyr Leu Ser Lys Leu Gly 1305 1310 1315 AGT AAC TTT GCA GAA TGG TCA GCA TCT TGG GCA GGT TAT CTT ATT ACA 4337 Ser Asn Phe Ala Glu Trp Ser Ala Ser Trp Ala Gly Tyr Leu He Thr 1320 1325 1330 1335 AAG GTT CGA CAT GAT CTT GCC AGT AAA ATT TTC ACC TGC TGT AGC ATT 4385 Lys Val Arg His Asp Leu Ala Ser Lys He Phe Thr Cys Cys Ser He 1340 1345 1350 ATG ATG AAG CAT GAT TTC AAA GTG ACC ATC TAT CTT CTT CCA CAT ATT 4433 Met Met Lys His Asp Phe Lys Val Thr He Tyr Leu Leu Pro His He 1355 1360 1365 CTG GTG TAT GTC TTA CTG GGT TGT AAT CAA GAA GAT CAG CAG GAG GTT 4481 Leu Val Tyr Val Leu Leu Gly Cys Asn Gin Glu Asp Gin Gin Glu Val 1370 1375 1380 TAT GCA GAA ATT ATG GCA GTT CTA AAG CAT GAC GAT CAG CAT ACC ATA 4529 Tyr Ala Glu He Met Ala Val Leu Lys His Asp Asp Gin His Thr He 1385 1390 1395 AAT ACC CAA GAC ATT GCA TCT GAT CTG TGT CAA CTC AGT ACA CAG ACT 4577 Asn Thr Gin Asp He Ala Ser Asp Leu Cys Gin Leu Ser Thr Gin Thr 1400 1405 1410 1415 GTG TTC TCC ATG CTT GAC CAT CTC ACA CAG TGG GCA AGG CAC AAA TTT 4625 Val Phe Ser Met Leu Asp His Leu Thr Gin Trp Ala Arg His Lys Phe 1420 1425 1430 CAG GCA CTG AAA GCT GAG AAA TGT CCA CAC AGC AAA TCA AAC AGA AAT 4673 Gin Ala Leu Lys Ala Glu Lys Cys Pro His Ser Lys Ser Asn Arg Asn 1435 1440 1445 AAG GTA GAC TCA ATG GTA TCT ACT GTG GAT TAT GAA GAC TAT CAG AGT 4721 Lys Val Asp Ser Met Val Ser Thr Val Asp Tyr Glu Asp Tyr Gin Ser 1450 1455 1460 GTA ACC CGT TTT CTA GAC CTC ATA CCC CAG GAT ACT CTG GCA GTA GCT 4769 Val Thr Arg Phe Leu Asp Leu He Pro Gin Asp Thr Leu Ala Val Ala 1465 1470 1475 TCC TTT CGC TCC AAA GCA TAC ACA CGA GCT GTA ATG CAC TTT GAA TCA 4817 Ser Phe Arg Ser Lys Ala Tyr Thr Arg Ala Val Met His Phe Glu Ser 1480 1485 1490 1495 TTT ATT ACA GAA AAG AAG CAA AAT ATT CAG GAA CAT CTT GGA TTT TTA 4865 Phe He Thr Glu Lys Lys Gin Asn He Gin Glu His Leu Gly Phe Leu 1500 1505 1510 CAG AAA TTG TAT GCT GCT ATG CAT GAA CCT GAT GGA GTG TCC GGA GTC 4913 Gin Lys Leu Tyr Ala Ala Met His Glu Pro Asp Gly Val Ser Gly Val 1515 1520 1525 AGT GCA ATT AGA AAG GCA GAA CCA TCT CTA AAA GAA CAG ATC CTT GAA 4961 Ser Ala He Arg Lys Ala Glu Pro Ser Leu Lys Glu Gin He Leu Glu 1530 1535 1540 CAT GAA AGC CTT GGC TTG CTG AGG GAT GCC ACT GCT TGT TAT GAC AGG 5009 His Glu Ser Leu Gly Leu Leu Arg Asp Ala Thr Ala Cys Tyr Asp Arg 1545 1550 1555 GCT ATT CAG CTA GAA CCA GAC CAG ATC ATT CAT TAC CAT GGT GTA GTA 5057 Ala He Gin Leu Glu Pro Asp Gin He He His Tyr His Gly Val Val 1560 1565 1570 1575 AAG TCC ATG TTA GGT CTT GGT CAG CTG TCT ACT GTT ATC ACT CAG GTG 5105 Lys Ser Met Leu Gly Leu Gly Gin Leu Ser Thr Val He Thr Gin Val 1580 1585 1590 AAT GGA GTG CAT GCT AAC AGG TCC GAG TGG ACA GAT GAA TTA AAC ACG 5153 Asn Gly Val His Ala Asn Arg Ser Glu Trp Thr Asp Glu Leu Asn Thr 1595 1600 1605 TAC AGA GTG GAA GCA GCT TGG AAA TTG TCA CAG TGG GAT TTG GTG GAA 5201 Tyr Arg Val Glu Ala Ala Trp Lys Leu Ser Gin Trp Asp Leu Val Glu 1610 1615 1620 AAC TAT TTG GCA GCA GAT GGA AAA TCT ACA ACA TGG AGT GTC AGA CTG 5249 Asn Tyr Leu Ala Ala Asp Gly Lys Ser Thr Thr Trp Ser Val Arg Leu 1625 1630 1635 GGA CAG CTA TTA TTA TCA GCC AAA AAA AGA GAT ATC ACA GCT TTT TAT 5297 Gly Gin Leu Leu Leu Ser Ala Lys Lys Arg Asp He Thr Ala Phe Tyr 1640 1645 1650 1655 GAC TCA CTG AAA CTA GTG AGA GCA GAA CAA ATT GTA CCT CTT TCA GCT 5345 Asp Ser Leu Lys Leu Val Arg Ala Glu Gin He Val Pro Leu Ser Ala 1660 1665 1670 GCA AGC TTT GAA AGA GGC TCC TAC CAA CGA GGA TAT GAA TAT ATT GTG 5393 Ala Ser Phe Glu Arg Gly Ser Tyr Gin Arg Gly Tyr Glu Tyr He Val 1675 1680 1685 AGA TTG CAC ATG TTA TGT GAG TTG GAG CAT AGC ATC AAA CCA CTT TTC 5441 Arg Leu H s Met Leu Cys Glu Leu Glu His Ser He Lys Pro Leu Phe 1690 1695 1700 CAG CAT TCT CCA GGT GAC AGT TCT CAA GAA GAT TCT CTA AAC TGG GTA 5489 Gin His Ser Pro Gly Asp Ser Ser Gin Glu Asp Ser Leu Asn Trp Val 1705 1710 1715 GCT CGA CTA GAA ATG ACC CAG AAT TCC TAC AGA GCC AAG GAG CCT ATC 5537 Ala Arg Leu Glu Met Thr Gin Asn Ser Tyr Arg Ala Lys Glu Pro He 1720 1725 1730 1735 CTG GCT CTC CGG AGG GCT TTA CTA AGC CTC AAC AAA AGA CCA GAT TAC 5585 Leu Ala Leu Arg Arg Ala Leu Leu Ser Leu Asn Lys Arg Pro Asp Tyr 1740 1745 1750 AAT GAA ATG GTT GGA GAA TGC TGG CTG CAG AGT GCC AGG GTA GCT AGA 5633 Asn Glu Met Val Gly Glu Cys Trp Leu Gin Ser Ala Arg Val Ala Arg 1755 1760 1765 AAG GCT GGT CAC CAC CAG ACA GCC TAC AAT GCT CTC CTT AAT GCA GGG 5681 Lys Ala Gly His His Gin Thr Ala Tyr Asn Ala Leu Leu Asn Ala Gly 1770 1775 1780 GAA TCA CGA CTC GCT GAA CTG TAC GTG GAA AGG GCA AAG TGG CTC TGG 5729 Glu Ser Arg Leu Ala Glu Leu Tyr Val Glu Arg Ala Lys Trp Leu Trp 1785 1790 1795 TCC AAG GGT GAT GTT CAC CAG GCA CTA ATT GTT CTT CAA AAA GGT GTT 5777 Ser Lys Gly Asp Val His Gin Ala Leu He Val Leu Gin Lys Gly Val 1800 1805 1810 1815 GAA TTA TGT TTT CCT GAA AAT GAA ACC CCA CCT GAG GGT AAG AAC ATG 5825 Glu Leu Cys Phe Pro Glu Asn Glu Thr Pro Pro Glu Gly Lys Asn Met 1820 1825 1830 TTA ATC CAT GGT CGA GCT ATG CTA CTA GTG GGC CGA TTT ATG GAA GAA 5873 Leu He His Gly Arg Ala Met Leu Leu Val Gly Arg Phe Met Glu Glu 1835 1840 1845 ACA GCT AAC TTT GAA AGC AAT GCA ATT ATG AAA AAA TAT AAG GAT GTG 5921 Thr Ala Asn Phe Glu Ser Asn Ala He Met Lys Lys Tyr Lys Asp Val 1850 1855 1860 ACC GCG TGC CTG CCA GAA TGG GAG GAT GGG CAT TTT TAC CTT GCC AAG 5969 Thr Ala Cys Leu Pro Glu Trp Glu Asp Gly His Phe Tyr Leu Ala Lys 1865 1870 1875 TAC TAT GAC AAA TTG ATG CCC ATG GTC ACA GAC AAC AAA ATG GAA AAG 6017 Tyr Tyr Asp Lys Leu Met Pro Met Val Thr Asp Asn Lys Met Glu Lys 1880 1885 1890 1895 CAA GGT GAT CTC ATC CGG TAT ATA GTT CTT CAT TTT GGC AGA TCT CTA 6065 Gin Gly Asp Leu He Arg Tyr He Val Leu His Phe Gly Arg Ser Leu 1900 1905 1910 CAA TAT GGA AAT CAG TTC ATA TAT CAG TCA ATG CCA CGA ATG TTA ACT 6113 Gin Tyr Gly Asn Gin Phe He Tyr Gin Ser Met Pro Arg Met Leu Thr 1915 1920 1925 CTA TGG CTT GAT TAT GGT ACA AAG GCA TAT GAA TGG GAA AAA GCT GGC 6161 Leu Trp Leu Asp Tyr Gly Thr Lys Ala Tyr Glu Trp Glu Lys Ala Gly 1930 1935 1940 CGC TCC GAT CGT GTA CAA ATG AGG AAT GAT TTG GGT AAA ATA AAC AAG 6209 Arg Ser Asp Arg Val Gin Met Arg Asn Asp Leu Gly Lys He Asn Lys 1945 1950 1955 GTT ATC ACA GAG CAT ACA AAC TAT TTA GCT CCA TAT CAA TTT TTG ACT 6257 Val He Thr Glu His Thr Asn Tyr Leu Ala Pro Tyr Gin Phe Leu Thr 1960 1965 1970 1975 GCT TTT TCA CAA TTG ATC TCT CGA ATT TGT CAT TCT CAC GAT GAA GTT 6305 Ala Phe Ser Gin Leu He Ser Arg He Cys His Ser His Asp Glu Val 1980 1985 1990 TTT GTT GTG CTT GAT GGA AAT AAT AGC CAA GTA TTT CTA GCC TAT CCT 6353 Phe Val Val Leu Asp Gly Asn Asn Ser Gin Val Phe Leu Ala Tyr Pro 1995 2000 2005 CAA CAA GCA ATG TGG ATG ATG ACA GCT GTG TCA AAG TCA TCT TAT CCC 6401 Gin Gin Ala Met Trp Met Met Thr Ala Val Ser Lys Ser Ser Tyr Pro 2010 2015 2020 ATG CGT GTG AAC AGA TGC AAG GAA ATC CTC AAT AAA GCT ATT CAT ATG 6449 Met Arg Val Asn Arg Cys Lys Glu He Leu Asn Lys Ala He His Met 2025 2030 2035 AAA AAA TCC TTA GAG AAG TTT GTT GGA GAT GCA ACT CGC CTA ACA GAT 6497 Lys Lys Ser Leu Glu Lys Phe Val Gly Asp Ala Thr Arg Leu Thr Asp 2040 2045 2050 2055 AAG CTT CTA GAA TTG TGC AAT AAA CCG GTG GAA ATT CTT GCT TCT CTT 6545 Lys Leu Leu Glu Leu Cys Asn Lys Pro Val Glu He Leu Ala Ser Leu 2060 2065 2070 CAG AAA CCA AAG AAG ATT TCT TTA AAA GGC TCA GAT GGA AAG TTC TAC 6593 Gin Lys Pro Lys Lys He Ser Leu Lys Gly Ser Asp Gly Lys Phe Tyr 2075 2080 2085 ATC ATG ATG TGT AAG CCA AAA GAT GAC CTG AGA AAG GAT TGT AGA CTA 6641 He Met Met Cys Lys Pro Lys Asp Asp Leu Arg Lys Asp Cys Arg Leu 2090 2095 2100 ATG GAA TTC AAT TCC TTG ATT AAT AAG TGC TTA AGA AAA GAT GCA GAG 6689 Met Glu Phe Asn Ser Leu He Asn Lys Cys Leu Arg Lys Asp Ala Glu 2105 2110 2115 TCT CGT AGA AGA GAA CTT CAT ATT CGA ACA TAT GCA GTT ATT CCA CTA 6737 Ser Arg Arg Arg Glu Leu His He Arg Thr Tyr Ala Val He Pro Leu 2120 2125 2130 2135 AAT GAT GAA TGT GGG ATT ATT GAA TGG GTG AAC AAC ACT GCT GGT TTG 6785 Asn Asp Glu Cys Gly He He Glu Trp Val Asn Asn Thr Ala Gly Leu 2140 2145 2150 AGA CCT ATT CTG ACC AAA CTA TAT AAA GAA AAG GGA GTG TAT ATG ACA 6833 Arg Pro He Leu Thr Lys Leu Tyr Lys Glu Lys Gly Val Tyr Met Thr 2155 2160 2165 GGA AAA GAA CTT CGC CAG TGT ATG CTA CCA AAG TCA GCA GCT TTA TCT 6881 Gly Lys Glu Leu Arg Gin Cys Met Leu Pro Lys Ser Ala Ala Leu Ser 2170 2175 2180 GAA AAA CTC AAA GTA TTC CGA GAA TTT CTC CTG CCC AGG CAT CCT CCT 6929 Glu Lys Leu Lys Val Phe Arg Glu Phe Leu Leu Pro Arg His Pro Pro 2185 2190 2195 ATT TTT CAT GAG TGG TTT CTG AGA ACA TTC CCT GAT CCT ACA TCA TGG 6977 He Phe His Glu Trp Phe Leu Arg Thr Phe Pro Asp Pro Thr Ser Trp 2200 2205 2210 2215 TAC AGT AGT AGA TCA GCT TAC TGC CGT TCC ACT GCA GTA ATG TCA ATG 7025 Tyr Ser Ser Arg Ser Ala Tyr Cys Arg Ser Thr Ala Val Met Ser Met 2220 2225 2230 GTT GGT TAT ATT CTG GGG CTT GGA GAC CGT CAT GGT GAA AAT ATT CTC 7073 Val Gly Tyr He Leu Gly Leu Gly Asp Arg His Gly Glu Asn He Leu 2235 2240 2245 TTT GAT TCT TTG ACT GGT GAA TGC GTA CAT GTA GAT TTC AAT TGT CTT 7121 Phe Asp Ser Leu Thr Gly Glu Cys Val His Val Asp Phe Asn Cys Leu 2250 2255 2260 TTC AAT AAG GGA GAA ACC TTT GAA GTT CCA GAA ATT GTG CCA TTT CGC 7169 Phe Asn Lys Gly Glu Thr Phe Glu Val Pro Glu He Val Pro Phe Arg 2265 2270 2275 CTG ACT CAT AAT ATG GTT AAT GGA ATG GGT CCT ATG GGA ACA GAG GGT 7217 Leu Thr His Asn Met Val Asn Gly Met Gly Pro Met Gly Thr Glu Gly 2280 2285 2290 2295 CTT TTT CGA AGA GCA TGT GAA GTT ACA ATG AGG CTG ATG CGT GAT CAG 7265 Leu Phe Arg Arg Ala Cys Glu Val Thr Met Arg Leu Met Arg Asp Gin 2300 2305 2310 CGA GAG CCT TTA ATG AGT GTC TTA AAG ACT TTT CTA CAT GAT CCT CTT 7313 Arg Glu Pro Leu Met Ser Val Leu Lys Thr Phe Leu His Asp Pro Leu 2315 2320 2325 GTG GAA TGG AGT AAA CCA GTG AAA GGG CAT TCC AAA GCG CCA CTG AAT 7361 Val Glu Trp Ser Lys Pro Val Lys Gly His Ser Lys Ala Pro Leu Asn 2330 2335 2340 GAA ACT GGA GAA GTT GTC AAT GAA AAG GCC AAG ACC CAT GTT CTT GAC 7409 Glu Thr Gly Glu Val Val Asn Glu Lys Ala Lys Thr His Val Leu Asp 2345 2350 2355 ATT GAG CAG CGA CTA CAA GGT GTA ATC AAG ACT CGA AAT AGA GTG ACA 7457 He Glu Gin Arg Leu Gin Gly Val He Lys Thr Arg Asn Arg Val Thr 2360 2365 2370 2375 GGA CTG CCG TTA TCT ATT GAA GGA CAT GTG CAT TAC CTT ATA CAA GAA 7505 Gly Leu Pro Leu Ser He Glu Gly His Val His Tyr Leu He Gin Glu 2380 2335 2390 GCT ACT GAT GAA AAC TTA CTA TGC CAG ATG TAT CTT GGT TGG ACT CCA 7553 Ala Thr Asp Glu Asn Leu Leu Cys Gin Met Tyr Leu Gly Trp Thr Pro 2395 2400 2405 TAT ATG TGAAATGAAA TTATGTAAAA GAATATGTTA ATAATCTAAA AGTAAAAAAA 7609 Tyr Met AAAAAAAAAA AA 7621 (2) INFORMATION FOR SEQ ID NO:2 : (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2409 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 2 : Met Gly His Ala Val Glu Trp Pro Val Val Met Ser Arg Phe Leu Ser 1 5 10 15 Gin Leu Asp Glu His Met Gly Tyr Leu Gin Ser Ala Pro Leu Gin Leu 20 25 30 Met Ser Met Gin Lys Leu Glu Phe He Glu Val Thr Leu Leu Thr Val 35 40 45 Leu Thr Arg He He Ala He Val Phe Phe Arg Arg Gin Glu Leu Leu 50 55 60 Leu Trp Gin He Gly Cys Val Leu Leu Glu Tyr Gly Ser Pro Lys He 65 70 75 80 Lys Ser Leu Ala He Ser Phe Leu Thr Glu Leu Phe Gin Leu Gly Gly 85 90 95 Leu Pro Ala Gin Pro Ala Ser Thr Phe Phe Ser Ser Phe Leu Glu Leu 100 105 110 Leu Lys His Leu Val Glu Met Asp Thr Asp Gin Leu Lys Leu Tyr Glu 115 120 125 Glu Pro Leu Ser Lys Leu He Lys Thr Leu Phe Pro Phe Glu Ala Glu 130 135 140 Ala Tyr Arg Asn He Glu Pro Val Tyr Leu Asn Met Leu Leu Glu Lys 145 150 155 160 Leu Cys Val Met Phe Glu Asp Gly Val Leu Met Arg Leu Lys Ser Asp 165 170 175 Leu Leu Lys Ala Ala Leu Cys His Leu Leu Gin Tyr Phe Leu Lys Phe 180 185 190 Val Pro Ala Gly Tyr Glu Ser Ala Leu Gin Val Arg Lys Val Tyr Val 195 200 205 Arg Asn He Cys Lys Ala Leu Leu Asp Val Leu Gly He Glu Val Asp 210 215 220 Ala Glu Tyr Leu Leu Gly Pro Leu Tyr Ala Ala Leu Lys Met Glu Ser 225 230 235 240 Met Glu He He Glu Glu He Gin Cys Gin Thr Gin Gin Glu Asn Leu 245 250 255 Ser Ser Asn Ser Asp Gly He Ser Pro Lys Arg Arg Arg Leu Ser Ser 260 265 270 Ser Leu Asn Pro Ser Lys Arg Ala Pro Lys Gin Thr Glu Glu He Lys 275 280 285 His Val Asp Met Asn Gin Lys Ser He Leu Trp Ser Ala Leu Lys Gin 290 295 300 Lys Ala Glu Ser Leu Gin He Ser Leu Glu Tyr Ser Gly Leu Lys Asn 305 310 315 320 Pro Val He Glu Met Leu Glu Gly He Ala Val Val Leu Gin Leu Thr 325 330 335 Ala Leu Cys Thr Val His Cys Ser His Gin Asn Met Asn Cys Arg Thr 340 345 350 Phe Lys Asp Cys Gin His Lys Ser Lys Lys Lys Pro Ser Val Val He 355 360 365 Thr Trp Met Ser Leu Asp Phe Tyr Thr Thr Val Leu Lys Ser Cys Arg 370 375 380 Arg Leu Leu Glu Ser Val Gin Lys Arg Thr Gly Gly Asn He Asp Lys 385 390 395 400 Val Val Lys He Tyr Asp Ala Leu He Tyr Met Gin Val Asn Ser Ser 405 410 415 Phe Glu Asp His He Leu Glu Asp Leu Cys Gly Met Leu Ser Leu Pro 420 425 430 Trp He Tyr Ser His Ser Asp Asp Gly Cys Leu Lys Leu Thr Thr Phe 435 440 445 Ala Ala Asn Leu Leu Thr Leu Ser Cys Arg He Ser Asp Ser Tyr Ser 450 455 460 Pro Gin Ala Gin Ser Arg Cys Val Phe Leu Leu Thr Leu Phe Pro Arg 465 470 475 480 Arg He Phe Leu Glu Trp Arg Thr Ala Val Tyr Asn Trp Ala Leu Gin 485 490 495 Ser Ser His Glu Val He Arg Ala Ser Cys Val Ser Gly Phe Phe He 500 505 510 Leu Leu Gin Gin Gin Asn Ser Cys Asn Arg Val Pro Lys He Leu He 515 520 525 Asp Lys Val Lys Asp Asp Ser Asp He Val Lys Lys Glu Phe Ala Ser 530 535 540 He Leu Gly Gin Leu Val Cys Thr Leu His Gly Met Phe Tyr Leu Thr 545 550 555 560 Ser Ser Leu Thr Glu Pro Phe Ser Glu His Gly His Val Asp Leu Phe 565 570 575 Cys Arg Asn Leu Lys Ala Thr Ser Gin His Glu Cys Ser Ser Ser Gin 580 585 590 Leu Lys Ala Ser Val Cys Lys Pro Phe Leu Phe Leu Leu Lys Lys Lys 595 600 605 He Pro Ser Pro Val Lys Leu Ala Phe He Asp Asn Leu His His Leu 610 615 620 Cys Lys His Leu Asp Phe Arg Glu Asp Glu Thr Asp Val Lys Ala Val 625 630 635 640 Leu Gly Thr Leu Leu Asn Leu Met Glu Asp Pro Asp Lys Asp Val Arg 645 650 655 Val Ala Phe Ser Gly Asn He Lys His He Leu Glu Ser Leu Asp Ser 660 665 670 Glu Asp Gly Phe He Lys Glu Leu Phe Val Leu Arg Met Lys Glu Ala 675 680 685 Tyr Thr His Ala Gin He Ser Arg Asn Asn Glu Leu Lys Asp Thr Leu 690 695 700 He Leu Thr Thr Gly Asp He Gly Arg Ala Ala Lys Gly Asp Leu Val 705 710 715 720 Pro Phe Ala Leu Leu His Leu Leu His Cys Leu Leu Ser Lys Ser Ala 725 730 735 Ser Val Ser Gly Ala Ala Tyr Thr Glu He Arg Ala Leu Val Ala Ala 740 745 750 Lys Ser Val Lys Leu Gin Ser Phe Phe Ser Gin Tyr Lys Lys Pro He 755 760 765 Cys Gin Phe Leu Val Glu Ser Leu His Ser Ser Gin Met Thr Ala Leu 770 775 780 Pro Asn Thr Pro Cys Gin Asn Ala Asp Val Arg Lys Gin Asp Val Ala 785 790 795 800 His Gin Arg Glu Met Ala Leu Asn Thr Leu Ser Glu He Ala Asn Val 805 810 815 Phe Asp Phe Pro Asp Leu Asn Arg Phe Leu Thr Arg Thr Leu Gin Val 820 825 830 Leu Leu Pro Asp Leu Ala Ala Lys Ala Ser Pro Ala Ala Ser Ala Leu 835 840 845 He Arg Thr Leu Gly Lys Gin Leu Asn Val Asn Arg Arg Glu He Leu 850 855 860 He Asn Asn Phe Lys Tyr He Phe Ser His Leu Val Cys Ser Cys Ser 865 870 875 880 Lys Asp Glu Leu Glu Arg Ala Leu His Tyr Leu Lys Asn Glu Thr Glu 885 890 895 He Glu Leu Gly Ser Leu Leu Arg Gin Asp Phe Gin Gly Leu His Asn 900 905 910 Glu Leu Leu Leu Arg He Gly Glu His Tyr Gin Gin Val Phe Asn Gly 915 920 925 Leu Ser He Leu Ala Ser Phe Ala Ser Ser Asp Asp Pro Tyr Gin Gly 930 935 940 Pro Arg Asp He He Ser Pro Glu Leu Met Ala Asp Tyr Leu Gin Pro 945 950 955 960 Lys Leu Leu Gly He Leu Ala Phe Phe Asn Met Gin Leu Leu Ser Ser 965 970 975 Ser Val Gly He Glu Asp Lys Lys Met Ala Leu Asn Ser Leu Met Ser 980 985 990 Leu Met Lys Leu Met Gly Pro Lys His Val Ser Ser Val Arg Val Lys 995 1000 1005 Met Met Thr Thr Leu Arg Thr Gly Leu Arg Phe Lys Asp Asp Phe Pro 1010 1015 1020 Glu Leu Cys Cys Arg Ala Trp Asp Cys Phe Val Arg Cys Leu Asp His 1025 1030 1035 1040 Ala Cys Leu Gly Ser Leu Leu Ser His Val He Val Ala Leu Leu Pro 1045 1050 1055 Leu He His He Gin Pro Lys Glu Thr Ala Ala He Phe His Tyr Leu 1060 1065 1070 He He Glu Asn Arg Asp Ala Val Gin Asp Phe Leu His Glu He Tyr 1075 1080 1085 Phe Leu Pro Asp His Pro Glu Leu Lys Lys He Lys Ala Val Leu Gin 1090 1095 1100 Glu Tyr Arg Lys Glu Thr Ser Glu Ser Thr Asp Leu Gin Thr Thr Leu 1105 1110 1115 1120 Gin Leu Ser Met Lys Ala He Gin His Glu Asn Val Asp Val Arg He 1125 1130 1135 His Ala Leu Thr Ser Leu Lys Glu Thr Leu Tyr Lys Asn Gin Glu Lys 1140 1145 1150 Leu He Lys Tyr Ala Thr Asp Ser Glu Thr Val Glu Pro He He Ser 1155 1160 1165 Gin Leu Val Thr Val Leu Leu Lys Gly Cys Gin Asp Ala Asn Ser Gin 1170 1175 1180 Ala Arg Leu Leu Cys Gly Glu Cys Leu Gly Glu Leu Gly Ala He Asp 1185 1190 1195 1200 Pro Gly Arg Leu Asp Phe Ser Thr Thr Glu Thr Gin Gly Lys Asp Phe 1205 1210 1215 Thr Phe Val Thr Gly Val Glu Asp Ser Ser Phe Ala Tyr Gly Leu Leu 1220 1225 1230 Met Glu Leu Thr Arg Ala Tyr Leu Ala Tyr Ala Asp Asn Ser Arg Ala 1235 1240 1245 Pro Asp Ser Ala Ala Tyr Ala He Gin Glu Leu Leu Ser He Tyr Asp 1250 1255 1260 Cys Arg Glu Met Glu Thr Asn Gly Pro Gly His Gin Leu Trp Arg Arg 1265 1270 1275 1280 Phe Pro Glu His Val Arg Glu He Leu Glu Pro His Leu Asn Thr Arg 1285 1290 1295 Tyr Lys Ser Ser Gin Lys Ser Thr Asp Trp Ser Gly Val Lys Lys Pro 1300 1305 1310 He Tyr Leu Ser Lys Leu Gly Ser Asn Phe Ala Glu Trp Ser Ala Ser 1315 1320 1325 Trp Ala Gly Tyr Leu He Thr Lys Val Arg His Asp Leu Ala Ser Lys 1330 1335 1340 He Phe Thr Cys Cys Ser He Met Met Lys His Asp Phe Lys Val Thr 1345 1350 1355 1360 He Tyr Leu Leu Pro His He Leu Val Tyr Val Leu Leu Gly Cys Asn 1365 1370 1375 Gin Glu Asp Gin Gin Glu Val Tyr Ala Glu He Met Ala Val Leu Lys 1380 1385 1390 His Asp Asp Gin His Thr He Asn Thr Gin Asp He Ala Ser Asp Leu 1395 1400 1405 Cys Gin Leu Ser Thr Gin Thr Val Phe Ser Met Leu Asp His Leu Thr 1410 1415 1420 Gin Trp Ala Arg His Lys Phe Gin Ala Leu Lys Ala Glu Lys Cys Pro 1425 1430 1435 1440 His Ser Lys Ser Asn Arg Asn Lys Val Asp Ser Met Val Ser Thr Val 1445 1450 1455 Asp Tyr Glu Asp Tyr Gin Ser Val Thr Arg Phe Leu Asp Leu He Pro 1460 1465 1470 Gin Asp Thr Leu Ala Val Ala Ser Phe Arg Ser Lys Ala Tyr Thr Arg 1475 1480 1485 Ala Val Met His Phe Glu Ser Phe He Thr Glu Lys Lys Gin Asn He 1490 1495 1500 Gin Glu His Leu Gly Phe Leu Gin Lys Leu Tyr Ala Ala Met His Glu 1505 1510 1515 1520 Pro Asp Gly Val Ser Gly Val Ser Ala He Arg Lys Ala Glu Pro Ser 1525 1530 1535 Leu Lys Glu Gin He Leu Glu His Glu Ser Leu Gly Leu Leu Arg Asp 1540 1545 1550 Ala Thr Ala Cys Tyr Asp Arg Ala He Gin Leu Glu Pro Asp Gin He 1555 1560 1565 He His Tyr His Gly Val Val Lys Ser Met Leu Gly Leu Gly Gin Leu 1570 1575 1580 Ser Thr Val He Thr Gin Val Asn Gly Val His Ala Asn Arg Ser Glu 1585 1590 1595 1600 Trp Thr Asp Glu Leu Asn Thr Tyr Arg Val Glu Ala Ala Trp Lyε Leu 1605 1610 1615 Ser Gin Trp Asp Leu Val Glu Asn Tyr Leu Ala Ala Asp Gly Lys Ser 1620 1625 1630 Thr Thr Trp Ser Val Arg Leu Gly Gin Leu Leu Leu Ser Ala Lys Lys 1635 1640 1645 Arg Asp He Thr Ala Phe Tyr Asp Ser Leu Lys Leu Val Arg Ala Glu 1650 1655 1660 Gin He Val Pro Leu Ser Ala Ala Ser Phe Glu Arg Gly Ser Tyr Gin 1665 1670 1675 1680 Arg Gly Tyr Glu Tyr He Val Arg Leu His Met Leu Cys Glu Leu Glu 1685 1690 1695 His Ser He Lys Pro Leu Phe Gin His Ser Pro Gly Asp Ser Ser Gin 1700 1705 1710 Glu Asp Ser Leu Asn Trp Val Ala Arg Leu Glu Met Thr Gin Asn Ser 1715 1720 1725 Tyr Arg Ala Lys Glu Pro He Leu Ala Leu Arg Arg Ala Leu Leu Ser 1730 1735 1740 Leu Asn Lys Arg Pro Asp Tyr Asn Glu Met Val Gly Glu Cys Trp Leu 1745 1750 1755 1760 Gin Ser Ala Arg Val Ala Arg Lys Ala Gly His His Gin Thr Ala Tyr 1765 1770 1775 Asn Ala Leu Leu Asn Ala Gly Glu Ser Arg Leu Ala Glu Leu Tyr Val 1780 1785 1790 Glu Arg Ala Lys Trp Leu Trp Ser Lys Gly Asp Val His Gin Ala Leu 1795 1800 1805 He Val Leu Gin Lys Gly Val Glu Leu Cys Phe Pro Glu Asn Glu Thr 1810 1815 1820 Pro Pro Glu Gly Lys Asn Met Leu He His Gly Arg Ala Met Leu Leu 1825 1830 1835 1840 Val Gly Arg Phe Met Glu Glu Thr Ala Asn Phe Glu Ser Asn Ala He 1845 1850 1855 Met Lys Lys Tyr Lys Asp Val Thr Ala Cys Leu Pro Glu Trp Glu Asp 1860 1865 1870 Gly His Phe Tyr Leu Ala Lys Tyr Tyr Asp Lys Leu Met Pro Met Val 1875 1880 1885 Thr Asp Asn Lys Met Glu Lys Gin Gly Asp Leu He Arg Tyr He Val 1890 1895 1900 Leu His Phe Gly Arg Ser Leu Gin Tyr Gly Asn Gin Phe He Tyr Gin 1905 1910 1915 1920 Ser Met Pro Arg Met Leu Thr Leu Trp Leu Asp Tyr Gly Thr Lys Ala 1925 1930 1935 Tyr Glu Trp Glu Lys Ala Gly Arg Ser Asp Arg Val Gin Met Arg Asn 1940 1945 1950 Asp Leu Gly Lys He Asn Lys Val He Thr Glu His Thr Asn Tyr Leu 1955 1960 1965 Ala Pro Tyr Gin Phe Leu Thr Ala Phe Ser Gin Leu He Ser Arg He 1970 1975 1980 Cys His Ser His Asp Glu Val Phe Val Val Leu Asp Gly Asn Asn Ser 1985 1990 1995 2000 Gln Val Phe Leu Ala Tyr Pro Gin Gin Ala Met Trp Met Met Thr Ala 2005 2010 2015 Val Ser Lys Ser Ser Tyr Pro Met Arg Val Asn Arg Cys Lys Glu He 2020 2025 2030 Leu Asn Lys Ala He His Met Lys Lys Ser Leu Glu Lys Phe Val Gly 2035 2040 2045 Asp Ala Thr Arg Leu Thr Asp Lys Leu Leu Glu Leu Cys Asn Lys Pro 2050 2055 2060 Val Glu He Leu Ala Ser Leu Gin Lys Pro Lys Lys He Ser Leu Lys 2065 2070 2075 2080 Gly Ser Asp Gly Lys Phe Tyr He Met Met Cys Lys Pro Lys Asp Asp 2085 2090 2095 Leu Arg Lys Asp Cys Arg Leu Met Glu Phe Asn Ser Leu He Asn Lys 2100 2105 2110 Cys Leu Arg Lys Asp Ala Glu Ser Arg Arg Arg Glu Leu His He Arg 2115 2120 2125 Thr Tyr Ala Val He Pro Leu Asn Asp Glu Cys Gly He He Glu Trp 2130 2135 2140 Val Asn Asn Thr Ala Gly Leu Arg Pro He Leu Thr Lys Leu Tyr Lys 2145 2150 2155 2160 Glu Lys Gly Val Tyr Met Thr Gly Lys Glu Leu Arg Gin Cys Met Leu 2165 2170 2175 Pro Lys Ser Ala Ala Leu Ser Glu Lys Leu Lys Val Phe Arg Glu Phe 2180 2185 2190 Leu Leu Pro Arg His Pro Pro He Phe His Glu Trp Phe Leu Arg Thr 2195 2200 2205 Phe Pro Asp Pro Thr Ser Trp Tyr Ser Ser Arg Ser Ala Tyr Cys Arg 2210 2215 2220 Ser Thr Ala Val Met Ser Met Val Gly Tyr He Leu Gly Leu Gly Asp 2225 2230 2235 2240 Arg His Gly Glu Asn He Leu Phe Asp Ser Leu Thr Gly Glu Cys Val 2245 2250 2255 His Val Asp Phe Asn Cys Leu Phe Asn Lys Gly Glu Thr Phe Glu Val 2260 2265 2270 Pro Glu He Val Pro Phe Arg Leu Thr His Asn Met Val Asn Gly Met 2275 2280 2285 Gly Pro Met Gly Thr Glu Gly Leu Phe Arg Arg Ala Cys Glu Val Thr 2290 2295 2300 Met Arg Leu Met Arg Asp Gin Arg Glu Pro Leu Met Ser Val Leu Lys 2305 2310 2315 2320 Thr Phe Leu His Asp Pro Leu Val Glu Trp Ser Lys Pro Val Lys Gly 2325 2330 2335 His Ser Lys Ala Pro Leu Asn Glu Thr Gly Glu Val Val Asn Glu Lys 2340 2345 2350 Ala Lys Thr His Val Leu Asp He Glu Gin Arg Leu Gin Gly Val He 2355 2360 2365 Lys Thr Arg Asn Arg Val Thr Gly Leu Pro Leu Ser He Glu Gly His 2370 2375 2380 Val His Tyr Leu He Gin Glu Ala Thr Asp Glu Asn Leu Leu Cys Gin 2385 2390 2395 2400 Met Tyr Leu Gly Trp Thr Pro Tyr Met 2405 (2) INFORMATION FOR SEQ ID NO:3 : (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2835 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: Single (D) TOPOLOGY: linear (il) MOLECULE TYPE: cDNA (vii) IMMEDIATE SOURCE: (B) CLONE: 517 (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 1..2610 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:3: GTG GAA GCA GCT TGG AAA TTG TCA CAG TGG GAT TTG GTG GAA AAC TAT 48 Val Glu Ala Ala Trp Lys Leu Ser Gin Trp Asp Leu Val Glu Asn Tyr 1 5 10 15 TTG GCA GCA GAT GGA AAA TCT ACA ACA TGG AGT GTC AGA CTG GGA CAG 96 Leu Ala Ala Asp Gly Lys Ser Thr Thr Trp Ser Val Arg Leu Gly Gin 20 25 30 CTA TTA TTA TCA GCC AAA AAA AGA GAT ATC ACA GCT TTT TAT GAC TCA 144 Leu Leu Leu Ser Ala Lys Lys Arg Asp He Thr Ala Phe Tyr Asp Ser 35 40 45 CTG AAA CTA GTG AGA GCA GAA CAA ATT GTA CCT CTT TCA GCT GCA AGC 192 Leu Lys Leu Val Arg Ala Glu Gin He Val Pro Leu Ser Ala Ala Ser 50 55 60 TTT GAA AGA GGC TCC TAC CAA CGA GGA TAT GAA TAT ATT GTG AGA TTG 240 Phe Glu Arg Gly Ser Tyr Gin Arg Gly Tyr Glu Tyr He Val Arg Leu 65 70 75 80 CAC ATG TTA TGT GAG TTG GAG CAT AGC ATC AAA CCA CTT TTC CAG CAT 288 His Met Leu Cys Glu Leu Glu His Ser He Lys Pro Leu Phe Gin His 85 90 95 TCT CCA GGT GAC AGT TCT CAA GAA GAT TCT CTA AAC TGG GTA GCT CGA 336 Ser Pro Gly Asp Ser Ser Gin Glu Asp Ser Leu Asn Trp Val Ala Arg 100 105 110 CTA GAA ATG ACC CAG AAT TCC TAC AGA GCC AAG GAG CCT ATC CTG GCT 384 Leu Glu Met Thr Gin Asn Ser Tyr Arg Ala Lys Glu Pro He Leu Ala 115 120 125 CTC CGG AGG GCT TTA CTA AGC CTC AAC AAA AGA CCA GAT TAC AAT GAA 432 Leu Arg Arg Ala Leu Leu Ser Leu Asn Lys Arg Pro Asp Tyr Asn Glu 130 135 140 ATG GTT GGA GAA TGC TGG CTG CAG AGT GCC AGG GTA GCT AGA AAG GCT 480 Met Val Gly Glu Cys Trp Leu Gin Ser Ala Arg Val Ala Arg Lys Ala 145 150 155 160 GGT CAC CAC CAG ACA GCC TAC AAT GCT CTC CTT AAT GCA GGG GAA TCA 528 Gly His His Gin Thr Ala Tyr Asn Ala Leu Leu Asn Ala Gly Glu Ser 165 170 175 CGA CTC GCT GAA CTG TAC GTG GAA AGG GCA AAG TGG CTC TGG TCC AAG 576 Arg Leu Ala Glu Leu Tyr Val Glu Arg Ala Lys Trp Leu Trp Ser Lys 180 185 190 GGT GAT GTT CAC CAG GCA CTA ATT GTT CTT CAA AAA GGT GTT GAA TTA 624 Gly Asp Val His Gin Ala Leu He Val Leu Gin Lys Gly Val Glu Leu 195 200 205 TGT TTT CCT GAA AAT GAA ACC CCA CCT GAG GGT AAG AAC ATG TTA ATC 672 Cys Phe Pro Glu Asn Glu Thr Pro Pro Glu Gly Lys Asn Met Leu He 210 215 220 CAT GGT CGA GCT ATG CTA CTA GTG GGC CGA TTT ATG GAA GAA ACA GCT 720 His Gly Arg Ala Met Leu Leu Val Gly Arg Phe Met Glu Glu Thr Ala 225 230 235 240 AAC TTT GAA AGC AAT GCA ATT ATG AAA AAA TAT AAG GAT GTG ACC GCG 768 Asn Phe Glu Ser Asn Ala He Met Lys Lys Tyr Lys Asp Val Thr Ala 245 250 255 TGC CTG CCA GAA TGG GAG GAT GGG CAT TTT TAC CTT GCC AAG TAC TAT 816 Cys Leu Pro Glu Trp Glu Asp Gly His Phe Tyr Leu Ala Lys Tyr Tyr 260 265 270 GAC AAA TTG ATG CCC ATG GTC ACA GAC AAC AAA ATG GAA AAG CAA GGT 864 Asp Lys Leu Met Pro Met Val Thr Asp Asn Lys Met Glu Lys Gin Gly 275 280 285 GAT CTC ATC CGG TAT ATA GTT CTT CAT TTT GGC AGA TCT CTA CAA TAT 912 Asp Leu He Arg Tyr He Val Leu His Phe Gly Arg Ser Leu Gin Tyr 290 295 300 GGA AAT CAG TTC ATA TAT CAG TCA ATG CCA CGA ATG TTA ACT CTA TGG 960 Gly Asn Gin Phe He Tyr Gin Ser Met Pro Arg Met Leu Thr Leu Trp 305 310 315 320 CTT GAT TAT GGT ACA AAG TCA TAT GAA TGG GAA AAA GCT GGC CGC TCC 1008 Leu Asp Tyr Gly Thr Lys Ser Tyr Glu Trp Glu Lys Ala Gly Arg Ser 325 330 335 GAT CGT GTA CAA ATG AGG AAT GAT TTG GGT AAA ATA AAC AAG GTT ATC 1056 Asp Arg Val Gin Met Arg Asn Asp Leu Gly Lys He Asn Lys Val He 340 345 350 ACA GAG CAT ACA AAC TAT TTA GCT CCA TAT CAA TTT TTG ACT GCT TTT 1104 Thr Glu His Thr Asn Tyr Leu Ala Pro Tyr Gin Phe Leu Thr Ala Phe 355 360 365 TCA CAA TTG ATC TCT CGA ATT TGT CAT TCT CAC GAT GAA GTT TTT GTT 1152 Ser Gin Leu He Ser Arg He Cys His Ser His Asp Glu Val Phe Val 370 375 380 GTC TTG ATG GAA ATA ATA GCC AAA GTA TTT CTA GCC TAT CCT CAA CAA 1200 Val Leu Met Glu He He Ala Lys Val Phe Leu Ala Tyr Pro Gin Gin 385 390 395 400 GCA ATG TGG ATG ATG ACA GCT GTG TCA AAG TCA TCT TAT CCC ATG CGT 1248 Ala Met Trp Met Met Thr Ala Val Ser Lys Ser Ser Tyr Pro Met Arg 405 410 415 GTG AAC AGA TGC AAG GAA ATC CTC AAT AAA GCT ATT CAT ATG AAA AAA 1296 Val Asn Arg Cys Lys Glu He Leu Asn Lys Ala He His Met Lys Lys 420 425 430 TCC TTA GAG AAG TTT GTT GGA GAT GCA ACT CGC CTA ACA GAT AAG CTT 1344 Ser Leu Glu Lys Phe Val Gly Asp Ala Thr Arg Leu Thr Asp Lys Leu 435 440 445 CTA GAA TTG TGC AAT AAA CCG GTT GAT GGA AGT AGT TCC ACA TTA AGC 1392 Leu Glu Leu Cys Asn Lys Pro Val Asp Gly Ser Ser Ser Thr Leu Ser 450 455 460 ATG AGC ACT CAT TTT AAA ATG CTT AAA AAG CTG GTA GAA GAA GCA ACA 1440 Met Ser Thr His Phe Lys Met Leu Lys Lys Leu Val Glu Glu Ala Thr 465 470 475 480 TTT AGT GAA ATC CTC ATT CCT CTA CAA TCA GTC ATG ATA CCT ACA CTT 1488 Phe Ser Glu He Leu He Pro Leu Gin Ser Val Met He Pro Thr Leu 485 490 495 CCA TCA ATT CTG GGT ACC CAT GCT AAC CAT GCT AGC CAT GAA CCA TTT 1536 Pro Ser He Leu Gly Thr His Ala Asn His Ala Ser His Glu Pro Phe 500 505 510 CCT GGA CAT TGG GCC TAT ATT GCA GGG TTT GAT GAT ATG GTG GAA ATT 1584 Pro Gly His Trp Ala Tyr He Ala Gly Phe Asp Asp Met Val Glu He 515 520 525 CTT GCT TCT CTT CAG AAA CCA AAG AAG ATT TCT TTA AAA GGC TCA GAT 1632 Leu Ala Ser Leu Gin Lys Pro Lys Lys He Ser Leu Lys Gly Ser Asp 530 535 540 GGA AAG TTC TAC ATC ATG ATG TGT AAG CCA AAA GAT GAC CTG AGA AAG 1680 Gly Lys Phe Tyr He Met Met Cys Lys Pro Lys Asp Asp Leu Arg Lys 545 550 555 560 GAT TGT AGA CTA ATG GAA TTC AAT TCC TTG ATT AAT AAG TGC TTA AGA 1728 Asp Cys Arg Leu Met Glu Phe Asn Ser Leu He Asn Lys Cys Leu Arg 565 570 575 AAA GAT GCA GAG TCT CGT AGA AGA GAA CTT CAT ATT CGA ACA TAT GCA 1776 Lys Asp Ala Glu Ser Arg Arg Arg Glu Leu His He Arg Thr Tyr Ala 580 585 590 GTT ATT CCA CTA AAT GAT GAA TGT GGG ATT ATT GAA TGG GTG AAC AAC 1824 Val He Pro Leu Asn Asp Glu Cys Gly He He Glu Trp Val Asn Asn 595 600 605 ACT GCT GGT TTG AGA CCT ATT CTG ACC AAA CTA TAT AAA GAA AAG GGA 1872 Thr Ala Gly Leu Arg Pro He Leu Thr Lys Leu Tyr Lys Glu Lys Gly 610 615 620 GTG TAT ATG ACA GGA AAA GAA CTT CGC CAG TGT ATG CTA CCA AAG TCA 1920 Val Tyr Met Thr Gly Lys Glu Leu Arg Gin Cys Met Leu Pro Lys Ser 625 630 635 640 GCA GCT TTA TCT GAA AAA CTC AAA GTA TTC CGA GAA TTT CTC CTG CCC 1968 Ala Ala Leu Ser Glu Lys Leu Lys Val Phe Arg Glu Phe Leu Leu Pro 645 650 655 AGG CAT CCT CCT ATT TTT CAT GAG TGG TTT CTG AGA ACA TTC CCT GAT 2016 Arg His Pro Pro He Phe His Glu Trp Phe Leu Arg Thr Pne Pro Asp 660 665 670 CCT ACA TCA TGG TAC AGT AGT AGA TCA GCT TAC TGC CGT TCC ACT GCA 2064 Pro Thr Ser Trp Tyr Ser Ser Arg Ser Ala Tyr Cys Arg Ser Thr Ala 675 680 685 GTA ATG TCA ATG GTT GGT TAT ATT CTG GGG CTT GGA GAC CGT CAT GGT 2112 Val Met Ser Met Val Gly Tyr He Leu Gly Leu Gly Asp Arg His Gly 690 695 700 GAA AAT ATT CTC TTT GAT TCT TTG ACT GGT GAA TGC GTA CAT GTA GAT 2160 Glu Asn He Leu Phe Asp Ser Leu Thr Gly Glu Cys Val His Val Asp 705 710 715 720 TTC AAT TGT CTT TTC AAT AAG GGA GAA ACC TTT GAA GTT CCA GAA ATT 2208 Phe Asn Cys Leu Phe Asn Lys Gly Glu Thr Phe Glu Val Pro Glu He 725 730 735 GTG CCA TTT CGC CTG ACT CAT AAT ATG GTT AAT GGA ATG GGT CCT ATG 2256 Val Pro Phe Arg Leu Thr His Asn Met Val Asn Gly Met Gly Pro Met 740 745 750 GGA ACA GAG GGT CTT TTT CGA AGA GCA TGT GAA GTT ACA ATG AGG CTG 2304 Gly Thr Glu Gly Leu Phe Arg Arg Ala Cys Glu Val Thr Met Arg Leu 755 760 765 ATG CGT GAT CAG CGA GAG CCT TTA ATG AGT GTC TTA AAG ACT TTT CTA 2352 Met Arg Asp Gin Arg Glu Pro Leu Met Ser Val Leu Lys Thr Phe Leu 770 775 780 CAT GAT CCT CTT GTG GAA TGG AGT AAA CCA GTG AAA GGG CAT TCC AAA 2400 His Asp Pro Leu Val Glu Trp Ser Lys Pro Val Lys Gly His Ser Lys 785 790 795 800 GCG CCA CTG AAT GAA ACT GGA GAA GTT GTC AAT GAA AAG GCC AAG ACC 2448 Ala Pro Leu Asn Glu Thr Gly Glu Val Val Asn Glu Lys Ala Lys Thr 805 810 815 CAT GTT CTT GAC ATT GAG CAG CGA CTA CAA GGT GTA ATC AAG ACT CGA 2496 His Val Leu Asp He Glu Gin Arg Leu Gin Gly Val He Lys Thr Arg 820 825 830 AAT AGA GTG ACA GGA CTG CCG TTA TCT ATT GAA GGA CAT GTG CAT TAC 2544 Asn Arg Val Thr Gly Leu Pro Leu Ser He Glu Gly His Val His Tyr 835 840 845 CTT ATA CAA GAA GCT ACT GAT GAA AAC TTA CTA TGC CAG ATG TAT CTT 2592 Leu He Gin Glu Ala Thr Asp Glu Asn Leu Leu Cys Gin Met Tyr Leu 850 855 860 GGT TGG ACT CCA TAT ATG TGAAATGAAA TTATGTAAAA GAATATGTTA 2640 Gly Trp Thr Pro Tyr Met 865 870 ATAATCTAAA AGTAATGCAT TTGGTATGAA TCTGTGGTTG TATCTGTTCA ATTCTAAAGT 2700 ACAACATAAA TTTACGTTCT CAGCAACTGT TATTTCTCTC TGATCATTAA TTATATGTAA 2760 AATAATATAC ATTCAGTTAT TAAGAAATAA ACTGCTTTCT TAATAAAAAA AAAAAAAAAA 2820 AAAAAAAAAA AAAAA 2835 (2) INFORMATION FOR SEQ ID NO:4 : (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 870 ammo acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:4: Val Glu Ala Ala Trp Lys Leu Ser Gin Trp Asp Leu Val Glu Asn Tyr 1 5 10 15 Leu Ala Ala Asp Gly Lys Ser Thr Thr Trp Ser Val Arg Leu Gly Gin 20 25 30 Leu Leu Leu Ser Ala Lys Lys Arg Asp He Thr Ala Phe Tyr Asp Ser 35 40 45 Leu Lys Leu Val Arg Ala Glu Gin He Val Pro Leu Ser Ala Ala Ser 50 55 60 Phe Glu Arg Gly Ser Tyr Gin Arg Gly Tyr Glu Tyr He Val Arg Leu 65 70 75 80 His Met Leu Cys Glu Leu Glu His Ser He Lys Pro Leu Phe Gin His 85 90 95 Ser Pro Gly Asp Ser Ser Gin Glu Asp Ser Leu Asn Trp Val Ala Arg 100 105 110 Leu Glu Met Thr Gin Asn Ser Tyr Arg Ala Lys Glu Pro He Leu Ala 115 120 125 Leu Arg Arg Ala Leu Leu Ser Leu Asn Lys Arg Pro Asp Tyr Asn Glu 130 135 140 Met Val Gly Glu Cys Trp Leu Gin Ser Ala Arg Val Ala Arg Lys Ala 145 150 155 160 Gly His His Gin Thr Ala Tyr Asn Ala Leu Leu Asn Ala Gly Glu Ser 165 170 175 Arg Leu Ala Glu Leu Tyr Val Glu Arg Ala Lys Trp Leu Trp Ser Lys 180 185 190 Gly Asp Val His Gin Ala Leu He Val Leu Gin Lys Gly Val Glu Leu 195 200 205 Cys Phe Pro Glu Asn Glu Thr Pro Pro Glu Gly Lys Asn Met Leu He 210 215 220 His Gly Arg Ala Met Leu Leu Val Gly Arg Phe Met Glu Glu Thr Ala 225 230 235 240 Asn Phe Glu Ser Asn Ala He Met Lys Lys Tyr Lys Asp Val Thr Ala 245 250 255 Cys Leu Pro Glu Trp Glu Asp Gly His Phe Tyr Leu Ala Lys Tyr Tyr 260 265 270 Asp Lys Leu Met Pro Met Val Thr Asp Asn Lys Met Glu Lys Gin Gly 275 280 285 Asp Leu He Arg Tyr He Val Leu His Phe Gly Arg Ser Leu Gin Tyr 290 295 300 Gly Asn Gin Phe He Tyr Gin Ser Met Pro Arg Met Leu Thr Leu Trp 305 310 315 320 Leu Asp Tyr Gly Thr Lys Ser Tyr Glu Trp Glu Lys Ala Gly Arg Ser 325 330 335 Asp Arg Val Gin Met Arg Asn Asp Leu Gly Lys He Asn Lys Val He 340 345 350 Thr Glu His Thr Asn Tyr Leu Ala Pro Tyr Gin Phe Leu Thr Ala Phe 355 360 365 Ser Gin Leu He Ser Arg He Cys His Ser His Asp Glu Val Phe Val 370 375 380 Val Leu Met Glu He He Ala Lys Val Phe Leu Ala Tyr Pro Gin Gin 385 390 395 400 Ala Met Trp Met Met Thr Ala Val Ser Lys Ser Ser Tyr Pro Met Arg 405 410 415 Val Asn Arg Cys Lys Glu He Leu Asn Lys Ala He His Met Lys Lys 420 425 430 Ser Leu Glu Lys Phe Val Gly Asp Ala Thr Arg Leu Thr Asp Lys Leu 435 440 445 Leu Glu Leu Cys Asn Lys Pro Val Asp Gly Ser Ser Ser Thr Leu Ser 450 455 460 Met Ser Thr His Phe Lys Met Leu Lys Lys Leu Val Glu Glu Ala Thr 465 470 475 480 Phe Ser Glu He Leu He Pro Leu Gin Ser Val Met He Pro Thr Leu 485 490 495 Pro Ser He Leu Gly Thr His Ala Asn His Ala Ser His Glu Pro Phe 500 505 510 Pro Gly His Trp Ala Tyr He Ala Gly Phe Asp Asp Met Val Glu He 515 520 525 Leu Ala Ser Leu Gin Lys Pro Lys Lys He Ser Leu Lys Gly Ser Asp 530 535 540 Gly Lys Phe Tyr He Met Met Cys Lys Pro Lys Asp Asp Leu Arg Lys 545 550 555 560 Asp Cys Arg Leu Met Glu Phe Asn Ser Leu He Asn Lys Cys Leu Arg 565 570 575 Lys Asp Ala Glu Ser Arg Arg Arg Glu Leu His He Arg Thr Tyr Ala 580 585 590 Val He Pro Leu Asn Asp Glu Cys Gly He He Glu Trp Val Asn Asn 595 600 605 Thr Ala Gly Leu Arg Pro He Leu Thr Lys Leu Tyr Lys Glu Lys Gly 610 615 620 Val Tyr Met Thr Gly Lys Glu Leu Arg Gin Cys Met Leu Pro Lys Ser 625 630 635 640 Ala Ala Leu Ser Glu Lys Leu Lys Val Phe Arg Glu Phe Leu Leu Pro 645 650 655 Arg His Pro Pro He Phe His Glu Trp Phe Leu Arg Thr Phe Pro Asp 660 665 670 Pro Thr Ser Trp Tyr Ser Ser Arg Ser Ala Tyr Cys Arg Ser Thr Ala 675 680 685 Val Met Ser Met Val Gly Tyr He Leu Gly Leu Gly Asp Arg His Gly 690 695 700 Glu Asn He Leu Phe Asp Ser Leu Thr Gly Glu Cys Val His Val Asp 705 710 715 720 Phe Asn Cys Leu Phe Asn Lys Gly Glu Thr Phe Glu Val Pro Glu He 725 730 735 Val Pro Phe Arg Leu Thr His Asn Met Val Asn Gly Met Gly Pro Met 740 745 750 Gly Thr Glu Gly Leu Phe Arg Arg Ala Cys Glu Val Thr Met Arg Leu 755 760 765 Met Arg Asp Gin Arg Glu Pro Leu Met Ser Val Leu Lys Thr Phe Leu 770 775 780 His Asp Pro Leu Val Glu Trp Ser Lys Pro Val Lys Gly His Ser Lys 785 790 795 800 Ala Pro Leu Asn Glu Thr Gly Glu Val Val Asn Glu Lys Ala Lys Thr 805 810 815 His Val Leu Asp He Glu Gin Arg Leu Gin Gly Val He Lys Thr Arg 820 825 830 Asn Arg Val Thr Gly Leu Pro Leu Ser He Glu Gly His Val His Tyr 835 840 845 Leu He Gin Glu Ala Thr Asp Glu Asn Leu Leu Cys Gin Met Tyr Leu 850 855 860 Gly Trp Thr Pro Tyr Met 865 870 (2) INFORMATION FOR SEQ ID NO: 5 : (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 33 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (li) MOLECULE TYPE: DNA (vn) IMMEDIATE SOURCE: (B) CLONE: Primer oDH15a (ix) FEATURE: (A) NAME/KEY: modified_base (B) LOCATION: group(15, 18, 24, 30) (D) OTHER INFORMATION: The nucleotides at these positions are mosmes. (xι) SEQUENCE DESCRIPTION: SEQ ID NO:5 : GCAGACGGAT CCGGNWCNGA YGGNAAYHTN TAY 33 (2) INFORMATION FOR SEQ ID NO: 6 : (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 27 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (ix) FEATURE: (A) NAME/KEY: odified_base (B) LOCATION: group (15, 18, 24) (D) OTHER INFORMATION: The nucleotides at these positions are inoεmes . (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 6 : GCAGACGGAT CCGGNWCNGA YGGNAAY 27 (2) INFORMATION FOR SEQ ID NO: 7 : (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 30 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (vii) IMMEDIATE SOURCE: (B) CLONE: Primer 0DHI6 (ix) FEATURE: (A) NAME/KEY: modified_base (B) LOCATION: 24 (D) OTHER INFORMATION: The nucleotides at these positions are inosines. (xi) SEQUENCE DESCRIPTION: SEQ ID NO:7 : GCAGACGAAT TCRCARTYRA ARTCNACRTG 30 (2) INFORMATION FOR SEQ ID NO:8 : (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 41 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (li) MOLECULE TYPE: DNA (vii) IMMEDIATE SOURCE: (B) CLONE: Primer oDH17a (ix) FEATURE (A) NAME/KEY modifιed_base (B) LOCATION group (21, 24, 27, 30) (D) OTHER INFORMATION The nucleotides at these positions are mosines (xi) SEQUENCE DESCRIPTION SEQ ID NO 8 GCAGACGGAT CCAARTTYCC NCCNRTNYTN TAYSARTGGT T 41 (2) INFORMATION FOR SEQ ID NO 9 (l) SEQUENCE CHARACTERISTICS (A) LENGTH 41 base pairs (B) TYPE nucleic acid (C) STRANDEDNESS single (D) TOPOLOGY linear (ii) MOLECULE TYPE DNA (vii) IMMEDIATE SOURCE (B) CLONE Primer oDH17b (ix) FEATURE (A) NAME/KEY modifιed_base (B) LOCATION group (24, 27, 30, 33) (D) OTHER INFORMATION The nucleotides at these positions are mosines (xi) SEQUENCE DESCRIPTION SEQ ID NO 9 GCAGACGAAT CCAACCAYTS RTANARNAYN GGNGGRAAYT T 41 (2) INFORMATION FOR SEQ ID NO 10 (l) SEQUENCE CHARACTERISTICS (A) LENGTH 32 base pairs (B) TYPE nucleic acid (C) STRANDEDNESS single (D) TOPOLOGY linear (ii) MOLECULE TYPE DNA (vii) IMMEDIATE SOURCE (B) CLONE Primer oDHlθa (ix) FEATURE (A) NAME/KEY modifιed_base (B) LOCATION group (15, 18, 21, 24, 30) (D) OTHER INFORMATION The nucleotides at these positions are mosines (xi) SEQUENCE DESCRIPTION SEQ ID NO 10 GCAGACGGAT CCYTNGGNYT NGGNGAYCGN CA 32 (2) INFORMATION FOR SEQ ID NO:11: (l) SEQUENCE CHARACTERISTICS (A) LENGTH- 32 base pairs (B) TYPE, nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear In) MOLECULE TYPE. DNA (vii) IMMEDIATE SOURCE- (B) CLONE- Primer oDHlβb (ix) FEATURE (A) NAME/KEY: modifιed_baεe (B) LOCATION: group (15, 18, 21) (D) OTHER INFORMATION. The nucleotides at these positions are osines (xi) SEQUENCE DESCRIPTION. SEQ ID NO:11: GCAGACGGAT CCYTNGGNYT NGGNGAYAGR CA 32 (2) INFORMATION FOR SEQ ID NO:12 (l) SEQUENCE CHARACTERISTICS (A) LENGTH 33 base pairs (B) TYPE, nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY linear (n) MOLECULE TYPE. DNA (vii) IMMEDIATE SOURCE: (B) CLONE: Primer ODH23 (xi) SEQUENCE DESCRIPTION SEQ ID NO.12 GACGCAGAAT TCACCAGTCA AAGAATCAAA GAG 33 (2) INFORMATION FOR SEQ ID NO:13- (l) SEQUENCE CHARACTERISTICS- (A) LENGTH: 16 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY, linear In) MOLECULE TYPE: DNA (vii) IMMEDIATE SOURCE (B) CLONE: Primer mo3 (xi) SEQUENCE DESCRIPTION: SEQ ID N0-13- CTACAGAGCC AAGGAG 16 (2) INFORMATION FOR SEQ ID NO:14: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 22 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (vii) IMMEDIATE SOURCE: (B) CLONE: Primer mo6 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:14: TCGAGCTATG CTACTAGTGG GC 22 (2) INFORMATION FOR SEQ ID NO: 15: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 17 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (vii) IMMEDIATE SOURCE: (B) CLONE: Primer oHT9-l (xi) SEQUENCE DESCRIPTION: SEQ ID NO:15: CCAGTAAACT TGCTTTC 17 (2) INFORMATION FOR SEQ ID NO: 16: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (il) MOLECULE TYPE: DNA (vii) IMMEDIATE SOURCE: (B) CLONE: Primer OHT9-4 (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 16: TTTGCGGCCC TTCCAATATC 20 (2) INFORMATION FOR SEQ ID NO: 17: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 7440 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: Single (D) TOPOLOGY: linear (il) MOLECULE TYPE: cDNA (vii) IMMEDIATE SOURCE: (B) CLONE: MCCSlbeta (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 1..7437 (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 17: ATG GGT CAT GCT GTG GAA TGG CCA GTG GTC ATG AGC CGA TTT TTA AGT 48 Met Gly His Ala Val Glu Trp Pro Val Val Met Ser Arg Phe Leu Ser 1 5 10 15 CAA TTA GAT GAA CAC ATG GGA TAT TTA CAA TCA GCT CCT TTG CAG TTG 96 Gin Leu Asp Glu His Met Gly Tyr Leu Gin Ser Ala Pro Leu Gin Leu 20 25 30 ATG AGT ATG CAA AAA TTA GAA TTT ATT GAA GTC ACT TTA TTA ACG GTT 144 Met Ser Met Gin Lys Leu Glu Phe He Glu Val Thr Leu Leu Thr Val 35 40 45 CTT ACT CGT ATT ATT GCA ATT GTG TTT TTT AGA AGG CAA GAA CTC TTA 192 Leu Thr Arg He He Ala He Val Phe Phe Arg Arg Gin Glu Leu Leu 50 55 60 CTT TGG CAG ATA GGT TGT GTT CTG CTA GAG TAT GGT AGT CCA AAA ATT 240 Leu Trp Gin He Gly Cys Val Leu Leu Glu Tyr Gly Ser Pro Lys He 65 70 75 80 AAA TCC CTA GCA ATT AGC TTT TTA ACA GAA CTT TTT CAG CTT GGA GGA 288 Lys Ser Leu Ala He Ser Phe Leu Thr Glu Leu Phe Gin Leu Gly Gly 85 90 95 CTA CCA GCA CAA CCA GCT AGC ACT TTT TTC AGC TCA TTT TTG GAA TTA 336 Leu Pro Ala Gin Pro Ala Ser Thr Phe Phe Ser Ser Phe Leu Glu Leu 100 105 110 TTA AAA CAC CTT GTA GAA ATG GAT ACT GAC CAA TTG AAA CTC TAT GAA 384 Leu Lys His Leu Val Glu Met Asp Thr Asp Gin Leu Lys Leu Tyr Glu 115 120 125 GAG CCA TTA TCA AAG CTG ATA AAG ACA CTA TTT CCC TTT GAA GCA GAA 432 Glu Pro Leu Ser Lys Leu He Lys Thr Leu Phe Pro Phe Glu Ala Glu 130 135 140 GCT TAT AGA AAT ATT GAA CCT GTC TAT TTA AAT ATG CTG CTG GAA AAA 480 Ala Tyr Arg Asn He Glu Pro Val Tyr Leu Asn Met Leu Leu Glu Lys 145 150 155 160 CTC TGT GTC ATG TTT GAA GAC GGT GTG CTC ATG CGG CTT AAG TCT GAT 528 Leu Cys Val Met Phe Glu Asp Gly Val Leu Met Arg Leu Lys Ser Asp 165 170 175 TTG CTA AAA GCA GCT TTG TGC CAT TTA CTG CAG TAT TTC CTT AAA TTT 576 Leu Leu Lys Ala Ala Leu Cys His Leu Leu Gin Tyr Phe Leu Lys Phe 180 185 190 GTG CCA GCT GGG TAT GAA TCT GCT TTA CAA GTC AGG AAG GTC TAT GTG 624 Val Pro Ala Gly Tyr Glu Ser Ala Leu Gin Val Arg Lys Val Tyr Val 195 200 205 AGA AAT ATT TGT AAA GCT CTT TTG GAT GTG CTT GGA ATT GAG GTA GAT 672 Arg Asn He Cys Lys Ala Leu Leu Asp Val Leu Gly He Glu Val Asp 210 215 220 GCA GAG TAC TTG TTG GGC CCA CTT TAT GCA GCT TTG AAA ATG GAA AGT 720 Ala Glu Tyr Leu Leu Gly Pro Leu Tyr Ala Ala Leu Lys Met Glu Ser 225 230 235 240 ATG GAA ATC ATT GAG GAG ATT CAA TGC CAA ACT CAA CAG GAA AAC CTC 768 Met Glu He He Glu Glu He Gin Cys Gin Thr Gin Gin Glu Asn Leu 245 250 255 AGC AGT AAT AGT GAT GGA ATA TCA CCC AAA AGG CGT CGT CTC AGC TCG 816 Ser Ser Asn Ser Asp Gly He Ser Pro Lys Arg Arg Arg Leu Ser Ser 260 265 270 TCT CTA AAC CCT TCT AAA AGA GCA CCA AAA CAG ACT GAG GAA ATT AAA 864 Ser Leu Asn Pro Ser Lys Arg Ala Pro Lys Gin Thr Glu Glu He Lys 275 280 285 CAT GTG GAC ATG AAC CAA AAG AGC ATA TTA TGG AGT GCA CTG AAA CAG 912 His Val Asp Met Asn Gin Lys Ser He Leu Trp Ser Ala Leu Lys Gin 290 295 300 AAA GCT GAA TCC CTT CAG ATT TCC CTT GAA TAC AGT GGC CTA AAG AAT 960 Lys Ala Glu Ser Leu Gin He Ser Leu Glu Tyr Ser Gly Leu Lys Asn 305 310 315 320 CCT GTT ATT GAG ATG TTA GAA GGA ATT GCT GTT GTC TTA CAA CTG ACT 1008 Pro Val He Glu Met Leu Glu Gly He Ala Val Val Leu Gin Leu Thr 325 330 335 GCT CTG TGT ACT GTT CAT TGT TCT CAT CAA AAC ATG AAC TGC CGT ACT 1056 Ala Leu Cys Thr Val His Cys Ser His Gin Asn Met Asn Cys Arg Thr 340 345 350 TTC AAG GAC TGT CAA CAT AAA TCC AAG AAG AAA CCT TCT GTA GTG ATA 1104 Phe Lys Asp Cys Gin His Lys Ser Lys Lys Lys Pro Ser Val Val He 355 360 365 ACT TGG ATG TCA TTG GAT TTT TAC ACA ACA GTG CTT AAG AGC TGT AGA 1152 Thr Trp Met Ser Leu Asp Phe Tyr Thr Thr Val Leu Lys Ser Cys Arg 370 375 380 AGG TTG TTA GAA TCT GTT CAG AAA CGG ACT GGA GGC AAC ATT GAT AAG 1200 Arg Leu Leu Glu Ser Val Gin Lys Arg Thr Gly Gly Asn He Asp Lys 385 390 395 400 GTG GTG AAA ATT TAT GAT GCT TTG ATT TAT ATG CAA GTA AAC AGT TCA 1248 Val Val Lys He Tyr Asp Ala Leu He Tyr Met Gin Val Asn Ser Ser 405 410 415 TTT GAA GAT CAT ATC CTG GAA GAT TTA TGT GGA ATG CTC TCA CTT CCA 1296 Phe Glu Asp His He Leu Glu Asp Leu Cys Gly Met Leu Ser Leu Pro 420 425 430 TGG ATT TAT TCC CAT TCT GAT GAT GGC TGT TTA AAG TTG ACC ACA TTT 1344 Trp He Tyr Ser His Ser Asp Asp Gly Cys Leu Lys Leu Thr Thr Phe 435 440 445 GCC GCT AAT CTT CTA ACA TTA AGC TGT AGG ATT TCA GAT AGC TAT TCA 1392 Ala Ala Asn Leu Leu Thr Leu Ser Cys Arg He Ser Asp Ser Tyr Ser 450 455 460 CCA CAG GCA CAA TCA CGA TGT GTG TTT CTT CTG ACT CTG TTT CCA AGA 1440 Pro Gin Ala Gin Ser Arg Cys Val Phe Leu Leu Thr Leu Phe Pro Arg 465 470 475 480 AGA ATA TTC CTT GAG TGG AGA ACA GCA GTT TAC AAC TGG GCC CTG CAG 1488 Arg He Phe Leu Glu Trp Arg Thr Ala Val Tyr Asn Trp Ala Leu Gin 485 490 495 AGC TCC CAT GAA GTA ATC CGG GCT AGT TGT GTT AGT GGA TTT TTT ATC 1536 Ser Ser His Glu Val He Arg Ala Ser Cys Val Ser Gly Phe Phe He 500 505 510 TTA TTG CAG CAG CAG AAT TCT TGT AAC AGA GTT CCC AAG ATT CTT ATA 1584 Leu Leu Gin Gin Gin Asn Ser Cys Asn Arg Val Pro Lys He Leu He 515 520 525 GAT AAA GTC AAA GAT GAT TCT GAC ATT GTC AAG AAA GAA TTT GCT TCT 1632 Asp Lys Val Lys Asp Asp Ser Asp He Val Lys Lys Glu Phe Ala Ser 530 535 540 ATA CTT GGT CAA CTT GTC TGT ACT CTT CAC GGC ATG TTT TAT CTG ACA 1680 He Leu Gly Gin Leu Val Cys Thr Leu His Gly Met Phe Tyr Leu Thr 545 550 555 560 AGT TCT TTA ACA GAA CCT TTC TCT GAA CAC GGA CAT GTG GAC CTC TTC 1728 Ser Ser Leu Thr Glu Pro Phe Ser Glu His Gly His Val Asp Leu Phe 565 570 575 TGT AGG AAC TTG AAA GCC ACT TCT CAA CAT GAA TGT TCA TCT TCT CAA 1776 Cys Arg Asn Leu Lys Ala Thr Ser Gin His Glu Cys Ser Ser Ser Gin 580 585 590 CTA AAA GCT TCT GTC TGC AAG CCA TTC CTT TTC CTA CTG AAA AAA AAA 1824 Leu Lys Ala Ser Val Cys Lys Pro Phe Leu Phe Leu Leu Lys Lys Lys 595 600 605 ATA CCT AGT CCA GTA AAA CTT GCT TTC ATA GAT AAT CTA CAT CAT CTT 1872 He Pro Ser Pro Val Lys Leu Ala Phe He Asp Asn Leu His His Leu 610 615 620 TGT AAG CAT CTT GAT TTT AGA GAA GAT GAA ACA GAT GTA AAA GCA GTT 1920 Cys Lys His Leu Asp Phe Arg Glu Asp Glu Thr Asp Val Lys Ala Val 625 630 635 640 CTT GGA ACT TTA TTA AAT TTA ATG GAA GAT CCA GAC AAA GAT GTT AGA 1968 Leu Gly Thr Leu Leu Asn Leu Met Glu Asp Pro Asp Lys Asp Val Arg 645 650 655 GTG GCT TTT AGT GGA AAT ATC AAG CAC ATA TTG GAA TCC TTG GAC TCT 2016 Val Ala Phe Ser Gly Asn He Lys His He Leu Glu Ser Leu Asp Ser 660 665 670 GAA GAT GGA TTT ATA AAG GAG CTT TTT GTC TTA AGA ATG AAG GAA GCA 2064 Glu Asp Gly Phe He Lys Glu Leu Phe Val Leu Arg Met Lys Glu Ala 675 680 685 TAT ACA CAT GCC CAA ATA TCA AGA AAT AAT GAG CTG AAG GAT ACC TTG 2112 Tyr Thr His Ala Gin He Ser Arg Asn Asn Glu Leu Lys Asp Thr Leu 690 695 700 ATT CTT ACA ACA GGG GAT ATT GGA AGG GCC GCA AAA GGA GAT TTG GTA 2160 He Leu Thr Thr Gly Asp He Gly Arg Ala Ala Lys Gly Asp Leu Val 705 710 715 720 CCA TTT GCA CTC TTA CAC TTA TTG CAT TGT TTG TTA TCC AAG TCA GCA 2208 Pro Phe Ala Leu Leu His Leu Leu His Cys Leu Leu Ser Lys Ser Ala 725 730 735 TCT GTC TCT GGA GCA GCA TAC ACA GAA ATT AGA GCT CTG GTT GCA GCT 2256 Ser Val Ser Gly Ala Ala Tyr Thr Glu He Arg Ala Leu Val Ala Ala 740 745 750 AAA AGT GTT AAA CTG CAA AGT TTT TTC AGC CAG TAT AAG AAA CCC ATC 2304 Lys Ser Val Lys Leu Gin Ser Phe Phe Ser Gin Tyr Lys Lys Pro He 755 760 765 TGT CAG TTT TTG GTA GAA TCC CTT CAC TCT AGT CAG ATG ACA GCA CTT 2352 Cys Gin Phe Leu Val Glu Ser Leu His Ser Ser Gin Met Thr Ala Leu 770 775 780 CCG AAT ACT CCA TGC CAG AAT GCT GAC GTG CGA AAA CAA GAT GTG GCT 2400 Pro Asn Thr Pro Cys Gin Asn Ala Asp Val Arg Lys Gin Asp Val Ala 785 790 795 800 CAC CAG AGA GAA ATG GCT TTA AAT ACG TTG TCT GAA ATT GCC AAC GTT 2448 His Gin Arg Glu Met Ala Leu Asn Thr Leu Ser Glu He Ala Asn Val 805 810 815 TTC GAC TTT CCT GAT CTT AAT CGT TTT CTT ACT AGG ACA TTA CAA GTT 2496 Phe Asp Phe Pro Asp Leu Asn Arg Phe Leu Thr Arg Thr Leu Gin Val 820 825 830 CTA CTA CCT GAT CTT GCT GCC AAA GCA AGC CCT GCA GCT TCT GCT CTC 2544 Leu Leu Pro Asp Leu Ala Ala Lys Ala Ser Pro Ala Ala Ser Ala Leu 835 840 845 ATT CGA ACT TTA GGA AAA CAA TTA AAT GTC AAT CGT AGA GAG ATT TTA 2592 He Arg Thr Leu Gly Lys Gin Leu Asn Val Asn Arg Arg Glu He Leu 850 855 860 ATA AAC AAC TTC AAA TAT ATT TTT TCT CAT TTG GTC TGT TCT TGT TCC 2640 He Asn Asn Phe Lys Tyr He Phe Ser His Leu Val Cys Ser Cys Ser 865 870 875 880 AAA GAT GAA TTA GAA CGT GCC CTT CAT TAT CTG AAG AAT GAA ACA GAA 2688 Lys Asp Glu Leu Glu Arg Ala Leu His Tyr Leu Lys Asn Glu Thr Glu 885 890 895 ATT GAA CTG GGG AGC CTG TTG AGA CAA GAT TTC CAA GGA TTG CAT AAT 2736 He Glu Leu Gly Ser Leu Leu Arg Gin Asp Phe Gin Gly Leu His Asn 900 905 910 GAA TTA TTG CTG CGT ATT GGA GAA CAC TAT CAA CAG GTT TTT AAT GGT 2784 Glu Leu Leu Leu Arg He Gly Glu His Tyr Gin Gin Val Phe Asn Gly 915 920 925 TTG TCA ATA CTT GCC TCA TTT GCA TCC AGT GAT GAT CCA TAT CAG GGC 2832 Leu Ser He Leu Ala Ser Phe Ala Ser Ser Asp Asp Pro Tyr Gin Gly 930 935 940 CCG AGA GAT ATC ATA TCA CCT GAA CTG ATG GCT GAT TAT TTA CAA CCC 2880 Pro Arg Asp He He Ser Pro Glu Leu Met Ala Asp Tyr Leu Gin Pro 945 950 955 960 AAA TTG TTG GGC ATT TTG GCT TTT TTT AAC ATG CAG TTA CTG AGC TCT 2928 Lys Leu Leu Gly He Leu Ala Phe Phe Asn Met Gin Leu Leu Ser Ser 965 970 975 AGT GTT GGC ATT GAA GAT AAG AAA ATG GCC TTG AAC AGT TTG ATG TCT 2976 Ser Val Gly He Glu Asp Lys Lys Met Ala Leu Asn Ser Leu Met Ser 980 985 990 TTG ATG AAG TTA ATG GGA CCC AAA CAT GTC AGT TCT GTG AGG GTG AAG 3024 Leu Met Lys Leu Met Gly Pro Lys His Val Ser Ser Val Arg Val Lys 995 1000 1005 ATG ATG ACC ACA CTG AGA ACT GGC CTT CGA TTC AAG GAT GAT TTT CCT 3072 Met Met Thr Thr Leu Arg Thr Gly Leu Arg Phe Lys Asp Asp Phe Pro 1010 1015 1020 GAA TTG TGT TGC AGA GCT TGG GAC TGC TTT GTT CGC TGC CTG GAT CAT 3120 Glu Leu Cys Cys Arg Ala Trp Asp Cys Phe Val Arg Cys Leu Asp His 1025 1030 1035 1040 GCT TGT CTG GGC TCC CTT CTC AGT CAT GTA ATA GTA GCT TTG TTA CCT 3168 Ala Cys Leu Gly Ser Leu Leu Ser His Val He Val Ala Leu Leu Pro 1045 1050 1055 CTT ATA CAC ATC CAG CCT AAA GAA ACT GCA GCT ATC TTC CAC TAC CTC 3216 Leu He His He Gin Pro Lys Glu Thr Ala Ala He Phe His Tyr Leu 1060 1065 1070 ATA ATT GAA AAC AGG GAT GCT GTG CAA GAT TTT CTT CAT GAA ATA TAT 3264 He He Glu Asn Arg Asp Ala Val Gin Asp Phe Leu His Glu He Tyr 1075 1080 1085 TTT TTA CCT GAT CAT CCA GAA TTA AAA AAG ATA AAA GCC GTT CTC CAG 3312 Phe Leu Pro Asp His Pro Glu Leu Lys Lys He Lys Ala Val Leu Gin 1090 1095 1100 GAA TAC AGA AAG GAG ACC TCT GAG AGC ACT GAT CTT CAG ACA ACT CTT 3360 Glu Tyr Arg Lys Glu Thr Ser Glu Ser Thr Asp Leu Gin Thr Thr Leu 1105 1110 1115 1120 CAG CTC TCT ATG AAG GCC ATT CAA CAT GAA AAT GTC GAT GTT CGT ATT 3408 Gin Leu Ser Met Lys Ala He Gin His Glu Asn Val Asp Val Arg He 1125 1130 1135 CAT GCT CTT ACA AGC TTG AAG GAA ACC TTG TAT AAA AAT CAG GAA AAA 3456 His Ala Leu Thr Ser Leu Lys Glu Thr Leu Tyr Lys Asn Gin Glu Lys 1140 1145 1150 CTG ATA AAG TAT GCA ACA GAC AGT GAA ACA GTA GAA CCT ATT ATC TCA 3504 Leu He Lys Tyr Ala Thr Asp Ser Glu Thr Val Glu Pro He He Ser 1155 1160 1165 CAG TTG GTG ACA GTG CTT TTG AAA GGT TGC CAA GAT GCA AAC TCT CAA 3552 Gin Leu Val Thr Val Leu Leu Lys Gly Cys Gin Asp Ala Asn Ser Gin 1170 1175 1180 GCT CGG TTG CTC TGT GGG GAA TGT TTA GGG GAA TTG GGG GCG ATA GAT 3600 Ala Arg Leu Leu Cys Gly Glu Cys Leu Gly Glu Leu Gly Ala He Asp 1185 1190 1195 1200 CCA GGT CGA TTA GAT TTC TCA ACA ACT GAA ACT CAA GGA AAA GAT TTT 3648 Pro Gly Arg Leu Asp Phe Ser Thr Thr Glu Thr Gin Gly Lys Asp Phe 1205 1210 1215 ACA TTT GTG ACT GGA GTA GAA GAT TCA AGC TTT GCC TAT GGA TTA TTG 3696 Thr Phe Val Thr Gly Val Glu Asp Ser Ser Phe Ala Tyr Gly Leu Leu 1220 1225 1230 ATG GAG CTA ACA AGA GCT TAC CTT GCG TAT GCT GAT AAT AGC CGA GCT 3744 Met Glu Leu Thr Arg Ala Tyr Leu Ala Tyr Ala Asp Asn Ser Arg Ala 1235 1240 1245 CCA GAT TCA GCT GCC TAT GCC ATT CAG GAG TTG CTT TCT ATT TAT GAC 3792 Pro Asp Ser Ala Ala Tyr Ala He Gin Glu Leu Leu Ser He Tyr Asp 1250 1255 1260 TGT AGA GAG ATG GAG ACC AAC GGC CCA GGT CAC CAA TTG TGG AGG AGA 3840 Cys Arg Glu Met Glu Thr Asn Gly Pro Gly His Gin Leu Trp Arg Arg 1265 1270 1275 1280 TTT CCT GAG CAT GTT CGG GAA ATA CTA GAA CCT CAT CTA AAT ACC AGA 3888 Phe Pro Glu His Val Arg Glu He Leu Glu Pro His Leu Asn Thr Arg 1285 1290 1295 TAC AAG AGT TCT CAG AAG TCA ACC GAT TGG TCT GGA GTA AAG AAG CCA 3936 Tyr Lys Ser Ser Gin Lys Ser Thr Asp Trp Ser Gly Val Lys Lys Pro 1300 1305 1310 ATT TAC TTA AGT AAA TTG GGT AGT AAC TTT GCA GAA TGG TCA GCA TCT 3984 He Tyr Leu Ser Lys Leu Gly Ser Asn Phe Ala Glu Trp Ser Ala Ser 1315 1320 1325 TGG GCA GGT TAT CTT ATT ACA AAG GTT CGA CAT GAT CTT GCC AGT AAA 4032 Trp Ala Gly Tyr Leu He Thr Lys Val Arg His Asp Leu Ala Ser Lys 1330 1335 1340 ATT TTC ACC TGC TGT AGC ATT ATG ATG AAG CAT GAT TTC AAA GTG ACC 4080 He Phe Thr Cys Cys Ser He Met Met Lys His Asp Phe Lys Val Thr 1345 1350 1355 1360 ATC TAT CTT CTT CCA CAT ATT CTG GTG TAT GTC TTA CTG GGT TGT AAT 4128 He Tyr Leu Leu Pro His He Leu Val Tyr Val Leu Leu Gly Cys Asn 1365 1370 1375 CAA GAA GAT CAG CAG GAG GTT TAT GCA GAA ATT ATG GCA GTT CTA AAG 4176 Gin Glu Asp Gin Gin Glu Val Tyr Ala Glu He Met Ala Val Leu Lys 1380 1385 1390 CAT GAC GAT CAG CAT ACC ATA AAT ACC CAA GAC ATT GCA TCT GAT CTG 4224 His Asp Asp Gin His Thr He Asn Thr Gin Asp He Ala Ser Asp Leu 1395 1400 1405 TGT CAA CTC AGT ACA CAG ACT GTG TTC TCC ATG CTT GAC CAT CTC ACA 4272 Cys Gin Leu Ser Thr Gin Thr Val Phe Ser Met Leu Asp His Leu Thr 1410 1415 1420 CAG TGG GCA AGG CAC AAA TTT CAG GCA CTG AAA GCT GAG AAA TGT CCA 4320 Gin Trp Ala Arg His Lys Phe Gin Ala Leu Lys Ala Glu Lys Cys Pro 1425 1430 1435 1440 CAC AGC AAA TCA AAC AGA AAT AAG GTA GAC TCA ATG GTA TCT ACT GTG 4368 His Ser Lys Ser Asn Arg Asn Lys Val Asp Ser Met Val Ser Thr Val 1445 1450 1455 GAT TAT GAA GAC TAT CAG AGT GTA ACC CGT TTT CTA GAC CTC ATA CCC 4416 Asp Tyr Glu Asp Tyr Gin Ser Val Thr Arg Phe Leu Asp Leu He Pro 1460 1465 1470 CAG GAT ACT CTG GCA GTA GCT TCC TTT CGC TCC AAA GCA TAC ACA CGA 4464 Gin Asp Thr Leu Ala Val Ala Ser Phe Arg Ser Lys Ala Tyr Thr Arg 1475 1480 1485 GCT GTA ATG CAC TTT GAA TCA TTT ATT ACA GAA AAG AAG CAA AAT ATT 4512 Ala Val Met His Phe Glu Ser Phe He Thr Glu Lys Lys Gin Asn He 1490 1495 1500 CAG GAA CAT CTT GGA TTT TTA CAG AAA TTG TAT GCT GCT ATG CAT GAA 4560 Gin Glu His Leu Gly Phe Leu Gin Lys Leu Tyr Ala Ala Met His Glu 1505 1510 1515 1520 CCT GAT GGA GTG TCC GGA GTC AGT GCA ATT AGA AAG GCA GAA CCA TCT 4608 Pro Asp Gly Val Ser Gly Val Ser Ala He Arg Lys Ala Glu Pro Ser 1525 1530 1535 CTA AAA GAA CAG ATC CTT GAA CAT GAA AGC CTT GGC TTG CTG AGG GAT 4656 Leu Lys Glu Gin He Leu Glu His Glu Ser Leu Gly Leu Leu Arg Asp 1540 1545 1550 GCC ACT GCT TGT TAT GAC AGG GCT ATT CAG CTA GAA CCA GAC CAG ATC 4704 Ala Thr Ala Cys Tyr Asp Arg Ala He Gin Leu Glu Pro Asp Gin He 1555 1560 1565 ATT CAT TAC CAT GGT GTA GTA AAG TCC ATG TTA GGT CTT GGT CAG CTG 4752 He His Tyr His Gly Val Val Lys Ser Met Leu Gly Leu Gly Gin Leu 1570 1575 1580 TCT ACT GTT ATC ACT CAG GTG AAT GGA GTG CAT GCT AAC AGG TCC GAG 4800 Ser Thr Val He Thr Gin Val Asn Gly Val His Ala Asn Arg Ser Glu 1585 1590 1595 1600 TGG ACA GAT GAA TTA AAC ACG TAC AGA GTG GAA GCA GCT TGG AAA TTG 4848 Trp Thr Asp Glu Leu Asn Thr Tyr Arg Val Glu Ala Ala Trp Lys Leu 1605 1610 1615 TCA CAG TGG GAT TTG GTG GAA AAC TAT TTG GCA GCA GAT GGA AAA TCT 4896 Ser Gin Trp Asp Leu Val Glu Asn Tyr Leu Ala Ala Asp Gly Lys Ser 1620 1625 1630 ACA ACA TGG AGT GTC AGA CTG GGA CAG CTA TTA TTA TCA GCC AAA AAA 4944 Thr Thr Trp Ser Val Arg Leu Gly Gin Leu Leu Leu Ser Ala Lys Lys 1635 1640 1645 AGA GAT ATC ACA GCT TTT TAT GAC TCA CTG AAA CTA GTG AGA GCA GAA 4992 Arg Asp He Thr Ala Phe Tyr Asp Ser Leu Lys Leu Val Arg Ala Glu 1650 1655 1660 CAA ATT GTA CCT CTT TCA GCT GCA AGC TTT GAA AGA GGC TCC TAC CAA 5040 Gin He Val Pro Leu Ser Ala Ala Ser Phe Glu Arg Gly Ser Tyr Gin 1665 1670 1675 1680 CGA GGA TAT GAA TAT ATT GTG AGA TTG CAC ATG TTA TGT GAG TTG GAG 5088 Arg Gly Tyr Glu Tyr He Val Arg Leu His Met Leu Cys Glu Leu Glu 1685 1690 1695 CAT AGC ATC AAA CCA CTT TTC CAG CAT TCT CCA GGT GAC AGT TCT CAA 5136 H s Ser He Lys Pro Leu Phe Gin His Ser Pro Gly Asp Ser Ser Gin 1700 1705 1710 GAA GAT TCT CTA AAC TGG GTA GCT CGA CTA GAA ATG ACC CAG AAT TCC 5184 Glu Asp Ser Leu Asn Trp Val Ala Arg Leu Glu Met Thr Gin Asn Ser 1715 1720 1725 TAC AGA GCC AAG GAG CCT ATC CTG GCT CTC CGG AGG GCT TTA CTA AGC 5232 Tyr Arg Ala Lys Glu Pro He Leu Ala Leu Arg Arg Ala Leu Leu Ser 1730 1735 1740 CTC AAC AAA AGA CCA GAT TAC AAT GAA ATG GTT GGA GAA TGC TGG CTG 5280 Leu Asn Lys Arg Pro Asp Tyr Asn Glu Met Val Gly Glu Cys Trp Leu 1745 1750 1755 1760 CAG AGT GCC AGG GTA GCT AGA AAG GCT GGT CAC CAC CAG ACA GCC TAC 5328 Gin Ser Ala Arg Val Ala Arg Lys Ala Gly His His Gin Thr Ala Tyr 1765 1770 1775 AAT GCT CTC CTT AAT GCA GGG GAA TCA CGA CTC GCT GAA CTG TAC GTG 5376 Asn Ala Leu Leu Asn Ala Gly Glu Ser Arg Leu Ala Glu Leu Tyr Val 1780 1785 1790 GAA AGG GCA AAG TGG CTC TGG TCC AAG GGT GAT GTT CAC CAG GCA CTA 5424 Glu Arg Ala Lys Trp Leu Trp Ser Lys Gly Asp Val His Gin Ala Leu 1795 1800 1805 ATT GTT CTT CAA AAA GGT GTT GAA TTA TGT TTT CCT GAA AAT GAA ACC 5472 He Val Leu Gin Lys Gly Val Glu Leu Cys Phe Pro Glu Asn Glu Thr 1810 1815 1820 CCA CCT GAG GGT AAG AAC ATG TTA ATC CAT GGT CGA GCT ATG CTA CTA 5520 Pro Pro Glu Gly Lys Asn Met Leu He His Gly Arg Ala Met Leu Leu 1825 1830 1835 1840 GTG GGC CGA TTT ATG GAA GAA ACA GCT AAC TTT GAA AGC AAT GCA ATT 5568 Val Gly Arg Phe Met Glu Glu Thr Ala Asn Phe Glu Ser Asn Ala He 1845 1850 1855 ATG AAA AAA TAT AAG GAT GTG ACC GCG TGC CTG CCA GAA TGG GAG GAT 5616 Met Lys Lys Tyr Lys Asp Val Thr Ala Cys Leu Pro Glu Trp Glu Asp 1860 1865 1870 GGG CAT TTT TAC CTT GCC AAG TAC TAT GAC AAA TTG ATG CCC ATG GTC 5664 Gly His Phe Tyr Leu Ala Lys Tyr Tyr Asp Lys Leu Met Pro Met Val 1875 1880 1885 ACA GAC AAC AAA ATG GAA AAG CAA GGT GAT CTC ATC CGG TAT ATA GTT 5712 Thr Asp Asn Lys Met Glu Lys Gin Gly Asp Leu He Arg Tyr He Val 1890 1895 1900 CTT CAT TTT GGC AGA TCT CTA CAA TAT GGA AAT CAG TTC ATA TAT CAG 5760 Leu His Phe Gly Arg Ser Leu Gin Tyr Gly Asn Gin Phe He Tyr Gin 1905 1910 1915 1920 TCA ATG CCA CGA ATG TTA ACT CTA TGG CTT GAT TAT GGT ACA AAG GCA 5808 Ser Met Pro Arg Met Leu Thr Leu Trp Leu Asp Tyr Gly Thr Lys Ala 1925 1930 1935 TAT GAA TGG GAA AAA GCT GGC CGC TCC GAT CGT GTA CAA ATG AGG AAT 5856 Tyr Glu Trp Glu Lys Ala Gly Arg Ser Asp Arg Val Gin Met Arg Asn 1940 1945 1950 GAT TTG GGT AAA ATA AAC AAG GTT ATC ACA GAG CAT ACA AAC TAT TTA 5904 Asp Leu Gly Lys He Asn Lys Val He Thr Glu His Thr Asn Tyr Leu 1955 1960 1965 GCT CCA TAT CAA TTT TTG ACT GCT TTT TCA CAA TTG ATC TCT CGA ATT 5952 Ala Pro Tyr Gin Phe Leu Thr Ala Phe Ser Gin Leu He Ser Arg He 1970 1975 1980 TGT CAT TCT CAC GAT GAA GTT TTT GTT GTG CTT GAT GGA AAT AAT AGC 6000 Cys His Ser His Asp Glu Val Phe Val Val Leu Asp Gly Asn Asn Ser 1985 1990 1995 2000 CAA GTA TTT CTA GCC TAT CCT CAA CAA GCA ATG TGG ATG ATG ACA GCT 6048 Gin Val Phe Leu Ala Tyr Pro Gin Gin Ala Met Trp Met Met Thr Ala 2005 2010 2015 GTG TCA AAG TCA TCT TAT CCC ATG CGT GTG AAC AGA TGC AAG GAA ATC 60 6 Val Ser Lys Ser Ser Tyr Pro Met Arg Val Asn Arg Cys Lys Glu He 2020 2025 2030 CTC AAT AAA GCT ATT CAT ATG AAA AAA TCC TTA GAG AAG TTT GTT GGA 6144 Leu Asn Lys Ala He His Met Lys Lys Ser Leu Glu Lys Phe Val Gly 2035 2040 2045 GAT GCA ACT CGC CTA ACA GAT AAG CTT CTA GAA TTG TGC AAT AAA CCG 6192 Asp Ala Thr Arg Leu Thr Asp Lys Leu Leu Glu Leu Cys Asn Lys Pro 2050 2055 2060 GTT GAT GGA AGT AGT TCC ACA TTA AGC ATG AGC ACT CAT TTT AAA ATG 6240 Val Asp Gly Ser Ser Ser Thr Leu Ser Met Ser Thr His Phe Lys Met 2065 2070 2075 2080 CTT AAA AAG CTG GTA GAA GAA GCA ACA TTT AGT GAA ATC CTC ATT CCT 6288 Leu Lys Lys Leu Val Glu Glu Ala Thr Phe Ser Glu He Leu He Pro 2085 2090 2095 CTA CAA TCA GTC ATG ATA CCT ACA CTT CCA TCA ATT CTG GGT ACC CAT 6336 Leu Gin Ser Val Met He Pro Thr Leu Pro Ser He Leu Gly Thr His 2100 2105 2110 GCT AAC CAT GCT AGC CAT GAA CCA TTT CCT GGA CAT TGG GCC TAT ATT 6384 Ala Asn His Ala Ser His Glu Pro Phe Pro Gly His Trp Ala Tyr He 2115 2120 2125 GCA GGG TTT GAT GAT ATG GTG GAA ATT CTT GCT TCT CTT CAG AAA CCA 6432 Ala Gly Phe Asp Asp Met Val Glu He Leu Ala Ser Leu Gin Lys Pro 2130 2135 2140 AAG AAG ATT TCT TTA AAA GGC TCA GAT GGA AAG TTC TAC ATC ATG ATG 6480 Lys Lys He Ser Leu Lys Gly Ser Asp Gly Lys Phe Tyr He Met Met 2145 2150 2155 2160 TGT AAG CCA AAA GAT GAC CTG AGA AAG GAT TGT AGA CTA ATG GAA TTC 6528 Cys Lys Pro Lys Asp Asp Leu Arg Lys Asp Cys Arg Leu Met Glu Phe 2165 2170 2175 AAT TCC TTG ATT AAT AAG TGC TTA AGA AAA GAT GCA GAG TCT CGT AGA 6576 Asn Ser Leu He Asn Lys Cys Leu Arg Lys Asp Ala Glu Ser Arg Arg 2180 2185 2190 AGA GAA CTT CAT ATT CGA ACA TAT GCA GTT ATT CCA CTA AAT GAT GAA 6624 Arg Glu Leu His He Arg Thr Tyr Ala Val He Pro Leu Asn Asp Glu 2195 2200 2205 TGT GGG ATT ATT GAA TGG GTG AAC AAC ACT GCT GGT TTG AGA CCT ATT 6672 Cys Gly He He Glu Trp Val Asn Asn Thr Ala Gly Leu Arg Pro He 2210 2215 2220 CTG ACC AAA CTA TAT AAA GAA AAG GGA GTG TAT ATG ACA GGA AAA GAA 6720 Leu Thr Lys Leu Tyr Lys Glu Lys Gly Val Tyr Met Thr Gly Lys Glu 2225 2230 2235 2240 CTT CGC CAG TGT ATG CTA CCA AAG TCA GCA GCT TTA TCT GAA AAA CTC 6768 Leu Arg Gin Cys Met Leu Pro Lys Ser Ala Ala Leu Ser Glu Lys Leu 2245 2250 2255 AAA GTA TTC CGA GAA TTT CTC CTG CCC AGG CAT CCT CCT ATT TTT CAT 6816 Lys Val Phe Arg Glu Phe Leu Leu Pro Arg His Pro Pro He Phe His 2260 2265 2270 GAG TGG TTT CTG AGA ACA TTC CCT GAT CCT ACA TCA TGG TAC AGT AGT 6864 Glu Trp Phe Leu Arg Thr Phe Pro Asp Pro Thr Ser Trp Tyr Ser Ser 2275 2280 2285 AGA TCA GCT TAC TGC CGT TCC ACT GCA GTA ATG TCA ATG GTT GGT TAT 6912 Arg Ser Ala Tyr Cys Arg Ser Thr Ala Val Met Ser Met Val Gly Tyr 2290 2295 2300 ATT CTG GGG CTT GGA GAC CGT CAT GGT GAA AAT ATT CTC TTT GAT TCT 6960 He Leu Gly Leu Gly Asp Arg His Gly Glu Asn He Leu Phe Asp Ser 2305 2310 2315 2320 TTG ACT GGT GAA TGC GTA CAT GTA GAT TTC AAT TGT CTT TTC AAT AAG 7008 Leu Thr Gly Glu Cys Val His Val Asp Phe Asn Cys Leu Phe Asn Lys 2325 2330 2335 GGA GAA ACC TTT GAA GTT CCA GAA ATT GTG CCA TTT CGC CTG ACT CAT 7056 Gly Glu Thr Phe Glu Val Pro Glu He Val Pro Phe Arg Leu Thr His 2340 2345 2350 AAT ATG GTT AAT GGA ATG GGT CCT ATG GGA ACA GAG GGT CTT TTT CGA 7104 Asn Met Val Asn Gly Met Gly Pro Met Gly Thr Glu Gly Leu Phe Arg 2355 2360 2365 AGA GCA TGT GAA GTT ACA ATG AGG CTG ATG CGT GAT CAG CGA GAG CCT 7152 Arg Ala Cys Glu Val Thr Met Arg Leu Met Arg Asp Gin Arg Glu Pro 2370 2375 2380 TTA ATG AGT GTC TTA AAG ACT TTT CTA CAT GAT CCT CTT GTG GAA TGG 7200 Leu Met Ser Val Leu Lys Thr Phe Leu His Asp Pro Leu Val Glu Trp 2385 2390 2395 2400 AGT AAA CCA GTG AAA GGG CAT TCC AAA GCG CCA CTG AAT GAA ACT GGA 7248 Ser Lys Pro Val Lys Gly His Ser Lys Ala Pro Leu Asn Glu Thr Gly 2405 2410 2415 GAA GTT GTC AAT GAA AAG GCC AAG ACC CAT GTT CTT GAC ATT GAG CAG 7296 Glu Val Val Asn Glu Lys Ala Lys Thr His Val Leu Asp He Glu Gin 2420 2425 2430 CGA CTA CAA GGT GTA ATC AAG ACT CGA AAT AGA GTG ACA GGA CTG CCG 7344 Arg Leu Gin Gly Val He Lys Thr Arg Asn Arg Val Thr Gly Leu Pro 2435 2440 2445 TTA TCT ATT GAA GGA CAT GTG CAT TAC CTT ATA CAA GAA GCT ACT GAT 7392 Leu Ser He Glu Gly His Val His Tyr Leu He Gin Glu Ala Thr Asp 2450 2455 2460 GAA AAC TTA CTA TGC CAG ATG TAT CTT GGT TGG ACT CCA TAT ATG 7437 Glu Asn Leu Leu Cys Gin Met Tyr Leu Gly Trp Thr Pro Tyr Met 2465 2470 2475 TGA 7440 (2) INFORMATION FOR SEQ ID NO: 18: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2479 amino acids (B) TYPE: ammo acid (D) TOPOLOGY: linear (u) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:18: Met Gly His Ala Val Glu Trp Pro Val Val Met Ser Arg Phe Leu Ser 1 5 10 15 Gin Leu Asp Glu His Met Gly Tyr Leu Gin Ser Ala Pro Leu Gin Leu 20 25 30 Met Ser Met Gin Lys Leu Glu Phe He Glu Val Thr Leu Leu Thr Val 35 40 45 Leu Thr Arg He He Ala He Val Phe Phe Arg Arg Gin Glu Leu Leu 50 55 60 Leu Trp Gin He Gly Cys Val Leu Leu Glu Tyr Gly Ser Pro Lys He 65 70 75 80 Lys Ser Leu Ala He Ser Phe Leu Thr Glu Leu Phe Gin Leu Gly Gly 85 90 95 Leu Pro Ala Gin Pro Ala Ser Thr Phe Phe Ser Ser Phe Leu Glu Leu 100 105 110 Leu Lys His Leu Val Glu Met Asp Thr Asp Gin Leu Lys Leu Tyr Glu 115 120 125 Glu Pro Leu Ser Lys Leu He Lys Thr Leu Phe Pro Phe Glu Ala Glu 130 135 140 Ala Tyr Arg Asn He Glu Pro Val Tyr Leu Asn Met Leu Leu Glu Lys 145 150 155 160 Leu Cys Val Met Phe Glu Asp Gly Val Leu Met Arg Leu Lys Ser Asp 165 170 175 Leu Leu Lys Ala Ala Leu Cys His Leu Leu Gin Tyr Phe Leu Lys Phe 180 185 190 Val Pro Ala Gly Tyr Glu Ser Ala Leu Gin Val Arg Lys Val Tyr Val 195 200 205 Arg Asn He Cys Lys Ala Leu Leu Asp Val Leu Gly He Glu Val Asp 210 215 220 Ala Glu Tyr Leu Leu Gly Pro Leu Tyr Ala Ala Leu Lys Met Glu Ser 225 230 235 240 Met Glu He He Glu Glu He Gin Cys Gin Thr Gin Gin Glu Asn Leu 245 250 255 Ser Ser Asn Ser Asp Gly He Ser Pro Lys Arg Arg Arg Leu Ser Ser 260 265 270 Ser Leu Asn Pro Ser Lys Arg Ala Pro Lys Gin Thr Glu Glu He Lys 275 280 285 His Val Asp Met Asn Gin Lys Ser He Leu Trp Ser Ala Leu Lys Gin 290 295 300 Lys Ala Glu Ser Leu Gin He Ser Leu Glu Tyr Ser Gly Leu Lys Asn 305 310 315 320 Pro Val He Glu Met Leu Glu Gly He Ala Val Val Leu Gin Leu Thr 325 330 335 Ala Leu Cys Thr Val His Cys Ser His Gin Asn Met Asn Cys Arg Thr 340 345 350 Phe Lys Asp Cys Gin His Lys Ser Lys Lys Lys Pro Ser Val Val He 355 360 365 Thr Trp Met Ser Leu Asp Phe Tyr Thr Thr Val Leu Lys Ser Cys Arg 370 375 380 Arg Leu Leu Glu Ser Val Gin Lys Arg Thr Gly Gly Asn He Asp Lys 385 390 395 400 Val Val Lys He Tyr Asp Ala Leu He Tyr Met Gin Val Asn Ser Ser 405 410 415 Phe Glu Asp His He Leu Glu Asp Leu Cys Gly Met Leu Ser Leu Pro 420 425 430 Trp He Tyr Ser His Ser Asp Asp Gly Cys Leu Lys Leu Thr Thr Phe 435 440 445 Ala Ala Asn Leu Leu Thr Leu Ser Cys Arg He Ser Asp Ser Tyr Ser 450 455 460 Pro Gin Ala Gin Ser Arg Cys Val Phe Leu Leu Thr Leu Phe Pro Arg 465 470 475 480 Arg He Phe Leu Glu Trp Arg Thr Ala Val Tyr Asn Trp Ala Leu Gin 485 490 495 Ser Ser His Glu Val He Arg Ala Ser Cys Val Ser Gly Phe Phe He 500 505 510 Leu Leu Gin Gin Gin Asn Ser Cys Asn Arg Val Pro Lys He Leu He 515 520 525 Asp Lys Val Lys Asp Asp Ser Asp He Val Lys Lys Glu Phe Ala Ser 530 535 540 He Leu Gly Gin Leu Val Cys Thr Leu His Gly Met Phe Tyr Leu Thr 545 550 555 560 Ser Ser Leu Thr Glu Pro Phe Ser Glu His Gly His Val Asp Leu Phe 565 570 575 Cys Arg Asn Leu Lys Ala Thr Ser Gin His Glu Cys Ser Ser Ser Gin 580 585 590 Leu Lys Ala Ser Val Cys Lys Pro Phe Leu Phe Leu Leu Lys Lys Lys 595 600 605 He Pro Ser Pro Val Lys Leu Ala Phe He Asp Asn Leu His His Leu 610 615 620 Cys Lys His Leu Asp Phe Arg Glu Asp Glu Thr Asp Val Lys Ala Val 625 630 635 640 Leu Gly Thr Leu Leu Asn Leu Met Glu Asp Pro Asp Lys Asp Val Arg 645 650 655 Val Ala Phe Ser Gly Asn He Lys His He Leu Glu Ser Leu Asp Ser 660 665 670 Glu Asp Gly Phe He Lys Glu Leu Phe Val Leu Arg Met Lys Glu Ala 675 680 685 Tyr Thr His Ala Gin He Ser Arg Asn Asn Glu Leu Lys Asp Thr Leu 690 695 700 He Leu Thr Thr Gly Asp He Gly Arg Ala Ala Lys Gly Asp Leu Val 705 710 715 720 Pro Phe Ala Leu Leu His Leu Leu His Cys Leu Leu Ser Lys Ser Ala 725 730 735 Ser Val Ser Gly Ala Ala Tyr Thr Glu He Arg Ala Leu Val Ala Ala 740 745 750 Lys Ser Val Lys Leu Gin Ser Phe Phe Ser Gin Tyr Lys Lys Pro He 755 760 765 Cys Gin Phe Leu Val Glu Ser Leu His Ser Ser Gin Met Thr Ala Leu 770 775 780 Pro Asn Thr Pro Cys Gin Asn Ala Asp Val Arg Lys Gin Asp Val Ala 785 790 795 800 His Gin Arg Glu Met Ala Leu Asn Thr Leu Ser Glu He Ala Asn Val 805 810 815 Phe Asp Phe Pro Asp Leu Asn Arg Phe Leu Thr Arg Thr Leu Gin Val 820 825 830 Leu Leu Pro Asp Leu Ala Ala Lys Ala Ser Pro Ala Ala Ser Ala Leu 835 840 845 He Arg Thr Leu Gly Lys Gin Leu Asn Val Asn Arg Arg Glu He Leu 850 855 860 He Asn Asn Phe Lys Tyr He Phe Ser His Leu Val Cys Ser Cys Ser 865 870 875 880 Lys Asp Glu Leu Glu Arg Ala Leu His Tyr Leu Lys Asn Glu Thr Glu 885 890 895 He Glu Leu Gly Ser Leu Leu Arg Gin Asp Phe Gin Gly Leu His Asn 900 905 910 Glu Leu Leu Leu Arg He Gly Glu His Tyr Gin Gin Val Phe Asn Gly 915 920 925 Leu Ser He Leu Ala Ser Phe Ala Ser Ser Asp Asp Pro Tyr Gin Gly 930 935 940 Pro Arg Asp He He Ser Pro Glu Leu Met Ala Asp Tyr Leu Gin Pro 945 950 955 960 Lys Leu Leu Gly He Leu Ala Phe Phe Asn Met Gin Leu Leu Ser Ser 965 970 975 Ser Val Gly He Glu Asp Lys Lys Met Ala Leu Asn Ser Leu Met Ser 980 985 990 Leu Met Lys Leu Met Gly Pro Lys His Val Ser Ser Val Arg Val Lys 995 1000 1005 Met Met Thr Thr Leu Arg Thr Gly Leu Arg Phe Lys Asp Asp Phe Pro 1010 1015 1020 Glu Leu Cys Cys Arg Ala Trp Asp Cys Phe Val Arg Cys Leu Asp His 1025 1030 1035 1040 Ala Cys Leu Gly Ser Leu Leu Ser His Val He Val Ala Leu Leu Pro 1045 1050 1055 Leu He His He Gin Pro Lys Glu Thr Ala Ala He Phe His Tyr Leu 1060 1065 1070 He He Glu Asn Arg Asp Ala Val Gin Asp Phe Leu His Glu He Tyr 1075 1080 1085 Phe Leu Pro Asp His Pro Glu Leu Lys Lys He Lys Ala Val Leu Gin 1090 1095 1100 Glu Tyr Arg Lys Glu Thr Ser Glu Ser Thr Asp Leu Gin Thr Thr Leu 1105 1110 1115 1120 Gin Leu Ser Met Lys Ala He Gin His Glu Asn Val Asp Val Arg He 1125 1130 1135 His Ala Leu Thr Ser Leu Lys Glu Thr Leu Tyr Lys Asn Gin Glu Lys 1140 1145 1150 Leu He Lys Tyr Ala Thr Asp Ser Glu Thr Val Glu Pro He He Ser 1155 1160 1165 Gin Leu Val Thr Val Leu Leu Lys Gly Cys Gin Asp Ala Asn Ser Gin 1170 1175 1180 Ala Arg Leu Leu Cys Gly Glu Cys Leu Gly Glu Leu Gly Ala He Asp 1185 1190 1195 1200 Pro Gly Arg Leu Asp Phe Ser Thr Thr Glu Thr Gin Gly Lys Asp Phe 1205 1210 1215 Thr Phe Val Thr Gly Val Glu Asp Ser Ser Phe Ala Tyr Gly Leu Leu 1220 1225 1230 Met Glu Leu Thr Arg Ala Tyr Leu Ala Tyr Ala Asp Asn Ser Arg Ala 1235 1240 1245 Pro Asp Ser Ala Ala Tyr Ala He Gin Glu Leu Leu Ser He Tyr Asp 1250 1255 1260 Cys Arg Glu Met Glu Thr Asn Gly Pro Gly His Gin Leu Trp Arg Arg 1265 1270 1275 1280 Phe Pro Glu His Val Arg Glu He Leu Glu Pro His Leu Asn Thr Arg 1285 1290 1295 Tyr Lys Ser Ser Gin Lys Ser Thr Asp Trp Ser Gly Val Lys Lys Pro 1300 1305 1310 He Tyr Leu Ser Lys Leu Gly Ser Asn Phe Ala Glu Trp Ser Ala Ser 1315 1320 1325 Trp Ala Gly Tyr Leu He Thr Lys Val Arg His Asp Leu Ala Ser Lys 1330 1335 1340 He Phe Thr Cys Cys Ser He Met Met Lys His Asp Phe Lys Val Thr 1345 1350 1355 1360 He Tyr Leu Leu Pro His He Leu Val Tyr Val Leu Leu Gly Cys Asn 1365 1370 1375 Gin Glu Asp Gin Gin Glu Val Tyr Ala Glu He Met Ala Val Leu Lys 1380 1385 1390 His Asp Asp Gin His Thr He Asn Thr Gin Asp He Ala Ser Asp Leu 1395 1400 1405 Cys Gin Leu Ser Thr Gin Thr Val Phe Ser Met Leu Asp His Leu Thr 1410 1415 1420 Gin Trp Ala Arg His Lys Phe Gin Ala Leu Lys Ala Glu Lys Cys Pro 1425 1430 1435 1440 His Ser Lys Ser Asn Arg Asn Lys Val Asp Ser Met Val Ser Thr Val 1445 1450 1455 Asp Tyr Glu Asp Tyr Gin Ser Val Thr Arg Phe Leu Asp Leu He Pro 1460 1465 1470 Gin Asp Thr Leu Ala Val Ala Ser Phe Arg Ser Lys Ala Tyr Thr Arg 1475 1480 1485 Ala Val Met His Phe Glu Ser Phe He Thr Glu Lys Lys Gin Asn He 1490 1495 1500 Gin Glu His Leu Gly Phe Leu Gin Lys Leu Tyr Ala Ala Met His Glu 1505 1510 1515 1520 Pro Asp Gly Val Ser Gly Val Ser Ala He Arg Lys Ala Glu Pro Ser 1525 1530 1535 Leu Lys Glu Gin He Leu Glu His Glu Ser Leu Gly Leu Leu Arg Asp 1540 1545 1550 Ala Thr Ala Cys Tyr Asp Arg Ala He Gin Leu Glu Pro Asp Gin He 1555 1560 1565 He His Tyr His Gly Val Val Lys Ser Met Leu Gly Leu Gly Gin Leu 1570 1575 1580 Ser Thr Val He Thr Gin Val Asn Gly Val His Ala Asn Arg Ser Glu 1585 1590 1595 1600 Trp Thr Asp Glu Leu Asn Thr Tyr Arg Val Glu Ala Ala Trp Lys Leu 1605 1610 1615 Ser Gin Trp Asp Leu Val Glu Asn Tyr Leu Ala Ala Asp Gly Lys Ser 1620 1625 1630 Thr Thr Trp Ser Val Arg Leu Gly Gin Leu Leu Leu Ser Ala Lys Lys 1635 1640 1645 Arg Asp He Thr Ala Phe Tyr Asp Ser Leu Lys Leu Val Arg Ala Glu 1650 1655 1660 Gin He Val Pro Leu Ser Ala Ala Ser Phe Glu Arg Gly Ser Tyr Gin 1665 1670 1675 1680 Arg Gly Tyr Glu Tyr He Val Arg Leu His Met Leu Cys Glu Leu Glu 1685 1690 1695 His Ser He Lys Pro Leu Phe Gin His Ser Pro Gly Asp Ser Ser Gin 1700 1705 1710 Glu Asp Ser Leu Asn Trp Val Ala Arg Leu Glu Met Thr Gin Asn Ser 1715 1720 1725 Tyr Arg Ala Lys Glu Pro He Leu Ala Leu Arg Arg Ala Leu Leu Ser 1730 1735 1740 Leu Asn Lys Arg Pro Asp Tyr Asn Glu Met Val Gly Glu Cys Trp Leu 1745 1750 1755 1760 Gin Ser Ala Arg Val Ala Arg Lys Ala Gly His His Gin Thr Ala Tyr 1765 1770 1775 Asn Ala Leu Leu Asn Ala Gly Glu Ser Arg Leu Ala Glu Leu Tyr Val 1780 1785 1790 Glu Arg Ala Lys Trp Leu Trp Ser Lys Gly Asp Val His Gin Ala Leu 1795 1800 1805 He Val Leu Gin Lys Gly Val Glu Leu Cys Phe Pro Glu Asn Glu Thr 1810 1815 1820 Pro Pro Glu Gly Lys Asn Met Leu He His Gly Arg Ala Met Leu Leu 1825 1830 1835 1840 Val Gly Arg Phe Met Glu Glu Thr Ala Asn Phe Glu Ser Asn Ala He 1845 1850 1855 Met Lys Lys Tyr Lys Asp Val Thr Ala Cys Leu Pro Glu Trp Glu Asp 1860 1865 1870 Gly His Phe Tyr Leu Ala Lys Tyr Tyr Asp Lys Leu Met Pro Met Val 1875 1880 1885 Thr Asp Asn Lys Met Glu Lys Gin Gly Asp Leu He Arg Tyr He Val 1890 1895 1900 Leu His Phe Gly Arg Ser Leu Gin Tyr Gly Asn Gin Phe He Tyr Gin 1905 1910 1915 1920 Ser Met Pro Arg Met Leu Thr Leu Trp Leu Asp Tyr Gly Thr Lys Ala 1925 1930 1935 Tyr Glu Trp Glu Lys Ala Gly Arg Ser Asp Arg Val Gin Met Arg Asn 1940 1945 1950 Asp Leu Gly Lys He Asn Lys Val He Thr Glu His Thr Asn Tyr Leu 1955 1960 1965 Ala Pro Tyr Gin Phe Leu Thr Ala Phe Ser Gin Leu He Ser Arg He 1970 1975 1980 Cys His Ser His Asp Glu Val Phe Val Val Leu Asp Gly Asn Asn Ser 1985 1990 1995 2000 Gin Val Phe Leu Ala Tyr Pro Gin Gin Ala Met Trp Met Met Thr Ala 2005 2010 2015 Val Ser Lys Ser Ser Tyr Pro Met Arg Val Asn Arg Cys Lys Glu He 2020 2025 2030 Leu Asn Lys Ala He His Met Lys Lys Ser Leu Glu Lys Phe Val Gly 2035 2040 2045 Asp Ala Thr Arg Leu Thr Asp Lys Leu Leu Glu Leu Cys Asn Lys Pro 2050 2055 2060 Val Asp Gly Ser Ser Ser Thr Leu Ser Met Ser Thr His Phe Lys Met 2065 2070 2075 2080 Leu Lys Lys Leu Val Glu Glu Ala Thr Phe Ser Glu He Leu He Pro 2085 2090 2095 Leu Gin Ser Val Met He Pro Thr Leu Pro Ser He Leu Gly Thr His 2100 2105 2110 Ala Asn Hrs Ala Ser His Glu Pro Phe Pro Gly His Trp Ala Tyr He 2115 2120 2125 Ala Gly Phe Asp Asp Met Val Glu He Leu Ala Ser Leu Gin Lys Pro 2130 2135 2140 Lys Lys He Ser Leu Lys Gly Ser Asp Gly Lys Phe Tyr He Met Met 2145 2150 2155 2160 Cys Lys Pro Lys Asp Asp Leu Arg Lys Asp Cys Arg Leu Met Glu Phe 2165 2170 2175 Asn Ser Leu He Asn Lys Cys Leu Arg Lys Asp Ala Glu Ser Arg Arg 2180 2185 2190 Arg Glu Leu His He Arg Thr Tyr Ala Val He Pro Leu Asn Asp Glu 2195 2200 2205 Cys Gly He He Glu Trp Val Asn Asn Thr Ala Gly Leu Arg Pro He 2210 2215 2220 Leu Thr Lys Leu Tyr Lys Glu Lys Gly Val Tyr Met Thr Gly Lys Glu 2225 2230 2235 2240 Leu Arg Gin Cys Met Leu Pro Lys Ser Ala Ala Leu Ser Glu Lys Leu 2245 2250 2255 Lys Val Phe Arg Glu Phe Leu Leu Pro Arg His Pro Pro He Phe His 2260 2265 2270 Glu Trp Phe Leu Arg Thr Phe Pro Asp Pro Thr Ser Trp Tyr Ser Ser 2275 2280 2285 Arg Ser Ala Tyr Cys Arg Ser Thr Ala Val Met Ser Met Val Gly Tyr 2290 2295 2300 He Leu Gly Leu Gly Asp Arg His Gly Glu Asn He Leu Phe Asp Ser 2305 2310 2315 2320 Leu Thr Gly Glu Cys Val His Val Asp Phe Asn Cys Leu Phe Asn Lys 2325 2330 2335 Gly Glu Thr Phe Glu Val Pro Glu He Val Pro Phe Arg Leu Thr His 2340 2345 2350 Asn Met Val Asn Gly Met Gly Pro Met Gly Thr Glu Gly Leu Phe Arg 2355 2360 2365 Arg Ala Cys Glu Val Thr Met Arg Leu Met Arg Asp Gin Arg Glu Pro 2370 2375 2380 Leu Met Ser Val Leu Lys Thr Phe Leu His Asp Pro Leu Val Glu Trp 2385 2390 2395 2400 Ser Lys Pro Val Lys Gly His Ser Lys Ala Pro Leu Asn Glu Thr Gly 2405 2410 2415 Glu Val Val Asn Glu Lys Ala Lys Thr His Val Leu Asp He Glu Gin 2420 2425 2430 Arg Leu Gin Gly Val He Lys Thr Arg Asn Arg Val Thr Gly Leu Pro 2435 2440 2445 Leu Ser He Glu Gly His Val His Tyr Leu He Gin Glu Ala Thr Asp 2450 2455 2460 Glu Asn Leu Leu Cys Gin Met Tyr Leu Gly Trp Thr Pro Tyr Met 2465 2470 2475 (2) INFORMATION FOR SEQ ID NO 19 (l) SEQUENCE CHARACTERISTICS (A) LENGTH 23 base pairs (B) TYPE nucleic acid (C) STRANDEDNESS single (D) TOPOLOGY linear (ii) MOLECULE TYPE DNA (vii) IMMEDIATE SOURCE (B) CLONE Primer ODH26 (xi) SEQUENCE DESCRIPTION SEQ ID NO 19 TGGTTTCTGA GAACATTCCC TGA 23 (2) INFORMATION FOR SEQ ID NO 20 (l) SEQUENCE CHARACTERISTICS (A) LENGTH 9 amino acids (B) TYPE amino acid (D) TOPOLOGY: linear (u) MOLECULE TYPE- peptide (vii) IMMEDIATE SOURCE (B) CLONE FLAG tag (xi) SEQUENCE DESCRIPTION: SEQ ID NO:20: Met Asp Tyr Lys Asp Asp Asp Asp Lys 1 5 (2) INFORMATION FOR SEQ ID NO:21: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY- linear (n) MOLECULE TYPE: DNA (vii) IMMEDIATE SOURCE: (B) CLONE: Primer 279-3 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:21- TGGATGATGA CAGCTGTGTC 20 (2) INFORMATION FOR SEQ ID NO:22: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (u) MOLECULE TYPE: DNA (vii) IMMEDIATE SOURCE: (B) CLONE: Primer 279-6 (xi) SEQUENCE DESCRIPTION: SEQ ID NO.22: TGTAGTCGCT GCTCAATGTC 20 (2) INFORMATION FOR SEQ ID NO:23: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 7624 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (u) MOLECULE TYPE. cDNA (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 333..7562 (xi) SEQUENCE DESCRIPTION: SEQ ID NO.23: CTTGTGAAGA GAATGTTTTA CACTCTTGTT AGTGAAGTTT ATTCTTTAAA AGTCAATCGT 60 CAAGGATTTA GCAAATGAAT TAGCACTTCG GATATACTTG TTTATTTAAT ATCTTTTTTG 120 TTTATTTCAA AGAATTCAGT AATTGGATCA TAACGAGACT TCTGCGGATT GCAGCAACTC 180 CCTCCTGTCA TTTGTTACAC AAGAAAATCT GTGAAGTCAT CTGTTCATTA TTATTTCTTT 240 TTAAAAGCAA GAGTCCTGCT ATTTTTGGGG TACTCACAAA AGAATTATTA CAACTTTTTG 300 AAGACTTGGT TTACCTCCAT AGAAGAAATG TG ATG GGT CAT GCT GTG GAA TGG 353 Met Gly His Ala Val Glu Trp 1 5 CCA GTG GTC ATG AGC CGA TTT TTA AGT CAA TTA GAT GAA CAC ATG GGA 401 Pro Val Val Met Ser Arg Phe Leu Ser Gin Leu Asp Glu His Met Gly 10 15 20 TAT TTA CAA TCA GCT CCT TTG CAG TTG ATG AGT ATG CAA AAT TTA GAA 449 Tyr Leu Gin Ser Ala Pro Leu Gin Leu Met Ser Met Gin Asn Leu Glu 25 30 35 TTT ATT GAA GTC ACT TTA TTA ATG GTT CTT ACT CGT ATT ATT GCA ATT 497 Phe He Glu Val Thr Leu Leu Met Val Leu Thr Arg He He Ala He 40 45 50 55 GTG TTT TTT AGA AGG CAA GAA CTC TTA CTT TGG CAG ATA GGT TGT GTT 545 Val Phe Phe Arg Arg Gin Glu Leu Leu Leu Trp Gin He Gly Cys Val 60 65 70 CTG CTA GAG TAT GGT AGT CCA AAA ATT AAA TCC CTA GCA ATT AGC TTT 593 Leu Leu Glu Tyr Gly Ser Pro Lys He Lys Ser Leu Ala He Ser Phe 75 80 85 TTA ACA GAA CTT TTT CAG CTT GGA GGA CTA CCA GCA CAA CCA GCT AGC 641 Leu Thr Glu Leu Phe Gin Leu Gly Gly Leu Pro Ala Gin Pro Ala Ser 90 95 100 ACT TTT TTC AGC TCA TTT TTG GAA TTA TTA AAA CAC CTT GTA GAA ATG 689 Thr Phe Phe Ser Ser Phe Leu Glu Leu Leu Lys His Leu Val Glu Met 105 110 115 GAT ACT GAC CAA TTG AAA CTC TAT GAA GAG CCA TTA TCA AAG CTG ATA 737 Asp Thr Asp Gin Leu Lys Leu Tyr Glu Glu Pro Leu Ser Lys Leu He 120 125 130 135 AAG ACA CTA TTT CCC TTT GAA GCA GAA GCT TAT AGA AAT ATT GAA CCT 785 Lys Thr Leu Phe Pro Phe Glu Ala Glu Ala Tyr Arg Asn He Glu Pro 140 145 150 GTC TAT TTA AAT ATG CTG CTG GAA AAA CTC TGT GTC ATG TTT GAA GAC 833 Val Tyr Leu Asn Met Leu Leu Glu Lys Leu Cys Val Met Phe Glu Asp 155 160 165 GGT GTG CTC ATG CGG CTT AAG TCT GAT TTG CTA AAA GCA GCT TTG TGC 881 Gly Val Leu Met Arg Leu Lys Ser Asp Leu Leu Lys Ala Ala Leu Cys 170 175 180 CAT TTA CTG CAG TAT TTC CTT AAA TTT GTG CCA GCT GGG TAT GAA TCT 929 His Leu Leu Gin Tyr Phe Leu Lys Phe Val Pro Ala Gly Tyr Glu Ser 185 190 195 GCT TTA CAA GTC AGG AAG GTC TAT GTG AGA AAT ATT TGT AAA GCT CTT 977 Ala Leu Gin Val Arg Lys Val Tyr Val Arg Asn He Cys Lys Ala Leu 200 205 210 215 TTG GAT GTG CTT GGA ATT GAG GTA GAT GCA GAG TAC TTG TTG GGC CCA 1025 Leu Asp Val Leu Gly He Glu Val Asp Ala Glu Tyr Leu Leu Gly Pro 220 225 230 CTT TAT GCA GCT TTG AAA ATG GAA AGT ATG GAA ATC ATT GAG GAG ATT 1073 Leu Tyr Ala Ala Leu Lys Met Glu Ser Met Glu He He Glu Glu He 235 240 245 CAA TGC CAA ACT CAA CAG GAA AAC CTC AGC AGT AAT AGT GAT GGA ATA 1121 Gin Cys Gin Thr Gin Gin Glu Asn Leu Ser Ser Asn Ser Asp Gly He 250 255 260 TCA CCC AAA AGG CGT CGT CTC AGC TCG TCT CTA AAC CCT TCT AAA AGA 1169 Ser Pro Lys Arg Arg Arg Leu Ser Ser Ser Leu Asn Pro Ser Lys Arg 265 270 275 GCA CCA AAA CAG ACT GAG GAA ATT AAA CAT GTG GAC ATG AAC CAA AAG 1217 Ala Pro Lys Gin Thr Glu Glu He Lys His Val Asp Met Asn Gin Lys 280 285 290 295 AGC ATA TTA TGG AGT GCA CTG AAA CAG AAA GCT GAA TCC CTT CAG ATT 1265 Ser He Leu Trp Ser Ala Leu Lys Gin Lys Ala Glu Ser Leu Gin He 300 305 310 TCC CTT GAA TAC AGT GGC CTA AAG AAT CCT GTT ATT GAG ATG TTA GAA 1313 Ser Leu Glu Tyr Ser Gly Leu Lys Asn Pro Val He Glu Met Leu Glu 315 320 325 GGA ATT GCT GTT GTC TTA CAA CTG ACT GCT CTG TGT ACT GTT CAT TGT 1361 Gly He Ala Val Val Leu Gin Leu Thr Ala Leu Cys Thr Val His Cys 330 335 340 TCT CAT CAA AAC ATG AAC TGC CGT ACT TTC AAG GAC TGT CAA CAT AAA 1409 Ser His Gin Asn Met Asn Cys Arg Thr Phe Lys Asp Cys Gin His Lys 345 350 355 TCC AAG AAG AAA CCT TCT GTA GTG ATA ACT TGG ATG TCA TTG GAT TTT 1457 Ser Lys Lys Lys Pro Ser Val Val He Thr Trp Met Ser Leu Asp Phe 360 365 370 375 TAC ACA AAA GTG CTT AAG AGC TGT AGA AGT TTG TTA GAA TCT GTT CAG 1505 Tyr Thr Lys Val Leu Lys Ser Cys Arg Ser Leu Leu Glu Ser Val Gin 380 385 390 AAA CTG GAC CTG GAG GCA ACC ATT GAT AAG GTG GTG AAA ATT TAT GAT 1553 Lys Leu Asp Leu Glu Ala Thr He Asp Lys Val Val Lys He Tyr Asp 395 400 405 GCT TTG ATT TAT ATG CAA GTA AAC AGT TCA TTT GAA GAT CAT ATC CTG 1601 Ala Leu He Tyr Met Gin Val Asn Ser Ser Phe Glu Asp His He Leu 410 415 420 GAA GAT TTA TGT GGA ATG CTC TCA CTT CCA TGG ATT TAT TCC CAT TCT 1649 Glu Asp Leu Cys Gly Met Leu Ser Leu Pro Trp He Tyr Ser His Ser 425 430 435 GAT GAT GGC TGT TTA AAG TTG ACC ACA TTT GCC GCT AAT CTT CTA ACA 1697 Asp Asp Gly Cys Leu Lys Leu Thr Thr Phe Ala Ala Asn Leu Leu Thr 440 445 450 455 TTA AGC TGT AGG ATT TCA GAT AGC TAT TCA CCA CAG GCA CAA TCA CGA 1745 Leu Ser Cys Arg He Ser Asp Ser Tyr Ser Pro Gin Ala Gin Ser Arg 460 465 470 TGT GTG TTT CTT CTG ACT CTG TTT CCA AGA AGA ATA TTC CTT GAG TGG 1793 Cys Val Phe Leu Leu Thr Leu Phe Pro Arg Arg He Phe Leu Glu Trp 475 480 485 AGA ACA GCA GTT TAC AAC TGG GCC CTG CAG AGC TCC CAT GAA GTA ATC 1841 Arg Thr Ala Val Tyr Asn Trp Ala Leu Gin Ser Ser His Glu Val He 490 495 500 CGG GCT AGT TGT GTT AGT GGA TTT TTT ATC TTA TTG CAG CAG CAG AAT 1889 Arg Ala Ser Cys Val Ser Gly Phe Phe He Leu Leu Gin Gin Gin Asn 505 510 515 TCT TGT AAC AGA GTT CCC AAG ATT CTT ATA GAT AAA GTC AAA GAT GAT 1937 Ser Cys Asn Arg Val Pro Lys He Leu He Asp Lys Val Lys Asp Asp 520 525 530 535 TCT GAC ATT GTC AAG AAA GAA TTT GCT TCT ATA CTT GGT CAA CTT GTC 1985 Ser Asp He Val Lys Lys Glu Phe Ala Ser He Leu Gly Gin Leu Val 540 545 550 TGT ACT CTT CAC GGC ATG TTT TAT CTG ACA AGT TCT TTA ACA GAA CCT 2033 Cys Thr Leu His Gly Met Phe Tyr Leu Thr Ser Ser Leu Thr Glu Pro 555 560 565 TTC TCT GAA CAC GGA CAT GTG GAC CTC TTC TGT AGG AAC TTG AAA GCC 2081 Phe Ser Glu His Gly His Val Asp Leu Phe Cys Arg Asn Leu Lys Ala 570 575 580 ACT TCT CAA CAT GAA TGT TCA TCT TCT CAA CTA AAA GCT TCT GTC TGC 2129 Thr Ser Gin His Glu Cys Ser Ser Ser Gin Leu Lys Ala Ser Val Cys 585 590 595 AAG CCA TTC CTT TTC CTA CTG AAA AAA AAA ATA CCT AGT CCA GTA AAA 2177 Lys Pro Phe Leu Phe Leu Leu Lys Lys Lys He Pro Ser Pro Val Lys 600 605 610 615 CTT GCT TTC ATA GAT AAT CTA CAT CAT CTT TGT AAG CAT CTT GAT TTT 2225 Leu Ala Phe He Asp Asn Leu His His Leu Cys Lys His Leu Asp Phe 620 625 630 AGA GAA GAT GAA ACA GAT GTA AAA GCA GTT CTT GGA ACT TTA TTA AAT 2273 Arg Glu Asp Glu Thr Asp Val Lys Ala Val Leu Gly Thr Leu Leu Asn 635 640 645 TTA ATG GAA GAT CCA GAC AAA GAT GTT AGA GTG GCT TTT AGT GGA AAT 2321 Leu Met Glu Asp Pro Asp Lys Asp Val Arg Val Ala Phe Ser Gly Asn 650 655 660 ATC AAG CAC ATA TTG GAA TCC TTG GAC TCT GAA GAT GGA TTT ATA AAG 2369 He Lys His He Leu Glu Ser Leu Asp Ser Glu Asp Gly Phe He Lys 665 670 675 GAG CTT TTT GTC TTA AGA ATG AAG GAA GCA TAT ACA CAT GCC CAA ATA 2417 Glu Leu Phe Val Leu Arg Met Lys Glu Ala Tyr Thr His Ala Gin He 680 685 690 695 TCA AGA AAT AAT GAG CTG AAG GAT ACC TTG ATT CTT ACA ACA GGG GAT 2465 Ser Arg Asn Asn Glu Leu Lys Asp Thr Leu He Leu Thr Thr Gly Asp 700 705 710 ATT GGA AGG GCC GCA AAA GGA GAT TTG GTA CCA TTT GCA CTC TTA CAC 2513 He Gly Arg Ala Ala Lys Gly Asp Leu Val Pro Phe Ala Leu Leu His 715 720 725 TTA TTG CAT TGT TTG TTA TCC AAG TCA GCA TCT GTC TCT GGA GCA GCA 2561 Leu Leu His Cys Leu Leu Ser Lys Ser Ala Ser Val Ser Gly Ala Ala 730 735 740 TAC ACA GAA ATT AGA GCT CTG GTT GCA GCT AAA AGT GTT AAA CTG CAA 2609 Tyr Thr Glu He Arg Ala Leu Val Ala Ala Lys Ser Val Lys Leu Gin 745 750 755 AGT TTT TTC AGC CAG TAT AAG AAA CCC ATC TGT CAG TTT TTG GTA GAA 2657 Ser Phe Phe Ser Gin Tyr Lys Lys Pro He Cys Gin Phe Leu Val Glu 760 765 770 775 TCC CTT CAC TCT AGT CAG ATG ACA GCA CTT CCG AAT ACT CCA TGC CAG 2705 Ser Leu His Ser Ser Gin Met Thr Ala Leu Pro Asn Thr Pro Cys Gin 780 785 790 AAT GCT GAC GTG CGA AAA CAA GAT GTG GCT CAC CAG AGA GAA ATG GCT 2753 Asn Ala Asp Val Arg Lys Gin Asp Val Ala His Gin Arg Glu Met Ala 795 800 805 TTA AAT ACG TTG TCT GAA ATT GCC AAC GTT TTC GAC TTT CCT GAT CTT 2801 Leu Asn Thr Leu Ser Glu He Ala Asn Val Phe Asp Phe Pro Asp Leu 810 815 820 AAT CGT TTT CTT ACT AGG ACA TTA CAA GTT CTA CTA CCT GAT CTT GCT 2849 Asn Arg Phe Leu Thr Arg Thr Leu Gin Val Leu Leu Pro Asp Leu Ala 825 830 835 GCC AAA GCA AGC CCT GCA GCT TCT GCT CTC ATT CGA ACT TTA GGA AAA 2897 Ala Lys Ala Ser Pro Ala Ala Ser Ala Leu He Arg Thr Leu Gly Lys 840 845 850 855 CAA TTA AAT GTC AAT CGT AGA GAG ATT TTA ATA AAC AAC TTC AAA TAT 2945 Gin Leu Asn Val Asn Arg Arg Glu He Leu He Asn Asn Phe Lys Tyr 860 865 870 ATT TTT TCT CAT TTG GTC TGT TCT TGT TCC AAA GAT GAA TTA GAA CGT 2993 He Phe Ser His Leu Val Cys Ser Cys Ser Lys Asp Glu Leu Glu Arg 875 880 885 GCC CTT CAT TAT CTG AAG AAT GAA ACA GAA ATT GAA CTG GGG AGC CTG 3041 Ala Leu His Tyr Leu Lys Asn Glu Thr Glu He Glu Leu Gly Ser Leu 890 895 900 TTG AGA CAA GAT TTC CAA GGA TTG CAT AAT GAA TTA TTG CTG CGT ATT 3089 Leu Arg Gin Asp Phe Gin Gly Leu His Asn Glu Leu Leu Leu Arg He 905 910 915 GGA GAA CAC TAT CAA CAG GTT TTT AAT GGT TTG TCA ATA CTT GCC TCA 3137 Gly Glu His Tyr Gin Gin Val Phe Asn Gly Leu Ser He Leu Ala Ser 920 925 930 935 TTT GCA TCC AGT GAT GAT CCA TAT CAG GGC CCG AGA GAT ATC ATA TCA 3185 Phe Ala Ser Ser Asp Asp Pro Tyr Gin Gly Pro Arg Asp He He Ser 940 945 950 CCT GAA CTG ATG GCT GAT TAT TTA CAA CCC AAA TTG TTG GGC ATT TTG 3233 Pro Glu Leu Met Ala Asp Tyr Leu Gin Pro Lys Leu Leu Gly He Leu 955 960 965 GCT TTT TTT AAC ATG CAG TTA CTG AGC TCT AGT GTT GGC ATT GAA GAT 3281 Ala Phe Phe Asn Met Gin Leu Leu Ser Ser Ser Val Gly He Glu Asp 970 975 980 AAG AAA ATG GCC TTG AAC AGT TTG ATG TCT TTG ATG AAG TTA ATG GGA 3329 Lys Lys Met Ala Leu Asn Ser Leu Met Ser Leu Met Lys Leu Met Gly 985 990 995 CCC AAA CAT GTC AGT TCT GTG AGG GTG AAG ATG ATG ACC ACA CTG AGA 3377 Pro Lys His Val Ser Ser Val Arg Val Lys Met Met Thr Thr Leu Arg 1000 1005 1010 1015 ACT GGC CTT CGA TTC AAG GAT GAT TTT CCT GAA TTG TGT TGC AGA GCT 3425 Thr Gly Leu Arg Phe Lys Asp Asp Phe Pro Glu Leu Cys Cys Arg Ala 1020 1025 1030 TGG GAC TGC TTT GTT CGC TGC CTG GAT CAT GCT TGT CTG GGC TCC CTT 3473 Trp Asp Cys Phe Val Arg Cys Leu Asp His Ala Cys Leu Gly Ser Leu 1035 1040 1045 CTC AGT CAT GTA ATA GTA GCT TTG TTA CCT CTT ATA CAC ATC CAG CCT 3521 Leu Ser His Val He Val Ala Leu Leu Pro Leu He His He Gin Pro 1050 1055 1060 AAA GAA ACT GCA GCT ATC TTC CAC TAC CTC ATA ATT GAA AAC AGG GAT 3569 Lys Glu Thr Ala Ala He Phe His Tyr Leu He He Glu Asn Arg Asp 1065 1070 1075 GCT GTG CAA GAT TTT CTT CAT GAA ATA TAT TTT TTA CCT GAT CAT CCA 3617 Ala Val Gin Asp Phe Leu His Glu He Tyr Phe Leu Pro Asp His Pro 1080 1085 1090 1095 GAA TTA AAA AAG ATA AAA GCC GTT CTC CAG GAA TAC AGA AAG GAG ACC 3665 Glu Leu Lys Lys He Lys Ala Val Leu Gin Glu Tyr Arg Lys Glu Thr 1100 1105 1110 TCT GAG AGC ACT GAT CTT CAG ACA ACT CTT CAG CTC TCT ATG AAG GCC 3713 Ser Glu Ser Thr Asp Leu Gin Thr Thr Leu Gin Leu Ser Met Lys Ala 1115 1120 1125 ATT CAA CAT GAA AAT GTC GAT GTT CGT ATT CAT GCT CTT ACA AGC TTG 3761 He Gin His Glu Asn Val Asp Val Arg He His Ala Leu Thr Ser Leu 1130 1135 1140 AAG GAA ACC TTG TAT AAA AAT CAG GAA AAA CTG ATA AAG TAT GCA ACA 3809 Lys Glu Thr Leu Tyr Lys Asn Gin Glu Lys Leu He Lys Tyr Ala Thr 1145 1150 1155 GAC AGT GAA ACA GTA GAA CCT ATT ATC TCA CAG TTG GTG ACA GTG CTT 3857 Asp Ser Glu Thr Val Glu Pro He He Ser Gin Leu Val Thr Val Leu 1160 1165 1170 1175 TTG AAA GGT TGC CAA GAT GCA AAC TCT CAA GCT CGG TTG CTC TGT GGG 3905 Leu Lys Gly Cys Gin Asp Ala Asn Ser Gin Ala Arg Leu Leu Cys Gly 1180 1185 1190 GAA TGT TTA GGG GAA TTG GGG GCG ATA GAT CCA GGT CGA TTA GAT TTC 3953 Glu Cys Leu Gly Glu Leu Gly Ala He Asp Pro Gly Arg Leu Asp Phe 1195 1200 1205 TCA ACA ACT GAA ACT CAA GGA AAA GAT TTT ACA TTT GTG ACT GGA GTA 4001 Ser Thr Thr Glu Thr Gin Gly Lys Asp Phe Thr Phe Val Thr Gly Val 1210 1215 1220 GAA GAT TCA AGC TTT GCC TAT GGA TTA TTG ATG GAG CTA ACA AGA GCT 4049 Glu Asp Ser Ser Phe Ala Tyr Gly Leu Leu Met Glu Leu Thr Arg Ala 1225 1230 1235 TAC CTT GCG TAT GCT GAT AAT AGC CGA GCT CAA GAT TCA GCT GCC TAT 4097 Tyr Leu Ala Tyr Ala Asp Asn Ser Arg Ala Gin Asp Ser Ala Ala Tyr 1240 1245 1250 1255 GCC ATT CAG GAG TTG CTT TCT ATT TAT GAC TGT AGA GAG ATG GAG ACC 4145 Ala He Gin Glu Leu Leu Ser He Tyr Asp Cys Arg Glu Met Glu Thr 1260 1265 1270 AAC GGC CCA GGT CAC CAA TTG TGG AGG AGA TTT CCT GAG CAT GTT CGG 4193 Asn Gly Pro Gly His Gin Leu Trp Arg Arg Phe Pro Glu His Val Arg 1275 1280 1285 GAA ATA CTA GAA CCT CAT CTA AAT ACC AGA TAC AAG AGT TCT CAG AAG 4241 Glu He Leu Glu Pro His Leu Asn Thr Arg Tyr Lys Ser Ser Gin Lys 1290 1295 1300 TCA ACC GAT TGG TCT GGA GTA AAG AAG CCA ATT TAC TTA AGT AAA TTG 4289 Ser Thr Asp Trp Ser Gly Val Lys Lys Pro He Tyr Leu Ser Lys Leu 1305 1310 1315 GGT AGT AAC TTT GCA GAA TGG TCA GCA TCT TGG GCA GGT TAT CTT ATT 4337 Gly Ser Asn Phe Ala Glu Trp Ser Ala Ser Trp Ala Gly Tyr Leu He 1320 1325 1330 1335 ACA AAG GTT CGA CAT GAT CTT GCC AGT AAA ATT TTC ACC TGC TGT AGC 4385 Thr Lys Val Arg His Asp Leu Ala Ser Lys He Phe Thr Cys Cys Ser 1340 1345 1350 ATT ATG ATG AAG CAT GAT TTC AAA GTG ACC ATC TAT CTT CTT CCA CAT 4433 He Met Met Lys His Asp Phe Lys Val Thr He Tyr Leu Leu Pro His 1355 1360 1365 ATT CTG GTG TAT GTC TTA CTG GGT TGT AAT CAA GAA GAT CAG CAG GAG 4481 He Leu Val Tyr Val Leu Leu Gly Cys Asn Gin Glu Asp Gin Gin Glu 1370 1375 1380 GTT TAT GCA GAA ATT ATG GCA GTT CTA AAG CAT GAC GAT CAG CAT ACC 4529 Val Tyr Ala Glu He Met Ala Val Leu Lys His Asp Asp Gin His Thr 1385 1390 1395 ATA AAT ACC CAA GAC ATT GCA TCT GAT CTG TGT CAA CTC AGT ACA CAG 4577 He Asn Thr Gin Asp He Ala Ser Asp Leu Cys Gin Leu Ser Thr Gin 1400 1405 1410 1415 ACT GTG TTC TCC ATG CTT GAC CAT CTC ACA CAG TGG GCA AGG CAC AAA 4625 Thr Val Phe Ser Met Leu Asp His Leu Thr Gin Trp Ala Arg His Lys 1420 1425 1430 TTT CAG GCA CTG AAA GCT GAG AAA TGT CCA CAC AGC AAA TCA AAC AGA 4673 Phe Gin Ala Leu Lys Ala Glu Lys Cys Pro His Ser Lys Ser Asn Arg 1435 1440 1445 AAT AAG GTA GAC TCA ATG GTA TCT ACT GTG GAT TAT GAA GAC TAT CAG 4721 Asn Lys Val Asp Ser Met Val Ser Thr Val Asp Tyr Glu Asp Tyr Gin 1450 1455 1460 AGT GTA ACC CGT TTT CTA GAC CTC ATA CCC CAG GAT ACT CTG GCA GTA 4769 Ser Val Thr Arg Phe Leu Asp Leu He Pro Gin Asp Thr Leu Ala Val 1465 1470 1475 GCT TCC TTT CGC TCC AAA GCA TAC ACA CGA GCT GTA ATG CAC TTT GAA 4817 Ala Ser Phe Arg Ser Lys Ala Tyr Thr Arg Ala Val Met His Phe Glu 1480 1485 1490 1495 TCA TTT ATT ACA GAA AAG AAG CAA AAT ATT CAG GAA CAT CTT GGA TTT 4865 Ser Phe He Thr Glu Lys Lys Gin Asn He Gin Glu His Leu Gly Phe 1500 1505 1510 TTA CAG AAA TTG TAT GCT GCT ATG CAT GAA CCT GAT GGA GTG GCC GGA 4913 Leu Gin Lys Leu Tyr Ala Ala Met His Glu Pro Asp Gly Val Ala Gly 1515 1520 1525 GTC AGT GCA ATT AGA AAG GCA GAA CCA TCT CTA AAA GAA CAG ATC CTT 4961 Val Ser Ala He Arg Lys Ala Glu Pro Ser Leu Lys Glu Gin He Leu 1530 1535 1540 GAA CAT GAA AGC CTT GGC TTG CTG AGG GAT GCC ACT GCT TGT TAT GAC 5009 Glu His Glu Ser Leu Gly Leu Leu Arg Asp Ala Thr Ala Cys Tyr Asp 1545 1550 1555 AGG GCT ATT CAG CTA GAA CCA GAC CAG ATC ATT CAT TAC CAT GGT GTA 5057 Arg Ala He Gin Leu Glu Pro Asp Gin He He His Tyr His Gly Val 1560 1565 1570 1575 GTA AAG TCC ATG TTA GGT CTT GGT CAG CTG TCT ACT GTT ATC ACT CAG 5105 Val Lys Ser Met Leu Gly Leu Gly Gin Leu Ser Thr Val He Thr Gin 1580 1585 1590 GTG AAT GGA GTG CAT GCT AAC AGG TCC GAG TGG ACA GAT GAA TTA AAC 5153 Val Asn Gly Val His Ala Asn Arg Ser Glu Trp Thr Asp Glu Leu Asn 1595 1600 1605 ACG TAC AGA GTG GAA GCA GCT TGG AAA TTG TCA CAG TGG GAT TTG GTG 5201 Thr Tyr Arg Val Glu Ala Ala Trp Lys Leu Ser Gin Trp Asp Leu Val 1610 1615 1620 GAA AAC TAT TTG GCA GCA GAT GGA AAA TCT ACA ACA TGG AGT GTC AGA 5249 Glu Asn Tyr Leu Ala Ala Asp Gly Lys Ser Thr Thr Trp Ser Val Arg 1625 1630 1635 CTG GGA CAG CTA TTA TTA TCA GCC AAA AAA AGA GAT ATC ACA GCT TTT 5297 Leu Gly Gin Leu Leu Leu Ser Ala Lys Lys Arg ABp He Thr Ala Phe 1640 1645 1650 1655 TAT GAC TCA CTG AAA CTA GTG AGA GCA GAA CAA ATT GTA CCT CTT TCA 5345 Tyr Asp Ser Leu Lys Leu Val Arg Ala Glu Gin He Val Pro Leu Ser 1660 1665 1670 GCT GCA AGC TTT GAA AGA GGC TCC TAC CAA CGA GGA TAT GAA TAT ATT 5393 Ala Ala Ser Phe Glu Arg Gly Ser Tyr Gin Arg Gly Tyr Glu Tyr He 1675 1680 1685 GTG AGA TTG CAC ATG TTA TGT GAG TTG GAG CAT AGC ATC AAA CCA CTT 5441 Val Arg Leu His Met Leu Cys Glu Leu Glu His Ser He Lys Pro Leu 1690 1695 1700 TTC CAG CAT TCT CCA GGT GAC AGT TCT CAA GAA GAT TCT CTA AAC TGG 5489 Phe Gin His Ser Pro Gly Asp Ser Ser Gin Glu Asp Ser Leu Asn Trp 1705 1710 1715 GTA GCT CGA CTA GAA ATG ACC CAG AAT TCC TAC AGA GCC AAG GAG CCT 5537 Val Ala Arg Leu Glu Met Thr Gin Asn Ser Tyr Arg Ala Lys Glu Pro 1720 1725 1730 1735 ATC CTG GCT CTC CGG AGG GCT TTA CTA AGC CTC AAC AAA AGA CCA GAT 5585 He Leu Ala Leu Arg Arg Ala Leu Leu Ser Leu Asn Lys Arg Pro Asp 1740 1745 1750 TAC AAT GAA ATG GTT GGA GAA TGC TGG CTG CAG AGT GCC AGG GTA GCT 5633 Tyr Asn Glu Met Val Gly Glu Cys Trp Leu Gin Ser Ala Arg Val Ala 1755 1760 1765 AGA AAG GCT GGT CAC CAC CAG ACA GCC TAC AAT GCT CTC CTT AAT GCA 5681 Arg Lys Ala Gly His His Gin Thr Ala Tyr Asn Ala Leu Leu Asn Ala 1770 1775 1780 GGG GAA TCA CGA CTC GCT GAA CTG TAC GTG GAA AGG GCA AAG TGG CTC 5729 Gly Glu Ser Arg Leu Ala Glu Leu Tyr Val Glu Arg Ala Lys Trp Leu 1785 1790 1795 TGG TCC AAG GGT GAT GTT CAC CAG GCA CTA ATT GTT CTT CAA AAA GGT 5777 Trp Ser Lys Gly Asp Val His Gin Ala Leu He Val Leu Gin Lys Gly 1800 1805 1810 1815 GTT GAA TTA TGT TTT CCT GAA AAT GAA ACC CCA CCT GAG GGT AAG AAC 5825 Val Glu Leu Cys Phe Pro Glu Asn Glu Thr Pro Pro Glu Gly Lys Asn 1820 1825 1830 ATG TTA ATC CAT GGT CGA GCT ATG CTA CTA GTG GGC CGA TTT ATG GAA 5873 Met Leu He His Gly Arg Ala Met Leu Leu Val Gly Arg Phe Met Glu 1835 1840 1845 GAA ACA GCT AAC TTT GAA AGC AAT GCA ATT ATG AAA AAA TAT AAG GAT 5921 Glu Thr Ala Asn Phe Glu Ser Asn Ala He Met Lys Lys Tyr Lys Asp 1850 1855 1860 GTG ACC GCG TGC CTG CCA GAA TGG GAG GAT GGG CAT TTT TAC CTT GCC 5969 Val Thr Ala Cys Leu Pro Glu Trp Glu Asp Gly His Phe Tyr Leu Ala 1865 1870 1875 AAG TAC TAT GAC AAA TTG ATG CCC ATG GTC ACA GAC AAC AAA ATG GAA 6017 Lys Tyr Tyr Asp Lys Leu Met Pro Met Val Thr Asp Asn Lys Met Glu 1880 1885 1890 1895 AAG CAA GGT GAT CTC ATC CGG TAT ATA GTT CTT CAT TTT GGC AGA TCT 6065 Lys Gin Gly Asp Leu He Arg Tyr He Val Leu His Phe Gly Arg Ser 1900 1905 1910 CTA CAA TAT GGA AAT CAG TTC ATA TAT CAG TCA ATG CCA CGA ATG TTA 6113 Leu Gin Tyr Gly Asn Gin Phe He Tyr Gin Ser Met Pro Arg Met Leu 1915 1920 1925 ACT CTA TGG CTT GAT TAT GGT ACA AAG GCA TAT GAA TGG GAA AAA GCT 6161 Thr Leu Trp Leu Asp Tyr Gly Thr Lys Ala Tyr Glu Trp Glu Lys Ala 1930 1935 1940 GGC CGC TCC GAT CGT GTA CAA ATG AGG AAT GAT TTG GGT AAA ATA AAC 6209 Gly Arg Ser Asp Arg Val Gin Met Arg Asn Asp Leu Gly Lys He Asn 1945 1950 1955 AAG GTT ATC ACA GAG CAT ACA AAC TAT TTA GCT CCA TAT CAA TTT TTG 6257 Lys Val He Thr Glu His Thr Asn Tyr Leu Ala Pro Tyr Gin Phe Leu 1960 1965 1970 1975 ACT GCT TTT TCA CAA TTG ATC TCT CGA ATT TGT CAT TCT CAC GAT GAA 6305 Thr Ala Phe Ser Gin Leu He Ser Arg He Cys His Ser His Asp Glu 1980 1985 1990 GTT TTT GTT GTG CTT GAT GGA AAT AAT AGC CAA GTA TTT CTA GCC TAT 6353 Val Phe Val Val Leu Asp Gly Asn Asn Ser Gin Val Phe Leu Ala Tyr 1995 2000 2005 CCT CAA CAA GCA ATG TGG ATG ATG ACA GCT GTG TCA AAG TCA TCT TAT 6401 Pro Gin Gin Ala Met Trp Met Met Thr Ala Val Ser Lys Ser Ser Tyr 2010 2015 2020 CCC ATG CGT GTG AAC AGA TGC AAG GAA ATC CTC AAT AAA GCT ATT CAT 6449 Pro Met Arg Val Asn Arg Cys Lys Glu He Leu Asn Lys Ala He His 2025 2030 2035 ATG AAA AAA TCC TTA GAG AAG TTT GTT GGA GAT GCA ACT CGC CTA ACA 6497 Met Lys Lys Ser Leu Glu Lys Phe Val Gly Asp Ala Thr Arg Leu Thr 2040 2045 2050 2055 GAT AAG CTT CTA GAA TTG TGC AAT AAA CCG GTG GAA ATT CTT GCT TCT 6545 Asp Lys Leu Leu Glu Leu Cys Asn Lys Pro Val Glu He Leu Ala Ser 2060 2065 2070 CTT CAG AAA CCA AAG AAG ATT TCT TTA AAA GGC TCA GAT GGA AAG TTC 6593 Leu Gin Lys Pro Lys Lys He Ser Leu Lys Gly Ser Asp Gly Lys Phe 2075 2080 2085 TAC ATC ATG ATG TGT AAG CCA AAA GAT GAC CTG AGA AAG GAT TGT AGA 6641 Tyr He Met Met Cys Lys Pro Lys Asp Asp Leu Arg Lys Asp Cys Arg 2090 2095 2100 CTA ATG GAA TTC AAT TCC TTG ATT AAT AAG TGC TTA AGA AAA GAT GCA 6689 Leu Met Glu Phe Asn Ser Leu He Asn Lys Cys Leu Arg Lys Asp Ala 2105 2110 2115 GAG TCT CGT AGA AGA GAA CTT CAT ATT CGA ACA TAT GCA GTT ATT CCA 6737 Glu Ser Arg Arg Arg Glu Leu His He Arg Thr Tyr Ala Val He Pro 2120 2125 2130 2135 CTA AAT GAT GAA TGT GGG ATT ATT GAA TGG GTG AAC AAC ACT GCT GGT 6785 Leu Asn Asp Glu Cys Gly He He Glu Trp Val Asn Asn Thr Ala Gly 2140 2145 2150 TTG AGA CCT ATT CTG ACC AAA CTA TAT AAA GAA AAG GGA GTG TAT ATG 6833 Leu Arg Pro He Leu Thr Lys Leu Tyr Lys Glu Lys Gly Val Tyr Met 2155 2160 2165 ACA GGA AAA GAA CTT CGC CAG TGT ATG CTA CCA AAG TCA GCA GCT TTA 6881 Thr Gly Lys Glu Leu Arg Gin Cys Met Leu Pro Lys Ser Ala Ala Leu 2170 2175 2180 TCT GAA AAA CTC AAA GTA TTC CGA GAA TTT CTC CTG CCC AGG CAT CCT 6929 Ser Glu Lys Leu Lys Val Phe Arg Glu Phe Leu Leu Pro Arg His Pro 2185 2190 2195 CCT ATT TTT CAT GAG TGG TTT CTG AGA ACA TTC CCT GAT CCT ACA TCA 6977 Pro He Phe His Glu Trp Phe Leu Arg Thr Phe Pro Asp Pro Thr Ser 2200 2205 2210 2215 TGG TAC AGT AGT AGA TCA GCT TAC TGC CGT TCC ACT GCA GTA ATG TCA 7025 Trp Tyr Ser Ser Arg Ser Ala Tyr Cys Arg Ser Thr Ala Val Met Ser 2220 2225 2230 ATG GTT GGT TAT ATT CTG GGG CTT GGA GAC CGT CAT GGT GAA AAT ATT 7073 Met Val Gly Tyr He Leu Gly Leu Gly Asp Arg His Gly Glu Asn He 2235 2240 2245 CTC TTT GAT TCT TTG ACT GGT GAA TGC GTA CAT GTA GAT TTC AAT TGT 7121 Leu Phe Asp Ser Leu Thr Gly Glu Cys Val His Val Asp Phe Asn Cys 2250 2255 2260 CTT TTC AAT AAG GGA GAA ACC TTT GAA GTT CCA GAA ATT GTG CCA TTT 7169 Leu Phe Asn Lys Gly Glu Thr Phe Glu Val Pro Glu He Val Pro Phe 2265 2270 2275 CGC CTG ACT CAT AAT ATG GTT AAT GGA ATG GGT CCT ATG GGA ACA GAG 7217 Arg Leu Thr His Asn Met Val Asn Gly Met Gly Pro Met Gly Thr Glu 2280 2285 2290 2295 GGT CTT TTT CGA AGA GCA TGT GAA GTT ACA ATG AGG CTG ATG CGT GAT 7265 Gly Leu Phe Arg Arg Ala Cys Glu Val Thr Met Arg Leu Met Arg Asp 2300 2305 2310 CAG CGA GAG CCT TTA ATG AGT GTC TTA AAG ACT TTT CTA CAT GAT CCT 7313 Gin Arg Glu Pro Leu Met Ser Val Leu Lys Thr Phe Leu His Asp Pro 2315 2320 2325 CTT GTG GAA TGG AGT AAA CCA GTG AAA GGG CAT TCC AAA GCG CCA CTG 7361 Leu Val Glu Trp Ser Lys Pro Val Lys Gly His Ser Lys Ala Pro Leu 2330 2335 2340 AAT GAA ACT GGA GAA GTT GTC AAT GAA AAG GCC AAG ACC CAT GTT CTT 7409 Asn Glu Thr Gly Glu Val Val Asn Glu Lys Ala Lys Thr His Val Leu 2345 2350 2355 GAC ATT GAG CAG CGA CTA CAA GGT GTA ATC AAG ACT CGA AAT AGA GTG 7457 Asp He Glu Gin Arg Leu Gin Gly Val He Lys Thr Arg Asn Arg Val 2360 2365 2370 2375 ACA GGA CTG CCG TTA TCT ATT GAA GGA CAT GTG CAT TAC CTT ATA CAA 7505 Thr Gly Leu Pro Leu Ser He Glu Gly His Val His Tyr Leu He Gin 2380 2385 2390 GAA GCT ACT GAT GAA AAC TTA CTA TGC CAG ATG TAT CTT GGT TGG ACT 7553 Glu Ala Thr Asp Glu Asn Leu Leu Cys Gin Met Tyr Leu Gly Trp Thr 2395 2400 2405 CCA TAT ATG TGAAATGAAA TTATGTAAAA GAATATGTTA ATAATCTAAA 7602 Pro Tyr Met 2410 AGTAAAAAAA AAAAAAAAAA AA 7624 (2) INFORMATION FOR SEQ ID NO:24: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2410 amino acids (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:24: Met Gly His Ala Val Glu Trp Pro Val Val Met Ser Arg Phe Leu Ser 1 5 10 15 Gin Leu Asp Glu His Met Gly Tyr Leu Gin Ser Ala Pro Leu Gin Leu 20 25 30 Met Ser Met Gin Asn Leu Glu Phe He Glu Val Thr Leu Leu Met Val 35 40 45 Leu Thr Arg He He Ala He Val Phe Phe Arg Arg Gin Glu Leu Leu 50 55 60 Leu Trp Gin He Gly Cys Val Leu Leu Glu Tyr Gly Ser Pro Lys He 65 70 75 80 Lys Ser Leu Ala He Ser Phe Leu Thr Glu Leu Phe Gin Leu Gly Gly 85 90 95 Leu Pro Ala Gin Pro Ala Ser Thr Phe Phe Ser Ser Phe Leu Glu Leu 100 105 110 Leu Lys His Leu Val Glu Met Asp Thr Asp Gin Leu Lys Leu Tyr Glu 115 120 125 Glu Pro Leu Ser Lys Leu He Lys Thr Leu Phe Pro Phe Glu Ala Glu 130 135 140 Ala Tyr Arg Asn He Glu Pro Val Tyr Leu Asn Met Leu Leu Glu Lys 145 150 155 160 Leu Cys Val Met Phe Glu Asp Gly Val Leu Met Arg Leu Lys Ser Asp 165 170 175 Leu Leu Lys Ala Ala Leu Cys His Leu Leu Gin Tyr Phe Leu Lys Phe 180 185 190 Val Pro Ala Gly Tyr Glu Ser Ala Leu Gin Val Arg Lys Val Tyr Val 195 200 205 Arg Asn He Cys Lys Ala Leu Leu Asp Val Leu Gly He Glu Val Asp 210 215 220 Ala Glu Tyr Leu Leu Gly Pro Leu Tyr Ala Ala Leu Lys Met Glu Ser 225 230 235 240 Met Glu He He Glu Glu He Gin Cys Gin Thr Gin Gin Glu Asn Leu 245 250 255 Ser Ser Asn Ser Asp Gly He Ser Pro Lys Arg Arg Arg Leu Ser Ser 260 265 270 Ser Leu Asn Pro Ser Lys Arg Ala Pro Lys Gin Thr Glu Glu He Lys 275 280 285 His Val Asp Met Asn Gin Lys Ser He Leu Trp Ser Ala Leu Lys Gin 290 295 300 Lys Ala Glu Ser Leu Gin He Ser Leu Glu Tyr Ser Gly Leu Lys Asn 305 310 315 320 Pro Val He Glu Met Leu Glu Gly He Ala Val Val Leu Gin Leu Thr 325 330 335 Ala Leu Cys Thr Val His Cys Ser His Gin Asn Met Asn Cys Arg Thr 340 345 350 Phe Lys Asp Cys Gin His Lys Ser Lys Lys Lys Pro Ser Val Val He 355 360 365 Thr Trp Met Ser Leu Asp Phe Tyr Thr Lys Val Leu Lys Ser Cys Arg 370 375 380 Ser Leu Leu Glu Ser Val Gin Lys Leu Asp Leu Glu Ala Thr He Asp 385 390 395 400 Lys Val Val Lys He Tyr Asp Ala Leu He Tyr Met Gin Val Asn Ser 405 410 415 Ser Phe Glu Asp His He Leu Glu Asp Leu Cys Gly Met Leu Ser Leu 420 425 430 Pro Trp He Tyr Ser His Ser Asp Asp Gly Cys Leu Lys Leu Thr Thr 435 440 445 Phe Ala Ala Asn Leu Leu Thr Leu Ser Cys Arg He Ser Asp Ser Tyr 450 455 460 Ser Pro Gin Ala Gin Ser Arg Cys Val Phe Leu Leu Thr Leu Phe Pro 465 470 475 480 Arg Arg He Phe Leu Glu Trp Arg Thr Ala Val Tyr Asn Trp Ala Leu 485 490 495 Gin Ser Ser His Glu Val He Arg Ala Ser Cys Val Ser Gly Phe Phe 500 505 510 He Leu Leu Gin Gin Gin Asn Ser Cys Asn Arg Val Pro Lys He Leu 515 520 525 He Asp Lys Val Lys Asp Asp Ser Asp He Val Lys Lys Glu Phe Ala 530 535 540 Ser He Leu Gly Gin Leu Val Cys Thr Leu His Gly Met Phe Tyr Leu 545 550 555 560 Thr Ser Ser Leu Thr Glu Pro Phe Ser Glu His Gly His Val Asp Leu 565 570 575 Phe Cys Arg Asn Leu Lys Ala Thr Ser Gin His Glu Cys Ser Ser Ser 580 585 590 Gin Leu Lys Ala Ser Val Cys Lys Pro Phe Leu Phe Leu Leu Lys Lys 595 600 605 Lys He Pro Ser Pro Val Lys Leu Ala Phe He Asp Asn Leu His His 610 615 620 Leu Cys Lys His Leu Asp Phe Arg Glu Asp Glu Thr Asp Val Lys Ala 625 630 635 640 Val Leu Gly Thr Leu Leu Asn Leu Met Glu Asp Pro Asp Lys Asp Val 645 650 655 Arg Val Ala Phe Ser Gly Asn He Lys His He Leu Glu Ser Leu Asp 660 665 670 Ser Glu Asp Gly Phe He Lys Glu Leu Phe Val Leu Arg Met Lys Glu 675 680 685 Ala Tyr Thr His Ala Gin He Ser Arg Asn Asn Glu Leu Lys Asp Thr 690 695 700 Leu He Leu Thr Thr Gly Asp He Gly Arg Ala Ala Lys Gly Asp Leu 705 710 715 720 Val Pro Phe Ala Leu Leu His Leu Leu His Cys Leu Leu Ser Lys Ser 725 730 735 Ala Ser Val Ser Gly Ala Ala Tyr Thr Glu He Arg Ala Leu Val Ala 740 745 750 Ala Lys Ser Val Lys Leu Gin Ser Phe Phe Ser Gin Tyr Lys Lys Pro 755 760 765 He Cys Gin Phe Leu Val Glu Ser Leu His Ser Ser Gin Met Thr Ala 770 775 780 Leu Pro Asn Thr Pro Cys Gin Asn Ala Asp Val Arg Lys Gin Asp Val 785 790 795 800 Ala His Gin Arg Glu Met Ala Leu Asn Thr Leu Ser Glu He Ala Asn 805 810 815 Val Phe Asp Phe Pro Asp Leu Asn Arg Phe Leu Thr Arg Thr Leu Gin 820 825 830 Val Leu Leu Pro Asp Leu Ala Ala Lys Ala Ser Pro Ala Ala Ser Ala 835 840 845 Leu He Arg Thr Leu Gly Lys Gin Leu Asn Val Asn Arg Arg Glu He 850 855 860 Leu He Asn Asn Phe Lys Tyr He Phe Ser His Leu Val Cys Ser Cys 865 870 875 880 Ser Lys Asp Glu Leu Glu Arg Ala Leu His Tyr Leu Lys Asn Glu Thr 885 890 895 Glu He Glu Leu Gly Ser Leu Leu Arg Gin Asp Phe Gin Gly Leu His 900 905 910 Asn Glu Leu Leu Leu Arg He Gly Glu His Tyr Gin Gin Val Phe Asn 915 920 925 Gly Leu Ser He Leu Ala Ser Phe Ala Ser Ser Asp Asp Pro Tyr Gin 930 935 940 Gly Pro Arg Asp He He Ser Pro Glu Leu Met Ala Asp Tyr Leu Gin 945 950 955 960 Pro Lys Leu Leu Gly He Leu Ala Phe Phe Asn Met Gin Leu Leu Ser 965 970 975 Ser Ser Val Gly He Glu Asp Lys Lys Met Ala Leu Asn Ser Leu Met 980 985 990 Ser Leu Met Lys Leu Met Gly Pro Lys His Val Ser Ser Val Arg Val 995 1000 1005 Lys Met Met Thr Thr Leu Arg Thr Gly Leu Arg Phe Lys Asp Asp Phe 1010 1015 1020 Pro Glu Leu Cys Cys Arg Ala Trp Asp Cys Phe Val Arg Cys Leu Asp 1025 1030 1035 1040 His Ala Cys Leu Gly Ser Leu Leu Ser His Val He Val Ala Leu Leu 1045 1050 1055 Pro Leu He His He Gin Pro Lys Glu Thr Ala Ala He Phe His Tyr 1060 1065 1070 Leu He He Glu Asn Arg Asp Ala Val Gin Asp Phe Leu His Glu He 1075 1080 1085 Tyr Phe Leu Pro Asp His Pro Glu Leu Lys Lys He Lys Ala Val Leu 1090 1095 1100 Gin Glu Tyr Arg Lys Glu Thr Ser Glu Ser Thr Asp Leu Gin Thr Thr 1105 1110 1115 1120 Leu Gin Leu Ser Met Lys Ala He Gin His Glu Asn Val Asp Val Arg 1125 1130 1135 He His Ala Leu Thr Ser Leu Lys Glu Thr Leu Tyr Lys Asn Gin Glu 1140 1145 1150 Lys Leu He Lys Tyr Ala Thr Asp Ser Glu Thr Val Glu Pro He He 1155 1160 1165 Ser Gin Leu Val Thr Val Leu Leu Lys Gly Cys Gin Asp Ala Asn Ser 1170 1175 1180 Gin Ala Arg Leu Leu Cys Gly Glu Cys Leu Gly Glu Leu Gly Ala He 1185 1190 1195 1200 Asp Pro Gly Arg Leu Asp Phe Ser Thr Thr Glu Thr Gin Gly Lys Asp 1205 1210 1215 Phe Thr Phe Val Thr Gly Val Glu Asp Ser Ser Phe Ala Tyr Gly Leu 1220 1225 1230 Leu Met Glu Leu Thr Arg Ala Tyr Leu Ala Tyr Ala Asp Asn Ser Arg 1235 1240 1245 Ala Gin Asp Ser Ala Ala Tyr Ala He Gin Glu Leu Leu Ser He Tyr 1250 1255 1260 Asp Cys Arg Glu Met Glu Thr Asn Gly Pro Gly His Gin Leu Trp Arg 1265 1270 1275 1280 Arg Phe Pro Glu His Val Arg Glu He Leu Glu Pro His Leu Asn Thr 1285 1290 1295 Arg Tyr Lys Ser Ser Gin Lys Ser Thr Asp Trp Ser Gly Val Lys Lys 1300 1305 1310 Pro He Tyr Leu Ser Lys Leu Gly Ser Asn Phe Ala Glu Trp Ser Ala 1315 1320 1325 Ser Trp Ala Gly Tyr Leu He Thr Lys Val Arg His Asp Leu Ala Ser 1330 1335 1340 Lys He Phe Thr Cys Cys Ser He Met Met Lys His Asp Phe Lys Val 1345 1350 1355 1360 Thr He Tyr Leu Leu Pro His He Leu Val Tyr Val Leu Leu Gly Cys 1365 1370 1375 Asn Gin Glu Asp Gin Gin Glu Val Tyr Ala Glu He Met Ala Val Leu 1380 1385 1390 Lys His Asp Asp Gin His Thr He Asn Thr Gin Asp He Ala Ser Asp 1395 1400 1405 Leu Cys Gin Leu Ser Thr Gin Thr Val Phe Ser Met Leu Asp His Leu 1410 1415 1420 Thr Gin Trp Ala Arg His Lys Phe Gin Ala Leu Lys Ala Glu Lys Cys 1425 1430 1435 1440 Pro His Ser Lys Ser Asn Arg Asn Lys Val Asp Ser Met Val Ser Thr 1445 1450 1455 Val Asp Tyr Glu Asp Tyr Gin Ser Val Thr Arg Phe Leu Asp Leu He 1460 1465 1470 Pro Gin Asp Thr Leu Ala Val Ala Ser Phe Arg Ser Lys Ala Tyr Thr 1475 1480 1485 Arg Ala Val Met His Phe Glu Ser Phe He Thr Glu Lys Lys Gin Asn 1490 1495 1500 He Gin Glu His Leu Gly Phe Leu Gin Lys Leu Tyr Ala Ala Met His 1505 1510 1515 1520 Glu Pro Asp Gly Val Ala Gly Val Ser Ala He Arg Lys Ala Glu Pro 1525 1530 1535 Ser Leu Lys Glu Gin He Leu Glu His Glu Ser Leu Gly Leu Leu Arg 1540 1545 1550 Asp Ala Thr Ala Cys Tyr Asp Arg Ala He Gin Leu Glu Pro Asp Gin 1555 1560 1565 He He His Tyr His Gly Val Val Lys Ser Met Leu Gly Leu Gly Gin 1570 1575 1580 Leu Ser Thr Val He Thr Gin Val Asn Gly Val His Ala Asn Arg Ser 1585 1590 1595 1600 Glu Trp Thr Asp Glu Leu Asn Thr Tyr Arg Val Glu Ala Ala Trp Lys 1605 1610 1615 Leu Ser Gin Trp Asp Leu Val Glu Asn Tyr Leu Ala Ala Asp Gly Lys 1620 1625 1630 Ser Thr Thr Trp Ser Val Arg Leu Gly Gin Leu Leu Leu Ser Ala Lys 1635 1640 1645 Lys Arg Asp He Thr Ala Phe Tyr Asp Ser Leu Lys Leu Val Arg Ala 1650 1655 1660 Glu Gin He Val Pro Leu Ser Ala Ala Ser Phe Glu Arg Gly Ser Tyr 1665 1670 1675 1680 Gin Arg Gly Tyr Glu Tyr He Val Arg Leu His Met Leu Cys Glu Leu 1685 1690 1695 Glu His Ser He Lys Pro Leu Phe Gin His Ser Pro Gly Asp Ser Ser 1700 1705 1710 Gin Glu Asp Ser Leu Asn Trp Val Ala Arg Leu Glu Met Thr Gin Asn 1715 1720 1725 Ser Tyr Arg Ala Lys Glu Pro He Leu Ala Leu Arg Arg Ala Leu Leu 1730 1735 1740 Ser Leu Asn Lys Arg Pro Asp Tyr Asn Glu Met Val Gly Glu Cys Trp 1745 1750 1755 1760 Leu Gin Ser Ala Arg Val Ala Arg Lys Ala Gly His His Gin Thr Ala 1765 1770 1775 Tyr Asn Ala Leu Leu Asn Ala Gly Glu Ser Arg Leu Ala Glu Leu Tyr 1780 1785 1790 Val Glu Arg Ala Lys Trp Leu Trp Ser Lys Gly Asp Val His Gin Ala 1795 1800 1805 Leu He Val Leu Gin Lys Gly Val Glu Leu Cys Phe Pro Glu Asn Glu 1810 1815 1820 Thr Pro Pro Glu Gly Lys Asn Met Leu He His Gly Arg Ala Met Leu 1825 1830 1835 1840 Leu Val Gly Arg Phe Met Glu Glu Thr Ala Asn Phe Glu Ser Asn Ala 1845 1850 1855 He Met Lys Lys Tyr Lys Asp Val Thr Ala Cys Leu Pro Glu Trp Glu 1860 1865 1870 Asp Gly His Phe Tyr Leu Ala Lys Tyr Tyr Asp Lys Leu Met Pro Met 1875 1880 1885 Val Thr Asp Asn Lys Met Glu Lys Gin Gly Asp Leu He Arg Tyr He 1890 1895 1900 Val Leu His Phe Gly Arg Ser Leu Gin Tyr Gly Asn Gin Phe He Tyr 1905 1910 1915 1920 Gin Ser Met Pro Arg Met Leu Thr Leu Trp Leu Asp Tyr Gly Thr Lys 1925 1930 1935 Ala Tyr Glu Trp Glu Lys Ala Gly Arg Ser Asp Arg Val Gin Met Arg 1940 1945 1950 Asn Asp Leu Gly Lys He Asn Lys Val He Thr Glu His Thr Asn Tyr 1955 1960 1965 Leu Ala Pro Tyr Gin Phe Leu Thr Ala Phe Ser Gin Leu He Ser Arg 1970 1975 1980 He Cys His Ser His Asp Glu Val Phe Val Val Leu Asp Gly Asn Asn 1985 1990 1995 2000 Ser Gin Val Phe Leu Ala Tyr Pro Gin Gin Ala Met Trp Met Met Thr 2005 2010 2015 Ala Val Ser Lys Ser Ser Tyr Pro Met Arg Val Asn Arg Cys Lys Glu 2020 2025 2030 He Leu Asn Lys Ala He His Met Lys Lys Ser Leu Glu Lys Phe Val 2035 2040 2045 Gly Asp Ala Thr Arg Leu Thr Asp Lys Leu Leu Glu Leu Cys Asn Lys 2050 2055 2060 Pro Val Glu He Leu Ala Ser Leu Gin Lys Pro Lys Lys He Ser Leu 2065 2070 2075 2080 Lys Gly Ser Asp Gly Lys Phe Tyr He Met Met Cys Lys Pro Lys Asp 2085 2090 2095 Asp Leu Arg Lys Asp Cys Arg Leu Met Glu Phe Asn Ser Leu He Asn 2100 2105 2110 Lys Cys Leu Arg Lys Asp Ala Glu Ser Arg Arg Arg Glu Leu His He 2115 2120 2125 Arg Thr Tyr Ala Val He Pro Leu Asn Asp Glu Cys Gly He He Glu 2130 2135 2140 Trp Val Asn Asn Thr Ala Gly Leu Arg Pro He Leu Thr Lys Leu Tyr 2145 2150 2155 2160 Lys Glu Lys Gly Val Tyr Met Thr Gly Lys Glu Leu Arg Gin Cys Met 2165 2170 2175 Leu Pro Lys Ser Ala Ala Leu Ser Glu Lys Leu Lys Val Phe Arg Glu 2180 2185 2190 Phe Leu Leu Pro Arg His Pro Pro He Phe His Glu Trp Phe Leu Arg 2195 2200 2205 Thr Phe Pro Asp Pro Thr Ser Trp Tyr Ser Ser Arg Ser Ala Tyr Cys 2210 2215 2220 Arg Ser Thr Ala Val Met Ser Met Val Gly Tyr He Leu Gly Leu Gly 2225 2230 2235 2240 Asp Arg His Gly Glu Asn He Leu Phe Asp Ser Leu Thr Gly Glu Cys 2245 2250 2255 Val His Val Asp Phe Asn Cys Leu Phe Asn Lys Gly Glu Thr Phe Glu 2260 2265 2270 Val Pro Glu He Val Pro Phe Arg Leu Thr His Asn Met Val Asn Gly 2275 2280 2285 Met Gly Pro Met Gly Thr Glu Gly Leu Phe Arg Arg Ala Cys Glu Val 2290 2295 2300 Thr Met Arg Leu Met Arg Asp Gin Arg Glu Pro Leu Met Ser Val Leu 2305 2310 2315 2320 Lys Thr Phe Leu His Asp Pro Leu Val Glu Trp Ser Lys Pro Val Lys 2325 2330 2335 Gly His Ser Lys Ala Pro Leu Asn Glu Thr Gly Glu Val Val Asn Glu 2340 2345 2350 Lys Ala Lys Thr His Val Leu Asp He Glu Gin Arg Leu Gin Gly Val 2355 2360 2365 Ile Lys Thr Arg Asn Arg Val Thr Gly Leu Pro Leu Ser He Glu Gly 2370 2375 2380 His Val His Tyr Leu He Gin Glu Ala Thr Asp Glu Asn Leu Leu Cys 2385 2390 2395 2400 Gin Met Tyr Leu Gly Trp Thr Pro Tyr Met 2405 2410 (2) INFORMATION FOR SEQ ID NO:25: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 7502 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (u) MOLECULE TYPE: cDNA (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 1..7440 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:25: ATG GGT CAT GCT GTG GAA TGG CCA GTG GTC ATG AGC CGA TTT TTA AGT 48 Met Gly His Ala Val Glu Trp Pro Val Val Met Ser Arg Phe Leu Ser 1 5 10 15 CAA TTA GAT GAA CAC ATG GGA TAT TTA CAA TCA GCT CCT TTG CAG TTG 96 Gin Leu Asp Glu His Met Gly Tyr Leu Gin Ser Ala Pro Leu Gin Leu 20 25 30 ATG AGT ATG CAA AAT TTA GAA TTT ATT GAA GTC ACT TTA TTA ATG GTT 144 Met Ser Met Gin Asn Leu Glu Phe He Glu Val Thr Leu Leu Met Val 35 40 45 CTT ACT CGT ATT ATT GCA ATT GTG TTT TTT AGA AGG CAA GAA CTC TTA 192 Leu Thr Arg He He Ala He Val Phe Phe Arg Arg Gin Glu Leu Leu 50 55 60 CTT TGG CAG ATA GGT TGT GTT CTG CTA GAG TAT GGT AGT CCA AAA ATT 240 Leu Trp Gin He Gly Cys Val Leu Leu Glu Tyr Gly Ser Pro Lys He 65 70 75 80 AAA TCC CTA GCA ATT AGC TTT TTA ACA GAA CTT TTT CAG CTT GGA GGA 288 Lys Ser Leu Ala He Ser Phe Leu Thr Glu Leu Phe Gin Leu Gly Gly 85 90 95 CTA CCA GCA CAA CCA GCT AGC ACT TTT TTC AGC TCA TTT TTG GAA TTA 336 Leu Pro Ala Gin Pro Ala Ser Thr Phe Phe Ser Ser Phe Leu Glu Leu 100 105 110 TTA AAA CAC CTT GTA GAA ATG GAT ACT GAC CAA TTG AAA CTC TAT GAA 384 Leu Lys His Leu Val Glu Met Asp Thr Asp Gin Leu Lys Leu Tyr Glu 115 120 125 GAG CCA TTA TCA AAG CTG ATA AAG ACA CTA TTT CCC TTT GAA GCA GAA 432 Glu Pro Leu Ser Lys Leu He Lys Thr Leu Phe Pro Phe Glu Ala Glu 130 135 140 GCT TAT AGA AAT ATT GAA CCT GTC TAT TTA AAT ATG CTG CTG GAA AAA 480 Ala Tyr Arg Asn He Glu Pro Val Tyr Leu Asn Met Leu Leu Glu Lys 145 150 155 160 CTC TGT GTC ATG TTT GAA GAC GGT GTG CTC ATG CGG CTT AAG TCT GAT 528 Leu Cys Val Met Phe Glu Asp Gly Val Leu Met Arg Leu Lys Ser Asp 165 170 175 TTG CTA AAA GCA GCT TTG TGC CAT TTA CTG CAG TAT TTC CTT AAA TTT 576 Leu Leu Lys Ala Ala Leu Cys His Leu Leu Gin Tyr Phe Leu Lys Phe 180 185 190 GTG CCA GCT GGG TAT GAA TCT GCT TTA CAA GTC AGG AAG GTC TAT GTG 624 Val Pro Ala Gly Tyr Glu Ser Ala Leu Gin Val Arg Lys Val Tyr Val 195 200 205 AGA AAT ATT TGT AAA GCT CTT TTG GAT GTG CTT GGA ATT GAG GTA GAT 672 Arg Asn He Cys Lys Ala Leu Leu Asp Val Leu Gly He Glu Val Asp 210 215 220 GCA GAG TAC TTG TTG GGC CCA CTT TAT GCA GCT TTG AAA ATG GAA AGT 720 Ala Glu Tyr Leu Leu Gly Pro Leu Tyr Ala Ala Leu Lys Met Glu Ser 225 230 235 240 ATG GAA ATC ATT GAG GAG ATT CAA TGC CAA ACT CAA CAG GAA AAC CTC 768 Met Glu He He Glu Glu He Gin Cys Gin Thr Gin Gin Glu Asn Leu 245 250 255 AGC AGT AAT AGT GAT GGA ATA TCA CCC AAA AGG CGT CGT CTC AGC TCG 816 Ser Ser Asn Ser Asp Gly He Ser Pro Lys Arg Arg Arg Leu Ser Ser 260 265 270 TCT CTA AAC CCT TCT AAA AGA GCA CCA AAA CAG ACT GAG GAA ATT AAA 864 Ser Leu Asn Pro Ser Lys Arg Ala Pro Lys Gin Thr Glu Glu He Lys 275 280 285 CAT GTG GAC ATG AAC CAA AAG AGC ATA TTA TGG AGT GCA CTG AAA CAG 912 His Val Asp Met Asn Gin Lys Ser He Leu Trp Ser Ala Leu Lys Gin 290 295 300 AAA GCT GAA TCC CTT CAG ATT TCC CTT GAA TAC AGT GGC CTA AAG AAT 960 Lys Ala Glu Ser Leu Gin He Ser Leu Glu Tyr Ser Gly Leu Lys Asn 305 310 315 320 CCT GTT ATT GAG ATG TTA GAA GGA ATT GCT GTT GTC TTA CAA CTG ACT 1008 Pro Val He Glu Met Leu Glu Gly He Ala Val Val Leu Gin Leu Thr 325 330 335 GCT CTG TGT ACT GTT CAT TGT TCT CAT CAA AAC ATG AAC TGC CGT ACT 1056 Ala Leu Cys Thr Val His Cys Ser His Gin Asn Met Asn Cys Arg Thr 340 345 350 TTC AAG GAC TGT CAA CAT AAA TCC AAG AAG AAA CCT TCT GTA GTG ATA 1104 Phe Lys Asp Cys Gin His Lys Ser Lys Lys Lys Pro Ser Val Val He 355 360 365 ACT TGG ATG TCA TTG GAT TTT TAC ACA AAA GTG CTT AAG AGC TGT AGA 1152 Thr Trp Met Ser Leu Asp Phe Tyr Thr Lys Val Leu Lys Ser Cys Arg 370 375 380 AGT TTG TTA GAA TCT GTT CAG AAA CTG GAC CTG GAG GCA ACC ATT GAT 1200 Ser Leu Leu Glu Ser Val Gin Lys Leu Asp Leu Glu Ala Thr He Asp 385 390 395 400 AAG GTG GTG AAA ATT TAT GAT GCT TTG ATT TAT ATG CAA GTA AAC AGT 1248 Lys Val Val Lys He Tyr Asp Ala Leu He Tyr Met Gin Val Asn Ser 405 410 415 TCA TTT GAA GAT CAT ATC CTG GAA GAT TTA TGT GGA ATG CTC TCA CTT 1296 Ser Phe Glu Asp His He Leu Glu Asp Leu Cys Gly Met Leu Ser Leu 420 425 430 CCA TGG ATT TAT TCC CAT TCT GAT GAT GGC TGT TTA AAG TTG ACC ACA 1344 Pro Trp He Tyr Ser His Ser Asp Asp Gly Cys Leu Lys Leu Thr Thr 435 440 445 TTT GCC GCT AAT CTT CTA ACA TTA AGC TGT AGG ATT TCA GAT AGC TAT 1392 Phe Ala Ala Asn Leu Leu Thr Leu Ser Cys Arg He Ser Asp Ser Tyr 450 455 460 TCA CCA CAG GCA CAA TCA CGA TGT GTG TTT CTT CTG ACT CTG TTT CCA 1440 Ser Pro Gin Ala Gin Ser Arg Cys Val Phe Leu Leu Thr Leu Phe Pro 465 470 475 480 AGA AGA ATA TTC CTT GAG TGG AGA ACA GCA GTT TAC AAC TGG GCC CTG 1488 Arg Arg He Phe Leu Glu Trp Arg Thr Ala Val Tyr Asn Trp Ala Leu 485 490 495 CAG AGC TCC CAT GAA GTA ATC CGG GCT AGT TGT GTT AGT GGA TTT TTT 1536 Gin Ser Ser His Glu Val He Arg Ala Ser Cys Val Ser Gly Phe Phe 500 505 510 ATC TTA TTG CAG CAG CAG AAT TCT TGT AAC AGA GTT CCC AAG ATT CTT 1584 He Leu Leu Gin Gin Gin Asn Ser Cys Asn Arg Val Pro Lys He Leu 515 520 525 ATA GAT AAA GTC AAA GAT GAT TCT GAC ATT GTC AAG AAA GAA TTT GCT 1632 He Asp Lys Val Lys Asp Asp Ser Asp He Val Lys Lys Glu Phe Ala 530 535 540 TCT ATA CTT GGT CAA CTT GTC TGT ACT CTT CAC GGC ATG TTT TAT CTG 1680 Ser He Leu Gly Gin Leu Val Cys Thr Leu His Gly Met Phe Tyr Leu 545 550 555 560 ACA AGT TCT TTA ACA GAA CCT TTC TCT GAA CAC GGA CAT GTG GAC CTC 1728 Thr Ser Ser Leu Thr Glu Pro Phe Ser Glu His Gly His Val Asp Leu 565 570 575 TTC TGT AGG AAC TTG AAA GCC ACT TCT CAA CAT GAA TGT TCA TCT TCT 1776 Phe Cys Arg Asn Leu Lys Ala Thr Ser Gin His Glu Cys Ser Ser Ser 580 585 590 CAA CTA AAA GCT TCT GTC TGC AAG CCA TTC CTT TTC CTA CTG AAA AAA 1824 Gin Leu Lys Ala Ser Val Cys Lys Pro Phe Leu Phe Leu Leu Lys Lys 595 600 605 AAA ATA CCT AGT CCA GTA AAA CTT GCT TTC ATA GAT AAT CTA CAT CAT 1872 Lys He Pro Ser Pro Val Lys Leu Ala Phe He Asp Asn Leu His His 610 615 620 CTT TGT AAG CAT CTT GAT TTT AGA GAA GAT GAA ACA GAT GTA AAA GCA 1920 Leu Cys Lys His Leu Asp Phe Arg Glu Asp Glu Thr Asp Val Lys Ala 625 630 635 640 GTT CTT GGA ACT TTA TTA AAT TTA ATG GAA GAT CCA GAC AAA GAT GTT 1968 Val Leu Gly Thr Leu Leu Asn Leu Met Glu Asp Pro Asp Lys Asp Val 645 650 655 AGA GTG GCT TTT AGT GGA AAT ATC AAG CAC ATA TTG GAA TCC TTG GAC 2016 Arg Val Ala Phe Ser Gly Asn He Lys His He Leu Glu Ser Leu Asp 660 665 670 TCT GAA GAT GGA TTT ATA AAG GAG CTT TTT GTC TTA AGA ATG AAG GAA 2064 Ser Glu Asp Gly Phe He Lys Glu Leu Phe Val Leu Arg Met Lys Glu 675 680 685 GCA TAT ACA CAT GCC CAA ATA TCA AGA AAT AAT GAG CTG AAG GAT ACC 2112 Ala Tyr Thr His Ala Gin He Ser Arg Asn Asn Glu Leu Lys Asp Thr 690 695 700 TTG ATT CTT ACA ACA GGG GAT ATT GGA AGG GCC GCA AAA GGA GAT TTG 2160 Leu He Leu Thr Thr Gly Asp He Gly Arg Ala Ala Lys Gly Asp Leu 705 710 715 720 GTA CCA TTT GCA CTC TTA CAC TTA TTG CAT TGT TTG TTA TCC AAG TCA 2208 Val Pro Phe Ala Leu Leu His Leu Leu His Cys Leu Leu Ser Lys Ser 725 730 735 GCA TCT GTC TCT GGA GCA GCA TAC ACA GAA ATT AGA GCT CTG GTT GCA 2256 Ala Ser Val Ser Gly Ala Ala Tyr Thr Glu He Arg Ala Leu Val Ala 740 745 750 GCT AAA AGT GTT AAA CTG CAA AGT TTT TTC AGC CAG TAT AAG AAA CCC 2304 Ala Lys Ser Val Lys Leu Gin Ser Phe Phe Ser Gin Tyr Lys Lys Pro 755 760 765 ATC TGT CAG TTT TTG GTA GAA TCC CTT CAC TCT AGT CAG ATG ACA GCA 2352 He Cys Gin Phe Leu Val Glu Ser Leu His Ser Ser Gin Met Thr Ala 770 775 780 CTT CCG AAT ACT CCA TGC CAG AAT GCT GAC GTG CGA AAA CAA GAT GTG 2400 Leu Pro Asn Thr Pro Cys Gin Asn Ala Asp Val Arg Lys Gin Asp Val 785 790 795 800 GCT CAC CAG AGA GAA ATG GCT TTA AAT ACG TTG TCT GAA ATT GCC AAC 2448 Ala His Gin Arg Glu Met Ala Leu Asn Thr Leu Ser Glu He Ala Asn 805 810 815 GTT TTC GAC TTT CCT GAT CTT AAT CGT TTT CTT ACT AGG ACA TTA CAA 2496 Val Phe Asp Phe Pro Asp Leu Asn Arg Phe Leu Thr Arg Thr Leu Gin 820 825 830 GTT CTA CTA CCT GAT CTT GCT GCC AAA GCA AGC CCT GCA GCT TCT GCT 2544 Val Leu Leu Pro Asp Leu Ala Ala Lys Ala Ser Pro Ala Ala Ser Ala 835 840 845 CTC ATT CGA ACT TTA GGA AAA CAA TTA AAT GTC AAT CGT AGA GAG ATT 2592 Leu He Arg Thr Leu Gly Lys Gin Leu Asn Val Asn Arg Arg Glu He 850 855 860 TTA ATA AAC AAC TTC AAA TAT ATT TTT TCT CAT TTG GTC TGT TCT TGT 2640 Leu He Asn Asn Phe Lys Tyr He Phe Ser His Leu Val Cys Ser Cys 865 870 875 880 TCC AAA GAT GAA TTA GAA CGT GCC CTT CAT TAT CTG AAG AAT GAA ACA 2688 Ser Lys Asp Glu Leu Glu Arg Ala Leu His Tyr Leu Lys Asn Glu Thr 885 890 895 GAA ATT GAA CTG GGG AGC CTG TTG AGA CAA GAT TTC CAA GGA TTG CAT 2736 Glu He Glu Leu Gly Ser Leu Leu Arg Gin Asp Phe Gin Gly Leu His 900 905 910 AAT GAA TTA TTG CTG CGT ATT GGA GAA CAC TAT CAA CAG GTT TTT AAT 2784 Asn Glu Leu Leu Leu Arg He Gly Glu His Tyr Gin Gin Val Phe Asn 915 920 925 GGT TTG TCA ATA CTT GCC TCA TTT GCA TCC AGT GAT GAT CCA TAT CAG 2832 Gly Leu Ser He Leu Ala Ser Phe Ala Ser Ser Asp Asp Pro Tyr Gin 930 935 940 GGC CCG AGA GAT ATC ATA TCA CCT GAA CTG ATG GCT GAT TAT TTA CAA 2880 Gly Pro Arg Asp He He Ser Pro Glu Leu Met Ala Asp Tyr Leu Gin 945 950 955 960 CCC AAA TTG TTG GGC ATT TTG GCT TTT TTT AAC ATG CAG TTA CTG AGC 2928 Pro Lys Leu Leu Gly He Leu Ala Phe Phe Asn Met Gin Leu Leu Ser 965 970 975 TCT AGT GTT GGC ATT GAA GAT AAG AAA ATG GCC TTG AAC AGT TTG ATG 2976 Ser Ser Val Gly He Glu Asp Lys Lys Met Ala Leu Asn Ser Leu Met 980 985 990 TCT TTG ATG AAG TTA ATG GGA CCC AAA CAT GTC AGT TCT GTG AGG GTG 3024 Ser Leu Met Lys Leu Met Gly Pro Lys His Val Ser Ser Val Arg Val 995 1000 1005 AAG ATG ATG ACC ACA CTG AGA ACT GGC CTT CGA TTC AAG GAT GAT TTT 3072 Lys Met Met Thr Thr Leu Arg Thr Gly Leu Arg Phe Lys Asp Asp Phe 1010 1015 1020 CCT GAA TTG TGT TGC AGA GCT TGG GAC TGC TTT GTT CGC TGC CTG GAT 3120 Pro Glu Leu Cys Cys Arg Ala Trp Asp Cys Phe Val Arg Cys Leu Asp 1025 1030 1035 1040 CAT GCT TGT CTG GGC TCC CTT CTC AGT CAT GTA ATA GTA GCT TTG TTA 3168 His Ala Cys Leu Gly Ser Leu Leu Ser His Val He Val Ala Leu Leu 1045 1050 1055 CCT CTT ATA CAC ATC CAG CCT AAA GAA ACT GCA GCT ATC TTC CAC TAC 3216 Pro Leu He His He Gin Pro Lys Glu Thr Ala Ala He Phe His Tyr 1060 1065 1070 CTC ATA ATT GAA AAC AGG GAT GCT GTG CAA GAT TTT CTT CAT GAA ATA 3264 Leu He He Glu Asn Arg Asp Ala Val Gin Asp Phe Leu His Glu He 1075 1080 1085 TAT TTT TTA CCT GAT CAT CCA GAA TTA AAA AAG ATA AAA GCC GTT CTC 3312 Tyr Phe Leu Pro Asp His Pro Glu Leu Lys Lys He Lys Ala Val Leu 1090 1095 1100 CAG GAA TAC AGA AAG GAG ACC TCT GAG AGC ACT GAT CTT CAG ACA ACT 3360 Gin Glu Tyr Arg Lys Glu Thr Ser Glu Ser Thr Asp Leu Gin Thr Thr 1105 1110 1115 1120 CTT CAG CTC TCT ATG AAG GCC ATT CAA CAT GAA AAT GTC GAT GTT CGT 3408 Leu Gin Leu Ser Met Lys Ala He Gin His Glu Asn Val Asp Val Arg 1125 1130 1135 ATT CAT GCT CTT ACA AGC TTG AAG GAA ACC TTG TAT AAA AAT CAG GAA 3456 He His Ala Leu Thr Ser Leu Lys Glu Thr Leu Tyr Lys Asn Gin Glu 1140 1145 1150 AAA CTG ATA AAG TAT GCA ACA GAC AGT GAA ACA GTA GAA CCT ATT ATC 3504 Lys Leu He Lys Tyr Ala Thr Asp Ser Glu Thr Val Glu Pro He He 1155 1160 1165 TCA CAG TTG GTG ACA GTG CTT TTG AAA GGT TGC CAA GAT GCA AAC TCT 3552 Ser Gin Leu Val Thr Val Leu Leu Lys Gly Cys Gin Asp Ala Asn Ser 1170 1175 1180 CAA GCT CGG TTG CTC TGT GGG GAA TGT TTA GGG GAA TTG GGG GCG ATA 3600 Gin Ala Arg Leu Leu Cys Gly Glu Cys Leu Gly Glu Leu Gly Ala He 1185 1190 1195 1200 GAT CCA GGT CGA TTA GAT TTC TCA ACA ACT GAA ACT CAA GGA AAA GAT 3648 Asp Pro Gly Arg Leu Asp Phe Ser Thr Thr Glu Thr Gin Gly Lys Asp 1205 1210 1215 TTT ACA TTT GTG ACT GGA GTA GAA GAT TCA AGC TTT GCC TAT GGA TTA 3696 Phe Thr Phe Val Thr Gly Val Glu Asp Ser Ser Phe Ala Tyr Gly Leu 1220 1225 1230 TTG ATG GAG CTA ACA AGA GCT TAC CTT GCG TAT GCT GAT AAT AGC CGA 3744 Leu Met Glu Leu Thr Arg Ala Tyr Leu Ala Tyr Ala Asp Asn Ser Arg 1235 1240 1245 GCT CAA GAT TCA GCT GCC TAT GCC ATT CAG GAG TTG CTT TCT ATT TAT 3792 Ala Gin Asp Ser Ala Ala Tyr Ala He Gin Glu Leu Leu Ser He Tyr 1250 1255 1260 GAC TGT AGA GAG ATG GAG ACC AAC GGC CCA GGT CAC CAA TTG TGG AGG 3840 Asp Cys Arg Glu Met Glu Thr Asn Gly Pro Gly His Gin Leu Trp Arg 1265 1270 1275 1280 AGA TTT CCT GAG CAT GTT CGG GAA ATA CTA GAA CCT CAT CTA AAT ACC 3888 Arg Phe Pro Glu His Val Arg Glu He Leu Glu Pro His Leu Asn Thr 1285 1290 1295 AGA TAC AAG AGT TCT CAG AAG TCA ACC GAT TGG TCT GGA GTA AAG AAG 3936 Arg Tyr Lys Ser Ser Gin Lys Ser Thr Asp Trp Ser Gly Val Lys Lys 1300 1305 1310 CCA ATT TAC TTA AGT AAA TTG GGT AGT AAC TTT GCA GAA TGG TCA GCA 3984 Pro He Tyr Leu Ser Lys Leu Gly Ser Asn Phe Ala Glu Trp Ser Ala 1315 1320 1325 TCT TGG GCA GGT TAT CTT ATT ACA AAG GTT CGA CAT GAT CTT GCC AGT 4032 Ser Trp Ala Gly Tyr Leu He Thr Lys Val Arg His Asp Leu Ala Ser 1330 1335 1340 AAA ATT TTC ACC TGC TGT AGC ATT ATG ATG AAG CAT GAT TTC AAA GTG 4080 Lys He Phe Thr Cys Cys Ser He Met Met Lys His Asp Phe Lys Val 1345 1350 1355 1360 ACC ATC TAT CTT CTT CCA CAT ATT CTG GTG TAT GTC TTA CTG GGT TGT 4128 Thr He Tyr Leu Leu Pro His He Leu Val Tyr Val Leu Leu Gly Cys 1365 1370 1375 AAT CAA GAA GAT CAG CAG GAG GTT TAT GCA GAA ATT ATG GCA GTT CTA 4176 Asn Gin Glu Asp Gin Gin Glu Val Tyr Ala Glu He Met Ala Val Leu 1380 1385 1390 AAG CAT GAC GAT CAG CAT ACC ATA AAT ACC CAA GAC ATT GCA TCT GAT 4224 Lys His Asp Asp Gin His Thr He Asn Thr Gin Asp He Ala Ser Asp 1395 1400 1405 CTG TGT CAA CTC AGT ACA CAG ACT GTG TTC TCC ATG CTT GAC CAT CTC 4272 Leu Cys Gin Leu Ser Thr Gin Thr Val Phe Ser Met Leu Asp His Leu 1410 1415 1420 ACA CAG TGG GCA AGG CAC AAA TTT CAG GCA CTG AAA GCT GAG AAA TGT 4320 Thr Gin Trp Ala Arg His Lys Phe Gin Ala Leu Lys Ala Glu Lys Cys 1425 1430 1435 1440 CCA CAC AGC AAA TCA AAC AGA AAT AAG GTA GAC TCA ATG GTA TCT ACT 4368 Pro His Ser Lys Ser Asn Arg Asn Lys Val Asp Ser Met Val Ser Thr 1445 1450 1455 GTG GAT TAT GAA GAC TAT CAG AGT GTA ACC CGT TTT CTA GAC CTC ATA 4416 Val Asp Tyr Glu Asp Tyr Gin Ser Val Thr Arg Phe Leu Asp Leu He 1460 1465 1470 CCC CAG GAT ACT CTG GCA GTA GCT TCC TTT CGC TCC AAA GCA TAC ACA 4464 Pro Gin Asp Thr Leu Ala Val Ala Ser Phe Arg Ser Lys Ala Tyr Thr 1475 1480 1485 CGA GCT GTA ATG CAC TTT GAA TCA TTT ATT ACA GAA AAG AAG CAA AAT 4512 Arg Ala Val Met His Phe Glu Ser Phe He Thr Glu Lys Lys Gin Asn 1490 1495 1500 ATT CAG GAA CAT CTT GGA TTT TTA CAG AAA TTG TAT GCT GCT ATG CAT 4560 He Gin Glu His Leu Gly Phe Leu Gin Lys Leu Tyr Ala Ala Met His 1505 1510 1515 1520 GAA CCT GAT GGA GTG GCC GGA GTC AGT GCA ATT AGA AAG GCA GAA CCA 4608 Glu Pro Asp Gly Val Ala Gly Val Ser Ala He Arg Lys Ala Glu Pro 1525 1530 1535 TCT CTA AAA GAA CAG ATC CTT GAA CAT GAA AGC CTT GGC TTG CTG AGG 4656 Ser Leu Lys Glu Gin He Leu Glu His Glu Ser Leu Gly Leu Leu Arg 1540 1545 1550 GAT GCC ACT GCT TGT TAT GAC AGG GCT ATT CAG CTA GAA CCA GAC CAG 4704 Asp Ala Thr Ala Cys Tyr Asp Arg Ala He Gin Leu Glu Pro Asp Gin 1555 1560 1565 ATC ATT CAT TAC CAT GGT GTA GTA AAG TCC ATG TTA GGT CTT GGT CAG 4752 He He His Tyr His Gly Val Val Lys Ser Met Leu Gly Leu Gly Gin 1570 1575 1580 CTG TCT ACT GTT ATC ACT CAG GTG AAT GGA GTG CAT GCT AAC AGG TCC 4800 Leu Ser Thr Val He Thr Gin Val Asn Gly Val His Ala Asn Arg Ser 1585 1590 1595 1600 GAG TGG ACA GAT GAA TTA AAC ACG TAC AGA GTG GAA GCA GCT TGG AAA 4848 Glu Trp Thr Asp Glu Leu Asn Thr Tyr Arg Val Glu Ala Ala Trp Lys 1605 1610 1615 TTG TCA CAG TGG GAT TTG GTG GAA AAC TAT TTG GCA GCA GAT GGA AAA 4896 Leu Ser Gin Trp Asp Leu Val Glu Asn Tyr Leu Ala Ala Asp Gly Lys 1620 1625 1630 TCT ACA ACA TGG AGT GTC AGA CTG GGA CAG CTA TTA TTA TCA GCC AAA 4944 Ser Thr Thr Trp Ser Val Arg Leu Gly Gin Leu Leu Leu Ser Ala Lys 1635 1640 1645 AAA AGA GAT ATC ACA GCT TTT TAT GAC TCA CTG AAA CTA GTG AGA GCA 4992 Lys Arg Asp He Thr Ala Phe Tyr Asp Ser Leu Lys Leu Val Arg Ala 1650 1655 1660 GAA CAA ATT GTA CCT CTT TCA GCT GCA AGC TTT GAA AGA GGC TCC TAC 5040 Glu Gin He Val Pro Leu Ser Ala Ala Ser Phe Glu Arg Gly Ser Tyr 1665 1670 1675 1680 CAA CGA GGA TAT GAA TAT ATT GTG AGA TTG CAC ATG TTA TGT GAG TTG 5088 Gin Arg Gly Tyr Glu Tyr He Val Arg Leu His Met Leu Cys Glu Leu 1685 1690 1695 GAG CAT AGC ATC AAA CCA CTT TTC CAG CAT TCT CCA GGT GAC AGT TCT 5136 Glu His Ser He Lys Pro Leu Phe Gin His Ser Pro Gly Asp Ser Ser 1700 1705 1710 CAA GAA GAT TCT CTA AAC TGG GTA GCT CGA CTA GAA ATG ACC CAG AAT 5184 Gin Glu Asp Ser Leu Asn Trp Val Ala Arg Leu Glu Met Thr Gin Asn 1715 1720 1725 TCC TAC AGA GCC AAG GAG CCT ATC CTG GCT CTC CGG AGG GCT TTA CTA 5232 Ser Tyr Arg Ala Lys Glu Pro He Leu Ala Leu Arg Arg Ala Leu Leu 1730 1735 1740 AGC CTC AAC AAA AGA CCA GAT TAC AAT GAA ATG GTT GGA GAA TGC TGG 5280 Ser Leu Asn Lys Arg Pro Asp Tyr Asn Glu Met Val Gly Glu Cys Trp 1745 1750 1755 1760 CTG CAG AGT GCC AGG GTA GCT AGA AAG GCT GGT CAC CAC CAG ACA GCC 5328 Leu Gin Ser Ala Arg Val Ala Arg Lys Ala Gly His His Gin Thr Ala 1765 1770 1775 TAC AAT GCT CTC CTT AAT GCA GGG GAA TCA CGA CTC GCT GAA CTG TAC 5376 Tyr Asn Ala Leu Leu Asn Ala Gly Glu Ser Arg Leu Ala Glu Leu Tyr 1780 1785 1790 GTG GAA AGG GCA AAG TGG CTC TGG TCC AAG GGT GAT GTT CAC CAG GCA 5424 Val Glu Arg Ala Lys Trp Leu Trp Ser Lys Gly Asp Val His Gin Ala 1795 1800 1805 CTA ATT GTT CTT CAA AAA GGT GTT GAA TTA TGT TTT CCT GAA AAT GAA 5472 Leu He Val Leu Gin Lys Gly Val Glu Leu Cys Phe Pro Glu Asn Glu 1810 1815 1820 ACC CCA CCT GAG GGT AAG AAC ATG TTA ATC CAT GGT CGA GCT ATG CTA 5520 Thr Pro Pro Glu Gly Lys Asn Met Leu He His Gly Arg Ala Met Leu 1825 1830 1835 1840 CTA GTG GGC CGA TTT ATG GAA GAA ACA GCT AAC TTT GAA AGC AAT GCA 5568 Leu Val Gly Arg Phe Met Glu Glu Thr Ala Asn Phe Glu Ser Asn Ala 1845 1850 1855 ATT ATG AAA AAA TAT AAG GAT GTG ACC GCG TGC CTG CCA GAA TGG GAG 5616 He Met Lys Lys Tyr Lys Asp Val Thr Ala Cys Leu Pro Glu Trp Glu 1860 1865 1870 GAT GGG CAT TTT TAC CTT GCC AAG TAC TAT GAC AAA TTG ATG CCC ATG 5664 Asp Gly His Phe Tyr Leu Ala Lys Tyr Tyr Asp Lys Leu Met Pro Met 1875 1880 1885 GTC ACA GAC AAC AAA ATG GAA AAG CAA GGT GAT CTC ATC CGG TAT ATA 5712 Val Thr Asp Asn Lys Met Glu Lys Gin Gly Asp Leu He Arg Tyr He 1890 1895 1900 GTT CTT CAT TTT GGC AGA TCT CTA CAA TAT GGA AAT CAG TTC ATA TAT 5760 Val Leu His Phe Gly Arg Ser Leu Gin Tyr Gly Asn Gin Phe He Tyr 1905 1910 1915 1920 CAG TCA ATG CCA CGA ATG TTA ACT CTA TGG CTT GAT TAT GGT ACA AAG 5808 Gin Ser Met Pro Arg Met Leu Thr Leu Trp Leu Asp Tyr Gly Thr Lys 1925 1930 1935 GCA TAT GAA TGG GAA AAA GCT GGC CGC TCC GAT CGT GTA CAA ATG AGG 5856 Ala Tyr Glu Trp Glu Lys Ala Gly Arg Ser Asp Arg Val Gin Met Arg 1940 1945 1950 AAT GAT TTG GGT AAA ATA AAC AAG GTT ATC ACA GAG CAT ACA AAC TAT 5904 Asn Asp Leu Gly Lys He Asn Lys Val He Thr Glu His Thr Asn Tyr 1955 1960 1965 TTA GCT CCA TAT CAA TTT TTG ACT GCT TTT TCA CAA TTG ATC TCT CGA 5952 Leu Ala Pro Tyr Gin Phe Leu Thr Ala Phe Ser Gin Leu He Ser Arg 1970 1975 1980 ATT TGT CAT TCT CAC GAT GAA GTT TTT GTT GTG CTT GAT GGA AAT AAT 6000 He Cys His Ser His Asp Glu Val Phe Val Val Leu Asp Gly Asn Asn 1985 1990 1995 2000 AGC CAA GTA TTT CTA GCC TAT CCT CAA CAA GCA ATG TGG ATG ATG ACA 6048 Ser Gin Val Phe Leu Ala Tyr Pro Gin Gin Ala Met Trp Met Met Thr 2005 2010 2015 GCT GTG TCA AAG TCA TCT TAT CCC ATG CGT GTG AAC AGA TGC AAG GAA 6096 Ala Val Ser Lys Ser Ser Tyr Pro Met Arg Val Asn Arg Cys Lys Glu 2020 2025 2030 ATC CTC AAT AAA GCT ATT CAT ATG AAA AAA TCC TTA GAG AAG TTT GTT 6144 He Leu Asn Lys Ala He His Met Lys Lys Ser Leu Glu Lys Phe Val 2035 2040 2045 GGA GAT GCA ACT CGC CTA ACA GAT AAG CTT CTA GAA TTG TGC AAT AAA 6192 Gly Asp Ala Thr Arg Leu Thr Asp Lys Leu Leu Glu Leu Cys Asn Lys 2050 2055 2060 CCG GTT GAT GGA AGT AGT TCC ACA TTA AGC ATG AGC ACT CAT TTT AAA 6240 Pro Val Asp Gly Ser Ser Ser Thr Leu Ser Met Ser Thr His Phe Lys 2065 2070 2075 2080 ATG CTT AAA AAG CTG GTA GAA GAA GCA ACA TTT AGT GAA ATC CTC ATT 6288 Met Leu Lys Lys Leu Val Glu Glu Ala Thr Phe Ser Glu He Leu He 2085 2090 2095 CCT CTA CAA TCA GTC ATG ATA CCT ACA CTT CCA TCA ATT CTG GGT ACC 6336 Pro Leu Gin Ser Val Met He Pro Thr Leu Pro Ser He Leu Gly Thr 2100 2105 2110 CAT GCT AAC CAT GCT AGC CAT GAA CCA TTT CCT GGA CAT TGG GCC TAT 6384 His Ala Asn His Ala Ser His Glu Pro Phe Pro Gly His Trp Ala Tyr 2115 2120 2125 ATT GCA GGG TTT GAT GAT ATG GTG GAA ATT CTT GCT TCT CTT CAG AAA 6432 He Ala Gly Phe Asp Asp Met Val Glu He Leu Ala Ser Leu Gin Lys 2130 2135 2140 CCA AAG AAG ATT TCT TTA AAA GGC TCA GAT GGA AAG TTC TAC ATC ATG 6480 Pro Lys Lys He Ser Leu Lys Gly Ser Asp Gly Lys Phe Tyr He Met 2145 2150 2155 2160 ATG TGT AAG CCA AAA GAT GAC CTG AGA AAG GAT TGT AGA CTA ATG GAA 6528 Met Cys Lys Pro Lys Asp Asp Leu Arg Lys Asp Cys Arg Leu Met Glu 2165 2170 2175 TTC AAT TCC TTG ATT AAT AAG TGC TTA AGA AAA GAT GCA GAG TCT CGT 6576 Phe Asn Ser Leu He Asn Lys Cys Leu Arg Lys Asp Ala Glu Ser Arg 2180 2185 2190 AGA AGA GAA CTT CAT ATT CGA ACA TAT GCA GTT ATT CCA CTA AAT GAT 6624 Arg Arg Glu Leu His He Arg Thr Tyr Ala Val He Pro Leu Asn Asp 2195 2200 2205 GAA TGT GGG ATT ATT GAA TGG GTG AAC AAC ACT GCT GGT TTG AGA CCT 6672 Glu Cys Gly He He Glu Trp Val Asn Asn Thr Ala Gly Leu Arg Pro 2210 2215 2220 ATT CTG ACC AAA CTA TAT AAA GAA AAG GGA GTG TAT ATG ACA GGA AAA 6720 He Leu Thr Lys Leu Tyr Lys Glu Lys Gly Val Tyr Met Thr Gly Lys 2225 2230 2235 2240 GAA CTT CGC CAG TGT ATG CTA CCA AAG TCA GCA GCT TTA TCT GAA AAA 6768 Glu Leu Arg Gin Cys Met Leu Pro Lys Ser Ala Ala Leu Ser Glu Lys 2245 2250 2255 CTC AAA GTA TTC CGA GAA TTT CTC CTG CCC AGG CAT CCT CCT ATT TTT 6816 Leu Lys Val Phe Arg Glu Phe Leu Leu Pro Arg His Pro Pro He Phe 2260 2265 2270 CAT GAG TGG TTT CTG AGA ACA TTC CCT GAT CCT ACA TCA TGG TAC AGT 6864 His Glu Trp Phe Leu Arg Thr Phe Pro Asp Pro Thr Ser Trp Tyr Ser 2275 2280 2285 AGT AGA TCA GCT TAC TGC CGT TCC ACT GCA GTA ATG TCA ATG GTT GGT 6912 Ser Arg Ser Ala Tyr Cys Arg Ser Thr Ala Val Met Ser Met Val Gly 2290 2295 2300 TAT ATT CTG GGG CTT GGA GAC CGT CAT GGT GAA AAT ATT CTC TTT GAT 6960 Tyr He Leu Gly Leu Gly Asp Arg His Gly Glu Asn He Leu Phe Asp 2305 2310 2315 2320 TCT TTG ACT GGT GAA TGC GTA CAT GTA GAT TTC AAT TGT CTT TTC AAT 7008 Ser Leu Thr Gly Glu Cys Val His Val Asp Phe Asn Cys Leu Phe Asn 2325 2330 2335 AAG GGA GAA ACC TTT GAA GTT CCA GAA ATT GTG CCA TTT CGC CTG ACT 7056 Lys Gly Glu Thr Phe Glu Val Pro Glu He Val Pro Phe Arg Leu Thr 2340 2345 2350 CAT AAT ATG GTT AAT GGA ATG GGT CCT ATG GGA ACA GAG GGT CTT TTT 7104 His Asn Met Val Asn Gly Met Gly Pro Met Gly Thr Glu Gly Leu Phe 2355 2360 2365 CGA AGA GCA TGT GAA GTT ACA ATG AGG CTG ATG CGT GAT CAG CGA GAG 7152 Arg Arg Ala Cys Glu Val Thr Met Arg Leu Met Arg Asp Gin Arg Glu 2370 2375 2380 CCT TTA ATG AGT GTC TTA AAG ACT TTT CTA CAT GAT CCT CTT GTG GAA 7200 Pro Leu Met Ser Val Leu Lys Thr Phe Leu His Asp Pro Leu Val Glu 2385 2390 2395 2400 TGG AGT AAA CCA GTG AAA GGG CAT TCC AAA GCG CCA CTG AAT GAA ACT 7248 Trp Ser Lys Pro Val Lys Gly His Ser Lys Ala Pro Leu Asn Glu Thr 2405 2410 2415 GGA GAA GTT GTC AAT GAA AAG GCC AAG ACC CAT GTT CTT GAC ATT GAG 7296 Gly Glu Val Val Asn Glu Lys Ala Lys Thr His Val Leu Asp He Glu 2420 2425 2430 CAG CGA CTA CAA GGT GTA ATC AAG ACT CGA AAT AGA GTG ACA GGA CTG 7344 Gin Arg Leu Gin Gly Val He Lys Thr Arg Asn Arg Val Thr Gly Leu 2435 2440 2445 CCG TTA TCT ATT GAA GGA CAT GTG CAT TAC CTT ATA CAA GAA GCT ACT 7392 Pro Leu Ser He Glu Gly His Val His Tyr Leu He Gin Glu Ala Thr 2450 2455 2460 GAT GAA AAC TTA CTA TGC CAG ATG TAT CTT GGT TGG ACT CCA TAT ATG 7440 Asp Glu Asn Leu Leu Cys Gin Met Tyr Leu Gly Trp Thr Pro Tyr Met 2465 2470 2475 2480 TGAAATGAAA TTATGTAAAA GAATATGTTA ATAATCTAAA AGTAAAAAAA AAAAAAAAAA 7500 AA 7502 (2) INFORMATION FOR SEQ ID NO:26: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2480 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:26: Met Gly His Ala Val Glu Trp Pro Val Val Met Ser Arg Phe Leu Ser 1 5 10 15 Gin Leu Asp Glu His Met Gly Tyr Leu Gin Ser Ala Pro Leu Gin Leu 20 25 30 Met Ser Met Gin Asn Leu Glu Phe He Glu Val Thr Leu Leu Met Val 35 40 45 Leu Thr Arg He He Ala He Val Phe Phe Arg Arg Gin Glu Leu Leu 50 55 60 Leu Trp Gin He Gly Cys Val Leu Leu Glu Tyr Gly Ser Pro Lys He 65 70 75 80 Lyε Ser Leu Ala He Ser Phe Leu Thr Glu Leu Phe Gin Leu Gly Gly 85 90 95 Leu Pro Ala Gin Pro Ala Ser Thr Phe Phe Ser Ser Phe Leu Glu Leu 100 105 110 Leu Lys His Leu Val Glu Met Asp Thr Asp Gin Leu Lys Leu Tyr Glu 115 120 125 Glu Pro Leu Ser Lys Leu He Lys Thr Leu Phe Pro Phe Glu Ala Glu 130 135 140 Ala Tyr Arg Asn He Glu Pro Val Tyr Leu Asn Met Leu Leu Glu Lys 145 150 155 160 Leu Cys Val Met Phe Glu Asp Gly Val Leu Met Arg Leu Lys Ser Asp 165 170 175 Leu Leu Lys Ala Ala Leu Cys His Leu Leu Gin Tyr Phe Leu Lys Phe 180 185 190 Val Pro Ala Gly Tyr Glu Ser Ala Leu Gin Val Arg Lys Val Tyr Val 195 200 205 Arg Asn He Cys Lys Ala Leu Leu Asp Val Leu Gly He Glu Val Asp 210 215 220 Ala Glu Tyr Leu Leu Gly Pro Leu Tyr Ala Ala Leu Lys Met Glu Ser 225 230 235 240 Met Glu He He Glu Glu He Gin Cys Gin Thr Gin Gin Glu Asn Leu 245 250 255 Ser Ser Asn Ser Asp Gly He Ser Pro Lys Arg Arg Arg Leu Ser Ser 260 265 270 Ser Leu Asn Pro Ser Lys Arg Ala Pro Lys Gin Thr Glu Glu He Lys 275 280 285 His Val Asp Met Asn Gin Lys Ser He Leu Trp Ser Ala Leu Lys Gin 290 295 300 Lys Ala Glu Ser Leu Gin He Ser Leu Glu Tyr Ser Gly Leu Lys Asn 305 310 315 320 Pro Val He Glu Met Leu Glu Gly He Ala Val Val Leu Gin Leu Thr 325 330 335 Ala Leu Cys Thr Val His Cys Ser His Gin Asn Met Asn Cys Arg Thr 340 345 350 Phe Lys Asp Cys Gin His Lys Ser Lys Lys Lys Pro Ser Val Val He 355 360 365 Thr Trp Met Ser Leu Asp Phe Tyr Thr Lys Val Leu Lys Ser Cys Arg 370 375 380 Ser Leu Leu Glu Ser Val Gin Lys Leu Asp Leu Glu Ala Thr He Asp 385 390 395 400 Lys Val Val Lys He Tyr Asp Ala Leu He Tyr Met Gin Val Asn Ser 405 410 415 Ser Phe Glu Asp His He Leu Glu Asp Leu Cys Gly Met Leu Ser Leu 420 425 430 Pro Trp He Tyr Ser His Ser Asp Asp Gly Cys Leu Lys Leu Thr Thr 435 440 445 Phe Ala Ala Asn Leu Leu Thr Leu Ser Cys Arg He Ser Asp Ser Tyr 450 455 460 Ser Pro Gin Ala Gin Ser Arg Cys Val Phe Leu Leu Thr Leu Phe Pro 465 470 475 480 Arg Arg He Phe Leu Glu Trp Arg Thr Ala Val Tyr Asn Trp Ala Leu 485 490 495 Gin Ser Ser His Glu Val He Arg Ala Ser Cys Val Ser Gly Phe Phe 500 505 510 He Leu Leu Gin Gin Gin Asn Ser Cys Asn Arg Val Pro Lys He Leu 515 520 525 He Asp Lys Val Lys Asp Asp Ser Asp He Val Lys Lys Glu Phe Ala 530 535 540 Ser He Leu Gly Gin Leu Val Cys Thr Leu His Gly Met Phe Tyr Leu 545 550 555 560 Thr Ser Ser Leu Thr Glu Pro Phe Ser Glu His Gly His Val Asp Leu 565 570 575 Phe Cys Arg Asn Leu Lys Ala Thr Ser Gin His Glu Cys Ser Ser Ser 580 585 590 Gin Leu Lys Ala Ser Val Cys Lys Pro Phe Leu Phe Leu Leu Lys Lys 595 600 605 Lys He Pro Ser Pro Val Lys Leu Ala Phe He Asp Asn Leu His His 610 615 620 Leu Cys Lys His Leu Asp Phe Arg Glu Asp Glu Thr Asp Val Lys Ala 625 630 635 640 Val Leu Gly Thr Leu Leu Asn Leu Met Glu Asp Pro Asp Lys Asp Val 645 650 655 Arg Val Ala Phe Ser Gly Asn He Lys His He Leu Glu Ser Leu Asp 660 665 670 Ser Glu Asp Gly Phe He Lys Glu Leu Phe Val Leu Arg Met Lys Glu 675 680 685 Ala Tyr Thr His Ala Gin He Ser Arg Asn Asn Glu Leu Lys Asp Thr 690 695 700 Leu He Leu Thr Thr Gly Asp He Gly Arg Ala Ala Lys Gly Asp Leu 705 710 715 720 Val Pro Phe Ala Leu Leu His Leu Leu His Cys Leu Leu Ser Lys Ser 725 730 735 Ala Ser Val Ser Gly Ala Ala Tyr Thr Glu He Arg Ala Leu Val Ala 740 745 750 Ala Lys Ser Val Lys Leu Gin Ser Phe Phe Ser Gin Tyr Lys Lys Pro 755 760 765 He Cys Gin Phe Leu Val Glu Ser Leu His Ser Ser Gin Met Thr Ala 770 775 780 Leu Pro Asn Thr Pro Cys Gin Asn Ala Asp Val Arg Lys Gin Asp Val 785 790 795 800 Ala His Gin Arg Glu Met Ala Leu Asn Thr Leu Ser Glu He Ala Asn 805 810 815 Val Phe Asp Phe Pro Asp Leu Asn Arg Phe Leu Thr Arg Thr Leu Gin 820 825 830 Val Leu Leu Pro Asp Leu Ala Ala Lys Ala Ser Pro Ala Ala Ser Ala 835 840 845 Leu He Arg Thr Leu Gly Lys Gin Leu Asn Val Asn Arg Arg Glu He 850 855 860 Leu He Asn Asn Phe Lys Tyr He Phe Ser His Leu Val Cys Ser Cys 865 870 875 880 Ser Lys Asp Glu Leu Glu Arg Ala Leu His Tyr Leu Lys Asn Glu Thr 885 890 895 Glu He Glu Leu Gly Ser Leu Leu Arg Gin Asp Phe Gin Gly Leu His 900 905 910 Asn Glu Leu Leu Leu Arg He Gly Glu His Tyr Gin Gin Val Phe Asn 915 920 925 Gly Leu Ser He Leu Ala Ser Phe Ala Ser Ser Asp Asp Pro Tyr Gin 930 935 940 Gly Pro Arg Asp He He Ser Pro Glu Leu Met Ala Asp Tyr Leu Gin 945 950 955 960 Pro Lys Leu Leu Gly He Leu Ala Phe Phe Asn Met Gin Leu Leu Ser 965 970 975 Ser Ser Val Gly He Glu Asp Lys Lys Met Ala Leu Asn Ser Leu Met 980 985 990 Ser Leu Met Lys Leu Met Gly Pro Lys His Val Ser Ser Val Arg Val 995 1000 1005 Lys Met Met Thr Thr Leu Arg Thr Gly Leu Arg Phe Lys Asp Asp Phe 1010 1015 1020 Pro Glu Leu Cys Cys Arg Ala Trp Asp Cys Phe Val Arg Cys Leu Asp 1025 1030 1035 1040 His Ala Cys Leu Gly Ser Leu Leu Ser His Val He Val Ala Leu Leu 1045 1050 1055 Pro Leu He His He Gin Pro Lys Glu Thr Ala Ala He Phe His Tyr 1060 1065 1070 Leu He He Glu Asn Arg Asp Ala Val Gin Asp Phe Leu His Glu He 1075 1080 1085 Tyr Phe Leu Pro Asp His Pro Glu Leu Lys Lys He Lys Ala Val Leu 1090 1095 1100 Gin Glu Tyr Arg Lys Glu Thr Ser Glu Ser Thr Asp Leu Gin Thr Thr 1105 1110 1115 1120 Leu Gin Leu Ser Met Lys Ala He Gin His Glu Asn Val Asp Val Arg 1125 1130 1135 Ile His Ala Leu Thr Ser Leu Lys Glu Thr Leu Tyr Lys Asn Gin Glu 1140 1145 1150 Lys Leu He Lys Tyr Ala Thr Asp Ser Glu Thr Val Glu Pro He He 1155 1160 1165 Ser Gin Leu Val Thr Val Leu Leu Lys Gly Cys Gin Asp Ala Asn Ser 1170 1175 1180 Gin Ala Arg Leu Leu Cys Gly Glu Cys Leu Gly Glu Leu Gly Ala He 1185 1190 1195 1200 Asp Pro Gly Arg Leu Asp Phe Ser Thr Thr Glu Thr Gin Gly Lys Asp 1205 1210 1215 Phe Thr Phe Val Thr Gly Val Glu Asp Ser Ser Phe Ala Tyr Gly Leu 1220 1225 1230 Leu Met Glu Leu Thr Arg Ala Tyr Leu Ala Tyr Ala Asp Asn Ser Arg 1235 1240 1245 Ala Gin Asp Ser Ala Ala Tyr Ala He Gin Glu Leu Leu Ser He Tyr 1250 1255 1260 Asp Cys Arg Glu Met Glu Thr Asn Gly Pro Gly His Gin Leu Trp Arg 1265 1270 1275 1280 Arg Phe Pro Glu His Val Arg Glu He Leu Glu Pro His Leu Asn Thr 1285 1290 1295 Arg Tyr Lys Ser Ser Gin Lys Ser Thr Asp Trp Ser Gly Val Lys Lys 1300 1305 1310 Pro He Tyr Leu Ser Lys Leu Gly Ser Asn Phe Ala Glu Trp Ser Ala 1315 1320 1325 Ser Trp Ala Gly Tyr Leu He Thr Lys Val Arg His Asp Leu Ala Ser 1330 1335 1340 Lys He Phe Thr Cys Cys Ser He Met Met Lys His Asp Phe Lys Val 1345 1350 1355 1360 Thr He Tyr Leu Leu Pro His He Leu Val Tyr Val Leu Leu Gly Cys 1365 1370 1375 Asn Gin Glu Asp Gin Gin Glu Val Tyr Ala Glu He Met Ala Val Leu 1380 1385 1390 Lys His Asp Asp Gin His Thr He Asn Thr Gin Asp He Ala Ser Asp 1395 1400 1405 Leu Cys Gin Leu Ser Thr Gin Thr Val Phe Ser Met Leu Asp His Leu 1410 1415 1420 Thr Gin Trp Ala Arg His Lys Phe Gin Ala Leu Lys Ala Glu Lys Cys 1425 1430 1435 1440 Pro His Ser Lys Ser Asn Arg Asn Lys Val Asp Ser Met Val Ser Thr 1445 1450 1455 Val Asp Tyr Glu Asp Tyr Gin Ser Val Thr Arg Phe Leu Asp Leu He 1460 1465 1470 Pro Gin Asp Thr Leu Ala Val Ala Ser Phe Arg Ser Lys Ala Tyr Thr 1475 1480 1485 Arg Ala Val Met His Phe Glu Ser Phe He Thr Glu Lys Lys Gin Asn 1490 1495 1500 He Gin Glu His Leu Gly Phe Leu Gin Lys Leu Tyr Ala Ala Met His 1505 1510 1515 1520 Glu Pro Asp Gly Val Ala Gly Val Ser Ala He Arg Lys Ala Glu Pro 1525 1530 1535 Ser Leu Lys Glu Gin He Leu Glu His Glu Ser Leu Gly Leu Leu Arg 1540 1545 1550 Asp Ala Thr Ala Cys Tyr Asp Arg Ala He Gin Leu Glu Pro Asp Gin 1555 1560 1565 He He His Tyr His Gly Val Val Lys Ser Met Leu Gly Leu Gly Gin 1570 1575 1580 Leu Ser Thr Val He Thr Gin Val Asn Gly Val His Ala Asn Arg Ser 1585 1590 1595 1600 Glu Trp Thr Asp Glu Leu Asn Thr Tyr Arg Val Glu Ala Ala Trp Lys 1605 1610 1615 Leu Ser Gin Trp Asp Leu Val Glu Asn Tyr Leu Ala Ala Asp Gly Lys 1620 1625 1630 Ser Thr Thr Trp Ser Val Arg Leu Gly Gin Leu Leu Leu Ser Ala Lys 1635 1640 1645 Lys Arg Asp He Thr Ala Phe Tyr Asp Ser Leu Lys Leu Val Arg Ala 1650 1655 1660 Glu Gin He Val Pro Leu Ser Ala Ala Ser Phe Glu Arg Gly Ser Tyr 1665 1670 1675 1680 Gin Arg Gly Tyr Glu Tyr He Val Arg Leu His Met Leu Cys Glu Leu 1685 1690 1695 Glu His Ser He Lys Pro Leu Phe Gin His Ser Pro Gly Asp Ser Ser 1700 1705 1710 Gin Glu Asp Ser Leu Asn Trp Val Ala Arg Leu Glu Met Thr Gin Asn 1715 1720 1725 Ser Tyr Arg Ala Lys Glu Pro He Leu Ala Leu Arg Arg Ala Leu Leu 1730 1735 1740 Ser Leu Asn Lys Arg Pro Asp Tyr Asn Glu Met Val Gly Glu Cys Trp 1745 1750 1755 1760 Leu Gin Ser Ala Arg Val Ala Arg Lys Ala Gly His His Gin Thr Ala 1765 1770 1775 Tyr Asn Ala Leu Leu Asn Ala Gly Glu Ser Arg Leu Ala Glu Leu Tyr 1780 1785 1790 Val Glu Arg Ala Lys Trp Leu Trp Ser Lys Gly Asp Val His Gin Ala 1795 1800 1805 Leu He Val Leu Gin Lys Gly Val Glu Leu Cys Phe Pro Glu Asn Glu 1810 1815 1820 Thr Pro Pro Glu Gly Lys Asn Met Leu He His Gly Arg Ala Met Leu 1825 1830 1835 1840 Leu Val Gly Arg Phe Met Glu Glu Thr Ala Asn Phe Glu Ser Asn Ala 1845 1850 1855 He Met Lys Lys Tyr Lys Asp Val Thr Ala Cys Leu Pro Glu Trp Glu 1860 1865 1870 Asp Gly His Phe Tyr Leu Ala Lys Tyr Tyr Asp Lys Leu Met Pro Met 1875 1880 1885 Val Thr Asp Asn Lys Met Glu Lys Gin Gly Asp Leu He Arg Tyr He 1890 1895 1900 Val Leu His Phe Gly Arg Ser Leu Gin Tyr Gly Asn Gin Phe He Tyr 1905 1910 1915 1920 Gin Ser Met Pro Arg Met Leu Thr Leu Trp Leu Asp Tyr Gly Thr Lys 1925 1930 1935 Ala Tyr Glu Trp Glu Lys Ala Gly Arg Ser Asp Arg Val Gin Met Arg 1940 1945 1950 Asn Asp Leu Gly Lys He Asn Lys Val He Thr Glu His Thr Asn Tyr 1955 1960 1965 Leu Ala Pro Tyr Gin Phe Leu Thr Ala Phe Ser Gin Leu He Ser Arg 1970 1975 1980 He Cys His Ser His Asp Glu Val Phe Val Val Leu Asp Gly Asn Asn 1985 1990 1995 2000 Ser Gin Val Phe Leu Ala Tyr Pro Gin Gin Ala Met Trp Met Met Thr 2005 2010 2015 Ala Val Ser Lys Ser Ser Tyr Pro Met Arg Val Asn Arg Cys Lys Glu 2020 2025 2030 He Leu Asn Lys Ala He His Met Lys Lys Ser Leu Glu Lys Phe Val 2035 2040 2045 Gly Asp Ala Thr Arg Leu Thr Asp Lys Leu Leu Glu Leu Cys Asn Lys 2050 2055 2060 Pro Val Asp Gly Ser Ser Ser Thr Leu Ser Met Ser Thr His Phe Lys 2065 2070 2075 2080 Met Leu Lys Lys Leu Val Glu Glu Ala Thr Phe Ser Glu He Leu He 2085 2090 2095 Pro Leu Gin Ser Val Met He Pro Thr Leu Pro Ser He Leu Gly Thr 2100 2105 2110 His Ala Asn His Ala Ser His Glu Pro Phe Pro Gly His Trp Ala Tyr 2115 2120 2125 He Ala Gly Phe Asp Asp Met Val Glu He Leu Ala Ser Leu Gin Lys 2130 2135 2140 Pro Lys Lys He Ser Leu Lys Gly Ser Asp Gly Lys Phe Tyr He Met 2145 2150 2155 2160 Met Cys Lys Pro Lys Asp Asp Leu Arg Lys Asp Cys Arg Leu Met Glu 2165 2170 2175 Phe Asn Ser Leu He Asn Lys Cys Leu Arg Lys Asp Ala Glu Ser Arg 2180 2185 2190 Arg Arg Glu Leu His He Arg Thr Tyr Ala Val He Pro Leu Asn Asp 2195 2200 2205 Glu Cys Gly He He Glu Trp Val Asn Asn Thr Ala Gly Leu Arg Pro 2210 2215 2220 He Leu Thr Lys Leu Tyr Lys Glu Lys Gly Val Tyr Met Thr Gly Lys 2225 2230 2235 2240 Glu Leu Arg Gin Cys Met Leu Pro Lys Ser Ala Ala Leu Ser Glu Lys 2245 2250 2255 Leu Lys Val Phe Arg Glu Phe Leu Leu Pro Arg His Pro Pro He Phe 2260 2265 2270 His Glu Trp Phe Leu Arg Thr Phe Pro Asp Pro Thr Ser Trp Tyr Ser 2275 2280 2285 Ser Arg Ser Ala Tyr Cys Arg Ser Thr Ala Val Met Ser Met Val Gly 2290 2295 2300 Tyr He Leu Gly Leu Gly Asp Arg His Gly Glu Asn He Leu Phe Asp 2305 2310 2315 2320 Ser Leu Thr Gly Glu Cys Val His Val Asp Phe Asn Cys Leu Phe Asn 2325 2330 2335 Lys Gly Glu Thr Phe Glu Val Pro Glu He Val Pro Phe Arg Leu Thr 2340 2345 2350 His Asn Met Val Asn Gly Met Gly Pro Met Gly Thr Glu Gly Leu Phe 2355 2360 2365 Arg Arg Ala Cys Glu Val Thr Met Arg Leu Met Arg Asp Gin Arg Glu 2370 2375 2380 Pro Leu Met Ser Val Leu Lys Thr Phe Leu His Asp Pro Leu Val Glu 2385 2390 2395 2400 Trp Ser Lys Pro Val Lys Gly His Ser Lys Ala Pro Leu Asn Glu Thr 2405 2410 2415 Gly Glu Val Val Asn Glu Lys Ala Lys Thr His Val Leu Asp He Glu 2420 2425 2430 Gin Arg Leu Gin Gly Val He Lys Thr Arg Asn Arg Val Thr Gly Leu 2435 2440 2445 Pro Leu Ser He Glu Gly His Val His Tyr Leu He Gin Glu Ala Thr 2450 2455 2460 Asp Glu Asn Leu Leu Cys Gin Met Tyr Leu Gly Trp Thr Pro Tyr Met 2465 2470 2475 2480 (2) INFORMATION FOR SEQ ID NO:27: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 878 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear 111) MOLECULE TYPE: DNA (xi) SEQUENCE DESCRIPTION: SEQ ID NO:27- ATCCATTGTG TTGGAAAGGA ATGATGAATG TGGGATTATT GAATGGGTGA ACAATACTGC 60 TGGCTTGAGA CCTATTCTGA CCAAAATATA TAAAGAAAAG GGAGTGTATA TGACAGGAAA 120 GGAGCTTCGC CAGTGTATGC TACCAAAGTC AGCAGCTTTA TCTGAAAAAC TCAAAGTATT 180 CCAAGAATTA CTCCTGCCCA GGCATCCTCC TGTTTTTCAT GAGTGGTTTC TGAGAACATT 240 CCCTGATCCT ACATCATGGT ACAGTAGCAG ATCTGCATAT TGCCGCTCTA CTGCAGTCAT 300 GTCAATGGTT GGCTACATCC TGGGGCTTGG AGACCGTCAT GGTGAAAACA TTCTTTTTGA 360 CTCTTTCACT GGTGAATGTG TACATGTAGA TTTCAACTGT CTTTTTAATA AGGGAGAAAC 420 GTTTGAAGTT CCGGAAATTG TACCATTTCG ACTGACTCAT AATATGGTTA ATGGAATGGG 480 TCCTATGGGA ACAGAGGGTC TATTTCGAAG AGCATGTGAA GTTACACTGA GACTGATGAG 540 GGATCAGAGA GAACCTTTAA TGAGTGTCTT AAAGACTTTT CTACACGATC CTCTAGTGGA 600 GTGGAGTAAA CCAGTGAAAG GACACTCCAA AGCACCACTG AATGAAACCG GGGAAGTTGT 660 CAATGAGAAG GCCAAGACCC ATGTTCTTGA CATTGAACAA CGACTACAAG GTGTGATCAA 720 AACCCGAAAT AGAGTAACAG GGCTGCCATT ATCTATTGAA GGACATGTGC ATTACCTCAT 780 ACAAGAAGCT ACTGATGAAA ACTTACTCTG TCAGATGTAC CTTGGTTGGA CCCCATATAT 840 GTAAAATAAA ATTATTTCAA AGAAAAAAAA AAAAAAAA 878 (2) INFORMATION FOR SEQ ID NO:28: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 7935 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 1..7932 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:28: ATG GGG GAA CAT GGC CTG GAG CTG GCT TCC ATG ATC CCC GCC CTG CGG 48 Met Gly Glu His Gly Leu Glu Leu Ala Ser Met He Pro Ala Leu Arg 1 5 10 15 GAG CTG GGC AGT GCC ACA CCA GAG GAA TAT AAT ACA GTT GTA CAG AAG 96 Glu Leu Gly Ser Ala Thr Pro Glu Glu Tyr Asn Thr Val Val Gin Lys 20 25 30 CCA AGA CAA ATT CTG TGT CAA TTC ATT GAC CGG ATA CTT ACA GAT GTA 144 Pro Arg Gin He Leu Cys Gin Phe He Asp Arg He Leu Thr Asp Val 35 40 45 AAT GTT GTT GCT GTA GAA CTT GTA AAG AAA ACT GAC TCT CAG CCA ACC 192 Asn Val Val Ala Val Glu Leu Val Lys Lys Thr Asp Ser Gin Pro Thr 50 55 60 TCC GTG ATG TTG CTT GAT TTC ATC CAG CAT ATC ATG AAA TCC TCC CCA 240 Ser Val Met Leu Leu Asp Phe He Gin His He Met Lys Ser Ser Pro 65 70 75 80 CTT ATG TTT GTA AAT GTG AGT GGA AGC CAT GAG CGC AAA GGC AGT TGT 288 Leu Met Phe Val Asn Val Ser Gly Ser His Glu Arg Lys Gly Ser Cys 85 90 95 ATT GAA TTC AGT AAT TGG ATC ATA ACG AGA CTT CTG CGG ATT GCA GCA 336 He Glu Phe Ser Asn Trp He He Thr Arg Leu Leu Arg He Ala Ala 100 105 110 ACT CCC TCC TGT CAT TTG TTA CAC AAG AAA ATC TGT GAA GTC ATC TGT 384 Thr Pro Ser Cys His Leu Leu His Lys Lys He Cys Glu Val He Cys 115 120 125 TCA TTA TTA TTT CTT TTT AAA AGC AAG AGT CCT GCT ATT TTT GGG GTA 432 Ser Leu Leu Phe Leu Phe Lys Ser Lys Ser Pro Ala He Phe Gly Val 130 135 140 CTC ACA AAA GAA TTA TTA CAA CTT TTT GAA GAC TTG GTT TAC CTC CAT 480 Leu Thr Lys Glu Leu Leu Gin Leu Phe Glu Asp Leu Val Tyr Leu His 145 150 155 160 AGA AGA AAT GTG ATG GGT CAT GCT GTG GAA TGG CCA GTG GTC ATG AGC 528 Arg Arg Asn Val Met Gly His Ala Val Glu Trp Pro Val Val Met Ser 165 170 175 CGA TTT TTA AGT CAA TTA GAT GAA CAC ATG GGA TAT TTA CAA TCA GCT 576 Arg Phe Leu Ser Gin Leu Asp Glu His Met Gly Tyr Leu Gin Ser Ala 180 185 190 CCT TTG CAG TTG ATG AGT ATG CAA AAT TTA GAA TTT ATT GAA GTC ACT 624 Pro Leu Gin Leu Met Ser Met Gin Asn Leu Glu Phe He Glu Val Thr 195 200 205 TTA TTA ATG GTT CTT ACT CGT ATT ATT GCA ATT GTG TTT TTT AGA AGG 672 Leu Leu Met Val Leu Thr Arg He He Ala He Val Phe Phe Arg Arg 210 215 220 CAA GAA CTC TTA CTT TGG CAG ATA GGT TGT GTT CTG CTA GAG TAT GGT 720 Gin Glu Leu Leu Leu Trp Gin He Gly Cys Val Leu Leu Glu Tyr Gly 225 230 235 240 AGT CCA AAA ATT AAA TCC CTA GCA ATT AGC TTT TTA ACA GAA CTT TTT 768 Ser Pro Lys He Lys Ser Leu Ala He Ser Phe Leu Thr Glu Leu Phe 245 250 255 CAG CTT GGA GGA CTA CCA GCA CAA CCA GCT AGC ACT TTT TTC AGC TCA 816 Gin Leu Gly Gly Leu Pro Ala Gin Pro Ala Ser Thr Phe Phe Ser Ser 260 265 270 TTT TTG GAA TTA TTA AAA CAC CTT GTA GAA ATG GAT ACT GAC CAA TTG 864 Phe Leu Glu Leu Leu Lys His Leu Val Glu Met Asp Thr Asp Gin Leu 275 280 285 AAA CTC TAT GAA GAG CCA TTA TCA AAG CTG ATA AAG ACA CTA TTT CCC 912 Lys Leu Tyr Glu Glu Pro Leu Ser Lys Leu He Lys Thr Leu Phe Pro 290 295 300 TTT GAA GCA GAA GCT TAT AGA AAT ATT GAA CCT GTC TAT TTA AAT ATG 960 Phe Glu Ala Glu Ala Tyr Arg Asn He Glu Pro Val Tyr Leu Asn Met 305 310 315 320 CTG CTG GAA AAA CTC TGT GTC ATG TTT GAA GAC GGT GTG CTC ATG CGG 1008 Leu Leu Glu Lys Leu Cys Val Met Phe Glu Asp Gly Val Leu Met Arg 325 330 335 CTT AAG TCT GAT TTG CTA AAA GCA GCT TTG TGC CAT TTA CTG CAG TAT 1056 Leu Lys Ser Asp Leu Leu Lys Ala Ala Leu Cys His Leu Leu Gin Tyr 340 345 350 TTC CTT AAA TTT GTG CCA GCT GGG TAT GAA TCT GCT TTA CAA GTC AGG 1104 Phe Leu Lys Phe Val Pro Ala Gly Tyr Glu Ser Ala Leu Gin Val Arg 355 360 365 AAG GTC TAT GTG AGA AAT ATT TGT AAA GCT CTT TTG GAT GTG CTT GGA 1152 Lys Val Tyr Val Arg Asn He Cys Lys Ala Leu Leu Asp Val Leu Gly 370 375 380 ATT GAG GTA GAT GCA GAG TAC TTG TTG GGC CCA CTT TAT GCA GCT TTG 1200 He Glu Val Asp Ala Glu Tyr Leu Leu Gly Pro Leu Tyr Ala Ala Leu 385 390 395 400 AAA ATG GAA AGT ATG GAA ATC ATT GAG GAG ATT CAA TGC CAA ACT CAA 1248 Lys Met Glu Ser Met Glu He He Glu Glu He Gin Cys Gin Thr Gin 405 410 415 CAG GAA AAC CTC AGC AGT AAT AGT GAT GGA ATA TCA CCC AAA AGG CGT 1296 Gin Glu Asn Leu Ser Ser Asn Ser Asp Gly He Ser Pro Lys Arg Arg 420 425 430 CGT CTC AGC TCG TCT CTA AAC CCT TCT AAA AGA GCA CCA AAA CAG ACT 1344 Arg Leu Ser Ser Ser Leu Asn Pro Ser Lys Arg Ala Pro Lys Gin Thr 435 440 445 GAG GAA ATT AAA CAT GTG GAC ATG AAC CAA AAG AGC ATA TTA TGG AGT 1392 Glu Glu He Lys His Val Asp Met Asn Gin Lys Ser He Leu Trp Ser 450 455 460 GCA CTG AAA CAG AAA GCT GAA TCC CTT CAG ATT TCC CTT GAA TAC AGT 1440 Ala Leu Lys Gin Lys Ala Glu Ser Leu Gin He Ser Leu Glu Tyr Ser 465 470 475 480 GGC CTA AAG AAT CCT GTT ATT GAG ATG TTA GAA GGA ATT GCT GTT GTC 1488 Gly Leu Lys Asn Pro Val He Glu Met Leu Glu Gly He Ala Val Val 485 490 495 TTA CAA CTG ACT GCT CTG TGT ACT GTT CAT TGT TCT CAT CAA AAC ATG 1536 Leu Gin Leu Thr Ala Leu Cys Thr Val His Cys Ser His Gin Asn Met 500 505 510 AAC TGC CGT ACT TTC AAG GAC TGT CAA CAT AAA TCC AAG AAG AAA CCT 1584 Asn Cys Arg Thr Phe Lys Asp Cys Gin His Lys Ser Lys Lys Lys Pro 515 520 525 TCT GTA GTG ATA ACT TGG ATG TCA TTG GAT TTT TAC ACA AAA GTG CTT 1632 Ser Val Val He Thr Trp Met Ser Leu Asp Phe Tyr Thr Lys Val Leu 530 535 540 AAG AGC TGT AGA AGT TTG TTA GAA TCT GTT CAG AAA CTG GAC CTG GAG 1680 Lys Ser Cys Arg Ser Leu Leu Glu Ser Val Gin Lys Leu Asp Leu Glu 545 550 555 560 GCA ACC ATT GAT AAG GTG GTG AAA ATT TAT GAT GCT TTG ATT TAT ATG 1728 Ala Thr He Asp Lys Val Val Lys He Tyr Asp Ala Leu He Tyr Met 565 570 575 CAA GTA AAC AGT TCA TTT GAA GAT CAT ATC CTG GAA GAT TTA TGT GGT 1776 Gin Val Asn Ser Ser Phe Glu Asp His He Leu Glu Asp Leu Cys Gly 580 585 590 ATG CTC TCA CTT CCA TGG ATT TAT TCC CAT TCT GAT GAT GGC TGT TTA 1824 Met Leu Ser Leu Pro Trp He Tyr Ser His Ser Asp Asp Gly Cys Leu 595 600 605 AAG TTG ACC ACA TTT GCC GCT AAT CTT CTA ACA TTA AGC TGT AGG ATT 1872 Lys Leu Thr Thr Phe Ala Ala Asn Leu Leu Thr Leu Ser Cys Arg He 610 615 620 TCA GAT AGC TAT TCA CCA CAG GCA CAA TCA CGA TGT GTG TTT CTT CTG 1920 Ser Asp Ser Tyr Ser Pro Gin Ala Gin Ser Arg Cys Val Phe Leu Leu 625 630 635 640 ACT CTG TTT CCA AGA AGA ATA TTC CTT GAG TGG AGA ACA GCA GTT TAC 1968 Thr Leu Phe Pro Arg Arg He Phe Leu Glu Trp Arg Thr Ala Val Tyr 645 650 655 AAC TGG GCC CTG CAG AGC TCC CAT GAA GTA ATC CGG GCT AGT TGT GTT 2016 Asn Trp Ala Leu Gin Ser Ser His Glu Val He Arg Ala Ser Cys Val 660 665 670 AGT GGA TTT TTT ATC TTA TTG CAG CAG CAG AAT TCT TGT AAC AGA GTT 2064 Ser Gly Phe Phe He Leu Leu Gin Gin Gin Asn Ser Cys Asn Arg Val 675 680 685 CCC AAG ATT CTT ATA GAT AAA GTC AAA GAT GAT TCT GAC ATT GTC AAG 2112 Pro Lys He Leu He Asp Lys Val Lys Asp Asp Ser Asp He Val Lys 690 695 700 AAA GAA TTT GCT TCT ATA CTT GGT CAA CTT GTC TGT ACT CTT CAC GGC 2160 Lys Glu Phe Ala Ser He Leu Gly Gin Leu Val Cys Thr Leu His Gly 705 710 715 720 ATG TTT TAT CTG ACA AGT TCT TTA ACA GAA CCT TTC TCT GAA CAC GGA 2208 Met Phe Tyr Leu Thr Ser Ser Leu Thr Glu Pro Phe Ser Glu His Gly 725 730 735 CAT GTG GAC CTC TTC TGT AGG AAC TTG AAA GCC ACT TCT CAA CAT GAA 2256 His Val Asp Leu Phe Cys Arg Asn Leu Lys Ala Thr Ser Gin His Glu 740 745 750 TGT TCA TCT TCT CAA CTA AAA GCT TCT GTC TGC AAG CCA TTC CTT TTC 2304 Cys Ser Ser Ser Gin Leu Lys Ala Ser Val Cys Lys Pro Phe Leu Phe 755 760 765 CTA CTG AAA AAA AAA ATA CCT AGT CCA GTA AAA CTT GCT TTC ATA GAT 2352 Leu Leu Lys Lys Lys He Pro Ser Pro Val Lys Leu Ala Phe He Asp 770 775 780 AAT CTA CAT CAT CTT TGT AAG CAT CTT GAT TTT AGA GAA GAT GAA ACA 2400 Asn Leu His His Leu Cys Lys His Leu Asp Phe Arg Glu Asp Glu Thr 785 790 795 800 GAT GTA AAA GCA GTT CTT GGA ACT TTA TTA AAT TTA ATG GAA GAT CCA 2448 Asp Val Lys Ala Val Leu Gly Thr Leu Leu Asn Leu Met Glu Asp Pro 805 810 815 GAC AAA GAT GTT AGA GTG GCT TTT AGT GGA AAT ATC AAG CAC ATA TTG 2496 Asp Lys Asp Val Arg Val Ala Phe Ser Gly Asn He Lys His He Leu 820 825 830 GAA TCC TTG GAC TCT GAA GAT GGA TTT ATA AAG GAG CTT TTT GTC TTA 2544 Glu Ser Leu Asp Ser Glu Asp Gly Phe He Lys Glu Leu Phe Val Leu 835 840 845 AGA ATG AAG GAA GCA TAT ACA CAT GCC CAA ATA TCA AGA AAT AAT GAG 2592 Arg Met Lys Glu Ala Tyr Thr His Ala Gin He Ser Arg Asn Asn Glu 850 855 860 CTG AAG GAT ACC TTG ATT CTT ACA ACA GGG GAT ATT GGA AGG GCC GCA 2640 Leu Lys Asp Thr Leu He Leu Thr Thr Gly Asp He Gly Arg Ala Ala 865 870 875 880 AAA GGA GAT TTG GTA CCA TTT GCA CTC TTA CAC TTA TTG CAT TGT TTG 2688 Lys Gly Asp Leu Val Pro Phe Ala Leu Leu His Leu Leu His Cys Leu 885 890 895 TTA TCC AAG TCA GCA TCT GTC TCT GGA GCA GCA TAC ACA GAA ATT AGA 2736 Leu Ser Lys Ser Ala Ser Val Ser Gly Ala Ala Tyr Thr Glu He Arg 900 905 910 GCT CTG GTT GCA GCT AAA AGT GTT AAA CTG CAA AGT TTT TTC AGC CAG 2784 Ala Leu Val Ala Ala Lys Ser Val Lys Leu Gin Ser Phe Phe Ser Gin 915 920 925 TAT AAG AAA CCC ATC TGT CAG TTT TTG GTA GAA TCC CTT CAC TCT AGT 2832 Tyr Lys Lys Pro He Cys Gin Phe Leu Val Glu Ser Leu His Ser Ser 930 935 940 CAG ATG ACA GCA CTT CCG AAT ACT CCA TGC CAG AAT GCT GAC GTG CGA 2880 Gin Met Thr Ala Leu Pro Asn Thr Pro Cys Gin Asn Ala Asp Val Arg 945 950 955 960 AAA CAA GAT GTG GCT CAC CAG AGA GAA ATG GCT TTA AAT ACG TTG TCT 2928 Lys Gin Asp Val Ala His Gin Arg Glu Met Ala Leu Asn Thr Leu Ser 965 970 975 GAA ATT GCC AAC GTT TTC GAC TTT CCT GAT CTT AAT CGT TTT CTT ACT 2976 Glu He Ala Asn Val Phe Asp Phe Pro Asp Leu Asn Arg Phe Leu Thr 980 985 990 AGG ACA TTA CAA GTT CTA CTA CCT GAT CTT GCT GCC AAA GCA AGC CCT 3024 Arg Thr Leu Gin Val Leu Leu Pro Asp Leu Ala Ala Lys Ala Ser Pro 995 1000 1005 GCA GCT TCT GCT CTC ATT CGA ACT TTA GGA AAA CAA TTA AAT GTC AAT 3072 Ala Ala Ser Ala Leu He Arg Thr Leu Gly Lys Gin Leu Asn Val Asn 1010 1015 1020 CGT AGA GAG ATT TTA ATA AAC AAC TTC AAA TAT ATT TTT TCT CAT TTG 3120 Arg Arg Glu He Leu He Asn Asn Phe Lys Tyr He Phe Ser His Leu 1025 1030 1035 1040 GTC TGT TCT TGT TCC AAA GAT GAA TTA GAA CGT GCC CTT CAT TAT CTG 3168 Val Cys Ser Cys Ser Lys Asp Glu Leu Glu Arg Ala Leu His Tyr Leu 1045 1050 1055 AAG AAT GAA ACA GAA ATT GAA CTG GGG AGC CTG TTG AGA CAA GAT TTC 3216 Lys Asn Glu Thr Glu He Glu Leu Gly Ser Leu Leu Arg Gin Asp Phe 1060 1065 1070 CAA GGA TTG CAT AAT GAA TTA TTG CTG CGT ATT GGA GAA CAC TAT CAA 3264 Gin Gly Leu His Asn Glu Leu Leu Leu Arg He Gly Glu His Tyr Gin 1075 1080 1085 CAG GTT TTT AAT GGT TTG TCA ATA CTT GCC TCA TTT GCA TCC AGT GAT 3312 Gin Val Phe Asn Gly Leu Ser He Leu Ala Ser Phe Ala Ser Ser Asp 1090 1095 1100 GAT CCA TAT CAG GGC CCG AGA GAT ATC ATA TCA CCT GAA CTG ATG GCT 3360 Asp Pro Tyr Gin Gly Pro Arg Asp He He Ser Pro Glu Leu Met Ala 1105 1110 1115 1120 GAT TAT TTA CAA CCC AAA TTG TTG GGC ATT TTG GCT TTT TTT AAC ATG 3408 Asp Tyr Leu Gin Pro Lys Leu Leu Gly He Leu Ala Phe Phe Asn Met 1125 1130 1135 CAG TTA CTG AGC TCT AGT GTT GGC ATT GAA GAT AAG AAA ATG GCC TTG 3456 Gin Leu Leu Ser Ser Ser Val Gly He Glu Asp Lys Lys Met Ala Leu 1140 1145 1150 AAC AGT TTG ATG TCT TTG ATG AAG TTA ATG GGA CCC AAA CAT GTC AGT 3504 Asn Ser Leu Met Ser Leu Met Lys Leu Met Gly Pro Lys His Val Ser 1155 1160 1165 TCT GTG AGG GTG AAG ATG ATG ACC ACA CTG AGA ACT GGC CTT CGA TTC 3552 Ser Val Arg Val Lys Met Met Thr Thr Leu Arg Thr Gly Leu Arg Phe 1170 1175 1180 AAG GAT GAT TTT CCT GAA TTG TGT TGC AGA GCT TGG GAC TGC TTT GTT 3600 Lys Asp Asp Phe Pro Glu Leu Cys Cys Arg Ala Trp Asp Cys Phe Val 1185 1190 1195 1200 CGC TGC CTG GAT CAT GCT TGT CTG GGC TCC CTT CTC AGT CAT GTA ATA 3648 Arg Cys Leu Asp His Ala Cys Leu Gly Ser Leu Leu Ser His Val He 1205 1210 1215 GTA GCT TTG TTA CCT CTT ATA CAC ATC CAG CCT AAA GAA ACT GCA GCT 3696 Val Ala Leu Leu Pro Leu He His He Gin Pro Lys Glu Thr Ala Ala 1220 1225 1230 ATC TTC CAC TAC CTC ATA ATT GAA AAC AGG GAT GCT GTG CAA GAT TTT 3744 He Phe His Tyr Leu He He Glu Asn Arg Asp Ala Val Gin Asp Phe 1235 1240 1245 CTT CAT GAA ATA TAT TTT TTA CCT GAT CAT CCA GAA TTA AAA AAG ATA 3792 Leu His Glu He Tyr Phe Leu Pro Asp His Pro Glu Leu Lys Lys He 1250 1255 1260 AAA GCC GTT CTC CAG GAA TAC AGA AAG GAG ACC TCT GAG AGC ACT GAT 3840 Lys Ala Val Leu Gin Glu Tyr Arg Lys Glu Thr Ser Glu Ser Thr Asp 1265 1270 1275 1280 CTT CAG ACA ACT CTT CAG CTC TCT ATG AAG GCC ATT CAA CAT GAA AAT 3888 Leu Gin Thr Thr Leu Gin Leu Ser Met Lys Ala He Gin His Glu Asn 1285 1290 1295 GTC GAT GTT CGT ATT CAT GCT CTT ACA AGC TTG AAG GAA ACC TTG TAT 3936 Val Asp Val Arg He His Ala Leu Thr Ser Leu Lys Glu Thr Leu Tyr 1300 1305 1310 AAA AAT CAG GAA AAA CTG ATA AAG TAT GCA ACA GAC AGT GAA ACA GTA 3984 Lys Asn Gin Glu Lys Leu He Lys Tyr Ala Thr Asp Ser Glu Thr Val 1315 1320 1325 GAA CCT ATT ATC TCA CAG TTG GTG ACA GTG CTT TTG AAA GGT TGC CAA 4032 Glu Pro He He Ser Gin Leu Val Thr Val Leu Leu Lys Gly Cys Gin 1330 1335 1340 GAT GCA AAC TCT CAA GCT CGG TTG CTC TGT GGG GAA TGT TTA GGG GAA 4080 Asp Ala Asn Ser Gin Ala Arg Leu Leu Cys Gly Glu Cys Leu Gly Glu 1345 1350 1355 1360 TTG GGG GCG ATA GAT CCA GGT CGA TTA GAT TTC TCA ACA ACT GAA ACT 4128 Leu Gly Ala He Asp Pro Gly Arg Leu Asp Phe Ser Thr Thr Glu Thr 1365 1370 1375 CAA GGA AAA GAT TTT ACA TTT GTG ACT GGA GTA GAA GAT TCA AGC TTT 4176 Gin Gly Lys Asp Phe Thr Phe Val Thr Gly Val Glu Asp Ser Ser Phe 1380 1385 1390 GCC TAT GGA TTA TTG ATG GAG CTA ACA AGA GCT TAC CTT GCG TAT GCT 4224 Ala Tyr Gly Leu Leu Met Glu Leu Thr Arg Ala Tyr Leu Ala Tyr Ala 1395 1400 1405 GAT AAT AGC CGA GCT CAA GAT TCA GCT GCC TAT GCC ATT CAG GAG TTG 4272 Asp Asn Ser Arg Ala Gin Asp Ser Ala Ala Tyr Ala He Gin Glu Leu 1410 1415 1420 CTT TCT ATT TAT GAC TGT AGA GAG ATG GAG ACC AAC GGC CCA GGT CAC 4320 Leu Ser He Tyr Asp Cys Arg Glu Met Glu Thr Asn Gly Pro Gly His 1425 1430 1435 1440 CAA TTG TGG AGG AGA TTT CCT GAG CAT GTT CGG GAA ATA CTA GAA CCT 4368 Gin Leu Trp Arg Arg Phe Pro Glu His Val Arg Glu He Leu Glu Pro 1445 1450 1455 CAT CTA AAT ACC AGA TAC AAG AGT TCT CAG AAG TCA ACC GAT TGG TCT 4416 His Leu Asn Thr Arg Tyr Lys Ser Ser Gin Lys Ser Thr Asp Trp Ser 1460 1465 1470 GGA GTA AAG AAG CCA ATT TAC TTA AGT AAA TTG GGT AGT AAC TTT GCA 4464 Gly Val Lys Lys Pro He Tyr Leu Ser Lys Leu Gly Ser Asn Phe Ala 1475 1480 1485 GAA TGG TCA GCA TCT TGG GCA GGT TAT CTT ATT ACA AAG GTT CGA CAT 4512 Glu Trp Ser Ala Ser Trp Ala Gly Tyr Leu He Thr Lys Val Arg His 1490 1495 1500 GAT CTT GCC AGT AAA ATT TTC ACC TGC TGT AGC ATT ATG ATG AAG CAT 4560 Asp Leu Ala Ser Lys He Phe Thr Cys Cys Ser He Met Met Lys His 1505 1510 1515 1520 GAT TTC AAA GTG ACC ATC TAT CTT CTT CCA CAT ATT CTG GTG TAT GTC 4608 Asp Phe Lys Val Thr He Tyr Leu Leu Pro His He Leu Val Tyr Val 1525 1530 1535 TTA CTG GGT TGT AAT CAA GAA GAT CAG CAG GAG GTT TAT GCA GAA ATT 4656 Leu Leu Gly Cys Asn Gin Glu Asp Gin Gin Glu Val Tyr Ala Glu He 1540 1545 1550 ATG GCA GTT CTA AAG CAT GAC GAT CAG CAT ACC ATA AAT ACC CAA GAC 4704 Met Ala Val Leu Lys His Asp Asp Gin His Thr He Asn Thr Gin Asp 1555 1560 1565 ATT GCA TCT GAT CTG TGT CAA CTC AGT ACA CAG ACT GTG TTC TCC ATG 4752 He Ala Ser Asp Leu Cys Gin Leu Ser Thr Gin Thr Val Phe Ser Met 1570 1575 1580 CTT GAC CAT CTC ACA CAG TGG GCA AGG CAC AAA TTT CAG GCA CTG AAA 4800 Leu Asp His Leu Thr Gin Trp Ala Arg His Lys Phe Gin Ala Leu Lys 1585 1590 1595 1600 GCT GAG AAA TGT CCA CAC AGC AAA TCA AAC AGA AAT AAG GTA GAC TCA 4848 Ala Glu Lys Cys Pro His Ser Lys Ser Asn Arg Asn Lys Val Asp Ser 1605 1610 1615 ATG GTA TCT ACT GTG GAT TAT GAA GAC TAT CAG AGT GTA ACC CGT TTT 4896 Met Val Ser Thr Val Asp Tyr Glu Asp Tyr Gin Ser Val Thr Arg Phe 1620 1625 1630 CTA GAC CTC ATA CCC CAG GAT ACT CTG GCA GTA GCT TCC TTT CGC TCC 4944 Leu Asp Leu He Pro Gin Asp Thr Leu Ala Val Ala Ser Phe Arg Ser 1635 1640 1645 AAA GCA TAC ACA CGA GCT GTA ATG CAC TTT GAA TCA TTT ATT ACA GAA 4992 Lys Ala Tyr Thr Arg Ala Val Met His Phe Glu Ser Phe He Thr Glu 1650 1655 1660 AAG AAG CAA AAT ATT CAG GAA CAT CTT GGA TTT TTA CAG AAA TTG TAT 5040 Lys Lys Gin Asn He Gin Glu His Leu Gly Phe Leu Gin Lys Leu Tyr 1665 1670 1675 1680 GCT GCT ATG CAT GAA CCT GAT GGA GTG GCC GGA GTC AGT GCA ATT AGA 5088 Ala Ala Met His Glu Pro Asp Gly Val Ala Gly Val Ser Ala He Arg 1685 1690 1695 AAG GCA GAA CCA TCT CTA AAA GAA CAG ATC CTT GAA CAT GAA AGC CTT 5136 Lys Ala Glu Pro Ser Leu Lys Glu Gin He Leu Glu His Glu Ser Leu 1700 1705 1710 GGC TTG CTG AGG GAT GCC ACT GCT TGT TAT GAC AGG GCT ATT CAG CTA 5184 Gly Leu Leu Arg Asp Ala Thr Ala Cys Tyr Asp Arg Ala He Gin Leu 1715 1720 1725 GAA CCA GAC CAG ATC ATT CAT TAT CAT GGT GTA GTA AAG TCC ATG TTA 5232 Glu Pro Asp Gin He He His Tyr His Gly Val Val Lys Ser Met Leu 1730 1735 1740 GGT CTT GGT CAG CTG TCT ACT GTT ATC ACT CAG GTG AAT GGA GTG CAT 5280 Gly Leu Gly Gin Leu Ser Thr Val He Thr Gin Val Asn Gly Val His 1745 1750 1755 1760 GCT AAC AGG TCC GAG TGG ACA GAT GAA TTA AAC ACG TAC AGA GTG GAA 5328 Ala Asn Arg Ser Glu Trp Thr Asp Glu Leu Asn Thr Tyr Arg Val Glu 1765 1770 1775 GCA GCT TGG AAA TTG TCA CAG TGG GAT TTG GTG GAA AAC TAT TTG GCA 5376 Ala Ala Trp Lys Leu Ser Gin Trp Asp Leu Val Glu Asn Tyr Leu Ala 1780 1785 1790 GCA GAT GGA AAA TCT ACA ACA TGG AGT GTC AGA CTG GGA CAG CTA TTA 5424 Ala Asp Gly Lys Ser Thr Thr Trp Ser Val Arg Leu Gly Gin Leu Leu 1795 1800 1805 TTA TCA GCC AAA AAA AGA GAT ATC ACA GCT TTT TAT GAC TCA CTG AAA 5472 Leu Ser Ala Lys Lys Arg Asp He Thr Ala Phe Tyr Asp Ser Leu Lys 1810 1815 1820 CTA GTG AGA GCA GAA CAA ATT GTA CCT CTT TCA GCT GCA AGC TTT GAA 5520 Leu Val Arg Ala Glu Gin He Val Pro Leu Ser Ala Ala Ser Phe Glu 1825 1830 1835 1840 AGA GGC TCC TAC CAA CGA GGA TAT GAA TAT ATT GTG AGA TTG CAC ATG 5568 Arg Gly Ser Tyr Gin Arg Gly Tyr Glu Tyr He Val Arg Leu His Met 1845 1850 1855 TTA TGT GAG TTG GAG CAT AGC ATC AAA CCA CTT TTC CAG CAT TCT CCA 5616 Leu Cys Glu Leu Glu His Ser He Lys Pro Leu Phe Gin His Ser Pro 1860 1865 1870 GGT GAC AGT TCT CAA GAA GAT TCT CTA AAC TGG GTA GCT CGA CTA GAA 5664 Gly Asp Ser Ser Gin Glu Asp Ser Leu Asn Trp Val Ala Arg Leu Glu 1875 1880 1885 ATG ACC CAG AAT TCC TAC AGA GCC AAG GAG CCT ATC CTG GCT CTC CGG 5712 Met Thr Gin Asn Ser Tyr Arg Ala Lys Glu Pro He Leu Ala Leu Arg 1890 1895 1900 AGG GCT TTA CTA AGC CTC AAC AAA AGA CCA GAT TAC AAT GAA ATG GTT 5760 Arg Ala Leu Leu Ser Leu Asn Lys Arg Pro Asp Tyr Asn Glu Met Val 1905 1910 1915 1920 GGA GAA TGC TGG CTG CAG AGT GCC AGG GTA GCT AGA AAG GCT GGT CAC 5808 Gly Glu Cys Trp Leu Gin Ser Ala Arg Val Ala Arg Lys Ala Gly His 1925 1930 1935 CAC CAG ACA GCC TAC AAT GCT CTC CTT AAT GCA GGG GAA TCA CGA CTC 5856 His Gin Thr Ala Tyr Asn Ala Leu Leu Asn Ala Gly Glu Ser Arg Leu 1940 1945 1950 GCT GAA CTG TAC GTG GAA AGG GCA AAG TGG CTC TGG TCC AAG GGT GAT 5904 Ala Glu Leu Tyr Val Glu Arg Ala Lys Trp Leu Trp Ser Lys Gly Asp 1955 1960 1965 GTT CAC CAG GCA CTA ATT GTT CTT CAA AAA GGT GTT GAA TTA TGT TTT 5952 Val His Gin Ala Leu He Val Leu Gin Lys Gly Val Glu Leu Cys Phe 1970 1975 1980 CCT GAA AAT GAA ACC CCA CCT GAG GGT AAG AAC ATG TTA ATC CAT GGT 6000 Pro Glu Asn Glu Thr Pro Pro Glu Gly Lys Asn Met Leu He His Gly 1985 1990 1995 2000 CGA GCT ATG CTA CTA GTG GGC CGA TTT ATG GAA GAA ACA GCT AAC TTT 6048 Arg Ala Met Leu Leu Val Gly Arg Phe Met Glu Glu Thr Ala Asn Phe 2005 2010 2015 GAA AGC AAT GCA ATT ATG AAA AAA TAT AAG GAT GTG ACC GCG TGC CTG 6096 Glu Ser Asn Ala He Met Lys Lys Tyr Lys Asp Val Thr Ala Cys Leu 2020 2025 2030 CCA GAA TGG GAG GAT GGG CAT TTT TAC CTT GCC AAG TAC TAT GAC AAA 6144 Pro Glu Trp Glu Asp Gly His Phe Tyr Leu Ala Lys Tyr Tyr Asp Lys 2035 2040 2045 TTG ATG CCC ATG GTC ACA GAC AAC AAA ATG GAA AAG CAA GGT GAT CTC 61 2 Leu Met Pro Met Val Thr Asp Asn Lys Met Glu Lys Gin Gly Asp Leu 2050 2055 2060 ATC CGG TAT ATA GTT CTT CAT TTT GGC AGA TCT CTA CAA TAT GGA AAT 6240 He Arg Tyr He Val Leu His Phe Gly Arg Ser Leu Gin Tyr Gly Asn 2065 2070 2075 2080 CAG TTC ATA TAT CAG TCA ATG CCA CGA ATG TTA ACT CTA TGG CTT GAT 6288 Gin Phe He Tyr Gin Ser Met Pro Arg Met Leu Thr Leu Trp Leu Asp 2085 2090 2095 TAT GGT ACA AAG GCA TAT GAA TGG GAA AAA GCT GGC CGC TCC GAT CGT 6336 Tyr Gly Thr Lys Ala Tyr Glu Trp Glu Lys Ala Gly Arg Ser Asp Arg 2100 2105 2110 GTA CAA ATG AGG AAT GAT TTG GGT AAA ATA AAC AAG GTT ATC ACA GAG 6384 Val Gin Met Arg Asn Asp Leu Gly Lys He Asn Lys Val He Thr Glu 2115 2120 2125 CAT ACA AAC TAT TTA GCT CCA TAT CAA TTT TTG ACT GCT TTT TCA CAA 6432 His Thr Asn Tyr Leu Ala Pro Tyr Gin Phe Leu Thr Ala Phe Ser Gin 2130 2135 2140 TTG ATC TCT CGA ATT TGT CAT TCT CAC GAT GAA GTT TTT GTT GTC TTG 6480 Leu He Ser Arg He Cys His Ser His Asp Glu Val Phe Val Val Leu 2145 2150 2155 2160 ATG GAA ATA ATA GCC AAA GTA TTT CTA GCC TAT CCT CAA CAA GCA ATG 6528 Met Glu He He Ala Lys Val Phe Leu Ala Tyr Pro Gin Gin Ala Met 2165 2170 2175 TGG ATG ATG ACA GCT GTG TCA AAG TCA TCT TAT CCC ATG CGT GTG AAC 6576 Trp Met Met Thr Ala Val Ser Lys Ser Ser Tyr Pro Met Arg Val Asn 2180 2185 2190 AGA TGC AAG GAA ATC CTC AAT AAA GCT ATT CAT ATG AAA AAA TCC TTA 6624 Arg Cys Lys Glu He Leu Asn Lys Ala He His Met Lys Lys Ser Leu 2195 2200 2205 GAG AAG TTT GTT GGA GAT GCA ACT CGC CTA ACA GAT AAG CTT CTA GAA 6672 Glu Lys Phe Val Gly Asp Ala Thr Arg Leu Thr Asp Lys Leu Leu Glu 2210 2215 2220 TTG TGC AAT AAA CCG GTT GAT GGA AGT AGT TCC ACA TTA AGC ATG AGC 6720 Leu Cys Asn Lys Pro Val Asp Gly Ser Ser Ser Thr Leu Ser Met Ser 2225 2230 2235 2240 ACT CAT TTT AAA ATG CTT AAA AAG CTG GTA GAA GAA GCA ACA TTT AGT 6768 Thr H s Phe Lys Met Leu Lys Lys Leu Val Glu Glu Ala Thr Phe Ser 2245 2250 2255 GAA ATC CTC ATT CCT CTA CAA TCA GTC ATG ATA CCT ACA CTT CCA TCA 6816 Glu He Leu He Pro Leu Gin Ser Val Met He Pro Thr Leu Pro Ser 2260 2265 2270 ATT CTG GGT ACC CAT GCT AAC CAT GCT AGC CAT GAA CCA TTT CCT GGA 6864 He Leu Gly Thr His Ala Asn His Ala Ser His Glu Pro Phe Pro Gly 2275 2280 2285 CAT TGG GCC TAT ATT GCA GGG TTT GAT GAT ATG GTG GAA ATT CTT GCT 6912 His Trp Ala Tyr He Ala Gly Phe Asp Asp Met Val Glu He Leu Ala 2290 2295 2300 TCT CTT CAG AAA CCA AAG AAG ATT TCT TTA AAA GGC TCA GAT GGA AAG 6960 Ser Leu Gin Lys Pro Lys Lys He Ser Leu Lys Gly Ser Asp Gly Lys 2305 2310 2315 2320 TTC TAC ATC ATG ATG TGT AAG CCA AAA GAT GAC CTG AGA AAG GAT TGT 7008 Phe Tyr He Met Met Cys Lys Pro Lys Asp Asp Leu Arg Lys Asp Cys 2325 2330 2335 AGA CTA ATG GAA TTC AAT TCC TTG ATT AAT AAG TGC TTA AGA AAA GAT 7056 Arg Leu Met Glu Phe Asn Ser Leu He Asn Lys Cys Leu Arg Lys Asp 2340 2345 2350 GCA GAG TCT CGT AGA AGA GAA CTT CAT ATT CGA ACA TAT GCA GTT ATT 7104 Ala Glu Ser Arg Arg Arg Glu Leu His He Arg Thr Tyr Ala Val He 2355 2360 2365 CCA CTA AAT GAT GAA TGT GGG ATT ATT GAA TGG GTG AAC AAC ACT GCT 7152 Pro Leu Asn Asp Glu Cys Gly He He Glu Trp Val Asn Asn Thr Ala 2370 2375 2380 GGT TTG AGA CCT ATT CTG ACC AAA CTA TAT AAA GAA AAG GGA GTG TAT 7200 Gly Leu Arg Pro He Leu Thr Lys Leu Tyr Lys Glu Lys Gly Val Tyr 2385 2390 2395 2400 ATG ACA GGA AAA GAA CTT CGC CAG TGT ATG CTA CCA AAG TCA GCA GCT 7248 Met Thr Gly Lys Glu Leu Arg Gin Cys Met Leu Pro Lys Ser Ala Ala 2405 2410 2415 TTA TCT GAA AAA CTC AAA GTA TTC CGA GAA TTT CTC CTG CCC AGG CAT 7296 Leu Ser Glu Lys Leu Lys Val Phe Arg Glu Phe Leu Leu Pro Arg His 2420 2425 2430 CCT CCT ATT TTT CAT GAG TGG TTT CTG AGA ACA TTC CCT GAT CCT ACA 7344 Pro Pro He Phe H s Glu Trp Phe Leu Arg Thr Phe Pro Asp Pro Thr 2435 2440 2445 TCA TGG TAC AGT AGT AGA TCA GCT TAC TGC CGT TCC ACT GCA GTA ATG 7392 Ser Trp Tyr Ser Ser Arg Ser Ala Tyr Cys Arg Ser Thr Ala Val Met 2450 2455 2460 TCA ATG GTT GGT TAT ATT CTG GGG CTT GGA GAC CGT CAT GGT GAA AAT 7440 Ser Met Val Gly Tyr He Leu Gly Leu Gly Asp Arg His Gly Glu Asn 2465 2470 2475 2480 ATT CTC TTT GAT TCT TTG ACT GGT GAA TGC GTA CAT GTA GAT TTC AAT 7488 He Leu Phe Asp Ser Leu Thr Gly Glu Cys Val His Val Asp Phe Asn 2485 2490 2495 TGT CTT TTC AAT AAG GGA GAA ACC TTT GAA GTT CCA GAA ATT GTG CCA 7536 Cys Leu Phe Asn Lys Gly Glu Thr Phe Glu Val Pro Glu He Val Pro 2500 2505 2510 TTT CGC CTG ACT CAT AAT ATG GTT AAT GGA ATG GGT CCT ATG GGA ACA 7584 Phe Arg Leu Thr His Asn Met Val Asn Gly Met Gly Pro Met Gly Thr 2515 2520 2525 GAG GGT CTT TTT CGA AGA GCA TGT GAA GTT ACA ATG AGG CTG ATG CGT 7632 Glu Gly Leu Phe Arg Arg Ala Cys Glu Val Thr Met Arg Leu Met Arg 2530 2535 2540 GAT CAG CGA GAG CCT TTA ATG AGT GTC TTA AAG ACT TTT CTA CAT GAT 7680 Asp Gin Arg Glu Pro Leu Met Ser Val Leu Lys Thr Phe Leu His Asp 2545 2550 2555 2560 CCT CTT GTG GAA TGG AGT AAA CCA GTG AAA GGG CAT TCC AAA GCG CCA 7728 Pro Leu Val Glu Trp Ser Lys Pro Val Lys Gly His Ser Lys Ala Pro 2565 2570 2575 CTG AAT GAA ACT GGA GAA GTT GTC AAT GAA AAG GCC AAG ACC CAT GTT 7776 Leu Asn Glu Thr Gly Glu Val Val Asn Glu Lys Ala Lys Thr His Val 2580 2585 2590 CTT GAC ATT GAG CAG CGA CTA CAA GGT GTA ATC AAG ACT CGA AAT AGA 7824 Leu Asp He Glu Gin Arg Leu Gin Gly Val He Lys Thr Arg Asn Arg 2595 2600 2605 GTG ACA GGA CTG CCG TTA TCT ATT GAA GGA CAT GTG CAT TAC CTT ATA 7872 Val Thr Gly Leu Pro Leu Ser He Glu Gly His Val His Tyr Leu He 2610 2615 2620 CAA GAA GCT ACT GAT GAA AAC TTA CTA TGC CAG ATG TAT CTT GGT TGG 7920 Gin Glu Ala Thr Asp Glu Asn Leu Leu Cys Gin Met Tyr Leu Gly Trp 2625 2630 2635 2640 ACT CCA TAT ATG TGA 7935 Thr Pro Tyr Met (2) INFORMATION FOR SEQ ID NO:29: d) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2644 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:29: Met Gly Glu His Gly Leu Glu Leu Ala Ser Met He Pro Ala Leu Arg 1 5 10 15 Glu Leu Gly Ser Ala Thr Pro Glu Glu Tyr Asn Thr Val Val Gin Lys 20 25 30 Pro Arg Gin He Leu Cys Gin Phe He Asp Arg He Leu Thr Asp Val 35 40 45 Asn Val Val Ala Val Glu Leu Val Lys Lys Thr Asp Ser Gin Pro Thr 50 55 60 Ser Val Met Leu Leu Asp Phe He Gin His He Met Lys Ser Ser Pro 65 70 75 80 Leu Met Phe Val Asn Val Ser Gly Ser His Glu Arg Lys Gly Ser Cys 85 90 95 He Glu Phe Ser Asn Trp He He Thr Arg Leu Leu Arg He Ala Ala 100 105 110 Thr Pro Ser Cys His Leu Leu His Lys Lys He Cys Glu Val He Cys 115 120 125 Ser Leu Leu Phe Leu Phe Lys Ser Lys Ser Pro Ala He Phe Gly Val 130 135 140 Leu Thr Lys Glu Leu Leu Gin Leu Phe Glu Asp Leu Val Tyr Leu His 145 150 155 160 Arg Arg Asn Val Met Gly His Ala Val Glu Trp Pro Val Val Met Ser 165 170 175 Arg Phe Leu Ser Gin Leu Asp Glu His Met Gly Tyr Leu Gin Ser Ala 180 185 190 Pro Leu Gin Leu Met Ser Met Gin Asn Leu Glu Phe He Glu Val Thr 195 200 205 Leu Leu Met Val Leu Thr Arg He He Ala He Val Phe Phe Arg Arg 210 215 220 Gin Glu Leu Leu Leu Trp Gin He Gly Cys Val Leu Leu Glu Tyr Gly 225 230 235 240 Ser Pro Lys He Lys Ser Leu Ala He Ser Phe Leu Thr Glu Leu Phe 245 250 255 Gin Leu Gly Gly Leu Pro Ala Gin Pro Ala Ser Thr Phe Phe Ser Ser 260 265 270 Phe Leu Glu Leu Leu Lys His Leu Val Glu Met Asp Thr Asp Gin Leu 275 280 285 Lys Leu Tyr Glu Glu Pro Leu Ser Lys Leu He Lys Thr Leu Phe Pro 290 295 300 Phe Glu Ala Glu Ala Tyr Arg Asn He Glu Pro Val Tyr Leu Asn Met 305 310 315 320 Leu Leu Glu Lys Leu Cys Val Met Phe Glu Asp Gly Val Leu Met Arg 325 330 335 Leu Lys Ser Asp Leu Leu Lys Ala Ala Leu Cys His Leu Leu Gin Tyr 340 345 350 Phe Leu Lys Phe Val Pro Ala Gly Tyr Glu Ser Ala Leu Gin Val Arg 355 360 365 Lys Val Tyr Val Arg Asn He Cys Lys Ala Leu Leu Asp Val Leu Gly 370 375 380 He Glu Val Asp Ala Glu Tyr Leu Leu Gly Pro Leu Tyr Ala Ala Leu 385 390 395 400 Lys Met Glu Ser Met Glu He He Glu Glu He Gin Cys Gin Thr Gin 405 410 415 Gin Glu Asn Leu Ser Ser Asn Ser Asp Gly He Ser Pro Lys Arg Arg 420 425 430 Arg Leu Ser Ser Ser Leu Asn Pro Ser Lys Arg Ala Pro Lys Gin Thr 435 440 445 Glu Glu He Lys His Val Asp Met Asn Gin Lys Ser He Leu Trp Ser 450 455 460 Ala Leu Lys Gin Lys Ala Glu Ser Leu Gin He Ser Leu Glu Tyr Ser 465 470 475 480 Gly Leu Lys Asn Pro Val He Glu Met Leu Glu Gly He Ala Val Val 485 490 495 Leu Gin Leu Thr Ala Leu Cys Thr Val His Cys Ser His Gin Asn Met 500 505 510 Asn Cys Arg Thr Phe Lys Asp Cys Gin His Lys Ser Lys Lys Lys Pro 515 520 525 Ser Val Val He Thr Trp Met Ser Leu Asp Phe Tyr Thr Lys Val Leu 530 535 540 Lys Ser Cys Arg Ser Leu Leu Glu Ser Val Gin Lys Leu Asp Leu Glu 545 550 555 560 Ala Thr He Asp Lys Val Val Lys He Tyr Asp Ala Leu He Tyr Met 565 570 575 Gin Val Asn Ser Ser Phe Glu Asp His He Leu Glu Asp Leu Cys Gly 580 585 590 Met Leu Ser Leu Pro Trp He Tyr Ser His Ser Asp Asp Gly Cys Leu 595 600 605 Lys Leu Thr Thr Phe Ala Ala Asn Leu Leu Thr Leu Ser Cys Arg He 610 615 620 Ser Asp Ser Tyr Ser Pro Gin Ala Gin Ser Arg Cys Val Phe Leu Leu 625 630 635 640 Thr Leu Phe Pro Arg Arg He Phe Leu Glu Trp Arg Thr Ala Val Tyr 645 650 655 Asn Trp Ala Leu Gin Ser Ser His Glu Val He Arg Ala Ser Cys Val 660 665 670 Ser Gly Phe Phe He Leu Leu Gin Gin Gin Asn Ser Cys Asn Arg Val 675 680 685 Pro Lys He Leu He Asp Lys Val Lys Asp Asp Ser Asp He Val Lys 690 695 700 Lys Glu Phe Ala Ser He Leu Gly Gin Leu Val Cys Thr Leu His Gly 705 710 715 720 Met Phe Tyr Leu Thr Ser Ser Leu Thr Glu Pro Phe Ser Glu His Gly 725 730 735 His Val Asp Leu Phe Cys Arg Asn Leu Lys Ala Thr Ser Gin His Glu 740 745 750 Cys Ser Ser Ser Gin Leu Lys Ala Ser Val Cys Lys Pro Phe Leu Phe 755 760 765 Leu Leu Lys Lys Lys He Pro Ser Pro Val Lys Leu Ala Phe He Asp 770 775 780 Asn Leu His His Leu Cys Lys His Leu Asp Phe Arg Glu Asp Glu Thr 785 790 795 800 Asp Val Lys Ala Val Leu Gly Thr Leu Leu Asn Leu Met Glu Aεp Pro 805 810 815 Asp Lys Asp Val Arg Val Ala Phe Ser Gly Asn He Lys His He Leu 820 825 830 Glu Ser Leu Asp Ser Glu Asp Gly Phe He Lys Glu Leu Phe Val Leu 835 840 845 Arg Met Lys Glu Ala Tyr Thr His Ala Gin He Ser Arg Asn Asn Glu 850 855 860 Leu Lys Asp Thr Leu He Leu Thr Thr Gly Asp He Gly Arg Ala Ala 865 870 875 880 Lys Gly Asp Leu Val Pro Phe Ala Leu Leu His Leu Leu His Cys Leu 885 890 895 Leu Ser Lys Ser Ala Ser Val Ser Gly Ala Ala Tyr Thr Glu He Arg 900 905 910 Ala Leu Val Ala Ala Lys Ser Val Lys Leu Gin Ser Phe Phe Ser Gin 915 920 925 Tyr Lys Lys Pro He Cys Gin Phe Leu Val Glu Ser Leu His Ser Ser 930 935 940 Gin Met Thr Ala Leu Pro Asn Thr Pro Cys Gin Asn Ala Asp Val Arg 945 950 955 960 Lys Gin Asp Val Ala His Gin Arg Glu Met Ala Leu Asn Thr Leu Ser 965 970 975 Glu He Ala Asn Val Phe Asp Phe Pro Asp Leu Asn Arg Phe Leu Thr 980 985 990 Arg Thr Leu Gin Val Leu Leu Pro Asp Leu Ala Ala Lys Ala Ser Pro 995 1000 1005 Ala Ala Ser Ala Leu He Arg Thr Leu Gly Lys Gin Leu Asn Val Asn 1010 1015 1020 Arg Arg Glu He Leu He Asn Asn Phe Lys Tyr He Phe Ser His Leu 1025 1030 1035 1040 Val Cys Ser Cys Ser Lys Asp Glu Leu Glu Arg Ala Leu His Tyr Leu 1045 1050 1055 Lys Asn Glu Thr Glu He Glu Leu Gly Ser Leu Leu Arg Gin Asp Phe 1060 1065 1070 Gin Gly Leu His Asn Glu Leu Leu Leu Arg He Gly Glu His Tyr Gin 1075 1080 1085 Gin Val Phe Asn Gly Leu Ser He Leu Ala Ser Phe Ala Ser Ser Asp 1090 1095 1100 Asp Pro Tyr Gin Gly Pro Arg Asp He He Ser Pro Glu Leu Met Ala 1105 1110 1115 1120 Asp Tyr Leu Gin Pro Lys Leu Leu Gly He Leu Ala Phe Phe Asn Met 1125 1130 1135 Gin Leu Leu Ser Ser Ser Val Gly He Glu Asp Lys Lys Met Ala Leu 1140 1145 1150 Asn Ser Leu Met Ser Leu Met Lys Leu Met Gly Pro Lys His Val Ser 1155 1160 1165 Ser Val Arg Val Lys Met Met Thr Thr Leu Arg Thr Gly Leu Arg Phe 1170 1175 1180 Lys Asp Asp Phe Pro Glu Leu Cys Cys Arg Ala Trp Asp Cys Phe Val 1185 1190 1195 1200 Arg Cys Leu Asp His Ala Cys Leu Gly Ser Leu Leu Ser His Val He 1205 1210 1215 Val Ala Leu Leu Pro Leu He His He Gin Pro Lys Glu Thr Ala Ala 1220 1225 1230 He Phe His Tyr Leu He He Glu Asn Arg Asp Ala Val Gin Asp Phe 1235 1240 1245 Leu His Glu He Tyr Phe Leu Pro Asp His Pro Glu Leu Lys Lys He 1250 1255 1260 Lys Ala Val Leu Gin Glu Tyr Arg Lys Glu Thr Ser Glu Ser Thr Asp 1265 1270 1275 1280 Leu Gin Thr Thr Leu Gin Leu Ser Met Lys Ala He Gin His Glu Asn 1285 1290 1295 Val Asp Val Arg He His Ala Leu Thr Ser Leu Lys Glu Thr Leu Tyr 1300 1305 1310 Lys Asn Gin Glu Lys Leu He Lys Tyr Ala Thr Asp Ser Glu Thr Val 1315 1320 1325 Glu Pro He He Ser Gin Leu Val Thr Val Leu Leu Lys Gly Cys Gin 1330 1335 1340 Asp Ala Asn Ser Gin Ala Arg Leu Leu Cys Gly Glu Cys Leu Gly Glu 1345 1350 1355 1360 Leu Gly Ala He Asp Pro Gly Arg Leu Asp Phe Ser Thr Thr Glu Thr 1365 1370 1375 Gin Gly Lys Asp Phe Thr Phe Val Thr Gly Val Glu Asp Ser Ser Phe 1380 1385 1390 Ala Tyr Gly Leu Leu Met Glu Leu Thr Arg Ala Tyr Leu Ala Tyr Ala 1395 1400 1405 Asp Asn Ser Arg Ala Gin Asp Ser Ala Ala Tyr Ala He Gin Glu Leu 1410 1415 1420 Leu Ser He Tyr Aεp Cys Arg Glu Met Glu Thr Asn Gly Pro Gly His 1425 1430 1435 1440 Gin Leu Trp Arg Arg Phe Pro Glu His Val Arg Glu He Leu Glu Pro 1445 1450 1455 His Leu Asn Thr Arg Tyr Lys Ser Ser Gin Lys Ser Thr Aεp Trp Ser 1460 1465 1470 Gly Val Lys Lys Pro He Tyr Leu Ser Lys Leu Gly Ser Asn Phe Ala 1475 1480 1485 Glu Trp Ser Ala Ser Trp Ala Gly Tyr Leu He Thr Lys Val Arg His 1490 1495 1500 Asp Leu Ala Ser Lys He Phe Thr Cys Cys Ser He Met Met Lys His 1505 1510 1515 1520 Asp Phe Lys Val Thr He Tyr Leu Leu Pro His He Leu Val Tyr Val 1525 1530 1535 Leu Leu Gly Cys Asn Gin Glu Asp Gin Gin Glu Val Tyr Ala Glu He 1540 1545 1550 Met Ala Val Leu Lys His Asp Asp Gin His Thr He Asn Thr Gin Asp 1555 1560 1565 He Ala Ser Asp Leu Cys Gin Leu Ser Thr Gin Thr Val Phe Ser Met 1570 1575 1580 Leu Asp His Leu Thr Gin Trp Ala Arg His Lys Phe Gin Ala Leu Lys 1585 1590 1595 1600 Ala Glu Lys Cys Pro His Ser Lys Ser Asn Arg Asn Lys Val Asp Ser 1605 1610 1615 Met Val Ser Thr Val Asp Tyr Glu Asp Tyr Gin Ser Val Thr Arg Phe 1620 1625 1630 Leu Asp Leu He Pro Gin Asp Thr Leu Ala Val Ala Ser Phe Arg Ser 1635 1640 1645 Lys Ala Tyr Thr Arg Ala Val Met His Phe Glu Ser Phe He Thr Glu 1650 1655 1660 Lys Lys Gin Asn He Gin Glu His Leu Gly Phe Leu Gin Lys Leu Tyr 1665 1670 1675 1680 Ala Ala Met His Glu Pro Asp Gly Val Ala Gly Val Ser Ala He Arg 1685 1690 1695 Lys Ala Glu Pro Ser Leu Lys Glu Gin He Leu Glu His Glu Ser Leu 1700 1705 1710 Gly Leu Leu Arg Asp Ala Thr Ala Cys Tyr Asp Arg Ala He Gin Leu 1715 1720 1725 Glu Pro Asp Gin He He His Tyr His Gly Val Val Lys Ser Met Leu 1730 1735 1740 Gly Leu Gly Gin Leu Ser Thr Val He Thr Gin Val Asn Gly Val His 1745 1750 1755 1760 Ala Asn Arg Ser Glu Trp Thr Asp Glu Leu Asn Thr Tyr Arg Val Glu 1765 1770 1775 Ala Ala Trp Lys Leu Ser Gin Trp Asp Leu Val Glu Asn Tyr Leu Ala 1780 1785 1790 Ala Asp Gly Lys Ser Thr Thr Trp Ser Val Arg Leu Gly Gin Leu Leu 1795 1800 1805 Leu Ser Ala Lys Lys Arg Asp He Thr Ala Phe Tyr Asp Ser Leu Lys 1810 1815 1820 Leu Val Arg Ala Glu Gin He Val Pro Leu Ser Ala Ala Ser Phe Glu 1825 1830 1835 1840 Arg Gly Ser Tyr Gin Arg Gly Tyr Glu Tyr He Val Arg Leu His Met 1845 1850 1855 Leu Cys Glu Leu Glu His Ser He Lys Pro Leu Phe Gin His Ser Pro 1860 1865 1870 Gly Asp Ser Ser Gin Glu Asp Ser Leu Asn Trp Val Ala Arg Leu Glu 1875 1880 1885 Met Thr Gin Asn Ser Tyr Arg Ala Lys Glu Pro He Leu Ala Leu Arg 1890 1895 1900 Arg Ala Leu Leu Ser Leu Asn Lys Arg Pro Asp Tyr Asn Glu Met Val 1905 1910 1915 1920 Gly Glu Cys Trp Leu Gin Ser Ala Arg Val Ala Arg Lys Ala Gly His 1925 1930 1935 His Gin Thr Ala Tyr Asn Ala Leu Leu Asn Ala Gly Glu Ser Arg Leu 1940 1945 1950 Ala Glu Leu Tyr Val Glu Arg Ala Lys Trp Leu Trp Ser Lys Gly Asp 1955 1960 1965 Val His Gin Ala Leu He Val Leu Gin Lys Gly Val Glu Leu Cys Phe 1970 1975 1980 Pro Glu Asn Glu Thr Pro Pro Glu Gly Lys Asn Met Leu He His Gly 1985 1990 1995 2000 Arg Ala Met Leu Leu Val Gly Arg Phe Met Glu Glu Thr Ala Asn Phe 2005 2010 2015 Glu Ser Asn Ala He Met Lys Lys Tyr Lys Asp Val Thr Ala Cys Leu 2020 2025 2030 Pro Glu Trp Glu Asp Gly His Phe Tyr Leu Ala Lys Tyr Tyr Asp Lys 2035 2040 2045 Leu Met Pro Met Val Thr Asp Asn Lys Met Glu Lys Gin Gly Asp Leu 2050 2055 2060 He Arg Tyr He Val Leu His Phe Gly Arg Ser Leu Gin Tyr Gly Asn 2065 2070 2075 2080 Gin Phe He Tyr Gin Ser Met Pro Arg Met Leu Thr Leu Trp Leu Aεp 2085 2090 2095 Tyr Gly Thr Lys Ala Tyr Glu Trp Glu Lys Ala Gly Arg Ser Aεp Arg 2100 2105 2110 Val Gin Met Arg Aεn Asp Leu Gly Lys He Asn Lys Val He Thr Glu 2115 2120 2125 His Thr Asn Tyr Leu Ala Pro Tyr Gin Phe Leu Thr Ala Phe Ser Gin 2130 2135 2140 Leu He Ser Arg He Cys His Ser His Asp Glu Val Phe Val Val Leu 2145 2150 2155 2160 Met Glu He He Ala Lys Val Phe Leu Ala Tyr Pro Gin Gin Ala Met 2165 2170 2175 Trp Met Met Thr Ala Val Ser Lys Ser Ser Tyr Pro Met Arg Val Asn 2180 2185 2190 Arg Cys Lys Glu He Leu Asn Lys Ala He His Met Lys Lys Ser Leu 2195 2200 2205 Glu Lys Phe Val Gly Asp Ala Thr Arg Leu Thr Asp Lys Leu Leu Glu 2210 2215 2220 Leu Cys Asn Lys Pro Val Asp Gly Ser Ser Ser Thr Leu Ser Met Ser 2225 2230 2235 2240 Thr His Phe Lys Met Leu Lys Lys Leu Val Glu Glu Ala Thr Phe Ser 2245 2250 2255 Glu He Leu He Pro Leu Gin Ser Val Met He Pro Thr Leu Pro Ser 2260 2265 2270 He Leu Gly Thr His Ala Asn His Ala Ser His Glu Pro Phe Pro Gly 2275 2280 2285 His Trp Ala Tyr He Ala Gly Phe Asp Aεp Met Val Glu He Leu Ala 2290 2295 2300 Ser Leu Gin Lys Pro Lys Lys He Ser Leu Lys Gly Ser Asp Gly Lys 2305 2310 2315 2320 Phe Tyr He Met Met Cys Lys Pro Lys Asp Asp Leu Arg Lys Asp Cys 2325 2330 2335 Arg Leu Met Glu Phe Asn Ser Leu He Asn Lys Cys Leu Arg Lys Asp 2340 2345 2350 Ala Glu Ser Arg Arg Arg Glu Leu His He Arg Thr Tyr Ala Val He 2355 2360 2365 Pro Leu Asn Asp Glu Cys Gly He He Glu Trp Val Asn Asn Thr Ala 2370 2375 2380 Gly Leu Arg Pro He Leu Thr Lys Leu Tyr Lys Glu Lys Gly Val Tyr 2385 2390 2395 2400 Met Thr Gly Lys Glu Leu Arg Gin Cys Met Leu Pro Lys Ser Ala Ala 2405 2410 2415 Leu Ser Glu Lys Leu Lys Val Phe Arg Glu Phe Leu Leu Pro Arg His 2420 2425 2430 Pro Pro He Phe His Glu Trp Phe Leu Arg Thr Phe Pro Asp Pro Thr 2435 2440 2445 Ser Trp Tyr Ser Ser Arg Ser Ala Tyr Cys Arg Ser Thr Ala Val Met 2450 2455 2460 Ser Met Val Gly Tyr He Leu Gly Leu Gly Asp Arg His Gly Glu Asn 2465 2470 2475 2480 He Leu Phe Asp Ser Leu Thr Gly Glu Cys Val His Val Asp Phe Asn 2485 2490 2495 Cys Leu Phe Asn Lys Gly Glu Thr Phe Glu Val Pro Glu He Val Pro 2500 2505 2510 Phe Arg Leu Thr His Asn Met Val Asn Gly Met Gly Pro Met Gly Thr 2515 2520 2525 Glu Gly Leu Phe Arg Arg Ala Cys Glu Val Thr Met Arg Leu Met Arg 2530 2535 2540 Asp Gin Arg Glu Pro Leu Met Ser Val Leu Lys Thr Phe Leu His Asp 2545 2550 2555 2560 Pro Leu Val Glu Trp Ser Lys Pro Val Lys Gly His Ser Lys Ala Pro 2565 2570 2575 Leu Asn Glu Thr Gly Glu Val Val Asn Glu Lys Ala Lys Thr His Val 2580 2585 2590 Leu Asp He Glu Gin Arg Leu Gin Gly Val He Lys Thr Arg Asn Arg 2595 2600 2605 Val Thr Gly Leu Pro Leu Ser He Glu Gly His Val His Tyr Leu He 2610 2615 2620 Gin Glu Ala Thr Asp Glu Asn Leu Leu Cys Gin Met Tyr Leu Gly Trp 2625 2630 2635 2640 Thr Pro Tyr Met (2) INFORMATION FOR SEQ ID NO:30: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 7624 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 333..7562 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:30: CTTGTGAAGA GAATGTTTTA CACTCTTGTT AGTGAAGTTT ATTCTTTAAA AGTCAATCGT 60 CAAGGATTTA GCAAATGAAT TAGCACTTCG GATATACTTG TTTATTTAAT ATCTTTTTTG 120 TTTATTTCAA AGAATTCAGT AATTGGATCA TAACGAGACT TCTGCGGATT GCAGCAACTC 180 CCTCCTGTCA TTTGTTACAC AAGAAAATCT GTGAAGTCAT CTGTTCATTA TTATTTCTTT 240 TTAAAAGCAA GAGTCCTGCT ATTTTTGGGG TACTCACAAA AGAATTATTA CAACTTTTTG 300 AAGACTTGGT TTACCTCCAT AGAAGAAATG TG ATG GGT CAT GCT GTG GAA TGG 353 Met Gly His Ala Val Glu Trp 1 5 CCA GTG GTC ATG AGC CGA TTT TTA AGT CAA TTA GAT GAA CAC ATG GGA 401 Pro Val Val Met Ser Arg Phe Leu Ser Gin Leu Asp Glu His Met Gly 10 15 20 TAT TTA CAA TCA GCT CCT TTG CAG TTG ATG AGT ATG CAA AAT TTA GAA 449 Tyr Leu Gin Ser Ala Pro Leu Gin Leu Met Ser Met Gin Asn Leu Glu 25 30 35 TTT ATT GAA GTC ACT TTA TTA ATG GTT CTT ACT CGT ATT ATT GCA ATT 497 Phe He Glu Val Thr Leu Leu Met Val Leu Thr Arg He He Ala He 40 45 50 55 GTG TTT TTT AGA AGG CAA GAA CTC TTA CTT TGG CAG ATA GGT TGT GTT 545 Val Phe Phe Arg Arg Gin Glu Leu Leu Leu Trp Gin He Gly Cys Val 60 65 70 CTG CTA GAG TAT GGT AGT CCA AAA ATT AAA TCC CTA GCA ATT AGC TTT 593 Leu Leu Glu Tyr Gly Ser Pro Lys He Lys Ser Leu Ala He Ser Phe 75 80 85 TTA ACA GAA CTT TTT CAG CTT GGA GGA CTA CCA GCA CAA CCA GCT AGC 641 Leu Thr Glu Leu Phe Gin Leu Gly Gly Leu Pro Ala Gin Pro Ala Ser 90 95 100 ACT TTT TTC AGC TCA TTT TTG GAA TTA TTA AAA CAC CTT GTA GAA ATG 689 Thr Phe Phe Ser Ser Phe Leu Glu Leu Leu Lys His Leu Val Glu Met 105 110 115 GAT ACT GAC CAA TTG AAA CTC TAT GAA GAG CCA TTA TCA AAG CTG ATA 737 Asp Thr Asp Gin Leu Lys Leu Tyr Glu Glu Pro Leu Ser Lys Leu He 120 125 130 135 AAG ACA CTA TTT CCC TTT GAA GCA GAA GCT TAT AGA AAT ATT GAA CCT 785 Lys Thr Leu Phe Pro Phe Glu Ala Glu Ala Tyr Arg Asn He Glu Pro 140 145 150 GTC TAT TTA AAT ATG CTG CTG GAA AAA CTC TGT GTC ATG TTT GAA GAC 833 Val Tyr Leu Asn Met Leu Leu Glu Lys Leu Cys Val Met Phe Glu Asp 155 160 165 GGT GTG CTC ATG CGG CTT AAG TCT GAT TTG CTA AAA GCA GCT TTG TGC 881 Gly Val Leu Met Arg Leu Lys Ser Asp Leu Leu Lys Ala Ala Leu Cys 170 175 180 CAT TTA CTG CAG TAT TTC CTT AAA TTT GTG CCA GCT GGG TAT GAA TCT 929 His Leu Leu Gin Tyr Phe Leu Lys Phe Val Pro Ala Gly Tyr Glu Ser 185 190 195 GCT TTA CAA GTC AGG AAG GTC TAT GTG AGA AAT ATT TGT AAA GCT CTT 977 Ala Leu Gin Val Arg Lys Val Tyr Val Arg Asn He Cys Lys Ala Leu 200 205 210 215 TTG GAT GTG CTT GGA ATT GAG GTA GAT GCA GAG TAC TTG TTG GGC CCA 1025 Leu Asp Val Leu Gly He Glu Val Asp Ala Glu Tyr Leu Leu Gly Pro 220 225 230 CTT TAT GCA GCT TTG AAA ATG GAA AGT ATG GAA ATC ATT GAG GAG ATT 1073 Leu Tyr Ala Ala Leu Lys Met Glu Ser Met Glu He He Glu Glu He 235 240 245 CAA TGC CAA ACT CAA CAG GAA AAC CTC AGC AGT AAT AGT GAT GGA ATA 1121 Gin Cys Gin Thr Gin Gin Glu Asn Leu Ser Ser Asn Ser Asp Gly He 250 255 260 TCA CCC AAA AGG CGT CGT CTC AGC TCG TCT CTA AAC CCT TCT AAA AGA 1169 Ser Pro Lys Arg Arg Arg Leu Ser Ser Ser Leu Asn Pro Ser Lys Arg 265 270 275 GCA CCA AAA CAG ACT GAG GAA ATT AAA CAT GTG GAC ATG AAC CAA AAG 1217 Ala Pro Lys Gin Thr Glu Glu He Lys His Val Asp Met Asn Gin Lys 280 285 290 295 AGC ATA TTA TGG AGT GCA CTG AAA CAG AAA GCT GAA TCC CTT CAG ATT 1265 Ser He Leu Trp Ser Ala Leu Lys Gin Lys Ala Glu Ser Leu Gin He 300 305 310 TCC CTT GAA TAC AGT GGC CTA AAG AAT CCT GTT ATT GAG ATG TTA GAA 1 13 Ser Leu Glu Tyr Ser Gly Leu Lys Asn Pro Val He Glu Met Leu Glu 315 320 325 GGA ATT GCT GTT GTC TTA CAA CTG ACT GCT CTG TGT ACT GTT CAT TGT 1361 Gly He Ala Val Val Leu Gin Leu Thr Ala Leu Cys Thr Val His Cys 330 335 340 TCT CAT CAA AAC ATG AAC TGC CGT ACT TTC AAG GAC TGT CAA CAT AAA 1409 Ser His Gin Asn Met Asn Cys Arg Thr Phe Lys Aεp Cys Gin His Lys 345 350 355 TCC AAG AAG AAA CCT TCT GTA GTG ATA ACT TGG ATG TCA TTG GAT TTT 1457 Ser Lys Lys Lys Pro Ser Val Val He Thr Trp Met Ser Leu Asp Phe 360 365 370 375 TAC ACA AAA GTG CTT AAG AGC TGT AGA AGT TTG TTA GAA TCT GTT CAG 1505 Tyr Thr Lys Val Leu Lys Ser Cys Arg Ser Leu Leu Glu Ser Val Gin 380 385 390 AAA CTG GAC CTG GAG GCA ACC ATT GAT AAG GTG GTG AAA ATT TAT GAT 1553 Lys Leu Asp Leu Glu Ala Thr He Asp Lys Val Val Lys He Tyr Asp 395 400 405 GCT TTG ATT TAT ATG CAA GTA AAC AGT TCA TTT GAA GAT CAT ATC CTG 1601 Ala Leu He Tyr Met Gin Val Asn Ser Ser Phe Glu Asp His He Leu 410 415 420 GAA GAT TTA TGT GGA ATG CTC TCA CTT CCA TGG ATT TAT TCC CAT TCT 1649 Glu Asp Leu Cys Gly Met Leu Ser Leu Pro Trp He Tyr Ser His Ser 425 430 435 GAT GAT GGC TGT TTA AAG TTG ACC ACA TTT GCC GCT AAT CTT CTA ACA 1697 Asp Asp Gly Cys Leu Lys Leu Thr Thr Phe Ala Ala Asn Leu Leu Thr 440 445 450 455 TTA AGC TGT AGG ATT TCA GAT AGC TAT TCA CCA CAG GCA CAA TCA CGA 1745 Leu Ser Cys Arg He Ser Asp Ser Tyr Ser Pro Gin Ala Gin Ser Arg 460 465 470 TGT GTG TTT CTT CTG ACT CTG TTT CCA AGA AGA ATA TTC CTT GAG TGG 1793 Cys Val Phe Leu Leu Thr Leu Phe Pro Arg Arg He Phe Leu Glu Trp 475 480 485 AGA ACA GCA GTT TAC AAC TGG GCC CTG CAG AGC TCC CAT GAA GTA ATC 1841 Arg Thr Ala Val Tyr Asn Trp Ala Leu Gin Ser Ser His Glu Val He 490 495 500 CGG GCT AGT TGT GTT AGT GGA TTT TTT ATC TTA TTG CAG CAG CAG AAT 1889 Arg Ala Ser Cys Val Ser Gly Phe Phe He Leu Leu Gin Gin Gin Asn 505 510 515 TCT TGT AAC AGA GTT CCC AAG ATT CTT ATA GAT AAA GTC AAA GAT GAT 1937 Ser Cys Asn Arg Val Pro Lys He Leu He Asp Lys Val Lys Asp Asp 520 525 530 535 TCT GAC ATT GTC AAG AAA GAA TTT GCT TCT ATA CTT GGT CAA CTT GTC 1985 Ser Asp He Val Lys Lys Glu Phe Ala Ser He Leu Gly Gin Leu Val 540 545 550 TGT ACT CTT CAC GGC ATG TTT TAT CTG ACA AGT TCT TTA ACA GAA CCT 2033 Cys Thr Leu His Gly Met Phe Tyr Leu Thr Ser Ser Leu Thr Glu Pro 555 560 565 TTC TCT GAA CAC GGA CAT GTG GAC CTC TTC TGT AGG AAC TTG AAA GCC 2081 Phe Ser Glu His Gly His Val Asp Leu Phe Cys Arg Asn Leu Lys Ala 570 575 580 ACT TCT CAA CAT GAA TGT TCA TCT TCT CAA CTA AAA GCT TCT GTC TGC 2129 Thr Ser Gin His Glu Cys Ser Ser Ser Gin Leu Lys Ala Ser Val Cys 585 590 595 AAG CCA TTC CTT TTC CTA CTG AAA AAA AAA ATA CCT AGT CCA GTA AAA 2177 Lys Pro Phe Leu Phe Leu Leu Lys Lys Lys He Pro Ser Pro Val Lys 600 605 610 615 CTT GCT TTC ATA GAT AAT CTA CAT CAT CTT TGT AAG CAT CTT GAT TTT 2225 Leu Ala Phe He Asp Asn Leu His His Leu Cys Lys His Leu Asp Phe 620 625 630 AGA GAA GAT GAA ACA GAT GTA AAA GCA GTT CTT GGA ACT TTA TTA AAT 2273 Arg Glu Asp Glu Thr Asp Val Lys Ala Val Leu Gly Thr Leu Leu Asn 635 640 645 TTA ATG GAA GAT CCA GAC AAA GAT GTT AGA GTG GCT TTT AGT GGA AAT 2321 Leu Met Glu Asp Pro Asp Lys Asp Val Arg Val Ala Phe Ser Gly Asn 650 655 660 ATC AAG CAC ATA TTG GAA TCC TTG GAC TCT GAA GAT GGA TTT ATA AAG 2369 He Lys His He Leu Glu Ser Leu Asp Ser Glu Asp Gly Phe He Lys 665 670 675 GAG CTT TTT GTC TTA AGA ATG AAG GAA GCA TAT ACA CAT GCC CAA ATA 2417 Glu Leu Phe Val Leu Arg Met Lys Glu Ala Tyr Thr His Ala Gin He 680 685 690 695 TCA AGA AAT AAT GAG CTG AAG GAT ACC TTG ATT CTT ACA ACA GGG GAT 2465 Ser Arg Aεn Aεn Glu Leu Lys Asp Thr Leu He Leu Thr Thr Gly Asp 700 705 710 ATT GGA AGG GCC GCA AAA GGA GAT TTG GTA CCA TTT GCA CTC TTA CAC 2513 He Gly Arg Ala Ala Lys Gly Asp Leu Val Pro Phe Ala Leu Leu His 715 720 725 TTA TTG CAT TGT TTG TTA TCC AAG TCA GCA TCT GTC TCT GGA GCA GCA 2561 Leu Leu His Cyε Leu Leu Ser Lys Ser Ala Ser Val Ser Gly Ala Ala 730 735 740 TAC ACA GAA ATT AGA GCT CTG GTT GCA GCT AAA AGT GTT AAA CTG CAA 2609 Tyr Thr Glu He Arg Ala Leu Val Ala Ala Lys Ser Val Lys Leu Gin 745 750 755 AGT TTT TTC AGC CAG TAT AAG AAA CCC ATC TGT CAG TTT TTG GTA GAA 2657 Ser Phe Phe Ser Gin Tyr Lys Lyε Pro He Cys Gin Phe Leu Val Glu 760 765 770 775 TCC CTT CAC TCT AGT CAG ATG ACA GCA CTT CCG AAT ACT CCA TGC CAG 2705 Ser Leu His Ser Ser Gin Met Thr Ala Leu Pro Asn Thr Pro Cys Gin 780 785 790 AAT GCT GAC GTG CGA AAA CAA GAT GTG GCT CAC CAG AGA GAA ATG GCT 2753 Asn Ala Asp Val Arg Lys Gin Asp Val Ala His Gin Arg Glu Met Ala 795 800 805 TTA AAT ACG TTG TCT GAA ATT GCC AAC GTT TTC GAC TTT CCT GAT CTT 2801 Leu Asn Thr Leu Ser Glu He Ala Asn Val Phe Asp Phe Pro Asp Leu 810 815 820 AAT CGT TTT CTT ACT AGG ACA TTA CAA GTT CTA CTA CCT GAT CTT GCT 2849 Asn Arg Phe Leu Thr Arg Thr Leu Gin Val Leu Leu Pro Asp Leu Ala 825 830 835 GCC AAA GCA AGC CCT GCA GCT TCT GCT CTC ATT CGA ACT TTA GGA AAA 2897 Ala Lys Ala Ser Pro Ala Ala Ser Ala Leu He Arg Thr Leu Gly Lys 840 845 850 855 CAA TTA AAT GTC AAT CGT AGA GAG ATT TTA ATA AAC AAC TTC AAA TAT 2945 Gin Leu Asn Val Asn Arg Arg Glu He Leu He Asn Aεn Phe Lys Tyr 860 865 870 ATT TTT TCT CAT TTG GTC TGT TCT TGT TCC AAA GAT GAA TTA GAA CGT 2993 He Phe Ser His Leu Val Cys Ser Cys Ser Lys Asp Glu Leu Glu Arg 875 880 885 GCC CTT CAT TAT CTG AAG AAT GAA ACA GAA ATT GAA CTG GGG AGC CTG 3041 Ala Leu His Tyr Leu Lys Asn Glu Thr Glu He Glu Leu Gly Ser Leu 890 895 900 TTG AGA CAA GAT TTC CAA GGA TTG CAT AAT GAA TTA TTG CTG CGT ATT 3089 Leu Arg Gin Asp Phe Gin Gly Leu His Asn Glu Leu Leu Leu Arg He 905 910 915 GGA GAA CAC TAT CAA CAG GTT TTT AAT GGT TTG TCA ATA CTT GCC TCA 3137 Gly Glu His Tyr Gin Gin Val Phe Asn Gly Leu Ser He Leu Ala Ser 920 925 930 935 TTT GCA TCC AGT GAT GAT CCA TAT CAG GGC CCG AGA GAT ATC ATA TCA 3185 Phe Ala Ser Ser Asp Aεp Pro Tyr Gin Gly Pro Arg Asp He He Ser 940 945 950 CCT GAA CTG ATG GCT GAT TAT TTA CAA CCC AAA TTG TTG GGC ATT TTG 3233 Pro Glu Leu Met Ala Asp Tyr Leu Gin Pro Lyε Leu Leu Gly He Leu 955 960 965 GCT TTT TTT AAC ATG CAG TTA CTG AGC TCT AGT GTT GGC ATT GAA GAT 3281 Ala Phe Phe Asn Met Gin Leu Leu Ser Ser Ser Val Gly He Glu Asp 970 975 980 AAG AAA ATG GCC TTG AAC AGT TTG ATG TCT TTG ATG AAG TTA ATG GGA 3329 Lys Lys Met Ala Leu Aεn Ser Leu Met Ser Leu Met Lyε Leu Met Gly 985 990 995 CCC AAA CAT GTC AGT TCT GTG AGG GTG AAG ATG ATG ACC ACA CTG AGA 3377 Pro Lys His Val Ser Ser Val Arg Val Lyε Met Met Thr Thr Leu Arg 1000 1005 1010 1015 ACT GGC CTT CGA TTC AAG GAT GAT TTT CCT GAA TTG TGT TGC AGA GCT 3425 Thr Gly Leu Arg Phe Lyε Aεp Asp Phe Pro Glu Leu Cys Cys Arg Ala 1020 1025 1030 TGG GAC TGC TTT GTT CGC TGC CTG GAT CAT GCT TGT CTG GGC TCC CTT 3473 Trp Asp Cys Phe Val Arg Cys Leu Asp His Ala Cys Leu Gly Ser Leu 1035 1040 1045 CTC AGT CAT GTA ATA GTA GCT TTG TTA CCT CTT ATA CAC ATC CAG CCT 3521 Leu Ser Hiε Val He Val Ala Leu Leu Pro Leu He Hiε He Gin Pro 1050 1055 1060 AAA GAA ACT GCA GCT ATC TTC CAC TAC CTC ATA ATT GAA AAC AGG GAT 3569 Lys Glu Thr Ala Ala He Phe His Tyr Leu He He Glu Aεn Arg Asp 1065 1070 1075 GCT GTG CAA GAT TTT CTT CAT GAA ATA TAT TTT TTA CCT GAT CAT CCA 3617 Ala Val Gin Asp Phe Leu Hiε Glu He Tyr Phe Leu Pro Asp His Pro 1080 1085 1090 1095 GAA TTA AAA AAG ATA AAA GCC GTT CTC CAG GAA TAC AGA AAG GAG ACC 3665 Glu Leu Lys Lyε He Lyε Ala Val Leu Gin Glu Tyr Arg Lys Glu Thr 1100 1105 mo TCT GAG AGC ACT GAT CTT CAG ACA ACT CTT CAG CTC TCT ATG AAG GCC 3713 Ser Glu Ser Thr Asp Leu Gin Thr Thr Leu Gin Leu Ser Met Lys Ala 1115 1120 1125 ATT CAA CAT GAA AAT GTC GAT GTT CGT ATT CAT GCT CTT ACA AGC TTG 3761 He Gin His Glu Asn Val Asp Val Arg He His Ala Leu Thr Ser Leu 1130 1135 1140 AAG GAA ACC TTG TAT AAA AAT CAG GAA AAA CTG ATA AAG TAT GCA ACA 3809 Lys Glu Thr Leu Tyr Lys Asn Gin Glu Lys Leu He Lys Tyr Ala Thr 1145 1150 1155 GAC AGT GAA ACA GTA GAA CCT ATT ATC TCA CAG TTG GTG ACA GTG CTT 3857 Asp Ser Glu Thr Val Glu Pro He He Ser Gin Leu Val Thr Val Leu 1160 1165 1170 1175 TTG AAA GGT TGC CAA GAT GCA AAC TCT CAA GCT CGG TTG CTC TGT GGG 3905 Leu Lys Gly Cys Gin Asp Ala Aεn Ser Gin Ala Arg Leu Leu Cyε Gly 1180 1185 1190 GAA TGT TTA GGG GAA TTG GGG GCG ATA GAT CCA GGT CGA TTA GAT TTC 3953 Glu Cys Leu Gly Glu Leu Gly Ala He Asp Pro Gly Arg Leu Asp Phe 1195 1200 1205 TCA ACA ACT GAA ACT CAA GGA AAA GAT TTT ACA TTT GTG ACT GGA GTA 4001 Ser Thr Thr Glu Thr Gin Gly Lys Asp Phe Thr Phe Val Thr Gly Val 1210 1215 1220 GAA GAT TCA AGC TTT GCC TAT GGA TTA TTG ATG GAG CTA ACA AGA GCT 4049 Glu Aεp Ser Ser Phe Ala Tyr Gly Leu Leu Met Glu Leu Thr Arg Ala 1225 1230 1235 TAC CTT GCG TAT GCT GAT AAT AGC CGA GCT CAA GAT TCA GCT GCC TAT 4097 Tyr Leu Ala Tyr Ala Aεp Asn Ser Arg Ala Gin Asp Ser Ala Ala Tyr 1240 1245 1250 1255 GCC ATT CAG GAG TTG CTT TCT ATT TAT GAC TGT AGA GAG ATG GAG ACC 4145 Ala He Gin Glu Leu Leu Ser He Tyr Asp Cys Arg Glu Met Glu Thr 1260 1265 1270 AAC GGC CCA GGT CAC CAA TTG TGG AGG AGA TTT CCT GAG CAT GTT CGG 4193 Asn Gly Pro Gly His Gin Leu Trp Arg Arg Phe Pro Glu His Val Arg 1275 1280 1285 GAA ATA CTA GAA CCT CAT CTA AAT ACC AGA TAC AAG AGT TCT CAG AAG 4241 Glu He Leu Glu Pro His Leu Asn Thr Arg Tyr Lys Ser Ser Gin Lys 1290 1295 1300 TCA ACC GAT TGG TCT GGA GTA AAG AAG CCA ATT TAC TTA AGT AAA TTG 4289 Ser Thr Asp Trp Ser Gly Val Lys Lys Pro He Tyr Leu Ser Lys Leu 1305 1310 1315 GGT AGT AAC TTT GCA GAA TGG TCA GCA TCT TGG GCA GGT TAT CTT ATT 4337 Gly Ser Asn Phe Ala Glu Trp Ser Ala Ser Trp Ala Gly Tyr Leu He 1320 1325 1330 1335 ACA AAG GTT CGA CAT GAT CTT GCC AGT AAA ATT TTC ACC TGC TGT AGC 4385 Thr Lys Val Arg His Aεp Leu Ala Ser Lys He Phe Thr Cys Cys Ser 1340 1345 1350 ATT ATG ATG AAG CAT GAT TTC AAA GTG ACC ATC TAT CTT CTT CCA CAT 4433 He Met Met Lys Hiε Asp Phe Lys Val Thr He Tyr Leu Leu Pro His 1355 1360 1365 ATT CTG GTG TAT GTC TTA CTG GGT TGT AAT CAA GAA GAT CAG CAG GAG 4481 He Leu Val Tyr Val Leu Leu Gly Cys Asn Gin Glu Asp Gin Gin Glu 1370 1375 1380 GTT TAT GCA GAA ATT ATG GCA GTT CTA AAG CAT GAC GAT CAG CAT ACC 4529 Val Tyr Ala Glu He Met Ala Val Leu Lys His Asp Asp Gin His Thr 1385 1390 1395 ATA AAT ACC CAA GAC ATT GCA TCT GAT CTG TGT CAA CTC AGT ACA CAG 4577 He Asn Thr Gin Asp He Ala Ser Asp Leu Cys Gin Leu Ser Thr Gin 1400 1405 1410 1415 ACT GTG TTC TCC ATG CTT GAC CAT CTC ACA CAG TGG GCA AGG CAC AAA 4625 Thr Val Phe Ser Met Leu Asp His Leu Thr Gin Trp Ala Arg His Lys 1420 1425 1430 TTT CAG GCA CTG AAA GCT GAG AAA TGT CCA CAC AGC AAA TCA AAC AGA 4673 Phe Gin Ala Leu Lys Ala Glu Lys Cys Pro His Ser Lys Ser Asn Arg 1435 1440 1445 AAT AAG GTA GAC TCA ATG GTA TCT ACT GTG GAT TAT GAA GAC TAT CAG 4721 Asn Lys Val Asp Ser Met Val Ser Thr Val Asp Tyr Glu Asp Tyr Gin 1450 1455 1460 AGT GTA ACC CGT TTT CTA GAC CTC ATA CCC CAG GAT ACT CTG GCA GTA 4769 Ser Val Thr Arg Phe Leu Asp Leu He Pro Gin Asp Thr Leu Ala Val 1465 1470 1475 GCT TCC TTT CGC TCC AAA GCA TAC ACA CGA GCT GTA ATG CAC TTT GAA 4817 Ala Ser Phe Arg Ser Lyε Ala Tyr Thr Arg Ala Val Met His Phe Glu 1480 1485 1490 1495 TCA TTT ATT ACA GAA AAG AAG CAA AAT ATT CAG GAA CAT CTT GGA TTT 4865 Ser Phe He Thr Glu Lys Lyε Gin Asn He Gin Glu Hiε Leu Gly Phe 1500 1505 1510 TTA CAG AAA TTG TAT GCT GCT ATG CAT GAA CCT GAT GGA GTG GCC GGA 4913 Leu Gin Lys Leu Tyr Ala Ala Met His Glu Pro Asp Gly Val Ala Gly 1515 1520 1525 GTC AGT GCA ATT AGA AAG GCA GAA CCA TCT CTA AAA GAA CAG ATC CTT 4961 Val Ser Ala He Arg Lys Ala Glu Pro Ser Leu Lys Glu Gin He Leu 1530 1535 1540 GAA CAT GAA AGC CTT GGC TTG CTG AGG GAT GCC ACT GCT TGT TAT GAC 5009 Glu His Glu Ser Leu Gly Leu Leu Arg Asp Ala Thr Ala Cys Tyr Asp 1545 1550 1555 AGG GCT ATT CAG CTA GAA CCA GAC CAG ATC ATT CAT TAC CAT GGT GTA 5057 Arg Ala He Gin Leu Glu Pro Asp Gin He He His Tyr His Gly Val 1560 1565 1570 1575 GTA AAG TCC ATG TTA GGT CTT GGT CAG CTG TCT ACT GTT ATC ACT CAG 5105 Val Lys Ser Met Leu Gly Leu Gly Gin Leu Ser Thr Val He Thr Gin 1580 1585 1590 GTG AAT GGA GTG CAT GCT AAC AGG TCC GAG TGG ACA GAT GAA TTA AAC 5153 Val Asn Gly Val His Ala Asn Arg Ser Glu Trp Thr Aεp Glu Leu Asn 1595 1600 1605 ACG TAC AGA GTG GAA GCA GCT TGG AAA TTG TCA CAG TGG GAT TTG GTG 5201 Thr Tyr Arg Val Glu Ala Ala Trp Lys Leu Ser Gin Trp Asp Leu Val 1610 1615 1620 GAA AAC TAT TTG GCA GCA GAT GGA AAA TCT ACA ACA TGG AGT GTC AGA 5249 Glu Asn Tyr Leu Ala Ala Asp Gly Lys Ser Thr Thr Trp Ser Val Arg 1625 1630 1635 CTG GGA CAG CTA TTA TTA TCA GCC AAA AAA AGA GAT ATC ACA GCT TTT 5297 Leu Gly Gin Leu Leu Leu Ser Ala Lys Lys Arg Asp He Thr Ala Phe 1640 1645 1650 1655 TAT GAC TCA CTG AAA CTA GTG AGA GCA GAA CAA ATT GTA CCT CTT TCA 5345 Tyr Asp Ser Leu Lys Leu Val Arg Ala Glu Gin He Val Pro Leu Ser 1660 1665 1670 GCT GCA AGC TTT GAA AGA GGC TCC TAC CAA CGA GGA TAT GAA TAT ATT 5393 Ala Ala Ser Phe Glu Arg Gly Ser Tyr Gin Arg Gly Tyr Glu Tyr He 1675 1680 1685 GTG AGA TTG CAC ATG TTA TGT GAG TTG GAG CAT AGC ATC AAA CCA CTT 5441 Val Arg Leu His Met Leu Cys Glu Leu Glu His Ser He Lys Pro Leu 1690 1695 1700 TTC CAG CAT TCT CCA GGT GAC AGT TCT CAA GAA GAT TCT CTA AAC TGG 5489 Phe Gin His Ser Pro Gly Asp Ser Ser Gin Glu Asp Ser Leu Asn Trp 1705 1710 1715 GTA GCT CGA CTA GAA ATG ACC CAG AAT TCC TAC AGA GCC AAG GAG CCT 5537 Val Ala Arg Leu Glu Met Thr Gin Asn Ser Tyr Arg Ala Lys Glu Pro 1720 1725 1730 1735 ATC CTG GCT CTC CGG AGG GCT TTA CTA AGC CTC AAC AAA AGA CCA GAT 5585 He Leu Ala Leu Arg Arg Ala Leu Leu Ser Leu Aεn Lys Arg Pro Asp 1740 1745 1750 TAC AAT GAA ATG GTT GGA GAA TGC TGG CTG CAG AGT GCC AGG GTA GCT 5633 Tyr Asn Glu Met Val Gly Glu Cys Trp Leu Gin Ser Ala Arg Val Ala 1755 1760 1765 AGA AAG GCT GGT CAC CAC CAG ACA GCC TAC AAT GCT CTC CTT AAT GCA 5681 Arg Lys Ala Gly His His Gin Thr Ala Tyr Asn Ala Leu Leu Asn Ala 1770 1775 1780 GGG GAA TCA CGA CTC GCT GAA CTG TAC GTG GAA AGG GCA AAG TGG CTC 5729 Gly Glu Ser Arg Leu Ala Glu Leu Tyr Val Glu Arg Ala Lys Trp Leu 1785 1790 1795 TGG TCC AAG GGT GAT GTT CAC CAG GCA CTA ATT GTT CTT CAA AAA GGT 5777 Trp Ser Lys Gly Asp Val His Gin Ala Leu He Val Leu Gin Lys Gly 1800 1805 1810 1815 GTT GAA TTA TGT TTT CCT GAA AAT GAA ACC CCA CCT GAG GGT AAG AAC 5825 Val Glu Leu Cys Phe Pro Glu Aεn Glu Thr Pro Pro Glu Gly Lyε Asn 1820 1825 1830 ATG TTA ATC CAT GGT CGA GCT ATG CTA CTA GTG GGC CGA TTT ATG GAA 5873 Met Leu He His Gly Arg Ala Met Leu Leu Val Gly Arg Phe Met Glu 1835 1840 1845 GAA ACA GCT AAC TTT GAA AGC AAT GCA ATT ATG AAA AAA TAT AAG GAT 5921 Glu Thr Ala Asn Phe Glu Ser Aεn Ala He Met Lys Lys Tyr Lyε Asp 1850 1855 1860 GTG ACC GCG TGC CTG CCA GAA TGG GAG GAT GGG CAT TTT TAC CTT GCC 5969 Val Thr Ala Cys Leu Pro Glu Trp Glu Asp Gly His Phe Tyr Leu Ala 1865 1870 1875 AAG TAC TAT GAC AAA TTG ATG CCC ATG GTC ACA GAC AAC AAA ATG GAA 6017 Lys Tyr Tyr Asp Lyε Leu Met Pro Met Val Thr Asp Aεn Lyε Met Glu 1880 1885 1890 1895 AAG CAA GGT GAT CTC ATC CGG TAT ATA GTT CTT CAT TTT GGC AGA TCT 6065 Lys Gin Gly Aεp Leu He Arg Tyr He Val Leu His Phe Gly Arg Ser 1900 1905 1910 CTA CAA TAT GGA AAT CAG TTC ATA TAT CAG TCA ATG CCA CGA ATG TTA 6113 Leu Gin Tyr Gly Asn Gin Phe He Tyr Gin Ser Met Pro Arg Met Leu 1915 1920 1925 ACT CTA TGG CTT GAT TAT GGT ACA AAG GCA TAT GAA TGG GAA AAA GCT 6161 Thr Leu Trp Leu Asp Tyr Gly Thr Lys Ala Tyr Glu Trp Glu Lys Ala 1930 1935 1940 GGC CGC TCC GAT CGT GTA CAA ATG AGG AAT GAT TTG GGT AAA ATA AAC 6209 Gly Arg Ser Asp Arg Val Gin Met Arg Asn Asp Leu Gly Lys He Asn 1945 1950 1955 AAG GTT ATC ACA GAG CAT ACA AAC TAT TTA GCT CCA TAT CAA TTT TTG 6257 Lys Val He Thr Glu His Thr Asn Tyr Leu Ala Pro Tyr Gin Phe Leu 1960 1965 1970 1975 ACT GCT TTT TCA CAA TTG ATC TCT CGA ATT TGT CAT TCT CAC GAT GAA 6305 Thr Ala Phe Ser Gin Leu He Ser Arg He Cys His Ser His Asp Glu 1980 1985 1990 GTT TTT GTT GTC TTG ATG GAA ATA ATA GCC AAA GTA TTT CTA GCC TAT 6353 Val Phe Val Val Leu Met Glu He He Ala Lys Val Phe Leu Ala Tyr 1995 2000 2005 CCT CAA CAA GCA ATG TGG ATG ATG ACA GCT GTG TCA AAG TCA TCT TAT 6401 Pro Gin Gin Ala Met Trp Met Met Thr Ala Val Ser Lys Ser Ser Tyr 2010 2015 2020 CCC ATG CGT GTG AAC AGA TGC AAG GAA ATC CTC AAT AAA GCT ATT CAT 6449 Pro Met Arg Val Asn Arg Cys Lys Glu He Leu Asn Lys Ala He Hiε 2025 2030 2035 ATG AAA AAA TCC TTA GAG AAG TTT GTT GGA GAT GCA ACT CGC CTA ACA 6497 Met Lys Lys Ser Leu Glu Lys Phe Val Gly Asp Ala Thr Arg Leu Thr 2040 2045 2050 2055 GAT AAG CTT CTA GAA TTG TGC AAT AAA CCG GTG GAA ATT CTT GCT TCT 6545 Aεp Lys Leu Leu Glu Leu Cys Aεn Lys Pro Val Glu He Leu Ala Ser 2060 2065 2070 CTT CAG AAA CCA AAG AAG ATT TCT TTA AAA GGC TCA GAT GGA AAG TTC 6593 Leu Gin Lys Pro Lys Lys He Ser Leu Lys Gly Ser Asp Gly Lys Phe 2075 2080 2085 TAC ATC ATG ATG TGT AAG CCA AAA GAT GAC CTG AGA AAG GAT TGT AGA 6641 Tyr He Met Met Cys Lys Pro Lys Asp Asp Leu Arg Lys Asp Cys Arg 2090 2095 2100 CTA ATG GAA TTC AAT TCC TTG ATT AAT AAG TGC TTA AGA AAA GAT GCA 6689 Leu Met Glu Phe Asn Ser Leu He Aεn Lys Cys Leu Arg Lys Asp Ala 2105 2110 2115 GAG TCT CGT AGA AGA GAA CTT CAT ATT CGA ACA TAT GCA GTT ATT CCA 6737 Glu Ser Arg Arg Arg Glu Leu His He Arg Thr Tyr Ala Val He Pro 2120 2125 2130 2135 CTA AAT GAT GAA TGT GGG ATT ATT GAA TGG GTG AAC AAC ACT GCT GGT 6785 Leu Aεn Asp Glu Cyε Gly He He Glu Trp Val Asn Aεn Thr Ala Gly 2140 2145 2150 TTG AGA CCT ATT CTG ACC AAA CTA TAT AAA GAA AAG GGA GTG TAT ATG 6833 Leu Arg Pro He Leu Thr Lys Leu Tyr Lys Glu Lys Gly Val Tyr Met 2155 2160 2165 ACA GGA AAA GAA CTT CGC CAG TGT ATG CTA CCA AAG TCA GCA GCT TTA 6881 Thr Gly Lys Glu Leu Arg Gin Cys Met Leu Pro Lys Ser Ala Ala Leu 2170 2175 2180 TCT GAA AAA CTC AAA GTA TTC CGA GAA TTT CTC CTG CCC AGG CAT CCT 6929 Ser Glu Lyε Leu Lys Val Phe Arg Glu Phe Leu Leu Pro Arg His Pro 2185 2190 2195 CCT ATT TTT CAT GAG TGG TTT CTG AGA ACA TTC CCT GAT CCT ACA TCA 6977 Pro He Phe His Glu Trp Phe Leu Arg Thr Phe Pro Asp Pro Thr Ser 2200 2205 2210 2215 TGG TAC AGT AGT AGA TCA GCT TAC TGC CGT TCC ACT GCA GTA ATG TCA 7025 Trp Tyr Ser Ser Arg Ser Ala Tyr Cys Arg Ser Thr Ala Val Met Ser 2220 2225 2230 ATG GTT GGT TAT ATT CTG GGG CTT GGA GAC CGT CAT GGT GAA AAT ATT 7073 Met Val Gly Tyr He Leu Gly Leu Gly Asp Arg His Gly Glu Asn He 2235 2240 2245 CTC TTT GAT TCT TTG ACT GGT GAA TGC GTA CAT GTA GAT TTC AAT TGT 7121 Leu Phe Asp Ser Leu Thr Gly Glu Cys Val His Val Asp Phe Asn Cys 2250 2255 2260 CTT TTC AAT AAG GGA GAA ACC TTT GAA GTT CCA GAA ATT GTG CCA TTT 7169 Leu Phe Asn Lys Gly Glu Thr Phe Glu Val Pro Glu He Val Pro Phe 2265 2270 2275 CGC CTG ACT CAT AAT ATG GTT AAT GGA ATG GGT CCT ATG GGA ACA GAG 7217 Arg Leu Thr His Asn Met Val Asn Gly Met Gly Pro Met Gly Thr Glu 2280 2285 2290 2295 GGT CTT TTT CGA AGA GCA TGT GAA GTT ACA ATG AGG CTG ATG CGT GAT 7265 Gly Leu Phe Arg Arg Ala Cys Glu Val Thr Met Arg Leu Met Arg Asp 2300 2305 2310 CAG CGA GAG CCT TTA ATG AGT GTC TTA AAG ACT TTT CTA CAT GAT CCT 7313 Gin Arg Glu Pro Leu Met Ser Val Leu Lys Thr Phe Leu His Asp Pro 2315 2320 2325 CTT GTG GAA TGG AGT AAA CCA GTG AAA GGG CAT TCC AAA GCG CCA CTG 7361 Leu Val Glu Trp Ser Lys Pro Val Lys Gly His Ser Lys Ala Pro Leu 2330 2335 2340 AAT GAA ACT GGA GAA GTT GTC AAT GAA AAG GCC AAG ACC CAT GTT CTT 7409 Asn Glu Thr Gly Glu Val Val Asn Glu Lys Ala Lys Thr His Val Leu 2345 2350 2355 GAC ATT GAG CAG CGA CTA CAA GGT GTA ATC AAG ACT CGA AAT AGA GTG 7457 Asp He Glu Gin Arg Leu Gin Gly Val He Lys Thr Arg Asn Arg Val 2360 2365 2370 2375 ACA GGA CTG CCG TTA TCT ATT GAA GGA CAT GTG CAT TAC CTT ATA CAA 7505 Thr Gly Leu Pro Leu Ser He Glu Gly His Val His Tyr Leu He Gin 2380 2385 2390 GAA GCT ACT GAT GAA AAC TTA CTA TGC CAG ATG TAT CTT GGT TGG ACT 7553 Glu Ala Thr Aεp Glu Asn Leu Leu Cys Gin Met Tyr Leu Gly Trp Thr 2395 2400 2405 CCA TAT ATG TGAAATGAAA TTATGTAAAA GAATATGTTA ATAATCTAAA 7602 Pro Tyr Met 2410 AGTAAAAAAA AAAAAAAAAA AA 7624 (2) INFORMATION FOR SEQ ID NO:31. (l) SEQUENCE CHARACTERISTICS: (A) LENGTH. 2410 ammo acids (B) TYPE: amino acid (D) TOPOLOGY- linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION SEQ ID NO.31 Met Gly His Ala Val Glu Trp Pro Val Val Met Ser Arg Phe Leu Ser 1 5 10 15 Gin Leu Asp Glu His Met Gly Tyr Leu Gin Ser Ala Pro Leu Gin Leu 20 25 30 Met Ser Met Gin Asn Leu Glu Phe He Glu Val Thr Leu Leu Met Val 35 40 45 Leu Thr Arg He He Ala He Val Phe Phe Arg Arg Gin Glu Leu Leu 50 55 60 Leu Trp Gin He Gly Cys Val Leu Leu Glu Tyr Gly Ser Pro Lys He 65 70 75 80 Lyε Ser Leu Ala He Ser Phe Leu Thr Glu Leu Phe Gin Leu Gly Gly 85 90 95 Leu Pro Ala Gin Pro Ala Ser Thr Phe Phe Ser Ser Phe Leu Glu Leu 100 105 110 Leu Lys His Leu Val Glu Met Aεp Thr Asp Gin Leu Lys Leu Tyr Glu 115 120 125 Glu Pro Leu Ser Lys Leu He Lys Thr Leu Phe Pro Phe Glu Ala Glu 130 135 140 Ala Tyr Arg Asn He Glu Pro Val Tyr Leu Asn Met Leu Leu Glu Lys 145 150 155 160 Leu Cys Val Met Phe Glu Asp Gly Val Leu Met Arg Leu Lys Ser Asp 165 170 175 Leu Leu Lys Ala Ala Leu Cys His Leu Leu Gin Tyr Phe Leu Lys Phe 180 185 190 Val Pro Ala Gly Tyr Glu Ser Ala Leu Gin Val Arg Lys Val Tyr Val 195 200 205 Arg Asn He Cys Lyε Ala Leu Leu Asp Val Leu Gly He Glu Val Asp 210 215 220 Ala Glu Tyr Leu Leu Gly Pro Leu Tyr Ala Ala Leu Lys Met Glu Ser 225 230 235 240 Met Glu He He Glu Glu He Gin Cys Gin Thr Gin Gin Glu Asn Leu 245 250 255 Ser Ser Asn Ser Asp Gly He Ser Pro Lys Arg Arg Arg Leu Ser Ser 260 265 270 Ser Leu Asn Pro Ser Lys Arg Ala Pro Lys Gin Thr Glu Glu He Lys 275 280 285 His Val Asp Met Asn Gin Lys Ser He Leu Trp Ser Ala Leu Lys Gin 290 295 300 Lys Ala Glu Ser Leu Gin He Ser Leu Glu Tyr Ser Gly Leu Lys Aεn 305 310 315 320 Pro Val He Glu Met Leu Glu Gly He Ala Val Val Leu Gin Leu Thr 325 330 335 Ala Leu Cys Thr Val Hiε Cys Ser His Gin Asn Met Asn Cys Arg Thr 340 345 350 Phe Lys Asp Cys Gin His Lys Ser Lyε Lys Lys Pro Ser Val Val He 355 360 365 Thr Trp Met Ser Leu Asp Phe Tyr Thr Lys Val Leu Lys Ser Cys Arg 370 375 380 Ser Leu Leu Glu Ser Val Gin Lys Leu Asp Leu Glu Ala Thr He Asp 385 390 395 400 Lys Val Val Lys He Tyr Asp Ala Leu He Tyr Met Gin Val Asn Ser 405 410 415 Ser Phe Glu Asp His He Leu Glu Asp Leu Cys Gly Met Leu Ser Leu 420 425 430 Pro Trp He Tyr Ser His Ser Asp Asp Gly Cys Leu Lyε Leu Thr Thr 435 440 445 Phe Ala Ala Asn Leu Leu Thr Leu Ser Cys Arg He Ser Asp Ser Tyr 450 455 460 Ser Pro Gin Ala Gin Ser Arg Cys Val Phe Leu Leu Thr Leu Phe Pro 465 470 475 480 Arg Arg He Phe Leu Glu Trp Arg Thr Ala Val Tyr Asn Trp Ala Leu 485 490 495 Gin Ser Ser His Glu Val He Arg Ala Ser Cys Val Ser Gly Phe Phe 500 505 510 He Leu Leu Gin Gin Gin Asn Ser Cys Asn Arg Val Pro Lys He Leu 515 520 525 He Aεp Lyε Val Lys Asp Asp Ser Asp He Val Lys Lys Glu Phe Ala 530 535 540 Ser He Leu Gly Gin Leu Val Cys Thr Leu His Gly Met Phe Tyr Leu 545 550 555 560 Thr Ser Ser Leu Thr Glu Pro Phe Ser Glu His Gly His Val Asp Leu 565 570 575 Phe Cys Arg Aεn Leu Lyε Ala Thr Ser Gin His Glu Cys Ser Ser Ser 580 585 590 Gin Leu Lys Ala Ser Val Cys Lys Pro Phe Leu Phe Leu Leu Lys Lys 595 600 605 Lys He Pro Ser Pro Val Lys Leu Ala Phe He Asp Asn Leu His His 610 615 620 Leu Cys Lys His Leu Aεp Phe Arg Glu Aεp Glu Thr Aεp Val Lyε Ala 625 630 635 640 Val Leu Gly Thr Leu Leu Asn Leu Met Glu Asp Pro Asp Lys Asp Val 645 650 655 Arg Val Ala Phe Ser Gly Asn He Lys Hiε He Leu Glu Ser Leu Aεp 660 665 670 Ser Glu Asp Gly Phe He Lyε Glu Leu Phe Val Leu Arg Met Lys Glu 675 680 685 Ala Tyr Thr His Ala Gin He Ser Arg Asn Asn Glu Leu Lys Asp Thr 690 695 700 Leu He Leu Thr Thr Gly Asp He Gly Arg Ala Ala Lys Gly Asp Leu 705 710 715 720 Val Pro Phe Ala Leu Leu His Leu Leu His Cys Leu Leu Ser Lys Ser 725 730 735 Ala Ser Val Ser Gly Ala Ala Tyr Thr Glu He Arg Ala Leu Val Ala 740 745 750 Ala Lys Ser Val Lys Leu Gin Ser Phe Phe Ser Gin Tyr Lys Lys Pro 755 760 765 He Cys Gin Phe Leu Val Glu Ser Leu His Ser Ser Gin Met Thr Ala 770 775 780 Leu Pro Asn Thr Pro Cys Gin Asn Ala Asp Val Arg Lyε Gin Asp Val 785 790 795 800 Ala Hiε Gin Arg Glu Met Ala Leu Asn Thr Leu Ser Glu He Ala Asn 805 810 815 Val Phe Asp Phe Pro Asp Leu Asn Arg Phe Leu Thr Arg Thr Leu Gin 820 825 830 Val Leu Leu Pro Aεp Leu Ala Ala Lyε Ala Ser Pro Ala Ala Ser Ala 835 840 845 Leu He Arg Thr Leu Gly Lyε Gin Leu Asn Val Asn Arg Arg Glu He 850 855 860 Leu He Asn Asn Phe Lys Tyr He Phe Ser His Leu Val Cys Ser Cys 865 870 875 880 Ser Lys Asp Glu Leu Glu Arg Ala Leu His Tyr Leu Lys Asn Glu Thr 885 890 895 Glu He Glu Leu Gly Ser Leu Leu Arg Gin Asp Phe Gin Gly Leu Hiε 900 905 910 Asn Glu Leu Leu Leu Arg He Gly Glu His Tyr Gin Gin Val Phe Asn 915 920 925 Gly Leu Ser He Leu Ala Ser Phe Ala Ser Ser Asp Aεp Pro Tyr Gin 930 935 940 Gly Pro Arg Aεp He He Ser Pro Glu Leu Met Ala Asp Tyr Leu Gin 945 950 955 960 Pro Lys Leu Leu Gly He Leu Ala Phe Phe Asn Met Gin Leu Leu Ser 965 970 975 Ser Ser Val Gly He Glu Asp Lys Lys Met Ala Leu Asn Ser Leu Met 980 985 990 Ser Leu Met Lys Leu Met Gly Pro Lys His Val Ser Ser Val Arg Val 995 1000 1005 Lys Met Met Thr Thr Leu Arg Thr Gly Leu Arg Phe Lys Asp Asp Phe 1010 1015 1020 Pro Glu Leu Cys Cys Arg Ala Trp Asp Cys Phe Val Arg Cys Leu Aεp 1025 1030 1035 1040 His Ala Cys Leu Gly Ser Leu Leu Ser His Val He Val Ala Leu Leu 1045 1050 1055 Pro Leu He His He Gin Pro Lys Glu Thr Ala Ala He Phe His Tyr 1060 1065 1070 Leu He He Glu Asn Arg Asp Ala Val Gin Asp Phe Leu His Glu He 1075 1080 1085 Tyr Phe Leu Pro Asp His Pro Glu Leu Lys Lys He Lys Ala Val Leu 1090 1095 1100 Gin Glu Tyr Arg Lys Glu Thr Ser Glu Ser Thr Asp Leu Gin Thr Thr 1105 1110 1115 1120 Leu Gin Leu Ser Met Lys Ala He Gin His Glu Asn Val Asp Val Arg 1125 1130 1135 He His Ala Leu Thr Ser Leu Lys Glu Thr Leu Tyr Lys Asn Gin Glu 1140 1145 1150 Lys Leu He Lys Tyr Ala Thr Asp Ser Glu Thr Val Glu Pro He He 1155 1160 1165 Ser Gin Leu Val Thr Val Leu Leu Lys Gly Cys Gin Asp Ala Aεn Ser 1170 1175 1180 Gin Ala Arg Leu Leu Cys Gly Glu Cyε Leu Gly Glu Leu Gly Ala He 1185 1190 1195 1200 Asp Pro Gly Arg Leu Asp Phe Ser Thr Thr Glu Thr Gin Gly Lys Asp 1205 1210 1215 Phe Thr Phe Val Thr Gly Val Glu Aεp Ser Ser Phe Ala Tyr Gly Leu 1220 1225 1230 Leu Met Glu Leu Thr Arg Ala Tyr Leu Ala Tyr Ala Aεp Asn Ser Arg 1235 1240 1245 Ala Gin Asp Ser Ala Ala Tyr Ala He Gin Glu Leu Leu Ser He Tyr 1250 1255 1260 Asp Cys Arg Glu Met Glu Thr Asn Gly Pro Gly His Gin Leu Trp Arg 1265 1270 1275 1280 Arg Phe Pro Glu His Val Arg Glu He Leu Glu Pro His Leu Asn Thr 1285 1290 1295 Arg Tyr Lys Ser Ser Gin Lys Ser Thr Asp Trp Ser Gly Val Lys Lys 1300 1305 1310 Pro He Tyr Leu Ser Lys Leu Gly Ser Asn Phe Ala Glu Trp Ser Ala 1315 1320 1325 Ser Trp Ala Gly Tyr Leu He Thr Lys Val Arg His Asp Leu Ala Ser 1330 1335 1340 Lys He Phe Thr Cys Cys Ser He Met Met Lys Hiε Asp Phe Lys Val 1345 1350 1355 1360 Thr He Tyr Leu Leu Pro His He Leu Val Tyr Val Leu Leu Gly Cys 1365 1370 1375 Asn Gin Glu Asp Gin Gin Glu Val Tyr Ala Glu He Met Ala Val Leu 1380 1385 1390 Lys His Asp Asp Gin His Thr He Asn Thr Gin Asp He Ala Ser Asp 1395 1400 1405 Leu Cys Gin Leu Ser Thr Gin Thr Val Phe Ser Met Leu Aεp Hiε Leu 1410 1415 1420 Thr Gin Trp Ala Arg His Lys Phe Gin Ala Leu Lys Ala Glu Lys Cys 1425 1430 1435 1440 Pro His Ser Lys Ser Asn Arg Aεn Lyε Val Aεp Ser Met Val Ser Thr 1445 1450 1455 Val Aεp Tyr Glu Asp Tyr Gin Ser Val Thr Arg Phe Leu Aεp Leu He 1460 1465 1470 Pro Gin Aεp Thr Leu Ala Val Ala Ser Phe Arg Ser Lyε Ala Tyr Thr 1475 1480 1485 Arg Ala Val Met His Phe Glu Ser Phe He Thr Glu Lys Lys Gin Asn 1490 1495 1500 He Gin Glu His Leu Gly Phe Leu Gin Lys Leu Tyr Ala Ala Met His 1505 1510 1515 1520 Glu Pro Asp Gly Val Ala Gly Val Ser Ala He Arg Lys Ala Glu Pro 1525 1530 1535 Ser Leu Lys Glu Gin He Leu Glu His Glu Ser Leu Gly Leu Leu Arg 1540 1545 1550 Aεp Ala Thr Ala Cys Tyr Asp Arg Ala He Gin Leu Glu Pro Asp Gin 1555 1560 1565 He He His Tyr His Gly Val Val Lys Ser Met Leu Gly Leu Gly Gin 1570 1575 1580 Leu Ser Thr Val He Thr Gin Val Asn Gly Val Hiε Ala Asn Arg Ser 1585 1590 1595 1600 Glu Trp Thr Asp Glu Leu Asn Thr Tyr Arg Val Glu Ala Ala Trp Lyε 1605 1610 1615 Leu Ser Gin Trp Aεp Leu Val Glu Asn Tyr Leu Ala Ala Aεp Gly Lys 1620 1625 1630 Ser Thr Thr Trp Ser Val Arg Leu Gly Gin Leu Leu Leu Ser Ala Lys 1635 1640 1645 Lys Arg Asp He Thr Ala Phe Tyr Asp Ser Leu Lys Leu Val Arg Ala 1650 1655 1660 Glu Gin He Val Pro Leu Ser Ala Ala Ser Phe Glu Arg Gly Ser Tyr 1665 1670 1675 1680 Gin Arg Gly Tyr Glu Tyr He Val Arg Leu His Met Leu Cys Glu Leu 1685 1690 1695 Glu His Ser He Lyε Pro Leu Phe Gin His Ser Pro Gly Asp Ser Ser 1700 1705 1710 Gin Glu Asp Ser Leu Asn Trp Val Ala Arg Leu Glu Met Thr Gin Asn 1715 1720 1725 Ser Tyr Arg Ala Lys Glu Pro He Leu Ala Leu Arg Arg Ala Leu Leu 1730 1735 1740 Ser Leu Asn Lys Arg Pro Aεp Tyr Aεn Glu Met Val Gly Glu Cys Trp 1745 1750 1755 1760 Leu Gin Ser Ala Arg Val Ala Arg Lys Ala Gly His His Gin Thr Ala 1765 1770 1775 Tyr Asn Ala Leu Leu Asn Ala Gly Glu Ser Arg Leu Ala Glu Leu Tyr 1780 1785 1790 Val Glu Arg Ala Lys Trp Leu Trp Ser Lys Gly Asp Val His Gin Ala 1795 1800 1805 Leu He Val Leu Gin Lys Gly Val Glu Leu Cys Phe Pro Glu Asn Glu 1810 1815 1820 Thr Pro Pro Glu Gly Lys Asn Met Leu He His Gly Arg Ala Met Leu 1825 1830 1835 1840 Leu Val Gly Arg Phe Met Glu Glu Thr Ala Asn Phe Glu Ser Asn Ala 1845 1850 1855 He Met Lys Lys Tyr Lys Asp Val Thr Ala Cys Leu Pro Glu Trp Glu 1860 1865 1870 Asp Gly His Phe Tyr Leu Ala Lys Tyr Tyr Asp Lys Leu Met Pro Met 1875 1880 1885 Val Thr Asp Aεn Lyε Met Glu Lys Gin Gly Asp Leu He Arg Tyr He 1890 1895 1900 Val Leu His Phe Gly Arg Ser Leu Gin Tyr Gly Asn Gin Phe He Tyr 1905 1910 1915 1920 Gin Ser Met Pro Arg Met Leu Thr Leu Trp Leu Aεp Tyr Gly Thr Lys 1925 1930 1935 Ala Tyr Glu Trp Glu Lys Ala Gly Arg Ser Asp Arg Val Gin Met Arg 1940 1945 1950 Asn Asp Leu Gly Lys He Asn Lys Val He Thr Glu His Thr Asn Tyr 1955 1960 1965 Leu Ala Pro Tyr Gin Phe Leu Thr Ala Phe Ser Gin Leu He Ser Arg 1970 1975 1980 He Cys His Ser His Asp Glu Val Phe Val Val Leu Met Glu He He 1985 1990 1995 2000 Ala Lys Val Phe Leu Ala Tyr Pro Gin Gin Ala Met Trp Met Met Thr 2005 2010 2015 Ala Val Ser Lyε Ser Ser Tyr Pro Met Arg Val Asn Arg Cys Lys Glu 2020 2025 2030 He Leu Asn Lys Ala He His Met Lys Lys Ser Leu Glu Lys Phe Val 2035 2040 2045 Gly Asp Ala Thr Arg Leu Thr Aεp Lyε Leu Leu Glu Leu Cys Asn Lys 2050 2055 2060 Pro Val Glu He Leu Ala Ser Leu Gin Lys Pro Lys Lys He Ser Leu 2065 2070 2075 2080 Lys Gly Ser Asp Gly Lyε Phe Tyr He Met Met Cyε Lys Pro Lys Asp 2085 2090 2095 Asp Leu Arg Lys Asp Cys Arg Leu Met Glu Phe Asn Ser Leu He Asn 2100 2105 2110 Lys Cys Leu Arg Lyε Asp Ala Glu Ser Arg Arg Arg Glu Leu His He 2115 2120 2125 Arg Thr Tyr Ala Val He Pro Leu Asn Asp Glu Cys Gly He He Glu 2130 2135 2140 Trp Val Asn Asn Thr Ala Gly Leu Arg Pro He Leu Thr Lys Leu Tyr 2145 2150 2155 2160 Lys Glu Lys Gly Val Tyr Met Thr Gly Lys Glu Leu Arg Gin Cys Met 2165 2170 2175 Leu Pro Lys Ser Ala Ala Leu Ser Glu Lys Leu Lys Val Phe Arg Glu 2180 2185 2190 Phe Leu Leu Pro Arg His Pro Pro He Phe His Glu Trp Phe Leu Arg 2195 2200 2205 Thr Phe Pro Asp Pro Thr Ser Trp Tyr Ser Ser Arg Ser Ala Tyr Cys 2210 2215 2220 Arg Ser Thr Ala Val Met Ser Met Val Gly Tyr He Leu Gly Leu Gly 2225 2230 2235 2240 Asp Arg His Gly Glu Asn He Leu Phe Asp Ser Leu Thr Gly Glu Cys 2245 2250 2255 Val His Val Asp Phe Asn Cys Leu Phe Asn Lys Gly Glu Thr Phe Glu 2260 2265 2270 Val Pro Glu He Val Pro Phe Arg Leu Thr His Asn Met Val Asn Gly 2275 2280 2285 Met Gly Pro Met Gly Thr Glu Gly Leu Phe Arg Arg Ala Cys Glu Val 2290 2295 2300 Thr Met Arg Leu Met Arg Asp Gin Arg Glu Pro Leu Met Ser Val Leu 2305 2310 2315 2320 Lys Thr Phe Leu Hiε Aεp Pro Leu Val Glu Trp Ser Lyε Pro Val Lys 2325 2330 2335 Gly His Ser Lys Ala Pro Leu Asn Glu Thr Gly Glu Val Val Asn Glu 2340 2345 2350 Lys Ala Lys Thr His Val Leu Asp He Glu Gin Arg Leu Gin Gly Val 2355 2360 2365 He Lys Thr Arg Asn Arg Val Thr Gly Leu Pro Leu Ser He Glu Gly 2370 2375 2380 His Val Hiε Tyr Leu He Gin Glu Ala Thr Aεp Glu Asn Leu Leu Cys 2385 2390 2395 2400 Gin Met Tyr Leu Gly Trp Thr Pro Tyr Met 2405 2410 (2) INFORMATION FOR SEQ ID NO: 32: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 7502 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (11) MOLECULE TYPE: cDNA (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 1..7440 <xι) SEQUENCE DESCRIPTION: SEQ ID NO:32: ATG GGT CAT GCT GTG GAA TGG CCA GTG GTC ATG AGC CGA TTT TTA AGT 48 Met Gly His Ala Val Glu Trp Pro Val Val Met Ser Arg Phe Leu Ser 1 5 10 15 CAA TTA GAT GAA CAC ATG GGA TAT TTA CAA TCA GCT CCT TTG CAG TTG 96 Gin Leu Asp Glu His Met Gly Tyr Leu Gin Ser Ala Pro Leu Gin Leu 20 25 30 ATG AGT ATG CAA AAT TTA GAA TTT ATT GAA GTC ACT TTA TTA ATG GTT 144 Met Ser Met Gin Aεn Leu Glu Phe He Glu Val Thr Leu Leu Met Val 35 40 45 CTT ACT CGT ATT ATT GCA ATT GTG TTT TTT AGA AGG CAA GAA CTC TTA 192 Leu Thr Arg He He Ala He Val Phe Phe Arg Arg Gin Glu Leu Leu 50 55 60 CTT TGG CAG ATA GGT TGT GTT CTG CTA GAG TAT GGT AGT CCA AAA ATT 240 Leu Trp Gin He Gly Cys Val Leu Leu Glu Tyr Gly Ser Pro Lys He 65 70 75 80 AAA TCC CTA GCA ATT AGC TTT TTA ACA GAA CTT TTT CAG CTT GGA GGA 288 Lys Ser Leu Ala He Ser Phe Leu Thr Glu Leu Phe Gin Leu Gly Gly 85 90 95 CTA CCA GCA CAA CCA GCT AGC ACT TTT TTC AGC TCA TTT TTG GAA TTA 336 Leu Pro Ala Gin Pro Ala Ser Thr Phe Phe Ser Ser Phe Leu Glu Leu 100 105 110 TTA AAA CAC CTT GTA GAA ATG GAT ACT GAC CAA TTG AAA CTC TAT GAA 384 Leu Lys Hiε Leu Val Glu Met Aεp Thr Asp Gin Leu Lyε Leu Tyr Glu 115 120 125 GAG CCA TTA TCA AAG CTG ATA AAG ACA CTA TTT CCC TTT GAA GCA GAA 432 Glu Pro Leu Ser Lys Leu He Lys Thr Leu Phe Pro Phe Glu Ala Glu 130 135 140 GCT TAT AGA AAT ATT GAA CCT GTC TAT TTA AAT ATG CTG CTG GAA AAA 480 Ala Tyr Arg Asn He Glu Pro Val Tyr Leu Asn Met Leu Leu Glu Lys 145 150 155 160 CTC TGT GTC ATG TTT GAA GAC GGT GTG CTC ATG CGG CTT AAG TCT GAT 528 Leu Cys Val Met Phe Glu Aεp Gly Val Leu Met Arg Leu Lys Ser Asp 165 170 175 TTG CTA AAA GCA GCT TTG TGC CAT TTA CTG CAG TAT TTC CTT AAA TTT 576 Leu Leu Lys Ala Ala Leu Cys His Leu Leu Gin Tyr Phe Leu Lys Phe 180 185 190 GTG CCA GCT GGG TAT GAA TCT GCT TTA CAA GTC AGG AAG GTC TAT GTG 624 Val Pro Ala Gly Tyr Glu Ser Ala Leu Gin Val Arg Lys Val Tyr Val 195 200 205 AGA AAT ATT TGT AAA GCT CTT TTG GAT GTG CTT GGA ATT GAG GTA GAT 672 Arg Asn He Cys Lyε Ala Leu Leu Aεp Val Leu Gly He Glu Val Aεp 210 215 220 GCA GAG TAC TTG TTG GGC CCA CTT TAT GCA GCT TTG AAA ATG GAA AGT 720 Ala Glu Tyr Leu Leu Gly Pro Leu Tyr Ala Ala Leu Lys Met Glu Ser 225 230 235 240 ATG GAA ATC ATT GAG GAG ATT CAA TGC CAA ACT CAA CAG GAA AAC CTC 768 Met Glu He He Glu Glu He Gin Cys Gin Thr Gin Gin Glu Aεn Leu 245 250 255 AGC AGT AAT AGT GAT GGA ATA TCA CCC AAA AGG CGT CGT CTC AGC TCG 816 Ser Ser Asn Ser Asp Gly He Ser Pro Lys Arg Arg Arg Leu Ser Ser 260 265 270 TCT CTA AAC CCT TCT AAA AGA GCA CCA AAA CAG ACT GAG GAA ATT AAA 864 Ser Leu Aεn Pro Ser Lys Arg Ala Pro Lys Gin Thr Glu Glu He Lys 275 280 285 CAT GTG GAC ATG AAC CAA AAG AGC ATA TTA TGG AGT GCA CTG AAA CAG 912 His Val Aεp Met Asn Gin Lys Ser He Leu Trp Ser Ala Leu Lys Gin 290 295 300 AAA GCT GAA TCC CTT CAG ATT TCC CTT GAA TAC AGT GGC CTA AAG AAT 960 Lys Ala Glu Ser Leu Gin He Ser Leu Glu Tyr Ser Gly Leu Lyε Aεn 305 310 315 320 CCT GTT ATT GAG ATG TTA GAA GGA ATT GCT GTT GTC TTA CAA CTG ACT 1008 Pro Val He Glu Met Leu Glu Gly He Ala Val Val Leu Gin Leu Thr 325 330 335 GCT CTG TGT ACT GTT CAT TGT TCT CAT CAA AAC ATG AAC TGC CGT ACT 1056 Ala Leu Cys Thr Val Hiε Cyε Ser Hiε Gin Asn Met Asn Cys Arg Thr 340 345 350 TTC AAG GAC TGT CAA CAT AAA TCC AAG AAG AAA CCT TCT GTA GTG ATA 1104 Phe Lys Asp Cys Gin Hiε Lyε Ser Lyε Lyε Lyε Pro Ser Val Val He 355 360 365 ACT TGG ATG TCA TTG GAT TTT TAC ACA AAA GTG CTT AAG AGC TGT AGA 1152 Thr Trp Met Ser Leu Aεp Phe Tyr Thr Lyε Val Leu Lyε Ser Cyε Arg 370 375 380 AGT TTG TTA GAA TCT GTT CAG AAA CTG GAC CTG GAG GCA ACC ATT GAT 1200 Ser Leu Leu Glu Ser Val Gin Lyε Leu Asp Leu Glu Ala Thr He Asp 385 390 395 400 AAG GTG GTG AAA ATT TAT GAT GCT TTG ATT TAT ATG CAA GTA AAC AGT 1248 Lyε Val Val Lys He Tyr Aεp Ala Leu He Tyr Met Gin Val Aεn Ser 405 410 415 TCA TTT GAA GAT CAT ATC CTG GAA GAT TTA TGT GGA ATG CTC TCA CTT 1296 Ser Phe Glu Aεp Hiε He Leu Glu Asp Leu Cys Gly Met Leu Ser Leu 420 425 430 CCA TGG ATT TAT TCC CAT TCT GAT GAT GGC TGT TTA AAG TTG ACC ACA 1344 Pro Trp He Tyr Ser His Ser Asp Asp Gly Cys Leu Lys Leu Thr Thr 435 440 445 TTT GCC GCT AAT CTT CTA ACA TTA AGC TGT AGG ATT TCA GAT AGC TAT 1392 Phe Ala Ala Asn Leu Leu Thr Leu Ser Cys Arg He Ser Asp Ser Tyr 450 455 460 TCA CCA CAG GCA CAA TCA CGA TGT GTG TTT CTT CTG ACT CTG TTT CCA 1440 Ser Pro Gin Ala Gin Ser Arg Cys Val Phe Leu Leu Thr Leu Phe Pro 465 470 475 480 AGA AGA ATA TTC CTT GAG TGG AGA ACA GCA GTT TAC AAC TGG GCC CTG 1488 Arg Arg He Phe Leu Glu Trp Arg Thr Ala Val Tyr Aεn Trp Ala Leu 485 490 495 CAG AGC TCC CAT GAA GTA ATC CGG GCT AGT TGT GTT AGT GGA TTT TTT 1536 Gin Ser Ser His Glu Val He Arg Ala Ser Cyε Val Ser Gly Phe Phe 500 505 510 ATC TTA TTG CAG CAG CAG AAT TCT TGT AAC AGA GTT CCC AAG ATT CTT 1584 He Leu Leu Gin Gin Gin Aεn Ser Cyε Aεn Arg Val Pro Lys He Leu 515 520 525 ATA GAT AAA GTC AAA GAT GAT TCT GAC ATT GTC AAG AAA GAA TTT GCT 1632 He Asp Lys Val Lys Asp Asp Ser Asp He Val Lys Lys Glu Phe Ala 530 535 540 TCT ATA CTT GGT CAA CTT GTC TGT ACT CTT CAC GGC ATG TTT TAT CTG 1680 Ser He Leu Gly Gin Leu Val Cys Thr Leu His Gly Met Phe Tyr Leu 545 550 555 560 ACA AGT TCT TTA ACA GAA CCT TTC TCT GAA CAC GGA CAT GTG GAC CTC 1728 Thr Ser Ser Leu Thr Glu Pro Phe Ser Glu His Gly His Val Asp Leu 565 570 575 TTC TGT AGG AAC TTG AAA GCC ACT TCT CAA CAT GAA TGT TCA TCT TCT 1776 Phe Cyε Arg Aεn Leu Lyε Ala Thr Ser Gin His Glu Cyε Ser Ser Ser 580 585 590 CAA CTA AAA GCT TCT GTC TGC AAG CCA TTC CTT TTC CTA CTG AAA AAA 1824 Gin Leu Lyε Ala Ser Val Cyε Lys Pro Phe Leu Phe Leu Leu Lys Lyε 595 600 605 AAA ATA CCT AGT CCA GTA AAA CTT GCT TTC ATA GAT AAT CTA CAT CAT 1872 Lys He Pro Ser Pro Val Lyε Leu Ala Phe He Asp Asn Leu Hiε His 610 615 620 CTT TGT AAG CAT CTT GAT TTT AGA GAA GAT GAA ACA GAT GTA AAA GCA 1920 Leu Cys Lys His Leu Asp Phe Arg Glu Asp Glu Thr Asp Val Lyε Ala 625 630 635 640 GTT CTT GGA ACT TTA TTA AAT TTA ATG GAA GAT CCA GAC AAA GAT GTT 1968 Val Leu Gly Thr Leu Leu Asn Leu Met Glu Aεp Pro Aεp Lyε Aεp Val 645 650 655 AGA GTG GCT TTT AGT GGA AAT ATC AAG CAC ATA TTG GAA TCC TTG GAC 2016 Arg Val Ala Phe Ser Gly Aεn He Lyε His He Leu Glu Ser Leu Asp 660 665 670 TCT GAA GAT GGA TTT ATA AAG GAG CTT TTT GTC TTA AGA ATG AAG GAA 2064 Ser Glu Aεp Gly Phe He Lys Glu Leu Phe Val Leu Arg Met Lys Glu 675 680 685 GCA TAT ACA CAT GCC CAA ATA TCA AGA AAT AAT GAG CTG AAG GAT ACC 2112 Ala Tyr Thr His Ala Gin He Ser Arg Asn Asn Glu Leu Lys Asp Thr 690 695 700 TTG ATT CTT ACA ACA GGG GAT ATT GGA AGG GCC GCA AAA GGA GAT TTG 2160 Leu He Leu Thr Thr Gly Asp He Gly Arg Ala Ala Lyε Gly Asp Leu 705 710 715 720 GTA CCA TTT GCA CTC TTA CAC TTA TTG CAT TGT TTG TTA TCC AAG TCA 2208 Val Pro Phe Ala Leu Leu His Leu Leu His Cys Leu Leu Ser Lys Ser 725 730 735 GCA TCT GTC TCT GGA GCA GCA TAC ACA GAA ATT AGA GCT CTG GTT GCA 2256 Ala Ser Val Ser Gly Ala Ala Tyr Thr Glu He Arg Ala Leu Val Ala 740 745 750 GCT AAA AGT GTT AAA CTG CAA AGT TTT TTC AGC CAG TAT AAG AAA CCC 2304 Ala Lys Ser Val Lys Leu Gin Ser Phe Phe Ser Gin Tyr Lys Lys Pro 755 760 765 ATC TGT CAG TTT TTG GTA GAA TCC CTT CAC TCT AGT CAG ATG ACA GCA 2352 He Cyε Gin Phe Leu Val Glu Ser Leu His Ser Ser Gin Met Thr Ala 770 775 780 CTT CCG AAT ACT CCA TGC CAG AAT GCT GAC GTG CGA AAA CAA GAT GTG 2400 Leu Pro Asn Thr Pro Cys Gin Asn Ala Asp Val Arg Lyε Gin Aεp Val 785 790 795 800 GCT CAC CAG AGA GAA ATG GCT TTA AAT ACG TTG TCT GAA ATT GCC AAC 2448 Ala His Gin Arg Glu Met Ala Leu Asn Thr Leu Ser Glu He Ala Asn 805 810 815 GTT TTC GAC TTT CCT GAT CTT AAT CGT TTT CTT ACT AGG ACA TTA CAA 2496 Val Phe Asp Phe Pro Asp Leu Asn Arg Phe Leu Thr Arg Thr Leu Gin 820 825 830 GTT CTA CTA CCT GAT CTT GCT GCC AAA GCA AGC CCT GCA GCT TCT GCT 2544 Val Leu Leu Pro Asp Leu Ala Ala Lys Ala Ser Pro Ala Ala Ser Ala 835 840 845 CTC ATT CGA ACT TTA GGA AAA CAA TTA AAT GTC AAT CGT AGA GAG ATT 2592 Leu He Arg Thr Leu Gly Lys Gin Leu Asn Val Asn Arg Arg Glu He 850 855 860 TTA ATA AAC AAC TTC AAA TAT ATT TTT TCT CAT TTG GTC TGT TCT TGT 2640 Leu He Asn Asn Phe Lys Tyr He Phe Ser His Leu Val Cyε Ser Cyε 865 870 875 880 TCC AAA GAT GAA TTA GAA CGT GCC CTT CAT TAT CTG AAG AAT GAA ACA 2688 Ser Lys Asp Glu Leu Glu Arg Ala Leu His Tyr Leu Lyε Aεn Glu Thr 885 890 895 GAA ATT GAA CTG GGG AGC CTG TTG AGA CAA GAT TTC CAA GGA TTG CAT 2736 Glu He Glu Leu Gly Ser Leu Leu Arg Gin Aεp Phe Gin Gly Leu His 900 905 910 AAT GAA TTA TTG CTG CGT ATT GGA GAA CAC TAT CAA CAG GTT TTT AAT 2784 Asn Glu Leu Leu Leu Arg He Gly Glu His Tyr Gin Gin Val Phe Asn 915 920 925 GGT TTG TCA ATA CTT GCC TCA TTT GCA TCC AGT GAT GAT CCA TAT CAG 2832 Gly Leu Ser He Leu Ala Ser Phe Ala Ser Ser Asp Asp Pro Tyr Gin 930 935 940 GGC CCG AGA GAT ATC ATA TCA CCT GAA CTG ATG GCT GAT TAT TTA CAA 2880 Gly Pro Arg Aεp He He Ser Pro Glu Leu Met Ala Aεp Tyr Leu Gin 945 950 955 960 CCC AAA TTG TTG GGC ATT TTG GCT TTT TTT AAC ATG CAG TTA CTG AGC 2928 Pro Lys Leu Leu Gly He Leu Ala Phe Phe Asn Met Gin Leu Leu Ser 965 970 975 TCT AGT GTT GGC ATT GAA GAT AAG AAA ATG GCC TTG AAC AGT TTG ATG 2976 Ser Ser Val Gly He Glu Asp Lys Lyε Met Ala Leu Aεn Ser Leu Met 980 985 990 TCT TTG ATG AAG TTA ATG GGA CCC AAA CAT GTC AGT TCT GTG AGG GTG 3024 Ser Leu Met Lys Leu Met Gly Pro Lys His Val Ser Ser Val Arg Val 995 1000 1005 AAG ATG ATG ACC ACA CTG AGA ACT GGC CTT CGA TTC AAG GAT GAT TTT 3072 Lys Met Met Thr Thr Leu Arg Thr Gly Leu Arg Phe Lys Asp Asp Phe 1010 1015 1020 CCT GAA TTG TGT TGC AGA GCT TGG GAC TGC TTT GTT CGC TGC CTG GAT 3120 Pro Glu Leu Cys Cys Arg Ala Trp Asp Cys Phe Val Arg Cys Leu Asp 1025 1030 1035 1040 CAT GCT TGT CTG GGC TCC CTT CTC AGT CAT GTA ATA GTA GCT TTG TTA 3168 His Ala Cys Leu Gly Ser Leu Leu Ser His Val He Val Ala Leu Leu 1045 1050 1055 CCT CTT ATA CAC ATC CAG CCT AAA GAA ACT GCA GCT ATC TTC CAC TAC 3216 Pro Leu He His He Gin Pro Lys Glu Thr Ala Ala He Phe Hiε Tyr 1060 1065 1070 CTC ATA ATT GAA AAC AGG GAT GCT GTG CAA GAT TTT CTT CAT GAA ATA 3264 Leu He He Glu Asn Arg Asp Ala Val Gin Asp Phe Leu His Glu He 1075 1080 1085 TAT TTT TTA CCT GAT CAT CCA GAA TTA AAA AAG ATA AAA GCC GTT CTC 3312 Tyr Phe Leu Pro Asp His Pro Glu Leu Lys Lys He Lys Ala Val Leu 1090 1095 1100 CAG GAA TAC AGA AAG GAG ACC TCT GAG AGC ACT GAT CTT CAG ACA ACT 3360 Gin Glu Tyr Arg Lys Glu Thr Ser Glu Ser Thr Asp Leu Gin Thr Thr 1105 1110 1115 1120 CTT CAG CTC TCT ATG AAG GCC ATT CAA CAT GAA AAT GTC GAT GTT CGT 3408 Leu Gin Leu Ser Met Lys Ala He Gin His Glu Aεn Val Asp Val Arg 1125 1130 1135 ATT CAT GCT CTT ACA AGC TTG AAG GAA ACC TTG TAT AAA AAT CAG GAA 3456 He His Ala Leu Thr Ser Leu Lys Glu Thr Leu Tyr Lys Asn Gin Glu 1140 1145 1150 AAA CTG ATA AAG TAT GCA ACA GAC AGT GAA ACA GTA GAA CCT ATT ATC 3504 Lys Leu He Lys Tyr Ala Thr Asp Ser Glu Thr Val Glu Pro He He 1155 1160 1165 TCA CAG TTG GTG ACA GTG CTT TTG AAA GGT TGC CAA GAT GCA AAC TCT 3552 Ser Gin Leu Val Thr Val Leu Leu Lys Gly Cys Gin Asp Ala Asn Ser 1170 1175 1180 CAA GCT CGG TTG CTC TGT GGG GAA TGT TTA GGG GAA TTG GGG GCG ATA 3600 Gin Ala Arg Leu Leu Cys Gly Glu Cyε Leu Gly Glu Leu Gly Ala He 1185 1190 1195 1200 GAT CCA GGT CGA TTA GAT TTC TCA ACA ACT GAA ACT CAA GGA AAA GAT 3648 Aεp Pro Gly Arg Leu Aεp Phe Ser Thr Thr Glu Thr Gin Gly Lyε Aεp 1205 1210 1215 TTT ACA TTT GTG ACT GGA GTA GAA GAT TCA AGC TTT GCC TAT GGA TTA 3696 Phe Thr Phe Val Thr Gly Val Glu Asp Ser Ser Phe Ala Tyr Gly Leu 1220 1225 1230 TTG ATG GAG CTA ACA AGA GCT TAC CTT GCG TAT GCT GAT AAT AGC CGA 3744 Leu Met Glu Leu Thr Arg Ala Tyr Leu Ala Tyr Ala Asp Asn Ser Arg 1235 1240 1245 GCT CAA GAT TCA GCT GCC TAT GCC ATT CAG GAG TTG CTT TCT ATT TAT 3792 Ala Gin Asp Ser Ala Ala Tyr Ala He Gin Glu Leu Leu Ser He Tyr 1250 1255 1260 GAC TGT AGA GAG ATG GAG ACC AAC GGC CCA GGT CAC CAA TTG TGG AGG 3840 Asp Cys Arg Glu Met Glu Thr Asn Gly Pro Gly His Gin Leu Trp Arg 1265 1270 1275 1280 AGA TTT CCT GAG CAT GTT CGG GAA ATA CTA GAA CCT CAT CTA AAT ACC 3888 Arg Phe Pro Glu Hiε Val Arg Glu He Leu Glu Pro His Leu Asn Thr 1285 1290 1295 AGA TAC AAG AGT TCT CAG AAG TCA ACC GAT TGG TCT GGA GTA AAG AAG 3936 Arg Tyr Lys Ser Ser Gin Lys Ser Thr Asp Trp Ser Gly Val Lys Lys 1300 1305 1310 CCA ATT TAC TTA AGT AAA TTG GGT AGT AAC TTT GCA GAA TGG TCA GCA 3984 Pro He Tyr Leu Ser Lyε Leu Gly Ser Aεn Phe Ala Glu Trp Ser Ala 1315 1320 1325 TCT TGG GCA GGT TAT CTT ATT ACA AAG GTT CGA CAT GAT CTT GCC AGT 4032 Ser Trp Ala Gly Tyr Leu He Thr Lys Val Arg His Asp Leu Ala Ser 1330 1335 1340 AAA ATT TTC ACC TGC TGT AGC ATT ATG ATG AAG CAT GAT TTC AAA GTG 4080 Lyε He Phe Thr Cys Cys Ser He Met Met Lyε Hiε Aεp Phe Lyε Val 1345 1350 1355 1360 ACC ATC TAT CTT CTT CCA CAT ATT CTG GTG TAT GTC TTA CTG GGT TGT 4128 Thr He Tyr Leu Leu Pro Hiε He Leu Val Tyr Val Leu Leu Gly Cyε 1365 1370 1375 AAT CAA GAA GAT CAG CAG GAG GTT TAT GCA GAA ATT ATG GCA GTT CTA 4176 Aεn Gin Glu Asp Gin Gin Glu Val Tyr Ala Glu He Met Ala Val Leu 1380 1385 1390 AAG CAT GAC GAT CAG CAT ACC ATA AAT ACC CAA GAC ATT GCA TCT GAT 4224 Lyε Hiε Asp Asp Gin Hiε Thr He Aεn Thr Gin Aεp He Ala Ser Aεp 1395 1400 1405 CTG TGT CAA CTC AGT ACA CAG ACT GTG TTC TCC ATG CTT GAC CAT CTC 4272 Leu Cys Gin Leu Ser Thr Gin Thr Val Phe Ser Met Leu Asp His Leu 1410 1415 1420 ACA CAG TGG GCA AGG CAC AAA TTT CAG GCA CTG AAA GCT GAG AAA TGT 4320 Thr Gin Trp Ala Arg Hiε Lyε Phe Gin Ala Leu Lyε Ala Glu Lyε Cyε 1425 1430 1435 1440 CCA CAC AGC AAA TCA AAC AGA AAT AAG GTA GAC TCA ATG GTA TCT ACT 4368 Pro Hiε Ser Lyε Ser Asn Arg Asn Lys Val Asp Ser Met Val Ser Thr 1445 1450 1455 GTG GAT TAT GAA GAC TAT CAG AGT GTA ACC CGT TTT CTA GAC CTC ATA 4416 Val Aεp Tyr Glu Aεp Tyr Gin Ser Val Thr Arg Phe Leu Aεp Leu He 1460 1465 1470 CCC CAG GAT ACT CTG GCA GTA GCT TCC TTT CGC TCC AAA GCA TAC ACA 4464 Pro Gin Aεp Thr Leu Ala Val Ala Ser Phe Arg Ser Lys Ala Tyr Thr 1475 1480 1485 CGA GCT GTA ATG CAC TTT GAA TCA TTT ATT ACA GAA AAG AAG CAA AAT 4512 Arg Ala Val Met His Phe Glu Ser Phe He Thr Glu Lys Lys Gin Asn 1490 1495 1500 ATT CAG GAA CAT CTT GGA TTT TTA CAG AAA TTG TAT GCT GCT ATG CAT 4560 He Gin Glu His Leu Gly Phe Leu Gin Lyε Leu Tyr Ala Ala Met Hiε 1505 1510 1515 1520 GAA CCT GAT GGA GTG GCC GGA GTC AGT GCA ATT AGA AAG GCA GAA CCA 4608 Glu Pro Asp Gly Val Ala Gly Val Ser Ala He Arg Lyε Ala Glu Pro 1525 1530 1535 TCT CTA AAA GAA CAG ATC CTT GAA CAT GAA AGC CTT GGC TTG CTG AGG 4656 Ser Leu Lyε Glu Gin He Leu Glu Hiε Glu Ser Leu Gly Leu Leu Arg 1540 1545 1550 GAT GCC ACT GCT TGT TAT GAC AGG GCT ATT CAG CTA GAA CCA GAC CAG 4704 Aεp Ala Thr Ala Cys Tyr Aεp Arg Ala He Gin Leu Glu Pro Asp Gin 1555 1560 1565 ATC ATT CAT TAC CAT GGT GTA GTA AAG TCC ATG TTA GGT CTT GGT CAG 4752 He He His Tyr His Gly Val Val Lys Ser Met Leu Gly Leu Gly Gin 1570 1575 1580 CTG TCT ACT GTT ATC ACT CAG GTG AAT GGA GTG CAT GCT AAC AGG TCC 4800 Leu Ser Thr Val He Thr Gin Val Asn Gly Val His Ala Asn Arg Ser 1585 1590 1595 1600 GAG TGG ACA GAT GAA TTA AAC ACG TAC AGA GTG GAA GCA GCT TGG AAA 4848 Glu Trp Thr Asp Glu Leu Aεn Thr Tyr Arg Val Glu Ala Ala Trp Lys 1605 1610 1615 TTG TCA CAG TGG GAT TTG GTG GAA AAC TAT TTG GCA GCA GAT GGA AAA 4896 Leu Ser Gin Trp Asp Leu Val Glu Asn Tyr Leu Ala Ala Asp Gly Lys 1620 1625 1630 TCT ACA ACA TGG AGT GTC AGA CTG GGA CAG CTA TTA TTA TCA GCC AAA 4944 Ser Thr Thr Trp Ser Val Arg Leu Gly Gin Leu Leu Leu Ser Ala Lys 1635 1640 1645 AAA AGA GAT ATC ACA GCT TTT TAT GAC TCA CTG AAA CTA GTG AGA GCA 4992 Lys Arg Asp He Thr Ala Phe Tyr Asp Ser Leu Lyε Leu Val Arg Ala 1650 1655 1660 GAA CAA ATT GTA CCT CTT TCA GCT GCA AGC TTT GAA AGA GGC TCC TAC 5040 Glu Gin He Val Pro Leu Ser Ala Ala Ser Phe Glu Arg Gly Ser Tyr 1665 1670 1675 1680 CAA CGA GGA TAT GAA TAT ATT GTG AGA TTG CAC ATG TTA TGT GAG TTG 5088 Gin Arg Gly Tyr Glu Tyr He Val Arg Leu Hiε Met Leu Cyε Glu Leu 1685 1690 1695 GAG CAT AGC ATC AAA CCA CTT TTC CAG CAT TCT CCA GGT GAC AGT TCT 5136 Glu Hiε Ser He Lys Pro Leu Phe Gin His Ser Pro Gly Aεp Ser Ser 1700 1705 1710 CAA GAA GAT TCT CTA AAC TGG GTA GCT CGA CTA GAA ATG ACC CAG AAT 5184 Gin Glu Asp Ser Leu Asn Trp Val Ala Arg Leu Glu Met Thr Gin Aεn 1715 1720 1725 TCC TAC AGA GCC AAG GAG CCT ATC CTG GCT CTC CGG AGG GCT TTA CTA 5232 Ser Tyr Arg Ala Lyε Glu Pro He Leu Ala Leu Arg Arg Ala Leu Leu 1730 1735 1740 AGC CTC AAC AAA AGA CCA GAT TAC AAT GAA ATG GTT GGA GAA TGC TGG 5280 Ser Leu Asn Lyε Arg Pro Asp Tyr Asn Glu Met Val Gly Glu Cyε Trp 1745 1750 1755 1760 CTG CAG AGT GCC AGG GTA GCT AGA AAG GCT GGT CAC CAC CAG ACA GCC 5328 Leu Gin Ser Ala Arg Val Ala Arg Lyε Ala Gly Hiε Hiε Gin Thr Ala 1765 1770 1775 TAC AAT GCT CTC CTT AAT GCA GGG GAA TCA CGA CTC GCT GAA CTG TAC 5376 Tyr Aεn Ala Leu Leu Asn Ala Gly Glu Ser Arg Leu Ala Glu Leu Tyr 1780 1785 1790 GTG GAA AGG GCA AAG TGG CTC TGG TCC AAG GGT GAT GTT CAC CAG GCA 5424 Val Glu Arg Ala Lyε Trp Leu Trp Ser Lyε Gly Asp Val His Gin Ala 1795 1800 1805 CTA ATT GTT CTT CAA AAA GGT GTT GAA TTA TGT TTT CCT GAA AAT GAA 5472 Leu He Val Leu Gin Lys Gly Val Glu Leu Cys Phe Pro Glu Aεn Glu 1810 1815 1820 ACC CCA CCT GAG GGT AAG AAC ATG TTA ATC CAT GGT CGA GCT ATG CTA 5520 Thr Pro Pro Glu Gly Lyε Asn Met Leu He His Gly Arg Ala Met Leu 1825 1830 1835 1840 CTA GTG GGC CGA TTT ATG GAA GAA ACA GCT AAC TTT GAA AGC AAT GCA 5568 Leu Val Gly Arg Phe Met Glu Glu Thr Ala Aεn Phe Glu Ser Aεn Ala 1845 1850 1855 ATT ATG AAA AAA TAT AAG GAT GTG ACC GCG TGC CTG CCA GAA TGG GAG 5616 He Met Lyε Lyε Tyr Lyε Aεp Val Thr Ala Cys Leu Pro Glu Trp Glu 1860 1865 1870 GAT GGG CAT TTT TAC CTT GCC AAG TAC TAT GAC AAA TTG ATG CCC ATG 5664 Asp Gly His Phe Tyr Leu Ala Lys Tyr Tyr Aεp Lys Leu Met Pro Met 1875 1880 1885 GTC ACA GAC AAC AAA ATG GAA AAG CAA GGT GAT CTC ATC CGG TAT ATA 5712 Val Thr Asp Aεn Lys Met Glu Lys Gin Gly Aεp Leu He Arg Tyr He 1890 1895 1900 GTT CTT CAT TTT GGC AGA TCT CTA CAA TAT GGA AAT CAG TTC ATA TAT 5760 Val Leu Hiε Phe Gly Arg Ser Leu Gin Tyr Gly Aεn Gin Phe He Tyr 1905 1910 1915 1920 CAG TCA ATG CCA CGA ATG TTA ACT CTA TGG CTT GAT TAT GGT ACA AAG 5808 Gin Ser Met Pro Arg Met Leu Thr Leu Trp Leu Aεp Tyr Gly Thr Lyε 1925 1930 1935 GCA TAT GAA TGG GAA AAA GCT GGC CGC TCC GAT CGT GTA CAA ATG AGG 5856 Ala Tyr Glu Trp Glu Lyε Ala Gly Arg Ser Aεp Arg Val Gin Met Arg 1940 1945 1950 AAT GAT TTG GGT AAA ATA AAC AAG GTT ATC ACA GAG CAT ACA AAC TAT 5904 Asn Asp Leu Gly Lys He Asn Lys Val He Thr Glu His Thr Aεn Tyr 1955 1960 1965 TTA GCT CCA TAT CAA TTT TTG ACT GCT TTT TCA CAA TTG ATC TCT CGA 5952 Leu Ala Pro Tyr Gin Phe Leu Thr Ala Phe Ser Gin Leu He Ser Arg 1970 1975 1980 ATT TGT CAT TCT CAC GAT GAA GTT TTT GTT GTC TTG ATG GAA ATA ATA 6000 He Cys His Ser His Asp Glu Val Phe Val Val Leu Met Glu He He 1985 1990 1995 2000 GCC AAA GTA TTT CTA GCC TAT CCT CAA CAA GCA ATG TGG ATG ATG ACA 6048 Ala Lys Val Phe Leu Ala Tyr Pro Gin Gin Ala Met Trp Met Met Thr 2005 2010 2015 GCT GTG TCA AAG TCA TCT TAT CCC ATG CGT GTG AAC AGA TGC AAG GAA 6096 Ala Val Ser Lys Ser Ser Tyr Pro Met Arg Val Asn Arg Cyε Lyε Glu 2020 2025 2030 ATC CTC AAT AAA GCT ATT CAT ATG AAA AAA TCC TTA GAG AAG TTT GTT 6144 He Leu Aεn Lyε Ala He Hiε Met Lyε Lyε Ser Leu Glu Lys Phe Val 2035 2040 2045 GGA GAT GCA ACT CGC CTA ACA GAT AAG CTT CTA GAA TTG TGC AAT AAA 6192 Gly Asp Ala Thr Arg Leu Thr Aεp Lys Leu Leu Glu Leu Cyε Aεn Lys 2050 2055 2060 CCG GTT GAT GGA AGT AGT TCC ACA TTA AGC ATG AGC ACT CAT TTT AAA 6240 Pro Val Asp Gly Ser Ser Ser Thr Leu Ser Met Ser Thr His Phe Lys 2065 2070 2075 2080 ATG CTT AAA AAG CTG GTA GAA GAA GCA ACA TTT AGT GAA ATC CTC ATT 6288 Met Leu Lys Lys Leu Val Glu Glu Ala Thr Phe Ser Glu He Leu He 2085 2090 2095 CCT CTA CAA TCA GTC ATG ATA CCT ACA CTT CCA TCA ATT CTG GGT ACC 6336 Pro Leu Gin Ser Val Met He Pro Thr Leu Pro Ser He Leu Gly Thr 2100 2105 2110 CAT GCT AAC CAT GCT AGC CAT GAA CCA TTT CCT GGA CAT TGG GCC TAT 6384 His Ala Asn His Ala Ser His Glu Pro Phe Pro Gly His Trp Ala Tyr 2115 2120 2125 ATT GCA GGG TTT GAT GAT ATG GTG GAA ATT CTT GCT TCT CTT CAG AAA 6432 He Ala Gly Phe Asp Asp Met Val Glu He Leu Ala Ser Leu Gin Lys 2130 2135 2140 CCA AAG AAG ATT TCT TTA AAA GGC TCA GAT GGA AAG TTC TAC ATC ATG 6480 Pro Lys Lyε He Ser Leu Lyε Gly Ser Aεp Gly Lys Phe Tyr He Met 2145 2150 2155 2160 ATG TGT AAG CCA AAA GAT GAC CTG AGA AAG GAT TGT AGA CTA ATG GAA 6528 Met Cys Lys Pro Lys Asp Asp Leu Arg Lys Asp Cys Arg Leu Met Glu 2165 2170 2175 TTC AAT TCC TTG ATT AAT AAG TGC TTA AGA AAA GAT GCA GAG TCT CGT 6576 Phe Aεn Ser Leu He Aεn Lys Cyε Leu Arg Lyε Asp Ala Glu Ser Arg 2180 2185 2190 AGA AGA GAA CTT CAT ATT CGA ACA TAT GCA GTT ATT CCA CTA AAT GAT 6624 Arg Arg Glu Leu His He Arg Thr Tyr Ala Val He Pro Leu Asn Asp 2195 2200 2205 GAA TGT GGG ATT ATT GAA TGG GTG AAC AAC ACT GCT GGT TTG AGA CCT 6672 Glu Cys Gly He He Glu Trp Val Aεn Asn Thr Ala Gly Leu Arg Pro 2210 2215 2220 ATT CTG ACC AAA CTA TAT AAA GAA AAG GGA GTG TAT ATG ACA GGA AAA 6720 He Leu Thr Lys Leu Tyr Lys Glu Lys Gly Val Tyr Met Thr Gly Lys 2225 2230 2235 2240 GAA CTT CGC CAG TGT ATG CTA CCA AAG TCA GCA GCT TTA TCT GAA AAA 6768 Glu Leu Arg Gin Cys Met Leu Pro Lys Ser Ala Ala Leu Ser Glu Lyε 2245 2250 2255 CTC AAA GTA TTC CGA GAA TTT CTC CTG CCC AGG CAT CCT CCT ATT TTT 6816 Leu Lys Val Phe Arg Glu Phe Leu Leu Pro Arg His Pro Pro He Phe 2260 2265 2270 CAT GAG TGG TTT CTG AGA ACA TTC CCT GAT CCT ACA TCA TGG TAC AGT 6864 His Glu Trp Phe Leu Arg Thr Phe Pro Asp Pro Thr Ser Trp Tyr Ser 2275 2280 2285 AGT AGA TCA GCT TAC TGC CGT TCC ACT GCA GTA ATG TCA ATG GTT GGT 6912 Ser Arg Ser Ala Tyr Cys Arg Ser Thr Ala Val Met Ser Met Val Gly 2290 2295 2300 TAT ATT CTG GGG CTT GGA GAC CGT CAT GGT GAA AAT ATT CTC TTT GAT 6960 Tyr He Leu Gly Leu Gly Asp Arg His Gly Glu Asn He Leu Phe Asp 2305 2310 2315 2320 TCT TTG ACT GGT GAA TGC GTA CAT GTA GAT TTC AAT TGT CTT TTC AAT 7008 Ser Leu Thr Gly Glu Cyε Val His Val Asp Phe Aεn Cyε Leu Phe Aεn 2325 2330 2335 AAG GGA GAA ACC TTT GAA GTT CCA GAA ATT GTG CCA TTT CGC CTG ACT 7056 Lyε Gly Glu Thr Phe Glu Val Pro Glu He Val Pro Phe Arg Leu Thr 2340 2345 2350 CAT AAT ATG GTT AAT GGA ATG GGT CCT ATG GGA ACA GAG GGT CTT TTT 7104 His Asn Met Val Asn Gly Met Gly Pro Met Gly Thr Glu Gly Leu Phe 2355 2360 2365 CGA AGA GCA TGT GAA GTT ACA ATG AGG CTG ATG CGT GAT CAG CGA GAG 7152 Arg Arg Ala Cys Glu Val Thr Met Arg Leu Met Arg Asp Gin Arg Glu 2370 2375 2380 CCT TTA ATG AGT GTC TTA AAG ACT TTT CTA CAT GAT CCT CTT GTG GAA 7200 Pro Leu Met Ser Val Leu Lys Thr Phe Leu His Asp Pro Leu Val Glu 2385 2390 2395 2400 TGG AGT AAA CCA GTG AAA GGG CAT TCC AAA GCG CCA CTG AAT GAA ACT 7248 Trp Ser Lys Pro Val Lys Gly Hiε Ser Lys Ala Pro Leu Asn Glu Thr 2405 2410 2415 GGA GAA GTT GTC AAT GAA AAG GCC AAG ACC CAT GTT CTT GAC ATT GAG 7296 Gly Glu Val Val Aεn Glu Lyε Ala Lys Thr His Val Leu Asp He Glu 2420 2425 2430 CAG CGA CTA CAA GGT GTA ATC AAG ACT CGA AAT AGA GTG ACA GGA CTG 7344 Gin Arg Leu Gin Gly Val He Lys Thr Arg Asn Arg Val Thr Gly Leu 2435 2440 2445 CCG TTA TCT ATT GAA GGA CAT GTG CAT TAC CTT ATA CAA GAA GCT ACT 7392 Pro Leu Ser He Glu Gly His Val Hiε Tyr Leu He Gin Glu Ala Thr 2450 2455 2460 GAT GAA AAC TTA CTA TGC CAG ATG TAT CTT GGT TGG ACT CCA TAT ATG 7440 Aεp Glu Aεn Leu Leu Cys Gin Met Tyr Leu Gly Trp Thr Pro Tyr Met 2465 2470 2475 2480 TGAAATGAAA TTATGTAAAA GAATATGTTA ATAATCTAAA AGTAAAAAAA AAAAAAAAAA 7500 AA 7502 (2) INFORMATION FOR SEQ ID NO:33: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2480 amino acidε (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:33: Met Gly Hiε Ala Val Glu Trp Pro Val Val Met Ser Arg Phe Leu Ser 1 5 10 15 Gin Leu Asp Glu Hiε Met Gly Tyr Leu Gin Ser Ala Pro Leu Gin Leu 20 25 30 Met Ser Met Gin Aεn Leu Glu Phe He Glu Val Thr Leu Leu Met Val 35 40 45 Leu Thr Arg He He Ala He Val Phe Phe Arg Arg Gin Glu Leu Leu 50 55 60 Leu Trp Gin He Gly Cyε Val Leu Leu Glu Tyr Gly Ser Pro Lys He 65 70 75 80 Lys Ser Leu Ala He Ser Phe Leu Thr Glu Leu Phe Gin Leu Gly Gly 85 90 95 Leu Pro Ala Gin Pro Ala Ser Thr Phe Phe Ser Ser Phe Leu Glu Leu 100 105 110 Leu Lyε His Leu Val Glu Met Asp Thr Aεp Gin Leu Lys Leu Tyr Glu 115 120 125 Glu Pro Leu Ser Lys Leu He Lys Thr Leu Phe Pro Phe Glu Ala Glu 130 135 140 Ala Tyr Arg Asn He Glu Pro Val Tyr Leu Asn Met Leu Leu Glu Lys 145 150 155 160 Leu Cys Val Met Phe Glu Asp Gly Val Leu Met Arg Leu Lys Ser Asp 165 170 175 Leu Leu Lys Ala Ala Leu Cys Hiε Leu Leu Gin Tyr Phe Leu Lyε Phe 180 185 190 Val Pro Ala Gly Tyr Glu Ser Ala Leu Gin Val Arg Lys Val Tyr Val 195 200 205 Arg Asn He Cyε Lys Ala Leu Leu Asp Val Leu Gly He Glu Val Asp 210 215 220 Ala Glu Tyr Leu Leu Gly Pro Leu Tyr Ala Ala Leu Lys Met Glu Ser 225 230 235 240 Met Glu He He Glu Glu He Gin Cys Gin Thr Gin Gin Glu Asn Leu 245 250 255 Ser Ser Aεn Ser Aεp Gly He Ser Pro Lyε Arg Arg Arg Leu Ser Ser 260 265 270 Ser Leu Aεn Pro Ser Lys Arg Ala Pro Lys Gin Thr Glu Glu He Lys 275 280 285 His Val Asp Met Asn Gin Lys Ser He Leu Trp Ser Ala Leu Lys Gin 290 295 300 Lys Ala Glu Ser Leu Gin He Ser Leu Glu Tyr Ser Gly Leu Lys Asn 305 310 315 320 Pro Val He Glu Met Leu Glu Gly He Ala Val Val Leu Gin Leu Thr 325 330 335 Ala Leu Cys Thr Val His Cys Ser His Gin Asn Met Asn Cys Arg Thr 340 345 350 Phe Lys Asp Cys Gin His Lys Ser Lys Lys Lys Pro Ser Val Val He 355 360 365 Thr Trp Met Ser Leu Asp Phe Tyr Thr Lyε Val Leu Lyε Ser Cyε Arg 370 375 380 Ser Leu Leu Glu Ser Val Gin Lyε Leu Asp Leu Glu Ala Thr He Asp 385 390 395 400 Lys Val Val Lys He Tyr Asp Ala Leu He Tyr Met Gin Val Asn Ser 405 410 415 Ser Phe Glu Asp His He Leu Glu Asp Leu Cyε Gly Met Leu Ser Leu 420 425 430 Pro Trp He Tyr Ser His Ser Asp Asp Gly Cys Leu Lys Leu Thr Thr 435 440 445 Phe Ala Ala Asn Leu Leu Thr Leu Ser Cys Arg He Ser Asp Ser Tyr 450 455 460 Ser Pro Gin Ala Gin Ser Arg Cys Val Phe Leu Leu Thr Leu Phe Pro 465 470 475 480 Arg Arg He Phe Leu Glu Trp Arg Thr Ala Val Tyr Asn Trp Ala Leu 485 490 495 Gin Ser Ser His Glu Val He Arg Ala Ser Cys Val Ser Gly Phe Phe 500 505 510 Ile Leu Leu Gin Gin Gin Asn Ser Cys Asn Arg Val Pro Lys He Leu 515 520 525 He Asp Lys Val Lys Asp Asp Ser Asp He Val Lys Lys Glu Phe Ala 530 535 540 Ser He Leu Gly Gin Leu Val Cys Thr Leu His Gly Met Phe Tyr Leu 545 550 555 560 Thr Ser Ser Leu Thr Glu Pro Phe Ser Glu Hiε Gly His Val Asp Leu 565 570 575 Phe Cys Arg Aεn Leu Lyε Ala Thr Ser Gin Hiε Glu Cyε Ser Ser Ser 580 585 590 Gin Leu Lys Ala Ser Val Cys Lys Pro Phe Leu Phe Leu Leu Lyε Lys 595 600 605 Lys He Pro Ser Pro Val Lys Leu Ala Phe He Asp Asn Leu His His 610 615 620 Leu Cys Lyε His Leu Asp Phe Arg Glu Asp Glu Thr Asp Val Lys Ala 625 630 635 640 Val Leu Gly Thr Leu Leu Asn Leu Met Glu Asp Pro Asp Lys Asp Val 645 650 655 Arg Val Ala Phe Ser Gly Aεn He Lys Hiε He Leu Glu Ser Leu Aεp 660 665 670 Ser Glu Aεp Gly Phe He Lyε Glu Leu Phe Val Leu Arg Met Lyε Glu 675 680 685 Ala Tyr Thr Hiε Ala Gin He Ser Arg Asn Asn Glu Leu Lys Asp Thr 690 695 700 Leu He Leu Thr Thr Gly Asp He Gly Arg Ala Ala Lyε Gly Asp Leu 705 710 715 720 Val Pro Phe Ala Leu Leu Hiε Leu Leu Hiε Cyε Leu Leu Ser Lyε Ser 725 730 735 Ala Ser Val Ser Gly Ala Ala Tyr Thr Glu He Arg Ala Leu Val Ala 740 745 750 Ala Lys Ser Val Lyε Leu Gin Ser Phe Phe Ser Gin Tyr Lyε Lys Pro 755 760 765 He Cyε Gin Phe Leu Val Glu Ser Leu Hiε Ser Ser Gin Met Thr Ala 770 775 780 Leu Pro Aεn Thr Pro Cyε Gin Aεn Ala Aεp Val Arg Lyε Gin Aεp Val 785 790 795 800 Ala H s Gin Arg Glu Met Ala Leu Aεn Thr Leu Ser Glu He Ala Asn 805 810 815 Val Phe Aεp Phe Pro Asp Leu Asn Arg Phe Leu Thr Arg Thr Leu Gin 820 825 830 Val Leu Leu Pro Asp Leu Ala Ala Lys Ala Ser Pro Ala Ala Ser Ala 835 840 845 Leu He Arg Thr Leu Gly Lys Gin Leu Asn Val Asn Arg Arg Glu He 850 855 860 Leu He Asn Asn Phe Lys Tyr He Phe Ser His Leu Val Cys Ser Cys 865 870 875 880 Ser Lys Aεp Glu Leu Glu Arg Ala Leu His Tyr Leu Lys Asn Glu Thr 885 890 895 Glu He Glu Leu Gly Ser Leu Leu Arg Gin Asp Phe Gin Gly Leu His 900 905 910 Asn Glu Leu Leu Leu Arg He Gly Glu His Tyr Gin Gin Val Phe Asn 915 920 925 Gly Leu Ser He Leu Ala Ser Phe Ala Ser Ser Asp Asp Pro Tyr Gin 930 935 940 Gly Pro Arg Asp He He Ser Pro Glu Leu Met Ala Aεp Tyr Leu Gin 945 950 955 960 Pro Lyε Leu Leu Gly He Leu Ala Phe Phe Asn Met Gin Leu Leu Ser 965 970 975 Ser Ser Val Gly He Glu Asp Lys Lys Met Ala Leu Asn Ser Leu Met 980 985 990 Ser Leu Met Lys Leu Met Gly Pro Lys His Val Ser Ser Val Arg Val 995 1000 1005 Lys Met Met Thr Thr Leu Arg Thr Gly Leu Arg Phe Lys Asp Aεp Phe 1010 1015 1020 Pro Glu Leu Cyε Cys Arg Ala Trp Asp Cys Phe Val Arg Cyε Leu Aεp 1025 1030 1035 1040 His Ala Cys Leu Gly Ser Leu Leu Ser His Val He Val Ala Leu Leu 1045 1050 1055 Pro Leu He His He Gin Pro Lys Glu Thr Ala Ala He Phe His Tyr 1060 1065 1070 Leu He He Glu Asn Arg Asp Ala Val Gin Asp Phe Leu Hiε Glu He 1075 1080 1085 Tyr Phe Leu Pro Aεp Hiε Pro Glu Leu Lyε Lyε He Lys Ala Val Leu 1090 1095 1100 Gin Glu Tyr Arg Lys Glu Thr Ser Glu Ser Thr Asp Leu Gin Thr Thr 1105 1110 1115 1120 Leu Gin Leu Ser Met Lys Ala He Gin His Glu Asn Val Aεp Val Arg 1125 1130 1135 He Hiε Ala Leu Thr Ser Leu Lys Glu Thr Leu Tyr Lys Asn Gin Glu 1140 1145 1150 Lys Leu He Lyε Tyr Ala Thr Aεp Ser Glu Thr Val Glu Pro He He 1155 1160 1165 Ser Gin Leu Val Thr Val Leu Leu Lys Gly Cys Gin Asp Ala Asn Ser 1170 1175 1180 Gin Ala Arg Leu Leu Cys Gly Glu Cys Leu Gly Glu Leu Gly Ala He 1185 1190 1195 1200 sp Pro Gly Arg Leu Asp Phe Ser Thr Thr Glu Thr Gin Gly Lys Asp 1205 1210 1215 Phe Thr Phe Val Thr Gly Val Glu Asp Ser Ser Phe Ala Tyr Gly Leu 1220 1225 1230 Leu Met Glu Leu Thr Arg Ala Tyr Leu Ala Tyr Ala Asp Asn Ser Arg 1235 1240 1245 Ala Gin Asp Ser Ala Ala Tyr Ala He Gin Glu Leu Leu Ser He Tyr 1250 1255 1260 Asp Cys Arg Glu Met Glu Thr Asn Gly Pro Gly His Gin Leu Trp Arg 1265 1270 1275 1280 Arg Phe Pro Glu His Val Arg Glu He Leu Glu Pro His Leu Aεn Thr 1285 1290 1295 Arg Tyr Lys Ser Ser Gin Lys Ser Thr Asp Trp Ser Gly Val Lyε Lys 1300 1305 1310 Pro He Tyr Leu Ser Lyε Leu Gly Ser Asn Phe Ala Glu Trp Ser Ala 1315 1320 1325 Ser Trp Ala Gly Tyr Leu He Thr Lys Val Arg His Asp Leu Ala Ser 1330 1335 1340 Lys He Phe Thr Cys Cys Ser He Met Met Lyε Hiε Aεp Phe Lys Val 1345 1350 1355 1360 Thr He Tyr Leu Leu Pro His He Leu Val Tyr Val Leu Leu Gly Cys 1365 1370 1375 Asn Gin Glu Asp Gin Gin Glu Val Tyr Ala Glu He Met Ala Val Leu 1380 1385 1390 Lys His Asp Asp Gin His Thr He Asn Thr Gin Asp He Ala Ser Asp 1395 1400 1405 Leu Cys Gin Leu Ser Thr Gin Thr Val Phe Ser Met Leu Asp His Leu 1410 1415 1420 Thr Gin Trp Ala Arg His Lys Phe Gin Ala Leu Lys Ala Glu Lys Cys 1425 1430 1435 1440 Pro His Ser Lys Ser Asn Arg Asn Lys Val Asp Ser Met Val Ser Thr 1445 1450 1455 Val Asp Tyr Glu Asp Tyr Gin Ser Val Thr Arg Phe Leu Asp Leu He 1460 1465 1470 Pro Gin Aεp Thr Leu Ala Val Ala Ser Phe Arg Ser Lys Ala Tyr Thr 1475 1480 1485 Arg Ala Val Met His Phe Glu Ser Phe He Thr Glu Lys Lys Gin Asn 1490 1495 1500 He Gin Glu Hiε Leu Gly Phe Leu Gin Lyε Leu Tyr Ala Ala Met Hiε 1505 1510 1515 1520 Glu Pro Aεp Gly Val Ala Gly Val Ser Ala He Arg Lys Ala Glu Pro 1525 1530 1535 Ser Leu Lys Glu Gin He Leu Glu His Glu Ser Leu Gly Leu Leu Arg 1540 1545 1550 Asp Ala Thr Ala Cys Tyr Aεp Arg Ala He Gin Leu Glu Pro Aεp Gin 1555 1560 1565 Ile He His Tyr His Gly Val Val Lys Ser Met Leu Gly Leu Gly Gin 1570 1575 1580 Leu Ser Thr Val He Thr Gin Val Asn Gly Val His Ala Aεn Arg Ser 1585 1590 1595 1600 Glu Trp Thr Asp Glu Leu Asn Thr Tyr Arg Val Glu Ala Ala Trp Lyε 1605 1610 1615 Leu Ser Gin Trp Asp Leu Val Glu Aεn Tyr Leu Ala Ala Asp Gly Lyε 1620 1625 1630 Ser Thr Thr Trp Ser Val Arg Leu Gly Gin Leu Leu Leu Ser Ala Lyε 1635 1640 1645 Lyε Arg Aεp He Thr Ala Phe Tyr Aεp Ser Leu Lys Leu Val Arg Ala 1650 1655 1660 Glu Gin He Val Pro Leu Ser Ala Ala Ser Phe Glu Arg Gly Ser Tyr 1665 1670 1675 1680 Gin Arg Gly Tyr Glu Tyr He Val Arg Leu His Met Leu Cyε Glu Leu 1685 1690 1695 Glu His Ser He Lyε Pro Leu Phe Gin His Ser Pro Gly Asp Ser Ser 1700 1705 1710 Gin Glu Asp Ser Leu Asn Trp Val Ala Arg Leu Glu Met Thr Gin Asn 1715 1720 1725 Ser Tyr Arg Ala Lyε Glu Pro He Leu Ala Leu Arg Arg Ala Leu Leu 1730 1735 1740 Ser Leu Asn Lys Arg Pro Asp Tyr Aεn Glu Met Val Gly Glu Cyε Trp 1745 1750 1755 1760 Leu Gin Ser Ala Arg Val Ala Arg Lys Ala Gly Hiε Hiε Gin Thr Ala 1765 1770 1775 Tyr Aεn Ala Leu Leu Aεn Ala Gly Glu Ser Arg Leu Ala Glu Leu Tyr 1780 1785 1790 Val Glu Arg Ala Lyε Trp Leu Trp Ser Lyε Gly Aεp Val Hiε Gin Ala 1795 1800 1805 Leu He Val Leu Gin Lyε Gly Val Glu Leu Cyε Phe Pro Glu Aεn Glu 1810 1815 1820 Thr Pro Pro Glu Gly Lyε Aεn Met Leu He Hiε Gly Arg Ala Met Leu 1825 1830 1835 1840 Leu Val Gly Arg Phe Met Glu Glu Thr Ala Aεn Phe Glu Ser Aεn Ala 1845 1850 1855 He Met Lys Lys Tyr Lys Asp Val Thr Ala Cys Leu Pro Glu Trp Glu 1860 1865 1870 Asp Gly His Phe Tyr Leu Ala Lys Tyr Tyr Asp Lys Leu Met Pro Met 1875 1880 1885 Val Thr Asp Asn Lys Met Glu Lys Gin Gly Asp Leu He Arg Tyr He 1890 1895 1900 Val Leu His Phe Gly Arg Ser Leu Gin Tyr Gly Asn Gin Phe He Tyr 1905 1910 1915 1920 Gln Ser Met Pro Arg Met Leu Thr Leu Trp Leu Asp Tyr Gly Thr Lys 1925 1930 1935 Ala Tyr Glu Trp Glu Lys Ala Gly Arg Ser Asp Arg Val Gin Met Arg 1940 1945 1950 Asn Aεp Leu Gly Lyε He Aεn Lys Val He Thr Glu Hiε Thr Aεn Tyr 1955 1960 1965 Leu Ala Pro Tyr Gin Phe Leu Thr Ala Phe Ser Gin Leu He Ser Arg 1970 1975 1980 He Cys Hiε Ser His Asp Glu Val Phe Val Val Leu Met Glu He He 1985 1990 1995 2000 Ala Lys Val Phe Leu Ala Tyr Pro Gin Gin Ala Met Trp Met Met Thr 2005 2010 2015 Ala Val Ser Lys Ser Ser Tyr Pro Met Arg Val Asn Arg Cys Lys Glu 2020 2025 2030 He Leu Asn Lys Ala He His Met Lys Lys Ser Leu Glu Lys Phe Val 2035 2040 2045 Gly Aεp Ala Thr Arg Leu Thr Asp Lys Leu Leu Glu Leu Cys Aεn Lys 2050 2055 2060 Pro Val Asp Gly Ser Ser Ser Thr Leu Ser Met Ser Thr His Phe Lys 2065 2070 2075 2080 Met Leu Lys Lys Leu Val Glu Glu Ala Thr Phe Ser Glu He Leu He 2085 2090 2095 Pro Leu Gin Ser Val Met He Pro Thr Leu Pro Ser He Leu Gly Thr 2100 2105 2110 His Ala Aεn His Ala Ser Hiε Glu Pro Phe Pro Gly His Trp Ala Tyr 2115 2120 2125 He Ala Gly Phe Aεp Asp Met Val Glu He Leu Ala Ser Leu Gin Lys 2130 2135 2140 Pro Lys Lys He Ser Leu Lys Gly Ser Asp Gly Lys Phe Tyr He Met 2145 2150 2155 2160 Met Cys Lys Pro Lys Asp Aεp Leu Arg Lys Aεp Cys Arg Leu Met Glu 2165 2170 2175 Phe Asn Ser Leu He Aεn Lyε Cys Leu Arg Lys Asp Ala Glu Ser Arg 2180 2185 2190 Arg Arg Glu Leu Hiε He Arg Thr Tyr Ala Val He Pro Leu Aεn Aεp 2195 2200 2205 Glu Cyε Gly He He Glu Trp Val Asn Asn Thr Ala Gly Leu Arg Pro 2210 2215 2220 He Leu Thr Lys Leu Tyr Lys Glu Lyε Gly Val Tyr Met Thr Gly Lys 2225 2230 2235 2240 Glu Leu Arg Gin Cyε Met Leu Pro Lys Ser Ala Ala Leu Ser Glu Lys 2245 2250 2255 Leu Lys Val Phe Arg Glu Phe Leu Leu Pro Arg His Pro Pro He Phe 2260 2265 2270 His Glu Trp Phe Leu Arg Thr Phe Pro Asp Pro Thr Ser Trp Tyr Ser 2275 2280 2285 Ser Arg Ser Ala Tyr Cys Arg Ser Thr Ala Val Met Ser Met Val Gly 2290 2295 2300 Tyr He Leu Gly Leu Gly Asp Arg His Gly Glu Asn He Leu Phe Aεp 2305 2310 2315 2320 Ser Leu Thr Gly Glu Cyε Val Hiε Val Aεp Phe Aεn Cyε Leu Phe Aεn 2325 2330 2335 Lys Gly Glu Thr Phe Glu Val Pro Glu He Val Pro Phe Arg Leu Thr 2340 2345 2350 His Asn Met Val Asn Gly Met Gly Pro Met Gly Thr Glu Gly Leu Phe 2355 2360 2365 Arg Arg Ala Cys Glu Val Thr Met Arg Leu Met Arg Aεp Gin Arg Glu 2370 2375 2380 Pro Leu Met Ser Val Leu Lyε Thr Phe Leu Hiε Aεp Pro Leu Val Glu 2385 2390 2395 2400 Trp Ser Lys Pro Val Lys Gly His Ser Lys Ala Pro Leu Asn Glu Thr 2405 2410 2415 Gly Glu Val Val Asn Glu Lys Ala Lys Thr His Val Leu Asp He Glu 2420 2425 2430 Gin Arg Leu Gin Gly Val He Lyε Thr Arg Aεn Arg Val Thr Gly Leu 2435 2440 2445 Pro Leu Ser He Glu Gly Hiε Val His Tyr Leu He Gin Glu Ala Thr 2450 2455 2460 Asp Glu Aεn Leu Leu Cys Gin Met Tyr Leu Gly Trp Thr Pro Tyr Met 2465 2470 2475 2480 (2) INFORMATION FOR SEQ ID NO:34: (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9385 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear Ul) MOLECULE TYPE: cDNA (v) FRAGMENT TYPE: linear (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 190..9357 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:34: GCGAGAGGAG TCGGGATCTG CGCTGCAGCC ACCGCCGCGG TTGATACTAC TTTGACCTTC 60 CGAGTGCAGT GAGGCATACA TCACAATTTG GAATTATGCA TTGGTTTATC AATTTACTTG 120 TTTATTGTCA CCCTGCTGCC CAGATATGAC TTCATGAGGA CAGTGATGTG TGTTCTGAAA 180 TTGTGAACC ATG AGT CTA GTA CTT AAT GAT CTG CTT ATC TGC TGC CGT 228 Met Ser Leu Val Leu Asn Asp Leu Leu He Cys Cys Arg 1 5 10 CAA CTA GAA CAT GAT AGA GCT ACA GAA CGA AAG AAA GAA GTT GAG AAA 276 Gin Leu Glu His Asp Arg Ala Thr Glu Arg Lyε Lyε Glu Val Glu Lys 15 20 25 TTT AAG CGC CTG ATT CGA GAT CCT GAA ACA ATT AAA CAT CTA GAT CGG 324 Phe Lys Arg Leu He Arg Asp Pro Glu Thr He Lyε Hiε Leu Aεp Arg 30 35 40 45 CAT TCA GAT TCC AAA CAA GGA AAA TAT TTG AAT TGG GAT GCT GTT TTT 372 His Ser Aεp Ser Lyε Gin Gly Lyε Tyr Leu Aεn Trp Aεp Ala Val Phe 50 55 60 AGA TTT TTA CAG AAA TAT ATT CAG AAA GAA ACA GAA TGT CTG AGA ATA 420 Arg Phe Leu Gin Lys Tyr He Gin Lys Glu Thr Glu Cyε Leu Arg He 65 70 75 GCA AAA CCA AAT GTA TCA GCC TCA ACA CAA GCC TCC AGG CAG AAA AAG 468 Ala Lys Pro Aεn Val Ser Ala Ser Thr Gin Ala Ser Arg Gin Lyε Lyε 80 85 90 ATG CAG GAA ATC AGT AGT TTG GTC AAA TAC TTC ATC AAA TGT GCA AAC 516 Met Gin Glu He Ser Ser Leu Val Lyε Tyr Phe He Lyε Cys Ala Asn 95 100 105 AGA AGA GCA CCT AGG CTA AAA TGT CAA GAA CTC TTA AAT TAT ATC ATG 564 Arg Arg Ala Pro Arg Leu Lyε Cyε Gin Glu Leu Leu Aεn Tyr He Met 110 115 120 125 GAT ACA GTG AAA GAT TCA TCT AAT GGT GCT ATT TAC GGA GCT GAT TGT 612 Aεp Thr Val Lyε Aεp Ser Ser Asn Gly Ala He Tyr Gly Ala Asp Cyε 130 135 140 AGC AAC ATA CTA CTC AAA GAC ATT CTT TCT GTG AGA AAA TAC TGG TGT 660 Ser Aεn He Leu Leu Lyε Asp He Leu Ser Val Arg Lys Tyr Trp Cys 145 150 155 GAA ATA TCT CAG CAA CAG TGG TTA GAA TTG TTC TCT GTG TAC TTC AGG 708 Glu He Ser Gin Gin Gin Trp Leu Glu Leu Phe Ser Val Tyr Phe Arg 160 165 170 CTC TAT CTG AAA CCT TCA CAA GAT GTT CAT AGA GTT TTA GTG GCT AGA 756 Leu Tyr Leu Lys Pro Ser Gin Asp Val His Arg Val Leu Val Ala Arg 175 180 185 ATA ATT CAT GCT GTT ACC AAA GGA TGC TGT TCT CAG ACT GAC GGA TTA 804 He He His Ala Val Thr Lys Gly Cys Cys Ser Gin Thr Aεp Gly Leu 190 195 200 205 AAT TCC AAA TTT TTG GAC TTT TTT TCC AAG GCT ATT CAG TGT GCG AGA 852 Aεn Ser Lyε Phe Leu Aεp Phe Phe Ser Lys Ala He Gin Cys Ala Arg 210 215 220 CAA GAA AAG AGC TCT TCA GGT CTA AAT CAT ATC TTA GCA GCT CTT ACT 900 Gin Glu Lys Ser Ser Ser Gly Leu Aεn His He Leu Ala Ala Leu Thr 225 230 235 ATC TTC CTC AAG ACT TTG GCT GTC AAC TTT CGA ATT CGA GTG TGT GAA 948 He Phe Leu Lys Thr Leu Ala Val Asn Phe Arg He Arg Val Cys Glu 240 245 250 TTA GGA GAT GAA ATT CTT CCC ACT TTG CTT TAT ATT TGG ACT CAA CAT 996 Leu Gly Asp Glu He Leu Pro Thr Leu Leu Tyr He Trp Thr Gin His 255 260 265 AGG CTT AAT GAT TCT TTA AAA GAA GTC ATT ATT GAA TTA TTT CAA CTG 1044 Arg Leu Asn Asp Ser Leu Lys Glu Val He He Glu Leu Phe Gin Leu 270 275 280 285 CAA ATT TAT ATC CAT CAT CCG AAA GGA GCC AAA ACC CAA GAA AAA GGT 1092 Gin He Tyr He His His Pro Lys Gly Ala Lys Thr Gin Glu Lys Gly 290 295 300 GCT TAT GAA TCA ACA AAA TGG AGA AGT ATT TTA TAC AAC TTA TAT GAT 1140 Ala Tyr Glu Ser Thr Lys Trp Arg Ser He Leu Tyr Asn Leu Tyr Aεp 305 310 315 CTG CTA GTG AAT GAG ATA AGT CAT ATA GGA AGT AGA GGA AAG TAT TCT 1188 Leu Leu Val Aεn Glu He Ser Hiε He Gly Ser Arg Gly Lyε Tyr Ser 320 325 330 TCA GGA TTT CGT AAT ATT GCC GTC AAA GAA AAT TTG ATT GAA TTG ATG 1236 Ser Gly Phe Arg Aεn He Ala Val Lys Glu Asn Leu He Glu Leu Met 335 340 345 GCA GAT ATC TGT CAC CAG GTT TTT AAT GAA GAT ACC AGA TCC TTG GAG 1284 Ala Aεp He Cys Hiε Gin Val Phe Asn Glu Asp Thr Arg Ser Leu Glu 350 355 360 365 ATT TCT CAA TCT TAC ACT ACT ACA CAA AGA GAA TCT AGT GAT TAC AGT 1332 He Ser Gin Ser Tyr Thr Thr Thr Gin Arg Glu Ser Ser Asp Tyr Ser 370 375 380 GTC CCT TGC AAA AGG AAG AAA ATA GAA CTA GGC TGG GAA GTA ATA AAA 1380 Val Pro Cys Lys Arg Lys Lys He Glu Leu Gly Trp Glu Val He Lys 385 390 395 GAT CAC CTT CAG AAG TCA CAG AAT GAT TTT GAT CTT GTG CCT TGG CTA 1428 Aεp Hiε Leu Gin Lyε Ser Gin Aεn Aεp Phe Aεp Leu Val Pro Trp Leu 400 405 410 CAG ATT GCA ACC CAA TTA ATA TCA AAG TAT CCT GCA AGT TTA CCT AAC 1476 Gin He Ala Thr Gin Leu He Ser Lyε Tyr Pro Ala Ser Leu Pro Asn 415 420 425 TGT GAG CTG TCT CCA TTA CTG ATG ATA CTA TCT CAG CTT CTA CCC CAA 1524 Cys Glu Leu Ser Pro Leu Leu Met He Leu Ser Gin Leu Leu Pro Gin 430 435 440 445 CAG CGA CAT GGG GAA CGT ACA CCA TAT GTG TTA CGA TGC CTT ACG GAA 1572 Gin Arg His Gly Glu Arg Thr Pro Tyr Val Leu Arg Cys Leu Thr Glu 450 455 460 GTT GCA TTG TGT CAA GAC AAG AGG TCA AAC CTA GAA AGC TCA CAA AAG 1620 Val Ala Leu Cys Gin Asp Lys Arg Ser Aεn Leu Glu Ser Ser Gin Lyε 465 470 475 TCA GAT TTA TTA AAA CTC TGG AAT AAA ATT TGG TGT ATT ACC TTT CGT 1668 Ser Aεp Leu Leu Lys Leu Trp Asn Lys He Trp Cys He Thr Phe Arg 480 485 490 GGT ATA AGT TCT GAG CAA ATA CAA GCT GAA AAC TTT GGC TTA CTT GGA 1716 Gly He Ser Ser Glu Gin He Gin Ala Glu Asn Phe Gly Leu Leu Gly 495 500 505 GCC ATA ATT CAG GGT AGT TTA GTT GAG GTT GAC AGA GAA TTC TGG AAG 1764 Ala He He Gin Gly Ser Leu Val Glu Val Asp Arg Glu Phe Trp Lys 510 515 520 525 TTA TTT ACT GGG TCA GCC TGC AGA CCT TCA TGT CCT GCA GTA TGC TGT 1812 Leu Phe Thr Gly Ser Ala Cys Arg Pro Ser Cys Pro Ala Val Cys Cys 530 535 540 TTG ACT TTG GCA CTG ACC ACC AGT ATA GTT CCA GGA GCG GTA AAA ATG 1860 Leu Thr Leu Ala Leu Thr Thr Ser He Val Pro Gly Ala Val Lys Met 545 550 555 GGA ATA GAG CAA AAT ATG TGT GAA GTA AAT AGA AGC TTT TCT TTA AAG 1908 Gly He Glu Gin Asn Met Cyε Glu Val Aεn Arg Ser Phe Ser Leu Lys 560 565 570 GAA TCA ATA ATG AAA TGG CTC TTA TTC TAT CAG TTA GAG GGT GAC TTA 1956 Glu Ser He Met Lys Trp Leu Leu Phe Tyr Gin Leu Glu Gly Asp Leu 575 580 585 GAA AAT AGC ACA GAA GTG CCT CCA ATT CTT CAC AGT AAT TTT CCT CAT 2004 Glu Asn Ser Thr Glu Val Pro Pro He Leu His Ser Asn Phe Pro Hiε 590 595 600 605 CTT GTA CTG GAG AAA ATT CTT GTG AGT CTC ACT ATG AAA AAC TGT AAA 2052 Leu Val Leu Glu Lyε He Leu Val Ser Leu Thr Met Lys Aεn Cys Lys 610 615 620 GCT GCA ATG AAT TTT TTC CAA AGC GTG CCA GAA TGT GAA CAC CAC CAA 2100 Ala Ala Met Asn Phe Phe Gin Ser Val Pro Glu Cys Glu Hiε His Gin 625 630 635 AAA GAT AAA GAA GAA CTT TCA TTC TCA GAA GTA GAA GAA CTA TTT CTT 2148 Lys Asp Lys Glu Glu Leu Ser Phe Ser Glu Val Glu Glu Leu Phe Leu 640 645 650 CAG ACA ACT TTT GAC AAG ATG GAC TTT TTA ACC ATT GTG AGA GAA TGT 2196 Gin Thr Thr Phe Asp Lyε Met Aεp Phe Leu Thr He Val Arg Glu Cys 655 660 665 GGT ATA GAA AAG CAC CAG TCC AGT ATT GGC TTC TCT GTC CAC CAG AAT 2244 Gly He Glu Lys His Gin Ser Ser He Gly Phe Ser Val His Gin Asn 670 675 680 685 CTC AAG GAA TCA CTG GAT CGC TGT CTT CTG GGA TTA TCA GAA CAG CTT 2292 Leu Lys Glu Ser Leu Aεp Arg Cyε Leu Leu Gly Leu Ser Glu Gin Leu 690 695 700 CTG AAT AAT TAC TCA TCT GAG ATT ACA AAT TCA GAA ACT CTT GTC CGG 2340 Leu Asn Asn Tyr Ser Ser Glu He Thr Asn Ser Glu Thr Leu Val Arg 705 710 715 TGT TCA CGT CTT TTG GTG GGT GTC CTT GGC TGC TAC TGT TAC ATG GGT 2388 Cys Ser Arg Leu Leu Val Gly Val Leu Gly Cys Tyr Cys Tyr Met Gly 720 725 730 GTA ATA GCT GAA GAG GAA GCA TAT AAG TCA GAA TTA TTC CAG AAA GCC 2436 Val He Ala Glu Glu Glu Ala Tyr Lys Ser Glu Leu Phe Gin Lys Ala 735 740 745 AAC TCT CTA ATG CAA TGT GCA GGA GAA AGT ATC ACT CTG TTT AAA AAT 2484 Asn Ser Leu Met Gin Cys Ala Gly Glu Ser He Thr Leu Phe Lys Asn 750 755 760 765 AAG ACA AAT GAG GAA TTC AGA ATT GGT TCC TTG AGA AAT ATG ATG CAG 2532 Lys Thr Asn Glu Glu Phe Arg He Gly Ser Leu Arg Asn Met Met Gin 770 775 780 CTA TGT ACA CGT TGC TTG AGC AAC TGT ACC AAG AAG AGT CCA AAT AAG 2580 Leu Cys Thr Arg Cyε Leu Ser Asn Cys Thr Lyε Lyε Ser Pro Aεn Lyε 785 790 795 ATT GCA TCT GGC TTT TTC CTG CGA TTG TTA ACA TCA AAG CTA ATG AAT 2628 He Ala Ser Gly Phe Phe Leu Arg Leu Leu Thr Ser Lys Leu Met Asn 800 805 810 GAC ATT GCA GAT ATT TGT AAA AGT TTA GCA TCC TTC ATC AAA AAG CCA 2676 Aεp He Ala Asp He Cys Lys Ser Leu Ala Ser Phe He Lyε Lyε Pro 815 820 825 TTT GAC CGT GGA GAA GTA GAA TCA ATG GAA GAT GAT ACT AAT GGA AAT 2724 Phe Asp Arg Gly Glu Val Glu Ser Met Glu Asp Asp Thr Asn Gly Asn 830 835 840 845 CTA ATG GAG GTG GAG GAT CAG TCA TCC ATG AAT CTA TTT AAC GAT TAC 2772 Leu Met Glu Val Glu Asp Gin Ser Ser Met Asn Leu Phe Asn Asp Tyr 850 855 860 CCT GAT AGT AGT GTT AGT GAT GCA AAC GAA CCT GGA GAG AGC CAA AGT 2820 Pro Asp Ser Ser Val Ser Asp Ala Aεn Glu Pro Gly Glu Ser Gin Ser 865 870 875 ACC ATA GGT GCC ATT AAT CCT TTA GCT GAA GAA TAT CTG TCA AAG CAA 2868 Thr He Gly Ala He Aεn Pro Leu Ala Glu Glu Tyr Leu Ser Lyε Gin 880 885 890 GAT CTA CTT TTC TTA GAC ATG CTC AAG TTC TTG TGT TTG TGT GTA ACT 2916 Asp Leu Leu Phe Leu Asp Met Leu Lys Phe Leu Cys Leu Cyε Val Thr 895 900 905 ACT GCT CAG ACC AAT ACT GTG TCC TTT AGG GCA GCT GAT ATT CGG AGG 2964 Thr Ala Gin Thr Aεn Thr Val Ser Phe Arg Ala Ala Aεp He Arg Arg 910 915 920 925 AAA TTG TTA ATG TTA ATT GAT TCT AGC ACG CTA GAA CCT ACC AAA TCC 3012 Lys Leu Leu Met Leu He Aεp Ser Ser Thr Leu Glu Pro Thr Lyε Ser 930 935 940 CTC CAC CTG CAT ATG TAT CTA ATG CTT TTA AAG GAG CTT CCT GGA GAA 3060 Leu Hiε Leu His Met Tyr Leu Met Leu Leu Lys Glu Leu Pro Gly Glu 945 950 955 GAG TAC CCC TTG CCA ATG GAA GAT GTT CTT GAA CTT CTG AAA CCA CTA 3108 Glu Tyr Pro Leu Pro Met Glu Asp Val Leu Glu Leu Leu Lys Pro Leu 960 965 970 TCC AAT GTG TGT TCT TTG TAT CGT CGT GAC CAA GAT GTT TGT AAA ACT 3156 Ser Asn Val Cys Ser Leu Tyr Arg Arg Asp Gin Asp Val Cys Lys Thr 975 980 985 ATT TTA AAC CAT GTC CTT CAT GTA GTG AAA AAC CTA GGT CAA AGC AAT 3204 He Leu Asn His Val Leu His Val Val Lys Asn Leu Gly Gin Ser Asn 990 995 1000 1005 ATG GAC TCT GAG AAC ACA AGG GAT GCT CAA GGA CAG TTT CTT ACA GTA 3252 Met Asp Ser Glu Asn Thr Arg Asp Ala Gin Gly Gin Phe Leu Thr Val 1010 1015 1020 ATT GGA GCA TTT TGG CAT CTA ACA AAG GAG AGG AAA TAT ATA TTC TCT 3300 He Gly Ala Phe Trp His Leu Thr Lys Glu Arg Lys Tyr He Phe Ser 1025 1030 1035 GTA AGA ATG GCC CTA GTA AAT TGC CTT AAA ACT TTG CTT GAG GCT GAT 3348 Val Arg Met Ala Leu Val Aεn Cys Leu Lys Thr Leu Leu Glu Ala Asp 1040 1045 1050 CCT TAT TCA AAA TGG GCC ATT CTT AAT GTA ATG GGA AAA GAC TTT CCT 3396 Pro Tyr Ser Lys Trp Ala He Leu Asn Val Met Gly Lyε Asp Phe Pro 1055 1060 1065 GTA AAT GAA GTA TTT ACA CAA TTT CTT GCT GAC AAT CAT CAC CAA GTT 3444 Val Asn Glu Val Phe Thr Gin Phe Leu Ala Asp Asn Hiε Hiε Gin Val 1070 1075 1080 1085 CGC ATG TTG GCT GCA GAG TCA ATC AAT AGA TTG TTC CAG GAC ACG AAG 3492 Arg Met Leu Ala Ala Glu Ser He Aεn Arg Leu Phe Gin Asp Thr Lys 1090 1095 1100 GGA GAT TCT TCC AGG TTA CTG AAA GCA CTT CCT TTG AAG CTT CAG CAA 3540 Gly Asp Ser Ser Arg Leu Leu Lyε Ala Leu Pro Leu Lyε Leu Gin Gin 1105 1110 1115 ACA GCT TTT GAA AAT GCA TAC TTG AAA GCT CAG GAA GGA ATG AGA GAA 3588 Thr Ala Phe Glu Aεn Ala Tyr Leu Lyε Ala Gin Glu Gly Met Arg Glu 1120 1125 1130 ATG TCC CAT AGT GCT GAG AAC CCT GAA ACT TTG GAT GAA ATT TAT AAT 3636 Met Ser His Ser Ala Glu Aεn Pro Glu Thr Leu Aεp Glu He Tyr Asn 1135 1140 1145 AGA AAA TCT GTT TTA CTG ACG TTG ATA GCT GTG GTT TTA TCC TGT AGC 3684 Arg Lys Ser Val Leu Leu Thr Leu He Ala Val Val Leu Ser Cys Ser 1150 1155 1160 1165 CCT ATC TGC GAA AAA CAG GCT TTG TTT GCC CTG TGT AAA TCT GTG AAA 3732 Pro He Cys Glu Lys Gin Ala Leu Phe Ala Leu Cyε Lyε Ser Val Lyε 1170 1175 1180 GAG AAT GGA TTA GAA CCT CAC CTT GTG AAA AAG GTT TTA GAG AAA GTT 3780 Glu Asn Gly Leu Glu Pro His Leu Val Lys Lys Val Leu Glu Lys Val 1185 1190 1195 TCT GAA ACT TTT GGA TAT AGA CGT TTA GAA GAC TTT ATG GCA TCT CAT 3828 Ser Glu Thr Phe Gly Tyr Arg Arg Leu Glu Aεp Phe Met Ala Ser His 1200 1205 1210 TTA GAT TAT CTG GTT TTG GAA TGG CTA AAT CTT CAA GAT ACT GAA TAC 3876 Leu Asp Tyr Leu Val Leu Glu Trp Leu Asn Leu Gin Asp Thr Glu Tyr 1215 1220 1225 AAC TTA TCT TCT TTT CCT TTT ATT TTA TTA AAC TAC ACA AAT ATT GAG 3924 Asn Leu Ser Ser Phe Pro Phe He Leu Leu Asn Tyr Thr Asn He Glu 1230 1235 1240 1245 GAT TTC TAT AGA TCT TGT TAT AAG GTT TTG ATT CCA CAT CTG GTG ATT 3972 Asp Phe Tyr Arg Ser Cys Tyr Lyε Val Leu He Pro Hiε Leu Val He 1250 1255 1260 AGA AGT CAT TTT GAT GAG GTG AAG TCC ATT GCT AAT CAG ATT CAA GAG 4020 Arg Ser His Phe Asp Glu Val Lyε Ser He Ala Asn Gin He Gin Glu 1265 1270 1275 GAC TGG AAA AGT CTT CTA ACA GAC TGC TTT CCA AAG ATT CTT GTA AAT 4068 Aεp Trp Lys Ser Leu Leu Thr Asp Cyε Phe Pro Lyε He Leu Val Aεn 1280 1285 1290 ATT CTT CCT TAT TTT GCC TAT GAG GGT ACC AGA GAC AGT GGG ATG GCA 4116 He Leu Pro Tyr Phe Ala Tyr Glu Gly Thr Arg Asp Ser Gly Met Ala 1295 1300 1305 CAG CAA AGA GAG ACT GCT ACC AAG GTC TAT GAT ATG CTT AAA AGT GAA 4164 Gin Gin Arg Glu Thr Ala Thr Lys Val Tyr Asp Met Leu Lys Ser Glu 1310 1315 1320 1325 AAC TTA TTG GGA AAA CAG ATT GAT CAC TTA TTC ATT AGT AAT TTA CCA 4212 Asn Leu Leu Gly Lys Gin He Aεp His Leu Phe He Ser Aεn Leu Pro 1330 1335 1340 GAG ATT GTG GTG GAG TTA TTG ATG ACG TTA CAT GAG CCA GCA AAT TCT 4260 Glu He Val Val Glu Leu Leu Met Thr Leu His Glu Pro Ala Asn Ser 1345 1350 1355 AGT GCC AGT CAG AGC ACT GAC CTC TGT GAC TTT TCA GGG GAT TTG GAT 4308 Ser Ala Ser Gin Ser Thr Aεp Leu Cys Asp Phe Ser Gly Asp Leu Asp 1360 1365 1370 CCT GCT CCT AAT CCA CCT CAT TTT CCA TCG CAT GTG ATT AAA GCA ACA 4356 Pro Ala Pro Asn Pro Pro His Phe Pro Ser His Val He Lys Ala Thr 1375 1380 1385 TTT GCC TAT ATC AGC AAT TGT CAT AAA ACC AAG TTA AAA AGC ATT TTA 4404 Phe Ala Tyr He Ser Aεn Cys His Lys Thr Lys Leu Lyε Ser He Leu 1390 1395 1400 1405 GAA ATT CTT TCC AAA AGC CCT GAT TCC TAT CAG AAA ATT CTT CTT GCC 4452 Glu He Leu Ser Lys Ser Pro Asp Ser Tyr Gin Lys He Leu Leu Ala 1410 1415 1420 ATA TGT GAG CAA GCA GCT GAA ACA AAT AAT GTT TAT AAG AAG CAC AGA 4500 He Cys Glu Gin Ala Ala Glu Thr Aεn Aεn Val Tyr Lys Lys His Arg 1425 1430 1435 ATT CTT AAA ATA TAT CAC CTG TTT GTT AGT TTA TTA CTG AAA GAT ATA 4548 He Leu Lys He Tyr His Leu Phe Val Ser Leu Leu Leu Lys Aεp He 1440 1445 1450 AAA AGT GGC TTA GGA GGA GCT TGG GCC TTT GTT CTT CGA GAC GTT ATT 4596 Lys Ser Gly Leu Gly Gly Ala Trp Ala Phe Val Leu Arg Asp Val He 1455 1460 1465 TAT ACT TTG ATT CAC TAT ATC AAC CAA AGG CCT TCT TGT ATC ATG GAT 4644 Tyr Thr Leu He His Tyr He Asn Gin Arg Pro Ser Cys He Met Aεp 1470 1475 1480 1485 GTG TCA TTA CGT AGC TTC TCC CTT TGT TGT GAC TTA TTA AGT CAG GTT 4692 Val Ser Leu Arg Ser Phe Ser Leu Cys Cys Aεp Leu Leu Ser Gin Val 1490 1495 1500 TGC CAG ACA GCC GTG ACT TAC TGT AAG GAT GCT CTA GAA AAC CAT CTT 4740 Cyε Gin Thr Ala Val Thr Tyr Cys Lys Asp Ala Leu Glu Asn Hiε Leu 1505 1510 1515 CAT GTT ATT GTT GGT ACA CTT ATA CCC CTT GTG TAT GAG CAG GTG GAG 4788 His Val He Val Gly Thr Leu He Pro Leu Val Tyr Glu Gin Val Glu 1520 1525 1530 GTT CAG AAA CAG GTA TTG GAC TTG TTG AAA TAC TTA GTG ATA GAT AAC 4836 Val Gin Lys Gin Val Leu Asp Leu Leu Lys Tyr Leu Val He Asp Asn 1535 1540 1545 AAG GAT AAT GAA AAC CTC TAT ATC ACG ATT AAG CTT TTA GAT CCT TTT 4884 Lys Aεp Aεn Glu Aεn Leu Tyr He Thr He Lyε Leu Leu Asp Pro Phe 1550 1555 1560 1565 CCT GAC CAT GTT GTT TTT AAG GAT TTG CGT ATT ACT CAG CAA AAA ATC 4932 Pro Aεp His Val Val Phe Lys Asp Leu Arg He Thr Gin Gin Lyε He 1570 1575 1580 AAA TAC AGT AGA GGA CCC TTT TCA CTC TTG GAG GAA ATT AAC CAT TTT 4980 Lys Tyr Ser Arg Gly Pro Phe Ser Leu Leu Glu Glu He Asn Hiε Phe 1585 1590 1595 CTC TCA GTA AGT GTT TAT GAT GCA CTT CCA TTG ACA AGA CTT GAA GGA 5028 Leu Ser Val Ser Val Tyr Asp Ala Leu Pro Leu Thr Arg Leu Glu Gly 1600 1605 1610 CTA AAG GAT CTT CGA AGA CAA CTG GAA CTA CAT AAA GAT CAG ATG GTG 5076 Leu Lys Asp Leu Arg Arg Gin Leu Glu Leu His Lys Asp Gin Met Val 1615 1620 1625 GAC ATT ATG AGA GCT TCT CAG GAT AAT CCG CAA GAT GGG ATT ATG GTG 5124 Aεp He Met Arg Ala Ser Gin Aεp Aεn Pro Gin Aεp Gly He Met Val 1630 1635 1640 1645 AAA CTA GTT GTC AAT TTG TTG CAG TTA TCC AAG ATG GCA ATA AAC CAC 5172 Lys Leu Val Val Asn Leu Leu Gin Leu Ser Lys Met Ala He Asn Hiε 1650 1655 1660 ACT GGT GAA AAA GAA GTT CTA GAG GCT GTT GGA AGC TGC TTG GGA GAA 5220 Thr Gly Glu Lys Glu Val Leu Glu Ala Val Gly Ser Cys Leu Gly Glu 1665 1670 1675 GTG GGT CCT ATA GAT TTC TCT ACC ATA GCT ATA CAA CAT AGT AAA GAT 5268 Val Gly Pro He Aεp Phe Ser Thr He Ala He Gin His Ser Lyε Asp 1680 1685 1690 GCA TCT TAT ACC AAG GCC CTT AAG TTA TTT GAA GAT AAA GAA CTT CAG 5316 Ala Ser Tyr Thr Lys Ala Leu Lys Leu Phe Glu Asp Lyε Glu Leu Gin 1695 1700 1705 TGG ACC TTC ATA ATG CTG ACC TAC CTG AAT AAC ACA CTG GTA GAA GAT 5364 Trp Thr Phe He Met Leu Thr Tyr Leu Aεn Asn Thr Leu Val Glu Asp 1710 1715 1720 1725 TGT GTC AAA GTT CGA TCA GCA GCT GTT ACC TGT TTG AAA AAC ATT TTA 5412 Cyε Val Lys Val Arg Ser Ala Ala Val Thr Cys Leu Lys Asn He Leu 1730 1735 1740 GCC ACA AAG ACT GGA CAT AGT TTC TGG GAG ATT TAT AAG ATG ACA ACA 5460 Ala Thr Lys Thr Gly Hiε Ser Phe Trp Glu He Tyr Lys Met Thr Thr 1745 1750 1755 GAT CCA ATG CTG GCC TAT CTA CAG CCT TTT AGA ACA TCA AGA AAA AAG 5508 Asp Pro Met Leu Ala Tyr Leu Gin Pro Phe Arg Thr Ser Arg Lys Lys 1760 1765 1770 TTT TTA GAA GTA CCC AGA TTT GAC AAA GAA AAC CCT TTT GAA GGC CTG 5556 Phe Leu Glu Val Pro Arg Phe Aεp Lys Glu Asn Pro Phe Glu Gly Leu 1775 1780 1785 GAT GAT ATA AAT CTG TGG ATT CCT CTA AGT GAA AAT CAT GAC ATT TGG 5604 Asp Asp He Aεn Leu Trp He Pro Leu Ser Glu Asn His Asp He Trp 1790 1795 1800 1805 ATA AAG ACA CTG ACT TGT GCT TTT TTG GAC AGT GGA GGC ACA AAA TGT 5652 He Lys Thr Leu Thr Cys Ala Phe Leu Asp Ser Gly Gly Thr Lys Cys 1810 1815 1820 GAA ATT CTT CAA TTA TTA AAG CCA ATG TGT GAA GTG AAA ACT GAC TTT 5700 Glu He Leu Gin Leu Leu Lys Pro Met Cys Glu Val Lyε Thr Aεp Phe 1825 1830 1835 TGT CAG ACT GTA CTT CCA TAC TTG ATT CAT GAT ATT TTA CTC CAA GAT 5748 Cys Gin Thr Val Leu Pro Tyr Leu He His Asp He Leu Leu Gin Asp 1840 1845 1850 ACA AAT GAA TCA TGG AGA AAT CTG CTT TCT ACA CAT GTT CAG GGA TTT 5796 Thr Aεn Glu Ser Trp Arg Aεn Leu Leu Ser Thr His Val Gin Gly Phe 1855 1860 1865 TTC ACC AGC TGT CTT CGA CAC TTC TCG CAA ACG AGC CGA TCC ACA ACC 5844 Phe Thr Ser Cyε Leu Arg His Phe Ser Gin Thr Ser Arg Ser Thr Thr 1870 1875 1880 1885 CCT GCA AAC TTG GAT TCA GAG TCA GAG CAC TTT TTC CGA TGC TGT TTG 5892 Pro Ala Asn Leu Asp Ser Glu Ser Glu His Phe Phe Arg Cys Cys Leu 1890 1895 1900 GAT AAA AAA TCA CAA AGA ACA ATG CTT GCT GTT GTG GAC TAC ATG AGA 5940 Asp Lys Lyε Ser Gin Arg Thr Met Leu Ala Val Val Asp Tyr Met Arg 1905 1910 1915 AGA CAA AAG AGA CCT TCT TCA GGA ACA ATT TTT AAT GAT GCT TTC TGG 5988 Arg Gin Lys Arg Pro Ser Ser Gly Thr He Phe Asn Asp Ala Phe Trp 1920 1925 1930 CTG GAT TTA AAT TAT CTA GAA GTT GCC AAG GTA GCT CAG TCT TGT GCT 6036 Leu Asp Leu Asn Tyr Leu Glu Val Ala Lys Val Ala Gin Ser Cys Ala 1935 1940 1945 GCT CAC TTT ACA GCT TTA CTC TAT GCA GAA ATC TAT GCA GAT AAG AAA 6084 Ala His Phe Thr Ala Leu Leu Tyr Ala Glu He Tyr Ala Asp Lys Lys 1950 1955 1960 1965 AGT ATG GAT GAT CAA GAG AAA AGA AGT CTT GCA TTT GAA GAA GGA AGC 6132 Ser Met Asp Asp Gin Glu Lys Arg Ser Leu Ala Phe Glu Glu Gly Ser 1970 1975 1980 CAG AGT ACA ACT ATT TCT AGC TTG AGT GAA AAA AGT AAA GAA GAA ACT 6180 Gin Ser Thr Thr He Ser Ser Leu Ser Glu Lys Ser Lys Glu Glu Thr 1985 1990 1995 GGA ATA AGT TTA CAG GAT CTT CTC TTA GAA ATC TAC AGA AGT ATA GGG 6228 Gly He Ser Leu Gin Asp Leu Leu Leu Glu He Tyr Arg Ser He Gly 2000 2005 2010 GAG CCA GAT AGT TTG TAT GGC TGT GGT GGA GGG AAG ATG TTA CAA CCC 6276 Glu Pro Aεp Ser Leu Tyr Gly Cyε Gly Gly Gly Lyε Met Leu Gin Pro 2015 2020 2025 ATT ACT AGA CTA CGA ACA TAT GAA CAC GAA GCA ATG TGG GGC AAA GCC 6324 He Thr Arg Leu Arg Thr Tyr Glu His Glu Ala Met Trp Gly Lys Ala 2030 2035 2040 2045 CTA GTA ACA TAT GAC CTC GAA ACA GCA ATC CCC TCA TCA ACA CGC CAG 6372 Leu Val Thr Tyr Aεp Leu Glu Thr Ala He Pro Ser Ser Thr Arg Gin 2050 2055 2060 GCA GGA ATC ATT CAG GCC TTG CAG AAT TTG GGA CTC TGC CAT ATT CTT 6420 Ala Gly He He Gin Ala Leu Gin Asn Leu Gly Leu Cys His He Leu 2065 2070 2075 TCC GTC TAT TTA AAA GGA TTG GAT TAT GAA AAT AAA GAC TGG TGT CCT 6468 Ser Val Tyr Leu Lys Gly Leu Asp Tyr Glu Asn Lys Asp Trp Cys Pro 2080 2085 2090 GAA CTA GAA GAA CTT CAT TAC CAA GCA GCA TGG AGG AAT ATG CAG TGG 6516 Glu Leu Glu Glu Leu His Tyr Gin Ala Ala Trp Arg Asn Met Gin Trp 2095 2100 2105 GAC CAT TGC ACT TCC GTC AGC AAA GAA GTA GAA GGA ACC AGT TAC CAT 6564 Asp Hiε Cys Thr Ser Val Ser Lys Glu Val Glu Gly Thr Ser Tyr Hiε 2110 2115 2120 2125 GAA TCA TTG TAC AAT GCT CTA CAA TCT CTA AGA GAC AGA GAA TTC TCT 6612 Glu Ser Leu Tyr Asn Ala Leu Gin Ser Leu Arg Aεp Arg Glu Phe Ser 2130 2135 2140 ACA TTT TAT GAA AGT CTC AAA TAT GCC AGA GTA AAA GAA GTG GAA GAG 6660 Thr Phe Tyr Glu Ser Leu Lyε Tyr Ala Arg Val Lys Glu Val Glu Glu 2145 2150 2155 ATG TGT AAG CGC AGC CTT GAG TCT GTG TAT TCG CTC TAT CCC ACA CTT 6708 Met Cyε Lyε Arg Ser Leu Glu Ser Val Tyr Ser Leu Tyr Pro Thr Leu 2160 2165 2170 AGC AGG TTG CAG GCC ATT GGA GAG CTG GAA AGC ATT GGG GAG CTT TTC 6756 Ser Arg Leu Gin Ala He Gly Glu Leu Glu Ser He Gly Glu Leu Phe 2175 2180 2185 TCA AGA TCA GTC ACA CAT AGA CAA CTC TCT GAA GTA TAT ATT AAG TGG 6804 Ser Arg Ser Val Thr Hiε Arg Gin Leu Ser Glu Val Tyr He Lyε Trp 2190 2195 2200 2205 CAG AAA CAC TCC CAG CTT CTC AAG GAC AGT GAT TTT AGT TTT CAG GAG 6852 Gin Lys His Ser Gin Leu Leu Lyε Asp Ser Asp Phe Ser Phe Gin Glu 2210 2215 2220 CCT ATC ATG GCT CTA CGC ACA GTC ATT TTG GAG ATC CTG ATG GAA AAG 6900 Pro He Met Ala Leu Arg Thr Val He Leu Glu He Leu Met Glu Lyε 2225 2230 2235 GAA ATG GAC AAC TCA CAA AGA GAA TGT ATT AAG GAC ATT CTC ACC AAA 6948 Glu Met Aεp Aεn Ser Gin Arg Glu Cys He Lys Asp He Leu Thr Lys 2240 2245 2250 CAC CTT GTA GAA CTC TCT ATA CTG GCC AGA ACT TTC AAG AAC ACT CAG 6996 His Leu Val Glu Leu Ser He Leu Ala Arg Thr Phe Lys Asn Thr Gin 2255 2260 2265 CTC CCT GAA AGG GCA ATA TTT CAA ATT AAA CAG TAC AAT TCA GTT AGC 7044 Leu Pro Glu Arg Ala He Phe Gin He Lyε Gin Tyr Aεn Ser Val Ser 2270 2275 2280 2285 TGT GGA GTC TCT GAG TGG CAG CTG GAA GAA GCA CAA GTA TTC TGG GCA 7092 Cys Gly Val Ser Glu Trp Gin Leu Glu Glu Ala Gin Val Phe Trp Ala 2290 2295 2300 AAA AAG GAG CAG AGT CTT GCC CTG AGT ATT CTC AAG CAA ATG ATC AAG 7140 Lys Lys Glu Gin Ser Leu Ala Leu Ser He Leu Lyε Gin Met He Lys 2305 2310 2315 AAG TTG GAT GCC AGC TGT GCA GCG AAC AAT CCC AGC CTA AAA CTT ACA 7188 Lys Leu Asp Ala Ser Cys Ala Ala Asn Asn Pro Ser Leu Lys Leu Thr 2320 2325 2330 TAC ACA GAA TGT CTG AGG GTT TGT GGC AAC TGG TTA GCA GAA ACG TGC 7236 Tyr Thr Glu Cys Leu Arg Val Cys Gly Asn Trp Leu Ala Glu Thr Cys 2335 2340 2345 TTA GAA AAT CCT GCG GTC ATC ATG CAG ACC TAT CTA GAA AAG GCA GTA 7284 Leu Glu Aεn Pro Ala Val He Met Gin Thr Tyr Leu Glu Lys Ala Val 2350 2355 2360 2365 GAA GTT GCT GGA AAT TAT GAT GGA GAA AGT AGT GAT GAG CTA AGA AAT 7332 Glu Val Ala Gly Asn Tyr Asp Gly Glu Ser Ser Asp Glu Leu Arg Asn 2370 2375 2380 GGA AAA ATG AAG GCA TTT CTC TCA TTA GCC CGG TTT TCA GAT ACT CAA 7380 Gly Lys Met Lys Ala Phe Leu Ser Leu Ala Arg Phe Ser Asp Thr Gin 2385 2390 2395 TAC CAA AGA ATT GAA AAC TAC ATG AAA TCA TCG GAA TTT GAA AAC AAG 7428 Tyr Gin Arg He Glu Aεn Tyr Met Lyε Ser Ser Glu Phe Glu Aεn Lyε 2400 2405 2410 CAA GCT CTC CTG AAA AGA GCC AAA GAG GAA GTA GGT CTC CTT AGG GAA 7476 Gin Ala Leu Leu Lyε Arg Ala Lyε Glu Glu Val Gly Leu Leu Arg Glu 2415 2420 2425 CAT AAA ATT CAG ACA AAC AGA TAC ACA GTA AAG GTT CAG CGA GAG CTG 7524 His Lys He Gin Thr Asn Arg Tyr Thr Val Lys Val Gin Arg Glu Leu 2430 2435 2440 2445 GAG TTG GAT GAA TTA GCC CTG CGT GCA CTG AAA GAG GAT CGT AAA CGC 7572 Glu Leu Asp Glu Leu Ala Leu Arg Ala Leu Lys Glu Aεp Arg Lyε Arg 2450 2455 2460 TTC TTA TGT AAA GCA GTT GAA AAT TAT ATC AAC TGC TTA TTA AGT GGA 7620 Phe Leu Cyε Lys Ala Val Glu Asn Tyr He Asn Cys Leu Leu Ser Gly 2465 2470 2475 GAA GAA CAT GAT ATG TGG GTA TTC CGG CTT TGT TCC CTC TGG CTT GAA 7668 Glu Glu Hiε Aεp Met Trp Val Phe Arg Leu Cys Ser Leu Trp Leu Glu 2480 2485 2490 AAT TCT GGA GTT TCT GAA GTC AAT GGC ATG ATG AAG AGA GAC GGA ATG 7716 Asn Ser Gly Val Ser Glu Val Asn Gly Met Met Lys Arg Asp Gly Met 2495 2500 2505 AAG ATT CCA ACA TAT AAA TTT TTG CCT CTT ATG TAC CAA TTG GCT GCT 7764 Lys He Pro Thr Tyr Lys Phe Leu Pro Leu Met Tyr Gin Leu Ala Ala 2510 2515 2520 2525 AGA ATG GGG ACC AAG ATG ATG GGA GGC CTA GGA TTT CAT GAA GTC CTC 7812 Arg Met Gly Thr Lyε Met Met Gly Gly Leu Gly Phe His Glu Val Leu 2530 2535 2540 AAT AAT CTA ATC TCT AGA ATT TCA ATG GAT CAC CCC CAT CAC ACT TTG 7860 Asn Asn Leu He Ser Arg He Ser Met Aεp His Pro His His Thr Leu 2545 2550 2555 TTT ATT ATA CTG GCC TTA GCA AAT GCA AAC AGA GAT GAA TTT CTG ACT 7908 Phe He He Leu Ala Leu Ala Aεn Ala Asn Arg Asp Glu Phe Leu Thr 2560 2565 2570 AAA CCA GAG GTA GCC AGA AGA AGC AGA ATA ACT AAA AAT GTG CCT AAA 7956 Lys Pro Glu Val Ala Arg Arg Ser Arg He Thr Lys Asn Val Pro Lys 2575 2580 2585 CAA AGC TCT CAG CTT GAT GAG GAT CGA ACA GAG GCT GCA AAT AGA ATA 8004 Gin Ser Ser Gin Leu Asp Glu Asp Arg Thr Glu Ala Ala Asn Arg He 2590 2595 2600 2605 ATA TGT ACT ATC AGA AGT AGG AGA CCT CAG ATG GTC AGA AGT GTT GAG 8052 He Cys Thr He Arg Ser Arg Arg Pro Gin Met Val Arg Ser Val Glu 2610 2615 2620 GCA CTT TGT GAT GCT TAT ATT ATA TTA GCA AAC TTA GAT GCC ACT CAG 8100 Ala Leu Cys Asp Ala Tyr He He Leu Ala Asn Leu Asp Ala Thr Gin 2625 2630 2635 TGG AAG ACT CAG AGA AAA GGC ATA AAT ATT CCA GCA GAC CAG CCA ATT 8148 Trp Lys Thr Gin Arg Lyε Gly He Asn He Pro Ala Asp Gin Pro He 2640 2645 2650 ACT AAA CTT AAG AAT TTA GAA GAT GTT GTT GTC CCT ACT ATG GAA ATT 8196 Thr Lys Leu Lys Asn Leu Glu Asp Val Val Val Pro Thr Met Glu He 2655 2660 2665 AAG GTG GAC CAC ACA GGA GAA TAT GGA AAT CTG GTG ACT ATA CAG TCA 8244 Lys Val Asp Hiε Thr Gly Glu Tyr Gly Aεn Leu Val Thr He Gin Ser 2670 2675 2680 2685 TTT AAA GCA GAA TTT CGC TTA GCA GGA GGT GTA AAT TTA CCA AAA ATA 8292 Phe Lyε Ala Glu Phe Arg Leu Ala Gly Gly Val Aεn Leu Pro Lys He 2690 2695 2700 ATA GAT TGT GTA GGT TCC GAT GGC AAG GAG AGG AGA CAG CTT GTT AAG 8340 He Asp Cys Val Gly Ser Aεp Gly Lyε Glu Arg Arg Gin Leu Val Lyε 2705 2710 2715 GGC CGT GAT GAC CTG AGA CAA GAT GCT GTC ATG CAA CAG GTC TTC CAG 8388 Gly Arg Aεp Aεp Leu Arg Gin Aεp Ala Val Met Gin Gin Val Phe Gin 2720 2725 2730 ATG TGT AAT ACA TTA CTG CAG AGA AAC ACG GAA ACT AGG AAG AGG AAA 8436 Met Cyε Aεn Thr Leu Leu Gin Arg Aεn Thr Glu Thr Arg Lyε Arg Lyε 2735 2740 2745 TTA ACT ATC TGT ACT TAT AAG GTG GTT CCC CTC TCT CAG CGA AGT GGT 8484 Leu Thr He Cys Thr Tyr Lys Val Val Pro Leu Ser Gin Arg Ser Gly 2750 2755 2760 2765 GTT CTT GAA TGG TGC ACA GGA ACT GTC CCC ATT GGT GAA TTT CTT GTT 8532 Val Leu Glu Trp Cys Thr Gly Thr Val Pro He Gly Glu Phe Leu Val 2770 2775 2780 AAC AAT GAA GAT GGT GCT CAT AAA AGA TAC AGG CCA AAT GAT TTC AGT 8580 Asn Asn Glu Aεp Gly Ala His Lyε Arg Tyr Arg Pro Asn Asp Phe Ser 2785 2790 2795 GCC TTT CAG TGC CAA AAG AAA ATG ATG GAG GTG CAA AAA AAG TCT TTT 8628 Ala Phe Gin Cyε Gin Lyε Lys Met Met Glu Val Gin Lyε Lyε Ser Phe 2800 2805 2810 GAA GAG AAA TAT GAA GTC TTC ATG GAT GTT TGC CAA AAT TTT CAA CCA 8676 Glu Glu Lyε Tyr Glu Val Phe Met Aεp Val Cyε Gin Aεn Phe Gin Pro 2815 2820 2825 GTT TTC CGT TAC TTC TGC ATG GAA AAA TTC TTG GAT CCA GCT ATT TGG 8724 Val Phe Arg Tyr Phe Cyε Met Glu Lys Phe Leu Asp Pro Ala He Trp 2830 2835 2840 2845 TTT GAG AAG CGA TTG GCT TAT ACG CGC AGT GTA GCT ACT TCT TCT ATT 8772 Phe Glu Lys Arg Leu Ala Tyr Thr Arg Ser Val Ala Thr Ser Ser He 2850 2855 2860 GTT GGT TAC ATA CTT GGA CTT GGT GAT AGA CAT GTA CAG AAT ATC TTG 8820 Val Gly Tyr He Leu Gly Leu Gly Aεp Arg His Val Gin Aεn He Leu 2865 2870 2875 ATA AAT GAG CAG TCA GCA GAA CTT GTA CAT ATA GAT CTA GGT GTT GCT 8868 He Aεn Glu Gin Ser Ala Glu Leu Val His He Asp Leu Gly Val Ala 2880 2885 2890 TTT GAA CAG GGC AAA ATC CTT CCT ACT CCT GAG ACA GTT CCT TTT AGA 8916 Phe Glu Gin Gly Lyε He Leu Pro Thr Pro Glu Thr Val Pro Phe Arg 2895 2900 2905 CTC ACC AGA GAT ATT GTG GAT GGC ATG GGC ATT ACG GGT GTT GAA GGT 8964 Leu Thr Arg Asp He Val Aεp Gly Met Gly He Thr Gly Val Glu Gly 2910 2915 2920 2925 GTC TTC AGA AGA TGC TGT GAG AAA ACC ATG GAA GTG ATG AGA AAC TCT 9012 Val Phe Arg Arg Cyε Cys Glu Lys Thr Met Glu Val Met Arg Asn Ser 2930 2935 2940 CAG GAA ACT CTG TTA ACC ATT GTA GAG GTC CTT CTA TAT GAT CCA CTC 9060 Gin Glu Thr Leu Leu Thr He Val Glu Val Leu Leu Tyr Asp Pro Leu 2945 2950 2955 TTT GAC TGG ACC ATG AAT CCT TTG AAA GCT TTG TAT TTA CAG CAG AGG 9108 Phe Asp Trp Thr Met Asn Pro Leu Lys Ala Leu Tyr Leu Gin Gin Arg 2960 2965 2970 CCG GAA GAT GAA ACT GAG CTT CAC CCT ACT CTG AAT GCA GAT GAC CAA 9156 Pro Glu Asp Glu Thr Glu Leu Hiε Pro Thr Leu Asn Ala Asp Aεp Gin 2975 2980 2985 GAA TGC AAA CGA AAT CTC AGT GAT ATT GAC CAG AGT TTC GAC AAA GTA 9204 Glu Cyε Lys Arg Asn Leu Ser Asp He Asp Gin Ser Phe Asp Lyε Val 2990 2995 3000 3005 GCT GAA CGT GTC TTA ATG AGA CTA CAA GAG AAA CTG AAA GGA GTG GAA 9252 Ala Glu Arg Val Leu Met Arg Leu Gin Glu Lyε Leu Lyε Gly Val Glu 3010 3015 3020 GAA GGC ACT GTG CTC AGT GTT GGT GGA CAG GTG AAT TTG CTC ATA CAG 9300 Glu Gly Thr Val Leu Ser Val Gly Gly Gin Val Aεn Leu Leu He Gin 3025 3030 3035 CAG GCC ATA GAC CCC AAA AAT CTC AGC CGA CTT TTC CCA GGA TGG AAA 9348 Gin Ala He Asp Pro Lys Asn Leu Ser Arg Leu Phe Pro Gly Trp Lyε 3040 3045 3050 GCT TGG GTG TGATCTTCAG TATATGAATT ACCCTTTC 9385 Ala Trp Val 3055 (2) INFORMATION FOR SEQ ID NO:35- U) SEQUENCE CHARACTERISTICS- (A) LENGTH: 3056 am o acids (D) TOPOLOGY: linear Ui) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:35: Met Ser Leu Val Leu Asn Asp Leu Leu He Cys Cys Arg Gin Leu Glu 1 5 10 15 His Aεp Arg Ala Thr Glu Arg Lys Lyε Glu Val Glu Lys Phe Lys Arg 20 25 30 Leu He Arg Asp Pro Glu Thr He Lys His Leu Asp Arg His Ser Asp 35 40 45 Ser Lys Gin Gly Lys Tyr Leu Asn Trp Asp Ala Val Phe Arg Phe Leu 50 55 60 Gin Lys Tyr He Gin Lys Glu Thr Glu Cys Leu Arg He Ala Lys Pro 65 70 75 80 Asn Val Ser Ala Ser Thr Gin Ala Ser Arg Gin Lys Lys Met Gin Glu 85 90 95 He Ser Ser Leu Val Lys Tyr Phe He Lys Cyε Ala Asn Arg Arg Ala 100 105 110 Pro Arg Leu Lys Cyε Gin Glu Leu Leu Asn Tyr He Met Asp Thr Val 115 120 125 Lys Aεp Ser Ser Aεn Gly Ala He Tyr Gly Ala Aεp Cys Ser Asn He 130 135 140 Leu Leu Lys Asp He Leu Ser Val Arg Lys Tyr Trp Cys Glu He Ser 145 150 155 160 Gin Gin Gin Trp Leu Glu Leu Phe Ser Val Tyr Phe Arg Leu Tyr Leu 165 170 175 Lys Pro Ser Gin Asp Val His Arg Val Leu Val Ala Arg He He His 180 185 190 Ala Val Thr Lyε Gly Cyε Cys Ser Gin Thr Aεp Gly Leu Aεn Ser Lyε 195 200 205 Phe Leu Asp Phe Phe Ser Lys Ala He Gin Cys Ala Arg Gin Glu Lys 210 215 220 Ser Ser Ser Gly Leu Aεn His He Leu Ala Ala Leu Thr He Phe Leu 225 230 235 240 Lyε Thr Leu Ala Val Aεn Phe Arg He Arg Val Cyε Glu Leu Gly Aεp 245 250 255 Glu He Leu Pro Thr Leu Leu Tyr He Trp Thr Gin His Arg Leu Aεn 260 265 270 Aεp Ser Leu Lyε Glu Val He He Glu Leu Phe Gin Leu Gin He Tyr 275 280 285 He His His Pro Lys Gly Ala Lys Thr Gin Glu Lys Gly Ala Tyr Glu 290 295 300 Ser Thr Lyε Trp Arg Ser He Leu Tyr Asn Leu Tyr Asp Leu Leu Val 305 310 315 320 Asn Glu He Ser Hiε He Gly Ser Arg Gly Lyε Tyr Ser Ser Gly Phe 325 330 335 Arg Aεn He Ala Val Lyε Glu Asn Leu He Glu Leu Met Ala Asp He 340 345 350 Cys His Gin Val Phe Asn Glu Asp Thr Arg Ser Leu Glu He Ser Gin 355 360 365 Ser Tyr Thr Thr Thr Gin Arg Glu Ser Ser Asp Tyr Ser Val Pro Cyε 370 375 380 Lys Arg Lyε Lyε He Glu Leu Gly Trp Glu Val He Lys Asp His Leu 385 390 395 400 Gin Lys Ser Gin Asn Asp Phe Asp Leu Val Pro Trp Leu Gin He Ala 405 410 415 Thr Gin Leu He Ser Lys Tyr Pro Ala Ser Leu Pro Asn Cys Glu Leu 420 425 430 Ser Pro Leu Leu Met He Leu Ser Gin Leu Leu Pro Gin Gin Arg Hiε 435 440 445 Gly Glu Arg Thr Pro Tyr Val Leu Arg Cyε Leu Thr Glu Val Ala Leu 450 455 460 Cys Gin Aεp Lyε Arg Ser Asn Leu Glu Ser Ser Gin Lyε Ser Aεp Leu 465 470 475 480 Leu Lys Leu Trp Asn Lys He Trp Cys He Thr Phe Arg Gly He Ser 485 490 495 Ser Glu Gin He Gin Ala Glu Asn Phe Gly Leu Leu Gly Ala He He 500 505 510 Gin Gly Ser Leu Val Glu Val Asp Arg Glu Phe Trp Lys Leu Phe Thr 515 520 525 Gly Ser Ala Cys Arg Pro Ser Cys Pro Ala Val Cys Cys Leu Thr Leu 530 535 540 Ala Leu Thr Thr Ser He Val Pro Gly Ala Val Lys Met Gly He Glu 545 550 555 560 Gin Aεn Met Cys Glu Val Asn Arg Ser Phe Ser Leu Lys Glu Ser He 565 570 575 Met Lys Trp Leu Leu Phe Tyr Gin Leu Glu Gly Asp Leu Glu Asn Ser 580 585 590 Thr Glu Val Pro Pro He Leu His Ser Asn Phe Pro His Leu Val Leu 595 600 605 Glu Lys He Leu Val Ser Leu Thr Met Lyε Aεn Cyε Lyε Ala Ala Met 610 615 620 Asn Phe Phe Gin Ser Val Pro Glu Cyε Glu His Hiε Gin Lyε Aεp Lys 625 630 635 640 Glu Glu Leu Ser Phe Ser Glu Val Glu Glu Leu Phe Leu Gin Thr Thr 645 650 655 Phe Aεp Lys Met Asp Phe Leu Thr He Val Arg Glu Cyε Gly He Glu 660 665 670 Lys His Gin Ser Ser He Gly Phe Ser Val His Gin Asn Leu Lys Glu 675 680 685 Ser Leu Aεp Arg Cyε Leu Leu Gly Leu Ser Glu Gin Leu Leu Aεn Aεn 690 695 700 Tyr Ser Ser Glu He Thr Asn Ser Glu Thr Leu Val Arg Cys Ser Arg 705 710 715 720 Leu Leu Val Gly Val Leu Gly Cyε Tyr Cyε Tyr Met Gly Val He Ala 725 730 735 Glu Glu Glu Ala Tyr Lyε Ser Glu Leu Phe Gin Lyε Ala Aεn Ser Leu 740 745 750 Met Gin Cys Ala Gly Glu Ser He Thr Leu Phe Lyε Aεn Lyε Thr Aεn 755 760 765 Glu Glu Phe Arg He Gly Ser Leu Arg Aεn Met Met Gin Leu Cyε Thr 770 775 780 Arg Cys Leu Ser Asn Cyε Thr Lyε Lyε Ser Pro Asn Lys He Ala Ser 785 790 795 800 Gly Phe Phe Leu Arg Leu Leu Thr Ser Lys Leu Met Asn Asp He Ala 805 810 815 Asp He Cys Lyε Ser Leu Ala Ser Phe He Lyε Lyε Pro Phe Asp Arg 820 825 830 Gly Glu Val Glu Ser Met Glu Asp Asp Thr Asn Gly Asn Leu Met Glu 835 840 845 Val Glu Asp Gin Ser Ser Met Asn Leu Phe Asn Asp Tyr Pro Asp Ser 850 855 860 Ser Val Ser Asp Ala Aεn Glu Pro Gly Glu Ser Gin Ser Thr He Gly 865 870 875 880 Ala He Aεn Pro Leu Ala Glu Glu Tyr Leu Ser Lys Gin Asp Leu Leu 885 890 895 Phe Leu Aεp Met Leu Lys Phe Leu Cys Leu Cyε Val Thr Thr Ala Gin 900 9U5 910 Thr Asn Thr Val Ser Phe Arg Ala Ala Asp He Arg Arg Lys Leu Leu 915 920 925 Met Leu He Asp Ser Ser Thr Leu Glu Pro Thr Lys Ser Leu Hiε Leu 930 935 940 His Met Tyr Leu Met Leu Leu Lyε Glu Leu Pro Gly Glu Glu Tyr Pro 945 950 955 960 Leu Pro Met Glu Aεp Val Leu Glu Leu Leu Lyε Pro Leu Ser Aεn Val 965 970 975 Cyε Ser Leu Tyr Arg Arg Aεp Gin Asp Val Cys Lys Thr He Leu Aεn 980 985 990 Hiε Val Leu His Val Val Lys Asn Leu Gly Gin Ser Asn Met Aεp Ser 995 1000 1005 Glu Asn Thr Arg Asp Ala Gin Gly Gin Phe Leu Thr Val He Gly Ala 1010 1015 1020 Phe Trp His Leu Thr Lyε Glu Arg Lyε Tyr He Phe Ser Val Arg Met 1025 1030 1035 1040 Ala Leu Val Aεn Cyε Leu Lys Thr Leu Leu Glu Ala Asp Pro Tyr Ser 1045 1050 1055 Lys Trp Ala He Leu Asn Val Met Gly Lys Aεp Phe Pro Val Aεn Glu 1060 1065 1070 Val Phe Thr Gin Phe Leu Ala Asp Asn His Hiε Gin Val Arg Met Leu 1075 1080 1085 Ala Ala Glu Ser He Asn Arg Leu Phe Gin Asp Thr Lys Gly Asp Ser 1090 1095 1100 Ser Arg Leu Leu Lys Ala Leu Pro Leu Lys Leu Gin Gin Thr Ala Phe 1105 1110 1115 1120 Glu Asn Ala Tyr Leu Lys Ala Gin Glu Gly Met Arg Glu Met Ser His 1125 1130 1135 Ser Ala Glu Asn Pro Glu Thr Leu Asp Glu He Tyr Asn Arg Lyε Ser 1140 1145 1150 Val Leu Leu Thr Leu He Ala Val Val Leu Ser Cyε Ser Pro He Cyε 1155 1160 1165 Glu Lyε Gin Ala Leu Phe Ala Leu Cyε Lyε Ser Val Lyε Glu Aεn Gly 1170 1175 1180 Leu Glu Pro His Leu Val Lys Lys Val Leu Glu Lys Val Ser Glu Thr 1185 1190 1195 1200 Phe Gly Tyr Arg Arg Leu Glu Asp Phe Met Ala Ser His Leu Asp Tyr 1205 1210 1215 Leu Val Leu Glu Trp Leu Aεn Leu Gin Aεp Thr Glu Tyr Aεn Leu Ser 1220 1225 1230 Ser Phe Pro Phe He Leu Leu Aεn Tyr Thr Asn He Glu Asp Phe Tyr 1235 1240 1245 Arg Ser Cyε Tyr Lys Val Leu He Pro His Leu Val He Arg Ser His 1250 1255 1260 Phe Asp Glu Val Lys Ser He Ala Asn Gin He Gin Glu Asp Trp Lys 1265 1270 1275 1280 Ser Leu Leu Thr Asp Cys Phe Pro Lys He Leu Val Asn He Leu Pro 1285 1290 1295 Tyr Phe Ala Tyr Glu Gly Thr Arg Asp Ser Gly Met Ala Gin Gin Arg 1300 1305 1310 Glu Thr Ala Thr Lyε Val Tyr Aεp Met Leu Lyε Ser Glu Asn Leu Leu 1315 1320 1325 Gly Lys Gin He Aεp Hiε Leu Phe He Ser Aεn Leu Pro Glu He Val 1330 1335 1340 Val Glu Leu Leu Met Thr Leu Hiε Glu Pro Ala Asn Ser Ser Ala Ser 1345 1350 1355 1360 Gin Ser Thr Asp Leu Cys Aεp Phe Ser Gly Aεp Leu Asp Pro Ala Pro 1365 1370 1375 Aεn Pro Pro Hiε Phe Pro Ser His Val He Lys Ala Thr Phe Ala Tyr 1380 1385 1390 He Ser Asn Cys Hiε Lyε Thr Lys Leu Lyε Ser He Leu Glu He Leu 1395 1400 1405 Ser Lyε Ser Pro Asp Ser Tyr Gin Lyε He Leu Leu Ala He Cyε Glu 1410 1415 1420 Gin Ala Ala Glu Thr Asn Asn Val Tyr Lys Lyε His Arg He Leu Lys 1425 1430 1435 1440 He Tyr His Leu Phe Val Ser Leu Leu Leu Lys Asp He Lys Ser Gly 1445 1450 1455 Leu Gly Gly Ala Trp Ala Phe Val Leu Arg Asp Val He Tyr Thr Leu 1460 1465 1470 He Hiε Tyr He Aεn Gin Arg Pro Ser Cyε He Met Aεp Val Ser Leu 1475 1480 1485 Arg Ser Phe Ser Leu Cyε Cys Asp Leu Leu Ser Gin Val Cys Gin Thr 1490 1495 1500 Ala Val Thr Tyr Cys Lys Asp Ala Leu Glu Aεn Hiε Leu His Val He 1505 1510 1515 1520 Val Gly Thr Leu He Pro Leu Val Tyr Glu Gin Val Glu Val Gin Lyε 1525 1530 1535 Gin Val Leu Aεp Leu Leu Lys Tyr Leu Val He Asp Asn Lyε Aεp Asn 1540 1545 1550 Glu Asn Leu Tyr He Thr He Lys Leu Leu Asp Pro Phe Pro Asp His 1555 1560 1565 Val Val Phe Lys Asp Leu Arg He Thr Gin Gin Lys He Lys Tyr Ser 1570 1575 1580 Arg Gly Pro Phe Ser Leu Leu Glu Glu He Asn His Phe Leu Ser Val 1585 1590 1595 1600 Ser Val Tyr Asp Ala Leu Pro Leu Thr Arg Leu Glu Gly Leu Lys Asp 1605 1610 1615 Leu Arg Arg Gin Leu Glu Leu His Lys Asp Gin Met Val Asp He Met 1620 1625 1630 Arg Ala Ser Gin Asp Asn Pro Gin Asp Gly He Met Val Lys Leu Val 1635 1640 1645 Val Asn Leu Leu Gin Leu Ser Lys Met Ala He Asn His Thr Gly Glu 1650 1655 1660 Lys Glu Val Leu Glu Ala Val Gly Ser Cys Leu Gly Glu Val Gly Pro 1665 1670 1675 1680 He Aεp Phe Ser Thr He Ala He Gin His Ser Lys Asp Ala Ser Tyr 1685 1690 1695 Thr Lyε Ala Leu Lyε Leu Phe Glu Asp Lyε Glu Leu Gin Trp Thr Phe 1700 1705 1710 He Met Leu Thr Tyr Leu Aεn Aεn Thr Leu Val Glu Aεp Cyε Val Lyε 1715 1720 1725 Val Arg Ser Ala Ala Val Thr Cyε Leu Lys Asn He Leu Ala Thr Lys 1730 1735 1740 Thr Gly His Ser Phe Trp Glu He Tyr Lys Met Thr Thr Aεp Pro Met 1745 1750 1755 1760 Leu Ala Tyr Leu Gin Pro Phe Arg Thr Ser Arg Lys Lys Phe Leu Glu 1765 1770 1775 Val Pro Arg Phe Asp Lys Glu Asn Pro Phe Glu Gly Leu Asp Asp He 1780 1785 1790 Asn Leu Trp He Pro Leu Ser Glu Asn His Asp He Trp He Lys Thr 1795 1800 1805 Leu Thr Cys Ala Phe Leu Asp Ser Gly Gly Thr Lys Cyε Glu He Leu 1810 1815 1820 Gin Leu Leu Lyε Pro Met Cyε Glu Val Lyε Thr Aεp Phe Cyε Gin Thr 1825 1830 1835 1840 Val Leu Pro Tyr Leu He Hiε Aεp He Leu Leu Gin Asp Thr Aεn Glu 1845 1850 1855 Ser Trp Arg Aεn Leu Leu Ser Thr His Val Gin Gly Phe Phe Thr Ser 1860 1865 1870 Cys Leu Arg His Phe Ser Gin Thr Ser Arg Ser Thr Thr Pro Ala Aεn 1875 1880 1885 Leu Aεp Ser Glu Ser Glu Hiε Phe Phe Arg Cyε Cys Leu Asp Lys Lys 1890 1895 1900 Ser Gin Arg Thr Met Leu Ala Val Val Asp Tyr Met Arg Arg Gin Lys 1905 1910 1915 1920 Arg Pro Ser Ser Gly Thr He Phe Aεn Asp Ala Phe Trp Leu Asp Leu 1925 1930 1935 Asn Tyr Leu Glu Val Ala Lys Val Ala Gin Ser Cyε Ala Ala Hiε Phe 1940 1945 1950 Thr Ala Leu Leu Tyr Ala Glu He Tyr Ala Aεp Lys Lyε Ser Met Asp 1955 1960 1965 Asp Gin Glu Lys Arg Ser Leu Ala Phe Glu Glu Gly Ser Gin Ser Thr 1970 1975 1980 Thr He Ser Ser Leu Ser Glu Lys Ser Lys Glu Glu Thr Gly He Ser 1985 1990 1995 2000 Leu Gin Asp Leu Leu Leu Glu He Tyr Arg Ser He Gly Glu Pro Asp 2005 2010 2015 Ser Leu Tyr Gly Cyε Gly Gly Gly Lys Met Leu Gin Pro He Thr Arg 2020 2025 2030 Leu Arg Thr Tyr Glu His Glu Ala Met Trp Gly Lyε Ala Leu Val Thr 2035 2040 2045 Tyr Asp Leu Glu Thr Ala He Pro Ser Ser Thr Arg Gin Ala Gly He 2050 2055 2060 He Gin Ala Leu Gin Aεn Leu Gly Leu Cys His He Leu Ser Val Tyr 2065 2070 2075 2080 Leu Lys Gly Leu Asp Tyr Glu Asn Lys Asp Trp Cys Pro Glu Leu Glu 2085 2090 2095 Glu Leu His Tyr Gin Ala Ala Trp Arg Aεn Met Gin Trp Aεp Hiε Cyε 2100 2105 2110 Thr Ser Val Ser Lyε Glu Val Glu Gly Thr Ser Tyr Hiε Glu Ser Leu 2115 2120 2125 Tyr Aεn Ala Leu Gin Ser Leu Arg Aεp Arg Glu Phe Ser Thr Phe Tyr 2130 2135 2140 Glu Ser Leu Lys Tyr Ala Arg Val Lyε Glu Val Glu Glu Met Cyε Lyε 2145 2150 2155 2160 Arg Ser Leu Glu Ser Val Tyr Ser Leu Tyr Pro Thr Leu Ser Arg Leu 2165 2170 2175 Gin Ala He Gly Glu Leu Glu Ser He Gly Glu Leu Phe Ser Arg Ser 2180 2185 2190 Val Thr His Arg Gin Leu Ser Glu Val Tyr He Lyε Trp Gin Lys Hiε 2195 2200 2205 Ser Gin Leu Leu Lyε Asp Ser Asp Phe Ser Phe Gin Glu Pro He Met 2210 2215 2220 Ala Leu Arg Thr Val He Leu Glu He Leu Met Glu Lys Glu Met Asp 2225 2230 2235 2240 Asn Ser Gin Arg Glu Cys He Lys Asp He Leu Thr Lys His Leu Val 2245 2250 2255 Glu Leu Ser He Leu Ala Arg Thr Phe Lyε Aεn Thr Gin Leu Pro Glu 2260 2265 2270 Arg Ala He Phe Gin He Lys Gin Tyr Asn Ser Val Ser Cyε Gly Val 2275 2280 2285 Ser Glu Trp Gin Leu Glu Glu Ala Gin Val Phe Trp Ala Lyε Lyε Glu 2290 2295 2300 Gln Ser Leu Ala Leu Ser He Leu Lyε Gin Met He Lys Lys Leu Asp 2305 2310 2315 2320 Ala Ser Cyε Ala Ala Aεn Asn Pro Ser Leu Lys Leu Thr Tyr Thr Glu 2325 2330 2335 Cys Leu Arg Val Cys Gly Asn Trp Leu Ala Glu Thr Cyε Leu Glu Asn 2340 2345 2350 Pro Ala Val He Met Gin Thr Tyr Leu Glu Lys Ala Val Glu Val Ala 2355 2360 2365 Gly Asn Tyr Asp Gly Glu Ser Ser Asp Glu Leu Arg Aεn Gly Lyε Met 2370 2375 2380 Lys Ala Phe Leu Ser Leu Ala Arg Phe Ser Asp Thr Gin Tyr Gin Arg 2385 2390 2395 2400 He Glu Asn Tyr Met Lys Ser Ser Glu Phe Glu Aεn Lyε Gin Ala Leu 2405 2410 2415 Leu Lyε Arg Ala Lyε Glu Glu Val Gly Leu Leu Arg Glu Hiε Lyε He 2420 2425 2430 Gin Thr Aεn Arg Tyr Thr Val Lys Val Gin Arg Glu Leu Glu Leu Asp 2435 2440 2445 Glu Leu Ala Leu Arg Ala Leu Lyε Glu Aεp Arg Lyε Arg Phe Leu Cys 2450 2455 2460 Lys Ala Val Glu Asn Tyr He Asn Cyε Leu Leu Ser Gly Glu Glu Hiε 2465 2470 2475 2480 Aεp Met Trp Val Phe Arg Leu Cyε Ser Leu Trp Leu Glu Asn Ser Gly 2485 2490 2495 Val Ser Glu Val Asn Gly Met Met Lys Arg Aεp Gly Met Lyε He Pro 2500 2505 2510 Thr Tyr Lys Phe Leu Pro Leu Met Tyr Gin Leu Ala Ala Arg Met Gly 2515 2520 2525 Thr Lys Met Met Gly Gly Leu Gly Phe His Glu Val Leu Asn Asn Leu 2530 2535 2540 He Ser Arg He Ser Met Asp His Pro His His Thr Leu Phe He He 2545 2550 2555 2560 Leu Ala Leu Ala Asn Ala Asn Arg Asp Glu Phe Leu Thr Lys Pro Glu 2565 2570 2575 Val Ala Arg Arg Ser Arg He Thr Lys Asn Val Pro Lyε Gin Ser Ser 2580 2585 2590 Gin Leu Asp Glu Asp Arg Thr Glu Ala Ala Aεn Arg He He Cyε Thr 2595 2600 2605 He Arg Ser Arg Arg Pro Gin Met Val Arg Ser Val Glu Ala Leu Cys 2610 2615 2620 Asp Ala Tyr He He Leu Ala Asn Leu Asp Ala Thr Gin Trp Lyε Thr 2625 2630 2635 2640 Gin Arg Lyε Gly He Aεn He Pro Ala Aεp Gin Pro He Thr Lyε Leu 2645 2650 2655 Lvs Asn Leu Glu Asp Val Val Val Pro Thr Met Glu He Lys Val Asp 2660 2665 2670 His Thr Gly Glu Tyr Gly Asn Leu Val Thr He Gin Ser Phe Lys Ala 2675 2680 2685 Glu Phe Arg Leu Ala Gly Gly Val Aεn Leu Pro Lyε He He Aεp Cys 2690 2695 2700 Val Gly Ser Asp Gly Lys Glu Arg Arg Gin Leu Val Lys Gly Arg Asp 2705 2710 2715 2720 Asp Leu Arg Gin Asp Ala Val Met Gin Gin Val Phe Gin Met Cyε Aεn 2725 2730 2735 Thr Leu Leu Gin Arg Asn Thr Glu Thr Arg Lys Arg Lys Leu Thr He 2740 2745 2750 Cys Thr Tyr Lys Val Val Pro Leu Ser Gin Arg Ser Gly Val Leu Glu 2755 2760 2765 Trp Cys Thr Gly Thr Val Pro He Gly Glu Phe Leu Val Asn Asn Glu 2770 2775 2780 Aεp Gly Ala His Lys Arg Tyr Arg Pro Asn Asp Phe Ser Ala Phe Gin 2785 2790 2795 2800 Cys Gin Lys Lys Met Met Glu Val Gin Lys Lys Ser Phe Glu Glu Lys 2805 2810 2815 Tyr Glu Val Phe Met Aεp Val Cys Gin Aεn Phe Gin Pro Val Phe Arg 2820 2825 2830 Tyr Phe Cys Met Glu Lys Phe Leu Asp Pro Ala He Trp Phe Glu Lys 2835 2840 2845 Arg Leu Ala Tyr Thr Arg Ser Val Ala Thr Ser Ser He Val Gly Tyr 2850 2855 2860 He Leu Gly Leu Gly Asp Arg His Val Gin Asn He Leu He Aεn Glu 2865 2870 2875 2880 Gin Ser Ala Glu Leu Val His He Asp Leu Gly Val Ala Phe Glu Gin 2885 2890 2895 Gly Lys He Leu Pro Thr Pro Glu Thr Val Pro Phe Arg Leu Thr Arg 2900 2905 2910 Asp He Val Asp Gly Met Gly He Thr Gly Val Glu Gly Val Phe Arg 2915 2920 2925 Arg Cys Cyε Glu Lys Thr Met Glu Val Met Arg Asn Ser Gin Glu Thr 2930 2935 2940 Leu Leu Thr He Val Glu Val Leu Leu Tyr Asp Pro Leu Phe Asp Trp 2945 2950 2955 2960 Thr Met Asn Pro Leu Lys Ala Leu Tyr Leu Gin Gin Arg Pro Glu Asp 2965 2970 2975 Glu Thr Glu Leu His Pro Thr Leu Asn Ala Asp Asp Gin Glu Cys Lys 2980 2985 2990 Arg Aεn Leu Ser Aεp He Asp Gin Ser Phe Asp Lyε Val Ala Glu Arg 2995 3000 3005 Val Leu Met Arg Leu Gin Glu Lys Leu Lyε Gly Val Glu Glu Gly Thr 3010 3015 3020 Val Leu Ser Val Gly Gly Gin Val Asn Leu Leu He Gin Gin Ala He 3025 3030 3035 3040 Asp Pro Lys Asn Leu Ser Arg Leu Phe Pro Gly Trp Lys Ala Trp Val 3045 3050 3055 (2) INFORMATION FOR SEQ ID NO:36- (l) SEQUENCE CHARACTERISTICS: (A) LENGTH: 19 amino acids (D) TOPOLOGY: linear Ui) MOLECULE TYPE: peptide (xi) SEQUENCE DESCRIPTION: SEQ ID NO:36: Met Ser Gly Gly Ser Ser Cys Gin Thr Pro Ser Arg Ala He Pro Ala 1 5 10 15 Thr Arg Arg (2) INFORMATION FOR SEQ ID NO: 37: U) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 amino acidε (B) TYPE: amino acid (D) TOPOLOGY: linear Ui) MOLECULE TYPE, peptide (xi) SEQUENCE DESCRIPTION: SEQ ID NO:37: Gly Asp Tyr Ser Thr Thr Pro Gly Gly Thr Leu Phe Ser Thr Thr Pro 1 5 10 15 Gly Gly Thr Arg Arg 20 (2) INFORMATION FOR SEQ ID NO:38- U) SEQUENCE CHARACTERISTICS: (A) LENGTH: 12 amino acids (B) TYPE, amino acid (D) TOPOLOGY: linear Ui) MOLECULE TYPE: peptide (xi) SEQUENCE DESCRIPTION: SEQ ID NO:38- Glu Cyε Arg Asn Ser Pro Val Thr Lys Thr Arg Arg 1 5 10 (2) INFORMATION FOR SEQ ID NO:39 (l) SEQUENCE CHARACTERISTICS (A) LENGTH- 12 amino acids (D) TOPOLOGY- linear Ui) MOLECULE TYPE: peptide (xi) SEQUENCE DESCRIPTION: SEQ ID NO:39 Gly Val Thr Ser Pro Ser Ser Asp Glu Pro Arg Arg 1 5 10 (2) INFORMATION FOR SEQ ID NO:40: U) SEQUENCE CHARACTERISTICS: (A) LENGTH: 10 ammo acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (xi) SEQUENCE DESCRIPTION: SEQ ID NO:40: Met Glu Ala Ser Gin Ser His Leu Arg Arg 1 5 10 (2) INFORMATION FOR SEQ ID NO: 1: U) SEQUENCE CHARACTERISTICS. (A) LENGTH: 12 ammo acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (xi) SEQUENCE DESCRIPTION. SEQ ID NO.41. Arg Arg Aεn Ser Pro Glu Asp Lys Arg Ala Gly Gly 1 5 10 (2) INFORMATION FOR SEQ ID NO:42: U) SEQUENCE CHARACTERISTICS. (A) LENGTH: 12 amino acids (D) TOPOLOGY: linear Ui) MOLECULE TYPE: peptide (xi) SEQUENCE DESCRIPTION: SEQ ID NO:42: Gly Glu Glu Ser Gin Phe Glu Met Asp He Arg Arg 1 5 10 INDICATIONS RELATI NG TO A DEPOSITED MICROORGANISM (PCT Rule llbts) A. The indications made below relate to the microorganism referred to in the description on page 10 . l.nes 2-6 B. IDENTIFICATION OF DEPOSIT Further deposits are identified on an additional sheet f~\ Name of depositary institution American Type Culture Collec t ion Address of depositary institution (including postal code and country) 12301 Parklawn Drive Rockville , MD 20852 US Date of deposit Accession Number ε 7 November 1996 HB 12233 and HB 12 "> 34 C. ADDITIONAL INDICATIONS (leave blank if not applicable) This information is continued on an additional sheet | | "In respect of thoεe designations in which a European patent is sought, a sample of the deposited microorganism will be made available until the publication of the mention of the grant of the European patent or until the date on which the application has been refused or withdrawn or is deemed to be withdrawn, only by the issue of such a sample to an expert nominated by the person requesting the sample (Rule 28(A) EPC)." D. DESIGNATED STATES FOR WHICH INDICATIONS ARE MADE (if the indications are not for all designated States) EP E. SEPARATE FURNISHING OF INDICATIONS (leave blank if not applicable) Tbe indications listed below will be submitted to the International Bureau later (specify ύtcgcnaalnaiutc of theindicationseg , 'Accession Number of Deposit') For International Bureau use only I [ This sheet was received by the International Bureau on Authorized officer

Claims: CLAIMS We claim: 1 . A purified and isolated polynucleotide comprising a polynucleotide encoding the PIK-related kinase MCCSlα amino acid sequence set out in SEQ ID NO: 31 . 2. A purified and isolated polynucleotide comprising a polynucleotide encoding the PIK-related kinase MCCS 1/3 amino acid sequence set out in SEQ ID NO: 33. 3. The polynucleotide of claim 1 or 2 which is a DNA. 4. The DNA of claim 3 which is a cDNA. 5. A MCCSlα cDNA consisting of the DNA sequence set out in SEQ ID NO: 30. 6. A MCCS 1/5 DNA consisting of the DNA sequence set out in SEQ ID NO: 32. 7. The DNA of claim 3 which is a genomic DNA. 8. An RNA transcript of the DNA of claim 3. 9. The DNA of claim 3 which is a wholly or partially chemically synthesized DNA. 10. A DNA comprising a DNA encoding a full length mammalian MCCSl kinase selected from the group consisting of: a) a DNA which hybridizes under stringent conditions to the non- coding strand of the DNA of SEQ ID NO: 30; b) a DNA which hybridizes under stringent conditions to the non- coding strand of the DNA of SEQ ID NO: 3; and c) a DNA which hybridizes under stringent conditions to the non- coding strand of the DNA of SEQ ID NO: 32. 1 1. A vector comprising a DNA according to claim 3 or 10. 12. The vector of claim 1 1 wherein said DNA is operatively linked to an expression control DNA sequence. 13. A host cell stably transformed or transfected with a DNA according to claim 3 or 10 in a manner allowing the expression in said host cell of the MCCSl kinase. 14. A method for producing the PIK-related kinase MCCSl , said method comprising growing a host cell according to claim 1 1 in a suitable nutrient medium and isolating the MCCSl kinase from said cell or the medium of its growth. 15. A purified and isolated polypeptide comprising the PIK-related kinase MCCSlα amino acid sequence consisting of SEQ ID NO: 31. 16. A purified and isolated polypeptide comprising the PIK-related kinase MCCSlβ amino acid sequence consisting of SEQ ID NO: 33. 17. A polypeptide or peptide capable of specifically binding to PIK- related kinase MCCSl . 18. An antibody product according to claim 17. 19. A monoclonal antibody according to claim 18. 20. A hybridoma cell line producing a monoclonal antibody according to claim 19. 21. An assay for identifying modulators of MCCSl kinase activity comprising the steps of: a) incubating a MCCSl kinase preparation in kinase buffer with gamma- 32 P-ATP and an exogenous kinase substrate in the presence and absence of a test compound, and b) measuring the moles of phosphate transferred to said substrate; wherein an increase in the moles of 32 P-phosphate transferred to said substrate in presence of said test compound compared to the moles of 32 P-phosphate transferred to said substrate in the absence of said test compound indicates that said test compound is an activator of said MCCSl kinase and a decrease in the moles of 32 P- phosphate transferred to said substrate in presence of said test compound compared to the moles of 2 P-phosphate transferred to said substrate in the absence of said test compound indicates that said test compound is an inhibitor of said MCCSl kinase. 22. The hybridoma cell line 224C. 23. The hybridoma cell line 224F. 24. A method of identifying a compound that inhibits MCCS l comprising the steps of: a) expressing MCCSl in a genetically altered cell, thereby decreasing the sensitivity of the cell to DNA damage, said sensitivity being associated with the genetic alteration; b) exposing the genetically altered cell of step (a) to DNA damaging treatment in the presence and absence of a test modulator compound; c) measuring the sensitivity of the cell to DNA damage; and d) identifying a test compound that restores the sensitivity of the cell to DNA damage as an inhibitor of MCCSl activity. 25. A method of identifying a compound that inhibits ATM comprising the steps of: a) expressing ATM in a genetically altered cell, thereby decreasing the sensitivity of the cell to DNA damage, said sensitivity being associated with the genetic alteration; b) exposing the genetically altered cell of step (a) to DNA damaging treatment in the presence and absence of a test modulator compound; c) measuring the sensitivity of the cell to DNA damage; and d) identifying a test compound that restores the sensitivity of the cell to DNA damage as an inhibitor of ATM activity. 26. An assay for identifying modulators of ATM kinase activity comprising the steps of: a) incubating a ATM kinase preparation in kinase buffer with gamma- 32 P-ATP and an exogenous kinase substrate in the presence and absence of a test compound, and b) measuring the moles of phosphate transferred to said substrate; wherein an increase in the moles of 32 P-phosphate transferred to said substrate in presence of said test compound compared to the moles of 32 P-phosphate transferred to said substrate in the absence of said test compound indicates that said test compound is an activator of said ATM kinase and a decrease in the moles of 2 P- phosphate transferred to said substrate in presence of said test compound compared to the moles of 32 P-phosphate transferred to said substrate in the absence of said test compound indicates that said test compound is an inhibitor of said ATM kinase.

Inventors: HOEKSTRA MERL F, HOLTZMAN DOUG A, KEEGAN KATHLEEN S, HOEKSTRA, MERL, F., HOLTZMAN, DOUG, A., KEEGAN, KATHLEEN, S.
Applicants: HOEKSTRA MERL F, HOLTZMAN DOUG A, ICOS CORP, KEEGAN KATHLEEN S, HOEKSTRA, MERL, F., HOLTZMAN, DOUG, A., ICOS CORPORATION, KEEGAN, KATHLEEN, S.
Application year: 1996
Main classification: C12Q
IPC codes: C12N9