NON-A, NON-B, NON-C, NON-D, NON-E HEPATITIS REAGENTS AND METHODS FOR THEIR USE

Abstract: Hepatitis GB Virus (HGBV) nucleic acid and amino acid sequences useful for a variety of diagnostic and therapeutic applications, kits for using the HGBV nucleic acid or amino acid sequences, HGBV immunogenic particles, and antibodies which specifically bind to HGBV. Also provided are methods for producing antibodies, polyclonal or monoclonal, from the HGBV nucleic acid or amino acid sequences.

Description: NON-A, NON-B, NON-C, NON-D, NON-E HEPATITIS REAGENTS AND METHODS FOR THEIR USE This application is a continuation-in-part application of U.S. Serial No. 08/377,557 filed January 27, 1995, which is a continuation-in-part of U.S. Serial No. 08/344,185 filed November 23, 1994 and U.S. Serial No. 08/344,190 filed November 23, 1994, which are each continuation-in-part applications of 08/283,314 filed July 29, 1994, which is a continuation-in-part application of U.S. Serial No. 08/242,654, filed May 13, 1994, which is a continuation-in-part application of U.S. Serial No. 08/196,030 filed February 14, 1994, all of which enjoy common ownership and each of which is incorporated herein by reference. Background of the Invention This invention relates generally to a group of infectious viral agents causing hepatitis in man, and more particularly, relates to materials such as polynucleotides derived from this group of viruses, polypeptides encoded therein, antibodies which specifically bind to these polypeptides, and diagnostics and vaccines that employ these materials. Hepatitis is one of the most important diseases transmitted from a donor to a recipient by transfusion of blood products, organ transplantation and hemodialysis; it also can be transmitted via ingestion of contaminated food stuffs and water, and by person to person contact. Viral hepatitis is known to include a group of viral agents with distinctive viral genes and modes of replication, causing hepatitis with differing degrees of severity of hepatic damage through different routes of transmission. In some cases, acute viral hepatitis is clinically diagnosed by well-defined patient symptoms including jaundice, hepatic tenderness and an elevated level of liver transaminases such as aspartate transaminase (AST), alanine transaminase (ALT) and isocitrate dehydrogenase (ISD). In other cases, acute viral hepatitis may be clinically inapparent. The viral agents of hepatitis include hepatitis A virus (HAN), hepatitis B virus (HBN), hepatitis C virus (HCN), hepatitis delta virus (HDN), hepatitis E virus (HEN), Epstein-Barr virus (EBN) and cytomegalovirus (CMN). Although specific serologic assays available by the late 1960's to screen blood donations for the presence of HBV surface antigen (HBsAg) were successful in reducing the incidence of post-transfusion hepatitis (PTH) in blood recipients, PTH continued to occur at a significant rate. H. J. Alter et al., Ann. Int. Med. 77:691-699 (1972); H. J. Alter et al., Lancet ii:838-841 (1975). Investigators began to search for a new agent, termed "non-A, non-B hepatitis" (NANBH), that caused viral hepatitis not associated with exposure to viruses previously known to cause hepatitis in man (HAN, HBN, CMN and EBN). See, for example, S. M. Feinstone et al., New Engl. J. Med. 292:767-770 (1975); Anonymous editorial, Lancet ii:64-65 (1975); F. B. Hollinger in B. N. Fields and D. M. Knipe et al., Virology. Raven Press, New York, pp. 2239-2273 (1990). Several lines of epidemiological and laboratory evidence have suggested the existence of more than one parenterally transmitted NANB agent, including multiple attacks of acute NANBH in intraveneous drag users; distinct incubation periods of patients acquiring NANBH post-transfusion; the outcome of cross- challenge chimpanzee experiments; the ultrastructural liver pathology of infected chimpanzees; and the differential resistance of the putative agents to chloroform. J. L. Dienstag, Gastroenterologv 85:439-462 (1983); J. L. Dienstag, Gastroenterologv 85:743-768 (1983); F. B. Hollinger et al., J. Infect. Pis. 142:400-407 (1980); D. W. Bradley in F. Chisari, ed., Advances in Hepatitis Research. Masson, New York, pp. 268-280 (1984); and D. W. Bradley et al., Infect. Pis. 148:254-265 (1983). A serum sample obtained from a surgeon who had developed acute hepatitis was shown to induce hepatitis when inoculated into tamarins {Saguinus species). Four of four tamarins developed elevated liver enzymes within a few weeks following their inoculation, suggesting that an agent in the surgeon's serum could produce hepatitis in tamarins. Serial passage in various non-human primates demonstrated that this hepatitis was caused by a transmissable agent; filtration studies suggested the agent to be viral in nature. The transmissable agent responsible for these cases of hepatitis in the surgeon and tamarins was termed the "GB agent." F. Peinhardt et al., J. Exper. Med. 125:673-688 (1967). F. Pienhardt et al., J. Exper. Med.. supra; E.Tabor et al., J. Med. Virol. 5:103-108 (1980); R. O. Whittington et al., Viral and Immunological Piseases in Nonhuman Primates. Alan R. Liss, Inc., New York, pp. 221-224 (1983) Although it was suggested that the GB agent may be an agent causing NANBH in humans and that the GB agent was not related to the known NANBH agents studied in various laboratories, no definitive or conclusive studies on the GB agent are known, and no viral agent has been discovered or molecularly characterized. F. Peinhardt et al., Am. J. Med. Sci. 270:73-80 (1975); and J. L. Pienstag et al., Nature 264:260-261 (1976). See also E. Tabor et al., J. Med. Virol., supra: E. Tabor et al., J. Infect. Pis. 140:794-797 (1979); R. O. Whittington et al., supra: and P. Karayiannis et al., Hepatologv 9:186-192 (1989). Early studies indicated that the GB agent was unrelated to any known human hepatitis virus. S. M. Feinstone et al., Science 182:1026-1028 (1973); P. J. Provost et al., Proc. Soc. Exp. Biol. Med. 148:532-539 (1975); J. L. Melnick, Intervirology 18:105-106 (1982); A. W. Holmes et al., Nature 243:419-420 (1973); and F. Peinhardt et al., Am. J. Med. Sci.. supra. However, questions were raised regarding whether the GB agent was a virus which induced hepatitis infection in humans, or a latent tamarin virus activated by the GB serum and once activated, easily passaged to other tamarins, inducing hepatitis in them. Also, a small percentage of marmosets inoculated with GB-positive serum did not develop clinical hepatitis (4 of 52, or 7.6%), suggesting that these animals may have been naturally immune and thus, that the GB agent may be a marmoset virus. W. P. Parks et al., J. Infect. Pis. 120:539-547 (1969); W. P. Parks et al., J. Infect. Pis. 120:548-559 (1969). Morphological studies have been equivocal, with immune electron microscopy studies in one report indicating that the GB agent formed immune complexes with a size distribution of 20-22 nm and resembling the spherical structure of a parvoviras, while another study reported that immune electron microscopy data obtained from liver homogenates of GB-positive tamarins indicated that aggregares of 34-36 nm with icosahedral symmetry were detected, suggesting that the GB agent was a calici-like virus. See, for example, J. P. Almeida et al., Nature 261 :608-609 (1976); J. L. Pienstag et al., Nature, supra. Two hepatitis-causing viruses recently have been discovered and reported: HCV, which occurs primarily through parenteral transmission, and HEV, which is transmitted enterically. See, for example, Q. L. Choo et al., Science 244:359-362 (1989), G. Kuo et al., Science 244:362-364 (1989), E. P. Publication No. 0 318 216 (published May 31, 1989), G. R. Reyes et al., Science 247:1335-1339 (1990). HCV is responsible for a majority of PTH ascribed to the NANBH agent(s) and many cases of acute NANBH not acquired by transfusion. Anonymous editorial, Lancet 335:1431-1432 (1990); J. L. Pienstag, Gastroenterologv 99:1177-1180 (1990); and M. J. Alter et al., JAMA 264:2231- 2235 (1990). While the detection of HCV antibody in donor samples eliminates 70 to 80% of NANBH infected blood in the blood supply system, the discovery and detection of HCV has not totally prevented the transmission of hepatitis. H. Alter et al., New Eng. J. Med. 321:1494-1500 (1989). Recent publications have questioned whether additional hepatitis agents may be responsible for PTH and for community acquired acute and/or chronic hepatits that is not associated with PTH. For example, of 181 patients monitored in a prospective clinical survery conducted in France from 1988 to 1990, investigators noted a total of 18 cases of PTH. Thirteen of these 18 patients tested negative for anti-HCV antibodies, HBsAg, HBV and HCV nucleic acids. The authors speculated as to the potential importance of a non-A, non-B, non-C agent causing PTH. V. Thiers et al., Hepatology 18:34-39 (1993). Also, of 1,476 patients monitored in another study conducted in Germany from 1985 to 1988, 22 cases of documented cases of PTH were not related to infection with HBV or HCV. T. Peters et al., J. Med. Virol. 39:139-145 (1993). It would be advantageous to identify and provide materials derived from a group of novel and unique viruses causing hepatitis, such as, polynucleotides, recombinant and synthetic polypeptides encoded therein, antibodies which specifically bind to these polypeptides, and diagnostics and vaccines that employ these materials. Such materials could greatly enhance the ability of the medical community to more accurately diagnose acute and/or chronic viral hepatitis and could provide a safer blood and organ supply by detecting non-A, non-B and non- C hepatitis in these blood and organ donations. Summary of the Invention The present invention provides a purified polynucleotide or fragment thereof derived from hepatitis GB virus (HGBV) capable of selectively hybridizing to the genome of HGBV or the complement thereof, wherein said polynucleotide is characterized by a positive stranded RNA genome wherein said genome comprises an open reading frame (ORF) encoding a polyprotein wherein said polyprotein comprises an amino acid sequence having at least 35% identity, more preferably, 40% identity, even more preferably, 60% identity, and yet more preferably, 80% identity to an amino acid sequence selected from the group consisting of HGBV- A, HGB V-B and HGBV-C. Also provided is a recombinant polynucleotide or fragment therof derived from hepatitis GB virus (HGBV) capable of selectively hybridizing to the genome of HGBV or the complement thereof, wherein said nucleotide comprises a sequence that encodes at least one epitope of HGBV, and wherein said recombinant nucleotide is characterized by a positive stranded RNA genome wherein said genome comprises an open reading frame (ORF) encoding a polyprotein wherein said polyprotein comprises an amino acid sequence having at least 35% identity to an amino acid sequence selected from the group consisting of HGBV-A, HGBV-B and HGBV-C. Such a recombinant plynucleotide is contained within a recombinant vector and further comprises a host cell transformed with said vector. The present invention also probides a hepatitis GB virus (HGBV) recombinant polynucleotide or fragment thereof comprising a nucleotide sequence derived from an HGBV genome, wherein said polynucleotide is contained within a recombinant vector and further comprises a host cell transformed with said vector. and further wherein said sequence encodes an epitope of HGBV. The HGBV recombinant polynucleotide is characterized by a positive stranded RNA genome wherein said genome comprises an open reading frame (ORF) encoding a polyprotein wherein said polyprotein comprises an amino acid sequence having at least 35% identity to an amino acid sequence selected from the group consisting of HGBV-A, HGBV-B and HGBV-C. The present invention provides a recombinant expression system comprising an open reading frame of PNA or RNA derived from hepatitis GB virus (HGBV) wherein said open reading frame comprises a sequence of HGBV genome or cPNA and wherein said open reading frame is operably linked to a control sequence compatible with a desired host, and further comprises a cell transformed with said recombinant expression system and a polypeptide of at least about eight amino acids in length produced by said cell. The present invention additionally provides a purified hepatitis GB virus (HGBV) comprising a preparation of HGBV polypeptide or fragment thereof, a recombinant polypeptide comprising an amino acid sequence or fragment thereof wherein said sequence is characterized by a positive stranded RNA genome wherein said genome comprises an open reading frame (ORF) encoding a polyprotein wherein said polyprotein comprises an amino acid sequence having at least 35% identity, more preferably 40% identity and yet more preferably 60% identity to an amino acid sequence selected from the group consisting of HGBV-A, HGBV-B and HGBV-C. Antibodies, both polyclonal and monoclonal, are provided by the present invention, as well as, a fusion polypeptide comprising at least one hepatitis GB virus (HGBV) polypeptide or fragment thereof, a particle that is immunogenic against hepatitis GB virus (HGBV) infection, comprising a non-HGB V polypeptide having an amino acid sequence capable of forming a particle when said sequence is produced in a eukaryotic or prokaryotic host, and at least one HGBV epitope, and a polynucleotide probe for hepatitis GB virus (HGBV) wherein said polynucleotide probe is characterized by a positive stranded RNA genome wherein said genome comprises an open reading frame (ORF) encoding a polyprotein wherein said polyprotein comprises an amino acid sequence having at least 35% identity to an amino acid sequence selected from the group consisting of HGBV-A, HGBV-B and HGBV-C. Assay kits also are provided, as well as methods for producing a polypeptide containing at least one hepatitis GB virus (HGBV) epitope comprising incubating host cells transformed with an expression vector comprising a sequence encoding a polypeptide characterized by a positive stranded RNA genome wherein said genome comprises an open reading frame (ORF) encoding a polyprotein wherein said polyprotein comprises an amino acid sequence having at least 35% identity to an amino acid sequence selected from the group consisting of HGBV-A, HGBV-B and HGBV-C. Also provided are methods of detecting HGBV nucelic acids, antigens and antibodies in test samples, including methods which utilize solid phases, recombinant or synthetic peptides, or probes. Vaccines also are provided by the present invention, as are tissue culture grown cell infected with hepatitis GB virus (HGBV), a method for producing antibodies to hepatitis GB virus (HGBV) comprising administering to an individual an isolated immunogenic polypeptide or fragment thereof comprising at least one HGBV epitope in an amount sufficient to produce an immune response. Piagnostic reagents also are provided herein which comprises polynucleotides or polypeptides or fragments thereof. Brief Pescription of the Prawings FIGURES 1-12 are graphs of individual tamarins which plot the amount of liver enzyme (ALT or ICP) as measured in mU/ml against time (weeks post inoculation), where ALT CO indicates the cuttoff value for ALT, and ICO CO indicates the cutoff value of ICP, wherein FIGURE 1 shows the graph of tamarin T-1053; FIGURE 2 shows the graph of tamarin T- 1048 ; FIGURE 3 shows the graph of tamarin T-1057; FIGURE 4 shows the graph of tamarin T-1061 ; FIGURE 5 shows the graph of tamarin T-1047; FIGURE 6 shows the graph of tamarin T-1042; FIGURE 7 shows the graph of tamarin T- 1044; FIGURE 8 shows the graph of tamarin T-1034; FIGURE 9 shows the graph of tamarin T-1055; FIGURE 10 shows the graph of tamarin T-1051 ; FIGURE 11 shows the graph of tamarin T- 1038; and FIGURE 12 shows the graph of tamarin T- 1049. FIGURE 13 presents a flow diagram of the steps involved in representational difference analysis (RPA), the procedure used for identifying clones. FIGURE 14 shows an ethidium bromide stained 2.0% agarose gel of the products from the representational difference analysis (RPA) performed on pre- inoculation and acute phase HGBV-infectedtamarin plasma. FIGURE 15 shows an autoradiogram from a Southern blot of genomic PNA, amplicon PNA and products from the first three rounds of subtraction/hybridization. FIGURE 16 shows the same autoradiogram as described in FIGURE 15, except that an alternative radiolabeled probe is used. FIGURE 17 shows an ethidium bromide stained 1.5% agarose gel of polymerase chain reaction (PCR) amplified product from genomic PNA. FIGURE 18 shows an autoradiogram from a Southern blot of the 1.5% agarose gel in FIGURE 17. FIGURE 19 shows an ethidium bromide stained 1.5% agarose gel of RT- PCR product obtained from normal human serum and pre-inoculation and acute phase tamarin plasmas. FIGURE 20 shows an autoradiogram from a Southern blot of the same gel described in FIGURE 19. FIGURES 21 A and B show autoradiograms from Northern blots of total cellular RNA extracted from the liver of an uninfected tamarin and an HGBV- infected tamarin. FIGURE 22 shows a diagram that demonstrates each of the recombinant polynucleotide isolates are present on contiguous RNA species. FIGURES 23 A-C show dot plot analyses of the nucleic acid sequences wherein: FIGURE 23A shows a dot blot comparison of HGBV-A; FIGURE 23B shows a dot blot comparison of HGBV-B; FIGURE 23C shows a dot blot comparison of HGBV-A v. HGBV-B. FIGURES 24 A-B show the conserved residues as follows: FIGURE 24A shows the conserved residues in the putative NTP- binding helicase domain of predicted translation products of HGBV-A, HGBV-B and HCV-l NS3, FIGURE 24B shows the conserved residues of the RNA- dependent RNA polymerase domain of predicted translation products of HGBV-A, HGBV-B and HCV-1 NS5b. FIGURES 25 A-B show Coomassie-stained 10% SPS-polyacrylamide gels of CKS fusion protein whole cell ly sates; three CKS fusion proteins demonstrate immunoreactivity with HGBV-infected tamarin sera. FIGURES 26 to 30 are graphs of individual tamarins which plot 1) the amount of liver enzyme (ALT) as measured in mU/ml against time (weeks post inoculation) as shown by a solid line; 2) ELISA absorbance values for the CKS- 1.7 recombinant protein as shown by filled circles connected by dotted lines; 3) ELISA absorbance values for the CKS- 1.4 recombinant protein as shown by open circles connected by dotted lines; 4) ELISA absorbance values for the CKS-4.1 recombinant protein as shown by crosses connected by dotted lines; 5) negative PCR results using SEQ IP #21 primers as shown by empty squares; 6) postivive PCR results using SEQ IP #21 primers as shown by filled squares; 7) negative PCR results using SEQ IP #26 primers as shown by empty diamonds; 8) positive PCR results using SEQ IP #26 primers as shown by filled diamonds; 9) inoculation dates are indicated by the arrowheads, wherein FIGURE 26 shows the graph of tamarin T-1048; FIGURE 27 shows the graph of tamarin T-1057; FIGURE 28 shows the graph of tamarin T-1061; FIGURE 29 shows the graph of tamarin T-1051 ; and FIGURE 30 shows the graph of tamarin T-1034. FIGURES 31-34 are graphs of a human test specimens which plots 1) the amount of liver enzyme (ALT) as measured in mU/ml against time (weeks post inoculation) as shown by a solid line; 2) ELISA absorbance values for the CKS- 1.7 recombinant protein as shown by dotted lines, filled circles; 3) ELISA absorbance values for the CKS- 1.4 recombinant protein as shown by dotted lines, open circles, wherein FIGURE 31 shows a graph of patient 101; FIGURE 32 shows a graph of patient 257; FIGURE 33 shows a graph of patient 260; and FIGURE 34 shows a graph of patient 340. FIGURE 35 shows conserved residues, wherein FIGURE 35A shows the conserved residues in the putative NTP- binding helicase domain of predicted translation products of Contig. A, Contig. B and HCV-1 NS3, and FIGURE 35B shows the conserved residues of the RNA- dependent RNA polymerase domain of predicted translation products of Contig. A, Contig. B and HCV-1 NS5b. FIGURE 36 shows a nucleotide alignment of HGBV-A, HGBV-B, HGBV-C and HCV-1. FIGURE 37 shows a Phospholmage (Molecular Pynamics, Sunnyvale, CA) from a Southern blot of the PCR products after hybridization with the radiolabeled probe from GB-C FIGURE 38 shows a nucleotide alignment of HGBV-C with two variant clones . FIGURE 39 presents a schematic of the assembled contig of HGBV-C. FIGURE 40 shows a nucleotide alignment of HGBV-C with four variant clones. FIGURE 41 shows a Phospholmage (Molecular Pynamics, Sunnyvale, CA) of a Southern blot of PCR products generated from a Canadian hepatitis patient after hybridization with radiolabeled from Canadian patient GB-C.5. FIGURE 42 depicts a phylogenetic tree produced from alignment of the helicase domains of the viruses indicated. FIGURE 43 SCOTT depicts a phylogenetic tree produced from alignment of the RNA-dependent RNA polymerase domains of the viruses indicated. FIGURE 44 presents a phylogenetic tree produced from alignmen t of the large open reading frames (putative precursor polyproteins) of the viruses indicated. Petailed Description of the Invention The present invention provides characterization of a newly ascertained etiological agents of non-A, non-B, non-C, non-P and non-E hepatitis-causing agents, collectively so-termed "Hepatitis GB Virus," or "HGBV." The present invention provides a method for determining the presence of the HGBV etiological agents, methods for obtaining the nucleic acid of this etiological agents created from infected serum, plasma or liver homogenates from individuals, either humans or tamarins, with HGBV to detect newly synthesized antigens derived from the genome of heretofore unisolated viral agents, and of selecting clones which produced products which are only found in infectious individuals as compared to non-infected individuals. Portions of the nucleic acid sequences derived from HGBV are useful as probes to determine the presence of HGBV in test samples, and to isolate naturally occurring variants. These sequences also make available polypeptide sequences of HGBV antigens encoded within the HGBV genome(s) and permit the production of polypeptides which are useful as standards or reagents in diagnostic tests and/or as components of vaccines. Monoclonal and polyclonal antibodies directed against at least one epitope contained within these polypeptide sequences also are useful for diagnostic tests as well as therapeutic agents, for screening of antiviral agents, and for the isolation of the HGBV agent from which these nucleic acid sequences are derived. Isolation and sequencing of other portions of the HGBV genome also can be accomplished by utilizing probes or PCR primers derived from these nucleic acid sequences, thus allowing additional probes and polypeptides of the HGBV to be established, which will be useful in the diagnosis and/or treatment of HGBV, both as a prophylactic and therapeutic agent. According to one aspect of the invention, there will be provided a purified HGBV polynucleotide, a recombinant HGBV polynucleotide, a recombinant polynucleotide comprising a sequence derived from an HGBV genome; a recombinant polypeptide encoding an epitope of HGBV; a synthetic peptide encoding an epitope of HGBV; a recombinant vector containing any of the above described recombinant polypeptides, and a host cell transformed with any of these vectors. These recombinant polypeptides and synthetic peptides may be used alone or in combination, or in conjunction with other substances representing epitopes of HGBV. In another aspect of the invention there will be provided purified HGBV; a preparation of polypeptides from the purified HGBV; a purified HGBV polypeptide; a purified polypeptide comprising an epitope which is immunologically identical with an epitope contained in HGBV. In yet another aspect of the invention there will be provided a recombinant expression system comprising an open reading frame (ORF) of PNA derived from an HGBV genome or from HGBV cPNA, wherein the ORF is operably linked to a control sequence compatible with a desired host, a cell transformed with the recombinant expression system, and a polypeptide produced by the transformed cell. Additional aspects of the present invention include at least one recombinant HGBV polypeptide, at least one recombinant polypeptide comprised of a sequence derived from an HGBV genome or from HGBV cPNA; at least one recombinant polypeptide comprised of an HGBV epitope and at least one fusion polypeptide comprised of an HGBV polypeptide. The present invention also provides methods for producing a monoclonal antibody which specifically binds to at least one epitope of HGBV; a purified preparation of polyclonal antibodies which specifically bind to at least one HGBV epitope; and methods for using these antibodies, which include diagnostic, prognostic and therapeutic uses. In still another aspect of the invention there will be provided a particle which immunizes against HGBV infection comprising a non-HGBV polypeptide having an amino acid sequence capable of forming a particle when said sequence is produced in an eukaryotic host, and an HGBV epitope. A polynucleotide probe for HGBV also will be provided. The present invention provides kits containing reagents which can be used for the detection of the presence and/or amount of polynucleotides derived from HGBV, such reagents comprising a polynucleotide probe containing a nucleotide sequence from HGBV of about 8 or more nucleotides in a suitable container; a reagent for detecting the presence and/or amount of an HGBV antigen comprising an antibody directed against the HGBV antigen to be detected in a suitable container; a reagent for detecting the presence and/or amount of antibodies directed against an HGBV antigen comprising a polypeptide containing an HGBV epitope present in the HGBV antigen, provided in a suitable container. Other kits for various assay formats also are provided by the present invention as described herein. Other aspects of the present invention include a polypeptide comprising at least one HGBV epitope attached to a solid phase and an antibody to an HGBV epitope attached to a solid phase. Also included are methods for producing a polypeptide containing an HGBV epitope comprising incubating host cells transformed with an expression vector containing a sequence encoding a polypeptide containing an HGBV epitope under conditions which allow expression of the polypeptide, and a polypeptide containing an HGBV epitope produced by this method. The present invention also provides assays which utilize the recombinant or synthetic polypeptides provided by the invention, as well as the antibodies described herein in various formats, any of which may employ a signal generating compound in the assay. Assays which do not utilize signal generating compounds to provide a means of detection also are provided. All of the assays described generally detect either antigen or antibody, or both, and include contacting a test sample with at least one reagent provided herein to form at least one antigen/antibody complex and detecting the presence of the complex. These assays are described in detail herein. Vaccines for treatment of HGBV infection comprising an immunogenic peptide containing an HGBV epitope, or an inactivated preparation of HGBV, or an attenuated preparation of HGBV, or the use of recombinant vaccines that express HGBV epitope(s) and/or the use of synthetic peptides, also are included in the present invention. An effective vaccine may make use of combinations of these immunogenic peptides (such as, a cocktail of recombinant antigens, synthetic peptides and native viral antigens administered simultaneously or at different times); some of these may be utilized alone and be supplemented with other representations of immunogenic epitopes at later times. Also included in the present invention is a method for producing antibodies to HGBV comprising administering to an individual an isolated immunogenic polypeptide containing an HGBV epitope in an amount sufficient to produce an immune response in the inoculated individual. Also provided by the present invention is a tissue culture grown cell infected with HGBV. In yet another aspect of the present invention is provided a method for isolating PNA or cPNA derived from the genome of an unidentified infectious agent, which is a unique modification of representational difference analysis (RPA), and which is described in detail hereinbelow. Pefinitions The term "Hepatitis GB Virus" or "HGBV", as used herein, collectively denotes a viral species which causes non-A, non-B, non-C, non-P, non-E hepatitis in man, and attenuated strains or defective interfering particles derived therefrom. This may include acute viral hepatitis transmitted by contaminated foodstuffs, drinking water, and the like; hepatitis due to HGBV transmitted via person to person contact (including sexual transmission, respiratory and parenteral routes) or via intraveneous drug use. The methods as described herein will allow the identification of individuals who have acquired HGBV. Individually, the HGBV isolates are specifically referred to as "HGBV-A", "HGBV-B" and "HGBV-C." As described herein, the HGBV genome is comprised of RNA. Analysis of the nucleotide sequence and deduced amino acid sequence of the HGBV reveals that viruses of this group have a genome organization similar to that of the Flaviridae family. Based primarily, but not exclusively, upon similarities in genome organization, the International Committee on the Taxonomy of Viruses has recommended that this family be composed of three genera: Flavivirus, Pestivirus, and the hepatitis C group. Similarity searches at the amino acid level reveal that the hepatitis GB virus subclones have some, albeit low, sequence resemblence to hepatitis C virus. The information provided herein is sufficient to allow classification of other strains of HGBV. Several lines of evidence demonstrate that HGBV-C is not a genotype of HCV. First, sera containing HGB-C sequences were tested for the presence of HCV antibody. Routine detection of individuals exposed to or infected with HCV relies upon antibody tests which utilize antigens derived from three or more regions from HCV-1. These tests allow detection of antibodies to the known genotypes of HCV (See, for example, Sakamoto et al., J. Gen. Virol. 75:1761- 1768 (1994) and Stuyver et al., J. Gen. Virol. 74:1093-1102 (1993). HCV- specific ELISAs failed to detect sera containing GB-C sequences in six of eight cases (TABLE A). Second, several human sera that were seronegative for HCV antibodies have been shown to be positive for HCV genomic RNA by a highly sensitive RT-PCR assay (Sugitani, Lancet 339: 1018-1019 (1992). This assay failed to detect HCV RNA in seven of eight sera containing HGB-C sequences (TABLE A). Thus, HGBV-C is not a genotype of HCV based on both serologic and molecular assays. The alignment of a portion of the predicted translation product of HGB-C within the helicase region with the homologous region of HGBV-A, HGBV-B, HCV-1 and additional members of the Flaviviridae, followed by phylogenetic analysis of the aligned sequences suggests that HGBV-C is more closely related to HGBV-A than to any member of the HCV group. The sequences of HGBV-C and HGBV-A, while exhibiting an evolutionary distance of 0.42, are not as divergent as HGBV-C is from HGBV-B, which shows an evolutionary distance of 0.92 (TABLE 33, infra.). Thus, HGBV-A and HGBV-C may be considered to be members of one subgroup of the GB viruses and GB V-B a member of its own subgroup. The phylogenetic analysis of the helicase sequences from various HCV isolates show that they form a much less diverged group, exhibiting a maximum evolutionary distance of 0.20 (TABLE 32, infra.). A comparison of the HCV group and the HGBV group shows a minimum evolutionary distance between any two sequences from each group of 0.69. The distance values reported hereinabove were used to generate a phylogenic tree presented in FIGURE 42. The relatively high degree of divergence among these viruses suggests that the GB viruses are not merely types or subtypes within the hepatitis C group; rather, they constitute their own phyletic group (or groups). Phylogenetic analysis using sequence information derived from a small portion of HCV viral genomes has been shown to be an acceptable method for the assignment of new isolates into genotypic groups (Simmonds et al., Hepatologv 19: 1321-1324 (1994). In the current analysis, the use of a 110 amino acid sequence within the helicase gene from representative HCV isolates has properly grouped them into their respective genotypes (Simmonds et al., J. Gen. Virol. 75:1053-1061 (1994). Therefore, the evolutionary distances shown, in all liklihood, accurately refect the high degree of divergence between the GB viruses and the hepatitis C virus. In previous applications, it was stated that "HGBV strains are identifiable on the polypeptide level and that HGBV strains are more than 40% homologous, preferably more than about 60% homologous, and even more preferably more than about 80% homologous at the polypeptide level." As it is used, the term "homologous," when referring to the degree of relatedness of two polynucleotide or polypeptide sequences, can be ambiguous and actually implies an evolutionary relationship. As is now the current convention in the art, the term "homologous" is no longer used; instead the terms "similarity" and/or "identity" are used to describe the degree of relatedness between two polynucleotides or polypeptide sequences. The techniques for determining amino acid sequence "similarity" and/or "identity" are well-known in the art and include, for example, directly determining the amino acid sequence and comparing it to the seqeunces provided herein; determining the nucleotide sequence of the genomic material of the putative HGBV (usually via a cPNA intermediate), and determining the amino acid sequence encoded therein, and comparing the corresponding regions. In general, by "identity" is meant the exact match-up of either the nucleotide sequence of HGBV and that of another strain(s) or the amino acid sequence of HGBV and that of another strain(s) at the appropriate place on each genome. Also, in general, by "similarity" is meant the exact match-up of amino acid sequence of HGBV and that of another strain(s) at the appropriate place, where the amino acids are identical or possess similar chemical and/or physical porperties such as charge or hydrophobicity. The programs available in the Wisconsin Sequence Analysis Package, Version 8 (available from the Genetics Computer Group, Madison, Wisconsin, 53711), for example,, the GAP program, are capable of calculating both the identity and similarity between two polynucleotide or two polypeptide sequences. Other programs for calculating identity and similarity between two sequences are known in the art. Additionally, the following parameters are applicable, either alone or in combination, in identifying a strain of HGBV-A, HGBV-B or HGBV-C. It is expected that the overall nucleotide sequence identity of the genomes between HGBV-A, HGBV-B or HGBV-C and a strain of one of these hepatitis GB viruses will be about 45% or greater, since it is now believed that the HGBV strains may be genetically related, preferably about 60% or greater, and more preferably, about 80% or greater. Also, it is expected thjat the overall sequence identity of the genomes between HGBV-A and a strain of HGBV-A at the amino acid level will be about 35% or greater since it is now believed that the HGBV strains may be genetically related, preferably about 40% or greater, more preferably, about 60% or greater, and even more preferably, about 80% or greater. In addition, there will be corresponding contiguous sequences of at least about 13 nucleotides, which may be provided in combination of more than one contiguous sequence. Also, it is expected that the overall sequence identity of the genomes between HGBV-B and a strain of HGBV-B at the amino acid level will be about 35% or greater since it is now believed that the HGBV strains may be genetically related, preferably about 40% or greater, more preferably, about 60% or greater, and even more preferably, about 80% or greater. In addition, there will be corresponding contiguous sequences of at least about 13 nucleotides, which may be provided in combination of more than one contiguous sequence. Also, it is expected that the overall sequence identity of the genomes between HGBV-C and a strain of HGBV-C at the amino acid level will be about 35% or greater since it is now believed that the HGBV strains may be genetically related, preferably about 40% or greater, more preferably, about 60% or greater, and even more preferably, about 80% or greater. In addition, there will be corresponding contiguous sequences of at least about 13 nucleotides, which may be provided in combination of more than one contiguous sequence. The compositions and methods described herein will enable the propagation, identification, detection and isolation of HGBV and its possible strains. Moreover, they also will allow the preparation of diagnostics and vaccines for the possible different strains of HGBV, and will have utility in screening procedures for anti-viral agents. The information will be sufficient to allow a viral taxonomist to identify other strains which fall within the species. We believe that HGBV encodes the sequences that are included herein. Methods for assaying for the presence of these sequences are known in the art and include, for example, amplification methods such as ligase chain reaction (LCR), polymerase chain reaction (PCR) and hybridization. In addition, these sequences contain open reading frames from which an immunogenic viral epitope may be found. This epitope is unique to HGBV when compared to other known hepatitis-causing viruses. The uniqueness of the epitope may be determined by its immunological reactivity with HGBV and lack of immunological reactivity with Hepatitis A, B, C, O and E viruses. Methods for determining immunological reactivity are known in the art and include, for example, radioimmunoassay (RIA), enzyme-linked immunosorbant assay (ELISA), hemagglutination (HA), fluorescence polarization immunoassay (FPIA) and several examples of suitable techniques are described herein. A polynucleotide "derived from" a designated sequence for example, the HGBV cPNA, or from the HGBV genome, refers to a polynucleotide sequence which is comprised of a sequence of approximately at least about 6 nucleotides, is preferably at least about 8 nucleotides, is more preferably at least about 10-12 nucleotides, and even more preferably is at least about 15-20 nucleotides corresponding, i.e., similar to or complementary to, a region of the designated nucleotide sequence. Preferably, the sequence of the region from which the polynucleotide is derived is similar to or complementary to a sequence which is unique to the HGBV genome. Whether or not a sequence is complementary to or similar to a sequence which is unique to an HGBV genome can be determined by techniques known to those skilled in the art. Comparisons to sequences in databanks, for example, can be used as a method to determine the uniqueness of a designated sequence. Regions from which sequences may be derived include but are not limited to regions encoding specific epitopes, as well as non-translated and/or non-transcribed regions. The derived polynucleotide will not necessarily be derived physically from the nucleotide sequence of HGBV, but may be generated in any manner, including but not limited to chemical synthesis, replication or reverse transcription or transcription, which are based on the information provided by the sequence of bases in the region(s) from which the polynucleotide is derived. In addition, combinations of regions corresponding to that of the designated sequence may be modified in ways known in the art to be consistent with an intended use. A "polypeptide" or "amino acid sequence derived from a designated nucleic acid sequence or from the HGBV genome refers to a polypeptide having an amino acid sequence identical to that of a polypeptide encoded in the sequence or a portion thereof wherein the portion consists of at least 3 to 5 amino acids, and more preferably at least 8 to 10 amino acids, and even more preferably 15 to 20 amino acids, or which is immunologically identifiable with a polypeptide encoded in the sequence. A "recombinant polypeptide" as used herein means at least a polypeptide of genomic, semisynthetic or synthetic origin which by virtue of its origin or manipulation is not associated with all or a portion of the polypeptide with which it is associated in nature or in the form of a library and/or is linked to a polynucleotide other than that to which it is linked in nature. A recombinant or derived polypeptide is not necessarily translated from a designated nucleic acid sequence of HGBV or from an HGBV genome. It also may be generated in any manner, including chemical synthesis or expression of a recombinant expression system, or isolation from mutated HGBV. The term "synthetic peptide" as used herein means a polymeric form of amino acids of any length, which may be chemically synthesized by methods well- known to the routineer. These synthetic peptides are useful in various applications. The term "polynucleotide" as used herein means a polymeric form of nucleotides of any length, either ribonucleotides or deoxyribonucleotides. This term refers only to the primary structure of the molecule. Thus, the term includes double- and single-stranded PNA, as well as double- and single-stranded RNA. It also includes modifications, either by methylation and/or by capping, and unmodified forms of the polynucleotide. "HGBV containing a sequence corresponding to a cPNA" means that the HGBV contains a polynucleotide sequence which is similar to or complementary to a sequence in the designated PNA. The degree of similarity or complementarity to the cPNA will be approximately 50% or greater, will preferably be at least about 70%, and even more preferably will be at least about 90%. The sequence which corresponds will be at least about 70 nucleotides, preferably at least about 80 nucleotides, and even more preferably at least about 90 nucleotides in length. The correspondence between the HGBV and the cPNA can be determined by methods known in the art, and include, for example, a direct comparison of the sequenced material with the cPNAs described, or hybridization and digestion with single strand nucleases, followed by size determination of the digested fragments. "Purified viral polynucleotide" refers to an HGBV genome or fragment thereof which is essentially free, i.e., contains less than about 50%, preferably less than about 70%, and even more preferably, less than about 90% of polypeptides with which the viral polynucleotide is naturally associated. Techniques for purifying viral polynucleotides are well known in the art and include, for example, disruption of the particle with a chaotropic agent, and separation of the polynucleotide(s) and polypeptides by ion-exchange chromatography, affinity chromatography, and sedimentation according to density. Thus, "purified viral polypeptide" means an HGBV polypeptide or fragment thereof which.is essentially free, that is, contains less than about 50%, preferably less than about 70%, and even more preferably, less than about 90% of of cellular components with which the viral polypeptide is naturally associated. Methods for purifying are known to the routineer. "Polypeptide" as used herein indicates a molecular chain of amino acids and does not refer to a specific length of the product. Thus, peptides, oligopeptides, and proteins are included within the definition of polypeptide. This term, however, is not intended to refer to post-expression modifications of the polypeptide, for example, glycosylations, acetylations, phosphorylations and the like. "Recombinant host cells," "host cells," "cells," "cell lines," "cell cultures," and other such terms denoting microorganisms or higher eucaryotic cell lines cultured as unicellular entities refer to cells which can be, or have been, used as recipients for recombinant vector or other transfer PNA, and include the original progeny of the original cell which has been transfected. As used herein "replicon" means any genetic element, such as a plasmid, a chromosome or a virus, that behaves as an autonomous unit of polynucleotide replication within a cell. That is, it is capable of replication under its own control. A "vector" is a replicon in which another polynucleotide segment is attached, such as to bring about the replication and/or expression of the attached segment. The term "control sequence refers to polynucleotide sequences which are necessary to effect the expression of coding sequences to which they are ligated. The nature of such control sequences differs depending upon the host organism. In prokaryotes, such control sequences generally include promoter, ribosomal binding site and terminators; in eukaryotes, such control sequences generally include promoters, terminators and, in some instances, enhancers. The term "control sequence thus is intended to include at a minimum all components whose presence is necessary for expression, and also may include additional components whose presence is advantageous, for example, leader sequences. "Operably linked" refers to a situation wherein the components described are in a relationship permitting them to function in their intended manner. Thus, for example, a control sequence'Operably linked" to a coding sequence is ligated in such a manner that expression of the coding sequence is achieved under conditions compatible with the control sequences. The term "open reading frame" or "ORF" refers to a region of a polynucleotide sequencewhich encodes a polypeptide; this region mayjrepresenta portion of a coding sequence or a total coding sequence. A "coding sequence" is a polynucleotide sequencewhich is transcribed into mRNA and/or translated into a polypeptide when placed under the control of appropriate regulatory sequences. The boundaries of the coding sequence are determined by a translation start codon at the 5' -terminus and a translation stop codon at the 3' -terminus. A coding sequence can include, but is not limited to, mRNA, cPNA, and recombinant polynucleotide sequences. The term "immunologically identifiable with as" refers to the presence of epitope(s) and polypeptide(s) which also are present in and are unique to the designated polypeptide(s), usually HGBV proteins. Immunological identity may be determined by antibody binding and/or competition in binding. These techniques are known to the routineer and also are described herein. The uniqueness of an epitope also can be determined by computer searches of known data banks, such as GenBank, for the polynucleotide sequences which encode the epitope, and by amino acid sequence comparisons with other known proteins. As used herein, "epitope" means an antigenic determinant of a polypeptide. Conceivably, an epitope can comprise three amino acids in a spatial conformation which is unique to the epitope. Generally, an epitope consists of at least five such amino acids, and more usually, it consists of at least eight to ten amino acids. Methods of examining spatial conformation are known in the art and include, for example, x-ray crystallography and two-dimensional nuclear magnetic resonance. A polypeptide is "immunologically reactive" with an antibody when it binds to an antibody due to antibody recognition of a specific epitope contained within the polypeptide. Immunological reactivity may be determined by antibody binding, more particularly by the kinetics of antibody binding, and/or by competition in binding using as competitor(s) a known polypeptide(s) containing an epitope against which the antibody is directed. The methods for determining whether a polypeptide is immunologically reactive with an antibody are known in the art. As used herein, the term "immunogenic polypeptide containing an HGBV epitope" means naturally occurring HGBV polypeptides or fragments thereof, as well as polypeptides prepared by other means, for example, chemical synthesis or the expression of the polypeptide in a recombinant organism. The term "transformation" refers to the insertion of an exogenous polynucleotide into a host cell, irrespective of the method used for the insertion. For example, direct uptake, rransduction, or f-mating are included. The exogenous polynucleotide may be maintained as a non-integrated vector, for example, a plasmid, or alternatively, may be integrated into the host genome. "Treatment" refers to prophylaxis and/or therapy. The term "individual" as used herein refers to vertebrates, particularly members of the mammalian species and includes but is not limited to domestic animals, sports animals, primates and humans; more particularly the term refers to tamarins and humans. The term "plus strand" (or "+") as used herein denotes a nucleic acid that contains the sequencethat encodes the polypeptide. The term "minus strand" (or "-") denotes a nucleic acid that contains a sequence that is complementary to that of the "plus" strand. "Positive stranded genome" of a virus denotes that the genome, whether RNA or PNA, is single-stranded and which encodes a viral polypeptide(s). The term "test sample" refers to a component of an individual's body which is the source of the analyte (such as, antibodies of interest or antigens of interest). These components are well known in the art. These test samples include biological samples which can be tested by the methods of the present invention described herein and include human and animal body fluids such as whole blood, serum, plasma, cerebrospinal fluid, urine, lymph fluids, and various external secretions of the respiratory, intestinal and genitorurinary tracts, tears, saliva, milk, white blood cells, myelomas and the like; biological fluids such as cell culture supernatants; fixed tissue specimens; and fixed cell specimens. "Purified HGBV" refers to a preparation of HGBV which has been isolated from the cellular constituents with which the virus is normally associated, and from other types of viruses which may be present in the infected tissue. The techniques for isolating viruses are known to those skilled in the art and include, for example, centrifugation and affinity chromatography. "PNA" denotes a "peptide nucleic analog" which may be utilized in a procedure such as an assay to determine the presence of a target. PNAs are neutrally charged moieties which can be directed against RNA targets or PNA. PNA probes used in assays in place of, for example, PNA probes, offer advantages not acheivable when PNA probes are used. These advantages include manufacturability, large scale labeling, reproducibility, stability, insensitivity to changes in ionic strength and resistance to enzymatic degradation which is present in methods utilizing PNA or RNA. These PNAs can be labeled with such signal generating compounds as flouorescein, radionucleotides, chemiluminescent compounds, and the like. PNAs thus can be used in methods in place of PNA or RNA. Although assays are described herein utilizing PNA, it is within the scope of the routineer that PNAs can be substituted for RNA or PNA with appropriate changes if and as needed in assay reagents. General Uses After preparing recombinant proteins, synthetic peptides, or purified viral polypeptides of choice as described by the present invention, the recombinant or synthetic peptides can be used to develop unique assays as described herein to detect either the presence of antigen or antibody to HGBV. These compositions also can be used to develop monoclonal and/or polyclonal antibodies with a specific recombinant protein or synthetic peptide which specifically bind to the immunological epitope of HGBV which is desired by the routineer. Also, it is contemplated that at least one polynucleotide of the invention can be used to develop vaccines by following methods known in the art. It is contemplated that the reagent employed for the assay can be provided in the form of a test kit with one or more containers such as vials or bottles, with each container containing a separate reagent such as a monoclonal antibody, or a cocktail of monoclonal antibodies, or a polypeptide (either recombinant or synthetic) employed in the assay. Other components such as buffers, controls, and the like, known to those of ordinary skill in art, may be included in such test kits. "Solid phases" ("solid supports") are known to those in the art and include the walls of wells of a reaction tray, test tubes, polystyrene beads, magnetic beads, nitrocellulose strips, membranes, microparticles such as latex particles, sheep (or other animal) red blood cells, duracytes and others. The "solid phase" is not critical and can be selected by one skilled in the art. Thus, latex particles, microparticles, magnetic or non-magnetic beads, membranes, plastic tubes, walls of microtiter wells, glass or silicon chips, sheep (or other suitable animal's) red blood cells and duracytes are all suitable examples. Suitable methods for immobilizing peptides on solid phases include ionic, hydrophobic, covalent interactions and the like. A "solid phase", as used herein, refers to any material which is insoluble, or can be made insoluble by a subsequent reaction. The solid phase can be chosen for its intrinsic ability to attract and immobilize the capture reagent. Alternatively, the solid phase can retain an additional receptor which has the ability to attract and immobilize the capture reagent. The additional receptor can include a charged substance that is oppositely charged with respect to the capture reagent itself or to a charged substance conjugated to the capture reagent. As yet another alternative, the receptor molecule can be any specific binding member which is immobilized upon (attached to) the solid phase and which has the ability to immobilize the capture reagent through a specific binding reaction. The receptor molecule enables the indirect binding of the capture reagent to a solid phase material before the performance of the assay or during the performance of the assay. The solid phase thus can be a plastic, derivatized plastic, magnetic or non- magnetic metal, glass or silicon surface of a test tube, microtiter well, sheet, bead, microparticle, chip, sheep (or other suitable animal's) red blood cells, duracytes and other configurations known to those of ordinary skill in the art. It is contemplated and within the scope of the invention that the solid phase also can comprise any suitable porous material with sufficient porosity to allow access by detection antibodies and a suitable surface affinity to bind antigens. Microporous structures are generally preferred, but materials with gel structure in the hydrated state may be used as well. Such useful solid supports include: natural polymeric carbohydrates and their synthetically modified, cross-linked or substituted derivatives, such as agar, agarose, cross-linked alginic acid, substituted and cross-linked guar gums, cellulose esters, especially with nitric acid and carboxylic acids, mixed cellulose esters, and cellulose ethers; natural polymers containing nitrogen, such as proteins and derivatives, including cross-linked or modified gelatins; natural hydrocarbon polymers, such as latex and rubber; synthetic polymers which may be prepared with suitably porous structures, such as vinyl polymers, including polyethylene, polypropylene, polystyrene, polyvinylchloride, polyvinylacetate and its partially hydrolyzed derivatives, polyacrylamides, polymethacrylates, copolymers and terpolymers of the above polycondensates, such as polyesters, polyamides, and other polymers, such as polyurethanes or polyepoxides; porous inorganic materials such as sulfates or carbonates of alkaline earth metals and magnesium, including barium sulfate, calcium sulfate, calcium carbonate, silicates of alkali and alkaline earth metals, aluminum and magnesium; and aluminum or silicon oxides or hydrates, such as clays, alumina, talc, kaolin, zeolite, silica gel, or glass (these materials may be used as filters with the above polymeric materials); and mixtures or copolymers of the above classes, such as graft copolymers obtained by initializing polymerization of synthetic polymers on a pre-existing natural polymer. All of these materials may be used in suitable shapes, such as films, sheets, or plates, or they may be coated onto or bonded or laminated to appropriate inert carriers, such as paper, glass, plastic films, or fabrics. The porous structure of nitrocellulose has excellent absorption and adsorption qualities for a wide variety of reagents including monoclonal antibodies. Nylon also possesses similar characteristics and also is suitable. It is contemplated that such porous solid supports described hereinabove are preferably in the form of sheets of thickness from about 0.01 to 0.5 mm, preferably about 0.1 mm. The pore size may vary within wide limits, and is preferably from about 0.025 to 15 microns, especially from about 0.15 to 15 microns. The surfaces of such supports may be activated by chemical processes which cause covalent linkage of the antigen or antibody to the support. The irreversible binding of the antigen or antibody is obtained, however, in general, by adsorption on the porous material by poorly understood hydrophobic forces. Suitable solid supports also are described in U.S. Patent Application Serial No. 227,272. The "indicator reagent "comprises a "signal generating compound" (label) which is capable of generating and generates a measurable signal detectable by external means conjugated (attached) to a specific binding member for HGBV. "Specific binding member" as used herein means a member of a specific binding pair. That is, two different molecules where one of the molecules through chemical or physical means specifically binds to the second molecule. In addition to being an antibody member of a specific binding pair for HGBV, the indicator reagent also can be a member of any specific binding pair, including either hapten- anti-hapten systems such as biotin or anti-biotin, avidin or biotin, a carbohydrate or a lectin, a complementary nucleotide sequence, an effector or a receptor molecule, an enzyme cofactor and an enzyme, an enzyme inhibitor or an enzyme, and the like. An immunoreactive specific binding member can be an antibody, an antigen, or an antibody/antigen complex that is capable of binding either to HGBV as in a sandwich assay, to the capture reagent as in a competitive assay, or to the ancillary specific binding member as in an indirect assay. The various "signal generating compounds" (labels) contemplated include chromogens, catalysts such as enzymes, luminescent compounds such as fluorescein and rhodamine, chemiluminescent compounds such as dioxetanes, acridiniums, phenanthridiniums and luminol, radioactive elements, and direct visual labels. Examples of enzymes include alkaline phosphatase, horseradish peroxidase, beta-galactosidase, and the like. The selection of a particular label is not critical, but it will be capable of producing a signal either by itself or in conjunction with one or more additional substances. The present invention provides assays which utilize specific binding members. A "specific binding member," as used herein, is a member of a specific binding pair. That is, two different molecules where one of the molecules through chemical or physical means specifically binds to the second molecule—Therefore, in addition to antigen and antibody specific binding pairs of common immunoassays, other specific binding pairs can include biotin and avidin, carbohydrates and lectins, complementary nucleotide sequences, effector and receptor molecules, cofactors and enzymes, enzyme inhibitors and enzymes, and the like. Furthermore, specific binding pairs can include members that are analogs of the original specific binding members, for example, an analyte-analog. Immunoreactive specific binding members include antigens, antigen fragments, antibodies and antibody fragments, both monoclonal and polyclonal, and complexes thereof, including those formed by recombinant PNA molecules. The term "hapten", as used herein, refers to a partial antigen or non-protein binding member which is capable of binding to an antibody, but which is not capable of eliciting antibody formation unless coupled to a carrier protein. "Analyte," as used herein, is the substance to be detected which may be present in the test sample. The analyte can be any substance for which there exists a naturally occurring specific binding member (such as, an antibody), or for which a specific binding member can be prepared. Thus, an analyte is a substance that can bind to one or more specific binding members in an assay. "Analyte" also includes any antigenic substances, haptens, antibodies, and combinations thereof. As a member of a specific binding pair, the analyte can be detected by means of naturally occurring specific binding partners (pairs) such as the use of intrinsic factor protein as a member of a specific binding pair for the determination of Vitamin B 12, the use of folate-binding protein to determine folic acid, or the use of a lectin as a member of a specific binding pair for the determination of a carbohydrate. The analyte can include a protein, a peptide, an amino acid, a nucleotide target, and the like. Other embodiments which utilize various other solid phases also are contemplated and are within the scope of this invention. For example, ion capture procedures for immobilizing an immobilizable reaction complex with a negatively charged polymer, described in co-pending U. S. Patent Application Serial No. 150,278 corresponding to EP publication 0326100 and U. S. Patent Application Serial No. 375,029 (EP publication no. 0406473), can be employed according to the present invention to effect a fast solution-phase immunochemical reaction. An immobilizable immune complex is separated from the rest of the reaction mixture by ionic interactions between the negatively charged poly-anion/immune complex and the previously treated, positively charged porous matrix and detected by using various signal generating systems previously described, including those described in chemiluminescent signal measurements as described in co-pendingU.S. Patent Application Serial No.921,979 corresponding to EPO Publication No. 0 273,115. Also, the methods of the present invention can be adapted for use in systems which utilize microparticle technology including in automated and semi- automated systems wherein the solid phase comprises a microparticle (magnetic or non-magnetic). Such systems include those described in pending U. S. Patent Applications 425,651 and 425,643, which correspond to published EPO applications Nos. EP 0425 633 and EP 0424 634, respectively. The use of scanning probe microscopy (SPM) for immunoassays also is a technology to which the monoclonal antibodies of the present invention are easily adaptable. In scanning probe microscopy, in particular in atomic force microscopy, the capture phase, for example, at least one of the monoclonal antibodies of the invention, is adhered to a solid phase and a scanning probe microscope is utilized to detect antigen/antibody complexes which may be present on the surface of the solid phase. The use of scanning tunnelling microscopy eliminates the need for labels which normally must be utilized in many immunoassay systems to detect antigen/antibody complexes. Such a system is described in pending U. S. patent application Serial No. 662,147. The use of SPM to monitor specific binding reactions can occur in many ways. In one embodiment, one member of a specific binding partner (analyte specific substance which is the monoclonal antibody of the invention) is attached to a surface suitable for scanning. The attachment of the analyte specific substance may be by adsorption to a test piece which comprises a solid phase of a plastic or metal surface, following methods known to those of ordinary skill in the art. Or, covalent attachment of a specific binding partner (analyte specific substance) to a test piece which test piece comprises a solid phase of derivatized plastic, metal, silicon, or glass may be utilized. Covalent attachment methods are known to those skilled in the art and include a variety of means to irreversibly link specific binding partners to the test piece. If the test piece is silicon or glass, the surface must be activated prior to attaching the specific binding partner. Activated silane compounds such as triethoxy amino propyl silane (available from Sigma Chemical Co., St. Louis, MO), triethoxy vinyl silane (Aldrich Chemical Co., Milwaukee, WI), and (3-mercapto-propyl)-trimethoxy silane (Sigma Chemical Co., St. Louis, MO) can be used to introduce reactive groups such as amino-, vinyl, and thiol, respectively. Such activated surfaces can be used to link the binding partner directly (in the cases of amino or thiol) or the activated surface can be further reacted with linkers such as glutaraldehyde, bis (succinimidyl) suberate, SPPP 9 succinimidyl 3-[2-pyridyldithio] propionate), SMCC (succinimidyl-4τ[N- maleimidomethyl] cyclohexane-1-carboxylate), SIAB (succinimidyl [4-iodoacetyl] aminobenzoate), and SMPB (succinimidyl 4-[l-maleimidophenyl] butyrate) to separate the binding partner from the surface. The vinyl group can be oxidized to provide a means for covalent attachment. It also can be used as an anchor for the polymerization of various polymers such as poly acrylic acid, which can provide multiple attachment points for specific binding partners. The amino surface can be reacted with oxidized dextrans of various molecular weights to provide hydrophilic linkers of different size and capacity. Examples of oxidizable dextrans include Pextran T-40 (molecular weight 40,000 daltons), Pextran T-l 10 (molecular weight 110,000 daltons), Pextran T-500 (molecular weight 500,000 daltons), Pextran T-2M (molecular weight 2,000,000 daltons) (all of which are available from Pharmacia), or Ficoll (molecular weight 70,000 daltons (available from Sigma Chemical Co., St. Louis, MO). Also, polyelectrolyte interactions may be used to immobilize a specific binding partner on a surface of a test piece by using techniques and chemistries described by pending U. S. Patent applications Serial No. 150,278, filed January 29, 1988, and Serial No. 375,029, filed July 7, 1989. The preferred method of attachment is by covalent means. Following attachment of a specific binding member, the surface may be further treated with materials such as serum, proteins, or other blocking agents to minimize non-specific binding. The surface also may be scanned either at the site of manufacture or point of use to verify its suitability for assay purposes. The scanning process is not anticipated to alter the specific binding properties of the test piece. Various other assay formats may be used, including "sandwich" immunoassays and probe assays. For example, the monoclonal antibodies of the present invention can be employed in various assay systems to determine the presence, if any, of HGBV proteins in a test sample. Fragments of these monoclonal antibodies provided also may be used. For example, in a first assay format, a polyclonal or monoclonal anti-HGBV antibody or fragment thereof, or a combination of these antibodies, which has been coated on a solid phase, is contacted with a test sample which may contain HGBV proteins, to form a mixture. This mixture is incubated for a time and under conditions sufficient to form antigen/antibody complexes. Then, an indicator reagent comprising a monoclonal or a polyclonal antibody or a fragment thereof, which specifically binds to an HGBV region, or a combination of these antibodies, to which a signal generating compound has been attached, is contacted with the antigen/antibody complexes to form a second mixture. This second mixture then is incubated for a time and under conditions sufficient to form antibody/antigen/antibody complexes. The presence of HGBV antigen present in the test sample and captured on the solid phase, if any, is determined by detecting the measurable signal generated by the signal generating compound. The amount of HGBV antigen present in the test sample is proportional to the signal generated. Alternatively, a polyclonal or monoclonal anti-HGBV antibody or fragment thereof, or a combination of these antibodies which is bound to a solid support, the test sample and an indicator reagent comprising a monoclonal or polyclonal antibody or fragments thereof, which specifically binds to HGBV antigen, or a combination of these antibodies to which a signal generating compound is attached, are contacted to form a mixture. This mixture is incubated for a time and under conditions sufficient to form antibody/antigen/antibody complexes. The presence, if any, of HGBV proteins present in the test sample and captured on the solid phase is determined by detecting the measurable signal generated by the signal generating compound. The amount of HGBV proteins present in the test sample is proportional to the signal generated. In another alternate assay format, one or a combination of at least two monoclonal antibodies of the invention can be employed as a competitive probe for the detection of antibodies to HGBV protein. For example, HGBV proteins, either alone or in combination, can be coated on a solid phase. A test sample suspected of containing antibody to HGBV antigen then is incubated with an indicator reagent comprising a signal generating compound and at least one monoclonal antibody of the invention for a time and under conditions sufficient to form antigen/antibody complexes of either the test sample and indicator reagent to the solid phase or the indicator reagent to the solid phase. The reduction in binding of the monoclonal antibody to the solid phase can be quantitatively measured. A measurable reduction in the signal compared to the signal generated from a confirmed negative NANB, non-C, non-O, non-E hepatitis test sample indicates the presence of anti-HGBV antibody in the test sample. In yet another detection method, each of the monoclonal or polyclonal antibodies of the present invention can be employed in the detection of HGBV antigens in fixed tissue sections, as well as fixed cells by immunohistochemical analysis. Cytochemical analysis wherein these antibodies are labelled directly (fluorescein, colloidal gold, horseradish peroxidase, alkaline phosphatase, etc.) or are labelled by using secondary labelled anti-species antibodies (with various labels as exemplified herein) to track the histopathology of disease also are within the scope of the present invention. In addition, these monoclonal antibodies can be bound to matrices similar to CNBr-activated Sepharose and used for the affinity purification of specific HGBV proteins from cell cultures, or biological tissues such as blood and liver such as to purify recombinant and native viral HGBV antigens and proteins. The monoclonal antibodies of the invention can also be used for the generation of chimeric antibodies for therapeutic use, or other similar applications. The monoclonal antibodies or fragments thereof can be provided individually to detect HGBV antigens. Combinations of the monoclonal antibodies (and fragments thereof) provided herein also may be used together as components in a mixture or "cocktail" of at least one anti-HGBV antibody of the invention with antibodies to other HGBV regions, each having different binding specificities. Thus, this cocktail can include the monoclonal antibodies of the invention which are directed to HGBV proteins and other monoclonal antibodies to other antigenic determinants of the HGBV genome. The polyclonal antibody or fragment thereof which can be used in the assay formats should specifically bind to a specific HGBV region or other HGBV proteins used in the assay. The polyclonal antibody used preferably is of mammalian origin; human, goat, rabbit or sheep anti-HGBV polyclonal antibody can be used. Most preferably, the polyclonal antibody is rabbit polyclonal anti- HGBV antibody. The polyclonal antibodies used in the assays can be used either alone or as a cocktail of polyclonal antibodies. Since the cocktails used in the assay formats are comprised of either monoclonal antibodies or polyclonal antibodies having different HGBV specificity, they would be useful for diagnosis, evaluation and prognosis of HGBV infection, as well as for studying HGBV protein differentiation and specificity. It is contemplated and within the scope of the present invention that the HGBV group of viruses may be detectable in assays by use of a synthetic, recombinant or native peptide that is common to all HGBV viruses. It also is within the scope of the present invention that different synthetic, recombinant or native peptides isentifying different epitopes from HGBV-A, HGBV-B, HGBV- C, or yet other HGBV viruses, can be used in assay formats. In the later case, these can be coated onto one solid phase, or each separate peptide may be coated on separate solid phases, such as microparticles, and then combined to form a mixture of peptides which can be later used in assays. Such variations of assay formats are known to those of ordinary skill in the art and are discussed hereinbelow. In another assay format, the presence of antibody and/or antigen to HGBV can be detected in a simultaneous assay, as follows. A test sample is .. simultaneously contacted with a capture reagent of a first analyte, wherein said capture reagent comprises a first binding member specific for a first analyte attached to a solid phase and a capture reagent for a second analyte, wherein said capture reagent comprises a first binding member for a second analyte attached to a second solid phase, to thereby form a mixture. This mixture is incubated for a time and under conditions sufficient to form capture reagent/first analyte and capture reagent/second analyte complexes. These so-formed complexes then are contacted with an indicator reagent comprising a member of a binding pair specific for the first analyte labelled with a signal generating compound and an indicator reagent comprising a member of a binding pair specific for the second analyte labelled with a signal generating compound to form a second mixture. This second mixture is incubated for a time and under conditions sufficient to form capture reagent/first analyte/indicator reagent complexes and capture reagent/second analyte/indicator reagent complexes. The presence of one or more analytes is determined by detecting a signal generated in connection with the complexes formed on either or both solid phases as an indication of the presence of one or more analytes in the test sample. In this assay format, proteins derived from human expression systems may be utilized as well as monoclonal antibodies produced from the proteins derived from the mammalian expression systems as disclosed herein. Such assay systems are described in greater detail in pending U.S. Patent Application Serial No. 07/574,821 entitled Simultaneous Assay for Petecting One Or More Analytes, which corresponds to EP Publication No. 0473065. In yet other assay formats, recombinant proteins and or synthetic peptides may be utilized to detect the presence of anti-HGBV in test samples. For example, a test sample is incubated with a solid phase to which at least one recombinant protein or synthetic peptide has been attached. These are reacted for a time and under conditions sufficient to form antigen/antibody complexes. Following incubation, the antigen/antibody complex is detected. Indicator reagents may be used to facilitate detection, depending upon the assay system chosen. In another assay format, a test sample is contacted with a solid phase to which a recombinant protein or synthetic peptide produced as described herein is attached and also is contacted with a monoclonal or polyclonal antibody specific for the protein, which preferably has been labelled with an indicator reagent. After incubation for a time and under conditions sufficient for antibody/antigen complexes to form, the solid phase is separated from the free phase, and the label is detected in either the solid or free phase as an indication of the presence of HGBV antibody. Other assay formats utilizing the proteins of the present invention are contemplated. These include contacting a test sample with a solid phase to which at least one antigen from a first source has been attached, incubating the solid phase and test sample for a time and under conditions sufficient to form antigen/antibody complexes, and then contacting the solid phase with a labelled antigen, which antigen is derived from a second source different from the first source. For example, a recombinant protein derived from a first source such as E. coli is used as a capture antigen on a solid phase, a test sample is added to the so-prepared solid phase, and a recombinant protein derived from a different source (i.e., non-E. coli) is utilized as a part of an indicator reagent. Likewise, combinations of a recombinant antigen on a solid phase and synthetic peptide in the indicator phase also are possible. Any assay format which utilizes an antigen specific for HGBV from a first source as the capture antigen and an antigen specific for HGBV from a different second source are contemplated. Thus, various combinations of recombinant antigens, as well as the use of synthetic peptides, purified viral proteins, and the like, are within the scope of this invention. Assays such as this and others are described in U.S. Patent No. 5,254,458, which enjoys common ownership and is incorporated herein by reference. Other assay systems which utilize an antibody (polyclonal, monoclonal or naturally-occurring) which specifically binds HGBV viral particles or sub-viral particles housing the viral genome (or fragments thereof) by virtue of a contact between the specific antibody and the viral protein (peptide, etc.). This captured particle then can be analyzed by methods such as LCR or PCR to determine whether the viral genome is present in the test sample. Test samples which can be assayed according to this method include blood, liver, sputum, urine, fecal material, saliva, and the like. The advantage of utilizing such an antigen capture amplification method is that it can separate the viral genome from other molecules in the test specimen by use of a specific antibody. Such a method has been described in pending U.S. patent application Serial No. 08/141,429. While the present invention discloses the preference for the use of solid phases, it is contemplated that the reagents such as antibodies, proteins and peptides of the present invention can be utilized in non-solid phase assay systems. These assay systems are known to those skilled in the art, and are considered to be within the scope of the present invention. Materials and Methods General Techniques Conventional and well-known techniques and methods in the fields of molecular biology, microbiology, recombinant PNA and immunology are employed in the practice of the invention unless otherwise noted. Such techniques are explained and detailed in the literature. See, for example, J. Sambrook et al., Molecular Cloning: A Laboratory Manual. 2nd edition, Cold Spring Harbor Press, Cold Spring Harbor, N.Y. (1989); P. N. Glover, ed., PNA Cloning. Volumes I and ll (1985); M.J. Gait ed., Oligonucleotide Svnthesis. (1984); B.P. Hames et al., eds., Nucleic Acid Hybridization. (1984); B.P. Hames et al., eds., Transcription and Translation. (1984); R. I. Freshney ed., Animal Cell Culture. (1986); Immobilized Cells and Enzymes. IRL Press (1986); B. Perbal, A Practical Guide to Molecular Cloning. (1984): the series. Methods in Enzymology. Academic Press, Inc., Orlando, Florida; J. H. Miller et al., eds., Gene Transfer Vectors For Mammalian Cells. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y. (1987); Wu et al., eds., Methods in Enzymology, Vol. 154 and 155 ; Mayer et al., eds., Immunological Methods In Cell and Molecular Biology. Academic Press, London (1987); Scopes, Protein Purification: Principles and Practice. 2nd ed., Springer- Verlag, N.Y.; and P. Weir et al., eds., Handbook Of Experimental Immunology. Volumes I-JN (1986); Ν. Lisitisyn et al., Science 259:946-951 (1993). The reagents and methods of the present invention are made possible by the provision of a family of closely related nucleotide sequences, isolated by representational difference analysis modified as described herein, present in the plasma, serum or liver homogenate of an HGBN infected individual, either tamarin or human. This family of nucleotide sequences is not of human or tamarin origin, since it will be shown that it hybridizes to neither human nor tamarin genomic OΝA from uninfected individuals, since nucleotides of this family of sequences are present only in liver (or liver homogenates), plasma or serum of individuals infected with HGBV, and since the sequence is not present in GenBank. In addition, the family of sequences will show no significant identity at the nucleic acid level to sequences contained within the HAV, HBV, HCV, HPV and HEV genome, and low level identity, considered not significant, as translation products. Infectious sera, plasma or liver homogenates from HGBV infected humans contain these polynucleotide sequences, whereas sera, plasma or liver homogenates from non-infected humans do not contain these sequences. Northern blot analysis of infected liver with some of these polynucleotide sequences demonstrate that they are derived from a large RNA transcript similar in size to a viral genome. Sera, plasma or liver homogenates from HGBV-infected humans contain antibodies which bind to this polypeptide, whereas sera, plasma or liver homogenates from non-infected humans do not contain antibodies to this polypeptide; these antibodies are induced in individuals following acute non-A, non-B, non-C, non-P and non- E infection. By these criteria, it is believed that the sequence is a viral sequence, wherein the virus causes or is associated with non-A, non-B, non-C, non-P and non-E hepatitis. The availability of this family of nucleic acid sequences permits the construction of PNA probes and polypeptides useful in diagnosing non-A, non-B, non-C, non-P, non-E hepatitis due to HGBV infections, and in screening blood donors, donated blood, blood products and individuals for infection. For example, from the sequence it is possible to synthesize PNA oligomers of about eight to ten nucleotides, or larger, which are useful as hybridization probes or PCR primers to detect the presence of the viral genome in, for example, sera of subjects suspected of harboring the virus, or for screening donated blood for the presence of the virus. The family of nucleic acid sequences also allows the design and production of HGBV specific polypeptides which are useful as diagnostic reagents for the presence of antibodies raised during infection with HGBV. Antibodies to purified polypeptides derived from the nucleic acid sequences may also be used to detect viral antigens in infected individuals and in blood. These nucleic acid sequences also enable the design and production of polypeptides which may be used as vaccines against HGBV, and also for the production of antibodies, which then may be used for protection of the disease, and/or for therapy of HGBV infected individuals. The family of nucleic acid sequences also enables further characterization of the HGBV genome. Polynucleotide probes derived from these sequences may be used to screen genomic or cPNA libraries for additional overlapping nucleic acid sequences which then may be used to obtain more overlapping sequences. Unless the genome is segmented and the segments lack common sequences, this technique may be used to gain the sequence of the entire genome. However, if the genome is segmented, other segments of the genome can be obtained by either repeating the RPA cloning procedure as described and modified hereinbelow or by repeating the lambda-gtl 1 serological screening procedure discussed hereinbelow to isolate the clones which will be described herein, or alternatively by isolating the genome from purified HGBV particles. The family of cPNA sequences and the polypeptides derived from these sequences, as well as antibodies directed against these polypeptides, also are useful in the isolation and identification of the HGBV etiological agent(s). For example, antibodies directed against HGBV epitopes contained in polypeptides derived from the nucleic acid sequences may be used in methods based upon affinity chromatography to isolate the virus. Alternatively, the antibodies can be used to identify viral particles isolated by other techniques. The viral antigens and the genomic material within the isolated viral particles then may be further characterized. The information obtained from further sequencing of the HGBV genome(s), as well as from further characterization of the HGBV antigens and characterization of the genome enables the design and synthesis of additional probes and polypeptides and antibodies which may be used for diagnosis, prevention and therapy of HGBV induced non-A, non-B, non-C non-P, non-E hepatitis, and for screening of infected blood and blood-related products. The availability of probes for HGBV, including antigens, antibodies and polynucleotides derived from the genome from which the family of nucleic acid sequences is derived also allows for the development of tissue culture systems which will be of major use in elucidating the biology of HGBV. Once this is known, it is contemplated that new treatment regimens may be developed based upon antiviral compounds which preferentially inhibit the replication of or infection by HGBV. In one method used to identify and isolate the etiological agent of HGBV, the cloning/isolation of the GB agent was achieved by modifying the published procedure known as representational difference analysis (RPA), as reported by N. Lisitsyn et al., Science 259: 946-951 (1993). This method is based upon the principles of subtractive hybridization for cloning PNA differences between two complex mammalian genomes. Briefly, in this procedure, the two genomes under evaluation are identified generically as the "tester" (containing the target sequence of interest) and the "driver" (representing normal PNA). Lisitsyn et al.'s description of RPA is limited to identifying and cloning PNA differences between complex, but similar PNA backgrounds. These differences may include any large PNA viruses (eg. >25,000 base pairs of PNA) that is present in a cell line, blood, plasma or tissue sample and absent in an uninfected cell line, blood, plasma or tissue sample. Because previous literature suggested that HGBV may be a small virus containing either a PNA or RNA genome of < 10,000 bases, the RPA protocol was modified such as to allow the detection of small viruses. The major steps of the procedure are described hereinbelow and are diagramed in FIGURE 13. Briefly, in step 1 , total nucleic acid (PNA and RNA) is isolated using commercially available kits. RPA requires that the sample be highly matched. Ideally, tester and driver nucleic acid samples should be obtained from the same source (animal, human or other). It may be possible to use highly related, but non-identical, material for the source of the tester and driver nucleic acids. Pouble stranded PNA is generated from the total nucleic acid by random primed reverse transcription of the RNA followed by random primed PNA synthesis. This treatment converts single strand RNA viruses and single strand PNA viruses to double strand PNA molecules which are ammenable to RPA. If one chooses to assume that an unknown virus has a PNA or an RNA genome, a PNA-only or RNA-only extraction procedure can be employed and double-stranded PNA can be generated as described in the art. In step 2, the tester and driver nucleic acids are amplified to generate an abundant amount of material which represents the total nucleic acid extracted from the pre-inoculation and infectious plasma sources (ie. the tester amplicon and the driver amplicon). This is achieved by cleaving double-stranded PNA prepared as described above with a restriction endonuclease which has a 4 bp recognition site (such as Sau3A I). The PNA fragments are ligated to oligonucleotide adaptors (set #1). The PNA fragments are end-filled and PCR amplified. Following PCR amplification, the oligonucleotide adaptor (set #1) is then removed by restriction endonuclease digestion (for example, with Sau3 A I), liberating a large amount of tester and driver nucleic acid to be used in subsequent subtractive hybridization techniques. In step 3, the experimental design is to enrich for PNA unique to the tester genome. This is achieved by combining subtractive hybridization and kinetic enrichment into a single step. Briefly, an oligonucleotide adaptor set (#2 or #3) is ligated to the 5' ends of the tester amplicon. The tester amplicon and an excess of driver amplicon are mixed, denatured and allowed to hybridized for 20 hours. A large amount of the sequences that are held in common between the tester and driver PNA will anneal during this time. In addition, sequences that are unique to the tester amplicon will reanneal. However, because of the limited time of hybridization, some single-standed tester and driver PNA will remain. In step 4, the 3' ends of the reannealed tester and driver PNA are filled in using a thermostable PNA polymerase at elevated temperature as described in the art. The reannealed sequences that are unique to the tester contain the ligated adaptor on both strands of the annealed sequence. Thus, 3' end-filling of these molecules creates sequences complementary to PCR primers on both PNA strands. As such, these PNA species will be amplified exponentially when subjected to PCR. In contrast, the relatively large amount of hybrid molecules containing sequences held in common between tester and driver amplicons (ie. one strand was derived from the tester amplicon and one strand was derived from the driver amplicon) will be amplified linearly when subjected to PCR. This is because only one strand (derived from the tester amplicon) contains the ligated adaptor sequence, and 3' end filling will only generate sequences complementary to the PCR primer on the strand derived from the driver amplicon. In step 5, the double-strand PNA of interest is enriched quantitatively using PCR for 10 cycles of amplification. As stated above in step 4, reannealed tester sequences will be amplified exponentially whereas sequences held in common between tester and driver amplicons will be amplified linearly. In step 6, single-strand PNA which remains is removed by a single strand PNA nuclease digestion using mung bean nuclease as described in the art. In step 7, double-stranded PNA which remains after nuclease digestion is PCR amplified an additional 15 to 25 cycles. Finally in step 8, these PNA products are cleaved with restriction endonuclease to remove the oligonucleotide adaptors. These PNA products can then be subjected to subsequent rounds of amplification (beginning at step #3 using the oligonucleotide adaptor set that was not used in the previous cycle of RPA) or cloned into a suitable plasmid vector for further analysis. The RPA procedure as described supra is a modification of the representational difference analysis known in the art. The method was modified to isolate viral clones from pre-inoculation and infectious sera sources. These modifications are discussed further below and relate to the preparation of amplicons for both tester and driver PNA. First, the starting material was not double-stranded PNA obtained from the genomic PNA of mammalian cells as reported previously, but total nucleic acid extracted from infectious and pre- inoculation biological blood samples obtained from tamarins. It is possible that other biological samples (for example, organs, tissue, bile, feces or urine) could be used as sources of nucleic acid from which tester and driver amplicons are generated. Second, the amount of starting nucleic acid is substantially less than that described in the art. Third, a restriction endonuclease with a 4 bp instead of a 6 bp recognition site was used. This is substantially different from the prior art. Lisitsyn et al. teach that RPA works because the generation of amplicons (ie. representations) decreases the complexity of the PNA that is being hybridized (ie. subtracted). In the prior art, restriction enzymes that have 6 bp recognition sites were used to fragment the genome. These restriction endonucleases cleave.. approximately every 4000 bp. However, the PCR conditions described in the prior art amplify sequences <1500 bp in size. Therefore, subsequent PCR amplification of a complex species of PNA (such as a genome) that has been fragmented with a restriction enzyme that recognizes a 6 bp sequence results in the generation of amplicons that contain the fraction of the PNA that was <1500 bp in size after restriction endonuclease digestion. This reduction in PNA complexity (estimated to be a 10- to 50-fold reduction) is reported to be necessary for the hybridization step of RPA to work. If the complexity is not reduced, unique sequences in the tester will not be able to efficiently hybridize during the subtraction step, and therefore, these unique sequences will not be amplified exponentially during the subsequent PCR steps of RPA. The reduction of complexity of the nucleic acid sequences being subjected to RPA undermines using RPA effectively to isolate relatively small viruses. The odds of two 6 bp-recognition sites occurring within 1.5 kb of each other is sufficiently rare that one might miss a small (<10 kb) virus (TABLE 1). However, we have discovered that RPA may be useful in cloning small viruses if a more frequently cutting restriction endonuclease is used to fragment the PNA being subjected to RPA. As shown in TABLE 1, amplicons based on 4 bp recognition site enzymes will almost certainly contain several fragments from any small virus, as restriction endonucleases which have 4 bp recognition sites fragment PNA approximately every 250 base pairs. However, it is likely that amplicons will be as complex as the source of the nucleic acid from which they were generated because nearly all of the PNA species will be <1500 bp after digestion with a 4 bp recognizing restriction endonuclease and thus, subject to PCR amplification. Since the relative viral sequence copy number is predicted to be higher than any specific or endogenous sequence copy number, the unique viral sequences that are present in the tester amplicon should be able to form double stranded molecules during the hybridization step (step 3, above). Therefore, these sequences will be amplified expontentially as described above. It is reasoned that as the relative viral sequence copy number becomes closer to that of the background or endogenous nucleic acid sequence copy number, a restriction endonuclease which recognizes a redundant 6 bp sequence (for example BstYI or HincII) and cleaves approximately every 1000 bp, or the simultaneous use of several restriction endonuclease which recognizes 6 bp sequences, may be used to fragment the PNA prior to amplification by PCR. In this way, one can moderately reduce the complexity of the amplicons being subjected to RPA while minimizing the risk of excluding viral sequeces from the tester amplicon. The utility of this procedure is demonstrated by the cloning of HGBV sequences from infectious tamarin plasma described herein. Immunoscreening to identify HGBV immunoreactive epitopes Imrnunoscreening as described herein as follows also provided an additional means of identifying HGBV sequences. Pooled or individual serum, plasma or liver homogenates from an individual meeting the criteria and within the parameters set forth below with acute or chronic HGBV infection is used to isolate viral particles. Nucleic acids isolated from these particles are used as the template in the construction of a genomic and or cPNA library to the viral genome. The procedures used for isolation of putative HGBV particles and for constructing the genomic and/or cPNA library in lambda-gtl 1 or similar systems known in the art is discussed hereinbelow. Lambda-gtl 1 is a vector that has been developed specifically to express inserted cPNAs as fusion polypeptides with beta- galactosidase and to screen large numbers of recombinant phage with specific antisera raised against a defined antigen. The lambda-gtl 1 cPNA library generated from a cPNA pool containing cPNA is screened for encoded epitopes that can bind specifically with sera derived from individuals who previously had experienced non-A, non-B, non-C, non-P and non-E hepatitis. See V. Hunyh et al., in P. Glover, ed, PNA Cloning Techniques: A Practical Approach. IRL Press,Oxford, England, pp. 49-78 (1985). Approximately 10^ - 10^ phage are screened, from which positive phage are identified, purified, and then tested for specificity of binding to sera from different individuals previously infected with the HGBV agent. Phage which selectively bind sera or plasma from patients meeting the criteria described hereinbelow and not in patients who did not meet these described criteria, are preferred for further study. By utilizing the technique of isolating overlapping nucleic acid sequences, clones containing additional upstream and downstream HGBV sequences are obtained. Analysis of the nucleotide sequences of the HGBV nucleic acid sequences encoded within the isolated clones is performed to determine whether the composite sequence contains one long continuous ORF. The sequences (and their complements) retrieved from the HGBV sequence as provided herein, and the sequences or any portion thereof, can be prepared using synthetic methods or by a combination of synthetic methods with retrieval of partial sequences using methods similar to those described herein. This description thus provides one method by which genomic or cPNA sequences corresponding to the entire HGBV genome may be isolated. Other methods for isolating these sequences, however, will be obvious to those skilled in the art and are considered to be within the scope of the present invention. Peposit of Strains. Strains replicated (clones 2, 4, 10, 16, 18, 23 and 50) from the HGBV nucleic acid sequence library have been deposited at the American Type Culture Collection, 12301 Parklawn Prive, Rockville, Maryland 20852, as of February 10, 1994, under the terms of the Budapest Treaty and will be maintained for a period of thirty (30) years from the date of deposit, or for five (5) years after the last request for the deposit, or for the enforceable period of the U.S. patent, whichever is longer. The deposits and any other deposited material described herein are provided for convenience only, and are not required to practice the present invention in view of the teachings provided herein. The HGBV cPNA sequences in all of the deposited materials are incorporated herein by reference. The plasmids were accorded the following A.T.C.C. deposit numbers: Clone 2 was accorded A.T.C.C. Peposit No. 69556; Clone 4 was accorded A.T.C.C. Peposit No. 69557; Clone 10 was accorded A.T.C.C. Peposit No. 69558; Clone 16 was accorded A.T.C.C. Peposit No.69559; Clone 18 was accorded A.T.C.C. Peposit No. 69560; Clone 23 was accorded A.T.C.C. Peposit No. 69561; and Clone 50 was accorded A.T.C.C. Peposit No. 69562. Strains replicated (clones 11, 13, 48 and 119) from the HGBV nucleic acid sequence library have been deposited at the American Type Culture Collection, 12301 Parklawn Prive, Rockville, Maryland 20852, as of April 29, 1994, under the terms of the Budapest Treaty and will be maintained for a period of thirty (30) years from the date of deposit, or for five (5) years after the last request for the deposit, or for the enforceable period of the U.S. patent, whichever isJonger. The deposits and any other deposited material described herein are provided for convenience only, and are not required to practice the present invention in view of the teachings provided herein. The HGBV cPNA sequences in all of the deposited materials are incorporated herein by reference. The plasmids were accorded the following A.T.C.C. deposit numbers: Clone 11 was accorded A.T.C.C. Peposit No. No. 69613; Clone 13 was accorded A.T.C.C. Peposit No. 69611 ; Clone 48 was accorded A.T.C.C. Peposit No. 69610; and Clone 119 was accorded A.T.C.C. Peposit No. 69612. Additional strains (clones 4-B1.1, 66-3A1.49, 70-3A1.37 and 78-1C1.17) from the HGBV nucleic acid sequence library have been deposited at the American Type Culture Collection, 12301 Parklawn Prive, Rockville, Maryland 20852, as of July 28, 1994, under the terms of the Budapest Treaty and will be maintained for a period of thirty (30) years from the date of deposit, or for five (5) years after the last request for the deposit, or for the enforceable period of the U.S. patent, whichever is longer. The deposits and any other deposited material described herein are provided for convenience only, and are not required to practice the present invention in view of the teachings provided herein. The HGBV cPNA sequences in all of the deposited materials are incorporated herein by reference. The plasmids were accorded the following A.T.C.C. deposit numbers: Clone 4- B 1.1 was accorded A.T.C.C. Peposit No. No. 69666; Clone 66-3A1.49 was accorded A.T.C.C. Peposit No. 69665; Clone 70-3A1.37 was accorded A.T.C.C. Peposit No. 69664; and Clone 78-1C1.17 was accorded A.T.C.C. Peposit No. 69663. Clone pHGBV-C clone #1 was deposited at the American Type Culture Collection, 12301 Parklawn Prive, Rockville, Maryland 20852 as of November 8, 1994, under the terms of the Budapest Treaty and will be maintained for a period of thirty (30) years from the date of deposit, or for five (5) years after the last request for the deposit, or for the enforceable period of the U.S. patent, whichever is longer. The deposits and any other deposited material described herein are provided for convenience only, and are not required to practice the present invention in view of the teachings provided herein. pHGBV-C clone #1 was accorded A.T.C.C. Peposit No. 69711. The HGBV cPNA sequences in all of the deposited materials are incorporated herein by reference. Preparation of Viral Polypeptides and Fragments The availability of nucleic acid sequences permits the construction of expression vectors encoding antigenically active regions of the polypeptide encoded in either strand. These antigenically active regions may be derived from structural regions of the virus, including, for example, envelope (coat) or core antigens, in addition to nonstructural regions of the virus, including, for example, polynucleotide binding proteins, polynucleotide polymerase(s), and other viral proteins necessary for replication and/or assembly of the viral particle. Fragments encoding the desired polypeptides are derived from the genomic or cPNA clones using conventional restriction digestion or by synthetic methods, and are ligated into vectors which may, for example, contain portions of fusion sequences such as beta-galactosidase (β-gal) or superoxide dismutase (SOP) or CMP-KOO synthetase (CKS). Methods and vectors which are useful for the production of polypeptides which contain fusion sequences of SOP are described in EPO 0196056, published October 1 , 1986, and those of CKS are described in EPO Publication No. 0331961, published September 13, 1989. Any desired portion of the nucleic acid sequence containing an open reading frame, in either sense strand, can be obtained as a recombinant protein, such as a mature or fusion protein; alternatively, a polypeptide encoded in the HGBV genome or cPNA can be provided by chemical synthesis. The nucleic acid sequence encoding the desired polypeptide, whether in fused or mature form, and whether or not containing a signal sequence to permit secretion, may be ligated into expression vectors suitable for any convenient host. Both eucaryotic and prokaryotic host systems are used in the art to form recombinant proteins, and some of these are listed herein. The polypeptide then is isolated from lysed cells or from the culture medium and purified to the extent needed for its intended use. Purification can be performed by techniques known in the art, and include salt fractionation, chromatography on ion exchange resins, affinity chromatography, centrifugation, among others. Such polypeptides may be used as diagnostic reagents, or for passive immunotherapy. In addition, antibodies to these polypeptides are useful for isolating and identifying HGBV particles. The HGBV antigens also may be isolated from HGBV virions. These virions can be grown in HGBV infected cells in tissue culture, or in an infected individual. Preparation of Antigenic Polypeptides and Conjugation With Solid Phase An antigenic region or fragment of a polypeptide generally is relatively small, usually about 8 to 10 amino acids or less in length. Fragments of as few as 5 amino acids may characterize an antigenic region. These segments may correspond to regions of HGBV antigen. By using the HGBV genomic or cPNA sequences as a basis, nucleic acid sequences encoding short segments of HGBV polypeptides can be expressed recombinantly either as fusion proteins or as isolated polypeptides. These short amino acid sequences also can be obtained by chemical synthesis. The small chemically synthesized polypeptides may be linked to a suitable carrier molecule when the synthesized polypeptide provided is correctly configured to provide the correct epitope but too small to be antigenic. Linking methods are known in the art and include but are not limited to using N- succinimidyl-3-(2-pyrdylthio)propionate (SPPP) and succinimidyl 4-(N- maleimidomethyl)cyclohexane-l-carboxylate (SMCC). Polypeptides lacking sulfhydryl groups can be modified by adding a cysteine residue. These reagents create a disulfide linkage between themselves and peptide cysteine residues on one protein and an amide linkage through the epsilon-amino on a lysine, or other free amino group in the other. A variety of such ώsulfide/amide-forming agents are known. Other bifunctional coupling agents form a thioester rather than a disulfide linkage. Many of these thio-ether-forming agents are commercially available and are known to those of ordinary skill in the art. The carboxyl groups can be activated by combining them with succimmide or l-hydroxyl-2-nitro-4-sulfonic acid, sodium salt. Any carrier which does not itself induce the production of antibodies harmful to the host can be used. Suitable carriers include proteins, polysaccharides such as latex functionalized sepharose, agarose, cellulose, cellulose beads, polymeric amino acids such as polyglutamic acid, polylysine, amino acid copolymers and inactive virus particles, among others. Examples of protein substrates include serum albumins, keyhole limpet hemocyanin, immunoglobulin molecules, thyroglobulin, ovalbumin, tetanus toxoid, and yet other proteins known to those skilled in the art. Preparation of Hybrid Particle Immunogens Containing HGBV Epitopes The immunogenicity of HGBV epitopes also may be enhanced by preparing them in mammalian or yeast systems fused with or assembled with particle-forming proteins such as those associated with HBV surface antigen. Constructs wherein the HGBV epitope is linked directly to the particle-forming protein coding sequences produce hybrids which are immunogenic with respect to the HGBV epitope. In addition, all of the vectors prepared include epitopes specific for HGBV, having varying degrees of immunogenicity. Particles constructed from particle forming protein which include HGBV sequences are immunogenic with respect to HGBV and HBV. Hepatitis B surface antigen has been determined to be formed and assembled into particles in S. cerevisiae and mammalian cells; the formation of these particles has been reported to enhance the immunogenicity of the monomer suhunit. P. Valenzuela et al., Nature 298:334 (1982); P. Valenzuela et al., in I. Millman et al., eds., Hepatitis B. Plenum Press, pp. 225-236 (1984). The constructs may include immunodominant epitopes of HBsAg. Such constructs have been reported expressible in yeast, and hybrids including heterologous viral sequences for yeast expression have been disclosed. See, for example, EPO 174, 444 and EPO 174,261. These constructs also have been reported capable of being expressed in mammalian cells such as Chinese hamster ovary (CHO) cells. Michelle et al., International Symposium on Viral Hepatitis. 1984. In HGBV, portions of the particle-forming protein coding sequence may be replaced with codons encoding an HGBV epitope. In this replacement, regions that are not required to mediate the aggregation of the units to form immunogenic particles in yeast or mammals can be deleted, thus eliminating additional HGBV antigenic sites from competition with the HGBV epitope. Vaccine Preparation Vaccines may be prepared from one or more immunogenic polypeptides or nucleic acids derived from HGBV nucleic acid sequences or from the HGBV genome to which they correspond. Vaccines may comprise recombinant polypeptides containing epitope(s) of HGBV. These polypeptides may be expressed in bacteria, yeast or mammalian cells, or alternatively may be isolated from viral preparations. It also is anticipated that various structural proteins may contain epitopes of HGBV which give rise to protective anti-HGBV antibodies. Synthetic peptides therefore also can be utilized when preparing these vaccines. Thus, polypeptides containing at least one epitope of HGBV may be used, either singly or in combinations, in HGBV vaccines. It also is contemplated that nonstructural proteins as well as structural proteins may provide protection against viral pathogenicity, even if they do not cause the production of neutralizing antibodies. Considering the above, multivalent vaccines against HGBV may comprise one or more structural proteins, and/or one or more nonstructural proteins. These vaccines may be comprised of, for example, recombinant HGBV polypeptides and/or polypeptides isolated from the virions and/or synthetic peptides. These immunogenic epitopes can be used in combinations, i.e., as a mixture of recombinant proteins, synthetic peptides and/or polypeptides isolated from the virion; these may be administered at the same or different time. Additionally, it may be possible to use inactivated HGBV in vaccines. Such inactivation may be be preparation of viral lysates, or by other means known in the art to cause inactivation of hepatitis-like viruses, for example, treatment with organic solvents or detergents, or treatment with formalin. Attenuated HGBV strain preparation also is disclosed in the present invention. It is contemplated that some of the proteins in HGBV may cross-react with other known viruses, and thus that shared epitopes may exist between HGBV and other viruses which would then give rise to protective antibodies against one or more of the disorders caused by these pathogenic agents. It is contemplated that it may be possible to design multiple purpose vaccines based upon this belief. The preparation of vaccines which contain at least one immunogenic peptide as an active ingredient is known to one skilled in the art. Typically, such vaccines are prepared as injectables, either as liquid solutions or suspensions; solid forms suitable for solution in or suspension in liquid prior to injection also may be prepared. The preparation may be emulsified or the protein may be encapsulated in liposomes. The active immunogenic ingredients often are mixed with pharmacologically acceptable excipients which are compatible with the active ingredient. Suitable excipients include but are not limited to water, saline, dextrose, glycerol, ethanol and the like; combinations of these excipients in various amounts also may be used. The vaccine also may contain small amounts of auxiliary substances such as wetting or emulsifying reagents, pH buffering agents, and/or adjuvants which enhance the effectiveness of the vaccine. For example, such adjuvants can include aluminum hydroxide, N-acetyl-muramyl-L-threonyl-P- isoglutamine (thr-PMP), N-acetyl-nomuramyl-L-alanyl-P-isoglutamine (CGP 11687, also referred to as nor-MPP), N-acetylmuramyul-L-alanyl-P- isoglutaminyl-L-alanine-2-(r2'-dipalmitoyl-sn-glycero-3-hydroxphosphoryloxy)- ethylamine (CGP 19835A, also referred to as MTP-PE), and RIBI (MPL + TPM+ CWS) in a 2% squalene/Tween-80® emulsion. The effectiveness of an adjuvant may be determined by measuring the amount of antibodies directed against an immunogenic polypeptide containing an HGBV antigenic sequence resulting from administration of this polypeptide in vaccines which also are comprised of the various adjuvants. The vaccines usually are administered by intraveneous or intramuscular injection. Additional formulations which are suitable for other modes of administration include suppositories and, in some cases, oral formulations. For suppositories, traditional binders and carriers may include but are not limited to polyalkylene glycols or triglycerides. Such suppositories may be formed from mixtures containing the active ingredient in the range of about 0.5% to about 10%, preferably, about 1% to about 2%. Oral formulation include such normally employed excipients as, for example pharmaceutical grades of mannitol, lactose, starch, magnesium stearate, sodium saccharine, cellulose, magnesium carbonate and the like. These compositions may take the form of solutions, suspensions, tablets, pills, capsules, sustained release formulations or powders and contain about 10% to about 95% of active ingredient, preferably about 25% to about 70%. The proteins used in the vaccine may be formulated into the vaccine as neutral or salt forms. Pharmaceutically acceptable salts such as acid addition salts (formed with free amino groups of the peptide) and which are formed with inorganic acids such as hydrochloric or phosphoric acids, or such organic acids such as acetic, oxalic, tartaric, maleic, and others known to those skilled in the art. Salts formed with the free carboxyl groups also may be derived from inorganic bases such as sodium, potassium, ammonium, calcium or ferric hydroxides and the like, and such organic bases such as isopropylamine, trimethylamine, 2- ethylamino ethanol, histidine procaine, and others known to those skilled in the art. Vaccines are administered in a way compatible with the dosage formulation, and in such amounts as will be prophylactically and/or therapeutically effective. The quantity to be administered generally is in the range of about 5 micrograms to about 250 micrograms of antigen per dose, and depends upon the subject to be dosed, the capacity of the subject's immune system to synthesize antibodies, and the degree of protection sought. Precise amounts of active ingredient required to be administered also may depend upon the judgment of the practitioner and may be unique to each subject. The vaccine may be given in a single or multiple dose schedule. A multiple dose is one in which a primary course of vaccination may be with one to ten separate doses, followed by other doses given at subsequent time intervals required to maintain and/or to reinforce the immune response, for example, at one to four months for a second dose, and if required by the individual, a subsequent dose(s) after several months. The dosage regimen also will be determined, at least in part, by the need of the individual, and be dependent upon the practitioner's judgment. It is contemplated that the vaccine containing the immunogenic HGBV antigen(s) may be administered in conjunction with other immunoregulatory agents, for example, with immune globulins. Preparation of Antibodies Against HGBV Epitopes The immunogenic peptides prepared as described herein are used to produce antibodies, either polyclonal or monoclonal. When preparing polyclonal antibodies, a selected mammal (for example, a mouse, rabbit, goat, horse or the like) is immunized with an immunogenic polypeptide bearing at least one HGBV epitope. Serum from the immunized animal is collected after an appropriate incubation period and treated according to known procedures. If serum containing polyclonal antibodies to an HGBV epitope contains antibodies to other antigens, the polyclonal antibodies can be purified by, for example, immunoaffinity chromatography. Techniques for producing and processing polyclonal antibodies are known in the art and are described in, among others, Mayer and Walker, eds., Immunochemical Methods In Cell and Molecular Biology. Academic Press, London (1987). Polyclonal antibodies also may be obtained from a mammal previously infected with HGBV. An example of a method for purifying antibodies to HGBV epitopes from serum of an individual infected with HGBV using affinity chromatography is provided herein. Monoclonal antibodies directed against HGBV epitopes also can be produced by one skilled in the art. The general methodology for producing such antibodies is well-known and has been described in, for example, Kohler and Milstein, Nature 256:494 (1975) and reviewed in J.G.R. Hurrel, ed., Monoclonal Hybridoma Antibodies: Techniques and Applications. CRC Press Inc., Boco Raton, FL (1982), as well as that taught by L. T. Mimms et al., Virology 176:604- 619 (1990). Immortal antibody-producing cell lines can be created by cell fusion, and also by other techniques such as direct transformation of B lymphocytes with oncogenic PNA, or transfection with Epstein-Barr virus. See also, M. Schreier et al., Hybridoma Techniques, Scopes (1980) Protein Purification, Principles and Practice, 2nd Edition, Springer- Verlag, New York (1984); Hammerling et al., Monoclonal Antibodies and T-Cell Hybridomas (1981); Kennet et al., Monoclonal Antibodies (1980). Examples of uses and techniques of monoclonal antibodies are disclosed in U.S. patent applications Serial Nos. 748,292; 748,563;610,175, 648,473; 648,477; and 648,475. Monoclonal and polyclonal antibodies thus developed, directed against HGBV epitopes, are useful in diagnostic and prognostic applications, and also, those which are neutralizing are useful in passive immunotherapy. Monoclonal antibodies especially can be used to produce anti-idiotype antibodies. These anti- idiotype antibodies are immunoglobulins which carry an "internal image" of the antigen of the infectious agent against which protection is desired. See, for example, A. Nisonoff et al., Clin. Immunol. Immunopath. 21:397-406 (1981), and Preesman et al., J. Infect. Pis. 151:761 (1985). Techniques for raising such idiotype antibodies are known in the art and exemplified, for example, in Grych et al., Nature 316:74 (1985); MacNamara et al., Science 226:1325 (1984); and Uytdehaag et al., J. Immunol. 134:1225 (1985). These anti-idiotypic antibodies also may be useful for treatment of HGBV infection, as well as for elucidation of the immunogenic regions of HGBV antigens. Piagnostic Oligonucleotide Probes and Kits Using determined portions of the isolated HGBV nucleic acid sequences as a basis, oligomers of approximately eight nucleotides or more can be prepared, either by excision or synthetically, which hybridize with the HGBV genome and are useful in identification of the viral agent(s), further characterization of the viral genome, as well as in detection of the virus(es) in diseased individuals. The natural or derived probes for HGBV polynucleotides are a length which allows the detection of unique viral sequences by hybridization. While six to eight nucleotides may be a workable length, sequences of ten to twelve nucleotides are preferred, and those of about 20 nucleotides may be most preferred. These sequences preferably will derive from regions which lack heterogeneity. These probes can be prepared using routine, standard methods including automated oligonucleotide synthetic methods. A complement of any unique portion of the HGBV genome will be satisfactory. Complete complementarity is desirable for use as probes, although it may be unnecessary as the length of the fragment is increased. When used as diagnostic reagents, the test sample to be analyzed, such as blood or serum, may be treated such as to extract the nucleic acids contained therein. The resulting nucleic acid from the sample may be subjected to gel electrophoresis or other size separation techniques; or, the nucleic acid sample may be dot-blotted without size separation. The probes then are labelled. Suitable labels and methods for attaching labels to probes are known in the art, and include but are not limited to radioactive labels incorporated by nick translation or kinasing, biotin, fluorescent and chemiluminescent probes. Examples of many of these labels are disclosed herein. The nucleic acids extracted from the sample then are treated with the labelled probe under hybridization conditions of suitable stringencies. The probes can be made completely complementary to the HGBV genome. Therefore, usually high stringency conditions are desirable in order to prevent false positives. However, conditions of high stringency should be used only if the probes are complementary to regions of the HGBV genome which lack heterogeneity. The stringency of hybridization is determined by a number of factors during the washing procedure, including temperature, ionic strength, length of time and concentration of formamide. See, for example, J. Sambrook (supra). Hybridization can be carried out by a number of various techniques. Amplification can be performed, for example, by Ligase Chain Reaction (LCR), Polymerase Chain Reaction (PCR), Q-beta replicase, NASB A, etc. It is contemplated that the HGBV genome sequences may be present in serum of infected individuals at relatively low levels, for example, approximately lO^-lO^ sequences per ml. This level may require that amplification techniques be used in hybridization assays, such as the Ligase Chain Reaction or the Polymerase Chain Reaction. Such techniques are known in the art. For example, the "Bio- Bridge" system uses terminal deoxynucleotide transferase to add unmodified 3'- poly-dT-tails to a nucleic acid probe (Enzo Biochem. Corp.). The poly dt-tailed probe is hybridized to the target nucleotide sequence, and then to a biotin-modifϊed poly-A. Also, in EP 124221 there is described a PNA hybridization assay wherein the analyte is annealed to a single-stranded PNA probe that is complementary to an enzyme-labelled oligonucleotide, and the resulting tailed duplex is hybridized to an enzyme-labelled oligonucleotide. EP 204510 describes a PNA hybridization assay in which analyte PNA is contacted with a probe that has a tail, such as a poly-dT-tail, an amplifier strand that has a sequencethat hybridizes to to the tail of the probe, such as a poly-A sequence, and which is capable of binding a plurality of labelled strands. The technique first may involve amplification of the target HGBV sequences in sera to approximately 10^ sequences/ml. This may be accomplished by following the methods described by Saiki et al., Nature 324: 163 (1986). The amplified sequence(s) then may be detected using a hybridization assay such as those known in the art. The probes can be packaged in diagnostic kits which include the probe nucleic acid sequence which sequence may be labelled; alternatively, the probe may be unlabelled and the ingredients for labelling could be included with the kit. The kit also may contain other suitably packaged reagents and materials needed or desirable for the particular hybridization protocol, for example, standards as well as instructions for performing the assay. Other known amplification methods which can be utilized herein include but are not limited to the so-called "NASBA" or "3SR" technique taught in PNAS USA 87:1874-1878 (1990) and also discussed bin Nature:350 (No. 6313):91-92 ( 1991 ) and Q-beta replicase. Flourescence in situ hybridization ("FISH") also can be performed utilizing the reagents described herein. In situ hybridization involves taking morphologically intact tissues, cells or chromosomes through the nucleic acid hybridization process to demonstrate the presence of a particular piece of genetic information and its specific location within individual cells. Since it does not -require homogenization of cells and extraction of the target sequence, it provides precise localization and distribution of a sequence in cell populations. In situ hybridization can identify the sequence of interest concentrated in the cells containing it. It also can identify the type and fraction of the cells in a heterogeneous cell population containing the sequence of interest. PNA and RNA can be detected with the same assay reagents. PNAs can be utilized in FISH methods to detect targets without the need for amplification. If increased signal is desired, mutiple fluorophores can be used to increase signal and thus, sensitivity of the method. Various methods of FISH are known, including a one-step method using multiple oligonucleotides or the conventional multi-step method. It is within the scope of the present invention that these types of methods can be automated by various means including flow cytometry and image analysis. Immunoassay and Piagnostic Kits Both the polypeptides which react immunologically with serum containing HGBV antibodies and composites thereof, and the antibodies raised against the HGBV specific epitopes in these polypeptides are useful in immunoassays to detect the presence of HGBV antibodies, or the presence of the virus and/or viral antigens in biological test samples. The design of these immunoassays is subject to variation, and a variety of these are known in the art; a variety of these have been described herein. The immunoassay may utilize one viral antigen, such as a polypeptide derived from any clone-containing HGBV nucleic acid sequence, or from the composite nucleic acid sequences derived from the HGBV nucleic acid sequences in these clones, or from the HGBV genome from which the nucleic acid sequences in these clones is derived. Or, the immunoassay may use a combination of viral antigens derived from these sources. It may use, for example, a monoclonal antibody directed against the same viral antigen, or polyclonal antibodies directed against different viral antigens. Assays can include but are not limited to those based on competition, direct reaction or sandwich-type assays. Assays may use solid phases or may be performed by immunoprecipitation or any other methods which do not utilize solid phases. Examples of assays which utilize labels as the signal generating compound and those labels are described herein. Signals also may be amplified by using biotin and avidin, enzyme labels or biotin anti-biotin systems, such as that described in pending U.S. patent application Serial Nos. 608,849; 070,647; 418,981; and 687,785. Recombinant polypeptides which include epitopes from immunodominant regions of HGBV may be useful for the detection of viral antibodies in biological test samples of infected individuals. It also is contemplated that antibodies may be useful in discriminating acute froπuiQn-acute infections. Kits suitable for immunodiagnosis and containing the appropriate reagents are constructed by packaging the appropriate materials, including the polypeptides of the invention containing HGBV epitopes or antibodies directed against HGBV epitopes in suitable containers, along with the remaining reagents and materials required for the conduct of the assay, as well as suitable assay instructions. Assay formats can be designed which utilize the recombinant proteins detailed herein, and although we describe and detail CKS proteins, it also is comtemplated that other expression systems, such as superoxide dismutase (SOP), and others, can be used in the present invention to generate fusion proteins capable of use in a variety of ways, including as antigens in immunoassays, immunogens for antibody production, and the like. In an assay format to detect the presence of antibody against a specific analyte (for example, an infectious agent such as a virus) in a human test sample, the human test sample is contacted and incubated with a solid phase coated with at least one recombinant protein (polypeptide). If antibodies are present in the test sample, they will form a complex with the antigenic polypeptide and become affixed to the solid phase. After the complex has formed, unbound materials and reagents are removed by washing the solid phase. The complex is reacted with an indicator reagent and allowed to incubate for a time and under conditions for second complexes to form. The presence of antibody in the test sample to the CKS recombinant polypeptide(s) is determined by detecting the signal generated. Signal generated above a cut-off value is indicative of antibody to the analyte present in the test sample. With many indicator reagents, such as enzymes, the amount of antibody present is proportional to the signal generated. Pepending upon the type of test sample, it may be diluted with a suitable buffer reagent, concentrated, or contacted with the solid phase without any manipulation ("neat"). For example, it usually is preferred to test serum or plasma samples which previously have been diluted, or concentrate specimens such as urine, in order to determine the presence and/or amount of antibody present. In addition, more than one recombinant protein can be used in the assay format just described to test for the presence of antibody against a specific infectious agent by utilizing CKS fusion proteins against various antigenic epitopes of the viral genome of the infectious agent under study. Thus, it may be preferred to use recombinant polypeptides which contain epitopes within a specific viral antigenic region as well as epitopes from other antigenic regions from the viral genome to provide assays which have increased sensitivity and perhaps greater specificity ti artusmg apo-gfpeptide from one epitope. Such an assay can be utilized as a confirmatory assay. In this particular assay format, a known amount of test sample is contacted with (a) known amount(s) of at least one solid support coated with at least one recombinant protein for a time and under conditions sufficient to form recombinant protein/antibody complexes. The complexes are contacted with known amount(s) of appropriate indicator reagent(s)s for a time and under suitable conditions for a reaction to occur, wherein the resultant signal generated is compared to a negative test sample in order to determine the presence of antibody to the analyte in the test sample. It further is contemplated that, when using certain solid phases such as microparticles, each recombinant protein utilized in the assay can be attached to a separate microparticle, and a mixture of these microparticles made by combining the various coated microparticles, which can be optimized for each assay. Variations to the above-described assay formats include the incorporation of CKS-recombinant proteins of different analytes attached to the same or to different solid phases for the detection of the presence of antibody to either analyte (for example, CKS-recombinant proteins specific for certain antigenic regions of one infective agent coated on the same or different solid phase with CKS- recombinant proteins specific for certain antigenic region(s) of a different infective agent, to detect the presence of either (or both) infective agents. In yet another assay format, CKS recombinant proteins containing antigenic epitopes are useful in competitive assays such as neutralization assays. To perform a neutralization assay, a recombinant polypeptide representing epitopes of an antigenic region of an infectious agent such as a virus, is solubilized and mixed with a sample diluent to a final concentration of between 0.5 to 50.0 μg/ml. A known amount of test sample (preferably 10 μl), either diluted or non-diluted, is added to a reaction well, followed by 400 μl of the sample diluent containing the recombinant polypeptide. If desired, the mixture may be preincubated for approximately 15 minutes to two hours. A solid phase coated with the CKS recombinant protein described herein then is added to the reaction well, and incubated for one hour at approximately 40°C. After Washing, a known amount of an indicator reagent, for example, 200 μl of a peroxidase labelled goat anti-human IgG in a conjugate diluent is added and incubated for one hour at 40°C. After washing and when using an enzyme conjugate such as described, an enzyme substrate, for example, OPO substrate, is added and incubated at room temperature for thirty minutes. The reaction is terminated by adding a stopping reagent such as IN suifuric acid to the reaction well. Absorbance is read at 492 nm. Test samples which contain antibody to the-speeific polypeptide generate a reduced signal caused by the competitive binding of the peptides to these antibodies in solution. The percentage of competitive binding may be calculated by comparing absorbance value of the sample in the presence of recombinant polypeptide to the absorbance value of the sample assayed in the absence of a recombinant polypeptide at the same dilution. Thus, the difference in the signals generated between the sample in the presence of recombinant protein and the sample in the absence of recombinant protein is the measurement used to determine the presence or absence of antibody. In another assay format, the recombinant proteins can be used in immunodot blot assay systems. The immunodot blot assay system uses a panel of purified recombinant polypeptides placed in an array on a nitrocellulose solid support. The prepared solid support is contacted with a sample and captures specific antibodies (specific binding member) to the recombinant protein (other specific binding member) to form specific binding member pairs. The captured antibodies are detected by reaction with an indicator reagent. Preferably, the conjugate specific reaction is quantified using a reflectance optics assembly within an instrument which has been described in U. S. Patent Application Serial No. 07/227,408 filed August 2, 1988. The related U. S. Patent Application Serial No. 07/227,586 and 07/227.590 (both of which were filed on August 2, 1988) further described specific methods and apparatus useful to perform an immunodot assay, as well as U. S. Patent No. 5,075,077 (U.S. Serial No. 07/227,272 filed August 2, 1988), which enjoys common ownership and is incorporated herein by reference. Briefly, a nitrocellulose-base test cartridge is treated with multiple antigenic polypeptides. Each polypeptide is contained within a specific reaction zone on the test cartridge. After all the antigenic polypeptides have been placed on the nitrocellulose, excess binding sites on the nitrocellulose are blocked. The test cartridge then is contacted with a test sample such that each antigenic polypeptide in each reaction zone will react if the test sample contains the appropriate antibody. After reaction, the test cartridge is washed and any antigen-antibody reactions are identified using suitable well-known reagents. As described in the patents and patent applications listed herein, the entire process is amenable to automation. The specifications of these applications related to the method and apparatus for performing an immunodot blot assay are incorporated herein by reference. CKS fusion proteins can be used in assays which employ a first and second solid support, as follow, for detecting antibody to a specific antigen of an analyte in a test sample. In this assay format, a first aliquot of a test sample is contacted with a first solid support coated with CKS recombinant protein specific for an analyte for a time and under conditions sufficient to form recombinant protein/analyte antibody complexes. Then, the complexes are contacted with an indicator reagent specific for the recombinant antigen. The indicator reagent is detected to determine the presence of antibody to the recombinant protein in the test sample. Following this, the presence of a different antigenic determinant of the same analyte is determined by contacting a second aliquot of a test sample with a second solid support coated with CKS recombinant protein specific for the second antibody for a time and under conditions sufficient to form recombinant protein/ second antibody complexes. The complexes are contacted with a second indicator reagent specific for the antibody of the complex. The signal is detected in order to determine the presence of antibody in the test sample, wherein the presence of antibody to either analyte recombinant protein, or both, indicates the presence of anti-analyte in the test sample. It also is contemplated that the solid supports can be tested simultaneously. The use of haptens is known in the art. It is contemplated that haptens also can be used in assays employing CKS fusion proteins in order to enhance performance of the assay. Further Characterization of the HGBV Genome. Virions. and Viral Antigens Using Probes The HGBV nucleic acid sequences may be used to gain further information on the sequence of the HGBV genome, and for identification and isolation of the HGBV agent. Thus, it is contemplated that this knowledge will aid in the characterization of HGBV including the nature of the HGBV genome, the structure of the viral particle, and the nature of the antigens of which it is composed. This information, in turn, can lead to additional polynucleotide probes, polypeptides derived from the HGBV genome, and antibodies directed against HGBV epitopes which would be useful for the diagnosis and/or treatment of HGBV caused non-A, non-B, non-C, non-P and non-E hepatitis. The nucleic acid sequence information is useful for the design of probes or PCR primers for the isolation of additional nucleic acid sequences which are derived from yet undefined regions of the HGBV genome. For example, PCR primers or labelled probes containing a sequence of 8 or more nucleotides, and preferably 20 or more nucleotides, which are derived from regions close to the 5'- termini or 3'-termini of the family of HGBV nucleic acid sequences may be used to isolate overlapping nucleic acid sequences from HGBV genomic or cPNA libraries or directly from viral nucleic acid. These sequences which overlap the HGBV nucleic acid sequences, but which also contain sequences derived from regions of the genome from which the above-mentioned HGBV nucleic acid sequence are not derived, may then be used to synthesize probes for identification of other overlapping fragments which do not necessarily overlap the nucleic acid sequences in the clones. Unless the HGBN genome is segmented and the segments lack common sequences, it is possible to sequence the entire viral genome(s) utilizing the technique of isolation of overlapping nucleic acid sequences derived from the viral genome(s). Characterization of the genomic segments alternatively could be from the viral genome(s) isolated from purified HGBN particles. Methods for purifying HGBN particles and for detecting them during the purification procedure are described herein. Procedures for isolating polynucleotide genomes from viral particles are well-known in the art. The isolated genomic segments then could be cloned and sequenced. Thus, it is possible to clone and sequence the HGBN genome(s) irrespective of their nature. Methods for constructing HGBN genomic or cDΝA libraries are known in the art, and vectors useful for this purpose are known in the art. These vectors include lambda-gtl 1, lambda-gtlO, and others. The HGBN derived nucleic acid sequence detected by the probes derived from the HGBN genomic or cPΝAs, may be isolated from the clone by digestion of the isolated polynucleotide with the appropriate restriction enzyme(s), and sequenced. The sequence information derived from these overlapping HGBN nucleic acid sequences is useful for determining areas of homology and heterogeneity within the viral genome(s), which could indicate the presence of different strains of the genome and or of populations of defective particles. It is also useful for the design of hybridization probes to detect HGBV or HGBV antigens or HGBV nucleic acids in biological samples, and during the isolation of HGBV, utilizing the techniques described herein. The overlapping nucleic acid sequences may be used to create expression vectors for polypeptides derived from the HGBV genome(s). Encoded within the family of nucleic acid sequences are antigen(s) containing epitopes which are contemplated to be unique to HGBV, i.e., antibodies directed against these antigens are absent from individuals infected with HAV, HBV, HCV, and HEV, and with the genomic sequences in GenBank are contemplated to indicate that minimal homology exists between these nucleic acid sequences and the polynucleotide sequences of those sources. Thus, antibodies directed against the antigens encoded with the HGBV nucleic acid sequences may be used to identify the non-A, non-B, non-C, non-P and non-E particle isolated from infected individuals. In addition, they also are useful for the isolation of the HGBV agent(s). HGBV particles may be isolated from the sera of infected individuals-er from cell cultures by any of the methods known in the art, including, for example, techniques based on size discrimination such as sedimentation or exclusion methods, or techniques based on density such as ultracentrifugation in density gradients, or precipitation with agents such as polyethylene glycol (PEG), or chromatography on a variety of materials such as anionic or cationic exchange materials, and materials which bind due to hydrophobic interactions, as well as affinity columns. Puring the isolation procedure the presence of HGBV may be detected by hybridization analysis of the extracted genome, using probes derived from HGBV nucleic acid sequences or by immunoassay which utilize as probes antibodies directed against HGBV antigens encoded within the family of HGBV nucleic acid sequences. The antibodies may be polyclonal or monoclonal, and it may be desirable to purify the antibodies before their use in the immunoassay. Such antibodies directed against HGBV antigens which are affixed to solid phases are useful for the isolation of HGBV by immunoaffinity chromatography. Methods for immunoaffiriity chromatography are known in the art, and include methods for affixing antibodies to solid phases so that they retain their immunoselective activity. These methods include adsorption, and covalent binding. Spacer groups may be included in the bifunctional coupling agents such that the antigen binding site of the antibody remains accessible. Puring the purification procedure the presence of HGBV may be detected and/or verified by nucleic acid hybridization or PCR, utilizing as probes or primers polynucleotides derived from a family of HGBV genomic or cPNA sequences, as well as from overlapping HGBV nucleic acid sequences. Fractions are treated under conditions which would cause the disruption of viral particles, such as by use of detergents in the presence of chelating agents, and the presence of viral nucleic acid determined by hybridization techniques or PCR. Further confirmation that the isolated particles are the agents which induce HGBV infection may be obtained by infecting an individual which is preferably a tamarin with the isolated virus particles, followed by a determination of whether the symptoms of non-A, non-B, non-C, non-P and non-E hepatitis, as described herein, result from the infection. Such viral particles obtained from the purified preparations then may be further characterized. The genomic nucleic acid, once purified, can be tested to determine its sensitivity to RNAse or PNAse I; based on these tests, the determination of HGBV as a RNA genome or PNA genome may be made. The strandedness and circularity or non-circularity can be determined by methods known in*he-*rt including its visualization by electron microscopy, its migration in density gradients and its sedimentation characteristics. From hybridization of the HGBV genome, the negative or positive strandedness of the purified nucleic acid can be determined. In addition, the purified nucleic acid can be cloned and sequenced by known techniques, including reverse transcriptase, if the genomic material is RNA. Utilizing the nucleic acid derived from the viral particles, it then is possible to sequence the entire genome, whether or not it is segmented. Petermination of polypeptides containing conserved sequences may be useful for selecting probes which bind the HGBV genome, thus allowing its isolation. In addition, conserved sequences in conjunction with those derived from the HGBV nucleic acid sequences, may be used to design primers for use in systems which amplify genomic sequences. Further, the structure of HGBV also may be determined and its components isolated. The morphology and size may be determined by electron microscopy, for example. The identification and localization of specific viral polypeptide antigens such as envelope (coat) antigens, or internal antigens such as nucleic acid binding proteins or core antigens, and polynucleotide polymerase(s) also may be determined by ascertaining whether the antigens are present in major or minor viral components, as well as by utilizing antibodies directed against the specific antigens encoded within isolated nucleic acid sequences as probes. This information may be useful for diagnostic and therapeutic applications. For example, it may be preferable to include an exterior antigen in a vaccine preparation, or perhaps multivalent vaccines may be comprised of a polypeptide derived from the genome encoding a structural protein as well as a polypeptide from another portion of the genome, such as a nonstructural polypeptide. Cell Culture Systems and Animal Model Systems for HGBV Replication Generally, suitable cells or cell lines for culturing HGBV may include the following: monkey kidney cells such as MK2 and VERO, porcine kidney cell lines such as PS, baby hamster kidney cell lines such as BHK, murine macrophage cell lines such as P388O1, MK1 and Mml, human macrophage cell lines such as U- 937, human peripheral blood leukocytes, human adherent monocytes, hepatocytes or hepatocytic cell lines such as HUH7 and HepG2, embryos or embryonic cell such as chick embryo fibroblasts or cell lines derived from invertebrates, preferably from insects such as Drosophia cell lines or more preferably from arthropods such as mosquito cell lines or tick cell lines It also is possible that primary hepatocytes can be cultured and then infected with HGBV. Alternatively, the hepatocyte cultures could be derived from the livers of infected individuals (human or t-Miιarιns).- ThaMatter case is an example of a cell line which is infected in vivo being passaged in vitro. In addition, various immortalization methods can be used to obtain cell lines derived from hepatocyte cultures. For example, primary liver cultures (before and after enrichment of the hepatocyte population) may be fused to a variety of cells to maintain stability. Also, cultures may be infected with transforming viruses, or transfected with transforming genes in order to create permanent or semipermanent cell lines. In addition, cells in liver cultures may be fused to established cell lines such as PehG2. Methods for cell fusion are well-known to the routineer, and include the use of fusion agents such as PEG and Sendai Virus, among others. It is contemplated that HGBV infection of cell lines may be accomplished by techniques such as incubating the cells with viral preparations under conditions which allow viral entry into the cell. It also may be possible to obtain viral production by transfecting the cells with isolated viral polynucleotides. Methods for transfecting tissue culture cells are known in the art and include but are not limited to techniques which use electroporation and precipitation with PEAE- Pextran or calcium phosphate. Transfection with cloned HGBV genomic or cPNA should result in viral replication and the in vitro propagation of the virus. In addition to cultured cells, animal model systems may be used for viral replication. HGBV replication thus may occur in chimpanzees and also in, for example, marmosets and suckling mice. Screening for Anti-Viral Agents For HGBV The availability of cell culture and animal model systems for HGBV also renders screening for anti-viral agents which inhibit HGBV replication possible, and particularly for those agents which preferentially allow cell growth and multiplication while inhibiting viral replication. These screening methods are known in the art. Generally, the anti-viral agents are tested at a variety of concentrations, for their effect on preventing viral replication in cell culture systems which support viral replication, and then for an inhibition of infectivity or of viral pathogenicity, and a low level of toxicity, in an animal model system. The methods and composition provided herein for detecting HGBV antigens and HGBV polynucleotides are useful for screening of anti-viral agents because they provide an alternative, and perhaps a more sensitive means, for detecting the agent's effect on viral replication than the cell plaque assay or IP50 assay. For example, the HGBV polynucleotide probes described herein may be used to quantitate the amount of viral nucleic acid produced in a cell culture. This could be performed by hybridization or competition hybridization of the infected cell nucleic acids with a labelled HGB polynucteotide probe. Also, anti-HGBV antibodies may be used to identify and quantitate HGBV antigen(s) in the cell culture utilizing the immunoassays described herein. Also, since it may be desirable to quantitate HGBV antigens in the infected cell culture by a competition assay, the polypeptides encoded within the HGBV nucleic acid sequences described herein are useful for these assays. Generally, a recombinant HGBV polypeptide derived from the HGBV genomic or cPNA would be labelled, and the inhibition of binding of this labelled polypeptide to an HGBV polypeptide due to the antigen produced in the cell culture system would be monitored. These methods are especially useful in cases where the HGBV may be able to replicate in a cell lines without causing cell death. Preparation of Attenuated Strains of HGBV It may be possible to isolate attenuated strains of HGBV by utilizing the tissue culture systems and/or animal models systems provided herein. These attenuated strains would be useful for vaccines, or for the isolation of viral antigens. Attenuated strains are isolatable after multiple passages in cell culture and or an animal model. Petection of an attenuated strain in an infected cell or individual is achievable by following methods known in the art and could include the use of antibodies to one or more epitopes encoded in HGBV as a probe or the use of a polynucleotide containing an HGBV sequence of at least about 8 nucleotides in length as a probe. Also or alternatively, an attenuated strain may be constructed utilizing the genomic information of HGBV provided herein, and utilizing recombinant techniques. Usually an attempt is made to delete a region of the genome encoding a polypeptide related to pathogenicity but not to viral replication. The genomic construction would allow the expression of an epitope which gives rise to neutralizing antibodies for HGBV. The altered genome then could be used to transform cells which allow HGBV replication, and the cells grown under conditions to allow viral replication. Attenuated HGBV strains are useful not only for vaccine purposes, but also as sources for the commercial production of viral antigens, since the processing of these viruses would require less stringent protection measures for the employees involved in viral production and/or the production of viral products. Hosts and Expression Control Sequences Although the following are known in the art, included herein are general techniques used in extracting the genome from a virus, preparing and probing a genomic library, sequencing clones, constructing expression vectors, transforming cells, performing immunological assays, and for growing cell in culture. Both prokaryotic and eukaryotic host cells may be used for expression of desired coding sequences when appropriate control sequences which are compatible with the designated host are used. Among prokaryotic hosts, E. coli is most frequently used. Expression control sequences for prokaryotics include promoters, optionally containing operator portions, and ribosome binding sites. Transfer vectors compatible with prokaryotic hosts are commonly derived from the plasmid pBR322 which contains operons conferring ampicillin and tetracycline resistance, and the various pUC vectors, which also contain sequences conferring antibiotic resistance markers. These markers may be used to obtain successful transformants by selection. Commonly used prokaryotic control sequences include the beta-lactamase (penicillinase), lactose promoter system (Chang et al., Nature 198: 1056 [1977]) the tryptophan promoter system (reported by Goeddel et al., Nucleic Acid Res 8:4057 [1980]) and the lambda-derived PI promoter and N gene ribosome binding site (Shimatake et al., Nature 292: 128 [1981]) and the hybrid Tac promoter (Pe Boer et al., Proc. Natl. Acad. Sci. USA 292: 128 [1983]) derived from sequences of the tip. and iac UV5 promoters. The foregoing systems are particularly compatible with E. coli: however, other prokaryotic hosts such as strains of Bacillus or Pseudomonas may be used if desired, with corresponding control sequences. Eukaryotic hosts include yeast and mammalian cells in culture systems. Saccharomyces cerevisiae and Saccharomyces carlsbergensis are the most commonly used yeast hosts, and are convenient fungal hosts. Yeast compatible vectors carry markers which permit selection of successful transformants by conferring protrophy to auxotrophic mutants or resistance to heavy metals on wild- type strains. Yeast compatible vectors may employ the 2 micron origin of replication (as described by Broach et al., Meth. Enz. 101:307 [1983]), the combination of CEN3 and ARS 1 or other means for assuring replication, such as sequences which will result in incorporation of an appropriate fragment into the host cell genome. Control sequences for yeast vectors are known in the art and include promoters for the synthesis of glycolytic enzymes, including the promoter for 3 phosphophycerate kinase. See, for example, Hess et al., J. Adv. Enzyme Reg. 7: 149 (1968), Holland et al., Biochemistrv 17:4900 (1978) and Hitzeman I Biol. Chem. 255:2073 (1980). Terminators also may be included, such as those derived from the enolase gene as reported by Holland, J. Biol. Chem. 256:1385 (1981). It is contemplated that particularly useful control systems are those which comprise the glyceraldehyde-3 phosphate dehydrogenase (GAPPH) promoter or alcohol dehydrogenase (APH) regulatable promoter, terminators also derived from GAPPH, and if secretion is desired, leader sequences from yeast alpha factor. In addition, the transcriptional regulatory region and the transcriptional initiation region which are operably linked may be such that they are not naturally associated in the wild-type organism. Mammalian cell lines available as hosts for expression are known in the art and include many immortalized cell lines which are available from the American Type Culture Collection. These include HeLa cells, Chinese hamster ovary (CHO) cells, baby hamster kidney (BHK) cells, and others. Suitable promoters for mammalian cells also are known in the art and include viral promoters such as that from Simian Virus 40 (SV40), Rous sarcoma virus (RSV), adenovirus (APV), bovine papilloma virus (BPV), cytomegalovirus (CMV). Mammalian cells also may require terminator sequences and poly A addition sequences; enhancer sequences which increase expression also may be included, and sequences which cause amplification of the gene also may be desirable. These sequences are known in the art. Vectors suitable for replication in mammalian cells may include viral replicons, or sequences which insure integration of the appropriate sequences encoding non-A, non-B, non-C, non-P, non-E epitopes into the host genome. An example of a mammalian expression system for HCV is described in U.S. Patent Application Serial No. 07/830,024, filed January 31, 1992. Transformations Transformation may be by any known method for introducing polynucleotides into a host cell, including packaging the polynucleotide in a virus and transducing a host cell with the viras, and by direct uptake of the polynucleotide. The transformation procedures selected depends upon the host to be transformed. Bacterial transformation by direct uptake generally employs treatment with calcium or rubidium chloride. Cohen, Proc. Natl. Acad. Sci. USA 69:2110 (1972). Yeast transformation by direct uptake may be conducted using the calcium phosphate precipitation method of Graham et al., Virology 52:526 (1978), or modification thereof. Vector Construction Vector construction employs methods known in the art. Generally, site- specific PNA cleavage is performed by treating with suitable restriction enzymes under conditions which generally are specified by the manufacturer of these commercially available enzymes. Usually, about 1 microgram (μg) of plasmid or PNA sequence is cleaved by 1-10 units of enzyme in about 20 μl of buffer solution by incubation at 37°C for 1 to 2 hours. After incubation with the restriction enzyme, protein is removed by phenol chloroform extraction and the PNA recovered by precipitation with ethanol. The cleaved fragments may be separated using polyacrylamide or agarose gel electrophoresis methods, according to methods known by the routineer. Sticky end cleavage fragments may be blunt ended using E. coli PNA polymerase 1 (Klenow) in the presence of the appropriate deoxynucleotide triphosphates (dNTPs) present in the mixture. Treatment with S 1 nuclease also may be used, resulting in the hydrolysis of any single stranded PNA portions. Ligations are performed using standard buffer and temperature conditions using T4 PNA ligase and ATP. Sticky end ligations require less ATP and less ligase than blunt end ligations. When vector fragments are used as part of a ligation mixture, the vector fragment often is treated with bacterial alkaline phosphatase (BAP) or calf intestinal alkaline phosphatase to remove the 5'- phosphate and thus prevent religation of the vector. Or, restriction enzyme digestion of unwanted fragments can be used to prevent ligation. Ligation mixtures are transformed into suitable cloning hosts such as E. coli and successful transformants selected by methods including antibiotic resistance, and then screened for the correct construction. Construction of Pesired PNA Sequences Synthetic oligonucleotides may be prepared using an automated oligonucleotide synthesizer such as that described by Warner, PNA 3:401 (1984). If desired, the synthetic strands may be labelled with P by treatment with polynucleotide kinase in the presence of 32 P-ATP, using standard conditions for the reaction. PNA sequences including those isolated from genomic or cPNA libraries, may be modified by known methods which include site directed mutagenesis as described by Zoller, Nucleic Acids Res. 10:6487 (1982). Briefly, the PNA to be modified is packaged into phage as a single stranded sequence, and converted to a double stranded PNA with PNA polymerase using, as a primer, a synthetic oligonucleotide complementary to the portion of the PNA to be modified, and having the desired modification included in its own sequence. Culture of the transformed bacteria, which contain replications of each strand of the phage, are plated in agar to obtain plaques. Theoretically, 50% of the new plaques contain phage having the mutated sequence, and the remaining 50% have the original sequence. Replicates of the plaques are hybridized to labelled synthetic probe at temperatures and conditions suitable for hybridization with the correct strand, but not with the unmodified sequence. The sequences which have been identified by hybridization are recovered and cloned. -Hybridization With Probe HGBV genomic or PNA libraries may be probed using the procedure described by Granstein and Hogness, Proc. Natl. Acad. Sci. USA 73:3961 (1975). Briefly, the PNA to be probed is immobilized on nitrocellulose filters, denatured and prehybridized with a buffer which contains 0-50% formamide, 0.75 M NaCl, 75 mM Na citrate, 0.02% (w/v) each of bovine serum albumin (BS A), poly vinyl pyrollidone and Ficoll, 50 mM Na Phosphate (pH 6.5), 0.1% SPS and 100 μg/ml carrier denatured PNA. The percentage of formamide in the buffer, as well as the time and temperature conditions of the prehybridization and subsequent hybridization steps depends on the stringency required. Oligomeric probes which require lower stringency conditions are generally used with low percentages of formamide, lower temperatures, and longer hybridization times. Probes containing more than 30 or 40 nucleotides such as those derived from cPNA or genomic sequences generally employ higher temperatures, for example, about 40 to 42°C, and a high percentage, for example, 50% formamide. Following prehybridization, a 32 P-labelled oligonucleotide probe is added to the buffer, and the filters are incubated in this mixture under hybridization conditions. After washing, the treated filters are subjected to autoradiography to show the location of the hybridized probe. PNA in corresponding locations on the original agar plates is used as the source of the desired PNA. Verification of Construction and Sequencing For standard vector constructions, ligation mixtures are transformed into R coli strain XL-1 Blue or other suitable host, and successful transformants selected by antibiotic resistance or other markers. Plasmids from the transformants then are prepared according to the method of Clewell et al., Proc. Natl. Acad. Sci. USA 62: 1159 (1969) usually following chloramphenicol amplification as reported by Clewell et al., J. Bacteriol. 110:667 (1972). The PNA is isolated and analyzed usually by restriction enzyme analysis and/or sequencing. Sequencing may be by the well-known dideoxy method of S anger et al., Proc. Natl. Acad. Sci. USA 74:5463 (1977) as further described by Messing et al., Nucleic Acid Res. 9:309 (1981), or by the method reported by Maxam et al., Methods in Enzymology 65:499 (1980). Problems with band compression, which are sometimes observed in GC rich regions, are overcome by use of T-deazoguanosine according to the method reported by Barr et al., Biotechniques 4:428 (1986). Enzyme-Linked Immunosorbent Assay Enzyme-linked immunosorbent assay (ELISA) can be used to measure either antigen or antibody concentrations. This method depends upon conjugation of an enzyme label to either an antigen or antibody, and uses the bound enzyme activity (signal generated) as a quantitative label (measurable generated signal). Methods which utilize enzymes as labels are described herein, as are examples of such enzyme labels. Preparation of HGBV Nucleic Acid Sequences The source of the non-A, non-B,non-C, non-P, non-E agent is an individual or pooled plasma, serum or liver homogenate from a human or tamarin infected with the HGBV viras meeting the clinical and laboratory criteria described herein. A tamarin alternatively can be experimentally infected with blood from another individual with non-A, non-B, non-C, non-E hepatitis meeting the criteria described hereinbelow. A pool can be made by combining many individual plasma, serum or liver homogenate samples containing high levels of alanine transferase activity; this activity results from hepatic injury due to HGBV infection. The TIP (tamarin infective dose) of the viras has been calculated from one of our experiments to be > 4 x 10^/ml (see Example 2, below). For example, a nucleic acid library from plasma, serum or liver homogenate, preferably but not necessarily high titer, is generated as follows. First, viral particles are isolated from the plasma, serum or liver homogenate; then an aliquot is diluted in a buffered solution, such as one containing 50 mM Tris- HC1, pH 8.0, 1 mM EPTA, 100 mM NaCl. Pebris is removed by centrifugation, for example, for 20 minutes at 15,000 x g at 20°C. Viral particles in the resulting supernatant then are pelleted by centrifugation under appropriate conditions which can be determined routinely by one skilled in the art. To release the viral genome, the particles are disrupted by suspending the pellets in an aliquot of an SPS suspension, for example, one containing 1% SPS, 120 mM EPTA, 10 mM Tris- HCI, pH 7.5, which also contains 2 mg/ml proteinase K, which is followed by incubation at appropriate conditions, for example, 45°C for 90 minutes. Nucleic acids are isolated by adding, for example, 0.8 μg MS2 bacteriophage RNA as carrier, and extracting the mixture four times with a 1 : 1 mixture of phenokchloroform (phenol saturated with 0.5M Tris-HCl, pH 7.5, 0.1% (v/v) beta-mercaptoethanol, 0.1 % (w/v) hydroxy quinolone, followed by extraction two times with chloroform. The aqueous phase is concentrated with, for example, 1- butanol prior to precipitation with 2.5 volumes of absolute ethanol overnight at -20°C. Nucleic acids are recovered by centrifugation in, for example, a Beckman SW41 rotor at 40,000 rpm for 90 min at 4°C, and dissolved in water that is treated with 0.05% (v/v) diethylpyrocarbonate and autoclaved. Nucleie-acidobtained by-thr-above procedure is denatured with, for example, 17.5 mM CH3HgOH; cPNA then is synthesized using this denatured nucleic acid as template, and is cloned into the EcoRI site of phage lambda-gtl 1, for example, by using methods described by Huynh (1985) supra, except that random primers replace oligo(dT) 12-18 during the synthesis of the first nucleic acid strand by reverse transcriptase (see Taylor et al., [1976]). The resulting double stranded nucleic acid sequences are fractionated according to size on a Sepharose CL-4B column, for example. Eluted material of approximate mean size 400, 300, 200 and 100 base-pairs are pooled into genomic pools. The lambda- gtl 1 cPNA library is generated from the cPNA in at least one of the pools. Alternatively, if the etiological agent is a PNA virus, methods for cloning genomic PNA may be useful and are known to those skilled in the art. The so-generated lambda-gtl 1 genomic library is screened for epitopes that can bind specifically with serum, plasma or a liver homogenate from an individual who had previously experienced non-A, non-B, non-C, non-E hepatitis (one which meets the criteria as set forth hereinbelow). About lθ θ 7 phage are screened with sera, plasma, or liver homogenates using the methods of Huyng et al. (supra). Bound human antibody can be detected with sheep anti-human Ig antisera that is radio-labelled with 125 I or other suitable reporter molecules including HRPO, alkaline phosphatase and others. Positive phage are identified and purified. These phage then are tested for specificity of binding to sera from a pre-determined number of different humans previously infected with the HGBV agent , using the same method. Ideally, the phage will encode a polypeptide that reacts with all or a majority of the sera, plasma or liver homogenates that are tested, and will not react with sera, plasma or liver homogenates from individuals who are determined to be "negative" according to the criteria set forth herein for the HGBV agent as well as hepatitis A, B, C, P and E. By following these procedures, a clone that encodes a polypeptide which is specifically recognized immunologically by sera, plasma or liver homogenates from non-A, non-B, non- C, non-P and non-E-identified patients can be isolated. The present invention will now be described by way of examples, which are meant to illustrate, but not to limit, the spirit and scope of the invention. EXAMPLES The examples provided herein describe in detail methods which led to the discovery of the HGBV group of viruses. The examples are provided in chronological order so that the discovery of the HGBV-A, HGBV-B and HGB V- C viruses of the HGBV group an be followed. Generally, transmissibility and infectivity studies were initially performed; these studies and subsequent ones described herein led to evidence for the existence of two HCV-like virases in HGBN: GB-A and GB-B. Subsequent experiments also detailed herein utilizing degenerative primers led to the discovery of HGBN-C. The prevalence of this group of virases in humans as evidenced by serological studies, the viral characterization of this group of virases, the relatedness of HGBN to other viruses in its proposed genus and the interrelatedness of HGBN- A, HGBN-B and HGBN- C also is taught. Example 1. Transmissibility of HGBN A. Experimental Protocol. Sixteen tamarins (Saguinus labiatus) were secured through LEMSIP (Laboratory for Experimental Medicine and Surgery in Primates, Tuxedo, New York) for the transmissibility and infectivity studies. All animals were maintained and monitored at LEMSIP according to protocols approved by LEMSIP. (Note: one animal died of natural causes and one ailing animal was euthanized prior to the initiation of infectivity studies). Baseline serum liver enzyme values were established for serum liver enzymes alanine transaminase (ALT), gamma-glutamyltransferase (GGT) and isocitric dehydrogenase (ICO) for two to three months on serum specimens obtained weekly or bi-weekly. A minimum of eight serum liver enzyme values were obtained for each animal prior to inoculation. Cutoff values (CO) were determined for each animal, based on the mean liver enzyme value plus 3.75 times the standard deviation. Liver enzyme values above the cutoff value were interpreted as abnormal and suggestive of liver damage. Several tamarins were inoculated as described hereinbelow and monitored for changes in ALT, GGT and ICO serum levels. At specified times thereafter during the monitoring process, certain animals were sacrified in order to obtain serum and tissues for further studies. B. Inoculation of Animals (Initial Study). A pool of known infectious tamarin GB serum (passage 11, designated as H205 GB pass 11) was prepared from serum collected during the early acute phase (19-24 days post inoculation) of hepatitis from nine tamarins inoculated with the HGBV. This pool had been previously described and studied in an effort to determine the etiological agent involved. J. L. Dienstag et al., Nature 264 supra: E. Tabor et al., J. Med. Virol. 5, supra. Aliquots of this pool were maintained at Abbott Laboratories (North Chicago, J_L 60064) under liquid nitrogen storage conditions until utilized in this study. Other aliqouts of HGBV are available from he American Type Culture Collection (A.T.C.C), 12301 Parklawn Drive, Rockville, MD 20852, under A.T.C.C. Deposit.No. VR-806. On day one, four tamarins of the initial group of remaining 14 tamarins, identified as T-1053, T-1048, T-1057 and T-1061, were inoculated intravenously with 0.25 ml of pool H205, passage 11, previously diluted 1 :50. These animals were monitored weekly for changes in the liver enzymes ALT, GGT and ICD. TABLE 2 presents the pre- and post- inoculation liver enzyme data on these four tamarins (T-1053, T-1048, T-1057 and T-1061); FIGURES 1-4 present the pre- and post- inoculation ALT and ICD levels of these four tamarins. As the data demonstrate, significant rises in ALT, GGT and ICD above the CO were obtained in the four tamarins inoculated with the 1:50 dilution of pool H205. On the same day (day one), one tamarin (T-1047) was inoculated intravenously with 0.25 ml of pooled normal tamarin serum and used as a negative control, and another tamarin (T-1042) was inoculated intraveneously with 0.25 ml of pooled normal human serum and served as an additional negative control. FIGURES 5-6 and TABLE 3 present the pre- and post- inoculation ALT and ICD levels of the two control tamarins (T-1047 and T-1042). As the data demonstrate, no rise in ALT or ICD was documented post-inoculation for the two control tamarins for a period of eight weeks. On the same day (day one), one tamarin (T-1044) was inoculated intravenously with 0.2 ml of convalescent sera obtained from the surgeon (original GB source) approximately three weeks following the onset of acute hepatitis. This specimen had been stored at -20°C. F. Deinhardt et al., J. Exper. Med. 125:673-688 (1967). Another tamarin (T-1034) was inoculated with 0.1 ml of this convalescent sera. As FIGURES 7-8 and TABLE 4 demonstrate, no rise in serum liver enzymes was observed in these tamarins for a period of eleven weeks post inoculation. Thus, these data demonstrate that infective HGBV was not detectable in the convalescent sera obtained from the original patient and stored at -20°C, which could indicate that the individual had recovered from infection and that the viras had been cleared from the patient's serum or that the viral titer had been reduced to non-detectable levels upon storage at -20°C. C. Further Studies. Tamarin T-1053 showed a significant rise in serum liver enzymes one week post-inoculation, and was retested for liver enzymes on day 11 post-inoculation. At day 12 it was determined that significant elevations in serum liver enzymes were present, and the animal was sacrificed on that day. Plasma, liver and spleen tissue samples were obtained for further studies. The plasma from T-1053 served as the source for the RDA procedure discussed in Example 3 below; the liver tissue was utilized in Example 8 below. Tamarins T-1048, T-1057 and T-1061 were monitored for seram liver enzyme values; all were observed to exhibit elevated seram liver enzyme levels within two weeks following inoculation; these elevated values were noted for six or more weeks post inoculation. All three tamarins were observed to have decreasing seram liver enzyme levels below the CO by 84 days post inoculation. On day 97 post inoculation, these three tamarins (T-1048, T-1057 and T-1061) were re-challenged with 0.10 ml of neat plasma obtained from tamarin T-1053 (shown to be infectious, see Example 2) to determine whether hepatitis as documented by elevations in seram liver enzymes could be re-induced. The data are presented in TABLE 2 and FIGURES 1, 3 and 4. As the data indicates, seram liver enzyme levels of two tamarins (T-1057 and T-1061) remained below the CO for three weeks post reinoculation. One tamarin (T-1048) exhibited mild elevations in seram liver enzyme levels two weeks immediately post-reinoculation. It was hypothesized that the mild elevations in T-1048 were attributable to either reinfection of liver tissue by HGBV or incomplete recovery from the initial inoculation with H205. Example 2. Infectivity Studies A. Experimental Protocol. Baseline readings on four tamarins were obtained as described in Example 1(A). Briefly, baseline seram liver enzymes (ALT, GGT and ICD) were established for each animal prior to inoculation. Cutoff values (CO) were determined for each animal, based on the mean liver enzyme value plus 3.75 times the standard deviation. Liver enzyme values above the cutoff were interpreted as abnormal and suggestive of liver damage. B. Inoculation of Tamarins. The plasma from Tamarin T-1053, sacrificed at day 12 post inoculation (see Example 1 [C]), was used as the inoculum for further studies. On day one, one tamarin (T-1055) was inoculated intravenously with 0.25 ml of neat T-1053 plasma. On the same day, two tamarins (T-1038 and T- 1051) were inoculated intravenously with 0.25 ml of T-1053 plasma which had been serially diluted to either 10" 4 (T-1038) or 10" 5 (T-1051) in pooled normal tamarin plasma. On the same day, tamarin T-1049 was inoculated intravenously with 0.25 ml of plasma T-1053 which had been filtered through a series of filters of decreasing pore size (0.8 μm, 0.45 μm, 0.22 μm and 0.10 μm) and diluted at 10 ~ in pooled normal tamarin plasma. All tamarins (T-1055, T-1038, T-1051 and T-1049) were monitored weekly as described in Example 1 for changes in seram liver enzymes ALT, GGT and ICD. TABLE 5 presents the pre- and post- inoculation liver enzyme data on these four tamarins. FIGURE 9 presents the pre- and post- inoculation ALT and ICD values T-1055. Referring to FIGURE 9, it can be seen that elevations above the CO in seram liver enzymes ALT and ICD occurred. This tamarin was sacrified on day 12 post-inoculation. FIGURES 10 and 11 present the pre- and post- inoculation seram levels of ALT and ICD for tamarins T-1051 and T-1038, respectively. Referring to FIGURES 10 and 11, it can be seen that elevations in seram liver enzymes ALT and ICD occured in both animals by 11 days post- inoculation. T-1038 was sacrified on day 14 post inoculation. TABLE 5 and FIGURE 12 present the data obtained on T-1049. As can be seen from TABLE 5 and FIGURE 12, elevations in seram liver enzymes above the CO were observed in T-1049 within 11 days post-inoculation. The filtration study conducted on T-1049 indicates that HGBV can pass through a 0.1 Oμm filter, thereby suggesting that HGBV is likely to be viral in nature, and less than 0.1 μm in diameter. In addition, the infectivity titration experiment conducted on T-1038 demonstrates that the T 1053 seram contains at least 4 x 10^ tamarin infectious doses per ml. In order to show the transmissibility of a single HGBV agent, tamarin T- 1044 was inoculated with 0.25 ml of an inoculum consisting of T-1057 seram that had been obtained 7 days after the H205 inoculation and diluted 1:500 in normal tamarin seram. Mild elevations in ALT levels above the cutoff were observed from days 14-63 PI (that it, elevations in the range of 82 to 106). Tamarins T-1047 and T-1056 were subsequently inoculated with 0.25ml of T-1044 seram obtained 14 days PI and diluted 1:2 in normal tamarin seram. Elevations in ALT levels above the cutoff were first observed in T-1047 and T- 1056 at 42 days PI and returned to normal levels at days 64 and 91 PI, respectively. Tamarin T-1058 was inoculated with 0.25ml of neat T-1057 seram obtained 22 days after the challenge with T-1053 seram. Elevations in ALT levels have not been observed for 112 days PI. Example 3. Representational Difference Analysis (Subtractive Hybridization) A. Generation of double-stranded DNA for Amplicons Using the procedure described herein in Materials and Methods above and referring β-SIGURE 13, tester amplicon was prepared from total nucleic acid obtained from tamarin T-1053 infectious plasma on day 12 post inoculation with H205 seram (see Examples 1C and 2B). Driver amplicon was prepared from Tamarin T-1053 pre-inoculation plasma pooled from days -17 to -30 (see Example 1A). Briefly, both plasmas were filtered through a 0.1 μm filter as described in Example 2B. Next, 50 μl of each filtered plasma was extracted using a commercially available kit [United States Biochemical (USB), Cleveland, OH, cat. #73750] and 10 μg yeast tRNA as a carrier. This nucleic acid was subjected to random primed reverse transcription followed by random primed DNA synthesis using commercially available kits. Briefly, an 80 μl reverse transcription reaction was performed using Perkin Elmer's (Norwalk, CT) RNA PCR kit (cat. # N808-0017) as directed by the manufacturer using random hexamers and incubating for 10 minutes at 20°C followed by 2 hours incubation at 42°C. The reactions then were terminated and cDNA/RNA duplexes denatured by incubation at 99°C for 2 minutes. The reactions were supplemented with 10 μl lOx RP buffer [100 mM NaCl, 420 mM Tris (pH 8.0), 50 mM DTT, 100 μg/ml BSA], 250 pmoles random hexamers and 13 units Sequenase® version 2.0 polymerase (USB, cat. #70775) in a total volume of 20 μl. The reactions were incubated at 20°C for 10 minutes followed by 37°C for 2 hours. After phenohchloroform extraction and ethanol precipitation, the double stranded DNA products of these reactions were digested with 4 units of restriction endonuclease Sau3A I (New England Biolabs [NEB], cat. #169L) in 30 μl reaction volumes for 30 minutes, as directed by the supplier. B. Generation of amplicons. Sau3 AJ-digested DNA was extracted and precipitated as described above. The entire Sau3AI-digested product was annealed to 465 pmoles R Bgl 24 (SEQUENCE ID. NO. 1) and 465 pmoles R Bgl 12 (SEQUENCE I.D. NO. 2) in a 30 μl reaction volume buffered with lx T4 DNA ligase buffer (NEB) by placing the reaction in a 50-55°C dry heat block which was then incubated at 4°C for 1 hour. The annealed product was ligated by adding 400 units T4 DNA ligase (NEB, cat. # 202S). After incubation for 14 hours at 16°C, a small scale PCR was performed. Briefly, 10 μl of the ligation reaction was added to 60 μl H20, 20 μl 5x PCR buffer (335 mM Tris, pH 8.8, 80 mM [NH4] 2 SO 4 , 20 mM MgCl 2 , 0.5 μg/ml bovine seram albumin, and 50 mM 2-mercaptoethanol), 8 μl of 4 mM dNTP stock, 2 μl (124 pmoles) R Bgl 24 (SEQUENCE I.D. NO. 3) and 3.75 units of AmpliTaq® DNA polymerase (Perkin Elmer, cat. # N808-1012). The PCR amplification was performed in a GeneAmp® 9600 thermocycler (Perkin Elmer). Samples were incubated for 5 min. at 72°C to fill-in the 5'-protrading ends of the ligated adaptors. The samples were amplified for 25 to 30 cycles (1 min. at 95°C and 3 min. at 72°C) followed by extension of 72°C for 10 min. After agarose gel confirmation of successful amplicon generation (ie. a smear of PCR products ranging from approximately 100 bp to over 1500 bp), a large scale amplification of tester and driver amplicons was performed. Forty 100 μl PCRs and eight 100 μl PCRs were set up as described above for the prepartion of driver and tester amplicons, respectively. Two μl from the small scale PCR product per 100 μl reaction served as the template for the large scale amplicon generation. Thermocycling was performed as described above for an additional 15 to 20 cycles of amplification. The PCR reactions for both driver and tester DNA were then phenol chloroform extracted twice, isopropanol precipitated, washed with 70% ethanol and digested with Sau3AI to cleave away the adaptors. The tester amplicon was further purified on a low melting point agarose gel. Briefly, 10 μg of tester amplicon DNA was ran on a 2% SeaPlaque® gel (FMC Bioproducts, Rockland, ME). Fragments of 150-1500 base pairs were excised from the gel, the gel slice was melted at 72°C for 20 minutes with 3 ml H20, 400 μl 0.5 M MOPS and 400 μl NaCl. DNA was recovered from the melted gel slice using a Qiagen-tip 20 (Qiagen, Inc., Chatsworth, CA) as directed by the manufacturer. C. Hybridization and Selective Amplification of amplicons Approximately 2 μg of purified tester DNA amplicon was ligated to N Bgl 24 (SEQUENCE I.D. NO.3) and N Bgl 12 (SEQUENCE I.D. NO. 4) as described above. For the first subtractive hybridization, tester amplicon ligated to the N Bgl primer set (0.5 μg) and driver amplicon (20 μg) were mixed, phenol chloroform extracted and ethanol precipitated. The DNA was resuspended in 4 μl of EE x 3 buffer (30 mM EPPS, pH 8.0 at 20°C [Sigma, St. Loius,MO], 3 mM EDTA) and overlaid with 35 μl of mineral oil. Following heat denaturation (3 min at 99°C), 1 μl of 5 M NaCl was added to the denatured DNA and the DNA was allowed to hybridize at 67°C for 20 hours. The aqueous phase was removed to a new tube and 8 μl of tRNA (5 mg/ml) was added to the sample followed by 390 μl TE (10 mM Tris, pH 8.0 and 1 mM EDTA). Eighty μl of the hybridized DNA solution was added to 480 μl H2O, 160 μl 5x PCR buffer (above), 64 μl 4 mM dNTPs and 6 μl (30 units) AmpliTaq® polymerase. This solution was incubated at 72°C for 5 min. to fill in the 5' overhangs created by the ligated N Bgl 24 primer. N Bgl 24 (SEQUENCE I.D. NO. 3, 1.24 nmoles in 20 μl H O) was added, the reaction was aliquoted (100 μl/tube) and subjected to 10 cycles of amplification as described above. The reaction was pooled, phenol/chloroform extracted twice, isopropanol precipitated, washed with 70% ethanol and resuspended in 40 μl H2O. Single-stranded DNA was removed by mung bean nuclease (MBN) . Briefly, 20 μl amplified DNA was digested with 20 units MBN (NEB) in a 40 μl reaction as described by the supplier. One hundred and sixty μl 50 mM Tris, pH 8.8 was added to the MBN digest. The enzyme was heat inactivated at 99°C for 5 min. Eighty μl of the MBN-digested DNA was PCR amplified as described above for an additional 15 cycles. Again, the reaction was pooled, phenol/chloroform extracted twice, isopropanol precipitated, washed with 70% ethanol and resuspended in H2O. The amplified DNA (3 to 5 μg) was then digested with Sau3A I, extracted and precipitated as described above. The final DNA pellet was resuspended in 100 μl TE. D. Subsequent hybridization/amplification steps One hundred ng of the DNA from the previous hybridization/selective amplification was ligated to the J Bgl primer set (SEQUENCE I.D. NO. 5 and SEQUENCE LO. NO. 6) as described previously. This PNA (50 ng) was mixed with 20 μg of driver amplicon and the hybridization and amplificiation procedures were repeated as described above except that the extention temperature during the thremocycling was 70°C and not 72°C as for the N Bgl primer set (SEQUENCE IP. NO. 3 and SEQUENCE LO. NO. 4) and the final amplification step (after MBN digestion) was for 25 cycles. One hundred ng of the second hybridization- amplification product was then ligated to the N Bgl primer set (SEQUENCE I.D. NO. 3 and SEQUENCE I.D. NO. 4), and 200 pg of this material together with 20 μg of driver amplicon was taken for the third round of hybridization/amplification as described above with the final amplification for 25 cycles. A 2% agarose gel of the products from the representational difference analysis (RDA) performed on pre-HGBV inoculated and acute phase T-1053 plasma is shown in FIGURE 14. Referring to FIGURE 14, Lane 1 contains 150 ng of Haeiπ digested Phi-X174 DNA marker (NEB) with the appropriate size (in bp) of the DNA fragments. The complexity of the driver amplicon (lane 2) and the tester amplicon (lane 3) is evidenced by the smear of DNA products seen in these samples. This complexity drops dramatically as the tester sequences are subjected to one (lane 4), two (lane 5) or three (lane 6) rounds of hybridization/selective amplification. E. Cloning of the difference products The difference products were cloned into the BamHI site of pBluescript π KS+ (Stratagene, La Jolla, CA, cat. # 212207), as follows. Briefly, 0.5 μg pBluescript H was digested with BamHI ( 10 units, NEB) and 5' dephosphorylated with calf intestinal phosphatase (10 units, NEB) as directed by the supplier. The plasmid was phenokchloroform extracted, ethanol precipitated, washed with 70% ethanol and resuspended in 10 μl H2O (final concentration approximately 50 ng pBluescript π per μl). The four largest bands from the second hybridization/amplification products were excised from a 2% low melting point agarose gel as described above. Four μl of the melted (72°C, 5 min.) gel slices were ligated to 50 ng of the BamHI-cut, dephosphorylated pBluescript H in a 50 μl reaction using the Takara DNA ligation kit (Takara Biochemical, Berkeley, CA). After incubating at 16°C for 3.5 hours, 8 μl of the ligation reactions were used to transform E. coli competent XL-1 Blue cells (Stratagene) as directed by the supplier. The transformation mixtures were plated on LB plates supplemented with ampicllin (150 μg/ml) and incubated overnight at 37°C. The resulting colonies were grown up in liquid culture and miniprep plasmid DNA was analyzed as described in the art to confirm the existence of cloned product. In addition to the cloning of the four largest products from the second hybridization/amplification step, the entire population of products from the third hybridization/amplification step was cloned into pBluescript H. Briefly, 50 ng pBluescript π vector (prepared as above) was ligated to 10 ng of the third hybridization amplification products in a 50 μl reaction as described above. After incubation at 16°C for 2 hours, 10 μl ligation product was used to transform E. coli competent XL-1 Blue cells as before. Sixty colonies from the resultant transformation were grown up, and miniprep DNA was prepared and analyzed as described and known in the art. Restriction endonuclease digestion and dot blot hybridization experiments were used to identify unique clones. Example 4. Immunoisolation of a cPNA Clone Encoding an Antigenic Region of the HGBV Genome A. Preparation of Concentrated Viras as a Source of Cloning Material The following isolation scheme was employed to isolate the HGBV genome in addition to the procedures exemplified in Example 3. Three tamarins (T-1055, T-1038 and T-1049) were inoculated with seram prepared from tamarin T-1053 as described in Example 2. Referring to TABLE 5, elevated liver enzyme values were noted in all 3 tamarins by day 11 PI. Tamarin T-1055 was sacrificed on day 12 PI and tamarins T-1038 and T-1049 were sacrificed on day 14 PL Approximately 3-4 ml of seram from each of these three tamarins were pooled, providing a total volume of approximately 11.3 ml. The pooled seram was clarified by centrifugation at 10,000 x g for 15 min at 15°C. It was then passed successively through 0.8, 0.45, 0.2, and 0.1 μm syringe filters. This filtered material was then concentrated by centrifugation through a 0.3 ml CsCl cushion (density 1.6 g/ml, in 10 mM Tris, 150 mM NaCl, lmM EDTA, pH 8.0) in a SW41-Ti rotor at 41,000 rpm at 4°C for 68 min. The CsCl layer, approximately 0.6 ml, was removed following centrifigation and stored in three 0.2 ml aliquots at -70°C. Tamarin T-1034 was subsequently inoculated with 0.25 ml of a 10"6 dilution of this pelleted material (prepared in normal tamarin seram). Elevated ALT liver enzyme values were first noted in T-1034 at 2 weeks PI, and remained elevated for the next 7 weeks, finally normalizing by week 10 PI (see FIGURE 30, Example 14). This experiment demonstrated the infectivity of the material concentrated from the pooled tamarin sera. Since this material was shown to be of a relatively high titer, this concentrated source of viras was used as the source of nucleic acid for the preparation of a cDNA library, as described below. B. cDNA Library Construction An aliquot (0.2 ml) of the concentrated viras (described above) was extracted for RNA using a commercially available RNA extraction kit (Stratagene, La Jolla, CA) as instructed by the supplier. The sample was divided into four equal aliquots prior to the final precipitation step, and then precipitated in the presence of 5 μg/ml yeast tRNA. Only one of these aliquots was used for cDNA synthesis; the others were stored at -80°C. Phosphorylated, blunt-ended, double- stranded cDNA was prepared from the RNA using a commercially available kit (Stratagene, La Jolla, CA) as directed by the manufacturer. A double-stranded linker/primer was then ligated to the cDNA ends (sense strand, SEQUENCE I.D. NO. 7; antisense strand, SEQUENCE I.D. NO. 8) in a 10 μl reaction volume using a T4 DNA ligase kit (Stratagene, La Jolla, CA) as directed by the manufacturer. This provided all cDNAs in the mixture with identical 5' and 3' ends containing Not I and Eco RI restriction enzyme recognition sites. G. Reyes and J. Kim, Mol. Cell. Probes 5:473-481 (1991); A. Akowitz and L. Manuelidis, Gene 81:295-306 (1989); and G. Inchauspe et al., in Viral Hepatitis and Liver Disease. F.B. Hollinger et al., Eds., pp. 382-387 (1991). The sense-strand oligonucleotide of the linker/primer was then used as a primer in a PCR reaction such that all cDNAs were amplified independent of their sequence. This procedure allowed for the amplification of rare cDNAs present within the total cDN A population to a level which allowed them to be efficiently cloned, thus producing a cDNA library that is representative of the sequences within the starting material. PCR was performed on a 1 μl aliquot of the above ligate in the presence of the sense-strand oligonucleotide primer (final concentration: 1 μM; reaction volume: 50μl) using the GeneAmp PCR kit (Perkin-Elmer) as directed by the manufacturer in a PE-9600 thermocycler. Thirty cycles of PCR were performed as follows: denaturation at 94°C for 0.5 min, annealing at 55°C for 0.5 min, and extension at 72°C for 1.5 min. A 1 μl aliquot of the resulting products was then re-amplified as described above. The final PCR reaction products were then extracted once with an equal volume of phenol-chloroform (1:1, v/v) and once with an equal volume of chloroform, and then precipitated on dry ice for 10 min following the addition of sodium acetate (final concentration, 0.3 M) and 2.5 volumes of absolute ethanol. The resulting DNA pellet was resuspended in water and digested with the restriction enzyme Eco RI (New England Biolabs) as directed by the manufacturer. The digested cDNAs were then purified from the reaction mixture using a DNA binding resin (Prep-a-Gene, BioRad Laboratories) as directed by the manufacturer and eluted in 20 μl of distilled water. The cPNAs (8 μl) were ligated to 3 μg lambda gtl 1 vector PNA arms (Stratagene, La Jolla, CA) in a reaction volume of 30 μl at 4°C for 1-5 days. Eleven microliters of the ligate was packaged into phage heads using GigaPack m Gold packaging extract (Stratagene, La Jolla, CA) as directed by the manufacturer. The resulting library contained a total of approximately 1.73 million members (PFU) at a recombination frequency of 89.3% with an average insert size of approximately 350 base pairs. C. Immunoscreening of the Recombinant GB cPNA Library The antiseram used for immunoscreening of the cPNA library was obtained from tamarins that had demonstrated elevations in their seram liver enzyme levels following inoculation. Two separate pools of antisera were used for immunoscreening. The first pool contained seram from two animals (T-1048 and T-1051; see Example 1, TABLE 2, and Example 2, TABLE 5, respectively) while the second pool contained seram from a single animal (T1034; see FIGURE 30, Example 14). The specific sera used are shown in TABLE 6. At the time that these samples were chosen for use in cPNA library immunoscreening, they had not been tested for their immunoreactivity with either the 1.4 or 1.7 recombinant CKS proteins (Example 13). Therefore, the results shown herein were obtained independent of any information regarding the presence or absence of HGBV antibodies against these recombinant proteins within the antiseram used. TABLE 6 Tamarin Sera used for Immunoscreening of GB cPNA Library Tamarin " Tamarin Tamarin 1048a 105 lb 1034^ a Total T-1048 pool volume is 2.8 ml. b Total T-1051 pool volume is 6.4 ml. One ml of each pool was saved and the remainder of each was combined and used as the primary antiserum for immunoscreening. c Total T-1034 pool volume is 0.48 ml; the entire pool was used for immunoscreening. The procedure used for the immunoisolation of recombinant phage was based upon the method described by Young and Pavis with modifications as described below. R.A. Young and R.W. Pavis, PNAS 80: 1194-1198 (1983). Two immunoscreening experiments were performed, one utilizing antiseram pooled from T- 1048 and T- 1051 and the other utilizing antiseram from T- 1034. In both cases, the primary antiseram was pre-adsorbed against E. coli extract prior to use in order reduce non-specific interactions of antibody with E. coli proteins. In the first experiment, 1.29 million recombinant phage were immunoscreened with the T-1048/T-1051 antiseram pool; in the second experiment 0.30 million recombinant phage were immunoscreened with T-1034 antiseram. The recombinant phage library was plated on a lawn of E. coli strain Y1090r- and grown at 37°C for 3.5 hours. The plates were then overlayed with nylon filters that were saturated with IPTG (10 mM) and the plates incubated at 42°C for 3.5 hours. The filters were then blocked in Tris-saline buffer containing 1% BSA, 1% gelatin, and 3% Tween-20 ("blocking buffer") for 1 hour at 22°C. The filters were then incubated in primary antiseram (1:100 dilution in blocking buffer) at 4°C for 16 hours. Primary antiseram was then removed and saved for subsequent rounds of plaque purification, and the filters washed four times in Tris-saline containing 0.1% Tween-20. The filters were then incubated in blocking buffer containing 125-I-labeled (or alkaline-phosphatase conjugated) goat anti-human IgG (available from Jackson ImmunoResearch, West Grove, PA) for 60 min at 22°C, washed as described above, and then exposed to x-ray film (or subjected to color development according to established procedures, as in J. Sambrook et al., Molecular Cloning: A Laboratory Manual. 2nd edition, Cold Spring Harbor Press, Cold Spring Harbor, N.Y. , 1989). Five immunopositive phage (4-3B1, 48-1A1, 66-3 Al, 70-3 Al, 78-1C1) were isolated from this library and subsequently tested for specificity of binding to antisera from three infected tamarins (T-1048, T-1051, T-1034) using the method described above. These recombinants encoded polypeptides that reacted with convalescent sera, but not with pre-inoculation sera, from each of the three infected tamarins (data not shown). In order to verify the specificity of the immunological reactivity of the polypeptide encoded by the recombinant phage, each cPNA was rescued from the lambda phage genome by PCR using primers located 5' (SEQUENCE IP. NO. 9) and 3' (SEQUENCE O. NO. 10) to the Eco RI cloning site. The PCR products were then digested with Eco RI and subsequently ligated into the E. coli expression plasmid pJO201 as described in Example 13. Insertion of the cDNAs into the Eco RI site of pJO201 maintained the translational reading frame of this cDNA as present in the lambda phage clone. The subclones in the pJO201 expression vector were designated 4-3B1.1, 48-1A1.1, 66-3A1.49, 70-3A1.37, and 78-1C1.17. Immunoblot analysis (as in Example 13) of E. coli lysates prepared from cultures expressing these cDNAs with convalescent sera from tamarins T-1034, T-1048, and T-1051 (1:100 dilution) demonstrated specific immunologic reactivity with a protein of the size predicted for each CKS-fusion protein, (data not shown). The DNA sequence of each of the cDNAs was determined and it was found that these clones possessed nearly 100% sequence identity with that of HGBV-B viras (SEQUENCE I.D. NO. 11). The sequence of the 4-3B1.1 insert (SEQUENCE I.D. NOS. 12 and 13), although not determined in its entirety, those portions that have been sequenced exhibit 99.5% Sequence identity to a portion of the sequence within HGBV- B (SEQUENCE I.D. NO. 11) from base pairs 6834-7458. This region of the HGBV-B (SEQUENCE I.D. NO. 11) sequence showing identity with that of the sequence obtained from clone 4- 3B 1.1 was translated into the +1 reading frame and is presented in the sequence listing as SEQUENCE I.D. NO. 14. The sequence of the 48-1 Al.l insert (SEQUENCE I.D. NO. 15) exhibits 100% Sequence identity to a portion of the sequence from HGBV-B (SEQUENCE I.D. NO. 11 , see Example 9) from base pairs 4523-4752. The DNA sequence corresponding to SEQUENCE I.D. NO. 15 was translated into the +1 reading frame and is presented in the sequence listing as SEQUENCE I.D. NO. 16. The sequence of the 66-3 Al.49 insert (SEQUENCE I.D. NO. 17) exhibits essentially 100% sequence identity to that of clone 48- 1 Al .1 and thus no protein translation is shown in the sequence listing. The sequence of the 7.0-3 A1.3_7 insert (SEQUENCE I.D. NO. 18) exhibits 100% sequence identity to a portion of the sequence from HGBV-B (SEQUENCE I.D. NO. 11) from base pairs 6450-6732 except for a three base-pair deletion corresponding to bases 6630-6632 of the HGBV-B sequence (SEQUENCE I.D. NO. 11). The DNA sequence corresponding to SEQUENCE ID. NO. 18 was translated into the +2 reading frame and is presented in the sequence listing as SEQUENCE I.D. NO. 19. The sequence of the 78-1C1.17 insert (SEQUENCE I.D. NO. 20) exhibits 100% sequence identity to that of clone 70-3A1.37 and thus no protein translation is shown in the sequence listing. These data demonstrate that the cDNA clones isolated from the lambda gtl 1 cDNA library are derived from the genome of the HGBV agent and that it encodes polypeptides which are specifically recognized immunologically by sera from GB-infected tamarins. Clones 48-lAl.l("clone 48") 4-3B1.1, 66-3A1.49, 70-3A1.37, and 78-1C1.17 have been deposited at the American Type Culture Collection as provided hereinabove. Example 5. DNA sequence analysis of HGBV clones Unique clones obtained in Example 3 were sequenced using the dideoxynucleotide chain termination technique (Sanger, et al., supra) in a kit form (Sequenase® version 2.0, USB). These sequences are non-overlapping and are presented in the Sequence Listing as clone 4 (SEQUENCE I.D. NO. 21), clone 2 (SEQUENCE I.D. NO. 22), clone 10 (SEQUENCE I.D. NO. 23), clone 11 (SEQUENCE I.D. NO. 24), clone 13 (SEQUENCE ID. NO. 25), clone 16 (SEQUENCE I.D. NO. 26), clone 18 (SEQUENCE I.D. NO. 27), clone 23 (SEQUENCE I.D. NO. 28), clone 50 (SEQUENCE I.D. NO. 29) and clone 119 (SEQUENCE I.D. No. 30). Clones 4, 2, 10, 11, 13, 16, 18, 23, 50 and 119 have been deposited at the A.T.C.C. Clone 2 was accorded A.T.C.C. Deposit No. 69556; Clone 4 was accorded A.T.C.C. Deposit No. 69557; Clone 10 was accorded A.T.C.C. Deposit No. 69558; Clone 16 was accorded A.T.C.C. Deposit No.69559; Clone 18 was accorded A.T.C.C. Deposit No. 69560; Clone 23 was accorded A.T.C.C. Deposit No. 69561; and Clone 50 was accorded A.T.C.C. Deposit No. 69562; Clone 11 was accorded A.T.C.C. Deposit No. No. 69613; Clone 13 was accorded A.T.C.C. Deposit No. 69611; and Clone 119 was accorded A.T.C.C. Deposit No. 69612. The sequences were searched against the GenBank database using the BLASTN algorithm (Altschul et al, J. Mol. Biol. 215:403-410 [1990]). None of these sequences were found in GenBank, indicating that these sequences have not been previously characterized in the literature. The DNA sequences were translated into the six possible reading frames and are presented in the sequence listing (SEQUENCE I.D. NO. 21 translates to SEQUENCE I.D. NOS.31-36, SEQUENCE I.D. NO. 22 translates to SEQUENCE I.D. NOS. 37-42, SEQUENCE ID. NO. 23 translates to SEQUENCE I.D. NOS. 43-48, SEQUENCE I.D. NO. 26 translates to SEQUENCE I.D. NOS. 49-54, SEQUENCE I.D. NO. 27 translates to SEQUENCE I.D. NOS. 55-60, SEQUENCE I.D. NO. 28 translates to SEQUENCE I.D. NOS. 61-66, and SEQUENCE I.D. NO. 29 translates to SEQUENCE I.D. NOS. 67-72). SEQUENCE I.D. NO. 24 is contained within SEQUENCE I.D. NO. 73 (described in Example 9), which translates to SEQUENCE I.D. NOS. 74-79. SEQUENCE ID. NOS. 25 and 30 are contained within SEQUENCE I.D. NO. 80 (described in Example 9), which translates to SEQUENCE I.D. NO. 81-86. The translated sequences were used to search the SWISS-PROT database using the BLASTX algorithm (Gish et al., Nature Genetics 3:266-272 [1993]). Again, none of these sequences were found in SWISS-PROT indicating that these sequences have not been previously characterized in the literature. Homology searches conducted using the BLASTN, BLASTX and FASTdb algorithms demonstrate some, albeit low, sequence resemblence to hepatitis C viras (TABLE 7, below). Specifically, translations of clones 4 (SEQUENCE I.D. NO. 35), 10 (SEQUENCE I.D. NO. 44), 11 (residues 1-166 of GB-A, frame 3 [SEQUENCE I.D. NO. 76]), 16 (SEQUENCE I.D. NO. 50), 23 (SEQUENCE I.D. NO. 65), 50 (SEQUENCE I.D. NOS. 70 and 72) and 119 (residues 912-988 of GB- A, frame 3 [SEQUENCE I.D. NO. 83]), are between 24.1% and 45.1% homlogous to various HCV isolates at the amino acid level. Of particular interest, translation of clone 10 (SEQUENCE I.D. NO. 44) showed limited homology to the putative RNA-dependent RNA polymerase of HCV. A comparison of the conserved amino acids present in the putative RNA-dependent RNA polymerase of other positive strand virases (Jiang et al. PNAS 90: 10539- 10543 [1993]) with the putative amino acid translation of clone 10 (SEQUENCE I.D. NO. 44) revealed that conserved amino acid residues of other RNA-dependent RNA polymerases are also conserved in clone 10 (SEQUENCE I.D. NO. 44). This includes the canonical GDD (Gly- Asp- Asp) signature sequence of RNA- dependent RNA polymerases. Thus, clone 10 (SEQUENCE I.D. NO. 44) appears to encode a viral RNA-dependent RNA polymerase. Surprisingly, only clone 10 (SEQUENCE I.D. NO. 44) showed any sequence homology with HCV at the nucleotide level when the BLASTN algorithm was used. Clones 4 (SEQUENCE I.D. NO. 21), 16 (SEQUENCE I.D. NO. 26), 23 (SEQUENCE I.D. NO.28) and 50 (SEQUENCE I.D. NO. 29) and 119 (SEQUENCE ID. NO. 30) which have low HCV homology at the amino acid level, were not detected by BLASTN in searches of GenBank. In addition, clones 2 (SEQUENCE I.D. NOS. 37-42), 13 (SEQUENCE I.D. NO. 25 and 37-42) and 18 (SEQUENCE I.D. NOS. 27 and 55-60) showed no significant nucleotide or amino acid homology to HCV when searched against GenBank or SWISS-PROT as described hereinabove. - Homology found to HCV when GB clones were searched against GenBank using the BLAST algorithm. b Homology found to HCV when translated GB clone sequences were searched against SWISS- PROT using the FASTdb algorithm. c Most homologous strain of HCV (SWISS-PROT designation) d ' e Region of homology and reputed function of clone compared with HCV according to Houghton et al., Hepatology 14(2):381-388 (1991). f BLASTN detected a segment of clone 10 that was 64% homologous with HCV NS5 over 132 nucleotides. Alignment of the entire clone 10 sequences with the homologous nucleotide sequence of HCVJ6 shows 43.6% homology. Example 6. Exogenicity of HGBV clones The HGBV clones were not detected in normal or HGB V-infected tamarin liver DNA, normal human lymphocyte DNA, yeast DNA or E. coli DNA. This was demonstrated for HGBV clones 2 (SEQUENCE I.D. NO. 22) and 16 (SEQUENCE I.D. NO. 26) by Southern blot analysis. In addition, all HGBV clones were analyzed by genomic PCR to confirm the exogenous origin of the HGBV sequences with respect to the tamarin, human, yeast and E. coli genomes. These data are consistent with the viral nature of the HGBV sequences described in Example 5. A. Southern Blot analysis. Tamarin liver nuclei were obtained from low speed pelleting of liver homogenates of HGBV-infected and normal tamarins (described hereinbelow). DNA was extracted from nuclei using a commercially available kit (USB cat. # 73750) as directed by the supplier. The tamarin DNA was treated with RNase during the extraction procedure. Human placental DNA (Clontech, Palo Alto, CA), yeast DNA (Saccharomyces cerevisiae. Clontech) and E. coli DNA (Sigma) were obtained from commercial sources. Each DNA sample was digested with BamHI (NEB) according to the suppliers direction. Digested DNAs (10 μg) and RDA products (0.5 μg each from Example 3B) were electrophoresed on 1% agarose gels and capillary blotted to Hybond-N+ nylon membranes (Amersham, Arlington Heights, IL) as described in Sambrook et al. (pp. 9.34 ff). DNA was fixed to the membrane by alkali treatment as directed by the membrane supplier. Membranes were prehybridized in Rapid Hyb solution (Amersham) at 65°C for 30 min. Radiolabeled probes of the HGBV sequences were prepared by PCR. Briefly, 50 μl PCRs were set up using lx PCR buffer H (Perkin Elmer), 2 mM MgCl2, 20 μM dNTPs, 1 μM each of clone specific sense and antisense primers (for clone 2, SEQUENCE IX). NOS. 87 and 88; for clone 4, SEQUENCE I.D. NOS. 89 and 90; for clone 10, SEQUENCE I.D. NOS. 91 and 92; for clone 16, SEQUENCE I.D. NOS. 93 and 94; for clone 18, SEQUENCE I.D. NOS. 95 and 96; for clone 23, SEQUENCE I.D. NOS. 97 and 98; and for clone 50, SEQUENCE I.D. NOS. 99 and 100), 1 ng HGBV clone plasmid (described in Example 3[E]), 60 μCi α- 32 P-dATP (3000 Ci/mmol) and 1.25 units of AmpliTaq® polymerase (Perkin Elmer). The reactions were incubated at 94°C for 30 sec, 55°C for 30 sec, and 72°C for 30 sec. for a total of 30 cycles of amplification followed by a final extension at 72°C for 3 minutes. Unincorporated label was removed by Quick-Spin® G-50 spin columns (Boehringer Mannheim, Indianapolis, IN) as directed by the supplier. The probes were denatured (99°C, 2 min.) prior to addition to the pre-hybridized membranes. Radiolabeled probes were added to the prehybridized membranes (2 x 10 6 dpm/ml) and filters were hybridized at 65°C for 2.5 hours as directed by the Rapid Hyb® supplier. The hybridized membranes were washed under conditions of moderate stringency (lx SSC, 0.1% SDS at 65°C) before being exposed to autoradiographic film for 72 hours at -80°C with an intensifying screen. These conditions were designed to detect a single copy gene with a similar radiolabeled prohe. The results show that clone 2 (SEQUENCE I.D. NO. 22) and clone 16 (SEQUENCE I.D. NO. 26) sequences did not hybridize to DNA from normal or HGBN-infected tamarin liver (FIGURES 15 and 16, lanes IB and 3B, respectively), human DΝA (FIGURES 15 and 16, lane 1 A), yeast DΝA (FIGURES 15 and 16, lane 2A) or E. coli DΝA (FIGURES 15 and 16, lane 3 A). In addition, no hybridization was detected with the driver amplicon DΝA (FIGURES 15 and 16, lanes 4A, derived from pre-HGBN-inoculated tamarin plasma as described in Example 2.B). In contrast, strong hybridization signals were seen with the tester amplicon (FIGURES 15 arid 16, lane 6 A, derived from infectious HGBN tamarin plasma using total nucleic acid extraction and reverse transcription steps as described in Example 2.B) and the products of the three rounds of subtraction/selective amplification (FIGURES 15 and 16, lanes 7 A, 8 A and 4B referring to the products from the first, second and third rounds of subtraction/selective amplification, respectively). These data demonstrate that HGBN clones 2 (SEQUENCE I.D. NO. 22) and 16 (SEQUENCE I.D. NO. 26) can be detected in nucleic acid sequences amplified from infectious sources; HGBN clones 2 (SEQUENCE I.D. NO. 22) and 16 (SEQUENCE I.D. NO. 26) are not derived from tamarin, human, yeast or E. coli genomic DNA sequences. B. Genomic PCR analysis. To further demonstrate the exogenicity of the HGBV sequences and support their viral origin, PCR was performed on genomic DNA from tamarin, human, yeast and E. coli. DNA from normal tamarin kidney and liver tissue was prepared as described by J. Sambrook et al., supra. Yeast, Rhesus monkey kidney and human placental DNAs were obtained from Clontech. E. coli DNA was obtained from Sigma. PCR was performed using GeneAmp® reagents from Perkin-Elmer- Cetus essentially as directed by the supplier's instructions. Briefly, 300 ng of genomic DNA was used for each 100 μl reaction. PCR primers derived from HGBV cloned sequences (for clone 2, SEQUENCE I.D. NOS. 87 and 88; for clone 4, SEQUENCE I.D. NOS. 89 and 90; for clone 10, SEQUENCE I.D. NOS. 91 and 92; for clone 16, SEQUENCE I.D. NOS. 93 and 94; for clone 18, SEQUENCE I.D. NOS. 95 and 96; for clone 23, SEQUENCE I.D. NOS. 97 and 98; and for clone 50, SEQUENCE I.D. NOS. 99 and 100) were used at a final concentration of 0.5 μM. PCR was performed for 35 cycles (94°C, 1 min; 55°C, 1 min; 72°C, 1 min) followed by an extension cycle of 72°C for 7 min. The PCR products_were separated by agarose gel electrophoresis and visualized by UN irradiation after direct staining of the nucleic acid with ethidium bromide and/or hybridizaion to a radiolabelled probe after Southern blot transfer to a nitrocellulose filter. Probes were generated as described in Example 6A. Filters were prehybridized in Fast-Pair Hybridization Solution from Digene (Belstville, MD) for 3-5 hours and then hybridized in Fast-Pair Hybridization Solution with 100-200 cpm cm^ at 42°C for 15-25 hours. Filters were washed as described in G. G. Schlauder et al., J. Nirol. Methods 37:189-200 (1992) and exposed to Kodak X-Omat-AR film for 15 to 72 hours at -70°C with intensifying screens. FIGURE 17 shows an ethidium bromide stained 1.5% agarose gel. FIGURE 18 shows an autoradiogram from a Southern blot from the same gel after hybridization to the radiolabeled probe from clone 16 (SEQUENCE I.D. NO. 26). Consistent with its exogenous nature, clone 16 (SEQUENCE I.D. NO. 26) sequences were not detected in tamarin (FIGURE 17 and 18, lanes 9 and 10), Rhesus monkey (lane 11) or human genomic DNAs (lane 12) or in yeast or E. coli DNAs (data not shown) by genomic PCR analysis despite being able to detect clone 16 (SEQUENCE I.D. NO.26) sequences that have been spiked into normal tamarin liver and kidney DNA at 0.05 genome equivalents (lanes 17 and 18). In addition, primers derived from the human dopamine Dl receptor gene, 1000-1019 base pairs (sense primer) and 1533-1552 base pairs (antisense primer) (GenBank accession number X55760, R. K. Sunahara. et al., Nature 347:80-83 [1990]) successfully amplified the dopamine Dl receptor DNA from the primate genomic DNAs (FIGURE 17 lanes 2, 3, 4 and 5 coπesponding to tamarin kidney, tamarin liver, rhesus monkey and human DNAs) demonstrating the utility of this method for detecting low copy number (i.e. single copy) sequences. Lanes 1 and 8 are H 2 O contols for dopamine Dl receptor and clone 16 primers (SEQUENCE I.D. NOS. 93 and 94), respectively. Lane 6 contains lOOfg of clone 16 (SEQUENCE I.D. NO. 26) plasmid DNA amplified with the dopamine receptor primers. Lanes 14, 15, 16 and 20 contain 1, 3, 10, and lOOfg, respectively, of clone 16 (SEQUENCE I.D. NO. 26) plasmid DNA. Lanes 7 and 19 are markers. Similar results were obtained using PCR primers specific for clones 2, 4, 10, 18, 23 and 50 described above (data not shown). Clones 2 (SEQUENCE I.D. NO. 22), 4 (SEQUENCE I.D. NO. 21), 10 (SEQUENCE I.D. NO. 23), 18 (SEQUENCE I.D. NO. 27), 23 (SEQUENCE I.D. NO. 28) and 50 (SEQUENCE I.D. NO. 29) are inconclusive at this time. However, clones 4 (SEQUENCE I.D. NO. 21), 10 (SEQUENCE I.D. NO. 23), 18 (SEQUENCE I.D. NO. 27) and 50 (SEQUENCE I.D. NO. 29) sequences were not detected in tamarin, human, yeast and E. coli DNA, (Rhesus monkey was not tested) indicating that these sequences are exogenous to the genomic DNA sources tested and supporting the viral origin of these sequences. Example 7. Presence of HGBN sequences in tamarin sera The presence of the HGBN clone sequences in pre-inoculation and acute phase T-1053 plasma was examined by PCR. Because the HGBN genome could be DΝA or RΝA, PCR and RT-PCR was performed. Specifically, total nucleic acids were extracted from plasma as described in Example 3(A). PCR was performed on the equivalent of 5 μl plasma nucleic acids as described in Example 6(B) and RT-PCR was performed using the GeneAmp® RΝA PCR Kit from Perkin-Elmer-Cetus essentially according to the manufacturer's instructions using 1 μM concentration of primers (for clone 2, SEQUENCE I.D. NOS.87 and 88; for clone 4, SEQUENCE I.D. NOS. 89 and 90; for clone 10, SEQUENCE I.D. NOS. 91 and 92; for clone 16, SEQUENCE I.D. NOS. 93 and 94; for clone 18, SEQUENCE I.D. NOS. 95 and 96; for clone 23, SEQUENCE I.D. NOS. 97 and 98; and for clone 50, SEQUENCE I.D. NOS. 99 and 100) in the PCRs. cDNA synthesis was primed with random hexamers. Ethidium bromide staining and hybridization of the PCR products demonstrated the presence of HGBV clone sequences 2 (SEQUENCE I.D. NO. 22), 4 (SEQUENCE I.D. NO. 21), 10 (SEQUENCE I.D. NO. 23), 16 (SEQUENCE I.D. NO. 26), 18 (SEQUENCE I.D. NO. 27), 23 (SEQUENCE I.D. NO. 28) and 50 (SEQUENCE I.D. NO. 29) in the acute phase T-1053 plasma and not the pre-inoculation T-1053 plasma (data not shown). In addition, HGBV clones 2 (SEQUENCE I.D. NO. 22), 4 (SEQUENCE I.D. NO. 21), 10 (SEQUENCE I.D. NO. 23), 18 (SEQUENCE I.D. NO. 27), 23 (SEQUENCE ID. NO.28) and 50 (SEQUENCE I.D. NO. 29) sequences could be detected in H205, the HGBV inoculum that was injected into tamarin T-1053 (see Example IB). These results are summarized in TABLE 8. It should be noted that the HGBV clone sequences were only detected by RT-PCR in the acute phase plasma. The fact that the HGBV clone sequences were detected in the acute phase plasma by PCR only after a reverse transcription step to convert RNA to cDNA, taken together with the Umited homology of some of these clones with HCV isolates, and the presence of the sequences coding for the conserved amino acids found in the RNA-dependent RNA polymerase in HGBV clone 10 (SEQUENCE I.D. NO. 23; Example 5) suggest that HGBV is an RNA viras. RT-PCR analysis of a panel of tamarin plasmas with HGBV clone 16 sequence (SEQUENCE I.D. NO. 26) was undertaken to confirm the presence of HGBN clone 16 (SEQUENCE I.D. NO. 26) in other individuals who had been experimentally infected with HGBV. Briefly, nucleic acids were isolated as previously described (G. G. Schlauder et al., J. Virological Methods 37:189-200 [1992]) from 25 μl of plasma from tamarins obtained prior to and after experimental infection with the H205 inoculum. Ethanol precipitated nucleic acids were resuspended in 3 μl of DEPC-treated H2O. cDNA synthesis and PCR were performed using the GeneAmp RNA PCR Kit from Perkin-Elmer- Cetus essentially according to the manufacturer's instructions. cDNA synthesis was primed with random hexamers. The resulting cDNA was subjected to PCR using clone 16 primers (SEQUENCE I.D. NOS. 93 and 94) at a final concentration of 0.5 μM. PCR was performed for 35 cycles (94°C, 1 min; 55°C, 1 min; 72°C, 1 min) followed by an extension cycle of 72°C for 7 min. The PCR products were separated by agarose gel electrophoresis and visualized by UV irradiation after direct staining of the nucleic acid with ethidium bromide and/or hybridization to a radiolabelled probe after Southern blot transfer to a nitrocellulose filter as describes in Example 6B. FIGURE 19 shows an ethidium bromide stained 1.5% agarose gel. FIGURE 20 shows an autoradiogram from a Southern blot from the same gel after hybridization to the radiolabeled probe from clone 16 (SEQUENCE I.D. NO. 26). H2O and normal human seram are shown in lanes 1 and 2. Lanes 3, 19 and 20 are markers. Lanes 4, 8, 12,and 16 are from uninfected tamarin sera while lanes 6, 10, 14 and 18 are from infected tamarin sera. These results show that HGBV clone 16 sequence (SEQUENCE I.D. NO. 26) was detected in other individuals infected with HGBV, in addition to tamarin T-1053, and not in uninfected individuals. Acute phase sera from five H205-infected animals were tested. Clone 16 sequences (SEQUENCE I.D. NO. 26) were detected in sera from three of these animals [lane 10, T-1049, 14 days post-inoculation (dpi); lane 14, T-1051, 28 dpi; lane 18, T-1055, 16 dpi.]. The clone 16 sequence (SEQUENCE I.D. NO. 26) was not detected in pre-inoculation sera from any of the five animals (lane 4, T-1048; lane 8, T1049; lane 12, T-1051; lane 16, T- 1055; T-1057 not shown). These results suggest that the clone 16 sequence (SEQUENCE I.D. NO. 26) may be derived from the infectious HGBV agent. The absence of clone 16 sequence (SEQUENCE I.D. NO. 26) in two of five acute phase plasmas (lane 6, T-1048, 28 dpi; T-1057, 14 dpi, not shown) may be explained by the relative low sensitivity of the clone 16 RT-PCR (estimated to be able to detect approximately >1000 copies of clone 16 sequence (SEQUENCE I.D. NO. 26) coupled with the acute resolving nature of HGBV infection in tamarins. Thus, the acute plasma from the two negative animals may contain a titer of HGBV that is below the detection level of the RT-PCR assay employed. The observation that these two animals were positive for clone 4 (SEQUENCE I.D. NO.21) by RT-PCR (Example 14) may reflect the presence of RNA sequences of one virus (containing clone 4) and the absence of detectable RNA sequences from a second virus (containing clone 16). Example 8. Northern blot analysis of HGBV sequences in infected tamarin liver Because the HGBV clone sequences were detectable by RT-PCR in the acute phase tamarin plasma and the H205 inoculum, it was likely that these sequences originate from the HGBV genome. Additional RT-PCR studies demonstrated the presence of the HGBV sequences in liver RNA extracted from the H205-infected tamarin, T-1053 (data not shown). Therefore, to determine the size of the HGBV genome, Northern analysis of H205-infected and uninfected tamarin liver RNA was performed. Total cellular RNA was extracted from 1.25 g liver of H205-infected tamarin T-1053 and from 1.0 g of liver from a control (i.e. uninfected) tamarin T-1040 using an RNA isolation kit (Stratagene, La Jolla, CA) as directed by the manufacturer. Total RNA (30 μg) was electrophoresed through a 1% agarose gel containing 0.6 M formaldehyde (R.M. Fourney, et al., Focus 10: 5-7, [1988]) and then transfeπed to Hybond-N nylon membrane (Amersham) by capillary action in 20X SCC (pH 7.0) as previously described. J. Sambrook, et al.. Molecular Cloning - A Laboratory Manual. 2nd Edition (1989). The RNA was UV-crosslinked to the nylon membrane which was then baked in a vacuum oven at 80°C for 60 min. The blots were prehybridized at 60°C for 2 hours in 25 ml of a solution containing 0.05 M PIPES, 50 mM sodium phosphate, 100 mM NaCl, 1 mM EDTA, and 5% SDS. G.D. Virca, et al., Biotechniques 8:370-371 (1990). Prior to hybridization with the radiolabeled DNA probe, the solution was removed and 10 ml of fresh solution was added. The probes used for hybridization were clone 4 (SEQUENCE I.D. NO. 21; 221 bp) and clone 50 (SEQUENCE I.D. NO. 29; 337 bp) and the 2000 bp cDNA encoding human β-actin. P. Gunning, et al., Mol. and Cell. Biol. 3:787-795 (1983). The probes (50 ng) were radiolabeled using a random primer labeling kit (Stratagene. La Jolla, CA) in the presence of [α-32p]dATP as directed by the manufacturer. The specific activity of each probe was approximately 10^ cpm/μg. The blots were hybridized at 60°C for 16 hours and washed as described (G.D. Virca, et al., supra) and then exposed to Kodak X- Omat-AR film at -80°C. Photographs of the resulting autoradiographs are shown in FIGURE 21 A. Lanes 1, 3, and 5 contain liver RNA from T-1040 and lanes 2, 4, and 6 contain liver RNA from T-1053. Lanes 1 and 2 were hybridized with the human β-actin cDNA probe; lanes 3 and 4 were hybridized with the clone 4 probe (SEQUENCE ID. NO. 21); and lanes 5 and 6 were hybridized with the clone 50 probe (SEQUENCE I.D. NO. 29). Exposure times were as follows: lanes 1 and 2, 5 hours at -80°C; lanes 3-6, 56 hours at -80°C. The positions of the 28S and 18S ribosomal RNAs are indicated by the arrows. The relative sizes of these ribosomal RNAs are 6333 and 2366 nucleotides, respectively. J. Sambrook, et al., supra. Clone 4 (SEQUENCE IX ) . NO. 21) and clone 50 probes (SEQUENCE I.D. NO. 29) hybridized with an RNA species present in RNA extracted from the liver of the infected tamarin (T-1053) (FIGURE 21 A, lanes 4 and 6). The size of this hybridizable RNA species was calculated at approximately 8300 nucleotides based on its relative mobility with respect to 28S and 18S ribosomal RNAs. Both probes appear to hybridize to the same RNA species. Neither probe hybridized with RNA extracted from the liver of the uninfected tamarin (T- 1040) (FIGURE 21 A, lanes 3 and 5). These results suggest that the sequences of clones 4 (SEQUENCE IP. NO. 21) and 50 (SEQUENCE O. NO. 29) are present within the same 8.3 Kb transcript. In order to determine the strandedness of the HGBV RNA genome, strand- specific radiolabeled PNA probes were prepared by assymetric PCR using the GeneAmp® PCR kit from Perkin-Elmer essentially according to the manufacturer's instractions. Purified clone 50 PNA (SEQUENCE ID. NO. 29) was used as template in separate reactions containing either the clone 50 negative strand-specific primer (SEQUENCE LO. NO. 99) or the clone 50 positive strand- specific primer (SEQUENCE I.D. NO. 100) at 1 μM final concentrations. The reaction mixture contained [o,32p-dATP] (Amersham; 3000Ci/mmol) in place of the dATP normally included in the reaction mixture. Following 30-cycles of linear amplification of the template, the unincorprated [α^^p-dATP] was removed by Quick-Spin® Sephadex G50 spin columns (Boehringer-Mannheim, Indianapolis, LN) according to the manufacturer's instructions. Hybridization of the radiolabeled probes to DNA dot blots containing ten-fold serial dilutions of double-stranded clone 50 DNA (SEQUENCE I.D. NO. 29) demonstrated that the two probes possessed nearly identical sensitivities (data not shown). The radiolabled probes were then hybridized to RNA blots containing 30 μg of total liver RNA extracted from uninfected tamarin T- 1040 and from infected tamarin T- 1053 as described above. Photographs of the resulting autoradiographs are shown in FIGURE 21B. Lanes 1 and 3 contain liver RNA from T-1040 and lanes 2 and 4 contain liver RNA from T-1053. Lanes 1 and 2 were hybridized with the clone 50 positive strand probe (i.e., the positive strand is radiolabeled and will detect the negative strand; SEQUENCE I.D. NO. 100); lanes 3 and 4 were hybridized with the clone 50 negative strand probe (i.e., the negative strand is radiolabeled and will detect the positive strand; SEQUENCE I.D. NO.99). The blots were exposed for 18 hours at -80°C. The positions of the 28S and 18S ribosomal RNAs are indicated by the aπows. As shown in FIGURE 21B, the clone 50 positive and negative strand probes (SEQUENCE I.D. NOS.100 and 99, respectively) hybridized to an RNA species of approximately 8.3 kilobases extracted from the liver of the infected tamarin T-1053 (FIGURE 21B, lanes 2 and 4), but not to RNA extracted from the liver of the uninfected tamarin T-1040 (FIGURE 21B, lanes 1 and 3). This is consistent with the Northern blot results obtained with the clone 4 (SEQUENCE I.D. NO. 21) and clone 50 (SEQUENCE I.D. NO. 29) double-stranded probes shown above. The more intense signal obtained with the clone 50 negative strand probe (SEQUENCE I.D. NO. 99) (FIGURE 21B, lane 4 vs. lane 2) suggests that the predominant RNA species present in the liver of infected tamarins is the positive (i.e. coding) strand. Example 9. Extending the HGBV clone Sequence A. Generation of HGBV sequences. The clones obtained as described in Example 3 and sequenced as described in Example 5 hereinabove appear to be derived from separate regions of the HGBV genome. Therefore, to obtain sequences from additional regions of the HGBV genome that reside between the previously identified clones, and to confirm the sequence of the RDA clones, several PCR walking experiments were performed. Total nucleic acids were extracted from 50 μl aliquots of infectious T-1053 plasma as described in Example 3(A). Briefly, precipitated nucleic acids were resuspended in 10 μl PEPC-treated H2O. Standard RT-PCR was performed using the GeneAmp® RNA PCR kit (Perkin Elmer) as directed by the manufacturer. Briefly, PCR was performed on the cPNA products of random primed reverse transcription reactions of the extracted nucleic acids with 2 mM MgCl2 and 1 μM primers. Reactions were subjected to 35 cycles of denaturation-annealing- extension (94°C, 30 sec; 55°C, 30 sec; 72°C 2 min) followed by a 3 min extension at 72°C. The reactions were held at 4°C prior to agarose gel analysis. These products were cloned into pT7 Blue T-vector plasmid (Novagen) as described in the art. TABLE 9 presents the results obtained when these reactions were peformed. A modification of a PCR walking technique described by Sorensen et al. (J. Virol. 67:7118-7124 [1993]) was utilized to obtain additional HGBV sequences. Briefly, total nucleic acid were extracted from infectious tamarin T- 1053 plasma and reverse transcribed. The resultant cDNAs were amplified in 50 μl PCR reactions (PCR 1) as described by Sorensen et al. (supra) except that 2 mM MgCl2 was used. The reactions were subjected to 35 cycles of denaturation- annealing-extension (94°C, 30 sec; 55°C, 30 sec; 72°C, 2 min) followed by a 3 min extension at 72°C. Biotinylated products were isolated using streptavidin-coated paramagnetic beads (Promega) as described by Sorensen et al. (supra). Nested PCRs (PCR 2) were performed on the streptavidin-purified products as described by Sorensen et al. for a total of 20 to 35 cycles of denaturation-annealing-extension as described above. The resultant products and the PCR primers used to generate them are listed in TABLE 10. TABLE 10 Reaction Primer set PCR 1 Primer set PCR 2 Size of PCR product 2.1 SEQ HD #103 /SEQ ID #125 SEQ ID #668 /SEQ ID #126 500 bp 2.2 SEQ E #114 /SEQ ID #125 SEQ ID #105 /SEQ ID #126 1000 bp 2.3 SEQ fl) #92 / SEQ ID #125 SEQ ID #123 / SEQ ID #126 400 bp 2.4 SEQ ID #127 / SEQ ID #128 comp. of SEQ ID #88 / 420 bp SEQ ID #126 2.5 SEQ ID #108 /SEQ ID #128 SEQ E #106 /SEQ D #126 900 bp 2.6 SEQ ID #129 /SEQ ID #125 SEQ ID #98 /SEQ ID #126 750 bp 2.7 SEQ IP #116/ SEQ HD #128 SEQ IP #115 /SEQ ID #126 825 bp 2.8 SEQ ID #130 /SEQ ID #125 SEQ ID #107 /SEQ ID #126 630 bp 2.9 SEQ ID #110/ SEQ ID #135 SEQ ID #131 /SEQ ID #126 390 bp 2.10 SEQ ro #132 / SEQ ro #125 SEQ ID #109/ SEQ ro #126 1000 bp 2.11 SEQro#lll/SEQID#128SEQID#133/SEQID#126 600 bp 2.12 SEQ ro #134 /SEQ ID #135 SEQ ID #112 /SEQ ID #126 580 bp 2.13 SEQ ID #136 /SEQ ID #125 SEQ ID #137 /SEQ ID #126 400 bp 2.14 SEQ ID #138 /SEQ ID #128 SEQ ID #113 /SEQ ID #126 500 bp 2.15 SEQ ID #139 /SEQ ID #128 SEQ ID #140 /SEQ ID #126 900 bp 2.16 SEQ ro #121 /SEQ ID #135 SEQ ID #141 /SEQ ID #126 400 bp 2.17 SEQ π #142 / SEQ ID #125 comp. of SEQ ID #102/ 1000 bp SEQ ID #126 2.18 SEQ ID #143 /SEQ ID #135 SEQ ID #144 /SEQ ID #126 550 bp 2.19 SEQ.ro#87/SEQID#125 SEQXD#90/SEQID#126 220 bp These products were isolated from low melting point agarose gels and cloned into pT7 Blue T- vector plasmid (Novagen) as described in the art. RNA ligase-mediated 5' RACE (rapid amplification of cDNA ends) was employed to obtain the 5' end sequences from viral genomic RNAs as described hereinabove. Briefly, the 5' AmpliFLNDER™ RACE kit (Clontech, Palo Alto, CA) was used as directed by the manufacturer. The source of the viral RNA was acute phase T-1053 plasma that was extracted as described above. The virus- specific oligonucleotides utilized for the reverse transcription (RT), the first PCR amplification (PCR 1) and the second PCR amplification (PCR 2) are listed in TABLE- 11. The ligated anchor primer and its complementary PCR primer were provided by the manufacturer. PCRs were performed with the GeneAmp® PCR kit (Perkin Elmer) as directed by the manufacturer. The products generated by RNA ligase-mediated 5' RACE were isolated from low melting point agarose gels and cloned into pT7 Blue T- vector plasmid (Novagen) as described in the art. To obtain additional sequence at the 5' and 3' ends of HGBV-B SEQUENCE (see below, Evidence for the existence of two HCV-like flavivirases in HGBV). an RNA circularization experiment was performed. (This method is based on that described by C.W. Mandl et al. (1991) Biotechniques. Vol 10 (4): 485-486.) Total nucleic acids were purified from 50 μl of T-1057 plasma (14 days post H205 inoculation except that 1 μg glycogen replaced the tRNA in the precipitation. The nucleic acid pellet was dissolved in 16.3 μl of DEPC-treated water, and 25 μl of 2X TAP buffer ( 1X=50 mM NaOAC, pH 5.0, 1 mM EDTA, 10 mM 2-mercaptoethanol, 2mM ATP) and 8.7 μl of tobacco acid pyrophophatase (20 Units; Sigma) were added. The mixture was incubated at 37°C for 60 min. The sample was extracted with phenol (water-saturated) followed by chloroform and then precipitated with NaOAC/EtOH in the presence of glycogen (1 μg). The pellet was dissolved in 83 μl of DEPC water and 10 μl of 10X RNA ligase buffer (New England Biolabs, NEB), 2 μl of RNase inhibitor (Perkin Elmer), and 5 μl of T4 RNA ligase (NEB) was then added. The mixture was incubated at 4°C for 16 hours. The sample was then extracted with phenol (water-saturated) and then chloroform as before and then precipitated with NaOAC/EtOH. One-tenth of the ligated RNA was used in the reverse transcriptase (RT) reaction using Superscript RT (GIBCO/BRL) and SEQUENCE ID. NO. 146 as . the primer as directed by the manufacturer . One-half of the RT reaction mix was used for PCR1 in the presence of a biotinylated oligonucleotide primer (SEQUENCE ID. NO. 146) and and a second oligonucleotide primer (SEQUENCE ID. NO. 133) as described above. PCR1 products were purified from the reaction mixture using streptavidin-magnetic beads as described by Sorensen et al. Purified PCR1 products (2 μl out of 30 μl) were used as the template for PCR2. PCR2 using oligonucleotide primers (SEQUENCE LD. NOS. 147 and 154) yielded a 1200 bp product that was cloned into pT7 Blue T- vector plasmid and sequenced as described below. Sequence analysis of two independent clones from this experiment demonstrated 100% identity in the region of overlap with known sequence (although one clone possessed a sequence of 18 T residues and the other a sequence of 27 T residues), and an additional 270 bases of new sequence. The above circularization experiment provided sequence from both the 5'- and 3'-ends of the HGBV-B viral genome that was not obtained using standard 3'- or 5'-RACE techniques. However, the exact 5'-3' junction is difficult to determine even after additional PCR experiments are performed using primers designed from the newly obtained sequence. Thus, in order to better characterize the 5 '-end of the HGBV-B RNA genome a primer extension experiment was performed using RNA isolated from the liver of T-1053. Total cellular RNA was isolated from the liver of T-1053 and a control (i.e. uninfected) animal (T-1040) as described in Example 7. An antisense oligonucleotide (SEQUENCE I.D. NO. 155) was endlabeled with γ- 32 P-ATP using T4 polynucleotide kinase (NEB) to a specific activity of approximately 9.39 x 10 7 CPM/μg as described (Sambrook et al.). The primer was annealed to 30 μg of T-1053 and T-1040 liver RNA in separate reactions and then extended using MMLV reverse transcriptase (Perkin-Elmer) as previously described (Sambrook et al). The products were analyzed on a 6% sequencing gel. A sequence ladder generated from one of the HGBV-B circularization clones using the same primer as that utilized for the primer extension served as a size standard. Primer extension products of 176 bp were obtained from T-1053. These products were not obtained when primer extension was performed using liver RNA from an uninfected animal (T-1040) and therefore represent products derived from the HGBV-B genome. The length of the products obtained indicate that the 5 '-end of the genome, as present in the liver of infected animals, is located 442 nucleotides upstream of the initiator AUG codon. To confirm the 3' location of the sequence obtained in the circularization . experiment, RT-PCRs were performed using primers designed to the predicted 3' termini (see reaction 1.25, TABLE 2). RT-PCR of infectious T-1053 plasma as (described above) using SEQUENCE ID. NOS. 156 and SEQUENCE ID. NO. 157 yielded a product of 450 bp. In contrast, RT-PCR using the complement of SEQUENCE ID. NO.157 and SEQUENCE ID. NO. 147 did not yield a detectable PCR product (data not shown). These data suggest that the 3' end of the genome is located 50 nucleotides downstream of the poly T tract. The cloned products from TABLES 9, 10 and 11, and the RNA circularization experiment were sequenced as previously described in Example 5. Interestingly, the cloned products of reactions 1.4, 1.6, 1.9, 1.10 and 1.11 were found to contain only one of the two primer sequences at the termini, suggesting that these products were the result of false priming events. PCR sequencing experiments have linked sequences detected in products 1.4, 1.6, 1.9, 1.10 and 1.1 1 with clone 4 (SEQUENCE I.D. NO. 21) and/or clone 50 (SEQUENCE I.D. NO. 29). In addition, sequences derived from each of these reactions contain limited HCV identity. Thus, these products, although a result of false priming at one end of the PCR product, appear to contain authentic HGBV sequence. The product from reaction 1.14 also appeared to be a result of false priming. Here, the complement of SEQUENCE LD. NO. 160 is found at the 5' end of the product from reaction 1.14 (GB-B, FIGURE 22). This was unexpected because SEQUENCE LD. NO. 160 was derived from SEQUENCE I.D. NO. 161 which resides in GB-A. However, the sequence identity between products from reactions 1.14 and 2.8, together with additional PCRs/sequencing experiments (data not shown), demonstrate that reaction 1.14 contains authentic HGBV sequence. Apparently, the complement of SEQUENCE LD. NO. 160 had enough identity to GB-B sequences upstream of SEQUENCE I.D. NO. 162 to act as a PCR primer. The sequences obtained from the products described in TABLES 9, 10 and 11 hereinabove, and the RNA circularization experiment were assembled into contigs using the GCG Package (version 7) of programs. A schematic of the assembled contigs is presented in FIGURE 22). GB contig A (GB-A) is 9493 bp in length, all of which has been sequenced and is presented in SEQUENCE I.D. NO. 163. GB-A includes clones 2 (SEQUENCE LD. NO. 22), 16 (SEQUENCE LD. NO. 26), 23 (SEQUENCE I.D. NO. 28), 18 (SEQUENCE LO. NO. 27), 11 (SEQUENCE LO. NO. 24) and 10 (SEQUENCE I.D. NO. 23). SEQUENCE I.D. NO. 163 was translated into three possible reading frames and is presented in the Sequence Listing as SEQUENCE I.D. NOS. 164-392. GB contig B (GB-B) is 9143 bp and is presented in SEQUENCE I.D. NO. 393. GB-B (SEQUENCE LD. NO. 393) includes clones 4 (SEQUENCE I.D. NO. 21), 50 (SEQUENCE I.D. NO. 29), 119 (SEQUENCE I.D. NO. 30) and 13 (SEQUENCE I.D. NO. 25). SEQUENCE I.D. NO. 393 was translated into one open reading frame and is presented in the Sequence Listing as SEQUENCE I.D. 396 and 397. The UTRs from the 5' and the 3' ends can each be translated into six reading frames. B. Evidence for the existence of two HCV-like viruses in HGBV 1. Evidence for GB-A and GB-B representing two distinct RNA species. Comparison of GB-A (SEQUENCE I.D. NO. 163) GB-B (SEQUENCE LD. NO. 393) and HCV-1 (GenBank accession # M67463) demonstrate that GB- A (SEQUENCE I.D. NO. 163), GB-B (SEQUENCE I.D. NO. 393) and HCV-1 are all distinct sequences. Dot plot analyses of the nucleic acid sequences of GB- A (SEQUENCE I.D. NO. 163), GB-B (SEQUENCE I.D. NO. 393) and HCV-1 were performed using the GCG Package (version 7). Using a window size of 21 and a stringency of 14, GB-A (SEQUENCE I.D. NO. 163), GB-B (SEQUENCE I.D. NO. 393) and HCV-1 were found to clearly contain different nucleotide sequences (FIGURE 23). Therefore, GB-A (SEQUENCE I.D. NO. 163) and GB-B (SEQUENCE I.D. NO. 393) do not represent different strains or genotypes of HCV or of each other. Short regions of limited nucleotide identity are found in the putative NS3-like and NS5b-like sequences of GB-A (SEQ. ID. NO. 163) and GB-B (SEQ. LP. NO. 393) and the NS3 and NS5b sequences of HCV by this analysis. However, nucleotide identity in these regions is not surprising because NS3 and NS5b code for the putative NTP-binding helicase and the RNA- dependent RNA polymerase, respectively, which are conserved in all flavivirases (see below). That GB-A (SEQUENCE LP. NO. 163) and GB-B (SEQUENCE LO. NO. 393) represent separate RNA molecules and not different regions of the same RNA molecule is evidenced by the 5' RACE experiments (above) and supported by the Northern blot data (as described in Example 8. First, the 5' RACE experiments show distinct 5' ends for GB-A (SEQUENCE I.D. NO. 163) and GB-B (SEQUENCE I.D. NO. 393). Because RNA molecules can contain only one 5' end, GB-A (SEQUENCE I.D. NO. 163) and GB-B (SEQUENCE I.D. NO. 393) represent separate RNA molecules. Second, the 8300 base RNA molecule detected in infected tamarin liver RNA by probing Northern blots with clones 4 and 50 (SEQUENCE I.D. NOS. 21 and 29, respectively, both from GB- B [SEQUENCE I.D. NO. 393], see Example 8, corresponds closely to the size of GB-B (SEQUENCE I.D. NO. 393, 9143 bp). If GB-A and GB-B were part of the same RNA molecule, one would expect a Northern blot product of at least 17,000 bases. These data demonstrate that GB-A (SEQUENCE I.D. NO. 163) and GB-B (SEQUENCE LD. NO. 393) represent the nucleotide sequences of two distinct RNA molecules that are not variants of HCV or each other. Northern blot analysis and PCR studies of T-1053 provided evidence that the two RNA species corresponding to GB-A (SEQUENCE I.D. NO. 163) and GB-B (SEQUENCE I.D. NO. 393) were not at equivalent levels in the liver. As stated above, clones 4 and 50 (SEQUENCE I.D. NOS. 21 and 29, respectively), both from the GB-B (SEQUENCE LD. NO. 393), hybridized to an 8.3 kb RNA species present in infected liver of T-1053 (as described in Example 8). In contrast, clones 2 (SEQUENCE I.D. NO. 22), 10 (SEQUENCE I.D. NO. 23), 16 (SEQUENCE LD. NO. 26 and 23 (SEQUENCE I.D. NO. 28), all from GB-A (SEQUENCE LD. NO. 163), showed no hybridization with T-1053 liver RNA in identical experiments (data not shown). In addition, clone 16 PCR generated much less product than clone 4 PCR on cDNAs generated from T-1053 liver RNA by ethidium staining, despite equivalent sensitivities of clone 4 and clone 16 PCRs demonstrated using plasmid templates (data not shown). This is in contrast to what is found in T-1053 plasma at the time of sacrifice. PCR titration experiments for clone 4 (GB-B-specific, SEQUENCE I.D. NO. 393) and clone 16 (GB-A- specific, SEQUENCE LO. NO. 163) PCR on cDNAs generated from T-1053 plasma RNA suggest that equivalent amounts of GB-A (SEQUENCE I.D. NO. 163) RNA and GB-B (SEQUENCE I.D. NO. 393) RNA are present in T-1053 plasma (Example 4, E.2). Thus, although GB-A (SEQUENCE I.D. NO. 163) RNA and GB-B (SEQUENCE I.D. NO. 393) RNA were at equivalent levels in T- 1053 plasma, there appeared to be a greater amount of GB-B (SEQUENCE LD. NO. 393) RNA relative to GB-A (SEQUENCE I.D. NO. 163) RNA present in T- 1053 liver at the time of sacrifice. Together, these results provide further evidence for the existence of two different RNA molecules coπesponding to GB-A (SEQUENCE LD. NO. 163) and GB-B (SEQUENCE I.D. NO. 393) in T-1053 plasma and suggest that these RNAs are not necessarily present at equivalent levels in infected liver RNA. Therefore, it is unlikely that GB-A (SEQUENCE LD. NO. 163) and GB-B (SEQUENCE I.D. NO. 393) make up individual segments of a single viral genome. 2. Evidence that GB-A (SEQUENCE I.D. NO. 163) and GB-B (SEQUENCE LD. NO. 393) represent the genomes of two distinct viruses. Infectivity and PCR studies provide evidence for the viral nature of GB-A (SEQUENCE LD. NO. 163) and B (SEQUENCE I.D. NO. 393). Specifically, . tamarins T-1049 and T-1051 which were inoculated with T-1053 plasma that had been filtered (0.1 μm) and diluted to 10 -4 , or unfiltered and diluted to 10" 5 , respectively, were positive for both clone 4 (GB-B [SEQUENCE LD. NO. 393) and clone 16 (GB-A [SEQUENCE I.D. NO. 163]) sequences. Prior to inoculation, both of these animals were negative for clones 4 and 16 (Examples 4, E.4 and 4, E.5). Therefore, the two RNA species present in the acute phase T- 1053 plasma corresponding to GB-A and GB-B can be filtered, diluted and passaged to other animals consistent with the proposed viral nature of GB-A (SEQUENCE LD. NO. 163) and GB-B (SEQUENCE I.D. NO. 393). That GB- A and GB-B represent RNA molecules from separate viral particles is evidenced by PCR studies of the H205-inoculated tamarins. Specifically, four of four tamarins became positive for clone 4 (GB-B [SEQUENCE LD. NO. 393]) by RT- PCR after H205 inoculation. In contrast, only one of 4 H205-inoculated tamarins (T-1053) became positive for clone 16 (GB-A [SEQUENCE I.D. NO. 163]) by RT-PCR (Example 4.E.2). Therefore, assuming that GB-A (SEQUENCE I.D. NO. 163) sequences were truly absent from T-1048, T-1057 and T-1061, and that the negative clone 16 PCR results were not due to poor sensitivity, it would appear that the viras corresponding to GB-B (SEQUENCE I.D. NO. 393) sequences (i.e. hepatitis GB viras B [HGBV-B]) can be passaged independent of GB-A (SEQUENCE LD. NO. 163) sequences. An HGBV-B only sample from T-1057 has been passaged two additional times (Example 4). GB-A (SEQUENCE I.D. NO. 163) sequences have not been detected in these animals by RT-PCR. In addition, significant liver enzyme elevations have been noted in these animals (Example 4), demonstrating that HGBV-B alone caused hepatitis in tamarins. GB- A (SEQUENCE I.D. NO. 163) sequences have been identified in tamarins lacking detectable GB-B (SEQUENCE LD. NO. 393) sequences. Specifically, GB-B only animals (T-1048, T-1057 and T-1061) challenged with T-1053 plasma developed GB-A (SEQUENCE I.D. NO. 163) only viremias as detected by clone 16 specific RT-PCR. The GB-A only plasma from T-1057 has been passaged one additional time (Example 4). Thus, it appears that a viras corresponding to GB-A (SEQUENCE LD. NO. 163) sequences (hepatitis GB viras A [HGBV-A]) can replicate independent of HGBV-B. Additional passages of HGBV-A in the absence of HGBV-B is ongoing. At this time it is not known whether HGBV-A causes hepatitis in tamarins. However, the lack of elevated liver enzymes noted in the T-1053 challenged tamarins with HGBV-A viremias and in the passage of the HGBV-A only seram from T-1057 argue against the hepatotropic nature of HGBV-B in tamarins. The presence of two virases in acute phase T-1053 plasma can be traced back to the H205 inoculum. Specifically, data from Example 7 showed that clone 16 (SEQUENCE I.D. NO.26, found in GB-A [SEQUENCE I.D. NO. 163]) was absent in the preinoculation plasma from all 7 tamarins tested. In addition, clones 2, 10, 18 and 23 (SEQUENCE I.D. NOS. 22, 23, 27 and 28, respectively, all from GB-A [SEQUENCE LD. NO. 163]) have not been detected in any pre- HGBV-inoculated tamarin plasma tested (Example 7. Similar negative results were found when preinoculation tamarin plasma were tested for clones 4 and 50 (SEQUENCE I.D. NOS. 21 and 29, respectively, all from GB-B [SEQUENCE I.D. NO.393]). Thus, both HGBV-A and HGBV-B were absent in the preinoculation tamarin plasma. In contrast, all of these clones (i.e. clones 2, 10, 16, 18 and 23 from GB-A [SEQUENCE I.D. NO. 163], and clones 4 and 50 from GB-B [SEQUENCE I.D. NO. 393]) were detected in the H205 inoculum (TABLE 7). Interestingly, as found in cPNA made from T-1053 liver (above), several different PCR targets in GB-A (SEQUENCE LP. NO. 163) all generated less product than similar PCR targets in GB-B (SEQUENCE LO. NO. 393) using the same random primed cDNAs from H205 (data not shown). Thus, we conclude that HGBV-A and HGBV-B are present in the original GB inoculum, H205. However, HGBV-B appears to be more abundant than HGBV-A in H205. The low relative amount of HGBV-A in the H205 inoculum may explain why only one of four tamarins were positive for the HGBV-A after H205 inoculation (Example 4.E.2). 3. Evidence that HGBV-A and HGBV-B are members of the Flaviviridae. Searches of the SWISS-PROT database with the three frame translation products of GB-A (SEQUENCE I.D. NO. 165-268, 270-384, 386-392) and GB- B (SEQUENCE I.D. NO. 397) as described in Example 5 show limited, but significant amino acid sequence identity with various strains of HCV. Translation products from GB- A (SEQUENCE I.D. NO. 164) and GB- B (SEQUENCE I.D. NO. 393) show the closest homology to regions of the nonstructural proteins of various HCV isolates (i.e. NS2, NS3, NS4 and NS5). For example, as shown in FIGURE 24, the conserved residues (indicated by *) in the putative NTP-binding helicase domain of flavivirases (FIGURE 24A) and in the RNA-dependent RNA polymerase domain of all viral RNA-dependent RNA polymerases (FIGURE 24B) are held in common between HCV-1 NS3 and NS5b (SWISS-PROT accession number p26664), respectively, and the predicted translation products of GB-A (SEQUENCE LD. NO. 390) and GB- B (SEQUENCE I.D. NO. 397). (See Choo et al., PNAS 88:2451-2455 [1991] and Domier et al., Virology 158:20-27 [1987]). Therefore, it appears that both GB- A viras and GB- B viras encode functional NTP-binding helicases and RNA-dependent RNA polymerases. However, GB-A (SEQUENCE I.D. NO. 390) and GB-B (SEQUENCE LD. NO. 397) do not share complete amino acid identity to each other and/or to HCV in other regions of HCV NS3 and NS5b. Specifically, over the 200 residue region of NS3 shown in FIGURE 24A, GB- A (SEQUENCE I.D. NO. 390, residues 1252-1449) viras and HCV-1 (SEQ. ID. NO.398), GB-B (SEQUENCE I.D. NO. 397, residues 1212-1408) viras and HCV-1 (SEQUENCE I.D. NO.398), and GB- A (SEQUENCE I.D. NO. 390, residues 1252-1449) viras and GB- B (SEQUENCE LD. NO. 397, residues 1212-1408) viras are 47%, 55% and 43.5% identical, respectively. In addition, over the 100 residue region of NS5b shown in FIGURE 24B, GB-A (SEQUENCE I.D. NO. 390, residues 2644-2739) virus and HCV-1 (SEQUENCE I.D. NO. 398), GB- B (SEQUENCE I.D. NO. 397, residues 2513-1612) virus and HCV-1 (SEQUENCE I.D. NO.398), and GB-A (SEQUENCE I.D. NO. 390, residues 2644-2739) viras and GB- B (SEQUENCE LD. NO. 397, residues 2599-2698) viras are 36%, 41% and 44% identical, respectively. Lower levels of homology are found in other putative nonstructural genes of GB- A (SEQUENCE I.D. NO. 390) and GB-B (SEQUENCE I.D. NO. 397) when compared to HCV. The overall level of homology of the putative nonstructural proteins of GB- A viras and GB- B viras compared with HCV sequences present in GenBank suggests that both GB-A (SEQUENCE I.D. NO. 164) and GB-B (SEQUENCE I.D. NO. 393) are derived from two separate members of the Flaviviridae. Flavivirases contain a single genomic RNA molecule which code for one NTP-binding helicase domain and one RNA- dependent RNA polymerase domain. The presence of two contigs, each containing a putative RNA helicase domain and a putative RNA-dependent RNA polymerase is consistent with the presence of two HCV-like flavivirases in the acute phase T-1053 plasma. Example 10. PCR In order to determine the sequence relatedness of HGBV to hepatitis C virus the following PCR-based experiment was performed. PCR primers based on the 5 '-untranslated region (UTR) sequence of the HCV genome (J.H. Han, PNAS 88:1711-1715 [1991]), which are highly conserved in HCV isolates from a variety of geographic origins (Cha, T.-A., et al., J. Clin. Microbiol. 29:2528- 2534 [1991]) were utilized in attempts to detect similar sequences in H205-infected tamarin T-1053 liver RNA. Total cellular RNA was extracted from the liver of infected tamarin T1053 and from the liver of an uninfected tamarin (T-1040) as described in Example 8 A. Thirty micrograms of each RNA sample was reverse transcribed and PCR amplified using a kit available from Perkin-Elmer essentially as described in the manufacturer's instructions. An antisense primer (primer 1) was used for the reverse transcriptase reaction and comprised bases 249-268 of the HCV 5' -UTR. Primer 1 and a primer comprising bases 13-46 of the HCV 5'- UTR (primer 2) were then used for PCR amplification of the intervening sequence. The conditions used for thermocycling were essentially as described by Cha et al., supra. In order to increase the sensitivity of this assay for the detection of HCV 5' -UTR sequences in H205 infected tamarin T-1053, the above PCR reaction was subjected to a second amplification reacton which utilized "nested" PCR primers. These primers are derived from sequences found internal to the sequences of primers 1 and 2 above in the HCV 5' -UTR: Primer 3 comprised sequences from 47-69 and primer 4, an antisense primer, comprised bases 188-210 of the HCV 5' -UTR. In this "nested" PCR reaction, PCR products (2 μl out of a total of 100 μl reaction volume) from the first PCR reaction were used as the source of DNA template. The thermocycling parameters were essentially the same as described above except that the annealing temperature was 55°C instead of 60°C. The resulting PCR products from the second PCR reaction were then analyzed for the expected DNA products by agarose gel electrophoresis and ethidium bromide staining. The expected DNA fragment sizes, based on the sequence of the HCV 5'UTR (Han et al., supra) is 253 bp for the product of the first PCR reaction and 163 bp for the product of the nested PCR reation. PCR products of the anticipated size were obtained in control experiments performed using 30 μg of total celluar RNA extracted form the liver of an HCV infected chimpanzee as described in Example 8A (data not shown), thus demonstrating that this experimental procedure was able to detect the 5-UTR of HCV. However, neither of the expected products were observed on the resulting ethidium bromide stained agarose gel when either T-1053 liver RNA or T-1040 liver RNA were used (data not shown). This inability to produce the predicted result may suggest that (i) the sequence of the 5'- UTR of the agent differs significantly from that of HCV such that the oligonucleotide primers used would not be able to anneal efficiently thereby dissallowing PCR amplification from occurring or (ii) the agent lacks a 5' -UTR. In either case it appears from these results that the nucleotide sequence of the agent is significantly different from that of HCV. In addition, nucleic acids were isolated as in Example 7 from a chimpanzee plasma pool obtained during the acute phase of an experimental infection of HCV (G. Schlauder et al., J. Clin. Microbiologv 29:2175-2179 [1991]). RT-PCR was performed as described in Example 7 using clone 16 primers (SEQUENCE I.D. NOS. 93 and 94). No bands of the expected size for these primers were detected by ethidium bromide staining or after hybridization to a clone 16 specific probe (data not shown). These results support the unrelatedness of clone 16 sequence (SEQUENCE LO. NO. 26) to HCV. Example 11. Reactivity of HGBV Infected Serum to Other Hepatits Virases Seram specimens were obtained prior to, and after, inoculation with HGBV using either the H205 inoculum (T-1048, T-1057, T-1061) or the T-1053 inoculum (T- 1051 ) and tested for antibodies frequently detected following exposure to known hepatitis viruses. Specimens were tested for antibodies to hepatitis A viras (using the HAVAB assay, available from Abbott Laboratories, Abbott Park, LL), the core protein of hepatitis B core (using the Corzyme® test available from Abbott Laboratories, Abbott Park, LL), hepatitis E viras (HEV) (using the HEV EIA,-available from Abbott Laboratories, Abbott Park, IL) and hepatitis C viras (HCV) (utilizing HCV second generation test, available from Abbott Laboratories, Abbott Park, LL). These tests were performed according to the manufacturer's package inserts. None of the tamarins tested positive for antibodies to HCV or to HEV either prior to or after HGBV inoculation (see TABLE 12). Therefore, HGBV infection does not elicit detectable antisera against HCV or HEV. One of the tamarins (T-1061) was positive for antibodies to HAV prior to and after inoculation with HGBV, suggesting a previous exposure to HAV (TABLE 9, T-1061). However, the three remaining tamarins (T-1048, T-1057 and T- 1051 ) show no HAV-specific antibodies after HGBV inoculation. Therefore, HGBV infection does not elicit an anti-HAV response. One of the tamarins (T-1048) was negative for antibodies to HBV core both prior to and after inoculation with HGBV. Two of the tamarins (T-1061 and T-1057) were positive prior to inoculation with HGBV. One of the tamarins (T-1051) was borderline positive for antibodies to HBV prior to inoculation, but was negative after inoculation. Based on these data, there is no evidence that infection with the HGBV agent induces an immune response to HBV core. Taken together, these data support that the HGBV agent is a unique viral agent, and is not related to any of the viral agents commonly associated with hepatitis in man. Example 12. Western Blot Analysis of HGBV Infected Liver. As noted in Examples 1 and 2 above, elevated liver enzyme values are noted in tamarins inoculated with HGBV. If HGBV is indeed a hepatotropic virus, it would be expected that viral protein(s) would be produced in infected liver cells, and that an immune response to those proteins would be generated. In this example, evidence is presented which suggests that a unique protein appears in livers obtained from HGBV-infected tamarins; this protein appears to be specifically recognized via Western blot utilizing tamarin seram obtained in the convalescent stage following infection with HGBV. HGBV-infected tamarin livers and various control tamarin and chimpanzee livers were diced and homogenized in PBS (approximately 1 g liver to 5 ml) using a Omni-mixer homogenizer. The resulting suspension was clarified by centrifugation (10,000 x g, 1 hour, 4°C) and by micro-filtration through 5 μm, 0.8 μm and 0.45 μm filters. The clarified homogenate was centrifuged under conditions pelleting all components of 100S or greater. Pellets (100S liver fractions) were taken up in a small volume of buffer and stored at -70°C. SDS polyacrylamide gel electrophoresis (PAGE) was carried out using standard methods and reagents (Laemmli discontinuous gels). 100S liver fractions were diluted 1:20 in a sample buffer containing SDS and 2-mercaptoethanol and heated at 95°C for 5 minutes. The proteins were electrophoresed through either 12% acrylamide or 4-15% acrylamide linear gradient gels, 7cm x 8cm, at 200 volts for 30 to 45 minutes. Proteins were electro-transferred to nitrocellulose membranes using standard methods and reagents. Western blots were developed using standard methods. Briefly, the nitrocellulose membrane was briefly rinsed in TBS Tween and blocked overnight in TBS/CS (100 mM Tris, 150 mM NaCl, 10 mM EDTA, 0.18% Tween-20, 4.0% calf seram, pH 8.0) at 4°C. The nitrocellulose was placed in the Multi-screen apparatus and 600 μl of sera was placed in the channels and followed with a 2 hour room temperature and an overnight 4°C incubation. After removing the membrane from the Multi-screen apparatus, it was washed 3 times, 5 minutes each, in 15 ml TBS Tween (50 mM Tris, 150 mM NaCl, 0.05% Tween-20, pH 8.0). The membrane was incubated for 1 hour at room temperature in 15 ml goat anti-human:HRPO conjugate (0.2 μg/ml TBS/CS). After washing as before, the membrane was incubated in the TMB enzyme substrate solution, rinsed in water and dried. Proteins isolated from T-1053 liver at sacrifice (12 days post-GB inoculation) and blotted as described above showed a unique immunogenic protein with an apparent molecular weight of approximately 50 to 80 kDa when reacted with T-1057 sera from 5, 6, 7, 9 or 11 weeks post-GB inoculation. The band was not present when reacted with T-1057 sera pre-inoculation or 3 weeks post-GB inoculation. This band did not appear in the lanes containing liver proteins obtained from an uninoculated tamarin (T-1040) when reacted with any of these T- 1057 sera. In addition, a protein of the same size (50 to 80 kPa) was visible when the T-1053 liver proteins were reacted with other post-GB inoculation sera (T- 1048 at 11 weeks post-GB inoculation and T-1051 at 8 weeks post-GB inoculation) but not when they were reacted with pre-inoculation sera from these same animals. An additional Western blot experiment was performed to determine if this immunoreactive band would be detected in liver tissues from other GB-inoculated tamarins, or in liver tissues of chimpanzees infected either with HCV or HBV. In each case, the nitrocellulose strips containing the liver proteins were reacted with a pool of sera from T-1048 (5, 8, and 16 weeks post-GB inoculation) and T-1051 (8 and 12 weeks post-GB inoculation). All 5 sera in the pool were mixed in equal proportion. A reactive protein band of 50-80 kPa was seen with all of the tamarin liver samples obtained from GB inoculated tamarins ( T-1038, T-1049, and T- 1055 obtained at 14 days post-GB inoculation and T-1053 obtained at 12 days post-GB inoculation). This immunoreactive band was not detected in the liver preparations obtained from T-1040 (uninoculated) nor in any of the chimp liver preparations (CHAS-457 (pre-HCV inoculation), CHAS-457 (HCV+), CRAIG- 454 (HCV+) and MUNA-376 (HBV+). Taken together, these data demonstrate the existence of an immunogenic and antigenic protein with an apparent molecular weight of approximately 50 to 80 kPa specifically associated with HGBV-infected tamarin liver. The nature of this HGB V-associated protein (ie. whether it is viral encoded or of host origin) is cuπently under investigation. Regardless of the source of the HGB V-associated protein, these result are consistent with HGBV infection inducing an antibody response to an antigen which is present in HGBV-infected tamarin liver. Example 13. CKS-based expression and detection of immunogenic HGBV-A and HGBV-B polypeptides A. Cloning of HGBV-A and HGBV-B sequences The cloning vectors pJO200, pJO201, and pJO202 allow the fusion of recombinant proteins to the CMP-KPO synthetase (CKS) protein. Each of these plasmids consists of the plasmid pBR322 with a modified ]ac promoter fused to a kdsB gene fragment (encoding the first 239 of the entire 248 amino acids of the R coli CKS protein), and a synthetic linker fused to the end of the kdsB gene fragment. The synthetic linkers include: multiple restriction sites for insertion of genes, translational stop signals, and the trpA rho-independent transcriptional terminator. The unique restriction sites in this linker region include, from 5' to 3', EcoRI, Sad, Kpnl, Smal, BamHI, Xbal, Pstl, Sphl, and Hindlll. Each plasmid allows for insertion in a different reading frame within the multiple cloning site. The CKS method of protein synthesis as well as CKS vectors are disclosed in U.S. Patent No. 5,124,255, which enjoys common ownership and is incorporated herein by reference, and the use of CKS fusion proteins in assay formats and test kits is described in United States Serial No. 07/903,043, which enjoys common ownership and is incorporated herein by reference. The HGBV-A and HGBV-B sequences obtained from the walking experiments described in TABLES 9 and 10 (Example 9) were liberated from the appropriate pT7Blue T-vector clones using restriction enzymes listed in TABLES 13 and 14 (10 units, NEB), and purified from 1% low melting point agarose gels as described in Example 3B. Plasmids pJO200, pJO201, and pJO202 were digested with the same restriction enzymes (10 units, NEB) and dephosphorylated with bacterial alkaline phosphatase (GLBCO BRL, Grand Island, NY). Each purified HGBV fragment was ligated into the digested, dephosphorylated pJO200, pJO201 , and pJO202 and transformed into E. coli XL 1 Blue as described in Example 3B. Standard miniprep analyses confirmed the successful construction of the CKS/HGBV expression vectors. Two additional PCR products were generated specifically for expression. The 2 products, designated 4.1 and 4.2, were predicted to encode the HGBV-B and HGBV-A core regions, respectively (see FIGURE 22). PCR product 4.1 was generated using primers coreB-s and coreB-al (SEQUENCE LO. NOS- 708 and 709) and PCR product 4.2 was generated using primers coreA-s and 2.2.1' (SEQUENCE LD. NOS. 710 and 138), as described in Example 9. The 4.1 sense and antisense primers had EcoRI and BamHI restriction sites, respectively, designed into the ends. The 4.1 PCR product was digested, gel isolated, and ligated to pJO200, pJO201, and pJO202 as described above. The sense primer for the 4.2 PCR product had an EcoRI restriction site designed into the end, but the antisense primer did not have a restriction site. Thus, the product was cut with EcoRI, gel isolated, and ligated to pJO200, pJO201, and pJO202 which had been digested with BamHI, end-filled with the Klenow fragment of DNA polymerase and dNTPs, digested with EcoRI, and dephosphorylated with bacterial alkaline phosphatase as described in the art. B. Expression of HGBV-A and HGBV-B sequences. E. coli XL1 Blue cultures containing the CKS/HGBV expression vectors were grown at 37°C with shaking in media containing 32 gm/L tryptone, 20 gm/L yeast extract, 5 gm/L NaCl, pH7.4, plus 100 mg/L ampicillin and 3mM glucose. When the cultures reached an OD600 of between 1.0 and 2.0, IPTG was added to a final concentration of lmM to induce expression from the modified iac promoter. Cultures were allowed to grow at 37°C with shaking for an additional 3 hours, and were then harvested. The cell pellets were resuspended to an OD600 of 10 in SDS/PAGE loading buffer (62.5mM Tris pH6.8, 2% SDS, 10% glycerol, 5% 2- mercaptoethanol, and 0.1 mg/ml bromophenol blue), and boiled for 5 minutes. Aliquots of the prepared whole cell lysates were ran on a 10% SDS- polyacrylamide gel, stained in a solution of 0.2% Coomassie blue dye in 40% methanol/10% acetic acid and destained in 16.5% methanol/5% acetic acid until a clear background was obtained. The whole cell lysates were ran on a second 10% SDS-polyacrylamide gel, and electrophoretically transfeπed to nitrocellulose for immunoblotting. The nitrocellulose sheet containing the transferred proteins was incubated in blocking solution (5% Carnation nonfat dry milk in Tris-buffered saline) for 30 minutes at room temperature followed by incubation for 1 hour at room temperature in goat anti-CKS sera which had been preblocked against E. coli cell lysate then diluted 1 : 1000 in blocking solution. The nitrocellulose sheet was washed two times with Tris-buffered saline (TBS), then incubated for 1 hour at room temperature with alkaline phosphatase-conjugated rabbit anti-goat IgG, diluted 1:1000 in blocking solution. The nitrocellulose was washed two times with TBS and the color was developed in TBS containing nitroblue tetrazolium and 5-bromo-4-chloro-3-indolyl phosphate. The appropriate reading frame for each fragment was identified based on expression of an immunoreactive CKS fusion protein of the correct predicted size, and further confirmed by DNA sequencing across the vector-insert junction. After determining the appropriate reading frame for each of the fragments, samples from cultures containing the appropriate constructs were analyzed by SDS-polyacrylamide gel electrophoresis and Western blot. FIGURE 25A shows 2 Coomassie-stained 10% SDS-polyacrylamide gels containing the CKS fusion protein whole cell lysates. Lanes 1 and 16 contain molecular weight standards with the sizes in kilodaltons shown on the left. The loading order on gel 1 (HGBV-A samples) is as follows: lane 2, clone 1.17 prior to induction; lanes 3- 15, clone 4.2, clone 1.17, clone 1.8, clone 1.2, clone 1.18 (SEQUENCE I.D. NO. 390), clone 1.19, clone 1.20, clone 1.21, clone 1.22 (SEQUENCE I.D. NO. 390), clone 2.12, clone 1.5, clone 1.23, and clone 2.18 respectively, all after 3 hours of induction. The loading order on gel 2 (HGBV-B samples) is as follows: lane 17, clone 4.1 prior to induction; lanes 18-29, clone 4.1, clone 1.15, clone 1.14, clone 2.8, clone 1.13, clone 1.12, clone 2.1, clone 1.7, clone 1.3, clone 1.4, clone 1.16, and clone 2.12 respectively, all after 3 hours of induction. These proteins were ran on 2 additional 10% gels, in the same loading order, and transferred to nitrocellulose as described above. The samples were analyzed by Western blot using a pool of sera from 2 convalescent tamarins, T-1048 and T- 1051 , as follows: The nitrocellulose sheets containing the samples were incubated for 30 minutes in blocking solution, followed by transfer to blocking solution containing 10% E. coli lysate, 6mg/ml XLl-Blue/CKS lysate, and a 1:100 dilution of the pooled convalescent tamarin sera described in TABLE 6 (Example 4). After overnight incubation at room temperature, the nitrocellulose sheets were washed two times in TBS and then incubated for 1 hour at room temperature in HRPO- conjugated goat anti-human IgG, diluted 1:500 in blocking solution. The nitrocellulose sheets were washed two times in TBS and the color was developed in TBS containing 2 mg/ml 4-chloro-l-napthol, 0.02% hydrogen peroxide and 17% methanol. As shown in FIGURE 25B, three HGBV-B proteins demonstrated immunoreactivity with the pooled tamarin sera; CKS fusions of clones 1.4, 1.7, and 4.1. Clone 1.7 contains the sequence encoding an HGBV-B immunogenic region (SEQUENCE LO. NO. 610) and clone 1.4 contains the sequence encoding two HGBV-B immunogenic regions (SEQ. LD. NOS. 12, 13 and 18), identified by immunoscreening of a cDNA library (Example 4 ) using the same pool of convalescent tamarin sera. The samples described in the previous paragraph were also analyzed by Western blot as above using a 1 : 100 dilution of convalescent seram obtained approximately three weeks following the onset of acute hepatitis from the surgeon GB. The reactivities of the fusion proteins from HGBV-A and HGBV-B with this serum are indicated in TABLES 13 and 14. Only one HGBV-B protein (2.1) showed reactivity with this seram, and the reactivity was quite weak, while two HGBV-A proteins ( 1.22 [SEQUENCE I.D. NO. 390] and 2.17) exhibited strong reactivity with this seram. These two HGBV-A proteins overlap by 40 amino acids, so this may reflect reactivity with one epitope or more than one epitope. These two HGBV-A proteins were chosen for use in ELISA assays as described in Example 16. It is of interest to note that although tamarins infected with the eleventh passage GB material (H205 GB pass 11) demonstrate an immune response to several HGBV-B epitopes but no HGBV-A epitopes, seram from the original GB source demonstrates significant reactivity with at least one HGBV-A epitope. This suggests that HGBV-A may have been the causative agent of hepatitis in the surgeon GB. Four additional human sera which had indicated the presence of antibodies to one or more of the CKS/HGBV-A or CKS/HGBV-B fusion proteins by the 1.4, 1.7, or 2.17 ELISAS (see Examples 15 and 16) were chosen for Western blot analysis. Three of these sera (Gl-41, Gl-14 and Gl-31) are from the West African "at risk" population and the fourth (341 C) is from a nonA-E hepatitis (Egypt) sample (see Example 15 for detailed description of these populations). Additional 10% SDS-polyacrylamide gels containing the whole cell lysates from some of the CKS fusion proteins discussed above were ran and transferred to nitrocellulose as described previously. Each of these blots was preblocked as described, then incubated overnight with one of the human seram sample diluted 1 : 100 in blocking buffer containing 10% E. coli lysate and 6mg/ml XL1 - Blue/CKS lysate. The blots were washed two times in TBS, then reacted with HRPO-conjugated goat anti-human IgG and developed as indicated above. The CKS/HGBV-B proteins were analyzed with two of these sera, Gl-41 and Gl-14, and the reactivities are indicated in TABLE 13. In addition to the three proteins which showed reactivity with the tamarin sera, two additional proteins (1.16 and 2.1) showed reactivity with one or the other of the two human sera. The CKS/HGBV-A proteins were analyzed with all four of these human sera and the reactivities are indicated in TABLE 14. In addition to the two proteins which showed reactivity with GB serum, three additional proteins (1.5, 1.18, and 1.19) showed reactivity with one or more of the human sera. Two of these ( 1.5 and 1.18) were chosen for use in ELISA assays as described in Example 16_._ It is of particular interest to note that the Gl-31 serum, which shows reactivity by Western blot and/or ELISA (Examples 15 and 16) with two HGBV-A proteins (1.18 and 2.17) and one HGBV-B protein (1.7), is the seram from which the GB-C sequence (SEQUENCE I.D. No. 673, residues 2274-2640) was isolated (Example 17). a PCR product is as indicated in TABLE 9, TABLE 10, or Example 13. b Restriction digests used to liberate the PCR fragment from pT7Blue T- vector or for direct digestion of 4.1 PCR product. Example 14. Epitope mapping of immunoreactive HGBV-A and HGBV-B proteins A. Epitope mapping of HGBV-B protein 1.7 Overlapping subclones within the HGBV-B immunogenic protein 1.7 were generated by RT-PCR from T1053 seram as described in Example 7 in order to determine the location of the immunogenic region or regions. Each PCR primer had six extra bases on the 5' end to facilitate restriction enzyme digestion, followed by either an EcoRI site (sense primers) or a Hindm site (antisense primers). In addition, each antisense primer contained a stop codon just after the coding region. After digestion, each fragment was cloned into EcoRI/Hindπi-digested pJO201 as described in Example 13. The CKS fusion proteins were expressed and analyzed by Western blot with tamarin T1048/T1051 sera as described in Example 13. Five overlapping clones, designated 1.7-1 through 1.7-5, were generated. The clones encoded regions of the 1.7 protein ranging in size from 104 to 110 amino acids. The PCR primers used to generate each clone, the sizes of the encoded polypeptides, the location within the 1.7 sequence and the reactivity with tamarin T1048/T1051 sera are shown in TABLE 15. Two further overlapping clones were generated which encompassed the immunogenic region (SEQUENCE LD. NO. 678) identified by immunoscreening of a cDNA library (Example 4). Each of these clones, designated 1.7-6 and 1.7-7, encoded polypeptides of 75 amino acids. The PCR primers, sizes of encoded polypeptides, location within the 1.7 sequence and reactivity with tamarin T1048/T1051 sera are shown in TABLE 15. Two immunogenic regions were identified within the 507 amino acid long 1.7 protein; one near the N-terminus within residues 1-105, and another near the middle of the protein, encompassing residues 185 to 410. It remains to be determined whether there is a single epitope or multiple epitopes within each of these regions. B. Epitope mapping of HGBV-B protein 1.4 Overlapping subclones within the HGBV-B immunogenic protein 1.4 were generated by RT-PCR from T1053 seram as above in order to determine the location of the immunoreactive region or regions. Each PCR primer had six extra bases on the 5' end to facilitate restriction enzyme digestion, followed by either an EcoRI site (sense primers) or a BamHI site (antisense primers). In addition, each antisense primer contained a stop codon just after the coding region. After digestion, each fragment was cloned into EcoRJ BamHI-digested pJO201 as described in Example 13. The CKS fusion proteins were expressed and analyzed by Western blot with tamarin T1048/T1051 sera as described in Example 13. Four overlapping clones, designated 1.4-1 through 1.4-4, were generated. The clones encoded regions of the 1.4 protein ranging in size from 137 to 138 amino acids. The PCR primers used to generate each clone, the sizes of the encoded polypeptides, the location within the 1.4 sequence and the reactivity with tamarin T1048/T1051 sera are shown in TABLE 15. Two further overlapping clones were generated which encompassed an immunogenic region identified by immunoscreening of a cDNA library (Example 4). Each of these clones, designated 1.4-5 and 1.4-6, encoded polypeptides of 75 amino acids. The PCR primers, sizes of encoded polypeptides, location within the 1.4 sequence and reactivity with tamarin T1048/T1051 sera are shown in TABLE 15. A 265 amino acid sequence was identified as being the immunogenic region within the 522 amino acid long 1.4 protein, encompassing residues 129 to 393. It is likely that there are at least two epitopes within this region, since library immunoscreening (Example 4) identified two immunogenic non-contiguous clones within this sequence. C. Epitope mapping of HGBV-A proteins 1.22 (SEQUENCE LD. NO. 390) and 2.17 The HGBV-A proteins 1.22 (SEQUENCE LD. NO. 390) and 2.17 (SEQUENCE I.D. NO. 613) both showed immunoreactivity with GB serum by Western blot (Example 13). Since these two proteins overlap by 40 amino acids, the observed immunoreactivity may have resulted from the presence of one epitope or more than one epitope. The complete 1.22/2.17 sequence is 641 amino acids long. Overlapping subclones within this region were generated by RT-PCR from T1053 seram as above in order to determine the location of the immunogenic region or regions. Each PCR primer had six extra bases on the 5' end to facilitate restriction enzyme digestion, followed by either an EcoRI site (sense primers) or a BamHI site (antisense primers) for 1.22/2.17-2 through 1.22/2.17-6. However, since clone 1.22/2.17-1 had an internal EcoRI site, a BamHI site was used in the sense primer and a Hindm site was used in the antisense primer. In addition, each antisense primer contained a stop codon just after the coding region. After digestion, each fragment was cloned into EcoRI/BamHI-digested (or BamHLΗindHI-digested for 1.22/2.17-1) pJO201 as described in Example 13. The CKS fusion proteins were expressed and analyzed by Western blot with GB serum as described in Example 13. The clones encoded regions of 1.22/2.17 ranging in size from 115 to 116 amino acids. The PCR primers used to generate each clone, the sizes of the encoded polypeptides, the location within the HGBV-A polypeptide sequence and the reactivity with GB serum are shown in TABLE 15. The immunogenic region was narrowed down to a 220 amino acid long region in the middle of the 1.22/2.17 protein. This encompassed the 40 amino acid region of overlap between 1.22 and 2.17, and thus the immunoreactivity seen with the two proteins individually may have been due to a shared epitope or to multiple epitopes. Example 15. Serological Studies HGBV-B A. Recombinant Protein Purification Protocol Bacterial cell cultures expressing the CKS fusion proteins were frozen and stored at -70°C. The bacterial cells from each of the three constructs were thawed and disrapted by treating with lysozyme and DNAse, followed by sonication in the presence of phenylmethanesulfonyl fluoride and other protease inhibitors to produce mixtures of the individual recombinant antigen and R. coli proteins. Individually for each of the three cultures, the insoluble recombinant antigen was concentrated by centrifugation and subjected to a series of sequential washes to eliminate the majority of non-recombinant E. coli proteins. The washes used in this protocol included distilled water, 5% Triton X-100 and 50 mM Tris (pH 8.5). The resulting pellets were solubilized in the presence of sodium dodecyl sulfate (SDS). After determining protein concentration, 2-mercaptoethanol was added and the mixtures were subjected to gel filtration column chromatography, with Sephacryl S300 resin used to size and separate the various proteins. Fractions were collected and analyzed by SDS-polyacrylamide gel electrophoresis (SDS- PAGE) The electrophoretically separated proteins were then stained with Coomassie Brilliant Blue R250 and examined for the presence of a protein having a molecular weight of approximately 75 kD (CKS-1.7/SEQUENCE I.D. NO. 610), 80 kD (CKS-1.4/SEQUENCE I.D. NO. 611), 42 kD (CKS-4.1/ SEQUENCE I.D. NO. 612). Fractions containing the protein of interest were pooled and re-examined by SDS-PAGE. The immunogenicity and structural integrity of the pooled fractions containing the purified antigen were determined by immunoblot following electrotransfer to nitrocellulose as described in Example 13. In the absence of a qualified positive control, the recombinant proteins were identified by their reactivity with a monoclonal antibody directed against the CKS portion of each fusion protein. When the CKS-1.7 protein (SEQUENCE LD. NO. 610) was examined by Western blot, using the anti-CKS monoclonal antibody to detect the recombinant antigen, a single band at approximately 75 kD was observed. This corresponds to the expected size of the CKS-1.7 protein (SEQUENCE I.D. NO. 610). For the CKS- 1.4 protein (SEQUENCE I.D. NO. 611), the anti-CKS monoclonal antibody detects a quadruplet banding pattern between 60 and 70 kP. These observed bands are smaller than the expected size of the full length protein and probably represent truncation products. When the CKS-4.1 protein (SEQUENCE LP. NO. 52) was examined by Western blot, the anti-CKS monoclonal antibody detected the recombinant antigen as a single band at approximately 42 kP. This corresponds to the expected size of the CKS-4.1 protein (SEQUENCE LP. NO. 612). B. Polystyrene Bead Coating Procedure The proteins were dialyzed and evaluated for their antigenicity on polystyrene coated beads as described below. Separate enzyme-linked immunosorbent assays (ELISA's) were developed for detecting antibodies to HGBV using each of the three purified HGBV recombinant proteins (CKS-1.7 (SEQUENCE LP. NO. 610); CKS- 1.4 (SEQUENCE LP. NO. 611); and the CKS-4.1 protein (SEQUENCE LP. NO. 612). The ELISA's developed with these proteins are refeπed to as the 1.7 ELISA (utilizing the CKS-1.7 (SEQUENCE LP. NO. 610) recombinant protein), the 1.4 ELISA (utilizing the CKS- 1.4 (SEQUENCE P. NO. 611) recombinant protein), the 4.1 ELISA (utilizing the CKS-4.1 [SEQUENCE LP. NO. 612]) recombinant protein. In the first study, one-quarter inch polystyrene beads were coated with various concentrations with each of the purified proteins (approximately 60 beads per lot) and evaluated in an ELISA test (described below) using seram from an uninoculated tamarin as a negative control and convalescent sera from an inoculated tamarin as a positive control. Additional controls included the a pool of human seram from individuals testing negative for various hepatitis virases. An additional positive control consisted of monoclonal antibodies to the CKS protein to monitor the efficiency of bead coating. The bead coating conditions providing the highest ratio of positive control signal to negative control signal were selected for scaling up the bead coating process. For each of the four ELISA's at least two lots of 1,000 beads were produced and utilized for serological studies. Briefly, polystyrene beads were coated with the purified proteins by adding the washed beads to a scintillation vial and immersing the beads (approximately 0.233 ml per bead) in a buffered solution containing the recombinant antigen. Several different concentrations of each of the recombinant antigens were evaluated along with several different buffers prepared at pHs ranging from pH 5.0 to pH 9.5. The vials were then placed on a rotating device in a 40°C incubator for 2 hours after which the fluids were aspirated and the beads were washed three times in phosphate buffered saline (PBS), pH 6.8. The beads were then treated with 0.1% Triton X-100 for 1 hour at 40°C and washed three times in PBS. Next, the beads were overcoated with 5% bovine serum albumin and incubated at 40°C for 1 hour with agitation. After additional washing steps with PBS, the beads were overcoated with 5% sucrose for 20 minutes at room temperature and the fluids were aspirated. Finally, the beads were air dried and then utilized for developing ELISA's for detection of antibodies to HGBV. C. ELISA Protocol for Petection of Antibodies to HGBV An indirect assay format was utilized for the ELISA's. Briefly, sera or plasma was diluted in specimen diluent and reacted with the antigen coated solid phase. After a washing step, the beads were reacted with horseradish-peroxidase (HRPO) labeled antibodies directed against human immunoglobulins to detect tamarin or human antibodies bound to the solid phase. Specimens which produced signals above a cutoff value were considered reactive. Additional details pertaining to the ELISA's are described below. The format for the ELISA's entails contacting the antigen-coated solid phase with tamarin serum pre-diluted in specimen diluent (buffered solution containing animal sera and non-ionic detergents). This specimen diluent was formulated to reduce background signals obtained from non-specific binding of immunoglobulins to the solid phase while enhancing the binding of specific antibodies to the antigen-coated solid phase. Specifically, 10 μl of tamarin serum was diluted in 150 μl of specimen diluent and vortexed. Ten microliters of this pre-diluted specimen was then added to the well of a reaction tray, followed by the addition of 200 μl of specimen diluent and an antigen coated polystyrene bead. The reaction tray was then incubated in a Pynamic Incubator (Abbott Laboratories) set for constant agitation at room temperature. After a 1 hour incubation, the fluids were aspirated, and the wells containing the beads were washed three times in distilled water (5 ml per wash). Next, 200 μl of HRPO-labeled goat anti-human immunoglobulins diluted in a conjugate diluent (buffered solution containing animal sera and non-ionic detergents) was added to each well and the reaction tray was incubated again as above for 1 hour. The fluids were aspirated and the wells containing the beads were washed three times in distilled water as above. The beads containing antigen and bound immunoglobulins were removed from the wells, each was placed in a test tube and reacted with 300 μL of a solution of 0.3% o-phenylenediamine-2 HCI in 0.1 M citrate buffer (pH 5.5) with 0.02% H2O2. After 30 minutes at room temperature, the reaction was terminated by the addition of 1 N H2SO4 . The absorbance at 492 nm was read on a spectrophotometer. The color produced was directly proportional to the amount of antibody present in the test sample. For each group of specimens, a preliminary cutoff value was set to separate those specimens which presumably contain antibodies to the HGBV epitope from those which did not. P. Petection of HGBV derived RNA in Seram from Infected Individuals. In order to correlate serological data obtained for 1.7 and 1.4 ELISA's with the presence of HGBV RNA in tamarin seram or in human serum/plasma, RT- PCR was performed as described in Example 7 of U.S. Serial No. 08/283,314, previously incorporated herein by reference utilizing oligonucleotides derived from HGBV cloned sequences, at a final concentration of 0.5 μM for clone 4 (as described in Example 7) derived from the HGBV-B genome and for clone 16, derived from the HGBV-A genome. E. Tamarin Serological Profiles. Seram was obtained from tamarins housed at LEMSIP on a weekly basis and tested for liver enzyme levels; the remaining volume from these specimens was sent to Abbott Laboratories for further studies. 1. ELISA Results on Tamarins (Initial Infectivity Studies) Four tamarins (T-1053, T-1048, T-1057 and T-1061) were inoculated with GB seram (designated as H205 GB passage 11). Elevated liver enzymes were noted in Tamarin T-1053 during the first week post-inoculation (PI): this tamarin was euthanized on day 12 PI. Tamarins T-1048, T-1057 and T-1061 exhibited elevated liver enzyme values within two weeks following their inoculation; these elevated values persisted until 8-9 weeks PI (FIGURES 2-4) before returning to pre-inoculation levels. On week 14 PI, these three tamarins were re-challenged with 0.10 ml of neat seram obtained from tamarin T-1053 (which was shown to be infectious - Example 2). Sera from three convalescing tamarins (T-1048, T-1057 and T-1061) were tested for antibodies to the CKS-1.7 (SEQUENCE LP. NO. 610) recombinant protein, the CKS- 1.4 (SEQUENCE LP. NO. 611 ) recombinant protein, and the CKS 4.1 (SEQUENCE LP. NO. 612) recombinant protein, using separate ELISA's (FIGURES 3, 4 and 5). Specific antibodies to 1.7 (SEQUENCE LP. NO. 610), 1.4 (SEQUENCE LP. NO. 61 1), 4.1 (SEQUENCE LP. NO. 612, or 1.5 (SEQUENCE LP. N0.614) recombinant proteins were not detected in any of the pre-inoculation specimens. As shown in FIGURE 26, specific antibodies were detected in T-1048 sera with the 1.7 and 1.4 ELISA's on days 56-84 but not on days 97 and 137 PI. Specific antibodies were not detected in T-1048 sera tested with the 4.1 ELISA. As shown in FIGURE 27, antibodies to the 1.7 protein (SEQUENCE LP. NO. 610) were detected in T-1057 seram at 56 and 63 days PI, but not after 63 days PI. Antibodies to the 4.1 protein (SEQUENCE LP. N0.612) were detected on days 28-63 PI but not on days 84-97 PI. As noted above, tamarins were challenged with a second dose of the H205 inoculum on day 97 PI. Specific antibodies to the 4.1 protein (SEQUENCE LP. NO. 612) were detected on days 112 and 126 PI, suggesting an anamnestic response to the inoculum. No antibody reactivity was noted for the 1.4 recombinant protein (SEQUENCE LP. NO. 611). Specific antibodies to the recombinant 1.4 protein (SEQUENCE LP. NO. 611) were detected in the seram of tamarin T-1061 between 84 and 112 days PI, but were not detected after 126 days PI. As shown in FIGURE 28, Tamarin T- 1061 sera were negative for antibodies to the 1.7 protein (SEQUENCE LP. NO. 610) and to the 4.1 protein (SEQUENCE LP. NO. 612) for 350 days PI. 2. PCR Results on Tamarins (Initial Infectivity Studies) Selected sera obtained from tamarins T-1048 and T-1057 were tested for HGBV RNA via RT-PCR using primers from clone 4 as described in Example 7) and from clone 16 as described in Example 7. HGBV RNA was not detected via RT-PCR with either set of primers in the seram obtained 10 and 17 days prior to inoculation (T-1048) as shown in FIGURE 26, or 17, 37 and 59 days prior to inoculation (T-1057), as shown in FIGURE 27. For T-1048, HGBV RNA was detected via RT-PCR using primers from clone 4 on fifteen of seventeen different sera obtained between 7-137 days PI. HGBV RNA was not detected via RT-PCR using primers from clone 16 in any of the 10 sera obtained on days 7-97 PI. After the challenge with T-1053 plasma, four of five sera obtained between 8 and 40 days after the challenge were positive for clone 16. For T-1057, positive RT-PCR results were obtained on four sera obtained on days 7-28 PI, using primers from clone 4 , as shown in FIGURE 27. RT-PCR performed on specimens drawn beyond day 28 PI were negative for clone 4, except for day 287 which showed a weak hybridization signal. Neither of the six specimens obtained from T-1057 on day 7-97 PI were positive via RT-PCR using primers from clone 16. However, sera obtained between 8-85 days after the T-1053 challenge were positive using primers from clone 16. 3. ELISA Results on Tamarins (Titration/Transmissibilty Studies) As described in Example 2, serum from tamarin T-1053 was inoculated into four tamarins. Three of these four tamarins were euthanized during the acute stage of the disease (between days 12 and 14 PI). The RT-PCR results obtained on these three tamarins are described below. The surviving tamarin (T-1051) first developed elevated liver enzyme values by day 14 PI and these values persisted for at least 8 weeks PI. Specimens from tamarin T-1051 were tested in the 1.7 and 1.4 ELISA's; the results are shown in FIGURE 29. Specific antibodies were not detected in the pre-inoculation serum nor in serum drawn in the first 41 days PI. However, an antibody response was noted against the 1.4 protein (SEQUENCE LP. NO. 611), and the 1.7 protein (SEQUENCE LP. NO. 610) between 49 and 113 days PI and the 4.1 protein (SEQUENCE LP. NO. 612) between 28 and 105 days PL The tamarin was euthanized during the 113th day PI. Tamarin (T-1034) was previously inoculated with 0.1 ml of potentially infectious seram obtained from a patient (original GB source) who was recovering from a recent hepatitis infection as described in Example 1 and in TABLE 4. No elevations in liver enzyme values were noted in T-1034 for nearly 10 weeks after inoculation. For this reason, it was decided that tamarin T-1034 could be used in an additional study. Tamarin T-1034 was inoculated with a preparation of HGBV prepared as described in Example 4 ?? from a pool of seram obtained from three tamarins (T-1055, T-1038 and T-1049) previously inoculated with seram from tamarin T-1053. These three tamarins (T-1055, T-1038 and T-1049) were inoculated with seram prepared from tamarin T-1053 as described in Example 2. Elevated liver enzyme values were noted in all 3 tamarins by day 11 PI. Tamarin T-1055 was sacrificed on day 12 PI: tamarins T-1038 and T-1049 were sacrificed on day 14 PI. Serum from these tamarins was pooled, clarified and filtered. Tamarin T- 1034 was inoculated with 0.25 ml of a 10 "6 dilution (prepared in normal tamarin seram) of this filtered material. Elevated ALT liver enzyme values were first noted in T-1034 at 2 weeks PI, and remained elevated for the next 7 weeks, finally normalizing by week 10 PI. As demonstrated in FIGURE 30, a specific antibody response to the 1.4 (SEQUENCE LP. NO. 22) recombinant protein was first detected on day 49 PI and continued to be detected on days 56-118 PI. The antibody response to the 4.1 (SEQUENCE LP. NO. 52) recombinant protein was first detected on day 49 PI and continued to be detected between days 56-77 PI, but was not detected on between days 84-118 PI. The antibody response to the 1.7 (SEQUENCE LP. NO. 610) recombinant protein was first detected on day 56 PI and continued to be detected between days 63-118 PI. The tamarin was sacrificed on day 118 PI. As described in Example 2, tamarin T-1044 was inoculated with serum obtained from T-1057 that had been obtained 7 days after the H205 inoculation. This inoculum was positive only for sequences detected with clone 4 primers . The inoculum was negative by RT-PCR with clone 16 primers . Mild elevations in ALT levels above the cutoff were observed from days 14-63 PL As demonstrated previously, a specific antibody response to the 1.7 (SEQUENCE I.P-NO. 610) recombinant protein was detected between 63-84 days PI. No antibody response to the 4.1 (SEQUENCE LO. NO. 612) recombinant protein or to the 1.4 (SEQUENCE LO. NO. 611) recombinant protein was detected. The tamarin was sacrificed on 161 days PI. 4. PCR Results on Tamarins (Titration Transmissibilty Studies) Sera obtained from T-1049 and T-1055 during the 8th week prior to inoculation and T-1038 on the day of inoculation, were negative by RT-PCR for sequences to clone 16 (SEQUENCE LD. NO. 26) and clone 4 (SEQUENCE I.D. NO. 21). Tamarins T-1049 and T-1055 were positive for clone 4 sequences (SEQUENCE LD. NO. 21) by RT-PCR 1 week after inoculation (clone 16 PCR was not done). Prior to the day of sacrifice, T-1049 (14 days PI) as well as T- 1055 (11 days PI) were positive by RT-PCR for both clone 4 (SEQUENCE I.D. NO. 21) and clone 16 sequences (SEQUENCE I.D. NO. 26). Tamarin T-1038 was positive with both sets of primers on the day of sacrifice (14 days PI). As seen in FIGURE 30, T-1034 was positive by RT-PCR for sequences detected with clone 4 primers on the first serum sample obtained after inoculation (7 days PI) and remained positive to day 70 PI. A sample obtained on day 1 12 PI was negative. All of these samples were negative by RT-PCR with clone 16 primers. Samples obtained 70 and 101 days prior to inoculation were negative with both sets of primers. As can be seen in FIGURE 29 for tamarin T- 1051 , HGBV RNA was not detected with either set of primers (from clones 4 and 16 as described above) in the seram specimen obtained 8 weeks prior to inoculation. HGBV RNA was detected by RT-PCR using primers from clone 4 on six sera obtained between days 7-69 PI, but not on days 77, 84, 91, or 105 PI. HGBV RNA was detected by RT-PCR using primers from clone 16 on nine samples obtained after inoculation. As seen in FIGURE 7, T-1044 was positive by RT-PCR for sequences detected with clone 4 primers on the first seram sample obtained after inoculation (7 days PI) and remained positive to day 63 PI. Samples obtained between days 77-119 were negative. All of these samples were negative by RT-PCR with clone 16 primers. A sample obtained 42 days prior to inoculation was negative for both sets of primers. Tamarins T-1047 and T-1056 were inoculated with T-1044 serum obtained 14 days PI. Nine samples obtained between 7- 64 days PI from both of these animals were positive by RT-PCR with clone 4 primers (SEQUENCE I.D. NOS. 8 and 9) but negative with clone 16 primers . Tamarin T-1058 was inoculated with neat T-1057 seram obtained 22 days after the challenge with T-1053 seram. This inoculum was positive for sequences detected with clone 16 primers but negative with clone 4 primers. Serum samples obtained from this animal were tested with primers derived from GBV- sequences [clone 16 , clone 2 clone 10 and clone 18)] and GB-B sequences [clone 4 and clone 50]. A sample obtained 9 days prior to inoculation was negative with all primer sets. A sample obtained 14 days PI was positive only with clone 10 and 18 primers. A sample obtained 21 days PI was positive only with clone 16 , 10 and 18 primers. A sample obtained 28 days PI was positive only with clone 18 primers. A sample obtained 35 days PI was positive only with clone 2, 16 ( and 18 primers. A sample obtained 41 days PI was positive only with clone 16 and 18 primers. All samples tested were negative with primers from clone 4 and clone 50 5. Summary of Serological Studies in Tamarins Five tamarins were inoculated with various preparations of HGBV and developed elevated liver enzyme values by two weeks PI. These elevations persisted for the next six to eight weeks. A specific antibody response to one or more HGBV recombinant antigens, 1.7, 1.4, and 4.1 was noted in all five tamarins. In all cases, the antibodies were first detected by six to ten weeks PI, and persisted for two to seven or more weeks. In general, the antibody levels peaked and then declined rapidly over the next several weeks. It is observed that the antibodies become detectable shortly after the liver enzyme values returned to normal levels, suggesting that the generation of antibodies may play a role in clearing the viral infection. 6. Summary of PCR Studies on Tamarins The results of the genomic walking experiments suggest that clone 4 (SEQUENCE LD. NO.21) and clone 16 (SEQUENCE I.D. NO. 26) reside on separate RNA molecules. We previously provided arguments that supported the idea that there are two distinct viral genomes, one comprised partly of clone 4 (SEQUENCE LD. NO.21) and one comprised partly of clone 16 (SEQUENCE I.D. NO. 26). The observation that some animals are positive with primers from clone 4 and not with primers from clone 16 supported the existence of two distinct viral genomes. However, it can also be argued that the inability to detect clone 16 (SEQUENCE I.D. NO. 26) sequence in some of the infected tamarins may reflect a lower limit of sensitivity of the clone 16 primer set relative to the clone 4 primer set. If this latter possibility was the case, then a tamarin positive for both primer sets should exhibit a difference in sensitivity with these two primer sets. In order to support the explanation that these results are explained by the existence of two separate virases, and not differences in sensitivities of these two primer sets, PCR was performed on a dilution series of cDNA from tamarins T-1057 and T1053. T- 1057 seram was positive at 5 X 10 "3 but negative at 5 X 10' 4 ul serum equivalents with clone 4 primers. As much as 20 ul of T-1057 seram was used for RT-PCR with clone 16 primers with negative results. If this difference was due to the relative sensitivity of the two primer sets (clone 4 vs. clone 16), one would expect that other specimens would also show a 4000 fold higher endpoint dilution when tested by PCR. However, cDNA derived from T-1053 seram was found to be positive at 2.5 X 10 ~ 4 but negative at 2.5 X 10 ~ 5 ul seram equivalents for both clone 4 (SEQUENCE I.D. NO.21) and clone 16 (SEQUENCE I.D. NO. 26) sequences. These observations are therefore not consistent with a difference in sensitivity of primer sets but are consistent with the existence of contig B-clone 4 (SEQUENCE LD. NO.21) and contig A-clone 16 (SEQUENCE LP. NO. 26) sequences on separate viral genomes of roughly equal titer in T-1053 but differing in titer by at least 4000 fold in T-1057. This data is therefore consistent with the existence of two separate virases which may have different relative endpoint titers in different specimens. The observation that HGBV-B viremia alone was sufficient to cause elevations in liver enzyme levels and that no elevations were observed during a GBV-A-only viremic stage, indicated that HGBV-B was the probable causative agent for hepatitis in these tamarins. The immune response to the HGBV-B antigens appeared to be for a short duration, at most 150 days PI. One explanation could be that the selection of epitopes used in these ELISAs was not from the dominant epitopes to which the immune response is generated. Another explanation could be that in tamarins the hepatic challenge may not be significant enough to necessitate a long-lived response. This is consistent with histological evidence from animals that were sacrificed during the acute phase of the disease or had died of natural causes some time after the acute phase which showed that hepatic inflammation ranged from mild to not significant (results not shown). Five of six animals described in this study resolved viremia of HGBV-B by 112 days PI. In contrast, Tamarin T-1048 remained viremic for 136 days and was found to be viremic at the time of death (137 days PI). Of the four animals that were positive for GBV-A sequence, three showed resolution by 77 days after the first appearance of GBV-A sequence. In contrast, tamarin T-1061 was viremic for 245 days up to the time the animal was sacrificed. In addition, tamarin T-1051 was viremic up to the time of sacrifice (day 113 PI), however, it is unclear if this persistent viremia is due to the initial inoculation with T-1053 plasma or a result of the subsequent challenge with additional T-1053 plasma 69 days later. The average peak ALT value for the six animals positive for both HGBV-A and HGBV-B was higher than the average value for the four HGBV-B-only animals. In addition, the peak value occurred, on average, earlier in animals positive for GBV-A and GBV-B than for animals positive only for GBV-B. These results suggest that the intensity of the hepatitis may be related to the presence of both agents at significant levels. The observation from the additional passage of GBV-B into tamarins T-1047 and T-1056 that minimal elevation in liver enzymes occurred with GBV-B viremia supports this assumption that both agents may be necessary for major elevations in ALT levels to occur in tamarins. In addition to the passage of HGBV-B alone, initial results from the inoculation of T-1058 with HGBV-A inoculum suggest thatH GBV-A can be transmitted independent of any detectable HGBV-B as indicated by the absence of any detectable GB-B sequences with clone 4 and clone 50 primers. F. Experimental Protocol.for demonstrating exposure to HGBV in human populations Specimens were obtained from various human populations and tested for antibodies to HGBV utilizing three separate ELISA's utilizing recombinant proteins derived from HGBV-B. The 1.7 ELISA utilized the CKS-1.7 recombinant protein (SEQUENCE LP. NO.610) coated onto the solid phase; the 1.4 ELISA utilized the CKS- 1.4 recombinant proteins (SEQUENCE LP. NO.61 1) coated on the solid phase and the 4.1 ELISA utilized the 4.1 recombinant protein (SEQUENCE LP. NO.612) coated on the solid phase as described in Example 15.B. As also noted in Example 15.E, tamarins inoculated with HGBV produce a specific, but short-lived antibody response to these proteins. In view of the transient nature of this detectable immune response, a negative result in human populations would not necessarily exclude previous exposure to HGBV. The objective of the serological studies conducted with human specimens was two-fold. First, the seroprevalence of antibodies to the current HGBV recombinant antigens in various human populations was to be determined. These studies included testing (1) populations considered at "low risk" for exposure to HGBV (e.g. healthy volunteer blood donors in U.S.); (2) populations considered to be "at risk" for exposure to HGBV (e.g. specimens obtained from intravenous drug users and hemophiliacs are frequently seropositive for parenterally transmitted hepatitis virases (HBV and HCV); specimens obtained from individuals residing in developing nations are frequently seropositive for enterically transmitted viruses (HAV and HEV); (3) panels of specimens obtained from individuals with "non-A-E hepatitis" that is not associated with exposure to known hepatitis virases (HAV, HBV, HCV, HPV or HEV) or to other viruses associated with hepatitis such as cytomegalovirus (CMV) or Epstein-Barr Viras (EB V). In some cases, members of the panels under the general heading of non A-E hepatitis were not tested for antibodies to HEV. Therefore, all specimens in the non A-E group which were reactive with the 1.7, 1.4 or 4.1 ELISA's were retested with an HEV ELISA assay (available from Abbott Laboratories, Abbott Park, LL). Positive anti-HEV results were noted with samples from three sites (Pakistan, U.S. and New Zealand), as explained hereinbelow. One would expect to observe higher seroprevalence rates among populations "at risk" for exposure to HGBN and among individuals with non-A-E hepatitis, than among populations considered to be at "low risk" for exposure to HGBN. The second objective of the serological studies was to examine specimens found to be positive for antibodies to one or more HGBV epitopes by RT-PCR to determine if the virus is present in seram. It is well known that HBV and HCV can establish a viremic state which persists for months or years, and in general, that HAV and HEV establish a short-lived viremia persisting in general for several weeks. In cases of HBV and HCV infection which are acute, resolving hepatitis, the viremic stage may also be short-lived persisting for several weeks. Thus, RT- PCR can be used to provide evidence that the viras is present in an infected individual. However, because the viremic state can be short-lived, a negative RT- PCR result for a given agent can be observed in individuals who are infected with that agent. G. Cutoff Determination Previous experience with other ELISA's utilizing the indirect assay format indicated that a preliminary cutoff value can be calculated based on the absorbance values obtained on a population presumably negative for antibodies to the protein being studied. A preliminary cutoff value was calculated as the sum of the mean absorbance value of the population plus 10 standard deviations from the population mean. Since the cutoff value was to be used every time a panel was ran, a more convenient method to express the cutoff was as a factor of the negative control (pool of normal human plasma - ΝHP) which was run in replicates of five for each assay run. For the 1.7, 1.4 and 4.1 ELISA's, the negative control typically had an absorbance value of between 0.030 and 0.060. As described below, the cutoff values were calculated to be at an absorbance value of approximately 0.300 to 0.600, which was equivalent to an absorbance signal of ten times the negative control value. Thus, in order for a specimen to be considered reactive, the ratio of the sample (S) absorbance value to the negative (N) control absorbance value (S/N ratio) had to be equal to or greater than 10.0. H. Supplemental Testing Specimens which were initially reactive were typically retested in duplicate. If one or both of the retest absorbance values were above the cutoff value, the specimen was considered repeatably reactive. Specimens which were repeatably reactive were then tested with supplemental assays which may further support the ELISA data. Repeatably reactive specimens which had sufficient volume may be tested by Western blot to determine that the antibody response was directed against the CKS-1.7 (SEQUENCE I.D. NO. 610), a CKS-1.4 (SEQUENCE I.D. NO. 611) or CKS 4.1 (SEQUENCE I.D. NO. 612) antigens and not to E. coJLproteins which may have been co-coated on the solid phase with the major protein of interest. For a Western blot result to be considered positive, a visible band had to be detected at 80kD for the 1.7 protein (SEQUENCE I.D. NO. 610), 60-70 kD for the 1.4 protein (SEQUENCE I.D. NO. 611 ) or at 42 kD for the 4.1 protein (SEQUENCE I.D. NO. 612). Since the Western blot has not been optimized to match or exceed the sensitivity of the ELISA's, a negative result was not used to discard the ELISA data. However, a positive result reinforced the reactivity detected by the ELISA's. Repeatably reactive specimens which had sufficient volume may be tested by RT-PCR (performed as described in Example 15.D using clone 4 primers to identify HGBV specific nucleotide sequences in seram. A positive result would indicate a viremic specimen and would ultimately help in establishing the role of HGBV in human hepatitis. A negative result, however, was not to be construed to indicate that the ELISA results was incorrect. As noted in the tamarin study in Example 15.E, RT-PCR results were positive in the first several weeks after infection and then became negative at about the time when antibodies were just beginning to be detected with the current ELISA's. These later specimens may be RT-PCR negative but positive in one or both of the ELISA's. I. Serological Data Obtained with Low-Risk Specimens A population consisting of 100 sera and 100 plasma was obtained from healthy, volunteer blood donors in Southeastern Wisconsin and tested for antibodies to the 1.7 (SEQUENCE I.D. NO. 610) and 1.4 (SEQUENCE I.D. NO. 61 1) and 4.1 (SEQUENCE I.D. NO. 612) recombinant proteins utilizing the ELISA's described above. The absorbance values obtained with the 1.7, 1.4 and 4.1 ELISA's for serum and plasma were plotted separately (FIGURES 9-14). For the 1.7 ELISA, the mean absorbance values for the serum and plasma specimens were 0.072 [with a standard deviation (SD) of 0.061] and 0.083 (SD=0.055), respectively. Thus, for the 1.7 ELISA's, the tentative cutoff values for seram and plasma were 0.499 and 0.468, respectively. As discussed above, the cutoff also was expressed as a factor of the negative control absorbance valuei specimens having S/N values above 10.0 were considered reactive. Using this cutoff value, 0 of 200 specimens tested for antibodies to 1.7 (SEQUENCE I.D. NO. 610). For the 1.4 ELISA, several specimens (three from the seram population and six from the plasma population) had absorbance values greater than 0.300 (S/N's of 6-12, near or above the expected cutoff value). When retested, all nine of these specimens produced S/N values of less than 10.0. The mean absorbance value for the seram and plasma specimens were 0.072 (SD=0.052) and 0.108 (SD=0.062), respectively. The cutoff for the 1.4 ELISA was calculated using the formula described above; the cutoff values for seram and plasma populations were 0.436 and 0.542, respectively. One specimen from the seram population was initially reactive and when re-tested in duplicate was negative. Two specimens from the plasma population were initially reactive but were negative upon re-test. A second population of 200 normals was tested including 100 plasma and 100 seram. Using the proposed cutoff, two plasma and two sera were repeatably reactive. For the 4.1 ELISA, the mean absorbance values for the seram and plasma specimens were 0.070 [with a standard deviation (SD) of 0.037] and 0.063 (SD=0.040), respectively. Thus, for the 4.1 ELISA, the tentative cutoff values for seram and plasma were 0.329 and 0.511, respectively. As discussed above, the cutoff also was expressed as a factor of the negative control absorbance value; specimens having S/N values above 10.0 were considered reactive. Using this cutoff value, 0 of 100 plasma specimens and 0 of 100 serum specimens were initially reactive for antibodies to 4.1 (SEQUENCE I.D. N0.612). An additional 760 plasma donors from the Interstate Blood Bank (Ohio) were tested with the 1.7 and 1.4 ELISAs. A total of 9 specimens were repeatably reactive. None of the specimens were reactive in both ELISAs. All 9 specimens were repeatably reactive with the 1.4 ELISA. In total, 960 specimens from plasma or blood donors residing in the U.S. were tested for antibodies to the 1.7 and 1.4 proteins. A total of 13 specimens were repeatably reactive by the 1.4 ELISA. None of the specimens were repeataby reactive with the 1.7 ELISA. In summary, these data indicate that, with the existing ELISA's, a total of 13 of 960 specimens obtained from U.S. blood donors were reactive for antibodies in one or more of the ELISA's employing recombinant antigens from HGBV-B. These data suggest that HGBV may be endemic in the U.S. These data are summarized in TABLE 16. J. Specimens Considered "At Risk" for Hepatitis The data for these studies is summarized in TABLE 16. (i) Specimens from West Africa A total of 181 of 1300 specimens obtained from West Africa were repeatably reactive in one or more of the ELISA's. One specimen was repeatably reactive in all 3 ELISA's. A total of 43 specimens were repeatably reactive with the 1.7 ELISA, 91 specimens were repeatably reactive with the 1.4 ELISA and 51 specimens were repeatably reactive in the 4.1 ELISA. One of six specimens repeatably reactive in the 1.7 ELISA was reactive by Western blot for the 1.7 protein (SEQUENCE I.D. NO.610). Nine of 9 specimens (100%) which were repeatably reactive in the 1.4 ELISA were positive by Western blot for antibodies to the 1.4 protein (SEQUENCE I.D. NO. 611). One specimen was positive by Western blot for both proteins. Twelve of 12 specimens (100%) repeatably reactive in the 4.1 ELISA were positive by Western blot for the 4.1 protein (SEQUENCE I.D. NO.612. Three repeatably reactive specimens (including one specimen positive in the 1.4 ELISA and one specimen positive in both ELISA's and both Western blots) were tested for HGBV RNA by RT-PCR using primers from clone 4 as described above. All three specimens were negative by RT-PCR. These data suggest that HGBV may be endemic in West Africa, (ii) Specimens from Intravenous Drag Users (LVDU's) Set 1 : Three of 112 specimens were positive with the 1.4 ELISA. Five specimens were reactive on 4.1 ELISA and three on 1.7 ELISA. Two samples were positive on more than one ELISA. Set 2: A total of 99 specimens were obtained from a population of intravenous drug users, as part of a study being conducted at Hines Veteran's Administration Hospital, in Chicago, LL. None of these specimens were reactive in the 1.7 or 4.1 ELISA. One specimen was repeatably reactive in the 1.4 ELISA. This repeatably reactive specimen was tested for HGBV RNA by RT-PCR using primers from clone 4 as described above. This specimen was RT-PCR negative. K. Specimens obtained from individuals with non A-E Hepatitis The data for these studies is summarized in TABLE 16. Various populations of specimens were obtained from individuals diagnosed as having non-A-E hepatitis and tested with the 1.7, 1.4, and 4.1 ELISA's described in Example 15.C. These specimens included: 180 specimens obtained from a Japanese clinic; 56 specimens from a clinic in New Zealand; 73 specimens obtained from a clinic in Greece; 132 specimens from a clinic in Egypt; 64 specimens from a U.S. clinic in Texas (set T), 72 specimens from a research center in Minesota (set M); 62 specimens from U.S. (set #1); 82 specimens obtained from a clinic in Pakistan; 10 specimens from a clinic in Italy. (Due to insufficient volumes of some sera, certain specimens from these groups were not tested on all of the available ELISAs). (i) Specimens from Japan These 180 specimens were obtained from 85 different patients. These two reactive specimens came from 2 individuals. A total of 2 of 180 specimens were repeatably reactive in the 1.7 ELISA. These 2 specimens were tested by RT-PCR using primers from clone 4 as described above. None of the specimens were positive. None of the specimens were positive in the 1.4 ELISA. For the 4.1 ELISA, seven of 89 specimens were repeatably reactive in the 4.1 assay. (Note: these 89 specimens were obtained from 29 different patients). Five of the reactive specimens were obtained from one patient. The remaining two were from a different patient. (ii) Specimens from New Zealand A total four of 56 specimens were repeatably reactive in one or more of the ELISA's 1.7, 1.4, and 4.1. None of these specimens were reactive in two or more ELISA's. One specimen was repeatably reactive in the 1.7 ELISA and two specimens were repeatably reactive in the 1.4 ELISA. One specimen was repeatably reactive with the 4.1 ELISA. PCR was performed on two repeatably reactive specimens; both specimens were negative. One specimen which was repeatably reactive in the 1.4 ELISA was also reactive for antibodies to HEV. (iii) Specimens from Greece A total of 5 of 73 specimens were found to be reactive for antibodies in the 1.7 and/or 1.4 ELISA's. These 73 specimens were obtained from a total of 11 patients. Two of the five repeatably reactive specimens were repeatably reactive for both ELISA's and were obtained from one individual on different dates. Two repeatably reactive specimens were tested by RT-PCR and were negative. None of these specimens were reactive for antibodies with the 4.1 ELISA. (iv) Specimens from Egypt A total of 11 of 132 specimens were reactive in the 1.7, 1.4, or 4.1 ELISA's. Eight specimens were positive in both the 1.7 and 1.4 ELISA's. Nine specimens were reactive for antibodies in the 1.7 ELISA and 9 specimens were reactive in the 1.4 ELISA. One specimen repeatably reactive in the 4.1 ELISA but negative in the 1.7 and 1.4 ELISAs. One specimen repeatably reactive in the 1.7 ELISA was tested by Western blot and was negative for antibodies to the 1.7 recombinant protein (SEQUENCE I.D. NO. 610). Six of nine specimens repeatably reactive in the 1.4 ELISA tested positive by Western blot for antibodies to the 1.4 recombinant protein (SEQUENCE I.D. NO. 611). Seven of the repeatably reactive specimens were tested by RT-PCR; none of the specimens were reactive. These 132 specimens were obtained on different dates from 25 different individuals. The 11 repeatably reactive specimens were obtained from five different individuals. For one of these individuals (patient #101), the immune response clearly mimics that observed with the tamarins (FIGURE 31). Note that in FIGURE 31 , the ALT levels were elevated at the time of presentation of symptoms to the physician. In subsequent specimens, the ALT levels declined and antibodies were detected utilizing the 1.4 and 1.7 ELISA's. The antibody response declined over the next several weeks as was noted with the serologic profiles observed in the tamarins. Three additional patients (257, 260, and 340) exhibited serologic patterns similiar to patient #101 (as shown in FIGURES 32- 34. These data provide supportive evidence that HGBV may be the etiologic agent in these cases of hepatitis. None of the seven specimens obtained from these four patients were positive for HGBV RNA by RT-PCR. There are several potential reasons for these results. First, the viremic phase may have been very short-lived: the virus may have been cleared from the seram by the time of the first bleed date. Secondly, these specimens were shipped from Egypt and may potentially have been frozen and thawed or otherwise compromised during the storage and shipping process, thus reducing the potential to detect HGBV RNA. (v) Specimens from U.S. (Set T) None of 64 specimens from the U.S. (set T) were repeatably reactive in the 1.7, 1.4 or 4.1 ELISA. (vi) Specimens from U.S. (Set M) A total of 4 of 72 specimens from U.S. specimens (set M) were repeatably reactive in one or more of the ELISA's. Two specimens were reactive with the 1.7 and 4.1 ELISA's. One specimen was reactive only with 1.7 and one specimen was reactive only with the 4.1 ELISA. vii) Specimens from the United States (set 1 ) A total of three of 51 specimens from non A-E hepatitis U.S. set 1 were repeatably reactive in one or both of the ELISA's. One specimen was repeatably reactive in both ELISA's. One specimen was reactive in the 1.7 ELISA and three specimens were repeatably reactive in the 1.4 ELISA. The specimen positive in both ELISA's was positive by Western blot for the 1.4 recombinant protein (SEQUENCE LD. NO. 22) but negative for the 1.7 recombinant protein (SEQUENCE LD. NO. 23). One additional specimen was positive in the 1.4 ELISA and Western blot positive for the 1.4 recombinant protein (SEQUENCE I.D. NO.611). One specimen which was repeatably reactive in the 1.4 ELISA was reactive for antibodies to HEV. (viii) Specimens from Pakistan A total of four of 82 specimens were repeatably reactive for antibodies in 1.4 and/or 1.7 ELISAs. None of the specimens were reactive in both ELISA's. Two specimens were repeatably reactive in the 1.7 ELISA and two specimens were repeatably reactive in the 1.4 ELISA. Two specimens repeatably reactive in the 1.4 ELISA were also reactive for antibodies to HEV. None of these 82 specimens were positive with the 4.1 ELISA. (ix) Specimens from Italy None of the ten specimens were repeatably reactive in the 1.7, 1.4, or 4.1 ELISA. L. Statistical Significance of Serological Results These data indicate that specific antibodies to HGBV proteins ( i.e. specimens repeatably reactive for antibodies in 1.7, 1.4, or 4.1 ELISA's can be detected in all three categories of populations studied. Serological results obtained with the various categories of specimens ("low risk", "at risk" and non A-E hepatitis patients) were grouped together and analyzed for statistical significance using the Chi square test. The data indicated that there is a significant difference in comparing the seroprevalence of anti-HGBV in volunteer blood donors with either the individuals considered "at risk" for exposure to HGBV or to individuals diagnosed with hepatitis of an unknown etiology. Among West Africans, the seroprevalence rate is 13.9% and is significantly higher than the baseline group (TABLE 17) with a p value of 0.000. Similiarly, for the LVDU's, there was a statistically significant difference (p value of 0.000) when the results from LVDU's were compared with volunteer donors. In countries (including Japan, New Zealand, U.S., Egypt, and Pakistan), there were significant differences in antibody prevalence in patients with non A-E hepatitis when compared to the volunteer blood donors from the US. H. Summary These data suggest that the ELISA's described herein may be useful in diagnosing cases of hepatitis in humans in various geographical regions including Japan, New Zealand, U.S., Egypt, and Pakistan. It is likely that these data underestimate the seroprevalence of antibodies to HGBV among all categories of specimens tested. It is expected that as additional HGBV epitopes are discovered and evaluated, the utility of tests derived from the HGBV genome(s) will become more important in diagnosing hepatitis among patients whose diagnosis cannot currently be made. NOTE: Although the results of RT-PCR were negative in these initial studies, subsequent data revealed flavi-like vial sequences in seram of seropositive individuals (see Example 17). As we have discussed supra, more than one strain of the HGBV is present. These are considered to be within the scope of the present invention and are termed "hepatitis GB Viras ("HGBV"). Example 16. Serological studies with HGBV-A A. Recombinant Protein Purification Protocol Bacterial cells expreessing the CKS fusion proteins were frozen and stored at - 70C. The bacterial cells from each of the GBV-A contstructs were thawed and disrapted as described in Example 15 for GBV-B constructs. Further, the recombinant proteins were purified as described for GBV-B recombinant proteins in example 15. The fractions which were collected during the purification protocol were electrophoretically separated and stained with Coomassie Brilliant Blue R250 and examined for the presence of a protein having a molecular weight of approximately 60kD (CKS 1.5/SEQUENCE NO. 614), 65kD (CKS 2.17/ SEQUENCE NO. 613), 55kD (CKS 1.18/SEQUENCE NO. 390) and 66kD (CKS 1.22/SEQUENCE NO. 390). Fractions containing the protein of interest were pooled and re-examined by SDS-PAGE. The immunogenicity and structural integrity of the pooled fractions containing the purified antigen were determined by immunoblot following electrotransfer to nitrocellulose as described in Example 13. In the absence of a qualified positive control, the recombinant proteins were identified by their reactivity with a monoclonal antibody directed against the CKS portion_of each fusion protein. When the CKS-1.5 protein (SEQUENCE I.D. NO. 614) was examined by Western blot, using the anti-CKS monoclonal antibody to detect the recombinant antigen, a single band at approximately 60 kD was observed. This coπesponds to the expected size of the CKS- 1.5 protein (SEQUENCE I.D. NO. 614). Similiarly, bands of the expected sizes were noted for the CKS -2.17 protein (SEQUENCE LD. NO. 613), the the CKS 1.18 protein (SEQUENCE NO. 390) and the CKS-1.22 protein (SEQUENCE I.D. NO. 390) when examined by immunoblot. B. Polystyrene Bead Coating Procedure The proteins were dialyzed and evaluated for their antigenicity on polystyrene beads described in Example 15. C. ELISA Protocol for Detection of Antibodies to HGBV The ELISA's were performed as described in Example 15. D. Detection of HGBV RNA in Seram of infected Individuals Specimens which were repeatably reactive in the ELISAs were tested for HGBV RNA as described in section D. of Example 15. E. Tamarin Serological Profiles None of the sera from the tamarins produced a specific immune response when tested in the ELISA utilizing the CKS 1.5 protein, the CKS 2.17 protein, the CKS 1.18 protein or the CKS 1.22 protein, all derived from the HGBV-A genome. However, HGBV-A RNA was detected in several of the infected tamarins as described in the previous example. (See Example 15 for a summary of the tamarin serological profiles). F. Experimental Protocol for Serologic Studies on Human Populations In Example 15, ELISA's employing recombinant antigens from HGBV-B were utilized to evaluate the presence of antibodies to HGBV-B in various human populations. Many of the same specimens were then tested for antibodies to HGBV-A utilizing the 1.5 ELISA employing the CKS- 1.5 recombinant protein (SEQUENCE LD. NO. 614), the 2.17 ELISA employing the CKS-2.17 recombinant protein (SEQUENCE I.D. NO. 613), the 1.18 ELISA employing the CKS- 1.18 recombinant protein (SEQUENCE I.D. NO. 390), and the ELISA employing the CKS-1.22 recombinant protein (SEQUENCE I.D. NO. 390), coated on the solid phase (as described in Example 15). As noted in Example 15, all five of the convalescing tamarins inoculated with HGBV produced a specific but short-lived antibody response to the HGVB-B recombinant proteins (as detected with the 1.7, 1.4 and 4.1 ELISA's). Although none of the tamarins produced a detectable antibody response in the 1.5, 2.17, 1.18 or 1.22JELISAs, some human specimens from West Africa produced a specific antibody response to one or more of these recombinant proteins when tested via Western blot and one of the specimens obtained from the surgeon (who was the source of the GB agent) at 22 days after onset of hepatitis produced a specific antibody response to the 2.17 recombinant protein when tested by Western blot (see Example 3). In the current example, we evaluated the utility of the 1.5, 2.17, 1.18 and 1.22 ELISA's in detecting antibodies in various human populations. G. Cutoff Determination The cutoff for the 1.5, 2.17, 1.18, and 1.22 ELISAs were determined as described in Example 15. H. Supplemental Testing As noted in Example 15, specimens which were initially reactive were typically retested; if the specimen was repeatably reactive, additional tests (e.g. Western blot) may be performed to further support the ELISA data. For a Western blot result to be considered positive, a visible band should be observed at 60 kD for the 1.5 protein (SEQUENCE I.D. NO. 614) at 65 kD for the 2.17 protein (SEQUENCE LD. NO. 613), at 55kD for the 1.18 protein (SEQUENCE I.D. NO. 390) at 66 kD for the 1.22 protein (SEQUENCE I.D. NO. 390).. Since the Western blot had not been optimized to match or exceed the sensitivity of the ELISA's, a negative result was not used to discard the ELISA data. However, a positive result reinforced the reactivity detected by the ELISA's. As also noted in Example 15, repeatably reactive specimens which have sufficient volume may be tested by RT-PCR (performed as described in Example 15) using primers to identify HGBV specific nucleotide sequences in seram. I. Serological Data Obtained with Low-Risk Specimens A total of 252 plasma specimens were obtained from the Interstate Blood Bank in Ohio and tested for antibodies with the 1.5 ELISA which utilizes the 1.5 recombinant protein (SEQUENCE LD. NO. 614). The mean absorbance value for the population was 0.036 (SD=0.022). The cutoff was calculated to be 0.168, corresponding to an S/N value of 10.0. A total of 760 plasma specimens (including the 252 specimens utilized to determine the cutoff) were tested for antibodies with the 1.5 ELISA. None of the specimens were repeatably reactive. In addition, 100 plasma specimens were obtained from Southeastern Wisconsin and tested for antibodies with the 1.5 ELISA. None of the specimens were repeatably reactive. Thus, there is no evidence that antibodies to the 1.5 protein were present in U.S. blood donors. A total of 200 specimens were obtained from Wisconsin blood donors and tested for antibodies with the 2.17 ELISA which utilizes the 2.17 recombinant protein (SEQUENCE I.D. NO. 60). The mean absorbance value for the population was 0.058 (SD=0.025). The cutoff was calculated to be 0.208, coπesponding to an S/N value of approximately 10.0. One of the specimens was repeatably reactive. Thus, the seroprevalence in U.S. blood donors (N=200) is relatively low. The same 200 specimens described in the above paragraph were tested for antibodies with the 1.18 and 1.22 ELISAs. None of the specimens were repeatably reactive. Thus, there is no evidence that specimens from volunteer blood donors are antibody positive for HGBV-A proteins as determine by the 1.5, 2.17, 1.18 and 1.22 ELISAs. J. Specimens Considered "At Risk" for Hepatitis The data for these studies is summarized in TABLE 18. (i) Specimens from West Africa A total of 58 of 1300 specimens were reactive with the 1.5 ELISA. Twelve of 18 repeatably reactive specimens were positive by Western blot for antibodies to the 1.5 protein (SEQUENCE I.D. NO. 614). A total of 43 of 817 specimens were reactive in the 2.17 ELISA. These repeatably reactive specimens were not tested by Western blot for antibodies to the 2.17 protein (SEQUENCE I.D. NO. 613). Six of the 817 specimens were reactive with the 1.22 ELISA. Nine of the 353 specimens were reactive for 1.18 ELISA. Twenty-one specimens reactive with the 2.17 ELISA were tested by Western blot and 13 were reactive. All eight specimens that were repeatably reactive with the 1.18 ELISA was positive by Western blot. These data suggest that HGBV may be endemic in West Africa. (ii) Specimens from Intravenous Drug Users A total of 112 specimens were obtained from a population of intravenous drag users, as part of a study being conducted at Hines Veteran's Administration Hospital, in Chicago, IL. One specimen was repeatably reactive in the 2.17 ELISA and an additional specimen was reactive in the 1.18 ELISA. None of these specimens were positive in the 1.5 or 1.22 ELISA. K. Specimens obtained from individuals with non A-E Hepatitis The data for these studies is summarized in TABLE 18. Various populations of specimens (described in Example 15.K) were obtained from individuals with non-A-E hepatitis and tested with the 1,5, 2.17, 1.18 and 1.22 ELISAs (described in Example 15.C). Due to insufficient sample volume, not all specimens were tested in all of the ELISAs. (i) Specimens from Japan A total of four of 89 specimens were repeatably reactive in the 1.5 ELISA, with three of the specimens being from one individual and one of the specimens from a second individual. One specimen which had tested negative for the 1.5 ELISA, the 1.18 ELISA and the 1.22 ELISA was reactive in the 2.17 ELISA. None of the specimens were reactive in the 1.18 ELISA. These specimens were not tested with the 1.22 ELISA. (ii) Specimens from New Zealand None of these 56 specimens were reactive in the 1.5 ELISA. These specimens were not tested in the 2.17 ELISA, the 1.18 ELISA or the 1.22 ELISA.. (iii) Specimens from Greece None of the 67 specimens (obtained from a total of 10 patients) were reactive for antibodies with the 1.5, 2.17 or 1.22 ELISA. (iv) Specimens from Egypt None of 132 specimens were reactive in the 1.5 ELISA. A total of 7 of 132 specimens available for testing were reactive in the 2.17 ELISA. These specimens were obtained from 25 individuals with acute non A-E hepatitis. Three of the 25 patients were seropositive in the 2.17 ELISA on one or more separate dates following the onset of hepatitis. None were reactive in the 1.18 or 1.22 ELISA. (v) Specimen from the U.S. (Set M) None of the 72 specimens were reactive with the 1.5 ELISA. Three of the 72 specimens were reactive for the 1.18 ELISA. Two of the specimens were reactive in the 2.17 ELISA and four specimens were reactive with the 1.22 ELISA. Two of the samples were reactive in one of more of the ELISAs. (vi) Specimens from U.S. (Set T) None of the 64 specimens were reactive with the 1.5, 1.22 or 2.17 ELISAs. One specimen was reactive for the 1.18 ELISA. (vii) Specimens from U.S. (Set 1) A total of 3 of 62 specimens were reactive in one or more of the GBV-A ELISAs. One specimen was repeatly reactive in both the 2.17 and 1.22 ELISA. One specimen was reactive only in the 2.17 ELISA and an additional specimen was reactive only in the 1.22 ELISA. None of the specimens were reactive in the 1.5 or 1.18 ELISA. As we have discussed supra, it is possible that more than one strain of the HGBV may be present, or that more than one distinct virus may be represented by the sequences disclosed herein. These are considered to be within the scope of the present invention and are termed "hepatitis GB Viras ("HGBV"). L. Statistical Significance of Serological Results These data indicated that specific antibodies to HGBV-A proteins ( i.e. specimens repeatably reactive for antibodies in 1.5, 2.17, 1,18 and 1.22 ELISA's) were detected among individuals considered "at risk" for exposure to HGBV and among individuals diagnosed with non A-E hepatitis, but were not frequently detected either among volunteer or paid blood donors from the U.S. In TABLE 19, the serological results obtained with the various categories of specimens ("low risk", "at risk" and non A-E hepatitis patients as shown in TABLE 18) were grouped together and analyzed for statistical significance using the Chi square test. Unlike the data in TABLE 18, which compiled the seroprevalence of antibodies to HGBV proteins in the total number of specimens tested, the data in TABLE 19 reflect the results obtained with different individuals (persons). For the GBV-A ELISAs, the data indicate that there is a significant difference (with a p value of 0.000) in comparing the seroprevalence of anti-HGBV in volunteer blood donors with the individuals considered "at risk" for exposure to HGBV (West Africa) but not in the IVDUs. In addition, there was a statistically significant difference between the seroprevalence of antibodies to HGBV-A in individuals with non A-E hepatitis in Egypt and the U.S. when compared to volunteer donors These data suggest that exposure to HGBV-A was associated with non-A through E hepatitis. NOTE: although the results of RT-PCR were negative in these initial studies, subsequent data revealed flavi-like vial sequences in seram of seropositive individuals (see Example 19). M Summary These data suggest that the ELISA described herein may be useful in detecting antibodies among individuals residing in West Africa and among individuals with non-A through E hepatitis. The risk for hepatitis among the West Africans is relatively high; nearly 85% of these individuals are seropositive for antibodies to Hepatitis B viras, and approximately 5% are positive for antibodies to hepatitis C viras. It is likely that these data underestimate the seroprevalence of antibodies to HGBV among all categories of specimens tested. It is expected that as additional HGBV epitopes are discovered and evaluated, the utility of tests derived from the HGBV genome(s) will become more important in diagnosing hepatitis among patients whose diagnosis cannot cuπently be made. Example 18. Identification of a GB-related viras in humans A. Theory Epitopes from both HGBV-A and HGBV-B have been identified (Example 3). These have been used as serologic markers to screen human serum and plasma samples (Examples 5 and 6). A significant coπelation between seroreactivity with some of these markers and the incidence of nonA-E hepatitis has suggested that HGBV-B is the causative agent of nonA-E hepatitis in humans (Example 5.G). However, Western blot analysis of GB human sera gave no indication of reactivity to HGBV-B epitopes (Example 3). Instead, at least one HGBV-A epitope was identified with the GB human sera suggesting that HGBV-A was the causitive agent of hepatitis in GB. Neither HGBV-A nor HGBV-B sequences have been identified in patients with nonA-E hepatitis by RT-PCR (Example 5.E). Therefore, proof of HGBV-A and/or HGBV-B infection in humans with nonA-E hepatitis remains to be determined. The failure to identify HGBV-A and/or HGBV-B sequences in human sera or plasma sources may be due to several factors. First, we have looked at only a limited number of HGBV-A and/or HGBV-B -seropositive samples by RT-PCR, and the complete storage history of many of these samples is unknown. Thus, it is possible that viral RNA present in these samples was compromised by incoπect storage. Second, GB infection appears to be resolving in nature. As such, the window of time in which GB sequences are present in an infected individual's serum may be very narrow. Thus, the chances of obtaining seram samples containing GB sequences may be extremely low. Finally, a limited number of PCR primer sets were used to look for HGBV-A and/or HGBV-B sequences. HGBV-A and/or HGBV-B are RNA virases and, therefore, are likely to have high rates of mutation (Holland, et al. (1982) Science 215: 1577-1585). Thus, the sequence of HGBV-A and/or HGBV-B present in the examined human sera may be different enough from the sequence of our PCR primers such that HGBV-A and/or HGBV-B may be not be detected. To address the possibility that the genomic variability of HGBV-A and/or HGBV-B prevented these virases in our PCR studies, degenerate PCR primers were designed to the highly conserved NS3-like regions of HGBV-A and HGB V- B (see Fig.17). It was reasoned that these highly conserved regions serve a necessary function in the viral replicative cycle. Therefore, these sequences should be maintained in HGBV-A and HGBV-B variants. PCR primers designed within this region should be able to detect HGBV-A and/or HGBV-B genomic RNA by RT-PCR. In addition, by designing degenerate PCR primers that can specifically amplify HGBV-A, HGBV-B and HCV sequences, we reasoned that we might be able to amplify sequences from virases related to HGBV-A, HGBV-B and HCV. Thus, if the limited seroreactivity detected in human seram and plasma samples (Examples 5 and 6) is the result of cross-reactive antibodies to antigens from distinct HGBV-A- or HGB V-B-related virases, we may be able to obtain sequences from these GB-related virases. [This is similar to the experimental approach that Nichol and colleagues took to identify the unique Hantaviras associated with the recent outbreak of acute respiratory illness in the Southwest United States. Nichol, et al. Science 262:914-917 (1993)] B. Cloning the NS3-like region of hepatitis GB viras C (HGBV-C). In several models of virus infetions, viremia occurs during the early stages of infection and is often associated with the detection of IgM class antibodies to viral proteins. As noted in examples 5 and 6, several specimens were immunoreactive in ELISA's which detected IgG class antibodies to recombinant proteins derived from HGBV-A and HGBV-B. Additional ELISA's were performed to determine if IgM class antibodies could be detected to these proteins. Several seropositive specimens obtained from West African individuals (Example 5.E.i) were reactive for IgM class antibodies to the recombinant proteins (data not shown). These specimens were thought to have a high probability of containing virus. In addition, specimens obtained from HGBV-A- and HGBV-B- seropositive Egyptian individuals (Example 5.F.vii) suffering from acute hepatitis in the absence of detectable IgM class antibodies to HGBV-A or HGBV-B recombinant proteins were also examined due to the likelihood that acute liver disease is most likely linked to viral presence. A "hemi-nested" RT-PCR was performed on the nucleic acids from these samples with degenerate oligonucleotide primers which will amplify HGBV-A, HGBV-B and HCV-1 sequences using the GeneAmp® RNA PCR kit (Perkin Elmer) as directed by the manufacturer. Briefly, the first set of amplifications were performed on the cDNA products of random-primed reverse transcription reactions of the extracted nucleic acids with 2 mM MgCl 2 and 1 μM primers ns3.1-s and ns3.1-a (SEQUENCE IP. NOS. 671 and 672, respectively). Reactions were subjected to 40 cycles of denaturation- annealing-extension [three cycles of (94°C, 30 sec; 37°C, 30 sec; 2 min ramp to 72°C; 72°C, 30 sec) followed by 37 cycles of (94°C, 30 sec; 55°C, 30 sec; 72°C, 30 sec)] followed by a 10 min extension at 72°C. Completed reactions were held at 4°C. The second set of amplifications were as described above except that 4% of the first PCR products were used as the template, and ns3.1-s and ns3-a (SEQUENCE IP. NOS. 671 and 673, respectively) were used as the "hemi- nested" primer set. Products from the first and second sets of PCRs were analyzed by gel electrophoresis. One sample from West Africa had a PCR product from the hemi-nested reaction that migrated at approximately 386 bp (the expected size of a HGBV-A, HGBV-B or HCV product). This product was cloned into pT7 Blue T-vector plasmid (Novagen) as described in the art. The sequence obtained from this clone (GB contig C [GB-C], SEQUENCE H>. NO. 673, residues 2274-2640) was compared with GB contig A (GB-A, SEQUENCE IP. NO. 163, residues 4438- 4804), GB contig B (GB-B, SEQUENCE IP. NO. 393, residues 4218-4587) and HCV-1 (SEQUENCE IP. NO. 398). FIGURE 36 shows a nucleotide alignment of these sequences, while TABLE 20 shows the percent identity between these sequences. As demonstrated in FIGURE. 36 and TABLE 20, nucleotide comparisons of GB- A, GB-B and HCV-1 show that these sequences are 47.99 to 61.66% identical to one another. This is not surprising when one considers the conserved amino acid residues present in the NTP-binding helicase of these virases (Example 2.B.3, FIGURE. 17 A). The nucleotide comparison of the NS3 PCR product obtained from the West African sample (GB-C, SEQUENCE IP. NO. 673, residues 2274- 2640) with the other viruses suggests that the West African NS3 product (GB-C, SEQUENCE IP. NO. 673, residues 2274-2640) is related to, but distinct from the NS3 sequences from GB-A (SEQUENCE IP. NO. 163, residues 4438-4804), GB-B (SEQUENCE. IP. NO. 393, residues 4218-4587) and HCV-1 (SEQUENCE LD. NO. 398). This sequence comparison suggests that GB-C may be from a GB-like virus more closely related to GB-A than GB-B or HCV. BLASTN and BLASTX searches of nucleic acid and protein databases in the Wisconsin Sequence Analysis Package (Version 8) with GB-C (SEQUENCE LP. NO. 673, residues 2274-2640) finds limited sequence identity with several strains of HCV. The highest P values (i.e., odds of alignment being made by hance) for nucleotide and amino acid searches were 1.9 x 10" 20 and 5.3 x 10 -31 , respectively (data not shown). Together, these data suggest that GB-C (SEQUENCE LD. NO. 673, residues 2274-2640) may be from a unique GB-like viras related to HGBV- A, HGBV-B and HCV which we now designate, HGBV-C. C. GB-C is exogenous. PCR primers to GB-C sequence were utilized to determine whether this sequence could be detected in the genomes of humans, Rhesus monkeys, ! cerevisiae and E.coli as described, for example, in Example 6.B. PCR was performed using GeneAmp® reagents from Perkin-Elmer-Cetus essentially as directed by the supplier's instractions. Briefly, 300 ng of genomic PNA was used for each 100 μl reaction. PCR primers (SEQUENCE LP. NOS. 675 and 676) were used at a final concentration of 1.0 μM. PCR was performed for 40 cycles (94°C, 30 sec; 55°C, 30 sec; 72°C, 30 sec) followed by an extension at 72°C for 10 min. PCR products were separated by agarose gel electrophoresis and visualized by UV iπadiation after direct staining of the nucleic acid with ethidium bromide, followed by hybridization to a radiolabeled probe after Southern transfer to a Hybond-N+ nylon filter. FIGURE 37 shows a Phospholmage (Molecular Pynamics, Sunnyvale, CA) from a Southern blot of the PCR products after hybridization with the radiolabeled probe from GB-C (SEQUENCE LP. NO. 673, residues 2274-2640). GB-C (SEQUENCE LP. NO. 673) sequences were not detected in human (FIGURE 19, lane 1), Rhesus monkey (lane 2), S. cerevisiae (lane 3) or E. coli (lane 4) genomic PNAs despite the detection of -350 fg (one genome copy equivalent, lane 5) and -35 fg (0.1 genome copy equivalents, lane 6) of GB-C plasmid template in 300 ng human genomic PNA. (Lane 7 contains the PCR products from -3.5 fg [0.01 genome copy equivalents] GB-C plasmid template in 300 ng human genomic PNA.) Thus, using genomic PCR that can detect 0.1 genome copy equivalents, GB-C (SEQUENCE LP. NO. 673) cannot be detected in the genomes of human, Rhesus monkey, S. cerevisiae. and E. coli. These data are consistent with the purported exogenous (i.e. viral) origin of GB-C (SEQUENCE LO. NO. 673). O. GB-C can be detected in additional human serum samples. Additional HGBV-A and HGBV-B immunoreactive human seram samples were tested for the presence of GB-C sequences using RT-PCR. As in Example 7, nucleic acids extracted from seram samples were reverse transcribed using random hexamers, and cPNAs were subjected to 35-40 cycles of amplification (94°C, 30 sec; 55°C, 30 sec; 72°C, 30-90 sec) followed by an extension at 72°C for 10 min. GB-C-specific PCR primers (gl31-sl and gl31-al, SEQUENCE IP. NOS. 675 ANO 676) were used at 1.0 μM concentration. The PCR products were separated by agarose gel electrophoresis and visualized by UV iπadiation after direct staining of the nucleic acid with ethidium bromide and hybridization to a radiolabeled probe after Southern transfer to a Hybond-N+ nylon filter. A total of 48 HGB V-immunopositive samples were tested from West Africa. Including the original sample from which GB-C was identified, eight samples from West Africa were positive for GB-C sequences by RT-PCR. A total of ten GB seronegative West African seram samples were tested, none of which had detectable GB-C sequences. PCR products from four of the positive samples were cloned and sequenced as described above. Over the 156 nucleotides examined, two of four clones examined were identical to GB-C sequence (SEQUENCE LO. NO. 673, residues 2274-2640), and two clones (SEQUENCE I.D. NOS. 677 and 678) contained sequences that were 88.4% and 83.6% identical to GB-C (SEQUENCE LD. NO. 673, residues 2274-2640) (FIGURE 38). However, despite the divergence at the nucleotide level, the predicted translation product of each clone is remarkably similar with only one amino acid change occurring in the predicted translation of SEQUENCE ED NO. 678. Additional serum samples from individuals with nonA-E hepatitis from Greece, Egypt and the United States were tested for GB-C sequences as described above. None of these samples contained detectable GB-C sequences. The lack of detection of GB-C sequences in these samples may be due to several reasons (see above, Theory). However, the sequence variation noted above between GB-C (SEQUENCE LD. NO. 673, residues 2274-2640) and the two GB-C variants (SEQUENCE LD. NOS. 678 and 677) suggest that if the closely related HGBV- C's from West Africa can differ by 15.1% at the nucleotide level, it is likely that the GB-C-specific PCR primers (gl31-sl, gl31-al, SEQUENCE LD. NOS. 675 and 676) may not hybridize sufficiently to geographically distinct isolates of GB-C viras to generate a detectable PCR product. In this case, PCR primers designed to a more conserved region (5' UTR) of the genome may allow the detection of GB- C sequences in non-West African seram samples. E. Extension of the HGBV-C sequences. The PCR walking technique described in Example 2.A hereinabove was utilized to obtain additional GB-C sequences. Briefly, total nucleic acid were extracted from the West African human seram originally used to identify GB-C (SEQUENCE I.D. NO. 673, residues 2274-2640). This nucleic acid was reverse transcribed as described supra. The resultant cDNAs were amplified in 50 μl PCR reactions (PCR 1) as described by Sorensen et al. except that 2 mM MgC was used. Reactions were subjected to 35 cycles of denaturation-annealing-extension (94°C, 30 sec; 55°C, 30 sec; 72°C, 90 sec) followed by a 10 min extension at 72°C. Biotinylated products were isolated using streptavidin-coated paramagnetic beads (Promega) as described by Sorensen et al. Nested PCRs (PCR 2) were performed on the streptavidin-purified products as described by Sorensen et al. for a total of 35 cycles of denaturation-annealing-extension as described above. The resultant products and the PCR primers used to generate them are listed in TABLE 21. TABLE 21 In addition, a 1.3 kb product (C.l 6) was generated with oligonucleotide primers SEQ ID # 669 and SEQ ID # 670using PCR 1 conditions described above. This product, together with those described in TABLE 21 were isolated from agarose gels and cloned into pT7 Blue T-vector plasmid (Novagen) as described in the art. The cloned products were sequenced as described in Example 5. The sequences were assembled using the GCG Package (version 7) of programs. A schematic of the assembled contig is presented in FIGURE 39. GB-C is 9034 bp in length, all of which has been sequenced and is presented in SEQUENCE I.D. NO. 400-606. These SEQUENCE I.D.'s coπesond to the three forward translation frames. Example 19. CKS-based expression and detection of immunogenic HGBV-C polypeptides The HGBV-C sequences obtained from the walking experiments described in Example 17 (TABLE 13) were cloned into the CKS expression vectors pJO200, pJO201, and pJO202 using the restriction enzymes listed in TABLE 22 (10 units, NEB) as described in Example 13. Two additional PCR clones, designated C.3/2 and C.8/12, were also expressed (FIGURE 39). PCR product C.3/2 was generated using primers SEQUENCE I.D. NO. 681 and the complement of SEQUENCE I.D No. 685 and PCR product C.8/12 was generated using primers (SEQUENCE I.D. NO. 693 and its complement) as described in Example 9. The PCR products were cloned into pT7Blue as described previously, then liberated with the restriction enzymes listed in TABLE 22 and cloned into pJO200, pJO201 and ρJO202 as above. Two human sera which had indicated the presence of antibodies to one or more of the CKS/HGBV-A or CKS/HGBV-B fusion proteins by the 1.7, 4.1 or 2.17 ELISAS (see Examples 15 and 16) were chosen for Western blot analysis. One of these sera (240D) was from an individual with nonA-E hepatitis (Egypt) and the other (G8-81) was from a West African individual "at risk" for exposure to HGBV (see Example 15). The CKS/HGBV-C fusion proteins were expressed and transfeπed to nitrocellulose sheets as described above. The blots were preblocked as described and incubated overnight with one of the human seram sample diluted 1:100 in blocking buffer containing 10% E. coli lysate and 6mg/ml XLl-Blue/CKS lysate. The blots were washed two times in TBS, reacted with HRPO-conjugated goat anti-human IgG and developed as indicated above. The results are shown in TABLE 22. Several of the HGBV-C proteins showed reactivity with one or the other of the two sera, and three (C.l, C.6 and C.7) were chosen for use in ELISA assays (see Example 20). Thus, samples previously identified as reactive with HGBV-A and/or HGBV-B proteins additionally show reactivity with HGBV-C proteins. The reactivity with multiple proteins from the 3 HGBV viruses may be due to cross-reactivity resulting from shared epitopes between the viruses. Alternatively, this may be a result of infection with multiple viruses, or to other unidentified factors. TABLE 22 HGBV-C Samples a PCR product is as indicated in previous TABLES or Examples. "Restriction digests used to liberate the PCR fragment from pT7Blue T-vector. ND = not done. Example 20. Serological studies with GBV-C A. Recombinant Protein Purification Protocol Bacterial cells expressing the CKS fusion proteins were frozen and stored at - 70C The bacterial cells from each of the GBV-C constracts were thawed and disrapted as described in Example 15 for GBV-B constracts. Further, the recombinant proteins were purified as described for GBV-B recombinant proteins in example 15. The fractions which were collected during the purification protocol were electrophoretically separated and stained with Coomassie Brilliant Blue R250 and examined for the presence of a protein having a molecular weight of approximately 75kD (CKS Cl/SEQUENCE I.D. NO. 404), 71kD (CKS C.6/ SEQUENCE I.D. NO. 404 ), and 49kD (CKS C7/SEQUENCE I.D. NO.404). Proteins bands of the expected molecular weight were observed for the CKS-C.6 and CKS-C.7 recombinant proteins. For the CKS-C.l protein, a band was observed which coπesponded to a molecular weight of 62 kD rather than at the expected molecular weight of 75kD. It is unclear why there are differences between the expected and observed protein band. Fractions containing the protein of interest were pooled and re-examined by SDS-PAGE. The immunogenicity and structural integrity of the pooled fractions containing the purified antigen were determined by immunoblot following electrotransfer to nitrocellulose as described in Example 13. In the absence of a qualified positive control, the recombinant proteins were identified by their reactivity with a monoclonal antibody directed against the CKS portion of each fusion protein. When the CKS-C.l protein (SEQUENCE I.D. NO.404) was examined by Western blot, using the anti-CKS monoclonal antibody to detect the recombinant antigen, a single band at approximately 65kD was observed. This differs from the expected size of 75kD for the CKS-C 1 protein (SEQUENCE I.D. NO.404). Bands of the expected sizes were noted for the CKS-C.6 protein (SEQUENCE I.D. NO. 404), and the CKS C.7 protein (SEQUENCE I.D. NO. 404) were observed when examined by immunoblot. B. Polystyrene Bead Coating Procedure The proteins were dialyzed and evaluaed for their antigenicity on polystyrene beads described in Example 15. C. ELISA Protocol for Detection of Antibodies to HGBV The ELISA's were performed as described in the previous Example 15. D. Detection of HGBV RNA in Seram of infected Individuals Specimens which were repeatably reactive in the ELISAs were tested for HGBV RNA as described in section D. of the previous example 15. E. Tamarin Serological Profiles None of the sera from the tamarins produced a specific immune response when tested in the ELISA utilizing the CKS-C.l protein, the CKS-C.6 protein, or the CKS C.7 protein, all derived from the HGBV-C genome. See Example 15 for a description of the tamarin serological profiles. F. Supplemental Testing As noted in Example 15, specimens which were initially reactive were typically retested; if the specimen was repeatably reactive, additional tests (e.g. Western blot) may be performed to further support the ELISA data. For a Western blot result to be considered positive, a visible band should be observed at 65kD for the C.l protein (SEQUENCE LD. NO. 404), at 71kD for the C.6 protein (SEQUENCE LD. NO. 404), or at 49kD for the C.7 protein (SEQUENCE I.D. NO. 404).. Since the Western blot had not been optimized to match or exceed the sensitivity of the ELISA's, a negative result was not used to discard the ELISA data. However, a positive result reinforced the reactivity detected by the ELISA's. As also noted in Example 15, repeatably reactive specimens which have sufficient volume may be tested by RT-PCR (performed as described in Example 10 using primers coπesponding to SEQUENCE I.D. NOS. 8 and 9) to identify HGBV-C specific nucleotide sequences in seram. G. Experimental Protocol. In example 15, ELISA's employing recombinant antigens from HGBV-B were utilized to evaluate the presence of antibodies to HGBV-B AND HGBV-A in various human populations. Many of the same specimens were then tested for antibodies to HGBV-C utilizing the C.l ELISA employing the CKS-C.l recombinant protein (SEQUENCE I.D. NO. 404), the C.6 ELISA employing the CKS-C.6 recombinant protein (SEQUENCE I.D. NO. 404), the C.7 ELISA employing the CKS-C.7 recombinant protein (SEQUENCE I.D. NO. 404) coated on the solid phase (as described in Example 14). As noted in Example 15, all five of the convalescing tamarins inoculated with HGBV produced a specific but short- lived antibody response to the HGVB-B recombinant proteins (as detected with the 1.7, 1.4 and 4.1 ELISA's). Although none of the tamarins produced a detectable antibody response in the C.l, C.6, C.7 ELISAS, some of the human specimens produced a specific antibody response to the C.l, C.6, and C.7 recombinant protein when tested via Western blot (see Example 13) In the cuπent example, we evaluated the utility of the C.1 , C.6, and C.7 ELISA's in detecting antibodies in various human populations. H. Cutoff Determination The cutoff for the C.l, C.6, and C.7 ELISAs were determined as described in Example 15. I. Serological Data Obtained with Low-Risk Specimens A population consisting of 100 sera and 100 plasma was obtained from healthy, volunteer donors in Southeastern Wisconsin and tested for antibodies to three recombinant proteins from GBV-C including the CKS- C.l (SEQUENCE I.D. NO. 404) protein in the C.l ELISA, the CKS- C.6 (SEQUENCE I.D. NO. 404) protein in the C.6 ELISA, and the CKS- C.7 (SEQUENCE I.D. NO. 404) protein in the C.7 ELISA. For the C 1 ELISA, the mean absorbance values for the seram and plasma specimens were 0.049 {with a standard deviation (SD) of 0.040} and 0.038 (SD=0.029), respectively The cutoff for seram and plasma were calculated to be 0.214 and 0.286, respectively. As discussed above, the cutoff value was also expressed as a factor of the negative control absorbance value; specimens having S/N values above 10.0 were considered reactive. Using this cutoff, 0 of 100 plasma specimens and 1 of 100 serum specimens were initially reactive and repeatably reactive for antibodies to the C.l protein (SEQUENCE I.D. NO. 404). For the C.6 ELISA, the mean absorbance values for the seram and plasma specimens were 0.102{with a standard deviation (SD) of 0.046} and 0.105 (SD=0.047), respectively. Cutoff values were set such that specimens having an S/N value of 10 or greater were considered reactive Using this cutoff, three specimens (two from the seram population and one from the plasma population) were repeatably reactive (having S/N values of 10 or greater) for antibodies to the C.6 protein (SEQUENCE I.D. NO. 404). For the C.7 ELISA, the mean absorbance values for the seram and plasma specimens were 0.061 {with a standard deviation (SD) of 0.040} and 0.050 (SD=0.055), respectively. Cutoff values were set such that specimens having an S/N value of 10 or greater were considered reactive. Using this cutoff, none of the specimens were repeatably reactive for antibodies to the C.7 protein (SEQUENCE I.D. NO. 404). Thus, there is evidence that antibodies to the C.l, C.6, or C.7 proteins are present in approximately 1% of U.S. blood donors (N=200). J. Specimens Considered "At Risk" for Hepatitis The data for these studies is summarized in TABLE 23. (i) Specimens from West Africa A total of 20 of 137 specimens were reactive in one or more of the ELISAs utilizing GBV-C proteins. A total of 12 of 97 were repeatably reactive in the C.l ELISA , 3 of 52 were repeatably reactive in the C.6 ELISA, 5 of 137 specimens were reactive in the C.7 ELISA. Three of the C.1 reactive specimens were tested on Western blot and found to be reactive. These data suggest that HGBV may be endemic in West Africa. (ii) Specimens from Intravenous Drug Users A total of 112 specimens were obtained from a population of intravenous drag users, as part of a study being conducted at Hines Veteran's Administration Hospital, in Chicago, IL. A total of 2 of 112 specimens were repeatably reactive for one or more proteins. One specimen was repeatably reactive in the C.l ELISA, one specimen was repeatably reactive in the C.7 ELISA. None of these specimens were positive in the C.6 ELISA. K. Specimens obtained from individuals with non A-E Hepatitis The data for these studies is summarized in TABLE 23. Various populations of specimens (described in Example 15.K) were obtained from individuals with non-A-E hepatitis and tested with the 1.5, 2.17, 1.18 and 1.22 ELISAs (described in Example 15.C). Due to insufficient sample volume, not all specimens were tested in all of the ELISAs. (i) Specimens from Japan None of a total of 89 specimens were repeatably reactive in the C.1 ELISA. Due to lack of specimen volume, the specimens were not tested for antibodies in the C.6 or C.7 ELISAs. (ii) Specimens from Greece A total of 67 specimens were tested with the C.1 and C.7 ELISAs. None of the specimens were reactive. (ϋi) Specimens from Egypt A total of 18 specimens of 132 specimens were reactive in one or more ELISA. None of the specimens were reactive in the C.l ELISA. A total of 15 specimens were reactive in the C.6 ELISA and three were reactive in the C.7 ELISA. (iv) Specimens from U.S. (M set) A total of 6 specimens were reactive in one or more ELISA. Two specimens were repeatably reactive in the C.1 ELISA. Four specimens were repeatably reactive in the C.6 ELISA. None of the specimens were reactive in the C.7 ELISA. (v) Specimens from U.S. (T set) None of the 64 specimens were reactive in either the C.1 or the C.6 ELISAs. One specimen was repeatably reactive in the C.7 ELISA. (vi) Specimens from various U.S. clinical sites (set 1) In total, three of 62 specimens were reactive in one or more ELISA's. One specimen was repeatably reactive in both the C.1 and C.6 ELISA;s. Two specimens were repeatably reactive in the C.7 ELISA. As we have discussed supra, it is possible that more than one strain of the HGBV may be present, or that more than one distinct viras may be represented by the sequences disclosed herein. These are considered to be within the scope of the present invention and are termed "hepatitis GB Virus ("HGBV"). L. Statistical Significance of Serological Results These data indicated that specific antibodies to HGBV-C proteins ( i.e. specimens repeatably reactive for antibodies in C.l, C.6 and C.7 ELISA's) were detected among individuals considered "at risk" for exposure to HGBV and among individuals diagnosed with non A-E hepatitis, and at low rate among volunteer or paid blood donors from the U.S. In TABLE 24, the serological results obtained with the various categories of specimens ("low risk", "at risk" and non A-E hepatitis patients as shown in TABLE 23) were grouped together and analyzed for statistical significance using the Chi square test. Unlike the data in TABLE 23, which compiled the seroprevalence of antibodies to HGBV proteins in the total number of specimens tested, the data in TABLE 24 reflect the results obtained with different individuals (persons). For the GBV-C ELISAs, the data indicate that there is a significant difference (with a p value of 0.000) in comparing the seroprevalence of anti-HGBV in volunteer blood donors with the individuals considered "at risk" for exposure to HGBV (West Africa) but not for the IVDUs. In addition, there was a statistically significant difference between the seroprevalence of antibodies to HGBV-C in individuals with non A-E hepatitis in Egypt and the U.S. when compared to volunteer donors These data suggest that exposure to HGBV-C was associated with non-A through E hepatitis. NOTE: although the results of RT-PCR were negative in these initial studies, subsequent data revealed flavi-like vial sequences in seram of seropositive individuals (see Example 19). Example 21. Presence of HGBV-C in humans with non-A-E hepatitis. The generation of HGBV-C-specific ELISAs allowed the identification of immunopositive sera from patients with non-A-E hepatitis (Example for HGBV-C serology). These sera, together with several HGBV-A and/or HGBV-B- immunopositive sera from individuals with documented cases of non-A-E hepatitis (TABLE 25) were examined by RT-PCR for HGBV-C sequences. To increase the likelihood of detecting HGBV-C variants, RT-PCR was performed using degenerate NS3 oligonucleotide primers in a first round of amplification followed by a second round of amplification with nested GB-C-specific primers. Briefly, the first round amplification was performed on seram cDNA products generated as described in Example 6, using 2 mM MgCl2 and 1 μM primers ns3.2-sl and ns3.2-al (SEQ. ID. NOS. 711 and 712, respectively). Reactions were subjected to 40 cycles of denaturation-annealing-extension [three cycles of (94°C, 30 sec; 37°C, 30 sec; 2 min ramp to 72°C; 72°C, 30 sec) followed by 37 cycles of (94°C, 30 sec; 50°C, 30 sec; 72°C, 30 sec)] followed by a 10 min extension at 72°C. Completed reactions were held at 4°C A second round of amplification was performed utilizing 2 mM MgCl 2 , 1 μM GB-C-specific primers (SEQUENCE I.D. NOS. 675 and 676), and 4% of the first PCR products as template. The second round of amplification employed a thermocycling protocol designed to amplify specific products with oligonucleotide primers that may contain base pair mismatches with the template to be amplified [Roux, Bio/Techniques 16:812-814 (1994)]. Specifically, reactions were thermocycled 43 times (94°C, 20 sec; 55°C decreasing 0.3°C/cycle, 30 sec; 72°C, 1 min) followed by 10 cycles (94°C, 20 sec; 40°C, 30 sec; 72°C, 1 min) with a final extension at 72°C for 10 minutes. PCR products were separated by agarose gel electrophoresis, visualized by UV iπadiation after direct staining of the nucleic acid with ethidium bromide, then hybridized to a radiolabeled probe for GB-C after Southern transfer to Hybond-N+ nylon filter. PCR products were cloned and sequenced as described in the art. Using the above methodology, GB-C.4, GB-C.5, GB-C.6 and GB-C.7 were obtained. These sequences are 82.1-86.6% identical to GB-C (SEQUENCE LD. NO. 400,bases 4167-4365). FIGURE 40 displays the sequence differences of GB-C.4, GB-C.5, GB-C.6 and GB-C.7 aligned to the homologous region of GB-C in the predicted codon triplicates. As demonstrated, a majority of the nucleotide differences do not result in amino acid changes from GB-C. This overall sequence conservation at the amino acid level suggests that GB-C.4, GB- C.5, GB-C.6 and GB-C.7 were derived from different strains of the same viras, HGBV-C. In addition, the level of sequence divergence at the nucleotide level demonstrates that these PCR products are not a result of contamination with any of the previously identified GB-C sequences. Three of these individuals (the sources of GB-C.4, GB-C.5 and GB-C.7) had no evidence of infection with hepatitis A, hepatitis B or hepatitis C viruses. The presence of GB-C sequences in these individuals with hepatitis of unknown etiology suggests that HGBV-C is one of the causative agents of human hepatitis. Serial samples were available for two of the individuals (containing GB-C.4 and GB-C.5). To follow the HGBV-C sequence in these samples, clone specific RT- PCRs were developed. Briefly, nucleic acids extracted from seram were reverse transcribed using random hexamers as in Example 7. The resultant cDNAs were subjected to 40 cycles of amplification (94°C, 30 sec; 55°C, 30 sec; 72°C, 30 sec) followed by an extension at 72°C for 10 min. GB-C.4- or GB-C5-specific PCR primers (GB-C4-sl and GB-C4-al, or GB-C5-sl and GB-C5-al, respectively) were used at 1.0 μM concentration. PCR products were separated by agarose gel electrophoresis, visualized by UV iπadiation after direct staining of the nucleic acid with ethidium bromide, then hybridized to a radiolabeled probe after Southern transfer to Hybond-N+ nylon filter. GB-C.4 was found in sera from an Egyptian patient with acute non-A-E hepatitis. This patient was seropositive for a HGBV-A protein (see HGBV-A ELISA Example). RT-PCR of five serial samples from the Egyptian patient demonstrated a viremia that persisted for at least 20 days after normalization of the seram ALT values (TABLE 26). The presence of GB-C sequence after serum ALT normalization suggested that HGBV-C may establish chronic infections in some individuals. However, the absence of additional samples from this patient prevents a conclusion as to the chronic nature of HGBV-C. Additional samples are being pursued to resolve this question. GB-C.5 was obtained from a Canadian patient with hepatitis associated aplastic anemia. Each sample from this patient was seropositive in the C.7 ELISA (Example 20). GB-C.5 was detected in the samples obtained from the Canadian patient during aplastic anemia (day 13 post-presentation) and at the time of death (day 14, FIGURE. 41) using GB-C5-specific primers (GB-C.5-sl and GB-C.5- al). However, GB-C5-specific PCR failed to detect GB-C.5 sequence at the time of presentation (day 0, acute hepatitis) and on day 3 (liver failure). Thus, it is unclear whether GB-C.5 was present below the limit of detection in the first samples. If so, HGBV-C may have been the causative agent of this patient's aplastic anemia. However, because GB-C.5 was detected by RT-PCR only during aplastic crisis, GB-C.5 may have been acquired from a blood product administered to combat the anemia. In this case, HGBV-C's association with aplastic anemia would be similar to HCV's [Hibbs, et al.JAMA 267:2051-2054 (1992)]. Due to the distant relation of HGBV-C and HCV, it was of interest to determine whether cuπent methods for detecting HCV infection would recognize human samples containing HGBV-C. Routine detection of individuals exposed to or infected with HCV relies upon antibody tests which utilize antigens derived from three or more regions of HCV- 1. These tests allow detection of antibodies to all of the known genotypes of HCV in most individuals [Sakamoto, et al. J. Gen. Virol. 75:1761-1768 (1994); Stuyver, et al. J. Gen. Virol. 74:1093-1102 (1993)]. Second generation ELISAs for HCV were performed on the samples that contain HGBV-C as described in Example 10 (TABLE 25). One of the 4 samples that contain HGBV-C was seropositive for HCV antigens. A limited number of human sera which are seronegative for HCV have been shown to be positive for HCV genomic RNA by a highly sensitive RT-PCR assay [Sugitani, 1992 #65]. A similar RT-PCR assay (as described in Example 9) confirmed the presence of an HCV viremia in the seropositive sample. However, none of the HCV seronegative samples were HCV viremic. Therefore, although 1 of the 4 individuals containing HGBV-C sequences have evidence of HCV infection, the cuπent assays for the presence of HCV did not accurately predict the presence of HGBV-C. The one HCV-positive patient appears to be co-infected with HGBV-C. It is unclear whether the hepatitis noted in this patient was due to HCV, HGBV-C or the presence of both viruses. That HGBV-C and HCV are found in the same patient may suggest that common risk factors exist for acquiring these infections. Using the PCR protocol described above, GB-C sequences (-85% identical to the previous GB-C isolates shown in FIGURE 41, data not shown) were identified in "normal" units of blood from two volunteer U.S. donor obtained in 1994. These units tested negative for HBV, HCV, and had normal seram ALT values. However, these units tested positive in the 1.4 ELISA. Finding HGBV-C in at least two units of "normal" blood out of - 1000 units immunoscreened suggests that this viras is cuπently in the U.S. blood supply. However, using ELISAs developed from HGBV proteins and nucleotide probes from HGBV sequences, we demonstrate that these units of blood can be identified. The large amount of sequence variation in the various GB-C sequences (FIGURE 41) should be noted. Although highly sensitive, PCR based assays for viral nucleic acids are dependent on the sequence match between oligonucleotide primers and the viral template. Therefore, because the PCR primers utilized in this study were located in a region of the HGBV-C genome that is not well conserved in various isolates, not all HGBV-C viremic samples tested may have been detected by the RT-PCR assays employed here. Utilization of PCR primers from a highly conserved region of the HGBV-C genome, as have been found in the HCV 5' untranslated region [Cha, et al. J. Clin. Microbiol. 29:2528-2534 (1991)], should allow more accurate detection of HGBV-C viremic samples. TABLE 25 GB-C containing sera GB-C.5 Canada HA-AA 3 C 0.15 GB-C.6 U.S. history of C 1 1.51 + hepatitis GB-C.7 U.S . hepatitis A 0.26 0 1 Immunoreactivity detected to recombinant HGBV protein(s) from virus A, B or C. Sample to cutoff values reported. Values >1 (underlined) are considered positive. hepatitis associated aplastic anemia TABLE 27. Egyptian Serial Samples - Upper limit of normal: 45 U/l. 2 Sample to normal reported. Values >10 are considered positive. Example 21. Sequence Comparisons and Phylogentic Analysis Information about the degree of relatedness of virases can be obtained by performing comparisons, i.e. alignments, of nucleotide and predicted amino acid sequences. Performing alignments of the HGBV sequences with sequences of other virases can provide a quantitative assessment of the degree of similarity and identity between the sequences. This information can then be used to develop a rationale for the taxonomic classification of the HGBV virases. In general, the calculation of similarity between two amino acid sequences is based upon the degree of likeness exhibited between the side chains of an amino acid pair in an alignment. The degree of likeness is based upon the physical-chemical characteristics of the amino acid side chains, i.e. size, shape, charge, hydrogen- bonding capacity, and chemical reactivity, thus, similar amino acids possess side chains that have similar physical-chemical characteristics. For example, phenylalanine and tyrosine are amino acids containing aromatic side chains and are, therefore, regarded as chemically similar. A discussion of the chemistry of amino acids can be found in any basic biochemistry textbook, for example, Biochemistry. Third Edition, Lubert Stryer, Editor, W.H. Freeman and Company, New York, 1988. The calculation of identity between two aligned amino acid sequences is, in general, an arithmetic calculation which counts the number of identical pairs of amino acids in the alignment and divides this number by the length of the sequence(s) in the alignment. Analogous to the method used for amino acid sequence alignments, the determination of the degree of identity between two aligned nucleotide sequences is an arithmetic calculation which counts the number of identical pairs of nucleotide bases in the alignment and divides this number by the length of the sequence(s) in the alignment. The calculation of similarity between two aligned nucleotide sequences sometimes uses different values for transitions and transversions between paired (i.e. matched) nucleotides at various positions in the alignment; however, the magnitude of the similarity and identity scores between pairs of nucleotide sequences are usually very close, i.e. within one to two percent. As has been stated earlier, limited identity exists between amino acid sequences of the HGBV agents and hepatitis C genotypes. In order to more accurately determine the degree of relatedness between the HGBV agents and HCV, amino acid sequence alignments were performed using the sequence of the entire large open reading frame (ORF) of HGBV-A, B, and C, and the amino acid sequence of the large ORF of several representative HCV isolates. In addition, the degree of relatedness between the HGBV agents and HCV at the nucleotide level was determined using the entire genomic nucleotide sequence of HGBV-A, B, and C, and that of several representative HCV isolates. Alignment of the amino acid and nucleotide sequences was performed using the program GAP of the Wisconsin Sequence Analysis Package (Version 8) which is available from the Genetics Computer Group, Inc., 575 Science Drive, Madison, Wisconsin, 53711. The gap creation and gap extension penalties were 5.0 and 0.3, respectively, for nucleic acid sequence alignments, and 3.0 and 0.1, respectively, for amino acid sequence comparisons. The GAP program uses the algorithm of Needleman and Wunsch (J. Mol. Biol. 48:443-453, 1970) to calculate the degree of similarity and identity, expressed as percentages, between the two sequences being aligned. The nucleotide and amino acid sequences of selected members of the major hepatitis C viras (HCV) genotypes were obtained from GenBank and are shown below with their respective accession numbers: Results of pairwise comparisons of the predicted amino acid sequences of the large open reading frame (i.e. putative precursor polyprotein) and the nucleotide sequences between each of the above HCV genotypes and each of the HGBV isolates are shown in Tables 28 and 29, respectively. The genotype designation, which is based on the system of nomenclature for HCV isolates described by Simmonds P. et al (1994) Hepatologv. 19:1321-1324, of each of the HCV isolates are shown in the top row. The data shown in TABLE 28 demonstrate that the lower limit of amino acid sequence identity between the HCV genotypes is 69%. This value is very close to that shown by Simmonds et al. [Simmonds, P. et al. Hepatologv. 19:1321-1324, 1994] who reported that comparisons of the coding region (i.e. large open reading frame) of eight complete HCV genomes from two major groups showed amino acid sequence similarities of 67.1% to 68.6%; however, these authors did not describe the method by which the similarities were calculated. This value (69%) is also very close to the value of 71-84% identity reported by Okomoto et al., INirologv. 188:331-341, 1992] for comparisons of HCV-J8 with other major HCV isolates; however, these investigators did not describe the method by which the identities were calculated. Comparisons of the HGBV polyprotein sequences with each of the HCV genotypes reveals that the HGBV- encoded polyprotein sequences exhibit no more than 33% identity to any of the HCV polyproteins (TABLE 28). A comparison of the nucleotide sequences (TABLE 29) demonstrates a maximum sequence identity of 44.2% between any HGBV viras and any HCV isolate, whereas, the minimum nucleotide sequence identity between HCV isolates is 64.9%. Therefore, since HGBV-A, B, and C possess nucleotide and predicted amino acid sequence identity with HCV that is well outside the range of identities established for the known HCV genotypes, the HGBV virases cannot be considered genotypes of the hepatitis C virases. The relationship between the hepatitis C viruses and the hepatitis GB virases can be examined by performing phylogenetic analysis on their aligned nucleotide or deduced amino acid sequences (i.e. large open reading frames) or on a portion of these sequences. This approach has been applied to the hepatitis C viruses and showed that the variability of HCV isolates delineated six equally divergent main groups of sequences [Simmonds, P. et al., J. Gen. Virol. (1993) 74:2391-2399 and Simmonds, P. et al., J. Gen. Virol. (1994) 75: 1053-1061]. This analysis resulted in the establishment of a system of nomenclature for the hepatitis C virases [Simmonds, P. et al. Hepatologv. 19:1321-1324, 1994] where the isolates are classified into genotypes based upon the evolutionary distance between sequences. In order to determine the phylogenetic relationship between the hepatitis GB virases and the hepatitis C virases, alignments of amino acid sequences within the putative helicase gene of NS3 and the putative RNA-dependent RNA- polymerase (RdRp) of NS5B were performed. Also included in the alignments were related sequences from other virases in the Flaviviridae and virases that have been shown to possess evolutionary relatedness within their helicase or polymerase genes to members of the Flaviviridae [Koonin, EN. & Dolja, V.N. (1993) Crit. Rev. Biochem. Mol. Biol. 28, 375-430 and Koonin, EN. (1991) Gen. Virol. 72, 2179-2206] . The amino acid sequence alignments were made using the program PLLEUP of the Wisconsin Sequence Analysis Package (version 8). Phylogenetic distances between pairs of aligned sequences were determined using the PROTDIST program of the PHYLIP package (version 3.5c, 1993) kindly provided by J. Felsenstein [Felsenstein, J. (1989) Cladistics 5: 164-166]. These computed distances were used for the constraction of phylogenetic trees using the program NEIGHBOR (neighbor-joining setting). The trees were plotted using the program DRAWTREE. The trees shown are not rooted. The viral sequences used and their coπesponding GenBank accession numbers are shown in TABLES 31. The evolutionary distance between each HCV genotype and each of the HGBV virases for alignments made within the helicase, RdRp, or complete large open reading frame are presented below in TABLES 32, 33, and 34 respectively. The distances calculated between the HCV genotypes or the HGBV viruses and the other virases listed in TABLE 30 are not shown. The phylogenetic trees produced for amino acids alignments of the viral helicases, RdRps, or complete large open reading frames sequences are shown in FIGURES 42, 43 and 44, respectively. Amino acid sequence alignments of the putative RdRps, encoded within the NS5B region, of HGBV-A, B and C with the RdRp of several HCV genotypes, two of the pestivirases, several representative flavivirases, and several positive- strand RNA plant virases, show that they possess conserved sequence motifs associated with the RdRps of positive-strand RNA viruses (data not shown). Based on similar analyses, the HGBV-A and HGBV-B encoded helicases show significant identity with the helicases of these positive-strand RNA viruses (data not shown), with the exception of CARMV, TCV, and MNSV which presumably do not possess helicase genes [Guilley, H et al. (1985) Nucleic Acids Res. 13:6663-6677]. These results were not unexpected in view of the association of the helicase and RdRp genes of these virases into Supergroups demonstrated by previous phylogenetic analyses [Koonin, EN. & Dolja, V.V. (1993) Crit. Rev. Biochem. Mol. Biol. 28, 375-430]. However, examination of the phylogenetic distances between the HGBV isolates and the HCV isolates based upon alignment of the helicase or RdRp sequences (TABLES 30 and 31) demonstrates that there is considerable distance between the members of these two groups. The distances calculated demonstrate the close relationship among the HCV genotypes, where the maximum distance between any two genotypes is 0.3696 (RdRp distance). However, the distances calculated from the RdRp alignment between HGBV-A, -B, or -C and any member of the HCV group is 0.96042-1.46261. Similarly, the distances calculated from the helicase alignments for any two HCV genotype ranges from 0.044555-0.19706, while distances between any member of the HCV group and HGBV-A, -B, or -C ranges from 0.69130-0.87120. In addition, alignment of the predicted amino acid sequence of the entire large open reading frames of the HCV genotype and the GB virases demonstrates a narrow range of evolutionary distance for the HCV isolates (0.17918-0.39646) while the minimum distance between any GB viras and any HCV isolate is 1.68650. Thus, the hepatitis GB virases exhibit evolutionary distances that are clearly outside the range demonstrated for the hepatitis C viras genotypes. The phylogentic analysis of the HGBV and HCV sequences is attempting to answer the question, "How does the divergence of the HGBV sequences from the HCV sequences compare with the divergence among the HCV sequences? In particular, might it be that the HGBV sequences are no more diverged from HCV sequences than the HCV sequences are from one another?" A reasonable condition to be met, if the HGBV sequences were no more diverged from HCV sequences than HCV sequences are from one another, would be that the HGBV-A, HGB V- B, and/or HGBV-C sequences would be at least as close to one of the HCV sequences as the most distantly related pair of HCV sequences (i.e., the minimum distance from any HGBV sequence to any HCV sequence is less than or equal to the maximum observed distance among HCV sequences). This condition is not met by the present sequence data; in Table 31 (RdRp alignment), the minimum HCV-HGBV distance is 2.83 times the maximum HCV-HCV distance; and in Table 32 (helicase alignment), the minimum HCV-HGBV distance is 3.51 times the maximum HCV-HCV distance. Thus, the data do not support the idea that the HGBV sequences are members of a group whose diversity is delimited by previously characterized members of the HCV group. The distribution of these relative distances can be examined with a test based on the bootstrap [Efron, B. (1982) "The jackknife, the bootstrap,-and other resampling plans", Society Industrial and Applied Mathematics: Philadelphia; Efron, B. and Gong, G. (1983) "A leisurely look at the bootstrap, the jackknife, and cross-validation." Am. Stat. 37: 36-48]. The results obtained from the bootstrap sampling are shown in Table 32; which shows the comparison of the HCV-HGBV divergence (minimum of all HCV-HGBV distances) to the HCV diversity (maximum of all HCV-HCV distances) based on PAM distances as calculated using the PROTDIST program. In 1000 bootstrap resamplings of the columns in the sequence alignments, the greatest divergence among HCV sequences was never as large as the smallest of the divergences of the HGBV sequences from the HCV sequences (Table 32). Thus, in independent measurements based on alignments of coding regions from two separate genes, there was not a single instance in which the data were consistent with the HGBV sequences falling within the genetic sequence diversity of HCV genotypes. Leaning in the direction of a conservative estimate, there is less than one chance in 100,000 that the data for the HGBVs could be drawn from the same pool of sequences as the HCV sequences. TABLE 32 (a) Distances Determined from RdRp AlignmentAlignment Out of bootstrap 1000 samples: Average min(HCV-HGBV distance)/max(HCV-HCV distance) = 2.543645 +/- 0.367443 Minimum min(HCV-HGB V distance)/max(HC V-HC V distance) = 1.617575 (b) Distances Determined from Helicase Alignment Out of bootstrap 1000 samples: Average min(HCV-HGBV distance)/max(HCV-HCV distance) = 3.346040 +/- 0.511875 Minimum min(HCV-HGBV distance)/max(HCV-HCV distance) = 2.092055 Assuming that the HCV sequences utilized in this study are representative of the most divergent of the HCV genotypes, these results indicate that HGBV-A, B and C are not genotypes of HCV. In addition, it appears that HGBV-A and HGBV-C are more closely related to each other than either is to HGBV-B, which suggests that HGBV-A and HGBV-C may be representatives of a separate viral lineage. Similarly, HGBV-B may be the sole representative of its own viral lineage. The relative evolutionary distances between the viral sequences analyzed are readily apparent upon inspection of the unrooted phylogentic trees presented in Figures 45 and 46, where the branch lengths are proportional to the evolutionary distance. The close evolutionary relationship of the HCV virases is apparent and is consistent whether the analysis is performed using a portion of the encoded genomic sequence or the entire genome (FIGURE 44). The large degree of divergence between HGBV-A, HGBV-B, and HGBV-C and other Flaviviridae members demonstrate that, while being most closely related to the hepatitis C virases, the GB-agents cannot be considered genotypes of HCV and may actually be representatives of a new viras group, or groups, within the Flaviviridae. The present invention thus provides reagents and methods for determining the presence of HGBV-A, HGBV-B and HGBV-C in a test sample. It is contemplated and within the scope of the present invention that a polynucleotide or polypeptide (or fragment[s] thereof) specific for HGBV-A, HGBV-B and HGB V- C described herein, or antibodies produced from these polypeptides and polynucleotides, can be combined with commonly used assay reagents and incorporated into cuπent assay procedures for the detection of antibody to these virases. Alternatively, the polynucleotides or polypeptides specific for the HGBV- A, HGBV-B and HGBV-C (or fragment[s] thereof) described herein, or antibodies produced from such polypeptides and polynucleotides (or fragment[s] thereof), can be used separately for detection of the HGBV-A, HGBV-B and HGBV-C viruses. Other uses or variations of the present invention will be apparent to those of ordinary skill of the art when considering this disclosure. Therefore, the present invention is intended to be limited only by the appended claims. TABLE 2 T-1048 T-1053 T-1057 T-1061 30 o 27 13 CO 60.3 9.0 28.5 56.6 15.9 31.9 TABLE 5 CO 66.2 20.1 21.0 94.2 13.2 34.9 38.4 18.2 18.5 65.8 11.3 17.6 TABLE 8 23 369 bp ND ND ND 0/1 ND 1/1 + ND 50 337 bp ND neg. ND 0/1 0/1 1/1 + >7 kb - size of clone in base pairs (bp). b Southern blot analysis of tamarin.human, yeast and E. coli genomic DNA using GB clone sequence as a probe. Negative (neg.) indicates that clone did not hybridize with any of the genomic DNAs tested. c Genomic PCR was performed on tamarin, human yeast and E. coli DNAs with primers that amplify the cloned sequence. Neg. indidcates that the clone was not amplified from the DNA sources tested. d Tamarin plasmas, both pre-HGB V-inoculation (pre-inoc.) and acute phase (acute) were tested for the presence of cloned sequence by PCR (to detect DNA sequences) or RT-PCR (to detect RNA and DNA sequences). The results are reported as the number of PCR-positive samples per number of samples examined. e H205 was tested for the presence of the clones by RT-PCR. All clones were RT-PCR positive (+) in H205 source. f Northern blot analysis was performed on total liver RNA from normal tamarin liver and acute phase tamarin liver using radiolabel clone sequences. The estimated siz of the specific band detected in the acute phase liver RNA is given. 8 ND: not determined. ♦ Cutoff was determined: 0.4 x N/Cx + 0.6 x P/Cx ** Cutoff was determined: N/Cx + P/Cx / 2 *** Cutoff was determined: N/Cx + 25% P/C **** Cutoff was determined: S/N > 6 TABLE -.14 HGBV-A Samples e a PCR product is as indicated in Table 9, Table 10, or Example 13. ''Restriction digests used to liberate the PCR fragment from pT7Blue T- vector or for direct digestion of 4.2 PCR product. ND = not done. 164 Table 16 SEROLOGIC RESULTS HGBV- B POS/TO AL TABLE 1 7 HGBV-B Serological Results Repeatably Negative In X2* SIG ** Reactive 1.4, 1.7 or 1.4, 1.7 or 4.1 ELISA 4.1 ELISA 97* NS * 999 ??? * 999* ???* 999* 999* NS* NS* ??? 999? NS* 99? Assumed High Risk 191 1321 •?? Non A-E Hepatitis 21 431 - NS* Chi square value obtained by applying the Chi square test. Determination of statistical signficance based upon the Chi square analysis. ^Not statistically significant by the Chi square test. "Statistically signficant by the Chi square test, with p<0.050. Table 18- SEROLOGIC RESULTS - TABLE A POS/TOTAL * Separate ELISA's were developed and cutoffs determined ** Not Done TABLE..19HGBV-A Serolo g ical Results X2* ** SIG NS* NS ??? * 999* NS 5 NS 5 999* ??? 999 Assumed Low Risk 1 200 Paid Blood Donors 0 760 NS* Assumed High Risk 93 1319 ???• Non A-E Hepatitis 13 300 99999* Chi square value obtained by applying the Chi square test Determination of statistical signficance based upon the Chi square analysis. 'Not statistically significant by the Chi square test. 'Statistically signficant by the Chi square test, with p<0.050. 168 Table 23 SEROLOGIC RESULTS HGBV-C POS/TOTAL TABLE 24 HGBV-C Serological Results X2* ** SIG NS* NS* ???? NS* NS* NS* ???? ???? ??? NS* ??? Assumed High Risk 191 1330 ???• Non A-E Hepatitis 21 303 999* Chi square value obtained by applying the Chi square test. Determination of statistical signficance based upon the Chi square analysis. tNot statistically significant by the Chi square test. 'Statistically signficant by the Chi square test, with p<0.050. TABLE 2 . Nucleotide sequence identity across entire genomes (%) lb 2a 2b 3a JK1 J6 J8 K3A Tr 77.0 65.9 65.2 65.1 64.9 77.5 41.5 41.0 41.6 41.6 44.2 43.3 43.5 43.1 42.6 42.1 42.1 41.1 41.5 53.3 41.6 TABLE 30 GenBank Accession numbers TABLE 31 Evolutionary distances : RdRp sequences , HGBV-A HGBV-C HCV-J6 HCV-J8 HCV-1 HCV-JK1 HCV-3A HGBV-C 0.54878 HCV-J6 1.14632 1.43972 HCV-J8 1.16398 1.43043 0.11550 HCV-1 1.25705 1.36554 0.26824 0.26864 HCV-JK1 1.23506 1.46261 0.29041 0.29207 0.11347 HCV-3A 1.26876 1.40316 0.34880 0.36960 0.30535 0.35182 HGBV-B 1.14880 1.31596 1.00961 0.96402 1.07379 1.04486 1.01997 TABLE 32 Evolutionary distances : helecase sequences . HGBV-A HGBV-C HCV1 HCVJK1 HCVJ6 HCVJ8 HCV3A 0.73171 TABLE 33 Evolutionary distances: complete large open reading frames. HGBV-A HGBV-C HCVJ6 HCVJ8 HCV1 HCVJK1 HCV3A HGBV-C 0.92796 HCV-J6 2.41182 2.14894 HCV-J8 2.41162 2.16319 0.17918 HCV-1 2.38813 2.11644 0.35897 0.36481 HCV-JK1 2.40833 2.12664 ■ 0.36577 0.37948 0.17411 HCV-3A 2.44255 2.15842 0.38848 0.39646 0.32500 0.32271 HGBV-B 2.68767 2.47039 1.69983 1.68650 1.71216 1.71657 1.73779 SEQUENCE LISTING (1) GENERAL INFORMATION: (i) APPLICANT: JOHN N. SIMONS TAMI J. PILOT-MATIAS GEORGE J. DAWSON GEORGE G. SCHLAUDER SURESH M. DESAI THOMAS P. LEARY ANTHONY SCOTT MUERHOFF JAMES C. ERKER SHERI L. BUIJK ISA K. MUSHAHWAR (ii) TITLE OF INVENTION: NON-A, NON-B. NON-C, NON-D, NON-E HEPATITIS REAGENTS AND METHODS FOR THEIR USE (iii) NUMBER OF SEQUENCES: 720 (iv) CORRESPONDENCE ADDRESS: (A) ADDRESSEE: ABBOTT LABORATORIES D377/AP6D (B) STREET: ONE ABBOTT PARK ROAD (C) CITY: ABBOTT PARK (D) STATE: IL (E) COUNTRY: USA (F) ZIP: 60064-3500 (v) COMPUTER READABLE FORM: (A) MEDIUM TYPE: Floppy disk (B) COMPUTER: IBM PC compatible (C) OPERATING SYSTEM: PC-DOS/MS-DOS (D) SOFTWARE: Patentln Release #1.0, Version #1.25 (vi) CURRENT APPLICATION DATA: (A) APPLICATION NUMBER: (B) FILING DATE-. (C) CLASSIFICATION: (viii) ATTORNE /AGENT INFORMATION: (A) NAME: POREMBSKI, PRISCILLA E. (B) REGISTRATION NUMBER: 33,207 (C) REFERENCE/DOCKET NUMBER: 5527.PC01 (ix) TELECOMMUNICATION INFORMATION: (A) TELEPHONE: 708-937-6365 (B) TELEFAX: 708-938-2623 (2) INFORMATION FOR SEQ ID Nθ:l: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:l: AGCACTCTCC AGCCTCTCAC CGCA 24 (2) INFORMATION FOR SEQ ID NO:2: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 12 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:2: GATCTGCGGT GA 12 (2) INFORMATION FOR SEQ ID NO:3: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:3; AGGCAACTGT GCTATCCGAG GGAA 24 (2) INFORMATION FOR SEQ ID NO:4: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 12 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:4: GATCTTCCCT CG 12 (2) INFORMATION FOR SEQ ID NO:5: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (Xi) SEQUENCE DESCRIPTION: SEQ ID NO:5: ACCGACGTCG ACTATCCATG AACA 24 (2) INFORMATION FOR SEQ ID NO:6: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 12 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:6: GATCTGTTCA TG 12 (2) INFORMATION FOR SEQ ID NO:7: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 18 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:7: GGAATTCGCG GCCGCTCG 18 (2) INFORMATION FOR SEQ ID NO:8: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:8: CGAGCGGCCG CGAATTCCTT 20 (2) INFORMATION FOR SEQ ID NO:9: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:9: TTGACACCAG ACCAACTGGT AATG 24 (2) INFORMATION FOR SEQ ID NO:10: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:10: GGTGGCGACG ACTCCTGGAG CCCG 24 (2) INFORMATION FOR SEQ ID NO:11: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8912 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:11: TGAATTCGTG TGGGTTCGGT GGTGGTGGCG CTTTAGGCAG CCTCCACGCC CACCACCTCC 60 CAGATAGAGC GGCGGCACTG TAGGGAAGAC CGGGGACCGG TCACTACCAA GGACGCAGAC 120 CTCTTTTTGA GTATCACGCC TCCGGAAGTA GTTGGGCAAG CCCACCTAYA TGTGTTGGGA 180 TGGTTGGGGT TAGCCATCCA TACCGTACTG CCTGATAGGG TCCTTGCGAG GGGATCTGGG 240 AGTCTCGTAG ACCGTAGCAC ATGCCTGTTA TTTCTACTCA AACAAGTCCT GTACCTGCRC 300 CCAGAACGCG CAAGAACAAG CAGACGCAGG CTTCATATCC TGTGTCCATT AAAACATCTG 360 TTGAAAGGGG ACAACGAGCA ARGCGCAAAG TCCAGCGCGA TGCTCGGCCT CGTAATTACA 420 AAATTGCTGG TATCCATGAT GGCTTGCAGA CATTGGCTCA GGCTGCTTTR CCAGCTCATG 480 GTTGGGGACG CCAAGACCCT CGCCATAAGT CTCGCAATCT TGGAATCCTT CTGGATTACC 540 CTTTGGGGTG GATTGGTGAT GTTACAACTC ACACACCTCT AGTAGGCCCG CTGGTGGCAG 600 GAGCGGTCGT TCGACCAGTC TGCCAGATAG TACGCTTGCT GGAGGATGGA GTCAACTGGG 660 CTACTGGTTG GTTCGGTGTC CACCTTTTTG TGGTATGTCT GCTATYTTTG GCCTGTCCCT 720 GTAGTGGGGC GCGGGTCACT GACCCAGACA CAAATACCAC AATCCTGACC AATTGCTGCC 780 AGCGTAATCA GGTTATCTAY TGTTCTCCTT CCACTTGCCT ACACGAGCCT GGTTGTGTGA 840 TCTGTGYGGA CGAGTGCTGG GTTCCCGCCA ATCCRTACAT CTCACACCCT TCCAATTGGA 900 CTGGCACGGA CTCCTTCTTG GCTGACCACA TTGATTTTGT TATGGGCGCT CTTGTGACCT 960 GTGACGCCCT TGACATTGGT GAGTTGTGTG GTGCGTGTGT ATTAGTCGGT GACTGGCTTG 1020 TCAGGCACTG GCTTATTCAC ATAGACCTCA ATGAAACTGG TACTTGTTAC CTGGAAKTGC 1080 CTACTGGAAT AGATCCTGGG TTCCTAGGGT TTATCGGGTG GATGGCCGGC AAGGTCGAGG 1140 CTGTCATCTT CTTGACCAAA CTGGCTTCAC AAGTACCATA CGCTATTGCG ACTATGTTTA 1200 GCAGTGTACA CTACCTGGCG GTTGGCGCTC TGATCTACTA YGCCTCTCGG GGCAAGTGGT 1260 ATCAGTTGCT CCTAGCGCTT AYGCTTTACA TAGAAGCGAC CTCTGGAAAC CCYATCAGGG 1320 TGCCCACTGG ATGCTCAATA GCTGAGTTTT GCTCGCCTTT GATGATACCA TGTCCTTGCC 1380 ACTCTTATTT GAGTGAGAAT GTGTCAGAAG TCATTTGTTA CAGTCCAAAG TGGACCAGGC 1440 CTGTCACTCT AGAGTATAAB AACTCCATAT CTTGGTACCC CTATACAATC CCTGGTGCGA 1500 GGGGATGTAT GGTTAAATTC AAAAATAACA CATGGGGTTG CTGCCGWWTC GCAATGTGCC 1560 ATCGTACTGC ACTATGGGCA CTGATGCAGT GTGGAASSAC AGTCGCAACA CTTACGAAGC 1620 ATGCGGTGTA ACACCATGGC TAACAACCGC ATGGCACAAC GGCTCAGCCC TGAAATTGGC 1680 TATATTACAA TACCCTGGGT CTAAAGAAAT GTTTAAACCT CATAATTGGA TGTCAGGCCA 1740 CTTGTATTTT GAGGGATCAG ATACCCCTAT AGTTTACTTT TATGACCCTG TGAATTCCAC 1800 TCTCCTACCA CCGGAGAGGT GGGCTAGGTT GCCCGGTACC CCACCTGTGG TACGTGGTTC 1860 TTGGTTACAG GTTCCGCAAG GTTTTACAGT GATGTGAAAG ACCTAGCCAC AGGATTGATC 1920 ACCAAAGACA AAGCCTGGAA AAATTATCAG YTCTTATATT CCGCCACGGG TGCTTTGTCT 1980 CTTACGGGAG TTACCACCAA GGCCGTGGTG CTAATTCTGT TGGGGTTGTG TGGCAGCAAG 2040 TATCTTATTT TAGCCTACCT CTGTTACTTG TCCCTTTGTT TTGGGCGCGC TTCTGGTTAC 2100 MCTTTGCGTC CTGTGCTCCC ATCCCAGTCG TATCTCCAAG CTGGCTGGGA TGTTTTGTCT 2160 AAAGCTCAAG TAGCTCMTTT TGCTTTGATT TTCTTCATCT GTTGCTATCT CCGCTGCAGG 2220 CTACGTTATG CTGCCCTTTT AGGGTTTGTG CCCATGGCTG CGGGCTTGCC CCTAACTTTC 2280 TTTGTTGCAG CAGCTGCTGC CCAACCAGAT TATGACTGGT GGGTGCGACT GCTAGTGGCA 2340 GGGTTAGTTT TGTGGGCCGG CCGTGACCGT GGTCACGCAT AGCTCTGCTT GTAGGTCCTT 2400 GGCCTCTGGT AGCGCTTTYT AACCCTCTTG CATTTSSTKA CGCCTGCTTA GCTTTTGACA 2460 CCGAGATAAT TGGAGGGCTG ACAATACCAC CTGTAGTAGC ATTAGTTGTC ATGTCTCGTT 2520 TTGGCTTCTT TGCTCACTTG TTACCTCGCT GTGCTTTAGT TAACTCCTAT CTTTGGCAAC 2580 GTTGGGAGAA TTGGTTTTGG AACGTTACAC TAAGACCGGA GAGGTTTCTC CTTGYGCTGG 2640 TTTGTTTCCC CGGTGCGACA TATGACGTGC TGGTGACWTT CTGTGTGTGT CACGTAGCTC 2700 TTCTATGTTT AACATCCAGT GCAGCAYMGT TCTTTGGGAC TGACTCTAGG GTTAGGGCCC 2760 ATAGAATGTT GGTGCGTCTC GGAAAGTGTC ATGCTTGGTA TTCTCATTAT GTTCTTAAGT 2820 TTTTCCTCTT AGTGTTTGGT GAGAATGGTG TGTTTTTCTA KAAGCACTTG CATGGTGATG 2880 TCTTGCCTAA TGATTTTGCC TCGAAACTAC CATTGCAAGA GCCATTTTTC CCTTTTGAAG 2940 GCAAGGCAAG GGTCTATAGG AATGAAGGAA GACGCTTGGS KKGTGGGGAC ACGGTTGATG 3000 GTTTGSSCGT TGTBGCGCGT CTCGGCGACC TTGTTTTCGC AGGGTTAGCT ATGCCGCCAG 3060 ATGGGTGGGC CATTACCGCA CCTTTTACGC TGCAGTGTCT CTCTGAACGT GGCACGCTGT 3120 CAGCGATGGC AGTGGTCATG ACTGGTATAG ACCCCCGAAC TTGGACTGGA ACTATCTTCA 3180 GATTAGGATC TCTGGCCACT AGCTACATGG GATTTGTTTG TGACAACGTG TTGAATACTG 3240 CTCACCATGG CAGCAACGGG GGCCGGTTGG CTCATCCCAC AGGCTCCATA CACCCAATAA 3SO0 CCGTTGACGC GGCTAATGAC CAGGACATCT ATCAACCACC ATGTGGAGCT GGGTCCCTTA 3360 CTCGGTGCTC TTGCGGGGAG ACCAAGGGGT ATCTGGTAAC ACGACTGGGG TCATTGGTTG 3420 AGGTCAACAA ATCCGATGAC CCTTATTGGT GTGTGTGCGG GGCCCTTCCC ATGGCTGTTG 3480 CCAAGGGTTC TTCAGGTGCC CCGATTCTGT GCTCCTCCGG GCATGTTATT GGGATGTTCA 3540 CCGCTGCTAG AAATTCTGGC GGTTCAGTCG GCCAGATTAG GGTTAGGCCG TTGGTGTGTG 3600 CTGGATACCA TCCCCAGTAC ACAGCACATG CCACTCTTGA TACAAAACCT ACTGTGCCTA 3660 ACGAGTATTC AGTGCAAATT TTAATTGCCC CCACTGGCAG CGGCAAGTCA ACCAAATTAC 3720 CACTTTCTTA CATGCAGGRG AAGYATGAGG TCTTGGTCCT AAATCCCAGT GTGGCTACAA 3780 CAGCATCAAT GCCAAAGTAC ATGCACGCGA CGTACGGCGT GAATCCAAAT TGCTATTTTA 3840 ATGGCAAATG TACCAACACA GGGGCTTCAC TTACGTACAG CACATATGGC ATGTACCTGA 3900 CCGGACGATG TTCCCGGAAC TATGATGTAA TCATTTGTGA CGAATGCCAT GCTACCGATC 3960 GAACCACCGT GTTGGGCATT GGAAAGGTCC TAACCGAAGC TCCATCCAAA AATGTTAGGC 4020 TAGTGGTTCT TGCCACGGCT ACCCCCCCTG GAGTAATCCC TACACCACAT GCCAACATAA 4080 CTGAGATTCA ATTAACYGAT GAAGGCACTA TCCCCTTTCA TGGAAAAAAG ATTAAGGAGG 4140 AAAATCTGAA GAAAGGGAGA CACCTTATCT TTGAGGCTAC CAAAAAACAC TGTGATGAGC 4200 TTGCTAACGA GTTAGCTCGA AAGGGAATAA CAGCTGTCTC TTACTATAGG GGATGTGACA 4260 TCTCAAAAAT GCCTGAGGGC GACTGTGTAG TAGTTGCCAC TGATGCCTTG TGTACAGGGT 4320 ACACTGGTGA CTTTGATTCC GTGTATGACT GCAGCCTCAT GGTAGAAGGC ACATGCCATG 4380 TTGACCTTGA CCCTACTTTC ACCATGGGTG TTCGTGTGTG CGGGGTTTCA GCAATAGTTA 4440 AAGGCCAGCG TAGGGGCCGC ACAGGCCGTG GGAGAGCTGG CATATACTAC TATGTAGACG 4500 GGAGTTGTAC CCCTTCGGGT ATGGTTCCTG AATGCAACAT TGTTGAAGCC TTCGACGCAG 4560 CCAAGGCATG GTATGGTTTG TCATCAACAG AAGCTCAAAC TATTCTGGAC ACCTATCGCA 4620 CCCAACCTGG GTTACCTGCG ATAGGAGCAA ATTTGGACGA GTGGGCTGAT CTCTTTTCTA 4680 TGGTCAACCC CGAACCTTCA TTTGTCAATA CTGCAAAAAG AACTGCTGAC AATTATGTTT 4740 TGTTGACTGC AGCCCAACTA CAACTGTGTC ATCAGTATGG CTATGCTGCT CCCAATGACG 4800 CACCACGGTG GCAGGGAGCC CGGCTTGGGA AAAAACCTTG TGGGGTTCTG TGGCGCTTGG 4860 ACGGCTGTGA CGCCTGTCCT GGCCCAGAGC CCAGCGAGGT GACCAGATAC CAAATGTGCT 4920 TCACTGAAGT CAATACTTCT GGGACAGCCG CACTCGCTGT TGGCGTTGGA GTGGCTATGG 4980 CTTATCTAGC CATTGACACT TTTGGCGCCA CTTGTGTGCG OCGTTGCTGG TCTATTACAT 5040 CAGTCCCTAC CGGTGCTACT GTCGCCCCAG TGGTTGACGA AGAGGAAATC.GTGGAGGAGT 5100 GTGCATCATT CATTCCCTTG GAGGCCATGG TTGCTGCAAT TGACAAGCTG AAGAGTACAA 5160 TCACCACAAC TAGTCCTTTC ACATTGGAAA CCGCCCTTGA AAAACTTAAC ACCTTTCTTG 5220 GGCCTCATGC AGCTACAATC CTTGCTATCA TAGAGTATTG CTGTGGCTTA GTCACTTTAC 5280 CTGACAATCC CTTTGCATCA TGCGTGTTTG CTTTCATTGC GGGTATTACT ACCCCACTAC 5340 CTCACAAGAT CAAAATGTTC CTGTCATTAT TTGGAGGCGC AATTGCGTCC AAGCTTACAG 5400 ACGCTAGAGR CGCACTGGCG TTCATGATGG CCGGGGCTGY GGGAACAGCT CTTGGTACAT 5460 GGACATCGGT GGGTTTTGTC TTTGACATGC TAGGCGGCTA TGCTGGCGCC TCATCCACTG 5520 CTTGCTTGAC ATTTAAATGC TTGATGGGTG AGTGGCYCAC TATGGATCAG CTTGCTGGTT 5580 TAGTCTACTC CGCGTTCAAT CCGGCCGCAG GAGTTGTGGG CGTCTTGTCA GCTTGTGCAA 5640 TGTTTGCTTT GACAACAGCA GGGCCAGATC ACTGGCCCAA CAGACTTCTT ACTATGCTTG 5700 CTAGGAGCAA CACTGTATGT ARTGAGTACT TTATTGCCAC TCGTGACATC CGCAGGAAGA 5760 TACTGGGCAT TCTGGAGGCA TCTACCCCCT GGAGTRTCAT ATCAGCTTGC ATCCGTTGGC 5820 TYCACACCCC GACGGAGGAT GATTGCGGCC TCATTGCTTG GGGTCTARAG ATTTGGCAGT 5880 ATGTGTGCAA TTTCTTTGTG ATTTGCTTTA ATGTCCTTAA AGCTGGAGTT CAGAGCATGG 5940 TTAACATTCC TGGTTGTCCT TTCTACAGCT GCCAGAAGGG GTACAAGGGC CCCTGGATTG 6000 GATCAGGTAT GCTCCAAGCA CGCTGTCCAT GCGGTGCTGA ACTCATCTTT TCTGTTGAGA 6060 ATGGTTTTGC AAAACTTTAC AAAGGACCCA GAACTTGTTC AAATTACTGG AGAGGGGCTG 6120 TTCCAGTCAA CGCTAGGCTG TGTGGGTCGG CTAGACCGGA CCCAACTGAT TGGACTAGTC 6180 TTGTCGTCAA TTATGGCGTT AGGGACTACT GTAAATATGA GAAATTGGGA GATCACATTT 6240 TTGTTACAGC AGTATCCTCT CCAAATGTCT GTTTCACCCA GGTGCCCCCA ACCTTGAGAG 6300 CTGCAGTGGC CGTGGACCGC GTACAGGTTC AGYGTTATCT AGGTGAGCCC AAAACTCCTT 6360 GGACGACATC TGCTTGCTGT TACGGTCCTG ACGGTAAGGG TAAAACTGTT AAGCTTCCCT 6420 TCCGCGTTGA CGGACACACA CCTGGTGGTC GCATGCAACT TAATTTGCGT GATCGACTTG 6480 AGGCAAATGA CTGTAATTCC ATAAACAACA CTCCTAGTGA TGAAGCCGCA GTGTCCGCTC 6540 TTGTTTTCAA ACAGGAGTTG CGGCGTACAA ACCAATTGCT TGAGGCAATT TCAGCTGGCG 6600 TTGACACCAC CAAACTGCCA GCCCCCTCCC AGATCGAAGA GGTAGTGGTA AGAAAGCGCC 6660 AGTTCCGGGC AAGAACTGGT TCGCTTACCT TGCCTCCCCC TCCGAGATCC GTCCCAGGAG 6720 TGTCATGTCC TGAAAGCCTG CAACGAAGTG ACCCGTTAGA AGGTCCTTCA AjCCTCCCTT 6780 CTTCACCACC TGTTCTRCAG TTGGCCATGC CGATGCCCCT GTTGGGAGCA GGTGAGTGTA 6840 ACCCTTTCAC TGCAATTGGA TGTGCAATGA CCGAAACARG YGGAGKCCCl MAKRATTTAC 6900 CCAGTTACCC TCCCAAAAAG GAGGTCTCTG AATGGTCAGA CGAAAGTTGG TCAACGACTA 6960 CAACCGCTTC CAGCTACGTT ACTGGCCCCC CGTACCCTAA GATACGGGGC AAGGATTCCA 7020 CTCAATCAGC CACCGCCAAA CGGCCTACAA AAAAGAAGTT GGGAAAGAGT GAGTTTTCGT 7080 GCAGCATGAG CTACACTTGG ACCGACGTGA TTAGCTTCAA AACTGCTTCT AAAGTTCTGT 7140 CTGCAACTCG GGCCATCACT AGTGGTTTCC TCAAACAAAG ATCATTGGTG TATGTGACTG 7200 AGCCGCGGGA TGCGGAGCTT AGAAAACAAA AAGTCACTAT TAATAGACAA CCTCTGTTCC 7260 CCCCATCATA CCACAAGCAA GTGAGATTGG CTAAGGAAAA AGCTTCAAAA GTTGTCGGTG 7320 TCATGTGGGA CTATGATGAA GTAGCAGCTC ACACGCCCTC TAAGTCTGCT AAGTCCCACA 7380 TCACTGGCCT TCGGGGCACT GATGTTCGTT CTGGAGCGGC CCGCAAGGCT GTTCTGGACT 7440 TGCAGAAGTG TGTCGAGGCA GGTGAGATAC CGAGTCATTA TCGGCAAACT GTGATAGTTC 7500 CAAAGGAGGA GGTCTTCGTG AAGACCCCCC AGAAACCAAC AAAGAAACCC CCAAGGCTTA 7560 TCTCGTACCC CCACCTTGAA ATGAGATGTG TTGAGAAGAT GTACTACGGT CAGGTTGCTC 7620 CTGACGTAGT TAAAGCTGTC ATGGGAGATG CGTACGGGTT TGTAGATCCA CGTACCCGTG 7680 TCAAGCGTCT GTTGTCGATG TGGTCACCCG ATGCAGTCGG AGCCACATGC GATACAGTGT 7740 GTTTTGACAG TACCATCACA CCCGAGGATA TCATGGTGGA GACAGACATC TACTCAGCAG 7800 CTAAACTCAG TGACCAACAC CGAGCTGGCA TTCACACCAT TGCGAGGCAG TATCACGCTG 7860 GAGGACCGAT GATCGCTTAT GATGGCCGAG AGATCGGATA TCGTAGGTGT AGGTCTTCCG 7920 GCGTCTATAC TACCTCAAGT TCCAACAGTT TGACCTGCTG GCTGAAGGTA AATGCTGCAG 7980 CCGAACAGGC TGGCATGAAG AACCCTCGCT TCCTTATTTG CGGCGATGAT TGCACCGTAA 8040 TTTGGAAGAG CGCCGGAGCA GATGCAGACA AACAAGCAAT GCGTGTCTTT GCTAGCTGGA 8100 TGAAGGTGAT GGGTGCACCA CAAGATTGTG TGCCTCAACC CAAATACAGT TTGGAAGAAT 8160 TAACATCATG CTCATCAAAT GTTACCTCTG GAATTACCAA AAGTGGCAAG CCTTACTACT 8220 TTCTTACAAG AGATCCTCGT ATCCCCCTTG GCAGGTGCTC TGCCGAGGGT CTGGGATACA 8280 ACCCCAGKGC KGCGTGGATT GGGTATCTAA TACATCACTA CCCATGTTTG TGGGTTAGCC 8340 GTGTGTTGGC TGTCCATTTC ATGGAGCAGA TGCTCTTTGA GGACAAACTT CCCGAGACTG 8400 TGACCTTTGA CTGGTATGGG AAAAATTATA CGGTGCCTGT AGAAGATCTG CCCAGCATCA 8460 TTGCTGGTGT GCACGGTATT GAGGCTTTCT CGGTGGTGCG CTACACCAAC GCTGAGATCC 8520 TCAGAGTTTC CCAATCACTA ACAGACATGA CCATGCCCCC CCTGCGAGCC TGGCGAAAGA 8580 AAGCCAGGGC GGTCCTCGCC AGCGCCAAGA GGCGTGGCGG AGCACACGAA AATTGGCTCG 8640 CTTCCTTCTC TGGCATGCTA CATCTAGACC TCTACCAGAT TTGGATAAGA CGAGCGTGGC 8700 TCGGTACACC ACTTTCAATT ATTGTGATGT TTACTCCCSG AGRGGGATGT GTTTATTACA 8760 CCACAGAGAA GATTGCAGAA GTTTCTTGTG AAGTATTTGG CTGTCATTGT TTGTGCCCTA 8820 GGGCTCATTG CTGTTGGACT AGCCATCAGC TGAACCCCCA AATTCAAAAT TAATTAACAG 8880 TTTTTTTTTT TTTTTTTTTT TTTTTTTAGG GC 8912 (2) INFORMATION FOR SEQ ID NO:12: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 197 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:12: GAGTGTAACC CTTTCACTGC AATTGGATGT GCAATGACCG AAACAGGCGG AGGCCCTGAT 60 GATTTACCCA GTTACCCTCC CAAAAAGGAG GTCTCTGAAT GGTCAGACGA AAGTTGGTCA 120 ACGACTACAA CCGCTTCCAG CTACGTTACT GGCCCCCGTA CCCTAAGATA CGGGAAAGGA 180 TTCCACTCAA TTAGCCC 197 (2) INFORMATION FOR SEQ ID NO:13: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 207 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:13: CCTCGACACA CTTCTGCAAG TCCAGAACAG CCTTGCGGGC TGCTCCAGAA CGAACATCAG 60 TGCCCCGAAG CCAGTGATGT GGGACTTAGC AGACTTAGAG GGCGTGTGAG CTGCTACTTC 120 ATCATAGTCC CACATGACAC CGACAACTTT TGAAGCTTTT TCCTTAGCCA ATCTCACTTG -180 CTTGTGGTAT GATGGGGGGA ACAGAGG 207 (2) INFORMATION FOR SEQ ID NO:14: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 208 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:14: Glu Cys Asn Pro Phe Thr Ala He Gly Cys Ala Met Thr Glu Thr Xaa 1 5 10 15 Gly Xaa Xaa Xaa Xaa Leu Pro Ser Tyr Pro Pro Lys Lys Glu Val Ser 20 25 30 Glu Trp Ser Asp Glu Ser Trp Ser Thr Thr Thr Thr Ala Ser Ser Tyr 35 40 45 Val Thr Gly Pro Pro Tyr Pro Lys He Arg Gly Lys Asp Ser Thr Gin 50 55 60 Ser Ala Thr Ala Lys Arg Pro Thr Lys Lys Lys Leu Gly Lys Ser Glu 65 70 75 80 Phe Ser Cys Ser Met Ser Tyr Thr Trp Thr Asp Val He Ser Phe Lys 85 90 95 Thr Ala Ser Lys Val Leu Ser Ala Thr Arg Ala He Thr Ser Gly Phe 100 105 110 Leu Lys Gin Arg Ser Leu Val Tyr Val Thr Glu Pro Arg Asp Ala Glu 115 120 125 Leu Arg lys Gin Lys Val Thr He Asn Arg Gin Pro Leu Phe Pro Pro 130 135 140 Ser Tyr His Lys Gin Val Arg Leu Ala Lys Glu Lys Ala Ser Lys Val 145 150 155 160 Val Gly Val Met Trp Asp Tyr Asp Glu Val Ala Ala His Thr Pro Ser 165 170 175 Lys Ser Ala Lys Ser His He Thr Gly Leu Arg Gly Thr Asp Val Arg 180 185 190 Ser Gly Ala Ala Arg Lys Ala Val Leu Asp Leu Gin Lys Cys Val Glu 195 200 205 (2) INFORMATION FOR SEQ ID NO:15: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 230 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO-.15: GGTTCCTGAA TGCAACATTG TTGAAGCCTT CGACGCAGCC AAGGCATGGT ATGGTTTGTC 60 ATCAACAGAA GCTCAAACTA TTCTGGACAC CTATCGCACC CAACCTGGGT TACCTGCGAT 120 AGGAGCAAAT TTGGACGAGT GGGCTGATCT CTTTTCTATG GTCAACCCCG AACCTTCATT 180 TGTCAATACT GCAAAAAGAA CTGCTGACAA TTATGTTTTG TTGACTGCAG 230 (2) INFORMATION FOR SEQ ID NO:16: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 76 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:16: Val Pro Glu Cys Asn He Val Glu Ala Phe Asp Ala Ala Lys Ala Trp 5 10 15 Tyr Gly Leu Ser Ser Thr Glu Ala Gin Thr He Leu Asp Thr Tyr Arg 20 25 30 Thr Gin Pro Gly Leu Pro ' Ala He Gly Ala Asn Leu Asp Glu Trp Ala 35 40 45 Asp Leu Phe Ser Met Val Asn Pro Glu Pro Ser Phe Val Asn Thr Ala 50 55 60 Lys Arg Thr Ala Asp Asn Tyr Val Leu Leu Thr Ala 65 70 75 (2) INFORMATION FOR SEQ ID NO:17: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 291 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:17: GTATGGTTCC TGAATGCAAC ATTGTTGAAG CCTTCGACGC AGCCAAGGCA TGGTATGGTT 60 TGTCATCAAC AGAAGCTCAA ACTATTCTGG ACACCTATCG CACCCAACCT GGGTTACCTG 120 CGATAGGAGC AAATTTGGAC GAGTGGGCTG ATCTCTTTTC TATGGTCAAC CCCGAACCTT 180 CATTTGTCAA TACTGCAAAA AGAACTGCTG ACAATTATGT TTTGTTGACT GCAGCCCTGC 240 CACCGTGGTG CGTCATTGGG AGCAGCATAG CCATACTGAT GACACAGTTG T 291 (2) INFORMATION FOR SEQ ID NO:18: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 281 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:18: GCGCATGCAA CTTAATTTGC GTGATGCACT TGAGACAAAT GACTGTAATT CCATAAACAA 60 CACTCCTAGT GATGAAGCCG CAGTGTCCGC TCTTGTTTTC AAACAGGAGT TGCGGCGTAC 120 AAACCAATTG CTTGAGGCAA TTTCAGCTGG CGTTGACACC ACCAAACTGC CAGCCCCCTC 180 CATCGAAGAG GTAGTGGTAA GAAAGCGCCA GTTCCGGGCA AGAACTGGTT CGCTTACCTT 240 GCCTCCCCCT CCGAGATCCG TCCCAGGAGT GTCATGTCCT G 281 (2) INFORMATION FOR SEQ ID NO:19: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 93 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:19: Arg Met Gin Leu Asn Leu Arg Asp Ala Leu Glu Thr Asn Asp Cys Asn 1 5 10 15 Ser He Asn Asn Thr Pro Ser Asp Glu Ala Ala Val Ser Ala Leu Val 20 25 30 Phe Lys Gin Glu Leu Arg Arg Thr Asn Gin Leu Leu Glu Ala He Ser 35 40 45 Ala Gly Val Asp Thr Thr Lys Leu Pro Ala Pro Ser He Glu Glu Val 50 55 60 Val Val Arg Lys Arg Gin Phe Arg Ala Arg Thr Gly Ser Leu Thr Leu 65 70 75 80 Pro Pro Pro Pro Arg Ser Val Pro Gly Val Ser Cys Pro 85 90 (2) INFORMATION FOR SEQ ID NO:20: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 281 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:20: GCGCATGCAA CTTAATTTGC GTGATGCACT TGAGACAAAT GACTGTAATT CCATAAACAA 60 CACTCCTAGT GATGAAGCCG CAGTGTCCGC TCTTGTTTTC AAACAGGAGT TGCGGCGTAC 120 AAACCAATTG CTTGAGGCAA TTTCAGCTGG CGTTGACACC ACCAAACTGC CAGCCCCCTC 180 CATCGAAGAG GTAGTGGTAA GAAAGCGCCA GTTCCGGGCA AGAACTGGTT CGCTTACCTT 240 GCCTCCCCCT CCGAGATCCG TCCCAGGAGT GTCATGTCCT G 281 (2) INFORMATION FOR SEQ ID NO:21: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 221 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:21: GATCCATAGT GAGCCACTCA CCCATCAAGC ATTTAAATGT CAAGCAAGCA GTGGATGAGG 60 CGGCAGCATA GCCGCCTAGC ATGTCAAAGA CAAAACCCAC CGATGTCCAT GTACCAAGAG 120 CTGTTCCCAC AGCCCCGGCC ATCATGAACG CCAGTGCGTC TCTAGCGTCT GTAAGCTTGG 180 ACGCAATTGC GCCTCCAAAT AATGACAGGA ACATTTTGAT C 221 (2) INFORMATION FOR SEQ ID NO:22: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 737 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:22: GATCGAAGCA CACCTCAAGC CCTAAGACGC TGTGTCGCTC CCGGGTTACC CCGCAGCTAC 60 CACCAATACC AGCGGCAGAC GACCCCTTGC GAAGTGCATC GCCACAAGCA CGGCAGCCCT 120 CACAGAGCCC AGGACATTCA GGTACGCCAC GACACACATC ACACCCAGAC AACCAGTGAA 180 CCACCACTCC TGGGCTGCCC AGCCGACCAC CGGGGCGCAC ACCAGCTCGG GAGCCAGCGC 240 GCCTCGACGA CCGGCAAGTA AGCCCCAACA TTTGACAACC AGGCCAGACC GGCAGCGAAC 300 GTTCGCAGCT TGAGCCACGC GGGCCAGATG TCACCAACGA CGGCCTGAGC ACCATCATTG 360 GCAGCACCCC AGACCGCCTG AGCCCCGGCC GTCAGGCCTG CCACCATGTA GCAACCAGCA 420 TTGTAGGTAG AGTCCGCGAC TCCGGTGGTA GAATTCGGAC AAGATGGAGT TGGAACAGTG 480 GGCGGAGTCC ACAATGGAAC ACTTTCAGTG GACTTCGTGA CAGAAGGGTG TATGATAACA 540 ATAGTGGCGG CAGATGCTCC ATTCAACCAC CACCACATTG CCAGCATAAA CAGGGGGGCA 600 ACTCTAGCCT CAGCCAACTT CATCACTACC AACAGGGCCA GGACCATGTC AGTAAGCAAC 660 CAAGCCGCGG AAGACCTTCG CTGACCACTG TAAACCTGCT GTCTGTTGCC TTTAACATGG 720 ATGAAGCCGT TGTGATC 737 (2) INFORMATION FOR SEQ ID NO:23: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 307 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:23: GATCACTGTG GACGCCACTT GTTTCGACTC ATCGATTGAT GAGCACGATA TGCAGGTGGA 60 GGCCTCGGTG TTTGCGGCGG CTAGTGACAA CCCCTCAATG GTACATGCTT TGTGCAAGTA 120 CTACTCTGGT GGCCCTATGG TTTCCCCAGA TGGGGTTCCC TTGGGGTACC GCCAGTGTAG 180 GTCGTCGGGC GTGTTGACAA CTAGCTCGGC GAACAGCATC ACTTGTTACA TTAAGGTCAG 240 CGCGGCCTGC AGGCGGGTGG GGATTAAGGC ACCATCATTC TTTATAGCTG GAGATGATTG 300 CTTGATC 307 (2) INFORMATION FOR SEQ ID NO:24: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 500 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:24: GATCAGGCCG CTGAGCGGCC GAGAAGGTTA CAATCTGGAG GGGTGATAGG AAGTATGACA 60 AGCATTATGA GGCTGTCGTT GAGGCTGTCC TGAAAAAGGC AGCCGCGACG AAGTCTCATG 120 GCTGGACCTA TTCCCAGGCT ATAGCTAAAG TTAGGCGCCG AGCAGCCGCT GGATACGGCA 180 GCAAGGTGAC CGCCTCCACA TTGGCCACTG GTTGGCCTCA CGTGGAGGAG ATGCTGGACA 240 AAATAGCCAG GGGACAGGAA GTTCCTTTCA CTTTTGTGAC CAAGCGAGAG GTTTTCTTCT 300 CCAAAACTAC CCGTAAGCCC CCAAGATTCA TAGTTTTCCC ACCTTTGGAC TTCAGGATAG 360 CTGAAAAGAT GATTCTGGGT GACCCCGGCA TCGTTGCAAA GTCAATTCTG GGTGACGCTT 420 ATCTGTTCCA GTACACGCCC AATCAGAGGG TCAAAGCTCT GGTTAAGGCG TGGGAGGGGA ' 480 AGTTGCATCC CGCTGCGATC 500 (2) INFORMATION FOR SEQ ID NO:25: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 479 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:25: GATCACATTT TTGTTACAGC AGTATCCTCT CCAAATGTCT GTTTCACCCA GGTGCCCCCA 60 ACCTTGAGAG CTGCAGTGGC CGTGGACCGC GTACAGGTTC AGYGTTATCT AGGTGAGCCC 120 AAAACTCCTT GGACGACATC TGCTTGCTGT TACGGTCCTG ACGGTAAGGG TAAAACTGTT 180 AAGCTTCCCT TCCGCGTTGA CGGACACACA CCTGGTGGTC GCATGCAACT TAATTTGCGT 240 GATCGACTTG AGGCAAATGA CTGTAATTCC ATAAACAACA CTCCTAGTGA TGAAGCCGCA 300 GTGTCCGCTC TTGTTTTCAA ACAGGAGTTG CGGCGTACAA ACCAATTGCT TGAGGCAATT 360 TCAGCTGGCG TTGACACCAC CAAACTGCCA GCCCCCTCCC AGATCGAAGA GGTAGTGGTA 420 AGAAAGCGCC AGTTCCGGGC AAGAACTGGT TCGCTTACCT TGCCTCCCCC TCCGAGATC 479 (2) INFORMATION FOR SEQ ID NO:26: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 532 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:26: GATCAACACC TCGTCACCCC GTCTCGCAAC CACAGGTTTC CCGTGGACCA ACTGTCCACA 60 GCCTAACACA CGAGCAGAGT CCCGAACAAT AGCACAATCT TCCTTGGTTA TGCTAACAGG 120 CTCAAGCGCA AAACCCCACT CTCGCAAGCG GGCAGCACCG CGCCTGCTAG TGTGACCGGC 180 GTGCTCGTAG AGGAGGACGC CCTGCTTGCG CAGGACGCCC ACCAGCCAAG AGCAGGCCAG 240 CCGCTCCTCA GCAAGAGCTA AGGAGTCCAG CACCCGCGCC AAGCGCGCGA GATTTGGTGA 300 GTTAACCAAG AGTACTTCCA AGATGAAATC AATGACATCT AAACTGCTCA AACAGAGTAT 360 GAAGATGACG GAAACTGTGG CAACTGTTTG GGGGAAGAAC CAAGCCACAA CCAACCAAGC 420 TTTCCAGCAC GCCTCCAACG GCCAAAAGCT CCAACCGGCG AGTTGTTCAC CCACCGGCGA 480 ACCCTCTGGT AATTGACGGC CCACCTGGCA TACCAAGTCA ATCTGGCTGA TC 532 (2) INFORMATION FOR SEQ ID NO:27: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 306 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:27: GATCCATCTT GACAATGACA ACTTTCGCAG GACAGTAGAC ACCTTGGTGA CGAACTCATC 60 TTTGAGGAAG AAATCGTCAG GCATCACCGA ACTGCGTGGC ATCATCGTCA ACAATCTGTT 120 AACCCAATCT TGACCCACAC CCTTTTTGAC AGACCAGAGC AACAAGCCCA GAACCACACC 180 GGCCACCGAA GCCCCCGGAG AGGCCAGGCA ACTGACCAGG CACCAAGCGT CACTCGCTTG 240 TAACTTCCCC GCCAGGAGGT CGAAGGTGAG TGAGCGCGGT TCACCGCCCC CTCCCAGCCT 300 CTGATC 306 (2) INFORMATION FOR SEQ ID NO:28: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 369 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE:. DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:28: GATCACCCAC ACCCCGGTTG GTTGGCACTT GCATGCCTGA AGGCAAGAAG CACCATTAGG 60 GAGCGGGTAG ACCGTGACGT CGTCACTCGC TAACCACCAC CGAGCATTGA CAGGACCGAA 120 AGCCCCACCA TAGGCCGGAC GTTGGTACCA CGGTATGTCG TGTACATCAC TCCGTTCACG "180 CAGCAGCCCA TGGAACGAGT TGTTGAAGTC CCAAGGACCA CCACGTTCCC GTGATGTTCG 240 GACGAGTCCT TGCCTGTCAT GGAGGTCCTC ACAACCCCGA AGAATCCCTT GCCAGCTTGA 300 TGAAGCACCA CGGGAGCAGT GGGAACAAAG CCAGGCGGAA GGTCGAACCG ACTGTTCACA 360 CAACTGATC 369 (2) INFORMATION FOR SEQ ID NO:29: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 337 base pairs (B) TYPE: ' nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:29: GATCCAATCC AGGGGCCCTC GTACCCCTCC TGGCAGCTGT AGAAAGGACA ACCAGGAATG 60 TTAACCATGC TCTGAACTCC AGCTTTAAGG ACATTAAAGC AAATCACAAA GAAATTGCAC 120 ACATACTGCC AAATCTCTAG ACCCCAAGCA ATGAGGCCGC AATCATCCTC CGTCGGGGTG 180 TGGAGCCAAC GGATGCAAGC TGATATGATA CTCCAGGGGG TAGATGCCTC CAGAATGCCC 240 AGTATCTTCT GCGGATGTCA CGAGTGGCAA TAAAGTACTC ACTACATACA GTGTTGCTCC 300 TAGCAAGCAT AGTAAGAAGT CTGTTGGGCC AGTGATC 337 (2) INFORMATION FOR SEQ ID NO:30: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 234 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:30: GATCAGGTAT GCTCCAAGCA CGCTGTCCAT GCGGTGCTGA ACTCATCTTT TCTGTTGAGA 60 ATGGTTTTGC AAAACTTTAC AAAGGACCCA GAACTTGTTC AAATTACTGG AGAGGGGCTG 120 TTCCAGTCAA CGCTAGGCTG TGTGGGTCGG CTAGACCGGA CCCAACTGAT TGGACTAGTC 180 TTGTCGTCAA TTATGGCGTT AGGGACTACT GTAAATATGA GAAATTGGGA GATC 234 (2) INFORMATION FOR SEQ ID NO:31: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 73 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:31: Asp Pro Xaa Xaa Ala Thr His Pro Ser Ser He Xaa Met Ser Ser Lys 1 5 10 15 Gin Trp Met Arg Arg Gin His Ser Arg Leu Ala Cys Gin Arg Gin Asn 20 25 30 Pro Pro Met Ser Met Tyr Gin Glu Leu Phe Pro Gin Pro Arg Pro Ser 35 40 45 Xaa Thr Pro Val Arg Leu Xaa Arg Leu Xaa Ala Trp Thr Gin Leu Arg 50 55 60 Leu Gin He Met Thr Gly Thr Phe Xaa 65 70 (2) INFORMATION FOR SEQ ID NO:32: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 73 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:32: He His Ser Glu Pro Leu Thr His Gin Ala Phe Lys Cys Gin Ala Ser 1 5 10 15 Ser Gly Xaa Gly Gly Ser He Ala Ala Xaa His Val Lys Asp Lys Thr 20 25 30 His Arg Cys Pro Cys Thr Lys Ser Cys Ser His Ser Pro Gly His His 35 40 45 Glu Arg Gin Cys Val Ser Ser Val Cys Lys Leu Gly Arg Asn Cys Ala 50 55 60 Ser Lys Xaa Xaa Gin Glu His Phe Asp 65 70 (2) INFORMATION FOR SEQ ID NO:33: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 73 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:33: Ser He Val Ser His Ser Pro He Lys His Leu Asn Val Lys Gin Ala 1 5 10 15 Val Asp Glu Ala Ala Ala Xaa Pro Pro Ser Met Ser Lys Thr Lys Pro 20 25 30 Thr Asp Val His Val Pro Arg Ala Val Pro Thr Ala Pro Ala He Met 35 40 45 Asn Ala Ser Ala Ser Leu Ala Ser Val Ser Leu Asp Ala He Ala Pro 50 55 60 Pro Asn Asn Asp Arg Asn He Leu He 65 70 (2) INFORMATION FOR SEQ ID NO:34: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 73 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:34: Asp Gin Asn Val Pro Val He He Trp Arg Arg Asn Cys Val Gin Ala 1 5 10 15 Tyr Arg Arg Xaa Arg Arg Thr Gly Val His Asp Gly Arg Gly Cys Gly 20 25 30 Asn Ser Ser Trp Tyr Met Asp He Gly Gly Phe Cys Leu Xaa His Ala 35 40 45 Arg Arg Leu Cys Cys Arg Leu He His Cys Leu Leu Asp He Xaa Met 50 55 60 Leu Asp Gly Xaa Val Ala His Tyr Gly 65 70 (2) INFORMATION FOR SEQ ID NO:35: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 73 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:35: He Lys Met Phe Leu Ser Leu Phe Gly Gly Ala He Ala Ser Lys Leu 1 5 10 15 Thr Asp Ala Arg Asp Ala Leu Ala Phe Met Met Ala Gly Ala Val Gly 20 25 30 Thr Ala Leu Gly Thr Trp Thr Ser Val Gly Phe Val Phe Asp Met Leu 35 40 45 Gly Gly Tyr Ala Ala Ala Ser Ser Thr Ala Cys Leu Thr Phe Lys Cys 50 55 60 Leu Met Gly Glu Trp Leu Thr Met Asp 65 70 (2) INFORMATION FOR SEQ ID NO:36: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 73 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:36: Ser Lys Cys Ser Cys His Tyr Leu Glu Ala Gin Leu Arg Pro Ser Leu 1 5 10 15 Gin Thr Leu Glu Thr His Trp Arg Ser Xaa Trp Pro Gly Leu Trp Glu 20 25 30 Gin Leu Leu Val His Gly His Arg Trp Val Leu Ser Leu Thr Cys Xaa 35 40 45 Ala Ala Met Leu Pro Pro His Pro Leu Leu Ala Xaa His Leu Asn Ala 50 55 60 Xaa Trp Val Ser Gly Ser Leu Trp He 65 70 (2) INFORMATION FOR SEQ ID NO:37: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 245 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:37: Asp Arg Ser Thr Pro Gin Ala Leu Arg Arg Cys Val Ala Pro Gly Leu 1 5 10 15 Pro Arg Ser Tyr His Gin Tyr Gin Arg Gin Thr Thr Pro Cys Glu Val 20 25 30 His Arg His Lys His Gly Ser Pro His Arg Ala Gin Asp He Gin Val 35 40 45 Arg His Asp Thr His His Thr Gin Thr Thr Ser Glu Pro Pro Leu Leu 50 55 60 Gly Cys Pro Ala Asp His Arg Gly Ala His Gin Leu Gly Ser Gin Arg 65 70 75 80 Ala Ser Thr Thr Gly Lys Xaa Ala Pro Thr Phe Asp Asn Gin Ala Arg 85 90 95 Pro Ala Ala Asn Val Arg Ser Leu Ser His Ala Gly Gin Met Ser Pro 100 105 110 Thr Thr Ala Xaa Ala Pro Ser Leu Ala Ala Pro Gin Thr Ala Xaa Ala 115 120 125 Pro Ala Val Arg Pro Ala Thr Met Xaa Gin Pro Ala Leu Xaa Val Glu 130 135 140 Ser Ala Thr Pro Val Val Glu Phe Gly Gin Asp Gly Val Gly Thr Val 145 150 155 160 Gly Gly Val His Asn Gly Thr Leu Ser Val Asp Phe Val Thr Glu Gly 165 170 175 Cys Met He Thr He Val Ala Ala Asp Ala Pro Phe Asn His His His 180 185 190 He Ala Ser He Asn Arg Gly Ala Thr Leu Ala Ser Ala Asn Phe He 195 200 205 Thr Thr Asn Arg Ala Arg Thr Met Ser Val Ser Asn Gin Ala Ala Glu 210 215 220 Asp Leu Arg Xaa Pro Leu Xaa Thr Cys Cys Leu Leu Pro Leu Thr Trp 225 230 235 240 Met Lys Pro Leu Xaa 245 (2) INFORMATION FOR SEQ ID NO:38: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 245 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:38: He Glu Ala His Leu Lys Pro Xaa Aβp Ala Val Ser Leu Pro Gly Tyr 1 5 10 15 Pro Ala Ala Thr Thr Asn Thr Ser Gly Arg Arg Pro Leu Ala Lys Cys 20 25 30 He Ala Thr Ser Thr Ala Ala Leu Thr Glu Pro Arg Thr Phe Arg Tyr 35 40 45 Ala Thr Thr His He Thr Pro Arg Gin Pro Val Asn His His Ser Trp 50 55 60 Ala Ala Gin Pro Thr Thr Gly Ala His Thr Ser Ser Gly Ala Ser Ala 65 70 75 80 Pro Arg Arg Pro Ala Ser Lys Pro Gin His Leu Thr Thr Arg Pro Asp 85 90 95 Arg Gin Arg Thr Phe Ala Ala Xaa Ala Thr Arg Ala Arg Cys His Gin 100 105 110 Arg Arg Pro Glu His His His Trp Gin His Pro Arg Pro Pro Glu Pro 115 120 125 Arg Pro Ser Gly Leu Pro Pro Cys Ser Asn Gin His Cys Arg Xaa Ser 130 135 140 Pro Arg Leu Arg Trp Xaa Asn Ser Asp Lys Met Glu Leu Glu Gin Trp 145 150 155 160 Ala Glu Ser Thr Met Glu His Phe Gin Trp Thr Ser Xaa Gin Lys Gly 165 170 175 Val Xaa Xaa Gin Xaa Trp Arg Gin Met Leu His Ser Thr Thr Thr Thr 180 185 190 Leu Pro Ala Xaa Thr Gly Gly Gin Leu Xaa Pro Gin Pro Thr Ser Ser 195 200 205 Leu Pro Thr Gly Pro Gly Pro Cys Gin Xaa Ala Thr Lys Pro Arg Lys 210 215 220 Thr Phe Ala Asp His Cys Lys Pro Ala Val Cys Cys Leu Xaa His Gly 225 230 235 240 Xaa Ser Arg Cys Asp 245 (2) INFORMATION FOR SEQ ID NO:39: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 245 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:39: Ser Lys His Thr Ser Ser Pro Lys Thr Leu Cys Arg Ser Arg Val Thr 1 5 10 15 Pro Gin Leu Pro Pro He Pro Ala Ala Asp Asp Pro Leu Arg Ser Ala 20 25 30 Ser Pro Gin Ala Arg Gin Pro Ser Gin Ser Pro Gly His Ser Gly Thr 35 40 45 Pro Arg His Thr Ser His Pro Asp Asn Gin Xaa Thr Thr Thr Pro Gly 50 55 60 Leu Pro Ser Arg Pro Pro Gly Arg Thr Pro Ala Arg Glu Pro Ala Arg 65 70 75 80 Leu Asp Asp Arg Gin Val Ser Pro Asn He Xaa Gin Pro Gly Gin Thr 85 90 95 Gly Ser Glu Arg Ser Gin Leu Glu Pro Arg Gly Pro Asp Val Thr Asn 100 105 110 Asp Gly Leu Ser Thr He He Gly Ser Thr Pro Asp Arg Leu Ser Pro 115 120 125 Gly Arg Gin Ala Cys His His Val Ala Thr Ser He Val Gly Arg Val 130 135 140 Arg Asp Ser Gly Gly Arg He Arg Thr Arg Trp Ser Trp Asn Ser Gly 145 150 155 160 Arg Ser Pro Gin Trp Asn Thr Phe Ser Gly Leu Arg Asp Arg Arg Val 165 170 175 Tyr Asp Asn Asn Ser Gly Gly Arg Cys Ser He Gin Pro Pro Pro His 180 185 190 Cys Gin His Lys Gin Gly Gly Asn Ser Ser Leu Ser Gin Leu His His 195 200 205 Tyr Gin Gin Gly Gin Asp His Val Ser Lys Gin Pro Ser Arg Gly Arg 210 215 220 Pro Ser Leu Thr Thr Val Asn Leu Leu Ser Val Ala Phe Asn Met Asp 225 230 235 240 Glu Ala Val Val He 245 (2) INFORMATION FOR SEQ ID NO:40: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 245 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear ( ii) MOLECULE TYPE : protein (xi) SEQUENCE DESCRIPTION : SEQ ID NO:40 : Asp His Asn Gly Phe He His Val Lys Gly Asn Arg Gin Gin Val Tyr 1 5 10 15 Ser Gly Gin Arg Arg Ser Ser Ala Ala Trp Leu Leu Thr Asp Met Val 20 25 30 Leu Ala Leu Leu Val Val Met Lys Leu Ala Glu Ala Arg Val Ala Pro 35 40 45 Leu Phe Met Leu Ala Met Trp Trp Trp Leu Asn Gly Ala Ser Ala Ala 50 55 60 Thr He Val He He His Pro Ser Val Thr Lys Ser Thr Glu Ser Val 65 70 75 80 Pro Leu Trp Thr Pro Pro Thr Val Pro Thr Pro Ser Cys Pro Asn Ser 85 90 95 Thr Thr Gly Val Ala Asp Ser Thr Tyr Asn Ala Gly Cys Tyr Met Val 100 105 110 Ala Gly Leu Thr Ala Gly Ala Gin Ala Val Trp Gly Ala Ala Asn Asp 115 120 125 Gly Ala Gin Ala Val Val Gly Asp He Trp Pro Ala Trp Leu Lys Leu 130 135 140 Arg Thr Phe Ala Ala Gly Leu Ala Trp Leu Ser Asn Val Gly Ala Tyr 145 150 155 160 Leu Pro Val Val Glu Ala Arg Trp Leu Pro Ser Trp Cys Ala Pro Arg 165 170 175 Trp Ser Ala Gly Gin Pro Arg Ser Gly Gly Ser Leu Val Val Trp Val 180 185 190 Xaa Cys Val Ser Trp Arg Thr Xaa Met Ser Trp Ala Leu Xaa Gly Leu 195 200 205 Pro Cys Leu Trp Arg Cys Thr Ser Gin Gly Val Val Cys Arg Trp Tyr 210 215 220 Trp Trp Xaa Leu Arg Gly Asn Pro Gly Ala Thr Gin Arg Leu Arg Ala 225 230 235 240 Xaa Gly Val Leu Arg 245 (2) INFORMATION FOR SEQ ID NO:41: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 245 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:41: He Thr Thr Ala Ser Ser Met Leu Lys Ala Thr Asp Ser Arg Phe Thr 1 5 10 15 Val Val Ser Glu Gly Leu Pro Arg Leu Gly Cys Leu Leu Thr Trp Ser 20 25 30 Trp Pro Cys Trp Xaa Xaa Xaa Ser Trp Leu Arg Leu Glu Leu Pro Pro 35 40 45 Cys Leu Cys Trp Gin Cys Gly Gly Gly Xaa Met Glu His Leu Pro Pro " 50 55 60 Leu Leu Leu Ser Tyr Thr Leu Leu Ser Arg Ser Pro Leu Lys Val Phe 65 70 75 80 His Cys Gly Leu Arg Pro Leu Phe Gin Leu His Leu Val Arg He Leu 85 90 95 Pro Pro Glu Ser Arg Thr Leu Pro Thr Met Leu Val Ala Thr Trp Trp 100 105 110 Gin Ala Xaa Arg Pro Gly Leu Arg Arg Ser Gly Val Leu Pro Met Met 115 120 125 Val Leu Arg Pro Ser Leu Val Thr Ser Gly Pro Arg Gly Ser Ser Cys 130 135 140 Glu Arg Ser Leu Pro Val Trp Pro Gly Cys Gin Met Leu Gly Leu Thr 145 150 155 160 Cys Arg Ser Ser Arg Arg Ala Gly Ser Arg Ala Gly Val Arg Pro Gly 165 170 175 Gly Arg Leu Gly Ser Pro Gly Val Val Val His Trp Leu Ser Gly Cyβ 180 185 190 Asp Val Cys Arg Gly Val Pro Glu Cys Pro Gly Leu Cys Glu Gly Cys 195 200 205 Arg Ala Cys Gly Asp Ala Leu Arg Lys Gly Ser Ser Ala Ala Gly He 210 215 220 Gly Gly Ser Cys Gly Val Thr Arg Glu Arg His Ser Val Leu Gly Leu 225 230 235 240 Glu Val Cys Phe Asp 245 (2) INFORMATION FOR SEQ ID NO:42: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 245 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:42: Ser Gin Arg Leu His Pro Cys Xaa Arg Gin Gin Thr Ala Gly Leu Gin 1 5 10 15 Trp Ser Ala Lys Val Phe Arg Gly Leu Val Ala Tyr Xaa His Gly Pro- 20 25 30 Gly Pro Val Gly Ser Asp Glu Val Gly Xaa Gly Xaa Ser Cys Pro Pro 35 40 45 Val Tyr Ala Gly Asn Val Val Val Val Glu Trp Ser He Cys Arg His 50 55 60 Tyr Cys Tyr His Thr Pro Phe Cys His Glu Val His Xaa Lys Cys Ser 65 70 75 80 He Val Asp Ser Ala His Cys Ser Asn Ser He Leu Ser Glu Phe Tyr 85 90 95 His Arg Ser Arg Gly Leu Tyr Leu Gin Cys Trp Leu Leu His Gly Gly 100 105 110 Arg Pro Asp Gly Arg Gly Ser Gly Gly Leu Gly Cys Cys Gin Xaa Trp 115 120 125 Cys Ser Gly Arg Arg Trp Xaa His Leu Ala Arg Val Ala Gin Ala Ala 130 135 140 Asn Val Arg Cys Arg Ser Gly Leu Val Val Lys Cys Trp Gly Leu Leu 145 150 155 160 Ala Gly Arg Arg Gly Ala Leu Ala Pro Glu Leu Val Cys Ala Pro Val 165 170 175 Val Gly Trp Ala Ala Gin Glu Trp Trp Phe Thr Gly Cys Leu Gly Val 180 185 190 Met Cys Val Val Ala Tyr Leu Asn Val Leu Gly Ser Val Arg Ala Ala 195 200 205 Val Leu Val Ala Met His Phe Ala Arg Gly Arg Leu Pro Leu Val Leu 210 215 220 Val Val Ala Ala Gly Xaa Pro Gly Ser Asp Thr Ala Ser Xaa Gly Leu 225 230 235 240 Arg Cys Ala Ser He 245 (2) INFORMATION FOR SEQ ID NO:43 : (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 102 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO.-43: Asp His Cys Gly Arg His Leu Phe Arg Leu He Asp Xaa Xaa Ala Arg 1 5 10 15 Tyr Ala Gly Gly Gly Leu Gly Val Cys Gly Gly Xaa Xaa Gin Pro Leu 20 25 30 Asn Gly Thr Cys Phe Val Gin Val Leu Leu Trp Trp Pro Tyr Gly Phe 35 40 45 Pro Arg Trp Gly Ser Leu Gly Val Pro Pro Val Xaa Val Val Gly Arg 50 55 60 Val Asp Asn Xaa Leu Gly Glu Gin His His Leu Leu His Xaa Gly Gin 65 70 75 80 Arg Gly Leu Gin Ala Gly Gly Asp Xaa Gly Thr He He Leu Tyr Ser 85 90 95 Trp Arg Xaa Leu Leu Asp 100 (2) INFORMATION FOR SEQ ID NO:44: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 102 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:44: He Thr Val Asp Ala Thr Cys Phe Asp Ser Ser He Asp Glu His Asp 1 5 10 15 Met Gin Val Glu Ala Ser Val Phe Ala Ala Ala Ser Asp Asn Pro Ser 20 25 30 Met Val His Ala Leu Cys Lys Tyr Tyr Ser Gly Gly Pro Met Val Ser 35 40 45 Pro Asp Gly Val Pro Leu Gly Tyr Arg Gin Cys Arg Ser Ser Gly Val 50 55 60 Leu Thr Thr Ser Ser Ala Asn Ser He Thr Cys Tyr He Lys Val Ser 65 70 75 80 Ala Ala Cys Arg Arg Val Gly He Lys Ala Pro Ser Phe Phe He Ala 85 90 95 Gly Asp Asp Cys Leu He 100 (2) INFORMATION FOR SEQ ID NO:45: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 101 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:45: Ser Leu Trp Thr Pro Leu Val Ser Thr His Arg Leu Met Ser Thr He 1 5 10 15 Cys Arg Trp Arg Pro Arg Cys Leu Arg Arg Leu Val Thr Thr Pro Gin 20 25 30 Trp Tyr Met Leu Cys Ala Ser Thr Thr Leu Val Ala Leu Trp Phe Pro 35 40 45 Gin Met Gly Phe Pro Trp Gly Thr Ala Ser Val Gly Arg Arg Ala Cys 50 55 60 Xaa Gin Leu Ala Arg Arg Thr Ala Ser Leu Val Thr Leu Arg Ser Ala 65 70 75 80 Arg Pro Ala Gly Gly Trp Gly Leu Arg His His His Ser Leu Xaa Leu 85 90 95 Glu Met He Ala Xaa 100 (2) INFORMATION FOR SEQ ID NO:46: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 102 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear ( ii) MOLECULE TYPE : protein (xi) SEQUENCE DESCRIPTION : SEQ ID NO : 46 : Asp Gin Ala He He Ser Ser Tyr Lys Glu Xaa Trp Cys Leu Asn Pro 1 5 10 15 His Pro Pro Ala Gly Arg Ala Asp Leu Asn Val Thr Ser Asp Ala Val 20 25 30 Arg Arg Ala Ser Cys Gin His Ala Arg Arg Pro Thr Leu Ala Val Pro 35 40 45 Gin Gly Asn Pro He Trp Gly Asn His Arg Ala Thr Arg Val Val Leu 50 55 60 Ala Gin Ser Met Tyr His Xaa Gly Val Val Thr Ser Arg Arg Lys His 65 70 75 80 Arg Gly Leu His Leu His He Val Leu He Asn Arg Xaa Val Glu Thr 85 90 95 100 (2) INFORMATION FOR SEQ ID NO:47: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 102 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear ( ii) MOLECULE TYPE : protein (xi) SEQUENCE DESCRIPTION : SEQ ID NO : 47 : He Lys Gin Ser Ser Pro Ala He Lys Asn Asp Gly Ala Leu He Pro 1 5 10 15 Thr Arg Leu Gin Ala Ala Leu Thr Leu Met Xaa Gin Val Met Leu Phe 20 25 30 Ala Glu Leu Val Val Asn Thr Pro Asp Asp Leu His Trp Arg Tyr Pro 35 40 45 Lys Gly Thr Pro Ser Gly Glu Thr He Gly Pro Pro Glu Xaa Tyr Leu 50 55 60 His Lys Ala Cys Thr He Glu Gly Leu Ser Leu Ala Ala Ala Asn Thr 65 70 75 80 Glu Ala Ser Thr Cys He Ser Cys Ser Ser He Asp Glu Ser Lys Gin 85 90 95 Val Ala Ser Thr Val He 100 (2) INFORMATION FOR SEQ ID NO:48: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 101 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:48: Ser Ser Asn His Leu Gin Leu Xaa Arg Met Met Val Pro Xaa Ser Pro 1 5 10 15 Pro Ala Cys Arg Pro Arg Xaa Pro Xaa Cys Asn Lys Xaa Cys Cys Ser 20 25 30 Pro Ser Xaa Leu Ser Thr Arg Pro Thr Thr Tyr Thr Gly Gly Thr Pro 35 40 45 Arg Glu Pro His Leu Gly Lys Pro Xaa Gly His Gin Ser Ser Thr Cys 50 55 60 Thr Lys His Val Pro Leu Arg Gly Cys His Xaa Pro Pro Gin Thr Pro 65 70 75 80 Arg Pro Pro Pro Ala Tyr Arg Ala His Gin Ser Met Ser Arg Asn Lys 85 90 95 Trp Arg Pro Gin Xaa 100 (2) INFORMATION FOR SEQ ID NO:49: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 177 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:49: Asp Gin His Leu Val Thr Pro Ser Arg Asn His Arg Phe Pro Val Asp 1 5 10 15 Gin Leu Ser Thr Ala Xaa His Thr Ser Arg Val Pro Asn Asn Ser Thr 20 25 30 He Phe Leu Gly Tyr Ala Asn Arg Leu Lys Arg Lys Thr Pro Leu Ser 35 40 45 Gin Ala Gly Ser Thr Ala Pro Ala Ser Val Thr Gly Val Leu Val Glu_ 50 55 60 Glu Asp Ala Leu Leu Ala Gin Asp Ala His Gin Pro Arg Ala Gly Gin 65 70 75 80 Pro Leu Leu Ser Lys Ser Xaa Gly Val Gin His Pro Arg Gin Ala Arg 85 90 95 Glu He Trp Xaa Val Asn Gin Glu Tyr Phe Gin Asp Glu He Asn Asp 100 105 110 He Xaa Thr Ala Gin Thr Glu Tyr Glu Asp Asp Gly Asn Cys Gly Asn 115 120 125 Cys Leu Gly Glu Glu Pro Ser His Asn Gin Pro Ser Phe Pro Ala Arg 130 135 140 Leu Gin Arg Pro Lys Ala Pro Thr Gly Glu Leu Phe Thr His Arg Arg 145 150 155 160 Thr Leu Trp Xaa Leu Thr Ala His Leu Ala Tyr Gin Val Asn Leu Ala 165 170 175 Asp (2) INFORMATION FOR SEQ ID NO:50: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 177 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii). MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:50: He Asn Thr Ser Ser Pro Arg Leu Ala Thr Thr Gly Phe Pro Trp Thr 1 5 10 15 Asn Cys Pro Gin Pro Asn Thr Arg Ala Glu Ser Arg Thr He Ala Gin 20 25 30 Ser Ser Leu Val Met Leu Thr Gly Ser Ser Ala Lys Pro His Ser Arg 35 40 45 Lys Arg Ala Ala Pro Arg Leu Leu Val Xaa Pro Ala Cys Ser Xaa Arg 50 55 60 Arg Thr Pro Cys Leu Arg Arg Thr Pro Thr Ser Gin Glu Gin Ala Ser 65 70 75 80 Arg Ser Ser Ala Arg Ala Lys Glu Ser Ser Thr Arg Ala Lys Arg Ala 85 90 95 Arg Phe Gly Glu Leu Thr Lys Ser Thr Ser Lys Met Lys Ser Met Thr 100 105 110 Ser Lys Leu Leu Lys Gin Ser Met Lys Met Thr Glu Thr Val Ala Thr 115 120 125 Val Trp Gly Lys Asn Gin Ala Thr Thr Asn Gin Ala Phe Gin His Ala 130 135 140 Ser Asn Gly Gin Lys Leu Gin Pro Ala Ser Cys Ser Pro Thr Gly Glu 145 150 155 160 Pro Ser Gly Asn Xaa Arg Pro Thr Trp Hie Thr Lys Ser He Trp Leu 165 170 175 He (2) INFORMATION FOR SEQ ID NO:51: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 176 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:51: Ser Thr Pro Arg His Pro Val Ser Gin Pro Gin Val Ser Arg Gly Pro 1 5 10 15 Thr Val His Ser Leu Thr His Glu Gin Ser Pro Glu Gin Xaa His Asn 20 25 30 Leu Pro Trp Leu Cys Xaa Gin Ala Gin Ala Gin Asn Pro Thr Leu Ala 35 40 45 Ser Gly Gin His Arg Ala Cys Xaa Cys Asp Arg Arg Ala Arg Arg Gly 50 55 60 Gly Arg Pro Ala Cys Ala Gly Arg Pro Pro Ala Lys Ser Arg Pro Ala 65 70 75 80 Ala Pro Gin Gin Glu Leu Arg Ser Pro Ala Pro Ala Pro Ser Ala Arg 85 90 95 Asp Leu Val Ser Xaa Pro Arg Val Leu Pro Arg Xaa Asn Gin Xaa His 100 105 110 Leu Asn Cys Ser Asn Arg Val Xaa Arg Xaa Arg Lys Leu Trp Gin Leu 115 120 125 Phe Gly Gly Arg Thr Lys Pro Gin Pro Thr Lys Leu Ser Ser Thr Pro 130 135 140 Pro Thr Ala Lys Ser Ser Asn Arg Arg Val Val His Pro Pro Ala Asn 145 150 155 160 Pro Leu Val He Asp Gly Pro Pro Gly He Pro Ser Gin Ser Gly Xaa 165 170 175 (2) INFORMATION FOR SEQ ID NO:52: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 177 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE : protein (xi) SEQUENCE DESCRIPTION : SEQ ID NO : 52 : Asp Gin Pro Asp Xaa Leu Gly Met Pro Gly Gly Pro Ser He Thr Arg 1 5 10 15 Gly Phe Ala Gly Gly Xaa Thr Thr Arg Arg Leu Glu Leu Leu Ala Val 20 25 30 Gly Gly Val Leu Glu Ser Leu Val Gly Cys Gly Leu Val Leu Pro Pro 35 40 45 Asn Ser Cys His Ser Phe Arg His Leu His Thr Leu Phe Glu Gin Phe 50 55 60 Arg Cys His Xaa Phe His Leu Gly Ser Thr Leu Gly Xaa Leu Thr Lys 65 70 75 80 Ser Arg Ala Leu Gly Ala Gly Ala Gly Leu Leu Ser Ser Cys Xaa Gly 85 90 95 Ala Ala Gly Leu Leu Leu Ala Gly Gly Arg Pro Ala Gin Ala Gly Arg 100 105 110 Pro Pro Leu Arg Ala Arg Arg Ser His Xaa Gin Ala Arg Cys Cys Pro 115 120 125 Leu Ala Arg Val Gly Phe Cys Ala Xaa Ala Cys Xaa His Asn Gin Gly 130 135 140 Arg Leu Cys Tyr Cys Ser Gly Leu Cys Ser Cys Val Arg Leu Trp Thr 145 150 155 160 Val Gly Pro Arg Glu Thr Cys Gly Cys Glu Thr Gly Xaa Arg Gly Val 165 170 175 Asp (2) INFORMATION FOR SEQ ID NO:53: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 177 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:53: He Ser Gin He Asp Leu Val Cys Gin Val Gly Arg Gin Leu Pro Glu 1 5 10 15 Gly Ser Pro Val Gly Glu Gin Leu Ala Gly Trp Ser Phe Trp Pro Leu 20 25 30 Glu Ala Cys Trp Lys Ala Trp Leu Val Val Ala Trp Phe Phe Pro Gin 35 40 45 Thr Val Ala Thr Val Ser Val He Phe He Leu Cys Leu Ser Ser Leu 50 55 60 Asp Val He Asp Phe He Leu Glu Val Leu Leu Val Asn Ser Pro Asn 65 70 75 80 Leu Ala Arg Leu Ala Arg Val Leu Asp Ser Leu Ala Leu Ala Glu Glu 85 90 95 Arg Leu Ala Cys Ser Trp Leu Val Gly Val Leu Arg Lys Gin Gly Val 100 105 110 Leu Leu Tyr Glu His Ala Gly His Thr Ser Arg Arg Gly Ala Ala Arg 115 120 125 Leu Arg Glu Trp Gly Phe Ala Leu Glu Pro Val Ser He Thr Lys Glu 130 135 140 Asp Cys Ala He Val Arg Asp Ser Ala Arg Val Leu Gly Cys Gly Gin 145 150 155 160 Leu Val His Gly Lys Pro Val Val Ala Arg Arg Gly Asp Glu Val Leu 165 170 175 He (2) INFORMATION FOR SEQ ID NO:54: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 176 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:54: Ser Ala Arg Leu Thr Trp Tyr Ala Arg Trp Ala Val Asn Tyr Gin Arg 1 5 10 15 Val Arg Arg Trp Val Asn Asn Ser Pro Val Gly Ala Phe Gly Arg Trp 20 25 30 Arg Arg Ala Gly Lys Leu Gly Trp Leu Trp Leu Gly Ser Ser Pro Lys 35 40 45 Gin Leu Pro Gin Phe Pro Ser Ser Ser Tyr Ser Val Xaa Ala Val Xaa 50 55 60 Met Ser Leu He Ser Ser Trp Lys Tyr Ser Trp Leu Thr His Gin He 65 70 75 80 Ser Arg Ala Trp Arg Gly Cys Trp Thr Pro Xaa Leu Leu Leu Arg Ser 85 90 95 Gly Trp Pro Ala Leu Gly Trp Trp Ala Ser Cys Ala Ser Arg Ala Ser 100 105 110 Ser Ser Thr Ser Thr Pro Val Thr Leu Ala Gly Ala Val Leu Pro Ala 115 120 125 Cys Glu Ser Gly Val Leu Arg Leu Ser Leu Leu Ala Xaa Pro Arg Lys 130 135 140 He Val Leu Leu Phe Gly Thr Leu Leu Val Cys Xaa Ala Val Asp Ser 145 150 155 160 Trp Ser Thr Gly Asn Leu Trp Leu Arg Asp Gly Val Thr Arg Cys Xaa 165 170 175 (2) INFORMATION FOR SEQ ID NO:55: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 102 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:55: Asp Pro Ser Xaa Gin Xaa Gin Leu Ser Gin Asp Ser Arg His Leu Gly 1 5 10 15 Asp Glu Leu He Phe Glu Glu Glu He Val Arg His His Arg Thr Ala_ 20 25 30 Trp His His Arg Gin Gin Ser Val Asn Pro He Leu Thr His Thr Leu 35 40 45 Phe Asp Arg Pro Glu Gin Gin Ala Gin Asn His Thr Gly His Arg Ser 50 55 60 Pro Arg Arg Gly Gin Ala Thr Asp Gin Ala Pro Ser Val Thr Arg Leu 65 70 75 80 Xaa Leu Pro Arg Gin Glu Val Glu Gly Glu Xaa Ala Arg Phe Thr Ala 85 90 95 Pro Ser Gin Pro Leu He 100 (2) INFORMATION FOR SEQ ID NO:56: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 101 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:56: He His Leu Asp Asn Asp Asn Phe Arg Arg Thr Val Asp Thr Leu Val 1 5 10 15 Thr Asn Ser Ser Leu Arg Lys Lys Ser Ser Gly He Thr Glu Leu Arg 20 25 30 Gly He He Val Asn Asn Leu Leu Thr Gin Ser Xaa Pro Thr Pro Phe 35 40 45 Leu Thr Asp Gin Ser Asn Lys Pro Arg Thr Thr Pro Ala Thr Glu Ala 50 55 60 Pro Gly Glu Ala Arg Gin Leu Thr Arg His Gin Ala Ser Leu Ala Cys 65 70 75 80 Asn Phe Pro Ala Arg Arg Ser Lys Val Ser Glu Arg Gly Ser Pro Pro 85 90 95 Pro Pro Ser Leu Xaa 100 (2) INFORMATION FOR SEQ ID NO:57: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 101 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:57: Ser He Leu Thr Met Thr Thr Phe Ala Gly Gin Xaa Thr Pro Trp Xaa 1 5 10 15 Arg Thr His Leu Xaa Gly Arg Asn Arg Gin Ala Ser Pro Asn Cys Val 20 25 30 Ala Ser Ser Ser Thr He Cys Xaa Pro Asn Leu Asp Pro His Pro Phe 35 40 45 Xaa Gin Thr Arg Ala Thr Ser Pro Glu Pro His Arg Pro Pro Lys Pro 50 55 60 Pro Glu Arg Pro Gly Asn Xaa Pro Gly Thr Lys Arg His Ser Leu Val 65 70 75 80 Thr Ser Pro Pro Gly Gly Arg Arg Xaa Val Ser Ala Val His Arg Pro 85 90 95 Leu Pro Ala Ser Asp 100 (2) INFORMATION FOR SEQ ID NO:58: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 102 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:58: Asp Gin Arg Leu Gly Gly Gly Gly Glu Pro Arg Ser Leu Thr Phe Asp 1 5 10 15 Leu Leu Ala Gly Lys Leu Gin Ala Ser Asp Ala Trp Cys Leu Val Ser 20 25 30 Cys Leu Ala Ser Pro Gly Ala Ser Val Ala Gly Val Val Leu Gly Leu 35 40 45 Leu Leu Trp Ser Val Lys Lys Gly Val Gly Gin Asp Trp Val Asn Arg 50 55 60 Leu Leu Thr Met Met Pro Arg Ser Ser Val Met Pro Asp Asp Phe Phe 65 70 75 80 Leu Lys Asp Glu Phe Val Thr Lys Val Ser Thr Val Leu Arg Lys Leu 85 90 95 Ser Leu Ser Arg Trp He 100 (2) INFORMATION FOR SEQ ID NO:59: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 101 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear ( ii ) MOLECULE TYPE : protein (xi) SEQUENCE DESCRIPTION : SEQ ID NO : 59 : He Arg Gly Trp Glu Gly Ala Val Asn Arg Ala His Ser Pro Ser Thr 1 5 10 15 Ser Trp Arg Gly Ser Tyr Lys Arg Val Thr Leu Gly Ala Trp Ser Val 20 25 30 Ala Trp Pro Leu Arg Gly Leu Arg Trp Pro Val Trp Phe Trp Ala Cys 35 40 45 Cys Ser Gly Leu Ser Lys Arg Val Trp Val Lys He Gly Leu Thr Asp 50 55 60 Cys Xaa Arg Xaa Cys His Ala Val Arg Xaa Cys Leu Thr He Ser Ser 65 70 75 80 Ser Lys Met Ser Ser Ser Pro Arg Cys Leu Leu Ser Cys Glu Ser Cys 85 90 95 His Cys Gin Asp Gly 100 (2) INFORMATION FOR SEQ ID NO:60: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 101 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi ) SEQUENCE DESCRIPTION : SEQ ID NO : 60 : Ser Glu Ala Gly Arg Gly Arg Xaa Thr Ala Leu Thr His Leu Arg Pro 1 5 10 15 Pro Gly Gly Glu Val Thr Ser Glu Xaa Arg Leu Val Pro Gly Gin Leu 20 25 30 Pro Gly Leu Ser Gly Gly Phe Gly Gly Arg Cys Gly Ser Gly Leu Val 35 40 45 Ala Leu Val Cys Gin Lys Gly Cys Gly Ser Arg Leu Gly Xaa Gin He 50 55 60 Val Asp Asp Asp Ala Thr Gin Phe Gly Asp Ala Xaa Arg Phe Leu Pro 65 70 75 80 Gin Arg Xaa Val Arg His Gin Gly Val Tyr Cys Pro Ala Lys Val Val 85 90 95 He Val Lys Met Asp 100 (2) INFORMATION FOR SEQ ID NO:61: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 123 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO 61: Trp Leu Ala Leu Ala Cys Leu Lys Ala Arg 10 15 Val Asp Arg Asp Val Val Thr Arg Xaa Pro 25 30 Thr Glu Ser Pro Thr He Gly Arg Thr Leu 40 45 Tyr He Thr Pro Phe Thr Gin Gin Pro Met 55 60 Pro Arg Thr Thr Thr Phe Pro Xaa Cys Ser 75 80 Met Glu Val Leu Thr Thr Pro Lys Asn Pro 90 95 Thr Thr Gly Ala Val Gly Thr Lys Pro Gly 100 105 110 Gly Arg Ser Asn Arg Leu Phe Thr Gin Leu He 115 120 (2) INFORMATION FOR SEQ ID NO:62: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 122 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO 62: He Thr His Thr Pro Val Gly Trp His Leu His Ala Xaa Arg Gin Glu 1 5 10 15 Ala Pro Leu Gly Ser Gly Xaa Thr Val Thr Ser Ser Leu Ala Asn His 20 25 30 His Arg Ala Leu Thr Gly Pro Lys Ala Pro Pro Xaa Ala Gly Arg Trp 35 40 45 Tyr His Gly Met Ser Cys Thr Ser Leu Arg Ser Arg Ser Ser Pro Trp 50 55 60 Asn Glu Leu Leu Lys Ser Gin Gly Pro Pro Arg Ser Arg Asp Val Arg 65 70 75 80 Thr Ser Pro Cys Leu Ser Trp Arg Ser Ser Gin Pro Arg Arg He Pro 85 90 95 Cys Gin Leu Asp Glu Ala Pro Arg Glu Gin Trp Glu Gin Ser Gin Ala 100 105 110 Glu Gly Arg Thr Asp Cys Ser His Asn Xaa 115 120 (2) INFORMATION FOR SEQ ID NO:63: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 122 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 63: Ser Pro Thr Pro Arg Leu Val Gly Thr Cys Met Pro Glu Gly Lys Lys 1 5 10 15 His His Xaa Gly Ala Gly Arg Pro Xaa Arg Arg His Ser Leu Thr Thr 20 25 30 Thr Glu His Xaa Gin Asp Arg Lys Pro His His Arg Pro Asp Val Gly 35 40 45 Thr Thr Val Cys Arg Val His His Ser Val His Ala Ala Ala His Gly 50 55 60 Thr Ser Cys Xaa Ser Pro Lys Asp His His Val Pro Val Met Phe Gly 65 70 75 80 Arg Val Leu Ala Cys His Gly Gly Pro His Asn Pro Glu Glu Ser Leu 85 90 95 Ala Ser Leu Met Lys His His Gly Ser Ser Gly Asn Lys Ala Arg Arg 100 105 110 Lys Val Glu Pro Thr Val His Thr Thr Asp 115 120 (2) INFORMATION FOR SEQ ID NO:64: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 123 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO 64: Asp Gin Leu Cys Glu Gin Ser Val Arg Pro Ser Ala Trp Leu Cys Ser 1 5 10 15 His Cys Ser Arg Gly Ala Ser Ser Ser Trp Gin Gly He Leu Arg Gly 20 25 30 Cys Glu Asp Leu His Asp Arg Gin Gly Leu Val Arg Thr Ser Arg Glu 35 40 45 Arg Gly Gly Pro Trp Asp Phe Asn Asn Ser Phe His Gly Leu Leu Arg 50 55 60 Glu Arg Ser Asp Val His Asp He Pro Trp Tyr * <31n Arg Pro Ala Tyr 65 70 75 80 Gly Gly Ala Phe Gly Pro Val Asn Ala Arg Trp Trp Leu Ala Ser Asp 85 90 95 Asp Val Thr Val Tyr Pro Leu Pro Asn Gly Ala Ser Cys Leu Gin Ala 100 105 110 Cys Lys Cys Gin Pro Thr Gly Val Trp Val He 115 120 (2) INFORMATION FOR SEQ ID NO:65: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 122 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO 65; He Ser Cys Val Asn Ser Arg Phe Asp Leu Pro Pro Gly Phe Val Pro 1 5 10 15 Thr Ala Pro Val Val Leu His Gin Ala Gly Lys Gly Phe Phe Gly Val 20 25 30 Val Arg Thr Ser Met Thr Gly Lys Asp Ser Ser Glu His His Gly Asn 35 40 45 Val Val Val Leu Gly Thr Ser Thr Thr Arg Ser Met Gly Cys Cys Val 50 55 60 Aβn Gly Val Met Tyr Thr Thr Tyr Arg Gly Thr Asn Val Arg Pro Met 65 70 75 80 Val Gly Leu Ser Val Leu Ser Met Leu Gly Gly Gly Xaa Arg Val Thr 85 90 95 Thr Ser Arg Ser Thr Arg Ser Leu Met Val Leu Leu Ala Phe Arg His 100 105 110 Ala Ser Ala Asn Gin Pro Gly Cys Gly Xaa 115 120 (2) INFORMATION FOR SEQ ID NO:66: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 122 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:66: Ser Val Val Xaa Thr Val Gly Ser Thr Phe Arg Leu Ala Leu Phe Pro 1 5 10 15 Leu Leu Pro Trp Cys Phe He Lys Leu Ala Arg Asp Ser Ser Gly Leu 20 25 30 Xaa Gly Pro Pro Xaa Gin Ala Arg Thr Arg Pro Asn He Thr Gly Thr 35 40 45 Trp Trp Ser Leu Gly Leu Gin Gin Leu Val Pro Trp Ala Ala Ala Xaa 50 55 60 Thr Glu Xaa Cys Thr Arg His Thr Val Val Pro Thr Ser Gly Leu Trp 65 70 75 80 Trp Gly Phe Arg Ser Cys Gin Cys Ser Val Val Val Ser Glu Xaa Arg 85 90 95 Arg His Gly Leu Pro Ala Pro Xaa Trp Cys Phe Leu Pro Ser Gly Met 100 105 110 Gin Val Pro Thr Asn Arg Gly Val Gly Asp 115 120 (2) INFORMATION FOR SEQ ID NO:67: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 112 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE : protein (xi) SEQUENCE DESCRIPTION : SEQ ID NO : 67 : Asp Pro He Gin Gly Pro Ser Tyr Pro Ser Trp Gin Leu Xaa Lys Gly 1 5 10 15 Gin Pro Gly Met Leu Thr Met Leu Xaa Thr Pro Ala Leu Arg Thr Leu 20 25 30 Lys Gin He Thr Lys Lys Leu His Thr Tyr Cys Gin He Ser Arg Pro 35 40 45 Gin Ala Met Arg Pro Gin Ser Ser Ser Val Gly Val Trp Ser Gin Arg- 50 55 60 Met Gin Ala Asp Met He Leu Gin Gly Val Asp Ala Ser Arg Met Pro 65 70 75 80 Ser He Phe Cys Gly Cys His Glu Trp Gin Xaa Ser Thr His Tyr He 85 90 95 Gin Cys Cys Ser Xaa Gin Ala Xaa Xaa Glu Val Cys Trp Ala Ser Asp 100 105 110 (2) INFORMATION FOR SEQ ID NO:68: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 112 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:68: He Gin Ser Arg Gly Pro 1 5 Asn Gin Glu Cys Xaa Pro 20 Ser Lys Ser Gin Arg Asn 35 Lys Gin Xaa Gly Arg Asn 50 Cys Lys Leu He Xaa Tyr 65 70 Val Ser Ser Ala Asp Val 85 Ser Val Ala Pro Ser Lys 100 (2) INFORMATION FOR SEQ ID NO:69: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 111 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:69: Ser Asn Pro Gly Ala Leu Val Pro Leu Leu Ala Ala Val Glu Arg Thr 1 5 10 15 Thr Arg Asn Val Asn His Ala Leu Asn Ser Ser Phe Lys Asp He Lys 20 25 30 Ala Asn His Lys Glu He Ala His He Leu Pro Asn Leu Xaa Thr Pro 35 40 45 Ser Asn Glu Ala Ala He He Leu Arg Arg Gly Val Glu Pro Thr Asp 50 55 60 Ala Ser Xaa Tyr Asp Thr Pro Gly Gly Arg Cys Leu Gin Asn Ala Gin 65 70 75 80 Tyr Leu Leu Arg Met Ser Arg Val Ala He Lys Tyr Ser Leu His Thr 85 90 95 Val Leu Leu Leu Ala Ser He Val Arg Ser Leu Leu Gly Gin Xaa 100 105 110 (2) INFORMATION FOR SEQ ID NO:70: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 112 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:70: Asp His Trp Pro Asn Arg Leu Leu Thr Met Leu Ala Arg Ser Asn Thr 1 5 10 15 Val Cys Ser Glu Tyr Phe He Ala Thr Arg Asp He Arg Arg Arg Tyr 20 25 30 Trp Ala Phe Trp Arg His Leu Pro Pro Gly Val Ser Tyr Gin Leu Ala 35 40 45 Ser Val Gly Ser Thr Pro Arg Arg Arg Met He Ala Ala Ser Leu Leu 50 55 60 Gly Val Xaa Arg Phe Gly Ser Met Cys Ala He Ser Leu Xaa Phe Ala 65 70 75 80 Leu Met Ser Leu Lys Leu Glu Phe Arg Ala Trp Leu Thr Phe Leu Vai 85 90 95 Val Leu Ser Thr Ala Ala Arg Arg Gly Thr Arg Ala Pro Gly Leu Asp 100 105 110 (2) INFORMATION FOR SEQ ID NO:71; (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 112 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:71: He Thr Gly Pro Thr Asp Phe Leu Leu Cys Leu Leu Gly Ala Thr Leu 1 5 10 15 Tyr Val Val Ser Thr Leu Leu Pro Leu Val Thr Ser Ala Glu Asp Thr 20 25 30 Gly His Ser Gly Gly He Tyr Pro Leu Glu Tyr His He Ser Leu His 35 40 45 Pro Leu Ala Pro His Pro Asp Gly Gly Xaa Leu Arg Pro His Cys Leu 50 55 60 Gly Ser Arg Asp Leu Ala Val Cys Val Gin Phe Leu Cys Asp Leu Leu 65 70 75 80 Xaa Cys Pro Xaa Ser Trp Ser Ser Glu His Gly Xaa His Ser Trp Leu 85 90 95 Ser Phe Leu Gin Leu Pro Gly Gly Val Arg Gly Pro Leu Asp Trp He 100 105 110 (2) INFORMATION FOR SEQ ID NO:72: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 111 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:72: Ser Leu Ala Gin Gin Thr Ser Tyr Tyr Ala Cys Xaa Glu Gin His Cys 1 5 10 15 Met Xaa Xaa Val Leu Tyr Cys His Ser Xaa His Pro Gin Lys He Leu 20 25 30 Gly He Leu Glu Ala Ser Thr Pro Trp Ser He He Ser Ala Cys He 35 40 45 Arg Trp Leu His Thr Pro Thr Glu Asp Asp Cys Gly Leu He Ala Trp 50 55 60 Gly Leu Glu He Trp Gin Tyr Val Cys Asn Phe Phe Val He Cys Phe 65 70 75 80 Asn Val Leu Lys Ala Gly Val Gin Ser Met Val Asn He Pro Gly Cys 85 90 95 Pro Phe Tyr Ser Cys Gin Glu Gly Tyr Glu Gly Pro Trp He Gly 100 105 110 (2) INFORMATION FOR SEQ ID NO:73: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 795 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:73: GATCAGGCCG CTGAGCGGCC GAGAAGGTTA CAATCTGGAG GGGTGATAGG AAGTATGACA 60 AGCATTATGA GGCTGTCGTT GAGGCTGTCC TGAAAAAGGC AGCCGCGACG AAGTCTCATG 120 GCTGGACCTA TTCCCAGGCT ATAGCTAAAG TTAGGCGCCG AGCAGCCGCT GGATACGGCA 180 GCAAGGTGAC CGCCTCCACA TTGGCCACTG GTTGGCCTCA CGTGGAGGAG ATGCTGGACA 240 AAATAGCCAG GGGACAGGAA GTTCCTTTCA CTTTTGTGAC CAAGCGAGAG GTTTTCTTCT 300 CCAAAACTAC CCGTAAGCCC CCAAGATTCA TAGTTTTCCC ACCTTTGGAC TTCAGGATAG 360 CTGAAAAGAT GATTCTGGGT GACCCCGGCA TCGTTGCAAA GTCAATTCTG GGTGACGCTT 420 ATCTGTTCCA GTACACGCCC AATCAGAGGG TCAAAGCTCT GGTTAAGGCG TGGGAGGGGA 480 AGTTGCATCC CGCTGCGATC ACCGTGkACG CCACTTGTTT CGACTCATCG ATTGATGAGC 540 ACGACATGCA GGTGGAGGCT TCGGTGTTTG CGGCGGCTAG TGACAACCCC TCAATGGTAC 600 ATGCTTTGTG CAAGTACTAC TCTGGTGGCC CTATGGTTTC CCCAGATGGG GTTCCCTTGG 660 GGTACCGCCA GTGTAGGTCG TCGGGCGTGT TGACAACTAG CTCGGCGAAC AGCATCACTT 720 GTTACATTAA GGTCAGCGCG GCCTGCAGGC GGGTGGGGAT TAAGGCACCA TCATTCTTTA 780 TAGCTGGAGA TGATT 795 (2) INFORMATION FOR SEQ ID NO:74: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 265 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:74: Asp Gin Ala Ala Glu Arg Pro Arg Arg Leu Gin Ser Gly Gly Val He 1 5 10 15 Gly Ser Met Thr Ser He Met Arg Leu Ser Leu Arg Leu Ser Xaa Lys 20 25 30 Arg Gin Pro Arg Arg Ser Leu Met Ala Gly Pro He Pro Arg Leu Xaa 35 40 45 Leu Lys Leu Gly Ala Glu Gin Pro Leu Asp Thr Ala Ala Arg Xaa Pro 50 55 60 Pro Pro His Trp Pro Leu Val Gly Leu Thr Trp Arg Arg Cys Trp Thr 65 70 75 80 Lys Xaa Pro Gly Asp Arg Lys Phe Leu Ser Leu Leu Xaa Pro Ser Glu 85 90 95 Arg Phe Ser Ser Pro Lys Leu Pro Val Ser Pro Gin Asp Ser Xaa Phe 100 105 110 Ser His Leu Trp Thr Ser Gly Xaa Leu Lys Arg Xaa Phe Trp Val Thr 115 120 125 Pro Ala Ser Leu Gin Ser Gin Phe Trp Val Thr Leu He Cys Ser Ser 130 135 140 Thr Arg Pro He Arg Gly Ser Lys Leu Trp Leu Arg Arg Gly Arg Gly 145 150 155 160 Ser Cys He Pro Leu Arg Ser Pro Xaa Thr Pro Leu Val Ser Thr His 165 170 175 Arg Leu Met Ser Thr Thr Cys Arg Trp Arg Leu Arg Cys Leu Arg Arg 180 185 190 Leu Val Thr Thr Pro Gin Trp Tyr Met Leu Cys Ala Ser Thr Thr Leu 195 200 205 Val Ala Leu Trp Phe Pro Gin Met Gly Phe Pro Trp Gly Thr Ala Ser 210 215 220 Val Gly Arg Arg Ala Cys Xaa Gin Leu Ala Arg Arg Thr Ala Ser Leu 225 230 235 240 Val Thr Leu Arg Ser Ala Arg Pro Ala Gly Gly Trp Gly Leu Arg His 245 250 255 His His Ser Leu Xaa Leu Glu Met He 260 265 (2) INFORMATION FOR SEQ ID NO:75: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 264 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:75; He Arg Pro Leu Ser Gly Arg Glu Gly Tyr Asn Leu Glu Gly Xaa Xaa 1 5 10 15 Glu Val Xaa Gin Ala Leu Xaa Gly Cys Arg Xaa Gly Cys Pro Glu Lys 20 25 30 Gly Ser Arg Asp Glu Val Ser Trp Leu Asp Leu Phe Pro Gly Tyr Ser 35 40 * 45 Xaa Ser Xaa Ala Pro Ser Ser Arg Trp He Arg Gin Gin Gly Asp Arg 50 55 60 Leu His He Gly His Trp Leu Ala Ser Arg Gly Gly Asp Ala Gly Gin 65 70 75 80 Asn Ser Gin Gly Thr Gly Ser Ser Phe His Phe Cys Asp Gin Ala Arg 85 90 95 Gly Phe Leu Leu Gin Asn Tyr Pro Xaa Ala Pro Lys He His Ser Phe 100 105 110 Pro Thr Phe Gly Leu Gin Asp Ser Xaa Lys Asp Asp Ser Gly Xaa Pro 115 120 125 Arg His Arg Cys Lys Val Asn Ser Gly Xaa Arg Leu Ser Val Pro Val 130 135 140 His Ala Gin Ser Glu Gly Gin Ser Ser Gly Xaa Gly Val Gly Gly Glu 145 150 155 160 Val Ala Ser Arg Cys Asp His Arg Xaa Arg His Leu Phe Arg Leu He 165 170 175 Asp Xaa Xaa Ala Arg His Ala Gly Gly Gly Phe Gly Val Cys Gly Gly 180 185 190 Xaa Xaa Gin Pro Leu Asn Gly Thr Cys Phe Val Gin Val Leu Leu Trp 195 200 205 Trp Pro Tyr Gly Phe Pro Arg Trp Gly Ser Leu Gly Val Pro Pro Val 210 215 220 Xaa Val Val Gly Arg Val Asp Asn Xaa Leu Gly Glu Gin His His Leu 225 230 235 240 Leu His Xaa Gly Gin Arg Gly Leu Gin Ala Gly Gly Asp Xaa Gly Thr 245 250 255 He He Leu Tyr Ser Trp Arg Xaa 260 (2) INFORMATION FOR SEQ ID NO:76: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 264 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:76: Ser Gly Arg Xaa Ala Ala Glu Lys Val Thr He Trp Arg Gly Asp Arg 1 5 10 15 Lys Tyr Asp Lys His Tyr Glu Ala Val Val Glu Ala Val Leu Lys Lys 20 25 30 Ala Ala Ala Thr Lys Ser His Gly Trp Thr Tyr Ser Gin Ala He Ala 35 40 45 Lys Val Arg Arg Arg Ala Ala Ala Gly Tyr Gly Ser Lys Val Thr Ala 50 55 60 Ser Thr Leu Ala Thr Gly Trp Pro His Val Glu Glu Met Leu Asp Lys 65 70 75 80 He Ala Arg Gly Gin Glu Val Pro Phe Thr Phe Val Thr Lys Arg Glu 85 90 95 Val Phe Phe Ser Lys Thr Thr Arg Lys Pro Pro Arg Phe He Val Phe 100 105 110 Pro Pro Leu Asp Phe Arg He Ala Glu Lys Met He Leu Gly Asp Pro 115 120 125 Gly He Val Ala Lys Ser He Leu Gly Asp Ala Tyr Leu Phe Gin Tyr 130 135 140 Thr Pro Asn Gin Arg Val Lys Ala Leu Val Lys Ala Trp Glu Gly Lys 145 150 155 160 Leu His Pro Ala Ala He Thr Val Xaa Ala Thr Cys Phe Asp Ser Ser 165 170 175 He Asp Glu His Asp Met Gin Val Glu Ala Ser Val Phe Ala Ala Ala 180 185 190 Ser Asp Asn Pro Ser Met Val His Ala Leu Cys Lys Tyr Tyr Ser Gly 195 200 205 Gly Pro Met Val Ser Pro Asp Gly Val Pro Leu Gly Tyr Arg Gin Cys 210 215 220 Arg Ser Ser Gly Val Leu Thr Thr Ser Ser Ala Asn Ser He Thr Cys 225 230 235 240 Tyr He Lys Val Ser Ala Ala Cys Arg Arg Val Gly He Lys Ala Pro 245 250 255 Ser Phe Phe He Ala Gly Asp Asp 260 (2) INFORMATION FOR SEQ ID NO:77: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 265 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:77: Asn His Leu Gin Leu Xaa Arg Met Met Val Pro Xaa Ser Pro Pro Ala 1 5 10 15 Cys Arg Pro Arg Xaa Pro Xaa Cys Asn Lys Xaa Cys Cys Ser Pro Ser 20 25 30 Xaa Leu Ser Thr Arg Pro Thr Thr Tyr Thr Gly Gly Thr Pro Arg Glu 35 40 45 Pro His Leu Gly Lys Pro Xaa Gly His Gin Ser Ser Thr Cys Thr Lys 50 55 60 His Val Pro Leu Arg Gly Cys His Xaa Pro Pro Gin Thr Pro Lys Pro 65 70 75 80 Pro Pro Ala Cys Arg Ala His Gin Ser Met Ser Arg Asn Lys Trp Arg 85 90 95 Xaa Arg Xaa Ser Gin Arg Asp Ala Thr Ser Pro Pro Thr Pro Xaa Pro 100 105 110 Glu Leu Xaa Pro Ser Asp Trp Ala Cys Thr Gly Thr Asp Lys Arg His 115 120 125 Pro Glu Leu Thr Leu Gin Arg Cys Arg Gly His Pro Glu Ser Ser Phe 130 135 140 Gin Leu Ser Xaa Ser Pro Lys Val Gly Lys Leu Xaa He Leu Gly Ala 145 150 155 160 Tyr Gly Xaa Phe Trp Arg Arg Lys Pro Leu Ala Trp Ser Gin Lys Xaa 165 170 175 Lys Glu Leu Pro Val Pro Trp Leu Phe Cys Pro Ala Ser Pro Pro Arg 180 185 190 Glu Ala Asn Gin Trp Pro Met Trp Arg Arg Ser Pro Cys Cys Arg He 195 200 205 Gin Arg Leu Leu Gly Ala Xaa Leu Xaa Leu Xaa Pro Gly Asn Arg Ser 210 215 220 Ser His Glu Thr Ser Ser Arg Leu Pro Phe Ser Gly Gin Pro Gin Arg 225 230 235 240 Gin Pro His Asn Ala Cys His Thr Ser Tyr His Pro Ser Arg Leu Xaa 245 250 255 Pro Ser Arg Pro Leu Ser Gly Leu He 260 265 (2) INFORMATION FOR SEQ ID NO:78: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 264 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:78: He He Ser Ser Tyr Lys Glu Xaa Trp Cys Leu Asn Pro His Pro Pro 1 5 10 15 Ala Gly Arg Ala Asp Leu Asn Val Thr Ser Asp Ala Val Arg Arg Ala 20 25 30 Ser Cys Gin His Ala Arg Arg Pro Thr Leu Ala Val Pro Gin Gly Asn 35 40 45 Pro He Trp Gly Asn His Arg Ala Thr Arg Val Val Leu Ala Gin Ser 50 55 60 Met Tyr His Xaa Gly Val Val Thr Ser Arg Arg Lys His Arg Ser Leu 65 70 75 80 His Leu His Val Val Leu He Asn Arg Xaa Val Glu Thr Ser Gly Val 85 90 95 His Gly Asp Arg Ser Gly Met Gin Leu Pro Leu Pro Arg Leu Asn Gin 100 105 110 Ser Phe Asp Pro Leu He Gly Arg Val Leu Glu Gin He Ser Val Thr 115 120 125 Gin Asn Xaa Leu Cys Asn Asp Ala Gly Val Thr Gin Asn His Leu Phe 130 135 140 Ser Tyr Pro Glu Val Gin Arg Trp "Glu Asn Tyr Glu Ser Trp Gly Leu 145 150 155 160 Thr Gly Ser Phe Gly Glu Glu Asn Leu Ser Leu Gly His Lys Ser Glu 165 170 175 Arg Asn Phe Leu Ser Pro Gly Tyr Phe Val Gin His Leu Leu His Val 180 185 190 Arg Pro Thr Ser Gly Gin Cys Gly Gly Gly His Leu Ala Ala Val Ser 195 200 205 Ser Gly Cys Ser Ala Pro Asn Phe Ser Tyr Ser Leu Gly He Gly Pro 210 215 220 Ala Met Arg Leu Arg Arg Gly Cys Leu Phe Gin Asp Ser Leu Asn Asp 225 230 235 240 Ser Leu He Met Leu Val He Leu Pro He Thr Pro Pro Asp Cys Asn 245 250 255 Leu Leu Gly Arg Ser Ala Ala Xaa 260 (2) INFORMATION FOR SEQ ID NO:79: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 264 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:79: Ser Ser Pro Ala He Lys Asn Asp Gly Ala Leu He Pro Thr Arg Leu 1 5 10 15 Gin Ala Ala Leu Thr Leu Met Xaa Gin Val Met Leu Phe Ala Glu Leu 20 25 30 Val Val Asn Thr Pro Asp Asp Leu His Trp Arg Tyr Pro Lys Gly Thr 35 40 45 Pro Ser Gly Glu Thr He Gly Pro Pro Glu Xaa Tyr Leu His Lys Ala 50 55 60 Cys Thr He Glu Gly Leu Ser Leu Ala Ala Ala Asn Thr Glu Ala Ser 65 70 75 80 Thr Cys Met Ser Cys Ser Ser He Asp Glu Ser Lys Gin Val Ala Xaa 85 90 95 Thr Val He Ala Ala Gly Cys Asn Phe Pro Ser His Ala Leu Thr Arg 100 105 110 Ala Leu Thr Leu Xaa Leu Gly Val Tyr Trp Asn Arg Xaa Ala Ser Pro 115 120 125 Arg He Asp Phe Ala Thr Met Pro Gly Ser Pro Arg He He Phe Ser 130 135 140 Ala He Leu Lys Ser Lys Gly Gly Lys Thr Met Asn Leu Gly Gly Leu 145 150 155 160 Arg Val Val Leu Glu Lys Lys Thr Ser Arg Leu Val Thr Lys Val Lys 165 170 175 Gly Thr Ser Cys Pro Leu Ala He Leu Ser Ser He Ser Ser Thr Xaa 180 185 190 Gly Gin Pro Val Ala Asn Val Glu Ala Val Thr Leu Leu Pro Tyr Pro 195 200 205 Ala Ala Ala Arg Arg Leu Thr Leu Ala He Ala Trp Glu Xaa Val Gin 210 215 220 Pro Xaa Asp Phe Val Ala Ala Ala Phe Phe Arg Thr Ala Ser Thr Thr 225 230 235 240 Ala Ser Xaa Cys Leu Ser Tyr Phe Leu Ser Pro Leu Gin He Val Thr 245 250 255 Phe Ser Ala Ala Gin Arg Pro Asp 260 (2) INFORMATION FOR SEQ ID NO:80: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4268 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:80: TGGCTCATCC CACAGGCTCC ATACACCCAA TAACCGTTGA CGCGGCTAAT GACCAGGACA 60 TCTATCAACC ACCATGTGGA GCTGGGTCCC TTACTCGGTG CTCTTGCGGG GAGACCAAGG 120 GGTATCTGGT AACACGACTG GGGTCATTGG TTGAGGTCAA CAAATCCGAT GACCCTTATT 180 GGTGTGTGTG CGGGGCCCTT CCCATGGCTG TTGCCAAGGG TTCTTCAGGT GCCCCGATTC 240 TGTGCTCCTC CGGGCATGTT ATTGGGATGT TCACCGCTGC TAGAAATTCT GGCGGTTCAG 300 TCGGCCAGAT TAGGGTTAGG CCGTTGGTGT GTGCTGGATA CCATCCCCAG TACACAGCAC 360 ATGCCACTCT TGATACAAAA CCTACTGTGC CTAACGAGTA TTCAGTGCAA ATTTTAATTG 420 CCCCCACTGG CAGCGGCAAG TCAACCAAAT TACCACTTTC TTACATGCAG GRGAAGYATG 480 AGGTCTTGGT CCTAAATCCC AGTGTGGCTA CAACAGCATC AATGCCAAAG TACATGCACG 540 CGACGTACGG CGTGAATCCA AATTGCTATT TTAATGGCAA ATGTACCAAC ACAGGGGCTT 600 CACTTACGTA CAGCACATAT GGCATGTACC TGACCGGACG ATGTTCCCGG AACTATGATG 660 TAATCATTTG TGACGAATGC CATGCTACCG ATCGAACCAC CGTGTTGGGC ATTGGAAAGG 720 TCCTAACCGA AGCTCCATCC AAAAATGTTA GGCTAGTGGT TCTTGCCACG GCTACCCCCC 780 CTGGAGTAAT CCCTACACCA CATGCCAACA TAACTGAGAT TCAATTAACY GATGAAGGCA 840 CTATCCCCTT TCATGGAAAA AAGATTAAGG AGGAAAATCT GAAGAAAGGG AGACACCTTA 900 TCTTTGAGGC TACCAAAAAA CACTGTGATG AGCTTGCTAA CGAGTTAGCT CGAAAGGGAA 960 TAACAGCTGT CTCTTACTAT AGGGGATGTG ACATCTCAAA AATGCCTGAG GGCGACTGTG 1020 TAGTAGTTGC CACTGATGCC TTGTGTACAG GGTACACTGG TGACTTTGAT TCCGTGTATG 1080 ACTGCAGCCT CATGGTAGAA GGCACATGCC ATGTTGACCT ΥG&CS CΣliCτ .TTC CCATGG 1140 GTGTTCGTGT GTGCGGGGTT TCAGCAATAG TTAAAGGCCA GCGTAGGGGC CGCACAGGCC 1200 GTGGGAGAGC TGGCATATAC TACTATGTAG ACGGGAGTTG TACCCCTTCG GGTATGGTTC 1260 CTGAATGCAA CATTGTTGAA GCCTTCGACG CAGCCAAGGC ATGGTATGGT TTGTCATCAA 1320 CAGAAGCTCA AACTATTCTG GACACCTATC GCACCCAACC TGGGTTACCT GCGATAGGAG 1380 CAAATTTGGA CGAGTGGGCT GATCTCTTTT CTATGGTCAA CCCCGAACCT TCATTTGTCA 1440 ATACTGCAAA AAGAACTGCT GACAATTATG TTTTGTTGAC TGCAGCCCAA CTACAACTGT 1500 GTCATCAGTA TGGCTATGCT GCTCCCAATG ACGCACCACG GTGGCAGGGA GCCCGGCTTG 1560 GGAAAAAACC TTGTGGGGTT CTGTGGCGCT TGGACGGCTG TGACGCCTGT CCTGGCCCAG 1620 AGCCCAGCGA GGTGACCAGA TACCAAATGT GCTTCACTGA AGTCAATACT TCTGGGACAG 1680 CCGCACTCGC TGTTGGCGTT GGAGTGGCTA TGGCTTATCT AGCCATTGAC ACTTTTGGCG 1740 CCACTTGTGT GCGGCGTTGC TGGTCTATTA CATCAGTCCC TACCGGTGCT ACTGTCGCCC 1800 CAGTGGTTGA CGAAGAGGAA ATCGTGGAGG AGTGTGCATC ATTCATTCCC TTGGAGGCCA 1860 TGGTTGCTGC AATTGACAAG CTGAAGAGTA CAATCACCAC AACTAGTCCT TTCACATTGG 1920 AAACCGCCCT TGAAAAACTT AACACCTTTC TTGGGCCTCA TGCAGCTACA ATCCTTGCTA 1980 TCATAGAGTA TTGCTGTGGC TTAGTCACTT TACCTGACAA TCCCTTTGCA TCATGCGTGT 2040 TTGCTTTCAT TGCGGGTATT ACTACCCCAC TACCTCACAA GATCAAAATG TTCCTGTCAT 2100 TATTTGGAGG CGCAATTGCG TCCAAGCTTA CAGACGCTAG AGRCGCACTG GCGTTCATGA 2160 TGGCCGGGGC TGYGGGAACA GCTCTTGGTA CATGGACATC GGTGGGTTTT GTCTTTGACA 2220 TGCTAGGCGG CTATGCTGGC GCCTCATCCA CTGCTTGCTT GACATTTAAA TGCTTGATGG 2280 GTGAGTGGCY CACTATGGAT CAGCTTGCTG GTTTAGTCTA CTCCGCGTTC AATCCGGCCG 2340 CAGGAGTTGT GGGCGTCTTG TCAGCTTGTG CAATGTTTGC TTTGACAACA GCAGGGCCAG 2400 ATCACTGGCC CAACAGACTT CTTACTATGC TTGCTAGGAG CAACACTGTA TGTARTGAGT 2460 ACTTTATTGC CACTCGTGAC ATCCGCAGGA AGATACTGGG CATTCTGGAG GCATCTACCC 2520 CCTGGAGTRT CATATCAGCT TGCATCCGTT GGCTYCACAC CCCGACGGAG GATGATTGCG 2580 GCCTCATTGC TTGGGGTCTA RAGATTTGGC AGTATGTGTG CAATTTCTTT GTGATTTGCT 2640 TTAATGTCCT TAAAGCTGGA GTTCAGAGCA TGGTTAACAT TCCTGGTTGT CCTTTCTACA 2700 GCTGCCAGAA GGGGTACAAG GGCCCCTGGA TTGGATCAGG TATGCTCCAA GCACGCTGTC 2760 CATGCGGTGC TGAACTCATC TTTTCTGTTG AGAATGGTTT TGCAAAACTT TACAAAGGAC 2820 CCAGAACTTG TTCAAATTAC TGGAGAGGGG CTGTTCCAGT CAACGCTAGG CTGTGTGGGT 2880 CGGCTAGACC GGACCCAACT GATTGGACTA GTCTTGTCGT CAATTATGGC GTTAGGGACT 2940 ACTGTAAATA TGAGAAATTG GGAGATCACA TTTTTGTTAC AGCAGTATCC TCTCCAAATG 3000 TCTGTTTCAC CCAGGTGCCC CCAACCTTGA GAGCTGCAGT GGCCGTGGAC CGCGTACAGG 3060 TTCAGYGTTA TCTAGGTGAG CCCAAAACTC CTTGGACGAC ATCTGCTTGC TGTTACGGTC 3120 CTGACGGTAA GGGTAAAACT GTTAAGCTTC CCTTCCGCGT TGACGGACAC ACACCTGGTG 3180 GTCGCATGCA ACTTAATTTG CGTGATCGAC TTGAGGCAAA TGACTGTAAT TCCATAAACA 3240 ACACTCCTAG TGATGAAGCC GCAGTGTCCG CTCTTGTTTT CAAACAGGAG TTGCGGCGTA 3300 CAAACCAATT GCTTGAGGCA ATTTCAGCTG GCGTTGACAC CACCAAACTG CCAGCCCCCT 3360 CCCAGATCGA AGAGGTAGTG GTAAGAAAGC GCCAGTTCCG GGCAAGAACT GGTTCGCTTA 3420 CCTTGCCTCC CCCTCCGAGA TCCGTCCCAG GAGTGTCATG TCCTGAAAGC CTGCAACGAA 3480 GTGACCCGTT AGAAGGTCCT TCAAMCCTCC CTTCTTCACC ACCTGTTCTR CAGTTGGCCA 3540 TGCCGATGCC CCTGTTGGGA GCAGGTGAGT GTAACCCTTT CACTGCAATT GGATGTGCAA 3600 TGACCGAAAC ARGYGGAGKC CCWSAKRATT TACCCAGTTA CCCTCCCAAA AAGGAGGTCT 3660 CTGAATGGTC AGACGAAAGT TGGTCAACGA CTACAACCGC TTCCAGCTAC GTTACTGGCC 3720 CCCCGTACCC TAAGATACGG GGCAAGGATT CCACTCAATC AGCCACCGCC AAACGGCCTA 3780 CAAAAAAGAA GTTGGGAAAG AGTGAGTTTT CGTGCAGCAT GAGCTACACT TGGACCGACG 3840 TGATTAGCTT CAAAACTGCT TCTAAAGTTC TGTCTGCAAC TCGGGCCATC ACTAGTGGTT 3900 TCCTCAAACA AAGATCATTG GTGTATGTGA CTGAGCCGCG GGATGCGGAG CTTAGAAAAC 3960 AAAAAGTCAC TATTAATAGA CAACCTCTGT TCCCCCCATC ATACCACAAG CAAGTGAGAT 4020 TGGCTAAGGA AAAAGCTTCA AAAGTTGTCG GTGTCATGTG GGACTATGAT GAAGTAGCAG 080 CTCACACGCC CTCTAAGTCT GCTAAGTCCC ACATCACTGG CCTTCGGGGC ACTGATGTTC 4140 TGGACTTGCA GAAGTGTGTC GAGGCAGGTG AGATACCGAG TCATTATCGG CAAACTGTGA 4200 TAGTTCCAAA GGAGGAGGTC TTCGTGAAGA CCCCCCAGAA ACCAACAAAG AAACCCCCAA 4260 GGCTTATC 4268 (2) INFORMATION FOR SEQ ID NO:81: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1422 amino acidθ (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:81: Trp Leu He Pro Gin Ala Pro Tyr Thr Gin Xaa Pro Leu Thr Arg Leu 1 5 10 15 Met Thr Arg Thr Ser He Asn His His Val Glu Leu Gly Pro Leu Leu 20 25 30 Gly Ala Leu Ala Gly Arg Pro Arg Gly He Trp Xaa His Asp Trp Gly 35 40 45 His Trp Leu Arg Ser Thr Asn Pro Met Thr Leu He Gly Val Cys Ala 50 55 60 Gly Pro Phe Pro Trp Leu Leu Pro Arg Val Leu Gin Val Pro Arg Phe 65 70 75 80 Cys Ala Pro Pro Gly Met Leu Leu Gly Cys Ser Pro Leu Leu Glu He 85 90 95 Leu Ala Val Gin Ser Ala Arg Leu Gly Leu Gly Arg Trp Cys Val Leu 100 105 110 Asp Thr He Pro Ser Thr Gin His Met Pro Leu Leu He Gin Asn Leu 115 120 125 Leu Cys Leu Thr Ser He Gin Cys Lys Phe Xaa Leu Pro Pro Leu Ala 130 135 140 Ala Ala Ser Gin Pro Asn Tyr His Phe Leu Thr Cys Arg Xaa Ser Met 145 150 155 160 Arg Ser Trp Ser Xaa He Pro Val Trp Leu Gin Gin His Gin Cys Gin 165 170 175 Ser Thr Cys Thr Arg Arg Thr Ala Xaa He Gin He Ala He Leu Met 180 185 190 Ala Asn Val Pro Thr Gin Gly Leu His Leu Arg Thr Ala His Met Ala 195 200 205 Cys Thr Xaa Pro Asp Asp Val Pro Gly Thr Met Met Xaa Ser Phe Val 210 215 220 Thr Asn Ala Met Leu Pro He Glu Pro Pro Cys Trp Ala Leu Glu Arg 225 230 235 240 Ser Xaa Pro Lys Leu His Pro Lys Met Leu Gly Xaa Trp Phe Leu Pro 245 250 255 Arg Leu Pro Pro Leu Glu Xaa Ser Leu His His Met Pro Thr Xaa Leu 260 265 270 Arg Phe Asn Xaa Xaa Met Lys Ala Leu Ser Pro Phe Met Glu Lys Arg 275 280 285 Leu Arg Arg Lys He Xaa Arg Lys Gly Asp Thr Leu Ser Leu Arg Leu 290 295 300 Pro Lys Asn Thr Val Met Ser Leu Leu Thr Ser Xaa Leu Glu Arg Glu 305 310 315 320 Xaa Gin Leu Ser Leu Thr He Gly Asp Val Thr Ser Gin Lys Cys Leu 325 330 335 Arg Ala Thr Val Xaa Xaa Leu Pro Leu Met Pro Cys Val Gin Gly Thr 340 345 350 Leu Val Thr Leu He Pro Cys Met Thr Ala Ala Ser Trp Xaa Lys Ala 355 360 365 His Ala Met Leu Thr Leu Thr Leu Leu Ser Pro Trp Val Phe Val Cys 370 375 380 Ala Gly Phe Gin Gin Xaa Leu Lys Ala Ser Val Gly Ala Ala Gin Ala 385 390 395 400 Val Gly Glu Leu Ala Tyr Thr Thr Met Xaa Thr Gly Val Val Pro Leu 405 410 415 Arg Val Trp Phe Leu Asn Ala Thr Leu Leu Lys Pro Ser Thr Gin Pro 420 425 430 Arg His Gly Met Val Cys His Gin Gin Lys Leu Lys Leu Phe Trp Thr 435 440 445 Pro He Ala Pro Asn Leu Gly Tyr Leu Arg Xaa Glu Gin He Trp Thr 450 455 460 Ser Gly Leu He Ser Phe Leu Trp Ser Thr Pro Asn Leu His Leu Ser 465 470 475 480 He Leu Gin Lys Glu Leu Leu Thr He Met Phe Cys Xaa Leu Gin Pro 485 490 495 Asn Tyr Asn Cys Val He Ser Met Ala Met Leu Leu Pro Met Thr His 500 505 510 His Gly Gly Arg Glu Pro Gly Leu Gly Lys Asn Leu Val Gly Phe Cys 515 520 525 Gly Ala Trp Thr Ala Val Thr Pro Val Leu Ala Gin Ser Pro Ala Arg 530 535 540 Xaa Pro Asp Thr Lys Cys Ala Ser Leu Lys Ser He Leu Leu Gly Gin 545 550 555 560 .. Pro His Ser Leu Leu Ala Leu Glu Trp Leu Trp Leu He Xaa Pro Leu 565 570 575 Thr Leu Leu Ala Pro Leu Val Cys Gly Val Ala Gly Leu Leu His Gin 580 585 590 Ser Leu Pro Val Leu Leu Ser Pro Gin Trp Leu Thr Lys Arg Lys Ser 595 600 605 Trp Arg Ser Val His His Ser Phe Pro Trp Arg Pro Trp Leu Leu Gin 610 615 620 Leu Thr Ser Xaa Arg Val Gin Ser Pro Gin Leu Val Leu Ser His Trp 625 630 635 640 Lys Pro Pro Leu Lys Asn Leu Thr Pro Phe Leu Gly Leu Met Gin Leu 645 650 655 Gin Ser Leu Leu Ser Xaa Ser He Ala Val Ala Xaa Ser Leu Tyr Leu 660 665 670 Thr He Pro Leu His His Ala Cys Leu Leu Ser Leu Arg Val Leu Leu 675 680 685 Pro His Tyr Leu Thr Arg Ser Lys Cys Ser Cys His Tyr Leu Glu Ala 690 695 700 Gin Leu Arg Pro Ser Leu Gin Thr Leu Glu Xaa His Trp Arg Ser Xaa 705 710 715 720 Trp Pro Gly Leu Xaa Glu Gin Leu Leu Val His Gly His Arg Trp Val 725 730 735 Leu Ser Leu Thr Cys Xaa Ala Ala Met Leu Ala Pro His Pro Leu Leu 740 745 750 Ala Xaa His Leu Asn Ala Xaa Trp Val Ser Gly Xaa Leu Trp He Ser 755 760 765 Leu Leu Val Xaa Ser Thr Pro Arg Ser He Arg Pro Gin Glu Leu Trp 770 775 780 Ala Ser Cys Gin Leu Val Gin Cys Leu Leu Xaa Gin Gin Gin Gly Gin 785 790 795 800 He Thr Gly Pro Thr Asp Phe Leu Leu Cys Leu Leu Gly Ala Thr Leu 805 810 815 Tyr Val Xaa Ser Thr Leu Leu Pro Leu Val Thr Ser Ala Gly Arg Tyr 820 825 830 Trp Ala Phe Trp Arg His Leu Pro Pro Gly Val Ser Tyr Gin Leu Ala 835 840 845 Ser Val Gly Xaa Thr Pro Arg Arg Arg Met He Ala Ala Ser Leu Leu 850 855 860 Gly Val Xaa Arg Phe Gly Ser Met Cys Ala He Ser Leu Xaa Phe Ala 865 870 875 880 Leu Met Ser Leu Lys Leu Glu Phe Arg Ala Trp Leu Thr Phe Leu Val 885 890 895 Val Leu Ser Thr Ala Ala Arg Arg Gly Thr Arg Ala Pro Gly Leu Asp 900 905 910 Gin Val Cys Ser Lys His Ala Val His Ala Val Leu Asn Ser Ser Phe 915 920 925 Leu Leu Arg Met Val Leu Gin Asn Phe Thr Lys Asp Pro Glu Leu Val 930 935 940 Gin He Thr Gly Glu Gly Leu Phe Gin Ser Thr Leu Gly Cys Val Gly 945 950 955 960 Arg Leu Asp Arg Thr Gin Leu He Gly Leu Val Leu Ser Ser He Met 965 970 975 Ala Leu Gly Thr Thr Val Asn Met Arg Asn Trp Glu He Thr Phe Leu 980 985 990 Leu Gin Gin Tyr Pro Leu Gin Met Ser Val Ser Pro Arg Cys Pro Gin 995 1000 1005 Pro Xaa Glu Leu Gin Trp Pro Trp Thr Ala Tyr Arg Phe Ser Val He 1010 1015 1020 Xaa Val Ser Pro Lys Leu Leu Gly Arg His Leu Leu Ala Val Thr Val 1025 1030 1035 1040 Leu Thr Val Arg Val Lys Leu Leu Ser Phe Pro Ser Ala Leu Thr Asp 1045 1050 1055 Thr His Leu Val Val Ala Cys Asn Leu He Cys Val He Asp Leu Arg 1060 1065 1070 Gin Met Thr Val He Pro Xaa Thr Thr Leu Leu Val Met Lys Pro Gin 1075 1080 1085 Cys Pro Leu Leu Phe Ser Asn Arg Ser Cys Gly Val Gin Thr Asn Cys 1090 1095 1100 Leu Arg Gin Phe Gin Leu Ala Leu Thr Pro Pro Asn Cys Gin Pro Pro 1105 1110 1115 1120 Pro Arg Ser Lys Arg Xaa Trp Xaa Glu Ser Ala Ser Ser Gly Gin Glu 1125 1130 1135 Leu Val Arg Leu Pro Cys Leu Pro Leu Arg Asp Pro Ser Gin Glu Cys 1140 1145 1150 His Val Leu Lys Ala Cys Asn Glu Val Thr Arg Xaa Lys Val Leu Gin 1155 1160 1165 Xaa Ser Leu Leu His His Leu Phe Xaa Ser Trp Pro Cys Arg Cys Pro 1170 1175 1180 Cys Trp Glu Gin Val Ser Val Thr Leu Ser Leu Gin Leu Asp Val Gin 1185 1190 1195 1200 Xaa Pro Lys Gin Xaa Glu Xaa Xaa Xaa He Tyr Pro Val Thr Leu Pro 1205 1210 1215 Lys Arg Arg Ser Leu Asn Gly Gin Thr Lys Val Gly Gin Arg Leu Gin 1220 1225 1230 Pro Leu Pro Ala Thr Leu Leu Ala Pro Arg Thr Leu Arg Tyr Gly Ala 1235 1240 1245 Arg He Pro Leu Asn Gin Pro Pro Pro Asn Gly Leu Gin Lys Arg Ser 1250 1255 1260 Trp Glu Arg Val Ser Phe Arg Ala Ala Xaa Ala Thr Leu Gly Pro Thr 1265 1270 1275 1280 Xaa Leu Ala Ser Lys Leu Leu Leu Lys Phe Cys Leu Gin Leu Gly Pro 1285 1290 1295 Ser Leu Val Val Ser Ser Asn Lys Asp His Trp Cys Met Xaa Leu Ser 1300 1305 1310 Arg Gly Met Arg Ser Leu Glu Asn Lys Lys Ser Leu Leu He Asp Asn 1315 1320 1325 Leu Cys Ser Pro His His Thr Thr Ser Lys Xaa Asp Trp Leu Arg Lys 1330 1335 1340 Lys Leu Gin Lys Leu Ser Val Ser Cys Gly Thr Met Met Lys Xaa Gin 1345 1350 1355 1360 Leu Thr Arg Pro Leu Ser Leu Leu Ser Pro Thr Ser Leu Ala Phe Gly 1365 1370 1375 Ala Leu Met Phe Trp Thr Cys Arg Ser Val Ser Arg Gin Val Arg Tyr 1380 1385 1390 Arg Val He He Gly Lys Leu Xaa Xaa Phe Gin Arg Arg Arg Ser Ser 1395 1400 1405 Xaa Arg Pro Pro Arg Asn Gin Gin Arg Asn Pro Gin Gly Leu 1410 1415 1420 (2) INFORMATION FOR SEQ ID NO:82: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1422 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:82: Gly Ser Ser His Arg Leu His Thr Pro Asn Asn Arg Xaa Arg Gly Xaa 1 5 10 15 Xaa Pro Gly His Leu Ser Thr Thr Met Trp Ser Trp Val Pro Tyr Ser 20 25 30 Val Leu Leu Arg Gly Asp Gin Gly Val Ser Gly Asn Thr Thr Gly Val 35 40 45 He Gly Xaa Gly Gin Gin He Arg Xaa Pro Leu Leu Val Cys Val Arg 50 55 60 Gly Pro Ser His Gly Cys Cys Gin Gly Phe Phe Arg Cys Pro Asp Ser 65 70 75 80 Val Leu Leu Arg Ala Cys Tyr Trp Asp Val His Arg Cys Xaa Lys Phe 85 90 95 Trp Arg Phe Ser Arg Pro Asp Xaa Gly Xaa Ala Val Gly Val Cys Trp 100 105 110 He Pro Ser Pro Val His Ser Thr Cys His Ser Xaa Tyr Lys Thr Tyr 115 120 125 Cys Ala Xaa Arg Val Phe Ser Ala Asn Phe Asn Cys Pro His Trp Gin 130 135 140 Arg Gin Val Asn Gin He Thr Thr Phe Leu His Ala Gly Glu Xaa Xaa 145 150 155 160 Gly Leu Gly Pro Lys Ser Gin Cys Gly Tyr Asn Ser He Asn Ala Lys 165 170 175 Val His Ala Arg Asp Val Arg Arg Glu Ser Lys Leu Leu Phe Xaa Trp 180 185 190 Gin Met Tyr Gin His Arg Gly Phe Thr Tyr Val Gin His He Trp His 195 200 205 Val Pro Asp Arg Thr Met Phe Pro Glu Leu Xaa Cys Asn His Leu Xaa 210 215 220 Arg Met Pro Cys Tyr Arg Ser Asn His Arg Val Gly His Trp Lys Gly 225 230 235 240 Pro Asn Arg Ser Ser He Gin Lys Cys Xaa Ala Ser Gly Ser Cys His 245 250 255 Gly Tyr Pro Pro Trp Ser Asn Pro Tyr Thr Thr Cys Gin His Asn Xaa 260 265 270 Asp Ser He Asn Xaa Xaa Arg His Tyr Pro Leu Ser Trp Lys Lys Asp 275 280 285 Xaa Gly Gly Lys Ser Glu Glu Arg Glu Thr Pro Tyr Leu Xaa Gly Tyr 290 295 300 Gin Lys Thr Leu Xaa Xaa Ala Cys Xaa Arg Val Ser Ser Lys Gly Asn 305 310 315 320 Asn Ser Cys Leu Leu Leu Xaa Gly Met Xaa His Leu Lys Asn Ala Xaa 325 330 335 Gly Arg Leu Cys Ser Ser Cys His Xaa Cys Leu Val Tyr Arg Val His 340 345 350 Trp Xaa Leu Xaa Phe Arg Val Xaa Leu Gin Pro His Gly Arg Arg His 355 360 365 Met Pro Cys Xaa Pro Xaa Pro Tyr Phe His His Gly Cys Ser Cys Val 370 375 380 Arg Gly Phe Ser Asn Ser Xaa Arg Pro Ala Xaa Gly Pro His Arg Pro 385 390 395 400 Trp Glu Ser Trp His He Leu Leu Cys Arg Arg Glu Leu Tyr Pro Phe 405 410 415 Gly Tyr Gly Ser Xaa Met Gin His Cys Xaa Ser Leu Arg Arg Ser Gin 420 425 430 Gly Met Val Trp Phe Val He Asn Arg Ser Ser Asn Tyr Ser Gly His 435 440 445 Leu Ser His Pro Thr Trp Val Thr Cys Asp Arg Ser Lys Phe Gly Arg 450 455 460 Val Gly Xaa Ser Leu Phe Tyr Gly Gin Pro Arg Thr Phe He Cys Gin 465 470 475 480 Tyr Cys Lys Lys Asn Cys Xaa Gin Leu Cys Phe Val Asp Cys Ser Pro 485 490 495 Thr Thr Thr Val Ser Ser Val Trp Leu Cys Cys Ser Gin Xaa Arg Thr 500 505 510 Thr Val Ala Gly Ser Pro Ala Trp Glu Lys Thr Leu Trp Gly Ser Val 515 520 525 Ala Leu Gly Arg Leu Xaa Arg Leu Ser Trp Pro Arg Ala Gin Arg Gly 530 535 540 Asp Gin He Pro Asn Val Leu His Xaa Ser Gin Tyr Phe Trp Asp Ser 545 550 555 560 Arg Thr Arg Cys Trp Arg Trp Ser Gly Tyr Gly Leu Ser Ser His Xaa 565 570 575 His Phe Trp Arg His Leu Cys Ala Ala Leu Leu Val Tyr Tyr He Ser 580 585 590 Pro Tyr Arg Cys Tyr Cys Arg Pro Ser Gly Xaa Arg Arg Gly Asn Arg 595 600 605 Gly Gly Val Cys He He His Ser Leu Gly Gly His Gly Cys Cys Asn 610 615 620 Xaa Gin Ala Glu Glu Tyr Asn His His Asn Xaa Ser Phe His He Gly 625 630 635 640 Asn Arg Pro Xaa Lys Thr Xaa His Leu Ser Trp Ala Ser Cys Ser Tyr 645 650 655 Asn Pro Cys Tyr His Arg Val Leu Leu Trp Leu Ser His Phe Thr Xaa 660 665 670 Gin Ser Leu Cys He Met Arg Val Cys Phe His Cys Gly Tyr Tyr Tyr 675 680 685 Pro Thr Thr Ser Gin Asp Gin Asn Val Pro Val He He Trp Arg Arg 690 695 700 Asn Cys Val Gin Ala Tyr Arg Arg Xaa Arg Arg Thr Gly Val His Asp 705 710 715 720 Gly Arg Gly Cys Gly Asn Ser Ser Trp Tyr Met Asp He Gly Gly Phe 725 730 735 Cys Leu Xaa His Ala Arg Arg Leu Cys Trp Arg Leu He His Cys Leu 740 745 750 Leu Asp He Xaa Met Leu Asp Gly Xaa Val Ala His Tyr Gly Ser Ala 755 760 765 Cys Trp Phe Ser Leu Leu Arg Val Gin Ser Gly Arg Arg Ser Cys Gly 770 775 780 Arg Leu Val Ser Leu Cys Asn Val Cys Phe Asp Asn Ser Arg Ala Arg 785 790 795 800 Ser Leu Ala Gin Gin Thr Ser Tyr Tyr Ala Cys Xaa Glu Gin His Cys 805 810 815 Met Xaa Xaa Val Leu Tyr Cys His Ser Xaa His Pro Gin Glu Asp Thr 820 825 830 Gly His Ser Gly Gly He Tyr Pro Leu Glu Xaa His He Ser Leu His 835 840 845 Pro Leu Ala Xaa His Pro Asp Gly Gly Xaa Leu Arg Pro His Cys Leu 850 855 860 Gly Ser Xaa Asp Leu Ala Val Cys Val Gin Phe Leu Cys Asp Leu Leu 865 870 875 880 Xaa Cys Pro Xaa Ser Trp Ser Ser Glu His Gly Xaa His Ser Trp Leu 885 890 895 Ser Phe Leu Gin Leu Pro Glu Gly Val Gin Gly Pro Leu Asp Trp He 900 905 910 Arg Tyr Ala Pro Ser Thr Leu Ser Met Arg Cys Xaa Thr His Leu Phe 915 920 925 Cys Xaa Glu Trp Phe Cys Lys Thr Leu Gin Arg Thr Gin Asn Leu Phe 930 935 940 Lys Leu Leu Glu Arg Gly Cys Ser Ser Gin Arg Xaa Ala Val Trp Val 945 950 955 960 Gly Xaa Thr Gly Pro Asn Xaa Leu Asp Xaa Ser Cys Arg Gin Leu Trp 965 970 975 Arg Xaa Gly Leu Leu Xaa He Xaa Glu He Gly Arg Ser His Phe Cys 980 985 990 Tyr Ser Ser He Leu Ser Lys Cys Leu Phe His Pro Gly Ala Pro Asn 995 1000 1005 Leu Glu Ser Cys Ser Gly Arg Gly Pro Arg Thr Gly Ser Xaa Leu Ser 1010 1015 1020 Arg Xaa Ala Gin Asn Ser Leu Asp Asp He Cys Leu Leu Leu Arg Ser 1025 1030 1035 1040 Xaa Arg Xaa Gly Xaa Asn Cys Xaa Ala Ser Leu Pro Arg Xaa Arg Thr 1045 1050 1055 His Thr Trp Trp Ser His Ala Thr Xaa Phe Ala Xaa Ser Thr Xaa Gly 1060 1065 1070 Lys Xaa Leu Xaa Phe His Lys Gin His Ser Xaa Xaa Xaa Ser Arg Ser 1075 1080 1085 Val Arg Ser Cys Phe Gin Thr Gly Val Ala Ala Tyr Lys Pro He Ala 1090 1095 1100 Xaa Gly Asn Phe Ser Trp Arg Xaa His His Gin Thr Ala Ser Pro Leu 1105 1110 1115 1120 Pro Asp Arg Arg Gly Ser Gly Lys Lys Ala Pro Val Pro Gly Lys Asn 1125 1130 1135 Trp Phe Ala Tyr Leu Ala Ser Pro Ser Glu He Arg Pro Arg Ser Val 1140 1145 1150 Met Ser Xaa Lys Pro Ala Thr Lys Xaa Pro Val Arg Arg Ser Phe Xaa 1155 1160 1165 Pro Pro Phe Phe Thr Thr Cys Ser Xaa Val Gly His Ala Asp Ala Pro 1170 1175 1180 Val Gly Ser Arg Xaa Val Xaa Pro Phe His Cys Asn Trp Met Cys Asn 1185 1190 1195 1200 Asp Arg Asn Xaa Xaa Xaa Pro Xaa Xaa Phe Thr Gin Leu Pro Ser G n 1205 1210 1215 Lys Gly Gly Leu Xaa Met Val Arg Arg Lys Leu Val Asn Asp Tyr Asn 1220 1225 1230 Arg Phe Gin Leu Arg Tyr Trp Pro Pro Val Pro Xaa Asp Thr Gly Gin 1235 1240 1245 Gly Phe His Ser He Ser His Arg Gin Thr Ala Tyr Lys Lyø Glu Val 1250 1255 1260 Gly Lys Glu Xaa Val Phe Val Gin His Glu Leu His Leu Asp Arg Arg 1265 1270 1275 1280 Asp Xaa Leu Gin Asn Cys Phe Xaa Ser Ser Val Cys Asn Ser Gly His 1285 1290 1295 His Xaa Trp Phe Pro Gin Thr Lys He He Gly Val Cys Asp Xaa Ala 1300 1305 1310 Ala Gly Cys Gly Ala Xaa Lys Thr Lys Ser His Tyr Xaa Xaa Thr Thr 1315 1320 1325 Ser Val Pro Pro He He Pro Gin Ala Ser Glu He Gly Xaa Gly Lys 1330 1335 1340 Ser Phe Lys Ser Cys Arg Cys His Val Gly Leu Xaa Xaa Ser Ser Ser 1345 1350 1355 1360 Ser His Ala Leu Xaa Val Cys Xaa Val Pro His His Trp Pro Ser Gly 1365 1370 1375 His Xaa Cys Ser Gly Leu Ala Glu Val Cys Arg Gly Arg Xaa Asp Thr 1380 1385 1390 Glu Ser Leu Ser Ala Asn Cys Asp Ser Ser Lys Gly Gly Gly Leu Arg 1395 1400 1405 Glu Asp Pro Pro Glu Thr Asn Lys Glu Thr Pro Lys Ala Tyr 1410 1415 1420 (2) INFORMATION FOR SEQ ID NO:83: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1422 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:83: Ala His Pro Thr Gly Ser He His Pro He Thr Val Asp Ala Ala Asn 1 5 10 15 Asp Gin Asp He Tyr Gin Pro Pro Cys Gly Ala Gly Ser Leu Thr Arg 20 25 30 Cys Ser Cys Gly Glu Thr Lys Gly Tyr Leu Val Thr Arg Leu Gly Ser 35 40 45 Leu Val Glu Val Asn Lys Ser Asp Asp Pro Tyr Trp Cys Val Cys Gly 50 55 60 Ala Leu Pro Met Ala Val Ala Lys Gly Ser Ser Gly Ala Pro He Leu 65 70 75 80 Cys Ser Ser Gly His Val He Gly Met Phe Thr Ala Ala Arg Asn Ser 85 90 95 Gly Gly Ser Val Gly Gin He Arg Val Arg Pro Leu Val Cys Ala Gly 100 105 110 Tyr His Pro Gin Tyr Thr Ala His Ala Thr Leu Asp Thr Lys Pro Thr 115 120 125 Val Pro Asn Glu Tyr Ser Val Gin He Leu He Ala Pro Thr Gly Ser 130 135 140 Gly Lys Ser Thr Lys Leu Pro Leu Ser Tyr Met Gin Xaa Lys Xaa Glu 145 150 155 160 Val Leu Val Leu Asn Pro Ser Val Ala Thr Thr Ala Ser Met Pro Lys 165 170 175 Tyr Met His Ala Thr Tyr Gly Val Asn Pro Asn Cys Tyr Phe Asn Gly 180 185 190 Lys Cys Thr Asn Thr Gly Ala Ser Leu Thr Tyr Ser Thr Tyr Gly Met 195 200 205 Tyr Leu Thr Gly Arg Cys Ser Arg Asn Tyr Asp Val He He Cys Asp 210 215 220 Glu Cys His Ala Thr Asp Arg Thr Thr Val Leu Gly He Gly Lys Val 225 230 235 240 Leu Thr Glu Ala Pro Ser Lys Asn Val Arg Leu Val Val Leu Ala Thr 245 250 255 Ala Thr Pro Pro Gly Val He Pro Thr Pro His Ala Asn He Thr Glu 260 265 270 He Gin Leu Thr Asp Glu Gly Thr He Pro Phe His Gly Lys Lys He. 275 280 285 Lys Glu Glu Asn Leu Lys Lys Gly Arg His Leu He Phe Glu Ala Thr 290 295 300 Lys Lys His Cys Asp Glu Leu Ala Asn Glu Leu Ala Arg Lys Gly He 305 310 315 320 Thr Ala Val Ser Tyr Tyr Arg Gly Cys Asp He Ser Lys Met Pro Glu 325 330 335 Gly Asp Cys Val Val Val Ala Thr Asp Ala Leu Cys Thr Gly Tyr Thr 340 345 350 Gly Asp Phe Asp Ser Val Tyr Asp Cys Ser Leu Met Val Glu Gly Thr 355 360 365 Cys His Val Asp Leu Asp Pro Thr Phe Thr Met Gly Val Arg Val Cys 370 375 380 Gly Val Ser Ala He Val Lys Gly Gin Arg Arg Gly Arg Thr Gly Arg 385 390 395 400 Gly Arg Ala Gly He Tyr Tyr Tyr Val Asp Gly Ser Cys Thr Pro Ser 405 410 415 Gly Met Val Pro Glu Cys Asn He Val Glu Ala Phe Asp Ala Ala Lys 420 425 430 Ala Trp Tyr Gly Leu Ser Ser Thr Glu Ala Gin Thr He Leu Asp Thr 435 440 445 Tyr Arg Thr Gin Pro Gly Leu Pro Ala He Gly Ala Asn Leu Asp Glu 450 455 460 Trp Ala Asp Leu Phe Ser Met Val Asn Pro Glu Pro Ser Phe Val Asn 465 470 475 480 Thr Ala Lys Arg Thr Ala Asp Asn Tyr Val Leu Leu Thr Ala Ala Gin 485 490 495 Leu Gin Leu Cys His Gin Tyr Gly Tyr Ala Ala Pro Asn Asp Ala Pro 500 505 510 Arg Trp Gin Gly Ala Arg Leu Gly Lys Lys Pro Cys Gly Val Leu Trp 515 520 525 Arg Leu Asp Gly Cys Asp Ala Cys Pro Gly Pro Glu Pro Ser Glu Val 530 535 540 Thr Arg Tyr Gin Met Cys Phe Thr Glu Val Asn Thr Ser Gly Thr Ala 545 550 555 560 Ala Leu Ala Val Gly Val Gly Val Ala Met Ala Tyr Leu Ala He Asp 565 570 575 Thr Phe Gly Ala Thr Cys Val Arg Arg Cys Trp Ser He Thr Ser Val 580 585 590 Pro Thr Gly Ala Thr Val Ala Pro Val Val Asp Glu Glu Glu He Val 595 600 605 Glu Glu Cys Ala Ser Phe He Pro Leu Glu Ala Met Val Ala Ala He 610 615 620 Asp Lys Leu Lys Ser Thr He Thr Thr Thr Ser Pro Phe Thr Leu Glu 625 630 635 640 Thr Ala Leu Glu Lys Leu Asn Thr Phe Leu Gly Pro His Ala Ala Thr 645 650 655 He Leu Ala He He Glu Tyr Cys Cys Gly Leu Val Thr Leu Pro Asp 660 665 670 Asn Pro Phe Ala Ser Cys Val Phe Ala Phe He Ala Gly He Thr Thr 675 680 685 Pro Leu Pro His Lys He Lys Met Phe Leu Ser Leu Phe Gly Gly Ala 690 695 700 He Ala Ser Lys Leu Thr Asp Ala Arg Xaa Ala Leu Ala Phe Met Met 705 710 715 720 Ala Gly Ala Xaa Gly Thr Ala Leu Gly Thr Trp Thr Ser Val Gly Phe 725 730 735 Val Phe Asp Met Leu Gly Gly Tyr Ala Gly Ala Ser Ser Thr Ala Cys 740 745 750 Leu Thr Phe Lys Cys Leu Met Gly Glu Trp Xaa Thr Met Asp Gin Leu 755 760 765 Ala Gly Leu Val Tyr Ser Ala Phe Asn Pro Ala Ala Gly Val Val Gly 770 775 780 Val Leu Ser Ala Cys Ala Met Phe Ala Leu Thr Thr Ala Gly Pro Asp 785 790 795 800 His Trp Pro Asn Arg Leu Leu Thr Met Leu Ala Arg Ser Asn Thr Val 805 810 815 Cys Xaa Glu Tyr Phe He Ala Thr Arg Asp He Arg Arg Lys He Leu 820 825 830 Gly He Leu Glu Ala Ser Thr Pro Trp Ser Xaa He Ser Ala Cys He 835 840 845 Arg Trp Leu His Thr Pro Thr Glu Asp Asp Cys Gly Leu He Ala Trp 850 855 860 Gly Leu Xaa He Trp Gin Tyr Val Cys Asn Phe Phe Val He Cys Phe 865 870 875 880 Asn Val Leu Lys Ala Gly Val Gin Ser Met Val Asn He Pro Gly Cys. 885 890 895 Pro Phe Tyr Ser Cys Gin Lys Gly Tyr Lys Gly Pro Trp He Gly Ser 900 905 910 Gly Met Leu Gin Ala Arg Cys Pro Cys Gly Ala Glu Leu He Phe Ser 915 920 925 Val Glu Asn Gly Phe Ala Lys Leu Tyr Lys Gly Pro Arg Thr Cys Ser 930 935 940 Asn Tyr Trp Arg Gly Ala Val Pro Val Asn Ala Arg Leu Cys Gly Ser 945 950 955 960 Ala Arg Pro Asp Pro Thr Asp Trp Thr Ser Leu Val Val Asn Tyr Gly 965 970 975 Val Arg Asp Tyr Cys Lys Tyr Glu Lys Leu Gly Asp His He Phe Val 980 985 990 Thr Ala Val Ser Ser Pro Asn Val Cys Phe Thr Gin Val Pro Pro Thr 995 1000 1005 Leu Arg Ala Ala Val Ala Val Asp Arg Val Gin Val Gin Xaa Tyr Leu 1010 1015 1020 Gly Glu Pro Lys Thr Pro Trp Thr Thr Ser Ala Cys Cys Tyr Gly Pro 1025 1030 1035 1040 Asp Gly Lys Gly Lys Thr Val Lys Leu Pro Phe Arg Val Asp Gly His 1045 1050 1055 Thr Pro Gly Gly Arg Met Gin Leu Asn Leu Arg Asp Arg Leu Glu Ala 1060 1065 1070 Asn Asp Cys Asn Ser He Asn Asn Thr Pro Ser Asp Glu Ala Ala Val 1075 1080 1085 Ser Ala Leu Val Phe Lys Gin Glu Leu Arg Arg Thr Asn Gin Leu Leu 1090 1095 1100 Glu Ala He Ser Ala Gly Val Asp Thr Thr Lys Leu Pro Ala Pro Ser 1105 1110 1115 1120 Gin He Glu Glu Val Val Val Arg Lys Arg Gin Phe Arg Ala Arg Thr 1125 1130 1135 Gly Ser Leu Thr Leu Pro Pro Pro Pro Arg Ser Val Pro Gly Val Ser 1140 1145 1150 Cys Pro Glu Ser Leu Gin Arg Ser Asp Pro Leu Glu Gly Pro Ser Xaa 1155 1160 1165 Leu Pro Ser Ser Pro Pro Val Leu Gin Leu Ala Met Pro Met Pro Leu 1170 1175 1180 Leu Gly Ala Gly Glu Cys Asn Pro Phe Thr Ala He Gly Cys Ala Met 1185 1190 1195 1200 Thr Glu Thr Xaa Gly Xaa Pro Xaa Xaa Leu Pro Ser Tyr Pro Pro Lys 1205 1210 1215 Lys Glu Val Ser Glu Trp Ser Asp Glu Ser Trp Ser Thr Thr Thr Thr 1220 1225 1230 Ala Ser Ser Tyr Val Thr Gly Pro Pro Tyr Pro Lys He Arg Gly Lys 1235 1240 1245 Asp Ser Thr Gin Ser Ala Thr Ala Lys Arg Pro Thr Lys Lys Lys Leu 1250 1255 1260 Gly Lys Ser Glu Phe Ser Cys Ser Met Ser Tyr Thr Trp Thr Asp Val 1265 1270 1275 1280 He Ser Phe Lys Thr Ala Ser Lys Val Leu Ser Ala Thr Arg Ala He 1285 1290 1295 Thr Ser Gly Phe Leu Lys Gin Arg Ser Leu Val Tyr Val Thr Glu Pro 1300 1305 1310 Arg Asp Ala Glu Leu Arg Lys Gin Lys Val Thr He Asn Arg Gin Pro 1315 1320 1325 Leu Phe Pro Pro Ser Tyr His Lys Gin Val Arg Leu Ala Lys Glu Lys 1330 1335 1340 Ala Ser Lys Val Val Gly Val Met Trp Asp Tyr Asp Glu Val Ala Ala 1345 1350 1355 1360 His Thr Pro Ser Lys Ser Ala Lys Ser His He Thr Gly Leu Arg Gly 1365 1370 1375 Thr Asp Val Leu Asp Leu Gin Lys Cys Val Glu Ala Gly Glu He Pro 1380 1385 1390 Ser His Tyr Arg Gin Thr Val He Val Pro Lys Glu Glu Val Phe Val 1395 1400 1405 Lys Thr Pro Gin Lys Pro Thr Lys Lys Pro Pro Arg Leu He 1410 1415 1420 (2) INFORMATION FOR SEQ ID NO:84: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1422 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:84: Asp Lys Pro Trp Gly Phe Leu Cys Trp Phe Leu Gly Gly Leu His Glu 1 5 10 15 Asp Leu Leu Leu Trp Asn Tyr His Ser Leu Pro He Met Thr Arg Tyr 20 25 30 Leu Thr Cys Leu Asp Thr Leu Leu Gin Val Gin Asn He Ser Ala Pro 35 40 45 Lys Ala Ser Asp Val Gly Leu Ser Arg Leu Arg Gly Arg Val Ser Cys 50 55 60 Tyr Phe He He Val Pro His Asp Thr Asp Asn Phe Xaa Ser Phe Phe 65 70 75 80 Leu Ser Gin Ser His Leu Leu Val Val Xaa Trp Gly Glu Gin Arg Leu 85 90 95 Ser He Asn Ser Asp Phe Leu Phe Ser Lys Leu Arg He Pro Arg Leu 100 105 110 Ser His He His Gin Xaa Ser Leu Phe Glu Glu Thr Thr Ser Asp Gly 115 120 125 Pro Ser Cys Arg Gin Asn Phe Arg Ser Ser Phe Glu Ala Asn His Val 130 135 140 Gly Pro Ser Val Ala His Ala Ala Arg Lys Leu Thr Leu Ser Gin Leu 145 150 155 160 Leu Phe Cys Arg Pro Phe Gly Gly Gly Xaa Leu Ser Gly He Leu Ala 165 170 175 Pro Tyr Leu Arg Val Arg Gly Ala Ser Asn Val Ala Gly Ser Gly Cys 180 185 190 Ser Arg Xaa Pro Thr Phe Val Xaa Pro Phe Arg Asp Leu Leu Phe Gly 195 200 205 Arg Val Thr Gly Xaa He Xaa Xaa Xaa Ser Xaa Cyβ Phe Gly His Cys 210 215 220 Thr Ser Asn Cys Ser Glu Arg Val Thr Leu Thr Cys Ser Gin Gin Gly 225 230 235 240 His Arg His Gly Gin Leu Xaa Asn Arg Trp Xaa Arg Arg Glu Xaa Xaa 245 250 255 Arg Thr Phe Xaa Arg Val Thr Ser Leu Gin Ala Phe Arg Thr Xaa His 260 265 270 Ser Trp Asp Gly Ser Arg Arg Gly Arg Gin Gly Lys Arg Thr Ser Ser 275 280 285 Cys Pro Glu Leu Ala Leu Ser Tyr His Tyr Leu Phe Asp Leu Gly Gly 290 295 300 Gly Trp Gin Phe Gly Gly Val Asn Ala Ser Xaa Asn Cys Leu Lys Gin 305 310 315 320 Leu Val Cys Thr Pro Gin Leu Leu Phe Glu Asn Lys Ser Gly His Cys 325 330 335 Gly Phe He Thr Arg Ser Val Val Tyr Gly He Thr Val He Cys Leu 340 345 350 Lys Ser He Thr Gin He Lys Leu His Ala Thr Thr Arg Cys Val Ser 355 360 365 Val Asn Ala Glu Gly Lys Leu Asn Ser Phe Thr Leu Thr Val Arg Thr 370 375 380 Val Thr Ala Ser Arg Cys Arg Pro Arg Ser Phe Gly Leu Thr Xaa He 385 390 395 400 Thr Leu Asn Leu Tyr Ala Val His Gly His Cys Ser Ser Gin Gly Trp 405 410 415 Gly His Leu Gly Glu Thr Asp He Trp Arg Gly Tyr Cys Cys Asn Lys 420 425 430 Asn Val He Ser Gin Phe Leu He Phe Thr Val Val Pro Asn Ala He 435 440 445 He Asp Asp Lys Thr Ser Pro He Ser Trp Val Arg Ser Ser Arg Pro 450 455 460 Thr Gin Pro Ser Val Asp Trp Asn Ser Pro Ser Pro Val He Xaa Thr 465 470 475 480 Ser Ser Gly Ser Phe Val Lys Phe Cys Lys Thr He Leu Asn Arg Lys 485 490 495 Asp Glu Phe Ser Thr Ala Trp Thr Ala Cys Leu Glu His Thr Xaa Ser 500 505 510 Asn Pro Gly Ala Leu Val Pro Leu Leu Ala Ala Val Glu Arg Thr Thr 515 520 525 Arg Asn Val Asn His Ala Leu Asn Ser Ser Phe Lys Asp He Lys Ala 530 535 540 Asn His Lys Glu He Ala His He Leu Pro Asn Leu Xaa Thr Pro Ser 545 550 555 560 Asn Glu Ala Ala He He Leu Arg Arg Gly Val Xaa Pro Thr Asp Ala 565 570 575 Ser Xaa Tyr Asp Thr Pro Gly Gly Arg Cys Leu Gin Asn Ala Gin Tyr 580 585 590 Leu Pro Ala Asp Val Thr Ser Gly Asn Lys Val Leu Xaa Thr Tyr Ser 595 600 605 Val Ala Pro Ser Lys His Ser Lys Lys Ser Val Gly Pro Val He Trp 610 615 620 Pro Cys Cys Cys Gin Ser Lys His Cys Thr Ser Xaa Gin Asp Ala His 625 630 635 640 Asn Ser Cyβ Gly Arg He Glu Arg Gly Val Asp Xaa Thr Ser Lys Leu 645 650 655 He His Ser Xaa Pro Leu Thr His Gin Ala Phe Lys Cys Gin Ala Ser 660 665 670 Ser Gly Xaa Gly Ala Ser He Ala Ala Xaa His Val Lye Asp Lys Thr 675 680 685 Hie Arg Cys Pro Cys Thr Lye Ser Cyβ Ser Xaa Ser Pro Gly Hie Hie 690 695 700 Glu Arg Gin Cyβ Xaa Ser Ser Val Cys Lys Leu Gly Arg Asn Cys Ala 705 710 715 720 Ser Lys Xaa Xaa Gin Glu His Phe Asp Leu Val Arg Xaa Trp Gly Ser 725 730 735 Asn Thr Arg Asn Glu Ser Lys His Ala Xaa Cys Lys Gly He Val Arg 740 745 750 Xaa Ser Asp Xaa Ala Thr Ala He Leu Tyr Asp Ser Lys Asp Cyβ Ser 755 760 765 Cys Met Arg Pro Lys Lys Gly Val Lys Phe Phe Lye Gly Gly Phe Gin 770 775 780 Cyβ Glu Arg Thr Ser Cys Gly Asp Cys Thr Leu Gin Leu Val Asn Cys 785 790 795 800 Ser Asn His Gly Leu Gin Gly Asn Glu Xaa Cys Thr Leu Leu His Asp 805 810 815 Phe Leu Phe Val Aβn Hie Trp Gly Asp Ser Ser Thr Gly Arg Asp Xaa 820 825 830 Cyβ Aβn Arg Pro Ala Thr Pro Hie Thr Ser Gly Ala Lye Ser Val Aβn 835 840 845 Gly Xaa He Ser Hie Ser Hie Ser Aβn Ala Asn Ser Glu Cys Gly Cys 850 855 860 Pro Arg Ser He Asp Phe Ser Glu Ala His Leu Val Ser Gly His Leu 865 870 875 880 Ala Gly Leu Trp Ala Arg Thr Gly Val Thr Ala Val Gin Ala Pro Gin 885 890 895 Asn Pro Thr Arg Phe Phe Pro Lys Pro Gly Ser Leu Pro Pro Trp Cys 900 905 910 Val He Gly Ser Ser He Ala He Leu Met Thr Gin Leu Xaa Leu Gly 915 920 925 Cye Ser Gin Gin Aβn He He Val Ser Ser Ser Phe Cye Ser He Asp 930 935 940 Lys Xaa Arg Phe Gly Val Asp Hie Arg Lye Glu He Ser Pro Leu Val 945 950 955 960 Gin He Cyβ Ser Tyr Arg Arg Xaa Pro Arg Leu Gly Ala He Gly Val 965 970 975 Gin Aβn Ser Leu Ser Phe Cyβ Xaa Xaa Gin Thr He Pro Cys Leu Gly 980 985 990 Cys Val Glu Gly Phe Asn Asn Val Ala Phe Arg Asn His Thr Arg Arg 995 1000 1005 Gly Thr Thr Pro Val Tyr He Val Val Tyr Ala Ser Ser Pro Thr Ala 1010 1015 1020 Cye Ala Ala Pro Thr Leu Ala Phe Aβn Tyr Cyβ Xaa Aβn Pro Ala His 1025 1030 1035 1040 Thr Asn Thr Hie Gly Glu Ser Arg Val Lye Val Aβn Met Ala Cye Ala 1045 1050 1055 Phe Tyr Hie Glu Ala Ala Val He Hie Gly He Lye Val Thr Ser Val 1060 1065 1070 Pro Cye Thr Gin Gly He Ser Gly Aβn Tyr Tyr Thr Val Ala Leu Arg 1075 1080 1085 Hie Phe Xaa Aep Val Thr Ser Pro He Val Arg Aep Ser Cye Tyr Ser 1090 1095 1100 Leu Ser Ser Xaa Leu Val Ser Lye Leu He Thr Val Phe Phe Gly Ser 1105 1110 1115 1120 Leu Lye Aep Lys Val Ser Pro Phe Leu Gin He Phe Leu Leu Asn Leu 1125 1130 1135 Phe Ser Met Lys Gly Asp Ser Ala Phe He Xaa Xaa Leu Asn Leu Ser 1140 1145 1150 Tyr Val Gly Met Trp Cys Arg Asp Tyr Ser Arg Gly Gly Ser Arg Gly 1155 1160 1165 Lys Asn Hie Xaa Pro Aβn He Phe Gly Trp Ser Phe Gly Xaa Aep Leu 1170 1175 1180 Ser Aβn Ala Gin His Gly Gly Ser He Gly Ser Met Ala Phe Val Thr 1185 1190 1195 1200 Aβn Aep Tyr He He Val Pro Gly Thr Ser Ser Gly Gin Val Hie Ala 1205 1210 1215 He Cys Ala Val Arg Lys Xaa Ser Pro Cys Val Gly Thr Phe Ala He 1220 1225 1230 Lys He Ala He Trp He Hie Ala Val Arg Arg Val Hie Val Leu Trp 1235 1240 1245 Hie Xaa Cyβ Cye Cye Ser Hie Thr Gly He Xaa Aep Gin Asp Leu Xaa 1250 1255 1260 Leu Xaa Leu His Val Arg Lye Trp Xaa Phe Gly Xaa Leu Ala Ala Ala 1265 1270 1275 1280 Ser Gly Gly Aen Xaa Aβn Leu Hie Xaa He Leu Val Arg His Ser Arg 1285 1290 1295 Phe Cys He Lys Ser Gly Met Cye Cyβ Val Leu Gly Met Val Ser Ser 1300 1305 1310 Thr Hie Gin Arg Pro Aβn Pro Aβn Leu Ala Aep Xaa Thr Ala Arg He 1315 1320 1325 Ser Ser Ser Gly Glu His Pro Asn Asn Met Pro Gly Gly Ala Gin Asn 1330 1335 1340 Arg Gly Thr Xaa Arg Thr Leu Gly Aβn Ser Hie Gly Lye Gly Pro Ala 1345 1350 1355 1360 His Thr Pro He Arg Val He Gly Phe Val Asp Leu Asn Gin Xaa Pro 1365 1370 1375 Gin Ser Cys Tyr Gin He Pro Leu Gly Leu Pro Ala Arg Ala Pro Ser 1380 1385 1390 Lys Gly Pro Ser Ser Thr Trp Trp Leu He Asp Val Leu Val He Ser 1395 1400 1405 Arg Val Asn Gly Tyr Trp Val Tyr Gly Ala Cys Gly Met Ser 1410 1415 1420 (2) INFORMATION FOR SEQ ID NO-.85: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1422 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear ( ii) MOLECULE TYPE : protein (xi) SEQUENCE DESCRIPTION : SEQ ID NO : 111 : He Ser Leu Gly Gly Phe Phe Val Gly Phe Trp Gly Val Phe Thr Lys 1 5 10 15 Thr Ser Ser Phe Gly Thr He Thr Val Cys Arg Xaa Xaa Leu Gly He 20 25 30 Ser Pro Ala Ser Thr His Phe Cys Lys Ser Arg Thr Ser Val Pro Arg 35 40 45 Arg Pro Val Met Trp Asp Leu Ala Asp Leu Glu Gly Val Xaa Ala Ala 50 55 60 Thr Ser Ser Xaa Ser Hie Met Thr Pro Thr Thr Phe Glu Ala Phe Ser 65 70 75 80 Leu Ala Asn Leu Thr Cys Leu Trp Tyr Asp Gly Gly Asn Arg Gly Cye 85 90 95 Leu Leu He Val Thr Phe Cys Phe Leu Ser Ser Ala Ser Arg Gly Ser 100 105 110 Val Thr Tyr Thr Asn Asp Leu Cys Leu Arg Lys Pro Leu Val Met Ala 115 120 125 Arg Val Ala Asp Arg Thr Leu Glu Ala Val Leu Lye Leu He Thr Ser 130 135 140 Val Gin Val Xaa Leu Met Leu Hie Glu Aβn Ser Leu Phe Pro Aβn Phe 145 150 155 160 Phe Phe Val Gly Arg Leu Ala Val Ala Aep Xaa Val Glu Ser Leu Pro 165 170 175 Arg He Leu Gly Tyr Gly Gly Pro Val Thr Xaa Leu Glu Ala Val Val 180 185 190 Val Val Aep Gin Leu Ser Ser Aep Hie Ser Glu Thr Ser Phe Leu Gly 195 200 205 Gly Xaa Leu Gly Lys Xaa Xaa Gly Xaa Pro Xaa Val Ser Val He Ala 210 215 220 His Pro He Ala Val Lys Gly Leu Hie Ser Pro Ala Pro Aβn Arg Gly 225 230 235 240 He Gly Met Ala Aβn Cyβ Arg Thr Gly Gly Glu Glu Gly Arg Xaa Glu 245 250 255 Gly Pro Ser Aβn Gly Ser Leu Arg Cyβ Arg Leu Ser Gly Hie Aep Thr 260 265 270 Pro Gly Thr Asp Leu Gly Gly Gly Gly Lys Val Ser Glu Pro Val Leu 275 280 285 Ala Arg Asn Trp Arg Phe Leu Thr Thr Thr Ser Ser He Trp Glu Gly 290 295 300 Ala Gly Ser Leu Val Val Ser Thr Pro Ala Glu He Ala Ser Ser Aβn 305 310 315 320 Trp Phe Val Arg Arg Asn Ser Cys Leu Lye Thr Arg Ala Aep Thr Ala 325 330 335 Ala Ser Ser Leu Gly Val Leu Phe Met Glu Leu Gin Ser Phe Ala Ser 340 345 350 Ser Arg Ser Arg Lys Leu Ser Cys Met Arg Pro Pro Gly Val Cyβ Pro 355 360 365 Ser Thr Arg Lye Gly Ser Leu Thr Val Leu Pro Leu Pro Ser Gly Pro 370 375 380 Xaa Gin Gin Ala Aep Val Val Gin Gly Val Leu Gly Ser Pro Arg Xaa 385 390 395 400 Xaa Xaa Thr Cyβ Thr Arg Ser Thr Ala Thr Ala Ala Leu Lye Val Gly 405 410 415 Gly Thr Trp Val Lys Gin Thr Phe Gly Glu Aep Thr Ala Val Thr Lys 420 425 430 Met Xaa Ser Pro Asn Phe Ser Tyr Leu Gin Xaa Ser Leu Thr Pro Xaa 435 440 445 Leu Thr Thr Arg Leu Val Gin Ser Val Gly Ser Gly Leu Ala Aep Pro 450 455 460 Hie Ser Leu Ala Leu Thr Gly Thr Ala Pro Leu Gin Xaa Phe Glu Gin 465 470 475 480 Val Leu Gly Pro Leu Xaa Ser Phe Ala Lye Pro Phe Ser Thr Glu Lye 485 490 495 Met Ser Ser Ala Pro His Gly Gin Arg Ala Trp Ser He Pro Asp Pro 500 505 510 He Gin Gly Pro Leu Tyr Pro Phe Trp Gin Leu Xaa Lys Gly Gin Pro 515 520 525 Gly Met Leu Thr Met Leu Xaa Thr Pro Ala Leu Arg Thr Leu Lye Gin 530 535 540 He Thr Lye Lye Leu Hie Thr Tyr Cyβ Gin He Xaa Arg Pro Gin Ala 545 550 555 560 Met Arg Pro Gin Ser Ser Ser Val Gly Val Xaa Ser Gin Arg Met Gin 565 570 575 Ala Aep Met Xaa Leu Gin Gly Val Aep Ala Ser Arg Met Pro Ser He 580 585 590 Phe Leu Arg Met Ser Arg Val Ala He Lye Tyr Ser Xaa His Thr Val 595 600 605 Leu Leu Leu Ala Ser He Val Arg Ser Leu Leu Gly Gin Xaa Ser Gly 610 615 620 Pro Ala Val Val Lys Ala Asn He Ala Gin Ala Asp Lye Thr Pro Thr 625 630 635 640 Thr Pro Ala Ala Gly Leu Aβn Ala Glu Xaa Thr Lye Pro Ala Ser Xaa 645 650 655 Ser He Val Xaa Hie Ser Pro He Lye His Leu Asn Val Lys Gin Ala 660 665 670 Val Asp Glu Ala Pro Ala Xaa Pro Pro Ser Met Ser Lye Thr Lys Pro 675 680 685 Thr Asp Val His Val Pro Arg Ala Val Pro Xaa Ala Pro Ala He Met 690 695 700 Asn Ala Ser Ala Xaa Leu Ala Ser Val Ser Leu Aep Ala He Ala Pro 705 710 715 720 Pro Aen Asn Asp Arg Asn He Leu He Leu Xaa Gly Ser Gly Val Val 725 730 735 He Pro Ala Met Lys Ala Asn Thr His Asp Ala Lys Gly Leu Ser Gly 740 745 750 Lys Val Thr Lys Pro Gin Gin Tyr Ser Met He Ala Arg He Val Ala 755 760 765 Ala Xaa Gly Pro Arg Lye Val Leu Ser Phe Ser Arg Ala Val Ser Aβn 770 * 775 780 Val Lye Gly Leu Val Val Val He Val Leu Phe Ser Leu Ser He Ala 785 790 795 800 Ala Thr Met Ala Ser Lye Gly Met Aβn Asp Ala His Ser Ser Thr He 805 810 815 Ser Ser Ser Ser Thr Thr Gly Ala Thr Val Ala Pro Val Gly Thr Asp 820 825 830 Val He Asp Gin Gin Arg Arg Thr Gin Val Ala Pro Lys Val Ser Met 835 840 845 Ala Arg Xaa Ala He Ala Thr Pro Thr Pro Thr Ala Ser Ala Ala Val 850 855 860 Pro Glu Val Leu Thr Ser Val Lys His He Trp Tyr Leu Val Thr Ser 865 870 875 880 Leu Gly Ser Gly Pro Gly Gin Ala Ser Gin Pro Ser Lys Arg His Arg 885 890 895 Thr Pro Gin Gly Phe Phe Pro Ser Arg Ala Pro Cys His Arg Gly Ala 900 905 910 Ser Leu Gly Ala Ala Xaa Pro Tyr Xaa Xaa His Ser Cys Ser Trp Ala 915 920 925 Ala Val Asn Lys Thr Xaa Leu Ser Ala Val Leu Phe Ala Val Leu Thr 930 935 940 Asn Glu Gly Ser Gly Leu Thr He Glu Lys Arg Ser Ala Hie Ser Ser 945 950 955 960 Lye Phe Ala Pro He Ala Gly Aβn Pro Gly Trp Val Arg Xaa Val Ser 965 970 975 Arg He Val Xaa Ala Ser Val Asp Asp Lys Pro Tyr His Ala Leu Ala 980 985 990 Ala Ser Lys Ala Ser Thr Met Leu His Ser Gly Thr He Pro Glu Gly 995 1000 1005 Val Gin Leu Pro Ser Thr Xaa Xaa Tyr Met Pro Ala Leu Pro Arg Pro 1010 1015 1020 Val Arg Pro Leu Arg Trp Pro Leu Thr He Ala Glu Thr Pro His Thr 1025 1030 1035 1040 Arg Thr Pro Met Val Lys Val Gly Ser Arg Ser Thr Trp Hie Val Pro 1045 1050 1055 Ser Thr Met Arg Leu Gin Ser Tyr Thr Glu Ser Lye Ser Pro Val Tyr 1060 1065 1070 Pro Val Hie Lye Ala Ser Val Ala Thr Thr Thr Gin Ser Pro Ser Gly 1075 1080 1085 He Phe Glu Met Ser His Pro Leu Xaa Xaa Glu Thr Ala Val He Pro 1090 1095 1100 Phe Arg Ala Asn Ser Leu Ala Ser Ser Ser Gin Cys Phe Leu Val Ala 1105 1110 1115 1120 Ser Lys He Arg Cys Leu Pro Phe Phe Arg Phe Ser Ser Leu He Phe 1125 1130 1135 Phe Pro Xaa Lys Gly He Val Pro Ser Ser Val Asn Xaa He Ser Val 1140 1145 1150 Met Leu Ala Cys Gly Val Gly He Thr Pro Gly Gly Val Ala Val Ala 1155 1160 1165 Arg Thr Thr Ser Leu Thr Phe Leu Asp Gly Ala Ser Val Arg Thr Phe 1170 1175 1180 Pro Met Pro Aβn Thr Val Val Arg Ser Val Ala Trp His Ser Ser Gin 1185 1190 1195 1200 Met He Thr Ser Xaa Phe Arg Glu His Arg Pro Val Arg Tyr Met Pro 1205 1210 1215 Tyr Val Leu Tyr Val Ser Glu Ala Pro Val Leu Val His Leu Pro Leu 1220 1225 1230 Lys Xaa Gin Phe Gly Phe Thr Pro Tyr Val Ala Cys Met Tyr Phe Gly 1235 1240 1245 He Asp Ala Val Val Ala Thr Leu Gly Phe Arg Thr Lye Thr Ser Xaa 1250 1255 1260 Phe Xaa Cys Met Xaa Glu Ser Gly Asn Leu Val Asp Leu Pro Leu Pro 1265 1270 1275 1280 Val Gly Ala He Lys He Cys Thr Glu Tyr Ser Leu Gly Thr Val Gly 1285 1290 1295 Phe Val Ser Arg Val Ala Cys Ala Val Tyr Trp Gly Trp Tyr Pro Ala 1300 1305 1310 Hie Thr Aβn Gly Leu Thr Leu He Trp Pro Thr Glu Pro Pro Glu Phe 1315 1320 1325 Leu Ala Ala Val Aβn He Pro He Thr Cys Pro Glu Glu His Arg He 1330 1335 1340 Gly Ala Pro Glu Glu Pro Leu Ala Thr Ala Met Gly Arg Ala Pro His 1345 1350 1355 1360 Thr Hie Gin Xaa Gly Ser Ser Aep Leu Leu Thr Ser Thr Aβn Asp Pro 1365 1370 1375 Ser Arg Val Thr Arg Tyr Pro Leu Val Ser Pro Gin Glu His Arg Val 1380 1385 1390 Arg Asp Pro Ala Pro His Gly Gly Xaa Xaa Met Ser Trp Ser Leu Ala 1395 1400 1405 Ala Ser Thr Val He Gly Cys Met Glu Pro Val Gly Xaa Ala 1410 1415 1420 (2) INFORMATION FOR SEQ ID NO:86: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1422 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:86: Xaa Ala Leu Gly Val Ser Leu Leu Val Ser Gly Gly Ser Ser Arg Arg 1 5 10 15 Pro Pro Pro Leu Glu Leu Ser Gin Phe Ala Asp Asn Asp Ser Val Ser 20 25 30 His Leu Pro Arg Hie Thr Ser Ala Ser Pro Glu Hie Gin Cyβ Pro Glu 35 40 45 Gly Gin Xaa Cye Gly Thr Xaa Gin Thr Xaa Arg Ala Cye Glu Leu Leu 50 55 60 Leu Hie Hie Ser Pro Thr Xaa Hie Arg Gin Leu Leu Lye Leu Phe Pro 65 70 75 80 Xaa Pro He Ser Leu Ala Cys Gly Met Met Gly Gly Thr Glu Val Val 85 90 95 Tyr Xaa Xaa Xaa Leu Phe Val Phe Xaa Ala Pro His Pro Ala Ala Gin 100 105 110 Ser His Thr Pro Met He Phe Val Xaa Gly Asn Hie Xaa Xaa Trp Pro 115 120 125 Glu Leu Gin Thr Glu Leu Xaa Lye Gin Phe Xaa Ser Xaa Ser Arg Arg 130 135 140 Ser Lye Cys Ser Ser Cys Cys Thr Lys Thr His Ser Phe Pro Thr Ser 145 150 155 160 Phe Leu Xaa Ala Val Trp Arg Trp Leu He Glu Trp Asn Pro Cyβ Pro 165 170 175 Val Ser Xaa Gly Thr Gly Gly Gin Xaa Arg Ser Trp Lye Arg Leu Xaa 180 185 190 Ser Leu Thr Asn Phe Arg Leu Thr He Gin Arg Pro Pro Phe Trp Glu 195 200 205 Gly Asn Trp Val Asn Xaa Xaa Gly Leu Xaa Xaa Phe Arg Ser Leu Hie 210 215 220 He Gin Leu Gin Xaa Lys Gly Tyr Thr His Leu Leu Pro Thr Gly Ala 225 230 235 240 Ser Ala Trp Pro Thr Xaa Glu Gin Val Val Lys Lys Gly Gly Leu Lys 245 250 255 Asp Leu Leu Thr Gly His Phe Val Ala Gly Phe Gin Aep Met Thr Leu 260 265 270 Leu Gly Arg He Ser Glu Gly Glu Ala Arg Xaa Ala Aβn Gin Phe Leu 275 280 285 Pro Gly Thr Gly Ala Phe Leu Pro Leu Pro Leu Arg Ser Gly Arg Gly 290 295 300 Leu Ala Val Trp Trp Cyβ Gin Arg Gin Leu Lye Leu Pro Gin Ala He 305 310 315 320 Gly Leu Tyr Ala Ala Thr Pro Val Xaa Lye Gin Glu Arg Thr Leu Arg 325 330 335 Leu His His Xaa Glu Cys Cys Leu Trp Asn Tyr Ser His Leu Pro Gin 340 345 350 Val Asp His Ala Asn Xaa Val Ala Cys Asp His Gin Val Cys Val Arg 355 360 365 Gin Arg Gly Arg Glu Ala Xaa Gin Phe Tyr Pro Tyr Arg Gin Asp Arg 370 375 380 Aen Ser Lye Gin Met Ser Ser Lye Glu Phe Trp Ala His Leu Asp Aβn 385 390 395 400 Xaa Glu Pro Val Arg Gly Pro Arg Pro Leu Gin Leu Ser Arg Leu Gly 405 410 415 Ala Pro Gly Xaa Asn Arg His Leu Glu Arg He Leu Leu Xaa Gin Lye 420 425 430 Cye Aep Leu Pro He Ser Hie He Tyr Ser Ser Pro Xaa Arg Hie Aβn 435 440 445 Xaa Arg Gin Aep Xaa Ser Aβn Gin Leu Gly Pro Val Xaa Pro Thr His 450 455 460 Thr Ala Xaa Arg Xaa Leu Glu Gin Pro Leu Ser Ser Asn Leu Asn Lys 465 470 475 480 Phe Trp Val Leu Cys Lys Val Leu Gin Asn His Ser Gin Gin Lye Arg 485 490 495 Xaa Val Gin Hie Arg Met Aep Ser Val Leu Gly Ala Tyr Leu He Gin 500 505 510 Ser Arg Gly Pro Cye Thr Pro Ser Gly Ser Cyβ Arg Lye Aep Aen Gin 515 520 525 Glu Cys Xaa Pro Cys Ser Glu Leu Gin Leu Xaa Gly Hie Xaa Ser Lye 530 535 540 Ser Gin Arg Aβn Cye Thr Hie Thr Ala Lye Ser Xaa Aep Pro Lys Gin 545 550 555 560 Xaa Gly Arg Asn His Pro Pro Ser Gly Cys Xaa Ala Asn Gly Cys Lys 565 570 575 Leu He Xaa Xaa Ser Arg Gly Xaa Met Pro Pro Glu Cys Pro Val Ser 580 585 590 Ser Cys Gly Cys Hie Glu Trp Gin Xaa Ser Thr Hie Tyr He Gin Cye 595 600 605 Cye Ser Xaa Gin Ala Xaa Xaa Glu Val Cys Trp Ala Ser Asp Leu Ala 610 615 620 Leu Leu Leu Ser Lys Gin Thr Leu Hie Lye Leu Thr Arg Arg Pro Gin 625 630 635 640 Leu Leu Arg Pro Aep Xaa Thr Arg Ser Arg Leu Aβn Gin Gin Ala Aep 645 650 655 Pro Xaa Xaa Ala Thr His Pro Ser Ser He Xaa Met Ser Ser Lys Gin 660 665 670 Trp Met Arg Arg Gin His Ser Arg Leu Ala Cys Gin Arg Gin Asn Pro 675 680 685 Pro Met Ser Met Tyr Gin Glu Leu Phe Pro Gin Pro Arg Pro Ser Xaa 690 695 700 Thr Pro Val Arg Leu Xaa Arg Leu Xaa Ala Trp Thr Gin Leu Arg Leu 705 710 715 720 Gin He Met Thr Gly Thr Phe Xaa Ser Cys Glu Val Val Gly Xaa Xaa 725 730 735 Tyr Pro Gin Xaa Lye Gin Thr Arg Met Met Gin Arg Aep Cye Gin Val 740 745 750 Lys Xaa Leu Ser His Ser Aβn Thr Leu Xaa Xaa Gin Gly Leu Xaa Leu 755 760 765 Hie Glu Ala Gin Glu Arg Cyβ Xaa Val Phe Gin Gly Arg Phe Pro Met 770 775 780 Xaa Lye Aep Xaa Leu Trp Xaa Leu Tyr Ser Ser Ala Cye Gin Leu Gin 785 790 795 800 Gin Pro Trp Pro Pro Arg Glu Xaa Met Met Hie Thr Pro Pro Arg Phe 805 810 815 Pro Leu Arg Gin Pro Leu Gly Arg Gin Xaa Hie Arg Xaa Gly Leu Met 820 825 830 Xaa Xaa Thr Ser Aen Ala Ala His Lye Trp Arg Gin Lys Cyβ Gin Trp 835 840 845 Leu Asp Lye Pro Xaa Pro Leu Gin Arg Gin Gin Arg Val Arg Leu Ser 850 855 860 Gin Lye Tyr Xaa Leu Gin Xaa Ser Thr Phe Gly He Trp Ser Pro Arg 865 870 875 880 Trp Ala Leu Gly Gin Aep Arg Arg His Ser Arg Pro Ser Ala Thr Glu 885 890 895 Pro His Lye Val Phe Ser Gin Ala Gly Leu Pro Ala Thr Val Val Arg 900 905 910 Hie Trp Glu Gin His Ser His Thr Asp Asp Thr Val Val Val Gly Leu 915 920 925 Gin Ser Thr Lye Hie Aβn Cyβ Gin Gin Phe Phe Leu Gin Tyr Xaa Gin 930 935 940 Met Lys Val Arg Gly Xaa Pro Xaa Lys Arg Asp Gin Pro Thr Arg Pro 945 950 955 960 Asn Leu Leu Leu Ser Gin Val Thr Gin Val Gly Cys Asp Arg Cyβ Pro 965 970 975 Glu Xaa Phe Glu Leu Leu Leu Met Thr Aβn Hie Thr Met Pro Trp Leu 980 985 990 Arg Arg Arg Leu Gin Gin Cye Cyβ He Gin Glu Pro Tyr Pro Lye Gly 995 1000 1005 Tyr Asn Ser Arg Leu His Ser Ser He Cyβ Gin Leu Ser His Gly Leu 1010 1015 1020 Cys Gly Pro Tyr Ala Gly Leu Xaa Leu Leu Leu Lys Pro Arg Thr His 1025 1030 1035 1040 Glu Hie Pro Trp Xaa Lye Xaa Gly Gin Gly Gin His Gly Met Cys Leu 1045 1050 1055 Leu Pro Xaa Gly Cys Ser His Thr Arg Asn Gin Ser Hie Gin Cyβ Thr 1060 1065 1070 Leu Tyr Thr Arg Hie Gin Trp Gin Leu Leu His Ser Arg Pro Gin Ala 1075 1080 1085 Phe Leu Arg Cys His He Pro Tyr Ser Lys Arg Gin Leu Leu Phe Pro 1090 1095 1100 Phe Glu Leu Thr Arg Xaa Gin Ala His His Ser Val Phe Trp Xaa Pro 1105 1110 1115 1120 Gin Arg Xaa Gly Val Ser Leu Ser Ser Asp Phe Pro Pro Xaa Ser Phe 1125 1130 1135 Phe Hie Glu Arg Gly Xaa Cye Leu Hie Xaa Leu He Glu Ser Gin Leu 1140 1145 1150 Cyβ Trp Hie Val Val Xaa Gly Leu Leu Gin Gly Gly Xaa Pro Trp Gin 1155 1160 1165 Glu Pro Leu Ala Xaa Hie Phe Trp Met Glu Leu Arg Leu Gly Pro Phe 1170 1175 1180 Gin Cye Pro Thr Arg Trp Phe Asp Arg Xaa His Gly He Arg His Lys 1185 1190 1195 1200 Xaa Leu His His Ser Ser Gly Asn He Val Arg Ser Gly Thr Cys His 1205 1210 1215 Met Cys Cys Thr Xaa Val Lys Pro Leu Cys Trp Tyr He Cys His Xaa 1220 1225 1230 Aβn Ser Asn Leu Asp Ser Arg Arg Thr Ser Arg Ala Cys Thr Leu Ala 1235 1240 1245 Leu Met Leu Leu Xaa Pro His Trp Asp Leu Gly Pro Arg Pro His Xaa 1250 1255 1260 Ser Pro Ala Cys Lys Lys Val Val He Trp Leu Thr Cys Arg Cyβ Gin 1265 1270 1275 1280 Trp Gly Gin Leu Lye Phe Ala Leu Asn Thr Arg Xaa Ala Gin Xaa Val 1285 1290 1295 Leu Tyr Gin Glu Trp His Val Leu Cye Thr Gly Asp Gly He Gin Hie 1300 1305 1310 Thr Pro Thr Ala Xaa Pro Xaa Ser Gly Arg Leu Asn Arg Gin Aen Phe 1315 1320 1325 Xaa Gin Arg Xaa Thr Ser Gin Xaa His Ala Arg Arg Ser Thr Glu Ser 1330 1335 1340 Gly His Leu Lys Asn Pro Trp Gin Gin Pro Trp Glu Gly Pro Arg Thr 1345 1350 1355 1360 His Thr Asn Lys Gly His Arg He Cye Xaa Pro Gin Pro Met Thr Pro 1365 1370 1375 Val Val Leu Pro Asp Thr Pro Trp Ser Pro Arg Lys Ser Thr Glu Xaa 1380 1385 1390 Gly Thr Gin Leu His Met Val Val Asp Arg Cys Pro Gly His Xaa Pro 1395 1400 1405 Arg Gin Arg Leu Leu Gly Val Trp Ser Leu Trp Aep Glu Pro 1410 1415 1420 (2) INFORMATION FOR SEQ ID NO:87: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 baβe pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:87: CTACCACCAA TACCAGCGGC 20 (2) INFORMATION FOR SEQ ID NO:88: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 22 baβe pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:88: GACATGGTCC TGGCCCTGTT GG 22 (2) INFORMATION FOR SEQ ID NO:89: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:89: GATCCATAGT GAGCCACTCA C 21 (2) INFORMATION FOR SEQ ID NO:90: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 23 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:90: CAAAATGTTC CTGTCATTAT TTG 23 (2) INFORMATION FOR SEQ ID NO:91: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 baβe pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:91: CAATCATCTC CAGCTATAAA G 21 (2) INFORMATION FOR SEQ ID NO:92: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:92: CTGTGGACGC CACTTGTTTC 20 (2) INFORMATION FOR SEQ ID NO:93: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:93: CAATAGCACA ATCTTCCTTG G 21 (2) INFORMATION FOR SEQ ID NO:94: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 94 : GAAAGCTTGG TTGGTTGTGG 20 (2) INFORMATION FOR SEQ ID NO:95: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 22 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:95: CATCTTGACA ATGACAACTT TC 22 (2) INFORMATION FOR SEQ ID NO:96: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:96: CCTCACTCAC CTTCGACCTC 20 (2) INFORMATION FOR SEQ ID NO:97: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:97: GGTTGGCACT TGCATGCCTG 20 (2) INFORMATION FOR SEQ ID NO:98: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:98: CCTGGCTTTG TTCCCACTGC 20 (2) INFORMATION FOR SEQ ID NO: 99: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 baβe pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:99: CTCGTACCCC TCCTGGCAGC 20 (2) INFORMATION FOR SEQ ID NO:100: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 baβe pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:100: GCTAGGAGCA ACACTGTATG 20 (2) INFORMATION FOR SEQ ID NO:101: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 27 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:101: CGCCATAATT GACGACAAGA CTAGTCC 27 (2) INFORMATION FOR SEQ ID NO:102: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 23 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:102: CTATTCCCAG GCTATAGCTA AAG 23 (2) INFORMATION FOR SEQ ID NO:103: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 26 baβe pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO-.103: CAGGTACATG CCATATGTGC TGTACG 26 (2) INFORMATION FOR SEQ ID NO:104: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:104: CTTGGACGCA ATTGCGCCTC 20 (2) INFORMATION FOR SEQ ID NO:105: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:105: GTCACTAGGT AACTGATGTT G 21 (2) INFORMATION FOR SEQ ID NO:106: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:106: CATGGTGGTT GATAGATGTC C 21 (2) INFORMATION FOR SEQ ID NO:107: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 baβe pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:107: GTGTCAAAAG CTAAGCAGGC 20 (2) INFORMATION FOR SEQ ID NO:108: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 19 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:108: AGATACCCCT TGGTCTCCC 19 (2) INFORMATION FOR SEQ ID NO:109: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:109: CAGGATCTAT TCCAGTAGGC 20 (2) INFORMATION FOR SEQ ID NO:110: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 22 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:110: GTATAGGGGT ACCAAGATAT GG 22 (2) INFORMATION FOR SEQ ID NO:111: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 25 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:lll: GTCTGCTAAG TCCCACATCA CTGGC 25 (2) INFORMATION FOR SEQ ID NO:112: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:112: CATGAAGAAC CCTCGCTTCC 20 (2) INFORMATION FOR SEQ ID NO:113: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:113: CACCCAACCC GAGGACTCCA G 21 (2) INFORMATION FOR SEQ ID NO:114: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 22 base paire (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:114: CACTTCAGCG CATGCCAATA GC 22 (2) INFORMATION FOR SEQ ID NO:115: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 23 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: eingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:115: GTACTAAACC CATCCATTGC CAC 23 (2) INFORMATION FOR SEQ ID NO:116: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:116: GCCGAATGAG TACGTCAAGG 20 (2) INFORMATION FOR SEQ ID NO:117: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 baβe pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:117: GTAGGTGTGG CCGTGGGAAA G 21 (2) INFORMATION FOR SEQ ID NO:118: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE; DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:118: CTGCCGAACT GAGGGCTCAG 20 (2) INFORMATION FOR SEQ ID NO:119: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:119: GGTTACCGTT CCCATTGACA ACCC 24 (2) INFORMATION FOR SEQ ID NO:120: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 23 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:120: GGACGGGGTC TCTGGTTGTA GTG 23 (2) INFORMATION FOR SEQ ID NO:121: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 base paire (B) TYPE: nucleic acid (C) STRANDEDNESS: eingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:121: GTGAACCGCG CTCACTCACC TTCG 24 (2) INFORMATION FOR SEQ ID NO:122: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:122: CCTCTAGAGC GGCCTGAGCA G 21 (2) INFORMATION FOR SEQ ID NO:123: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 base paire (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:123: GGATTAAGGC ACCATCATTC 20 (2) INFORMATION FOR SEQ ID NO:124: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 23 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:124: GCACGATTGG ATGCCGGGGA TAC 23 (2) INFORMATION FOR SEQ ID NO:125: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 34 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:125: CAGTTCAAGC TTGTCCAGGA ATTCNNNNNC CGGT 34 (2) INFORMATION FOR SEQ ID NO:126: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) ( i) SEQUENCE DESCRIPTION: SEQ ID NO:126; CAGTTCAAGC TTGTCCAGGA ATTC 24 (2) INFORMATION FOR SEQ ID NO:127: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:127: GCCTCAGCCA ACTTCATCAC 20 (2) INFORMATION FOR SEQ ID NO:128: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 34 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:128: CAGTTCAAGC TTGTCCAGGA ATTCNNNNNG CGCT 34 (2) INFORMATION FOR SEQ ID NO:129: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 22 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:129: GCGCTGAGCC TGTTAGCATA AC 22 (2) INFORMATION FOR SEQ ID NO:130: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 baβe pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:130: CAGGCGGTGG TATTGTCAGC 20 (2) INFORMATION FOR SEQ ID NO:131: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 23 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:131: CACTTTGGAC TGTAACAAAT GAC 23 (2) INFORMATION FOR SEQ ID NO:132: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:132: CATCCACCCG ATAAACCCTA G 21 (2) INFORMATION FOR SEQ ID NO:133: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 base paire (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:133: CTTGCAGAAG TGTGTCGAGG CAGG 24 (2) INFORMATION FOR SEQ ID NO:134: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:134: TAATGCTGCA GCCGACAGCT G 21 (2) INFORMATION FOR SEQ ID NO:135: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 34 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:135: CAGTTCAAGC TTGTCCAGGA ATTCNNNNNG GCCT 34 (2) INFORMATION FOR SEQ ID NO:136: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:136: CTTTCTCGGT GGTGCGCTAC 20 (2) INFORMATION FOR SEQ ID NO:137: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:137: CAACGCTGAG ATCCTCAGAG 20 (2) INFORMATION FOR SEQ ID NO:138: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 base paire (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:138: CCGTGAGAGG CGACTGGTGA G 21 (2) INFORMATION FOR SEQ ID NO:139: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:139: CGCAGGACAG TAGACACCTT GGTG 24 (2) INFORMATION FOR SEQ ID NO:140: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 23 baβe pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:140: CAGGCATCAC CGAACTGCGT GGC 23 (2) INFORMATION FOR SEQ ID NO:141: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 23 base paire (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:141: CGAGTGACGC TTGGTGCCTG GTC 23 (2) INFORMATION FOR SEQ ID NO:142: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:142: CACCTTGCTG CCGTATCCAG 20 (2) INFORMATION FOR SEQ ID NO:143: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:143: CCAATCGGCA GTGCTTTAGG GACC 24 (2) INFORMATION FOR SEQ ID NO:144: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 23 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:144: GTATCCCCGG CATCCAATCG TGC 23 (2) INFORMATION FOR SEQ ID NO:145: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 22 baee pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:145: CAACCATCCC AACACATGTA GG 22 (2) INFORMATION FOR SEQ ID NO:146: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 baee paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:146: GGGCTTGCCC AACTACTTCC 20 (2) INFORMATION FOR SEQ ID NO:147: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 base paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:147: GGAGGCGTGA TACTCAAAAA G 21 (2) INFORMATION FOR SEQ ID NO:148: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:148: CCGTGAGAGG CGACTGGTGA G 21 (2) INFORMATION FOR SEQ ID NO:149: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:149: CACCCAACCC GAGGACTCCA G 21 (2) INFORMATION FOR SEQ ID NO:150: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:150: CAGCAACCAC ACAGCCAAGC C 21 (2) INFORMATION FOR SEO ID NO:151: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:151; GGGCTTGCCC AACTACTTCC 20 (2) INFORMATION FOR SEQ ID NO:152: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:152; TAATGCTGCA GCCGACAGCT G 21 (2) INFORMATION FOR SEQ ID NO:153: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:153: GGAGGCGTGA TACTCAAAAA G 21 (2) INFORMATION FOR SEQ ID NO:154: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:154: CATGAAGAAC CCTCGCTTCC 20 (2) INFORMATION FOR SEQ ID NO:155: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 28 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:155: CCAAGTCAAG CTTGGCGCTT GTCATCAC 28 (2) INFORMATION FOR SEQ ID NO:156: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:156: CAACGCTGAG ATCCTCAGAG 20 (2) INFORMATION FOR SEQ ID NO:157: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 baβe pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:157: GATCCATAGT GAGCCACTCA C 21 (2) INFORMATION FOR SEO ID NO:158: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 221 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:158: GATCCATAGT GAGCCACTCA CCCATCAAGC ATTTAAATGT CAAGCAAGCA GTGGATGAGG 60 CGGCAGCATA GCCGCCTAGC ATGTCAAAGA CAAAACCCAC CGATGTCCAT GTACCAAGAG 120 CTGTTCCCAC AGCCCCGGCC ATCATGAACG CCAGTGCGTC TCTAGCGTCT GTAAGCTTGG 180 ACGCAATTGC GCCTCCAAAT AATGACAGGA ACATTTTGAT C 221 (2) INFORMATION FOR SEQ ID NO:159: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 337 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:159: GATCCAATCC AGGGGCCCTC GTACCCCTCC TGGCAGCTGT AGAAAGGACA ACCAGGAATG 60 TTAACCATGC TCTGAACTCC AGCTTTAAGG ACATTAAAGC AAATCACAAA GAAATTGCAC 120 ACATACTGCC AAATCTCTAG ACCCCAAGCA ATGAGGCCGC AATCATCCTC CGTCGGGGTG 180 TGGAGCCAAC GGATGCAAGC TGATATGATA CTCCAGGGGG TAGATGCCTC CAGAATGCCC 240 AGTATCTTCT GCGGATGTCA CGAGTGGCAA TAAAGTACTC ACTACATACA GTGTTGCTCC 300 TAGCAAGCAT AGTAAGAAGT CTGTTGGGCC AGTGATC 337 (2) INFORMATION FOR SEQ ID NO:160: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 base paire (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (qenomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:160: CCTCACTCAC CTTCGACCTC 20 (2) INFORMATION FOR SEQ ID NO:161: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 306 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:161: GATCCATCTT GACAATGACA ACTTTCGCAG GACAGTAGAC ACCTTGGTGA CGAACTCATC 60 TTTGAGGAAG AAATCGTCAG GCATCACCGA ACTGCGTGGC ATCATCGTCA ACAATCTGTT 120 AACCCAATCT TGACCCACAC CCTTTTTGAC AGACCAGAGC AACAAGCCCA GAACCACACC 180 GGCCACCGAA GCCCCCGGAG AGGCCAGGCA ACTGACCAGG CACCAAGCGT CACTCGCTTG 240 TAACTTCCCC GCCAGGAGGT CGAAGGTGAG TGAGCGCGGT TCACCGCCCC CTCCCAGCCT 300 CTGATC (2) INFORMATION FOR SEQ ID NO:162: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 baβe pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:162: GTGTCAAAAG CTAAGCAGGC 20 (2) INFORMATION FOR SEQ ID NO:163: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9364 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:163: CGTGGGAGTC CGGGGCCCCG GACCTCCCAC CGAGGTGGGG GGAAAGGGGC CCTGGACCGG 60 CCGGGTGGAA GGCCCGGAAC CGGTCCATCT TCCTCAAGGT TGAGGAAGGG GTACGTCTAT 120 CGGTCCGGTC GGTCCGAAAG GCGTCTGGAT GCCTAGTGTT AGGGTTCGTA GGTGGTAAAT 180 CCCAGCTAGG CGTGAAAGCG CTATAGGATA GGCTTATCCC GGTGACCGCT GCCCCGGAAC 240 CAGCCCCGCG GKTCTTTGGA CACGGTCCAC AGGTTGGGGG TACCGGTGTG AATAACCCCC 300 CGACTGAAGC GTCAGTCGTT AAACGGAGAC GGTCTCCTGA GATCGCAACG ACGCCCCACG 360 TACGGGAACG CCGCCAAAAC CTTCGGGACA GCTATGCGGG TTGACAATCC CAGTGGGGGG 420 CCGGGGACCA GCTGATTACT TGTCCTGCGA GTTCCTCTTG AGACTGGCCG AAAGGCAGCC 480 ACGGGGCCAC CAAGGCGGCG CAGCGCTGCA TGCGGCAAGG GGAAAAATCC TTCGGGTGAC 540 CCCTGGTGGC AATCCCTTCC CTTAGGAGCA TGAGTGTGGT CGACACATTC ACCATGGCTT 600 GGCTGTGGTT GCTGGTTTGC TTCCCCCTCG CGGGGGGGGT GCTCTTCAAC TCGCGGCACC 660 AGTGCTTCAA TGGGGACCAT TATGTGCTTT CCAATTGTTG TTCCCGAGAC GAGGTTTACT 720 TCTGTTTCGG GGACGGATGT CTGGTGGCTT ATGGCTGTAC TGTTTGCACA CAGTCTTGCT 780 GGAAGCTCTA CCGGCCTGGG GTGGCTACTC GGCCCGGGTC CGAACCAGGT GAGCTGCTGG 840 GGAGATTTGG GAGTGTAATT GGTCCGGTGT CGGCTTCGGC TTACACCGCT GGAGTCCTCG 900 GGTTGGGTGA ACCTTACAGT TTGGCCTTCT TGGGGACGTT CCTCACCAGT CGCCTCTCAC 960 GGATTCCCAA CGTCACCTGC GTGAAGGCTT GTGACCTTGA GTTTACCTAC CCAGGCTTGT 1020 CCATCGATTT TGACTGGGCG TTTACCAAGA TCTTGCAGTT GCCGGCCAAG CTGTGGCGAG 1080 GCCTAACGGC RGCWCCGGTC TTGAGCCTCC TCGTGATCCT CATGCTGGTC CTCGAGCAGC 1140 GCCTCCTGAT AGCCTTCCTA CTGCTTTTGG TAGTGGGCGA GGCTCAGAGG GGGATGTTCG 1200 ACAACTGCGT GTGTGGTTAC TGGGGGGGCA AGAGGCCCCC GTCGGTGACC CCGCTGTACC 1260 GTGGCAACGG TACTGTGGTG TGTGACTGTG ATTTTGGAAA AATGCATTGG GCCCCCCCCT 1320 TGTGTTCCGG YCTGGTGTGG CGGGACGGTC ATAGGAGGGG CACCGTGCGC GACCTCCCCC 1380 CGGTTTGCCC CCGGGAGGTT CTCGGCACGG TGACAGTCAT GTGTCAGTGG GGTTCTGCCT 1440 ACTGGATTTG GAGATTTGGG GACTGGGTTG CATTGTACGA CGAGCTACCA CGATCAGCTC 1500 TCTOTACTT CTTCTCAG T CATCWTCOAC AACCTΆAAOA TCTCTOARTC TTGAATCCAT 1R60 CCGGGGCACC TTGTGCTTCT TGCGTCGTTG ACCAGAGGCC GCTGAAATGT GGTTCCTGCG 1620 TCCGCGACTG CTGGGAGACG GGGGGTCCTG GGTTCGATGA GTGCGGTGTC GGTACTCGGA 1680 TGACGAAGCA CCTCGAGGCC GTCCTGGTTG ATGGAGGTGT GGAGTCCAAG GTGACAACGC 1740 CCAAGGGTGA GCGCCCCAAA TACATAGGTC AGCACGGTGT GGGAACCTAC TACGGCGCTG 1800 TCCGTAGCCT CAACATCAGT TACCTAGTGA CTGAGGTGGG GGGCTATTGG CATGCGCTGA 1860 AGTGCCCGTG CGACTTTGTG CCCCGAGTGC TCCCAGAAAG AATTCCAGGT AGGCCTGTGA 1920 ATGCATGTCT AGCTGGGAAG TCTCCGCACC CGTTCGCAAG TTGGGCTCCC GGTGGGTTTT 1980 ACGCCCCCGT GTTCACCAAG TGCAACTGGC CGAAGACCTC CGGAGTGGAT GTGTGTCCTG 2040 GGTTTGCTTT CGATTTCCCT GGTGATCACA ACGGCTTCAT CCATGTTAAA GGCAACAGAC 2100 AGCAGGTTTA CAGTGGTCAG CGAAGGTCTT CGCCGGCTTG GTTGCTTACT GACATGGTCC 2160 TGGCCCTGTT GGTGGTGATG AAGTTGGCTG AGGCTAGAGT TGTCCCCCTG TTTATGCTGG 2220 CAATGTGGTG GTGGTTGAAT GGAGCATCTG CTGCCACTAT TGTCATCATA CACCCTACTG 2280 TCACGAAGTC CACTGAAAGT GTTCCATTGT GGACTCCGCC CACTGTTCCA ACTCCATCTT 2340 GCCCGAATTC TACCACCGGA GTCGCGGACT CTACCTACAA TGCTGGTTGC TACATGGTGG 2400 CAGGCCTGGC GGCCGGGGCT CAGGCGGTCT GGGGTGCTGC CAATGATGGT GCTCAGGCCG 2460 TCGTTGGTGG CATCTGGCCC GCGTGGCTC AGCTGCGAAG CTTCGCTGCC GGTCTGGCCT 2520 GGTTGTCAAA TGTTGGGGCT TACTTGCCGG TCGTCGAGGC CGCVCTGGCT CCCGAGCTGG 2580 TGTGCACCCC GGTGGTCGGC TGGGCAGCCC AGGAGTGGTG GTTCACTGGT TGTCTGGGTG 2640 TGATGTGTGT CGTGGCGTAC CTGAATGTCC TGGGCTCTGT RAGGGCTGCC GTGCTTGTGG 2700 CGATGCACTT CGCAAGGGGT GCTCTGCCGC TGGTATTGGT GGTAGCTGCC GGGGTRACCC 2760 GGGAGCGGCA CAGCGTCTTA GGGCTTGAGG TGTGCTTCGA TCTGGATGGT GGAGACTGGC 2820 CRGACGCCAG TTGGTCTTGG GGTTTAGCAG GCGTGGTGAG CTGGGCCCTC CTGGTGGGGG 2880 GTCTGATGAC CCACGGTGGC CGATCAGCCA GAYTGACTTG GTAYGCCAGG TGGGCCGTCA 2940 ATTAYCAGAG GGTTCGYCGG TGGGTGAACA ACTCACCGGT TGGAGCYTTT GGYCGTTGGM 3000 GGCGYGCCTG GAAAGCYTGG TTRGTKGTGG CTTGGTTCTT CCCCCAGACA GTTGCCACAG 3060 TYTCCGTCAT CTTCATACTC TGTTTGAGCA GTTTAGATGT CATTGATTTC ATCTTGGARG 3120 TACTCTTGGT TAACTCACCA AATCTCGCGC GCTTGGCGCG R^TGCTGGAC TCCTTAGCTC 3180 THGCTGAGGA GCGGCTGGCC TGCTCTTGGC TGGTGGGCGT CCCGCGCAAG CGGGGCGTCC 3240 TCCTCTACGA GCACGCYGGT CACACTAGCA GGCGCGGTC5C TOrrTTSC G CGACJAO GCV; 330fl GYTTTGCGCT YGAGCCKGTT AGYATAACCA AGGAAGATTG YGCYATTGTT CGGGACTCTG 3360 CTCGTGTGTT GGGCTGTGGA CAATTGGTCC ATGGGAAACC AGTGGTCGCG AGGCGAGGCG 3420 ACGAGGTGTT GATCGGCTGT GTGAACAGTC GGTTCGACCT TCCGCCTGGC TTTGTTCCCA 3480 CTGCTCCCGT GGTSCTTCAT CARGCWGGCA ARGGRTTYTT YGGGGTTGTG AAGACMTCCA 3540 TGACAGGCAA GGACCCGTCC GAACACCACG GRAACGTGGT GGTCCTWGGG ACTTCAACAA 3600 CKCGTTCCAT GGGCTGCTGC GTGAACGGAG TAGTGTACAC RACATACCAT GGYACCAACG 3660 CCCGRCCKAT GGCGGGGCCK TTTGGKCCYG TCAAYGCTCG GTGGTGGTCW GCGAGYGACG 3720 ACGTCACGGT YTACCCGCTC CCWAATGGYG CTTCTTGCCT YCARGCWTGY AAGTGCCAAC 3780 CAACTGGGGT GTGGGTGATC CGGAATGACG GAGCTCTTTG CCATGGAACT CTCGGCAAGG 3840 TGGTGGATTT AGATATGCCC GCTGAGTTGT CAGACTTTCG CGGGTCTTCT GGATCACCAA 3900 TCTTGTGCGA TGAGGGTCAT GCTGTTGGCA TGCTGATTTC GGTGCTTCAT AGGGGGAGTA 3960 GGGTTTCCTC GGTGCGGTAT ACCAAACCTT GGGAAACTCT CCCTCGGGAG ATTGAGGCTC 4020 GATCGGAGGC CCCCCCTGTG CCAGGAACCA CTGGATACAG GGAGGCGCCA CTGTTCCTGC 4080 CCACCGGAGC TGGCAAGTCG ACGCGCGTGC CGAATGAGTA CGTCAAGGCT GGACACAARG 4140 TGCTTGTACT AAACCCATCC ATTGCCACAG TGAGGGCCAT GGGCCCTTAC ATGGAAAAGT 4200 TAACCGGCAA ACATCCGTCG GTGTACTGTG GCCATGACAC TACTGCATAT TCCAGGACTA 4260 CTGACTCATC TTTGACCTAC TGTACATACG GCAGGTTTAT GGCCAATCCC AGGAAATACT 4320 TGCGGGGGAA CGACGTCGTA ATTTGCGACG AGTTGCACGT CACCGACCCG ACCTCAATTT 4380 TGGGGATGGG TCGGGCGAGG TTACTCGCTC GCGAGTGCGG CGTACGCCTC CTGCTTTTCG 4440 CTACGGCGAC CCCACCGGTC TCTCCGATGG CGAAGCATGA ATCTATTCAT GAGGAGATGT '4500 TGGGCAGTGA GGGGGAGGTC CCCTTCTATT GCCAATTCCT CCCACTGAGT AGGTATGCTA 4560 CTGGGAGACA CCTGCTGTTT TGTCATTCCA AGGTAGARTG CACTAGGTTA TCCTCAGCTT 4620 TGGCCAGCTT TGGTGTCAAC ACCGTTGTGT ACTTCAGAGG CAAAGAAACT GACATTCCAA 4680 CTGGTGACGT GTGCGTTTGC GCCACAGACG CACTTTCCAC TGGTTACACT GGCAATTTTG 4740 ACACCGTAAC AGACTGTGGT TTAATGGTTG AGGAGGTAGT GGAAGTGACC CTGGACCCGA 4800 CCATCACTAT CGGTGTGAAG ACCGTCCCGG CCCCTGCCGA ACTGAGGGCT CAGAGGCGTG 4860 GTAGGTGTGG CCGTGGGAAA GCGGGCACTT ACTATCAGGC ATTGATGTCT TCGGCGCCGG 4920 CGGGAACSGT TCGGTCTGGG GCTCTCTGGG CAGCTGTTGA GGCTGGHGTC TCGTGGTATG 4980 GCCTAGAGCC CGATGCTATT GGAGACCTGC TTAGGGCCTA CGACTCGTGT CCTTATACTG 5040 CTGCCATCAG TGCGTCCATC GGAGAGGCCA TTGCCTTTTT TACTGGYCTA GTGCCAATGA 5100 GGAATTATCC TCAGGTGGTT TGGGCCAAGC AGAAGGGRCA CAACTGGCCA CTCTTGGTGG 5160 GTGTGCAGAG GCACATGTGT GAGGACGCGG GCTGTGGTCC KCCCGCTAAT GGTCCCGAAT 5220 GGAGCGGCAT CAGGGGAAAA GGGCCTGTTC CCCTGTTGTG CCGATGGGGT GGTGACTTGC 5280 CTGAGTCGGT GGCTCCGCAT CACTGGGTTG ATGACCTACA GGCCCGGCTC GGTGTGGCCG 5340 AGGGTTACAC TCCCTGCATT GCTGGACCGG TGCTTTTGGT CGGTTTGGCG ATGGCGGGGG 5400 GGGCTATCCT GGCACACTGG ACGGGGTCTC TGGTTGTAGT GACCAGTTGG GTTGTCAATG 5460 GGAACGGTAA CCCGCTGATA CAAAGCGCCT CTAGGGGCGT GGCKACYAGC GGTCCATACC 5520 CAGTACCCCC AGATGGTGGT GAACGGTACC CATCAGACAT CAAGCCAATY ACTGAGGCTG 5580 TGACCACCCT TGAGACTGCG TGCGGYTGGG GCCCAGCCGC GGCBAGTCTG GCTTATGTGA 5640 AGGCCTGTGA AACTGGAACC ATGTTGGCTG ACAARGCGAG TGCTGCGTGG CAGGCTTGGG 5700 CTGCAAACAA CTTTGTGCCT CCACCAGCAT CACACTCAAC TTCCTTGTTR CAGAGCTTGG 5760 AYGCTGCGTT CACTTCAGCT TGGGATAGCG TGTTCACTCA CGGCCGTTCC TTGCTTGTTG 5820 GGTTCACAGC TGCTTACGGC GCTCGGCGGA ACCCACCGCT GGGCGTCGGA GCCTCTTTCT 5880 TGCTGGGCAT GTCATCGAGC CACYTRACTC ACGTCAGACT TGCTGCTGCG TTGCTCCTCG 5940 GCGTCGGGGG TACCGTCCTA GGCACGCCTG CTACTGGGCT TGCTATGGCG GGTGCCTACT 6000 TCGCKGGGGG CAGCGTTACC GCTAACTGGC TGAGTATCAT TGTGGCTCTA ATCGGAGGCT 6060 GGGAGGGGGC RGTKAACGCA GCCTCACTCA CCTTCGAYCT CCTGGCKGGG AAGTTACAAG 6120 CKAGYGAYGC TTGGTGCCTR GTCAGYTGCY TGGCCTCTCC GGGGGCTTCG GTGGCYGGTG 6180 TGGCDCTVGG YCTDYTGCTV TGGTCTGTCA ARAAGGGTGT GGGWCARGAY TGGGTTAACA 6240 GAYTGTTGAC GATGATGCCA CGCAGTTCGG TGATGCCTGA CGATTTCTTC CTCAAAGATG 6300 AGTTCGTCAC CAAGGTGTCT ACTGTCCTGC GAAAGTTGTC ATTGTCAAGA TGGATCATGA 6360 CTCTTGTGGA CAAGCGGGAG ATGGAGATGG AGACMCCCGC TTCTCAGATT GTTTGGGACT 6420 TGCTTGACTG GTGCATCCGG CTRGGTCGGT TCCTGTACAA TAAACTYATG TTTGCTCTCC 6480 CTAGGTTGCG CCTGCCGCTT ATCGGTTGCA GTACCGGTTG GGGTGGCCCG TGGGAGGGCA 6540 ATGGTCATTT GGAAACAAGG TGTACTTGTG GCTGTGTGAT TACCGGTGAT ATTCACGATG 6600 GTATATTGCA CGACCTACAT TATACCTCCC TACTGTGCAG ACATTACTAC AAGAGGACAG 6660 TGCCTGTTGG CGTCATGGGC AATGCTGAGG GAGCAGTCCC CCTTGTGCCT ACTGGCGGTG 6720 GAATCAGGAC TTACCAAATT GGGACTTCTG ACTGGTTTGA GGCTGTGGTC GTGCATGGGA 6780 CAATCACGGT GCACGCCACC AGTTGCTATG AGTTGAAAGC TGCTGACGTT CGGAGGGCGG 6840 TGCGAGCCGG CCCGACTTAC GTTGGTGGCG TACCTTGCAG CTGGAGCGCG CCGTGTACTG 6900 CGCCTGCGCT CGTTTACAGG CTAGGCCAGG GCATCAAAAT CGATGGAGCG CGCCGACTGT 6960 TGCCCTGTGA CTTAGCACAG GGAGCGCGCC ACCCCCCGGT ATCTGGCAGT GTTGCCGGTA 7020 GTGGTTGGAC AGATGAGGAC GAGAGGGACT TGGTGGAAAC CAAGGCTGCC GCCATCGAGG 7080 CCATTGGGGC GGCCTTGCAC CTCCCTTCAC CGGAGGCTGC TCAGGCCGCT CTAGAGGCTT 7140 TGGAGGAGGC TGCCGTGTCC CTGTTGCCCC ATGTGCCCGT CATTATGGGT GATGACTGTT 7200 CATGCCGGGA TGAGGCGTTC CAAGGCCACT TCATCCCAGA ACCCAATGTG ACAGAGGTAC 7260 CCATTGAGCC CACGGTCGGA GACGTGGAGG CACTCAAGCT GCGGGCTGCA GACCTGACCG 7320 CCAGGTTGCA AGACTTGGAG GCCATGGCTC TCGCCCGCGC TGAGTCAATC GAGGATGCTC 7380 GCGCAGCTTC GATGCCTTCG CTCACCGAGG TGGACTCAAT GCCATCATTG GAGTCGAGCC 7440 CTTGCTCCTC CTTTGAACAA ATCTCTTTAA CTGAAAGTGA CCCTGAGACT GTCGTCGAGG 7500 CTGGCTTACC CTTGGAGTTC GTGAACTCCA ACACCGGGCC GTCTCCGGCT CGGAGGATTG 7560 TCAGAATCCG ACAGGCTTGC TGTTGTGACA GATCCACAAT GAAGGCCATG CCGTTGTCGT 7620 TCACTGTCGG GGAGTGCCTC TTCGTTACTC GCTATGACCC GGACGGTCAC CAACTGTTTG 7680 ACGAGCGAGG TCCGATAGAG GTATCTACTC CTATATGTGA AGTGATTGGG GACATCAGGC 7740 TTCAGTGTGA CCAAATTGAG GAAACTCCAA CATCTTACTC TTACATCTGG TCAGGGGCGC 7800 CCTTGGGTAC TGGGAGAAGT GTCCCCCAAC CCATGACGCG CCCTATAGGG ACCCATCTGA 7860 CTTGTGACAC TACCAAAGTT TATGTTACTG ACCCTGATCG GGCCGCTGAG CGGGCCGAGA 7920 AGGTTACAAT CTGGAGGGGT GATAGGAAGT ATGACAAGCA TTATGAGGCT GTCGTTGAGG 7980 CTGTCCTGAA AAAGGCAGCC GCGACGAAGT CTCATGGCTG GACCTATTCC CAGGCTATAG 8040 CTAAAGTTAG GCGCCGAGCA GCCGCTGGAT ACGGCAGCAA GGTGACCGCC TCCACATTGG 8100 CCACTGGTTG GCCTCACGTG GAGGAGATGC TGGACAAAAT AGCCAGGGGA CAGGAAGTTC 8160 CTTTCACTTT TGTGACCAAG CGAGAGGTTT TCTTCTCCAA AACTACCCGT AAGCCCCCAA 8220 GATTCATAGT TTTCCCACCT TTGGACTTCA GGATAGCTGA AAAGATGATT CTGGGTGACC 8280 CCGGCATCGT TGCAAAGTCA ATTCTGGGTG ACGCTTATCT GTTCCAGTAC ACGCCCAATC 8340 AGAGGGTCAA AGCTCTGGTT AAGGCGTGGG AGGGGAAGTT GCATCCCGCT GCGATCACTG 8400 TGGACGCCAC TTGTTTCGAC TCATCGATTG ATGAGCACGA CATGCAGGTG GAGGCTTCGG 8460 TGTTTGCGGC GGCTAGTGAC AACCCCTCAA TGGTACATGC TTTGTGCAAG TACTACTCTG 8520 GTGGCCCTAT GGTTTCCCCA GATGGGGTTC CCTTGGGGTA CCGCCAGTGT AGGTCGTCGG 8580 GCGTGTTAAC AACTAGCTCG GCGAACAGCA TCACTTGTTA CATTAAGGTC AGCGCGGCCT 8640 GCAGGCGGGT GGGGATTAAG GCACCATCAT TCTTTATAGC TGGAGATGAT TGCTTGATCA 8700 TCTATGAAAA TGATGGAACT GATCCCTGCC CTGCTCTTAA GGCTGCCCTG GCCAACTATG 8760 GATACAGGTG TGAACCAACA AAGCATGCTT CACTGGACAC AGCTGAGTGT TGCTCGGCCT 8820 ACTTGGCTGA GTGCGTAGCT GGGGGTGCCA AGCGCTGGTG GTTGAGCACG GACATGAGGA 8880 AGCCGCTCGC AAGGGCGTCT TCCGAATATT CGGACCCAAT CGGCAGTGCT TTAGGGACCA 8940 TCTTGATGTA TCCCCGGCAT CCAATCGTGC GGTATGTTCT AATACCACAC GTACTAATAA 9000 TGGCTTACAG GAGTGGCAGC ACACCGGATG AGTTGGTTAT GTGTCAGGTT CAGGGAAATC 9060 ATTACTCTTT CCCGCTGCGG CTGCTGCCTC GCGTCTTGGT CTCTCTACAT GGTCCGTGGT 9120 GCCTACAAGT CACCACGGAC AGTACGAAGA CTAGGATGGA GGCAGGCTCA GCSTTGCGGG 9180 ATTTAGGAAT GAAATCCCTA GCCTGGCACC GCCGACGTGC CGGAAATGTG CGCACTCGCC 9240 TCCTGAGGGG AGGCAAGGAG TGGGGGCACC TGGCCAGAGC CCTCCTCTGG CAYCCAGGKT 9300 TGAAGGAGCA YCCCCCRCCC ATAAATTCAC TTCCAGGTTT TCAGCTGGCG ACGCCTTACG 9360 AACACCATGA AGAGGTCTTG ATCTCGATCA AGAGTCGACC ACCTTGGATA AGGTGGATTC 9420 TTGGTGCTTG TCTCTCGTTG CTGGCCGCCT TGCTGTGAAT TCGCTCCAGG CAGTAGGACC 9480 TTCGGGTCGG GGG 9493 (2) INFORMATION FOR SEQ ID NO:164: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9493 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 1..9493 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:164: CGT GGG AGT CCG GGG CCC CGG ACC TCC CAC CGA GGT GGG GGG AAA GGG 48 Arg Gly Ser Pro Gly Pro Arg Thr Ser His Arg Gly Gly Gly Lye Gly 1 5 10 15 GCC CTG GAC CGG CCG GGT GGA AGG CCC GGA ACC GGT CCA TCT TCC TCA 96 Ala Leu Asp Arg Pro Gly Gly Arg Pro Gly Thr Gly Pro Ser Ser Ser 20 25 30 AGG TTG AGG AAG GGG TAC GTC TAT CGG TCC GGT CGG TCC GAA AGG CGT 144 Arg Leu Arg Lys Gly Tyr Val Tyr Arg Ser Gly Arg Ser Glu Arg Arg 35 40 45 CTG GAT GCC TAG TGT TAG GGT TCG TAG GTG GTA AAT CCC AGC TAG GCG 192 Leu Asp Ala * Cye * Gly Ser * Val Val Asn Pro Ser * Ala 50 55 60 TGA AAG CGC TAT AGG ATA GGC TTA TCC CGG TGA CCG CTG CCC CGG AAC 240 * Lys Arg Tyr Arg He Gly Leu Ser Arg * Pro Leu Pro Arg Asn 65 70 75 80 CAG CCC CGC GGK TCT TTG GAC ACG GTC CAC AGG TTG GGG GTA CCG GTG 288 Gin Pro Arg Xaa Ser Leu Asp Thr Val His Arg Leu Gly Val Pro Val 85 90 95 TGA ATA ACC CCC CGA CTG AAG CGT CAG TCG TTA AAC GGA GAC GGT CTC 336 * He Thr Pro Arg Leu Lys Arg Gin Ser Leu Asn Gly Asp Gly Leu 100 105 110 CTG AGA TCG CAA CGA CGC CCC ACG TAC GGG AAC GCC GCC AAA ACC TTC 384 Leu Arg Ser Gin Arg Arg Pro Thr Tyr Gly Asn Ala Ala Lys Thr Phe 115 120 125 GGG ACA GCT ATG CGG GTT GAC AAT CCC AGT GGG GGG CCG GGG ACC AGC 432 Gly Thr Ala Met Arg Val Asp Asn Pro Ser Gly Gly Pro Gly Thr Ser 130 135 140 TGA TTA CTT GTC CTG CGA GTT CCT CTT GAG ACT GGC CGA AAG GCA GCC 480 * Leu Leu Val Leu Arg Val Pro Leu Glu Thr Gly Arg Lys Ala Ala 145 150 155 160 ACG GGG CCA CCA AGG CGG CGC AGC GCT GCA TGC GGC AAG GGG AAA AAT 528 Thr Gly Pro Pro Arg Arg Arg Ser Ala Ala Cys Gly Lys Gly Lys Asn 165 170 175 CCT TCG GGT GAC CCC TGG TGG CAA TCC CTT CCC TTA GGA GCA TGA GTG 576 Pro Ser Gly Asp Pro Trp Trp Gin Ser Leu Pro Leu Gly Ala * Val 180 185 190 TGG TCG ACA CAT TCA CCA TGG CTT GGC TGT GGT TGC TGG TTT GCT TCC 624 Trp Ser Thr His Ser Pro Trp Leu Gly Cyβ Gly Cys Trp Phe Ala Ser 195 200 205 CCC TCG CGG GGG GGG TGC TCT TCA ACT CGC GGC ACC AGT GCT TCA ATG 672 Pro Ser Arg Gly Gly Cye Ser Ser Thr Arg Gly Thr Ser Ala Ser Met 210 215 220 GGG ACC ATT ATG TGC TTT CCA ATT GTT GTT CCC GAG ACG AGG TTT ACT 720 Gly Thr He Met Cye Phe Pro He Val Val Pro Glu Thr Arg Phe Thr 225 230 235 240.. TCT GTT TCG GGG ACG GAT GTC TGG TGG CTT ATG GCT GTA CTG TTT GCA 768 295 Ser Val Ser Gly Thr Asp Val Trp Trp Leu Met Ala Val Leu Phe Ala 245 250 255 CAC AGT CTT GCT GGA AGC TCT ACC GGC CTG GGG TGG CTA CTC GGC CCG 816 His Ser Leu Ala Gly Ser Ser Thr Gly Leu Gly Trp Leu Leu Gly Pro 260 265 270 GGT CCG AAC CAG GTG AGC TGC TGG GGA GAT TTG GGA GTG TAA TTG GTC 864 Gly Pro Asn Gin Val Ser Cye Trp Gly Aep Leu Gly Val * Leu Val 275 280 285 CGG TGT CGG CTT CGG CTT ACA CCG CTG GAG TCC TCG GGT TGG GTG AAC 912 Arg Cys Arg Leu Arg Leu Thr Pro Leu Glu Ser Ser Gly Trp Val Asn 290 295 300 CTT ACA GTT TGG CCT TCT TGG GGA CGT TCC TCA CCA GTC GCC TCT CAC 960 Leu Thr Val Trp Pro Ser Trp Gly Arg Ser Ser Pro Val Ala Ser His 305 310 315 320 GGA TTC CCA ACG TCA CCT GCG TGA AGG CTT GTG ACC TTG AGT TTA CCT 1008 Gly Phe Pro Thr Ser Pro Ala * Arg Leu Val Thr Leu Ser Leu Pro 325 330 335 ACC CAG GCT TGT CCA TCG ATT TTG ACT GGG CGT TTA CCA AGA TCT TGC 1056 Thr Gin Ala Cys Pro Ser He Leu Thr Gly Arg Leu Pro Arg Ser Cys 340 345 350 AGT TGC CGG CCA AGC TGT GGC GAG GCC TAA CGG CRG CWC CGG TCT TGA 1104 Ser Cys Arg Pro Ser Cys Gly Glu Ala * Arg Xaa Xaa Arg Ser * 355 360 365 GCC TCC TCG TGA TCC TCA TGC TGG TCC TCG AGC AGC GCC TCC TGA TAG 1152 Ala Ser Ser * Ser Ser Cys Trp Ser Ser Ser Ser Ala Ser * * 370 375 380 CCT TCC TAC TGC TTT TGG TAG TGG GCG AGG CTC AGA GGG GGA TGT TCG 1200 Pro Ser Tyr Cyβ Phe Trp * Trp Ala Arg Leu Arg Gly Gly Cys Ser 385 390 395 400 ACA ACT GCG TGT GTG GTT ACT GGG GGG GCA AGA GGC CCC CGT CGG TGA 1248 Thr Thr Ala Cyβ Val Val Thr Gly Gly Ala Arg Gly Pro Arg Arg * 405 410 415 CCC CGC TGT ACC GTG GCA ACG GTA CTG TGG TGT GTG ACT GTG ATT TTG 1296 Pro Arg Cys Thr Val Ala Thr Val Leu Trp Cys Val Thr Val He Leu 420 425 430 GAA AAA TGC ATT GGG CCC CCC CCT TGT GTT CCG GYC TGG TGT GGC GGG 1344 Glu Jbys Cys lie Gly Pro Pro Pro Cye Val Pro Xaa Trp Cys Gly Gly 435 440 445 ACG GTC ATA GGA GGG GCA CCG TGC GCG ACC TCC CCC CGG TTT GCC CCC 1392 Thr Val He Gly Gly Ala Pro Cys Ala Thr Ser Pro Arg Phe Ala Pro 450 455 460 GGG AGG TTC TCG GCA CGG TGA CAG TCA TGT GTC AGT GGG GTT CTG CCT 1440 Gly Arg Phe Ser Ala Arg * Gin Ser Cyβ Val Ser Gly Val Leu Pro 465 470 475 480 ACT GGA TTT GGA GAT TTG GGG ACT GGG TTG CAT TGT ACG ACG AGC TAC 1488 Thr Gly Phe Gly Aep Leu Gly Thr Gly Leu Hie Cye Thr Thr Ser Tyr 485 490 495 CAC GAT CAG CTC TCT GTA CTT TCT TCT CAG GTC ATG GTC CAC AAC CTA 1536 Hie Aep Gin Leu Ser Val Leu Ser Ser Gin Val Met Val His Aβn Leu 500 505 510 AAG ATC TCT CAG TCT TGA ATC CAT CCG GGG CAC CTT GTG CTT CTT GCG 1584 Lye He Ser Gin Ser * He Hie Pro Gly Hie Leu Val Leu Leu Ala 515 520 525 TCG TTG ACC AGA GGC CGC TGA AAT GTG GTT CCT GCG TCC GCG ACT GCT 1632 Ser Leu Thr Arg Gly Arg * Aen Val Val Pro Ala Ser Ala Thr Ala 530 535 540 GGG AGA CGG GGG GTC CTG GGT TCG ATG AGT GCG GTG TCG GTA CTC GGA 1680 Gly Arg Arg Gly Val Leu Gly Ser Met Ser Ala Val Ser Val Leu Gly 545 550 555 560 TGA CGA AGC ACC TCG AGG CCG TCC TGG TTG ATG GAG GTG TGG AGT CCA 1728 * Arg Ser Thr Ser Arg Pro Ser Trp Leu Met Glu Val Trp Ser Pro 565 570 575 AGG TGA CAA CGC CCA AGG GTG AGC GCC CCA AAT ACA TAG GTC AGC ACG 1776 Arg * Gin Arg Pro Arg Val Ser Ala Pro Asn Thr * Val Ser Thr 580 585 590 GTG TGG GAA CCT ACT ACG GCG CTG TCC GTA GCC TCA ACA TCA GTT ACC 1824 Val Trp Glu Pro Thr Thr Ala Leu Ser Val Ala Ser Thr Ser Val Thr 595 600 605 TAG TGA CTG AGG TGG GGG GCT ATT GGC ATG CGC TGA AGT GCC CGT GCG 1872 * * Leu Arg Trp Gly Ala He Gly Met Arg * Ser Ala Arg Ala 610 615 620 ACT TTG TGC CCC GAG TGC TCC CAG AAA GAA TTC CAG GTA GGC CTG TGA 1920 Thr Leu Cys Pro Glu Cyβ Ser Gin Lye Glu Phe Gin Val Gly Leu * 625 630 635 640 ATG CAT GTC TAG CTG GGA AGT CTC CGC ACC CGT TCG CAA GTT GGG CTC 1968 Met Hie Val * Leu Gly Ser Leu Arg Thr Arg Ser Gin Val Gly Leu 645 650 655 CCG GTG GGT TTT ACG CCC CCG TGT TCA CCA AGT GCA ACT GGC CGA AGA 2016 Pro Val Gly Phe Thr Pro Pro Cys Ser Pro Ser Ala Thr Gly Arg Arg 660 665 670 CCT CCG GAG TGG ATG TGT GTC CTG GGT TTG CTT TCG ATT TCC CTG GTG 2064 Pro Pro Glu Trp Met Cys Val Leu Gly Leu Leu Ser He Ser Leu Val 675 680 685 ATC ACA ACG GCT TCA TCC ATG TTA AAG GCA ACA GAC AGC AGG TTT ACA 2112 He Thr Thr Ala Ser Ser Met Leu Lys Ala Thr Asp Ser Arg Phe Thr 690 695 700 GTG GTC AGC GAA GGT CTT CGC CGG CTT GGT TGC TTA CTG ACA TGG TCC 2160 Val Val Ser Glu Gly Leu Arg Arg Leu Gly Cye Leu Leu Thr Trp Ser 705 710 715 720 TGG CCC TGT TGG TGG TGA TGA AGT TGG CTG AGG CTA GAG TTG TCC CCC 2208 Trp Pro Cys Trp Trp * * Ser Trp Leu Arg Leu Glu Leu Ser Pro 725 730 735 TGT TTA TGC TGG CAA TGT GGT GGT GGT TGA ATG GAG CAT CTG CTG CCA 2256 Cys Leu Cyβ Trp Gin Cyβ Gly Gly Gly * Met Glu Hie Leu Leu Pro 740 745 750 CTA TTG TCA TCA TAC ACC CTA CTG TCA CGA AGT CCA CTG AAA GTG TTC 2304 Leu Leu Ser Ser Tyr Thr Leu Leu Ser Arg Ser Pro Leu Lys Val Phe 755 760 765 CAT TGT GGA CTC CGC CCA CTG TTC CAA CTC CAT CTT GCC CGA ATT CTA 2352 Hie Cys Gly Leu Arg Pro Leu Phe Gin Leu His Leu Ala Arg He Leu 770 775 780 CCA CCG GAG TCG CGG ACT CTA CCT ACA ATG CTG GTT GCT ACA TGG TGG 2400 Pro Pro Glu Ser Arg Thr Leu Pro Thr Met Leu Val Ala Thr Trp Trp 785 790 795 800 CAG GCC TGG CGG CCG GGG CTC AGG CGG TCT GGG GTG CTG CCA ATG ATG 2448 Gin Ala Trp Arg Pro Gly Leu Arg Arg Ser Gly Val Leu Pro Met Met 805 810 815 GTG CTC AGG CCG TCG TTG GTG GCA TCT GGC CCG CGT GGC TCA AGC TGC 2496 Val Leu Arg Pro Ser Leu Val Ala Ser Gly Pro Arg Gly Ser Ser Cys 820 825 830 GAA GCT TCG CTG CCG GTC TGG CCT GGT TGT CAA ATG TTG GGG CTT ACT 2544 Glu Ala Ser Leu Pro Val Trp Pro Gly Cye Gin Met Leu Gly Leu Thr 835 840 845 TGC CGG TCG TCG AGG CCG CVC TGG CTC CCG AGC TGG TGT GCA CCC CGG 2592 Cys Arg Ser Ser Arg Pro Xaa Trp Leu Pro Ser Trp Cys Ala Pro Arg 850 855 860 TGG TCG GCT GGG CAG CCC AGG AGT GGT GGT TCA CTG GTT GTC TGG GTG 2640 Trp Ser Ala Gly Gin Pro Arg Ser Gly Gly Ser Leu Val Val Trp Val 865 870 875 880 TGA TGT GTG TCG TGG CGT ACC TGA ATG TCC TGG GCT CTG TRA GGG CTG 2688 * Cys Val Ser Trp Arg Thr * Met Ser Trp Ala Leu Xaa Gly Leu 885 890 895 CCG TGC TTG TGG CGA TGC ACT TCG CAA GGG GTG CTC TGC CGC TGG TAT 2736 Pro Cys Leu Trp Arg Cys Thr Ser Gin Gly Val Leu Cye Arg Trp Tyr 900 905 910 TGG TGG TAG CTG CCG GGG TRA CCC GGG AGC GGC ACA GCG TCT TAG GGC 2784 Trp Trp * Leu Pro Gly Xaa Pro Gly Ser Gly Thr Ala Ser * Gly 915 920 925 TTG AGG TGT GCT TCG ATC TGG ATG GTG GAG ACT GGC CRG ACG CCA GTT 2832 Leu Arg Cye Ala Ser He Trp Met Val Glu Thr Gly Xaa Thr Pro Val_. 930 935 940 GGT CTT GGG GTT TAG CAG GCG TGG TGA GCT GGG CCC TCC TGG TGG GGG 2880 Gly Leu Gly Val * Gin Ala Trp * Ala Gly Pro Ser Trp Trp Gly 945 950 955 960 GTC TGA TGA CCC ACG GTG GCC GAT CAG CCA GAY TGA CTT GGT AYG CCA 2928 Val * * Pro Thr Val Ala Asp Gin Pro Xaa * Leu Gly Xaa Pro 965 970 975 GGT GGG CCG TCA ATT AYC AGA GGG TTC GYC GGT GGG TGA ACA ACT CAC 2976 Gly Gly Pro Ser He Xaa Arg Gly Phe Xaa Gly Gly * Thr Thr His 980 985 990 CGG TTG GAG CYT TTG GYC GTT GGM GGC GYG CCT GGA AAG CYT GGT TRG 3024 Arg Leu Glu Xaa Leu Xaa Val Xaa Gly Xaa Pro Gly Lys Xaa Gly Xaa 995 1000 1005 TKG TGG CTT GGT TCT TCC CCC AGA CAG TTG CCA CAG TYT CCG TCA TCT 3072 Xaa Trp Leu Gly Ser Ser Pro Arg Gin Leu Pro Gin Xaa Pro Ser Ser 1010 1015 1020 TCA TAC TCT GTT TGA GCA GTT TAG ATG TCA TTG ATT TCA TCT TGG ARG 3120 Ser Tyr Ser Val * Ala Val * Met Ser Leu He Ser Ser Trp Xaa 1025 1030 1035 1040 TAC TCT TGG TTA ACT CAC CAA ATC TCG CGC GCT TGG CGC GRG TGC TGG 3168 Tyr Ser Trp Leu Thr His Gin He Ser Arg Ala Trp Arg Xaa Cys Trp 1045 1050 1055 ACT CCT TAG CTC THG CTG AGG AGC GGC TGG CCT GCT CTT GGC TGG TGG 3216 Thr Pro * Leu Xaa Leu Arg Ser Gly Trp Pro Ala Leu Gly Trp Trp 1060 1065 1070 GCG TCC TGC GCA AGC GGG GCG TCC TCC TCT ACG AGC ACG CYG GTC ACA 3264 Ala Ser Cys Ala Ser Gly Ala Ser Ser Ser Thr Ser Thr Xaa Val Thr 1075 1080 1085 CTA GCA GGC GCG GTG CTG CCC GCT TGC GAG AGT GGG GYT TTG CGC TYG 3312 Leu Ala Gly Ala Val Leu Pro Ala Cys Glu Ser Gly Xaa Leu Arg Xaa 1090 1095 1100 AGC CKG TTA GYA TAA CCA AGG AAG ATT GYG CYA TTG TTC GGG ACT CTG 3360 Ser Xaa Leu Xaa * Pro Arg Lys He Xaa Xaa Leu Phe Gly Thr Leu 1105 1110 1115 1120 CTC GTG TGT TGG GCT GTG GAC AAT TGG TCC ATG GGA AAC CAG TGG TCG 3408 Leu Val Cys Trp Ala Val Asp Aβn Trp Ser Met Gly Aβn Gin Trp Ser 1125 1130 1135 CGA GGC GAG GCG ACG AGG TGT TGA TCG GCT GTG TGA ACA GTC GGT TCG 3456 Arg Gly Glu Ala Thr Arg Cye * Ser Ala Val * Thr Val Gly Ser 1140 1145 1150 ACC TTC CGC CTG GCT TTG TTC CCA CTG CTC CCG TGG TSC TTC ATC ARG 3504 Thr Phe Arg Leu Ala Leu Phe Pro Leu Leu Pro Trp Xaa Phe He Xaa 1155 1160 1165 CWG GCA ARG GRT TYT TYG GGG TTG TGA AGA CMT CCA TGA CAG GCA AGG 3552 Xaa Ala Xaa Xaa Xaa Xaa Gly Leu * Arg Xaa Pro * Gin Ala Arg 1170 1175 1180 ACC CGT CCG AAC ACC ACG GRA ACG TGG TGG TCC TWG GGA CTT CAA CAA 3600 Thr Arg Pro Aβn Thr Thr Xaa Thr Trp Trp Ser Xaa Gly Leu Gin Gin 1185 1190 1195 1200 CKC GTT CCA TGG GCT GCT GCG TGA ACG GAG TAG TGT ACA CRA CAT ACC 3648 Xaa Val Pro Trp Ala Ala Ala * Thr Glu * Cye Thr Xaa His Thr 1205 1210 1215 ATG GYA CCA ACG CCC GRC CKA TGG CGG GGC CKT TTG GKC CYG TCA AYG 3696 Met Xaa Pro Thr Pro Xaa Xaa Trp Arg Gly Xaa Leu Xaa Xaa Ser Xaa 1220 1225 1230 CTC GGT GGT GGT CWG CGA GYG ACG ACG TCA CGG TYT ACC CGC TCC CWA 3744 Leu Gly Gly Gly Xaa Arg Xaa Thr Thr Ser Arg Xaa Thr Arg Ser Xaa 1235 1240 1245 ATG GYG CTT CTT GCC TYC ARG CWT GYA AGT GCC AAC CAA CTG GGG TGT 3792 Met Xaa Leu Leu Ala Xaa Xaa Xaa Xaa Ser Ala Asn Gin Leu Gly Cys 1250 1255 1260 GGG TGA TCC GGA ATG ACG GAG CTC TTT GCC ATG GAA CTC TCG GCA AGG 3840 Gly * Ser Gly Met Thr Glu Leu Phe Ala Met Glu Leu Ser Ala Arg 1265 1270 1275 1280 TGG TGG ATT TAG ATA TGC CCG CTG AGT TGT CAG ACT TTC GCG GGT CTT 3888 Trp Trp He * He Cys Pro Leu Ser Cyβ Gin Thr Phe Ala Gly Leu 1285 1290 1295 CTG GAT CAC CAA TCT TGT GCG ATG AGG GTC ATG CTG TTG GCA TGC TGA 3936 Leu Aep Hie Gin Ser Cye Ala Met Arg Val Met Leu Leu Ala Cyβ * 1300 1305 1310 TTT CGG TGC TTC ATA GGG GGA GTA GGG TTT CCT CGG TGC GGT ATA CCA 3984 Phe Arg Cys Phe He Gly Gly Val Gly Phe Pro Arg Cys Gly He Pro 1315 1320 1325 AAC CTT GGG AAA CTC TCC CTC GGG AGA TTG AGG CTC GAT CGG AGG CCC 4032 Asn Leu Gly Lys Leu Ser Leu Gly Arg Leu Arg Leu Aep Arg Arg Pro 1330 1335 1340 CCC CTG TGC CAG GAA CCA CTG GAT ACA GGG AGG CGC CAC TGT TCC TGC 4080 Pro Leu Cys Gin Glu Pro Leu Asp Thr Gly Arg Arg His Cye Ser Cyβ 1345 1350 1355 1360 CCA CCG GAG CTG GCA AGT CGA CGC GCG TGC CGA ATG AGT ACG TCA AGG 4128 Pro Pro Glu Leu Ala Ser Arg Arg Ala Cye Arg Met Ser Thr Ser Arg 1365 1370 1375 CTG GAC ACA ARG TGC TTG TAC TAA ACC CAT CCA TTG CCA CAG TGA GGG 4176 Leu Aep Thr Xaa Cyβ Leu Tyr * Thr Hie Pro Leu Pro Gin * Gly 1380 1385 1390 CCA TGG GCC CTT ACA TGG AAA AGT TAA CCG GCA AAC ATC CGT CGG TGT 4224 Pro Trp Ala Leu Thr Trp Lye Ser * Pro Ala Aβn He Arg Arg Cys__ 1395 1400 1405 ACT GTG GCC ATG ACA CTA CTG CAT ATT CCA GGA CTA CTG ACT CAT CTT 4272 Thr Val Ala Met Thr Leu Leu His He Pro Gly Leu Leu Thr His Leu 1410 1415 1420 TGA CCT ACT GTA CAT ACG GCA GGT TTA TGG CCA ATC CCA GGA AAT ACT 4320 * Pro Thr Val His Thr Ala Gly Leu Trp Pro He Pro Gly Aen Thr 1425 1430 1435 1440 TGC GGG GGA ACG ACG TCG TAA TTT GCG ACG AGT TGC ACG TCA CCG ACC 4368 Cyβ Gly Gly Thr Thr Ser * Phe Ala Thr Ser Cyβ Thr Ser Pro Thr 1445 1450 1455 CGA CCT CAA TTT TGG GGA TGG GTC GGG CGA GGT TAC TCG CTC GCG AGT 4416 Arg Pro Gin Phe Trp Gly Trp Val Gly Arg Gly Tyr Ser Leu Ala Ser 1460 1465 1470 GCG GCG TAC GCC TCC TGC TTT TCG CTA CGG CGA CCC CAC CGG TCT CTC 4464 Ala Ala Tyr Ala Ser Cys Phe Ser Leu Arg Arg Pro His Arg Ser Leu 1475 1480 1485 CGA TGG CGA AGC ATG AAT CTA TTC ATG AGG AGA TGT TGG GCA GTG AGG 4512 Arg Trp Arg Ser Met Asn Leu Phe Met Arg Arg Cyβ Trp Ala Val Arg 1490 1495 1500 GGG AGG TCC CCT TCT ATT GCC AAT TCC TCC CAC TGA GTA GGT ATG CTA 4560 Gly Arg Ser Pro Ser He Ala Aβn Ser Ser Hie * Val Gly Met Leu 1505 1510 1515 1520 CTG GGA GAC ACC TGC TGT TTT GTC ATT CCA AGG TAG ART GCA CTA GGT 4608 Leu Gly Aep Thr Cyβ Cys Phe Val He Pro Arg * Xaa Ala Leu Gly 1525 1530 1535 TAT CCT CAG CTT TGG CCA GCT TTG GTG TCA ACA CCG TTG TGT ACT TCA 4656 Tyr Pro Gin Leu Trp Pro Ala Leu Val Ser Thr Pro Leu Cyβ Thr Ser 1540 1545 1550 GAG GCA AAG AAA CTG ACA TTC CAA CTG GTG ACG TGT GCG TTT GCG CCA 4704 Glu Ala Lys Lys Leu Thr Phe Gin Leu Val Thr Cys Ala Phe Ala Pro 1555 1560 1565 CAG ACG CAC TTT CCA CTG GTT ACA CTG GCA ATT TTG ACA CCG TAA CAG 4752 Gin Thr Hie Phe Pro Leu Val Thr Leu Ala He Leu Thr Pro * Gin 1570 1575 1580 ACT GTG GTT TAA TGG TTG AGG AGG TAG TGG AAG TGA CCC TGG ACC CGA 4800 Thr Val Val * Trp Leu Arg Arg * Trp Lye * Pro Trp Thr Arg 1585 1590 1595 1600 CCA TCA CTA TCG GTG TGA AGA CCG TCC CGG CCC CTG CCG AAC TGA GGG 4848 P o Ser Leu Ser Val * Arg Pro Ser Arg Pro Leu Pro Asn * Gly 1605 1610 1615 CTC AGA GGC GTG GTA GGT GTG GCC GTG GGA AAG CGG GCA, CTT ACT ATC 4896 Leu Arg Gly Val Val Gly Val Ala Val Gly Lys Arg Ala Leu Thr He 1620 1625 1630 AGG CAT TGA TGT CTT CGG CGC CGG CGG GAA CSG TTC GGT CTG GGG CTC 4944 Arg Hie * Cys Leu Arg Arg Arg Arg Glu Xaa Phe Gly Leu Gly Leu 1635 1640 1645 TCT GGG CAG CTG TTG AGG CTG GHG TCT CGT GGT ATG GCC TAG AGC CCG 4992 Ser Gly Gin Leu Leu Arg Leu Xaa Ser Arg Gly Met Ala * Ser Pro 1650 1655 1660 ATG CTA TTG GAG ACC TGC TTA GGG CCT ACG ACT CGT GTC CTT ATA CTG 5040 Met Leu Leu Glu Thr Cys Leu Gly Pro Thr Thr Arg Val Leu He Leu 1665 1670 1675 1680 CTG CCA TCA GTG CGT CCA TCG GAG AGG CCA TTG CCT TTT TTA CTG GYC 5088 Leu Pro Ser Val Arg Pro Ser Glu Arg Pro Leu Pro Phe Leu Leu Xaa 1685 1690 1695 TAG TGC CAA TGA GGA ATT ATC CTC AGG TGG TTT GGG CCA AGC AGA AGG 5136 * Cys Gin * Gly He He Leu Arg Trp Phe Gly Pro Ser Arg Arg 1700 1705 1710 GRC ACA ACT GGC CAC TCT TGG TGG GTG TGC AGA GGC ACA TGT GTG AGG 5184 Xaa Thr Thr Gly His Ser Trp Trp Val Cys Arg Gly Thr Cye Val Arg 1715 1720 1725 ACG CGG GCT GTG GTC CKC CCG CTA ATG GTC CCG AAT GGA GCG GCA TCA 5232 Thr Arg Ala Val Val Xaa Pro Leu Met Val Pro Asn Gly Ala Ala Ser 1730 1735 1740 GGG GAA AAG GGC CTG TTC CCC TGT TGT GCC GAT GGG GTG GTG ACT TGC 5280 Gly Glu Lys Gly Leu Phe Pro Cys Cye Ala Aep Gly Val Val Thr Cys 1745 1750 1755 1760 CTG AGT CGG TGG CTC CGC ATC ACT GGG TTG ATG ACC TAC AGG CCC GGC 5328 Leu Ser Arg Trp Leu Arg He Thr Gly Leu Met Thr Tyr Arg Pro Gly 1765 1770 1775 TCG GTG TGG CCG AGG GTT ACA CTC CCT GCA TTG CTG GAC CGG TGC TTT 5376 Ser Val Trp Pro Arg Val Thr Leu Pro Ala Leu Leu Asp Arg Cys Phe 1780 1785 1790 TGG TCG GTT TGG CGA TGG CGG GGG GGG CTA TCC TGG CAC ACT GGA CGG 5424 Trp Ser Val Trp Arg Trp Arg Gly Gly Leu Ser Trp His Thr Gly Arg 1795 1800 1805 GGT CTC TGG TTG TAG TGA CCA GTT GGG TTG TCA ATG GGA ACG GTA ACC 5472 Gly Leu Trp Leu * * Pro Val Gly Leu Ser Met Gly Thr Val Thr 1810 1815 1820 CGC TGA TAC AAA GCG CCT CTA GGG GCG TGG CKA CYA GCG GTC CAT ACC 5520 Arg * Tyr Lys Ala Pro Leu Gly Ala Trp Xaa Xaa Ala Val His Thr 1825 1830 1835 1840 CAG TAC CCC CAG ATG GTG GTG AAC GGT ACC CAT CAG ACA TCA AGC CAA 5568 Gin Tyr Pro Gin Met Val Val Asn Gly Thr His Gin Thr Ser Ser Gin 1845 1850 1855 TYA CTG AGG CTG TGA CCA CCC TTG AGA CTG CGT GCG GYT GGG GCC CAG 5616. Xaa Leu Arg Leu * Pro Pro Leu Arg Leu Arg Ala Xaa Gly Ala Gin 1860 1865 1870 CCG CGG CBA GTC TGG CTT ATG TGA AGG CCT GTG AAA CTG GAA CCA TGT 5664 Pro Arg Xaa Val Trp Leu Met * Arg Pro Val Lye Leu Glu Pro Cye 1875 1880 1885 TGG CTG ACA ARG CGA GTG CTG CGT GGC AGG CTT GGG CTG CAA ACA ACT 5712 Trp Leu Thr Xaa Arg Val Leu Arg Gly Arg Leu Gly Leu Gin Thr Thr 1890 1895 1900 TTG TGC CTC CAC CAG CAT CAC ACT CAA CTT CCT TGT TRC AGA GCT TGG 5760 Leu Cys Leu Hie Gin Hie Hie Thr Gin Leu Pro Cys Xaa Arg Ala Trp 1905 1910 1915 1920 AYG CTG CGT TCA CTT CAG CTT GGG ATA GCG TGT TCA CTC ACG GCC GTT 5808 Xaa Leu Arg Ser Leu Gin Leu Gly He Ala Cys Ser Leu Thr Ala Val 1925 1930 1935 CCT TGC TTG TTG GGT TCA CAG CTG CTT ACG GCG CTC GGC GGA ACC CAC 5856 Pro Cye Leu Leu Gly Ser Gin Leu Leu Thr Ala Leu Gly Gly Thr His 1940 1945 1950 CGC TGG GCG TCG GAG CCT CTT TCT TGC TGG GCA TGT CAT CGA GCC ACY 5904 Arg Trp Ala Ser Glu Pro Leu Ser Cys Trp Ala Cye Hie Arg Ala Xaa 1955 1960 1965 TRA CTC ACG TCA GAC TTG CTG CTG CGT TGC TCC TCG GCG TCG GGG GTA 5952 Xaa Leu Thr Ser Aep Leu Leu Leu Arg Cys Ser Ser Ala Ser Gly Val 1970 1975 1980 CCG TCC TAG GCA CGC CTG CTA CTG GGC TTG CTA TGG CGG GTG CCT ACT 6000 Pro Ser * Ala Arg Leu Leu Leu Gly Leu Leu Trp Arg Val Pro Thr 1985 1990 1995 2000 TCG CKG GGG GCA GCG TTA CCG CTA ACT GGC TGA GTA TCA TTG TGG CTC 6048 Ser Xaa Gly Ala Ala Leu Pro Leu Thr Gly * Val Ser Leu Trp Leu 2005 2010 2015 TAA TCG GAG GCT GGG AGG GGG CRG TKA ACG CAG CCT CAC TCA CCT TCG 6096 * Ser Glu Ala Gly Arg Gly Xaa Xaa Thr Gin Pro His Ser Pro Ser 2020 2025 2030 AYC TCC TGG CKG GGA AGT TAC AAG CKA GYG AYG CTT GGT GCC TRG TCA 6144 Xaa Ser Trp Xaa Gly Ser Tyr Lys Xaa Xaa Xaa Leu Gly Ala Xaa Ser 2035 2040 2045 GYT GCY TGG CCT CTC CGG GGG CTT CGG TGG CYG GTG TGG CDC TVG GYC 6192 Xaa Xaa Trp Pro Leu Arg Gly Leu Arg Trp Xaa Val Trp Xaa Xaa Xaa 2050 2055 2060 TDY TGC TVT GGT CTG TCA ARA AGG GTG TGG GWC ARG AYT GGG TTA ACA 6240 Xaa Cys Xaa Gly Leu Ser Xaa Arg Val Trp Xaa Xaa Xaa Gly Leu Thr 2065 2070 2075 2080 GAY TGT TGA CGA TGA TGC CAC GCA GTT CGG TGA TGC CTG ACG ATT TCT 6288 Xaa Cys * Arg * Cys His Ala Val Arg * Cys Leu Thr He Ser 2085 2090 2095 TCC TCA AAG ATG AGT TCG TCA CCA AGG TGT CTA CTG TCC TGC GAA AGT 6336 Ser Ser Lys Met Ser Ser Ser Pro Arg Cys Leu Leu Ser Cys Glu Ser 2100 2105 2110 TGT CAT TGT CAA GAT GGA TCA TGA CTC TTG TGG ACA AGC GGG AGA TGG 6384 Cys His Cys Gin Asp Gly Ser * Leu Leu Trp Thr Ser Gly Arg Trp 2115 2120 2125 AGA TGG AGA CMC CCG CTT CTC AGA TTG TTT GGG ACT TGC TTG ACT GGT 6432 Arg Trp Arg Xaa Pro Leu Leu Arg Leu Phe Gly Thr Cys Leu Thr Gly 2130 2135 2140 GCA TCC GGC TRG GTC GGT TCC TGT ACA ATA AAC TYA TGT TTG CTC TCC 6480 Ala Ser Gly Xaa Val Gly Ser Cys Thr He Asn Xaa Cys Leu Leu Ser 2145 2150 2155 2160 CTA GGT TGC GCC TGC CGC TTA TCG GTT GCA GTA CCG GTT GGG GTG GCC 6528 Leu Gly Cys Ala Cys Arg Leu Ser Val Ala Val Pro Val Gly Val Ala 2165 2170 2175 CGT GGG AGG GCA ATG GTC ATT TGG AAA CAA GGT GTA CTT GTG GCT GTG 6576 Arg Gly Arg Ala Met Val He Trp Lys Gin Gly Val Leu Val Ala Val 2180 2185 2190 TGA TTA CCG GTG ATA TTC ACG ATG GTA TAT TGC ACG ACC TAC ATT ATA 6624 * Leu Pro Val He Phe Thr Met Val Tyr Cys Thr Thr Tyr He He 2195 2200 2205 CCT CCC TAC TGT GCA GAC ATT ACT ACA AGA GGA CAG TGC CTG TTG GCG 6672 Pro Pro Tyr Cys Ala Asp He Thr Thr Arg Gly Gin Cys Leu Leu Ala 2210 2215 2220 TCA TGG GCA ATG CTG AGG GAG CAG TCC CCC TTG TGC CTA CTG GCG GTG 6720 Ser Trp Ala Met Leu Arg Glu Gin Ser Pro Leu Cys Leu Leu Ala Val 2225 2230 2235 2240 GAA TCA GGA CTT ACC AAA TTG GGA CTT CTG ACT GGT TTG AGG CTG TGG 6768 Glu Ser Gly Leu Thr Lys Leu Gly Leu Leu Thr Gly Leu Arg Leu Trp 2245 2250 2255 TCG TGC ATG GGA CAA TCA CGG TGC ACG CCA CCA GTT GCT ATG AGT TGA 6816 Ser Cys Met Gly Gin Ser Arg Cye Thr Pro Pro Val Ala Met Ser * 2260 2265 2270 AAG CTG CTG ACG TTC GGA GGG CGG TGC GAG CCG GCC CGA CTT ACG TTG 6864 Lys Leu Leu Thr Phe Gly Gly Arg Cye Glu Pro Ala Arg Leu Thr Leu 2275 2280 2285 GTG GCG TAC CTT GCA GCT GGA GCG CGC CGT GTA CTG CGC CTG CGC TCG 6912 Val Ala Tyr Leu Ala Ala Gly Ala Arg Arg Val Leu Arg Leu Arg Ser 2290 2295 2300 TTT ACA GGC TAG GCC AGG GCA TCA AAA TCG ATG GAG CGC GCC GAC TGT 6960 Phe Thr Gly * Ala Arg Ala Ser Lye Ser Met Glu Arg Ala Aep Cys 2305 2310 2315 2320 TGC CCT GTG ACT TAG CAC AGG GAG CGC GCC ACC CCC CGG TAT CTG GCA 7008 Cyβ Pro Val Thr * Hie Arg Glu Arg Ala Thr Pro Arg Tyr Leu Ala 2325 2330 2335 GTG TTG CCG GTA GTG GTT GGA CAG ATG AGG ACG AGA GGG ACT TGG TGG 7056 Val Leu Pro Val Val Val Gly Gin Met Arg Thr Arg Gly Thr Trp Trp 2340 2345 2350 AAA CCA AGG CTG CCG CCA TCG AGG CCA TTG GGG CGG CCT TGC ACC TCC 7104 Lys Pro Arg Leu Pro Pro Ser Arg Pro Leu Gly Arg Pro Cys Thr Ser 2355 2360 2365 CTT CAC CGG AGG CTG CTC AGG CCG CTC TAG AGG CTT TGG AGG AGG CTG 7152 Leu Hie Arg Arg Leu Leu Arg Pro Leu * Arg Leu Trp Arg Arg Leu 2370 2375 2380 CCG TGT CCC TGT TGC CCC ATG TGC CCG TCA TTA TGG GTG ATG ACT GTT 7200 Pro Cyβ Pro Cyβ Cys Pro Met Cys Pro Ser Leu Trp Val Met Thr Val 2385 2390 2395 2400 CAT GCC GGG ATG AGG CGT TCC AAG GCC ACT TCA TCC CAG AAC CCA ATG 7248 Hie Ala Gly Met Arg Arg Ser Lye Ala Thr Ser Ser Gin Asn Pro Met 2405 2410 2415 TGA CAG AGG TAC CCA TTG AGC CCA CGG TCG GAG ACG TGG AGG CAC TCA 7296 * Gin Arg Tyr Pro Leu Ser Pro Arg Ser Glu Thr Trp Arg His Ser 2420 2425 2430 AGC TGC GGG CTG CAG ACC TGA CCG CCA GGT TGC AAG ACT TGG AGG CCA 7344 Ser Cys Gly Leu Gin Thr * Pro Pro Gly Cys Lys Thr Trp Arg Pro 2435 2440 2445 TGG CTC TCG CCC GCG CTG AGT CAA TCG AGG ATG CTC GCG CAG CTT CGA 7392 Trp Leu Ser Pro Ala Leu Ser Gin Ser Arg Met Leu Ala Gin Leu Arg 2450 2455 2460 TGC CTT CGC TCA CCG AGG TGG ACT CAA TGC CAT CAT TGG AGT CGA GCC 7440 Cyβ Leu Arg Ser Pro Arg Trp Thr Gin Cyβ Hie His Trp Ser Arg Ala 2465 2470 2475 2480 CTT GCT CCT CCT TTG AAC AAA TCT CTT TAA CTG AAA GTG ACC CTG AGA 7488 Leu Ala Pro Pro Leu Asn Lys Ser Leu * Leu Lys Val Thr Leu Arg 2485 2490 2495 CTG TCG TCG AGG CTG GCT TAC CCT TGG AGT TCG TGA ACT CCA ACA CCG 7536 Leu Ser Ser Arg Leu Ala Tyr Pro Trp Ser Ser * Thr Pro Thr Pro 2500 2505 2510 GGC CGT CTC CGG CTC GGA GGA TTG TCA GAA TCC GAC AGG CTT GCT GTT 7584 Gly Arg Leu Arg Leu Gly Gly Leu Ser Glu Ser Asp Arg Leu Ala Val 2515 2520 2525 GTG ACA GAT CCA CAA TGA AGG CCA TGC CGT TGT CGT TCA CTG TCG GGG 7632 Val Thr Asp Pro Gin * Arg Pro Cyβ Arg Cyβ Arg Ser Leu Ser Gly 2530 2535 2540 AGT GCC TCT TCG TTA CTC GCT ATG ACC CGG ACG GTC ACC AAC TGT TTG 7680 Ser Ala Ser Ser Leu Leu Ala Met Thr Arg Thr Val Thr Aβn Cys Leu 2545 2550 2555 2560 ACG AGC GAG GTC CGA TAG AGG TAT CTA CTC CTA TAT GTG AAG TGA TTG 7728 Thr Ser Glu Val Arg * Arg Tyr Leu Leu Leu Tyr Val Lys * Leu 2565 2570 2575 GGG ACA TCA GGC TTC AGT GTG ACC AAA TTG AGG AAA CTC CAA CAT CTT 7776 Gly Thr Ser Gly Phe Ser Val Thr Lys Leu Arg Lys Leu Gin His Leu 2580 2585 2590 ACT CTT ACA TCT GGT CAG GGG CGC CCT TGG GTA CTG GGA GAA GTG TCC 7824 Thr Leu Thr Ser Gly Gin Gly Arg Pro Trp Val Leu Gly Glu Val Ser 2595 2600 2605 CCC AAC CCA TGA CGC GCC CTA TAG GGA CCC ATC TGA CTT GTG ACA CTA 7872 Pro Aβn Pro * Arg Ala Leu * Gly Pro He * Leu Val Thr Leu 2610 2615 2620 CCA AAG TTT ATG TTA CTG ACC CTG ATC GGG CCG CTG AGC GGG CCG AGA 7920 Pro Lye Phe Met Leu Leu Thr Leu He Gly Pro Leu Ser Gly Pro Arg 2625 2630 2635 2640 AGG TTA CAA TCT GGA GGG GTG ATA GGA AGT ATG ACA AGC ATT ATG AGG 7968 Arg Leu Gin Ser Gly Gly Val He Gly Ser Met Thr Ser He Met Arg 2645 2650 2655 CTG TCG TTG AGG CTG TCC TGA AAA AGG CAG CCG CGA CGA AGT CTC ATG 8016 Leu Ser Leu Arg Leu Ser * Lys Arg Gin Pro Arg Arg Ser Leu Met 2660 2665 2670 GCT GGA CCT ATT CCC AGG CTA TAG CTA AAG TTA GGC GCC GAG CAG CCG 8064 Ala Gly Pro He Pro Arg Leu * Leu Lys Leu Gly Ala Glu Gin Pro 2675 2680 2685 CTG GAT ACG GCA GCA AGG TGA CCG CCT CCA CAT TGG CCA CTG GTT GGC 8112 Leu Aep Thr Ala Ala Arg * Pro Pro Pro His Trp Pro Leu Val Gly 2690 2695 2700 CTC ACG TGG AGG AGA TGC TGG ACA AAA TAG CCA GGG GAC AGG AAG TTC 8160 Leu Thr Trp Arg Arg Cys Trp Thr Lye * Pro Gly Aep Arg Lye Phe 2705 2710 2715 2720 CTT TCA CTT TTG TGA CCA AGC GAG AGG TTT TCT TCT CCA AAA CTA CCC 8208 Leu Ser Leu Leu * Pro Ser Glu Arg Phe Ser Ser Pro Lys Leu Pro 2725 2730 2735 GTA AGC CCC CAA GAT TCA TAG TTT TCC CAC CTT TGG ACT TCA GGA TAG 8256 Val Ser Pro Gin Aep Ser * Phe Ser Hie Leu Trp Thr Ser Gly * 2740 2745 2750 CTG AAA AGA TGA TTC TGG GTG ACC CCG GCA TCG TTG CAA AGT CAA TTC 8304 Leu Lys Arg * Phe Trp Val Thr Pro Ala Ser Leu Gin Ser Gin Phe 2755 2760 2765 TGG GTG ACG CTT ATC TGT TCC AGT ACA CGC CCA ATC AGA GGG TCA AAG 8352 Trp Val Thr Leu He Cys Ser Ser Thr Arg Pro He Arg Gly Ser Lys 2770 2775 2780 CTC TGG TTA AGG CGT GGG AGG GGA AGT TGC ATC CCG CTG CGA TCA CTG 8400 Leu Trp Leu Arg Arg Gly Arg Gly Ser Cys He Pro Leu Arg Ser Leu 2785 2790 2795 2800 TGG ACG CCA CTT GTT TCG ACT CAT CGA TTG ATG AGC ACG ACA TGC AGG 8448 Trp Thr Pro Leu Val Ser Thr His Arg Leu Met Ser Thr Thr Cys Arg 2805 2810 2815 TGG AGG CTT CGG TGT TTG CGG CGG CTA GTG ACA ACC CCT CAA TGG TAC 8496 Trp Arg Leu Arg Cys Leu Arg Arg Leu Val Thr Thr Pro Gin Trp Tyr 2820 2825 2830 ATG CTT TGT GCA AGT ACT ACT CTG GTG GCC CTA TGG TTT CCC CAG ATG 8544 Met Leu Cys Ala Ser Thr Thr Leu Val Ala Leu Trp Phe Pro Gin Met 2835 2840 2845 GGG TTC CCT TGG GGT ACC GCC AGT GTA GGT CGT CGG GCG TGT TAA CAA 8592 Gly Phe Pro Trp Gly Thr Ala Ser Val Gly Arg Arg Ala Cys * Gin 2850 2855 2860 CTA GCT CGG CGA ACA GCA TCA CTT GTT ACA TTA AGG TCA GCG CGG CCT 8640 Leu Ala Arg Arg Thr Ala Ser Leu Val Thr Leu Arg Ser Ala Arg Pro 2865 2870 2875 2880 GCA GGC GGG TGG GGA TTA AGG CAC CAT CAT TCT TTA TAG CTG GAG ATG 8688 Ala Gly Gly Trp Gly Leu Arg His His His Ser Leu * Leu Glu Met 2885 2890 2895 ATT GCT TGA TCA TCT ATG AAA ATG ATG GAA CTG ATC CCT GCC CTG CTC 8736 He Ala * Ser Ser Met Lys Met Met Glu Leu He Pro Ala Leu Leu 2900 2905 2910 TTA AGG CTG CCC TGG CCA ACT ATG GAT ACA GGT GTG AAC CAA CAA AGC 8784 Leu Arg Leu Pro Trp Pro Thr Met Asp Thr Gly Val Asn Gin Gin Ser 2915 2920 2925 ATG CTT CAC TGG ACA CAG CTG AGT GTT GCT CGG CCT ACT TGG CTG AGT 8832 Met Leu His Trp Thr Gin Leu Ser Val Ala Arg Pro Thr Trp Leu Ser 2930 2935 2940 GCG TAG CTG GGG GTG CCA AGC GCT GGT GGT TGA GCA CGG ACA TGA GGA 8880 Ala * Leu Gly Val Pro Ser Ala Gly Gly * Ala Arg Thr * Gly 2945 2950 2955 2960 AGC CGC TCG CAA GGG CGT CTT CCG AAT ATT CGG ACC CAA TCG GCA GTG 8928 Ser Arg Ser Gin Gly Arg Leu Pro Asn He Arg Thr Gin Ser Ala Val 2965 2970 2975 CTT TAG GGA CCA TCT TGA TGT ATC CCC GGC ATC CAA TCG TGC GGT ATG 8976 Leu * Gly Pro Ser * Cys He Pro Gly He Gin Ser Cys Gly Met 2980 2985 2990 TTC TAA TAC CAC ACG TAC TAA TAA TGG CTT ACA GGA GTG GCA GCA CAC 9024 Phe * Tyr His Thr Tyr * * Trp Leu Thr Gly Val Ala Ala His 2995 3000 3005 CGG ATG AGT TGG TTA TGT GTC AGG TTC AGG GAA ATC ATT ACT CTT TCC 9072 Arg Met Ser Trp Leu Cys Val Arg Phe Arg Glu He He Thr Leu Ser 3010 3015 3020 CGC TGC GGC TGC TGC CTC GCG TCT TGG TCT CTC TAC ATG GTC CGT GGT 9120 Arg Cys Gly Cys Cys Leu Ala Ser Trp Ser Leu Tyr Met Val Arg Gly 3025 3030 3035 3040 GCC TAC AAG TCA CCA CGG ACA GTA CGA AGA CTA GGA TGG AGG CAG GCT 9168 Ala Tyr Lys Ser Pro Arg Thr Val Arg Arg Leu Gly Trp Arg Gin Ala 3045 3050 3055 CAG CST TGC GGG ATT TAG GAA TGA AAT CCC TAG CCT GGC ACC GCC GAC 9216 Gin Xaa Cys Gly He * Glu * Asn Pro * Pro Gly Thr Ala Asp 3060 3065 3070 GTG CCG GAA ATG TGC GCA CTC GCC TCC TGA GGG GAG GCA AGG AGT GGG 9264 Val Pro Glu Met Cys Ala Leu Ala Ser * Gly Glu Ala Arg Ser Gly 3075 3080 3085 GGC ACC TGG CCA GAG CCC TCC TCT GGC AYC CAG GKT TGA AGG AGC AYC 9312 Gly Thr Trp Pro Glu Pro Ser Ser Gly Xaa Gin Xaa * Arg Ser Xaa 3090 3095 3100 CCC CRC CCA TAA ATT CAC TTC CAG GTT TTC AGC TGG CGA CGC CTT ACG 9360 Pro Xaa Pro * He His Phe Gin Val Phe Ser Trp Arg Arg Leu Thr 3105 3110 3115 3120 AAC ACC ATG AAG AGG TCT TGA TCT CGA TCA AGA GTC GAC CAC CTT GGA 9408 Asn Thr Met Lys Arg Ser * Ser Arg Ser Arg Val Asp His Leu Gly 3125 3130 3135 TAA GGT GGA TTC TTG GTG CTT GTC TCT CGT TGC TGG CCG CCT TGC TGT 9456 * Gly Gly Phe Leu Val Leu Val Ser Arg Cys Trp Pro Pro Cys Cys 3140 3145 3150 GAA TTC GCT CCA GGC AGT AGG ACC TTC GGG TCG GGG G 9493 Glu Phe Ala Pro Gly Ser Arg Thr Phe Gly Ser Gly 3155 3160 (2) INFORMATION FOR SEQ ID NO:165: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 51 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:165: Arg Gly Ser Pro Gly Pro Arg Thr Ser Hie Arg Gly Gly Gly Lys Gly 1 5 10 15 Ala Leu Asp Arg Pro Gly Gly Arg Pro Gly Thr Gly Pro Ser Ser Ser 20 25 30 Arg Leu Arg Lye Gly Tyr Val Tyr Arg Ser Gly Arg Ser Glu Arg Arg 35 40 45 Leu Aep Ala 50 (2) INFORMATION FOR SEQ ID NO:166: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 5 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:166: Val Val Aen Pro Ser 1 5 (2) INFORMATION FOR SEQ ID NO:167: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:167: Lyε Arg Tyr Arg He Gly Leu Ser Arg 1 5 (2) INFORMATION FOR SEQ ID NO:168: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:168: Pro Leu Pro Arg Asn Gin Pro Arg Xaa Ser Leu Asp Thr Val Hie Arg 1 5 10 15 Leu Gly Val Pro Val 20 (2) INFORMATION FOR SEQ ID NO:169: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 47 amino acide (B) TYPE: amino acid (D) TOPOLOGY: linear ( ii) MOLECULE TYPE : protein (xi) SEQUENCE DESCRIPTION : SEQ ID NO: 169 : He Thr Pro Arg Leu Lys Arg Gin Ser Leu Asn Gly Asp Gly Leu Leu 1 5 10 15 Arg Ser Gin Arg Arg Pro Thr Tyr Gly Asn Ala Ala Lys Thr Phe Gly 20 25 30 Thr Ala Met Arg Val Asp Asn Pro Ser Gly Gly Pro Gly Thr Ser 35 40 45 (2) INFORMATION FOR SEQ ID NO:170: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 40 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:170: Leu Leu Val Leu Arg Val Pro Leu Glu Thr Gly Arg Lys Ala Ala Thr 1 5 10 15 Gly Pro Pro Arg Arg Arg Ser Ala Ala Cys Gly Lys Gly Lys Asn Pro 20 25 25 Ser Gly Asp Pro Trp Trp Gin Ser Leu Pro Leu Gly Ala 30 35 40 (2) INFORMATION FOR SEQ ID NO:171: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 94 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:171: Val Trp Ser Thr His Ser Pro Trp Leu Gly Cys Gly Cye Trp Phe Ala 1 5 10 15 Ser Pro Ser Arg Gly Gly Cyβ Ser Ser Thr Arg Gly Thr Ser Ala Ser 20 25 30 Met Gly Thr He Met Cyβ Phe Pro He Val Val Pro Glu Thr Arg Phe 35 40 45 Thr Ser Val Ser Gly Thr Asp Val Trp Trp Leu Met Ala Val Leu Phe 50 55 60 Ala His Ser Leu Ala Gly Ser Ser Thr Gly Leu Gly Trp Leu Leu Gly 65 70 75 80 Pro Gly Pro Asn Gin Val Ser Cys Trp Gly Asp Leu Gly Val 85 90 (2) INFORMATION FOR SEQ ID NO:172: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 41 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:172: Leu Val Arg Cys Arg Leu Arg Leu Thr Pro Leu Glu Ser Ser Gly Trp 1 5 10 15 Val Asn Leu Thr Val Trp Pro Ser Trp Gly Arg Ser Ser Pro Val Ala 20 25 30 Ser His Gly Phe Pro Thr Ser Pro Ala 35 40 (2) INFORMATION FOR SEQ ID NO:173: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 33 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:173: Arg Leu Val Thr Leu Ser Leu Pro Thr Gin Ala Cys Pro Ser He Leu 1 5 10 15 Thr Gly Arg Leu Pro Arg Ser Cys Ser Cys Arg Pro Ser Cys Gly Glu 20 25 30 Ala (2) INFORMATION FOR SEQ ID NO:174: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 5 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:174: Arg Xaa Xaa Arg Ser 1 5 (2) INFORMATION FOR SEQ ID NO:175: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 10 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:175: Ser Ser Cys Trp Ser Ser Ser Ser Ala Ser 1 5 10 (2) INFORMATION FOR SEQ ID NO:176: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 6 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:176: Pro Ser Tyr Cys Phe Trp 1 5 (2) INFORMATION FOR SEQ ID NO:177: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:177: Trp Ala Arg Leu Arg Gly Gly Cys Ser Thr Thr Ala Cys Val Val Thr 1 5 10 15 Gly Gly Ala Arg Gly Pro Arg Arg 20 (2) INFORMATION FOR SEQ ID NO:178: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 54 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:178: Pro Arg Cys Thr Val Ala Thr Val Leu Trp Cys Val Thr Val He Leu 1 5 10 15 Glu Lys Cys He Gly Pro Pro Pro Cys Val Pro Xaa Trp Cys Gly Gly 20 25 30 Thr Val He Gly Gly Ala Pro Cys Ala Thr Ser Pro Arg Phe Ala Pro 35 40 45 Gly Arg Phe Ser Ala Arg 50 (2) INFORMATION FOR SEQ ID NO:179: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 46 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:179: Gin Ser Cys Val Ser Gly Val Leu Pro Thr Gly Phe Gly Asp Leu Gly 1 5 10 15 Thr Gly Leu Hie Cye Thr Thr Ser Tyr His Aep Gin Leu Ser Val Leu 20 25 30 Ser Ser Gin Val Met Val His Asn Leu Lys He Ser Gin Ser 35 40 45 (2) INFORMATION FOR SEQ ID NO:180: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 16 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:180: He Hie Pro Gly Hie Leu Val Leu Leu Ala Ser Leu Thr Arg Gly Arg 1 5 10 15 (2) INFORMATION FOR SEQ ID NO:181: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 25 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:181: Aen Val Val Pro Ala Ser Ala Thr Ala Gly Arg Arg Gly Val Leu Gly 1 5 10 15 Ser Met Ser Ala Val Ser Val Leu Gly 20 25 (2) INFORMATION FOR SEQ ID NO:182: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 16 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:182: Arg Ser Thr Ser Arg Pro Ser Trp Leu Met Glu Val Trp Ser Pro Arg 1 5 10 15 (2) INFORMATION FOR SEQ ID NO:183: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 10 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:183: Gin Arg Pro Arg Val Ser Ala Pro Asn Thr 1 5 10 (2) INFORMATION FOR SEQ ID NO:184: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 19 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:184: Val Ser Thr Val Trp Glu Pro Thr Thr Ala Leu Ser Val Ala Ser Thr 1 5 10 15 Ser Val Thr (2) INFORMATION FOR SEQ ID NO:185: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:185: Leu Arg Trp Gly Ala He Gly Met Arg 1 5 (2) INFORMATION FOR SEQ ID NO:186: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 19 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:186: Ser Ala Arg Ala Thr Leu Cye Pro Glu Cye Ser Gin Lys Glu Phe Gin 1 5 10 15 Val Gly Leu (2) INFORMATION FOR SEQ ID NO:187: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:187: Met His Val 1 (2) INFORMATION FOR SEQ ID NO:188: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 81 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:188: Leu Gly Ser Leu Arg Thr Arg Ser Gin Val Gly Leu Pro Val Gly Phe 1 5 10 15 Thr Pro Pro Cys Ser Pro Ser Ala Thr Gly Arg Arg Pro Pro Glu Trp 20 25 30 Met Cys Val Leu Gly Leu Leu Ser He Ser Leu Val He Thr Thr Ala 35 40 45 Ser Ser Met Leu Lys Ala Thr Asp Ser Arg Phe Thr Val Val Ser Glu 50 55 60 Gly Leu Arg Arg Leu Gly Cys Leu Leu Thr Trp Ser Trp Pro Cys Trp 65 70 75 80 Trp (2) INFORMATION FOR SEQ ID NO:189: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 18 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION : SEQ ID NO : 189 : Ser Trp Leu Arg Leu Glu Leu Ser Pro Cys Leu Cys Trp Gin Cys Gly 1 5 10 15 Gly Gly (2) INFORMATION FOR SEQ ID NO:190: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 134 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:190: Met Glu His Leu Leu Pro Leu Leu Ser Ser Tyr Thr Leu Leu Ser Arg 1 5 10 15 Ser Pro Leu Lys Val Phe His Cys Gly Leu Arg Pro Leu Phe Gin Leu 20 25 30 His Leu Ala Arg He Leu Pro Pro Glu Ser Arg Thr Leu Pro Thr Met 35 40 45 Leu Val Ala Thr Trp Trp Gin Ala Trp Arg Pro Gly Leu Arg Arg Ser 50 55 60 Gly Val Leu Pro Met Met Val Leu Arg Pro Ser Leu Val Ala Ser Gly 65 70 75 80 Pro Arg Gly Ser Ser Cys Glu Ala Ser Leu Pro Val Trp Pro Gly Cye 85 90 95 Gin Met Leu Gly Leu Thr Cyβ Arg Ser Ser Arg Pro Xaa Trp Leu Pro 100 105 110 Ser Trp Cyβ Ala Pro Arg Trp Ser Ala Gly Gin Pro Arg Ser Gly Gly 115 120 125 Ser Leu Val Val Trp Val 130 (2) INFORMATION FOR SEQ ID NO:191: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 6 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:191: Cys Val Ser Trp Arg Thr 1 5 (2) INFORMATION FOR SEQ ID NO:192: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 26 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:192: Met Ser Trp Ala Leu Xaa Gly Leu Pro Cys Leu Trp Arg Cyβ Thr Ser 1 5 10 15 Gin Gly Val Leu Cye Arg Trp Tyr Trp Trp 20 25 (2) INFORMATION FOR SEQ ID NO:193: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 11 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:193: Leu Pro Gly Xaa Pro Gly Ser Gly Thr Ala Ser 1 5 10 (2) INFORMATION FOR SEQ ID NO:194: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:194: Gly Leu Arg Cys Ala Ser He Trp Met Val Glu Thr Gly Xaa Thr Pro 1 5 10 15 Val Gly Leu Gly Val 20 (2) INFORMATION FOR SEQ ID NO:195: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:195: Ala Gly Pro Ser Trp Trp Gly Val 1 5 (2) INFORMATION FOR SEQ ID NO:196: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:196: Pro Thr Val Ala Aep Gin Pro Xaa 1 5 (2) INFORMATION FOR SEQ ID NO:197: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 16 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:197: Leu Gly Xaa Pro Gly Gly Pro Ser He Xaa Arg Gly Phe Xaa Gly Gly 1 5 10 15 (2) INFORMATION FOR SEQ ID NO:198: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 34 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear ( ii ) MOLECULE TYPE : protein (xi) SEQUENCE DESCRIPTION : SEQ ID NO : 198 : Thr Thr His Arg Leu Glu Xaa Leu Xaa Val Xaa Gly Xaa Pro Gly Lys 1 5 10 15 Xaa Gly Xaa Xaa Trp Leu Gly Ser Ser Pro Arg Gin Leu Pro Gin Xaa 20 25 30 Pro Ser Ser Ser Tyr Ser Val 35 (2) INFORMATION FOR SEQ ID NO:199: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 26 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:199: Met Ser Leu He Ser Ser Trp Xaa Tyr Ser Trp Leu Thr His Gin He 1 5 10 15 Ser Arg Ala Trp Arg Xaa Cyβ Trp Thr Pro 20 25 (2) INFORMATION FOR SEQ ID NO:200: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 45 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:200: Leu Xaa Leu Arg Ser Gly Trp Pro Ala Leu Gly Trp Trp Ala Ser Cys 1 5 10 15 Ala Ser Gly Ala Ser Ser Ser Thr Ser Thr Xaa Val Thr Leu Ala Gly 20 25 30 Ala Val Leu Pro Ala Cye Glu Ser Gly Xaa Leu Arg Xaa 35 40 45 (2) INFORMATION FOR SEQ ID NO:201: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:201: Ser Xaa Leu Xaa 1 (2) INFORMATION FOR SEQ ID NO:202: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 34 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:202: Pro Arg Lys He Xaa Xaa Leu Phe Gly Thr Leu Leu Val Cyβ Trp Ala 1 5 10 15 Val Aep Aen Trp Ser Met Gly Aβn Gin Trp Ser Arg Gly Glu Ala Thr 20 25 30 Arg Cys (2) INFORMATION FOR SEQ ID NO:203: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 28 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:203: Thr Val Gly Ser Thr Phe Arg Leu Ala Leu Phe Pro Leu Leu Pro Trp 1 5 10 15 Xaa Phe He Xaa Xaa Ala Xaa Xaa Xaa Xaa Gly Leu 20 25 (2) INFORMATION FOR SEQ ID NO:204: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 26 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:204: Gin Ala Arg Thr Arg Pro Aβn Thr Thr Xaa Thr Trp Trp Ser Xaa Gly 1 5 10 15 Leu Gin Gin Xaa Val Pro Trp Ala Ala Ala 20 25 (2) INFORMATION FOR SEQ ID NO:205: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 54 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:205: Cys Thr Xaa His Thr Met Xaa Pro Thr Pro Xaa Xaa Trp Arg Gly Xaa 1 5 10 15 Leu Xaa Xaa Ser Xaa Leu Gly Gly Gly Xaa Arg Xaa Thr Thr Ser Arg 20 25 30 Xaa Thr Arg Ser Xaa Met Xaa Leu Leu Ala Xaa Xaa Xaa Xaa Ser Ala 35 40 45 50 (2) INFORMATION FOR SEQ ID NO:206: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 17 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:206: Ser Gly Met Thr Glu Leu Phe Ala Met Glu Leu Ser Ala Arg Trp Trp 1 5 10 15 He (2) INFORMATION FOR SEQ ID NO:207: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 27 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:207: He Cys Pro Leu Ser Cys Gin Thr Phe Ala Gly Leu Leu Asp His Gin 1 5 10 15 Ser Cye Ala Met Arg Val Met Leu Leu Ala Cys 20 25 (2) INFORMATION FOR SEQ ID NO:208: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 71 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:208: Phe Arg Cyβ Phe He Gly Gly Val Gly Phe Pro Arg Cys Gly He Pro 1 5 10 15 Aen Leu Gly Lye Leu Ser Leu Gly Arg Leu Arg Leu Aep Arg Arg Pro 20 25 30 Pro Leu Cyβ Gin Glu Pro Leu Aep Thr Gly Arg Arg Hie Cys Ser Cye 35 40 45 Pro Pro Glu Leu Ala Ser Arg Arg Ala Cyβ Arg Met Ser Thr Ser Arg 50 55 60 Leu Asp Thr Xaa Cys Leu Tyr 65 70 (2) INFORMATION FOR SEQ ID NO:209: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 6 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:209: Thr His Pro Leu Pro Gin 1 5 (2) INFORMATION FOR SEQ ID NO:210: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:210: Gly Pro Trp Ala Leu Thr Trp Lye Ser 1 5 (2) INFORMATION FOR SEQ ID NO:211: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 23 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:211: Pro Ala Aen He Arg Arg Cye Thr Val Ala Met Thr Leu Leu Hie He 1 5 10 15 Pro Gly Leu Leu Thr Hiβ Leu 20 (2) INFORMATION FOR SEQ ID NO:212: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:212: Pro Thr Val His Thr Ala Gly Leu Trp Pro He Pro Gly Asn Thr Cys 1 5 10 15 Gly Gly Thr Thr Ser 20 (2) INFORMATION FOR SEQ ID NO:213: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 68 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:213: Phe Ala Thr Ser Cys Thr Ser Pro Thr Arg Pro Gin Phe Trp Gly Trp 1 5 10 15 Val Gly Arg Gly Tyr Ser Leu Ala Ser Ala Ala Tyr Ala Ser Cys Phe 20 25 30 Ser Leu Arg Arg Pro Hie Arg Ser Leu Arg Trp Arg Ser Met Asn Leu 35 40 45 Phe Met Arg Arg Cye Trp Ala Val Arg Gly Arg Ser Pro Ser He Ala 50 55 60 65 (2) INFORMATION FOR SEQ ID NO:214: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 15 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:214: Val Gly Met Leu Leu Gly Asp Thr Cys Cys Phe Val He Pro Arg 1 5 10 15 (2) INFORMATION FOR SEQ ID NO:215: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 50 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:215: Xaa Ala Leu Gly Tyr Pro Gin Leu Trp Pro Ala Leu Val Ser Thr Pro 1 5 10 15 Leu Cyβ Thr Ser Glu Ala Lye Lys Leu Thr Phe Gin Leu Val Thr Cys 20 25 30 Ala Phe Ala Pro Gin Thr His Phe Pro Leu Val Thr Leu Ala He Leu 35 40 45 Thr Pro 50 (2) INFORMATION FOR SEQ ID NO:216: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:216: Gin Thr Val Val 1 (2) INFORMATION FOR SEQ ID NO:217: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:217: Trp Leu Arg Arg 1 (2) INFORMATION FOR SEQ ID NO:218: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:218: Pro Trp Thr Arg Pro Ser Leu Ser Val 1 5 (2) INFORMATION FOR SEQ ID NO:219: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION : SEQ ID NO : 219 : Arg Pro Ser Arg Pro Leu Pro Aβn 1 5 (2) INFORMATION FOR SEQ ID NO:220: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 19 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:220: Gly Leu Arg Gly Val Val Gly Val Ala Val Gly Lye Arg Ala Leu Thr 1 5 10 15 (2) INFORMATION FOR SEQ ID NO:221: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:221: Cye Leu Arg Arg Arg Arg Glu Xaa Phe Gly Leu Gly Leu Ser Gly Gin 1 5 10 15 Leu Leu Arg Leu Xaa Ser Arg Gly Met Ala 20 25 (2) INFORMATION FOR SEQ ID NO:222: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 34 amino acide (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:222: Ser Pro Met Leu Leu Glu Thr Cys Leu Gly Pro Thr Thr Arg Val Leu 1 5 10 15 He Leu Leu Pro Ser Val Arg Pro Ser Glu Arg Pro Leu Pro Phe Leu 20 25 30 Leu Xaa (2) INFORMATION FOR SEQ ID NO:223: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 112 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:223: Gly He He Leu Arg Trp Phe Gly Pro Ser Arg Arg Xaa Thr Thr Gly 1 5 10 15 His Ser Trp Trp Val Cys Arg Gly Thr Cys Val Arg Thr Arg Ala Val 20 25 30 Val Xaa Pro Leu Met Val Pro Asn Gly Ala Ala Ser Gly Glu Lys Gly 35 40 45 Leu Phe Pro Cyβ Cyβ Ala Aep Gly Val Val Thr Cys Leu Ser Arg Trp 50 55 60 Leu Arg He Thr Gly Leu Met Thr Tyr Arg Pro Gly Ser Val Trp Pro 65 70 75 80 Arg Val Thr Leu Pro Ala Leu Leu Asp Arg Cyβ Phe Trp Ser Val Trp 85 90 95 Arg Trp Arg Gly Gly Leu Ser Trp Hiβ Thr Gly Arg Gly Leu Trp Leu 100 105 110 (2) INFORMATION FOR SEQ ID NO:224: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 11 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:224: Pro Val Gly Leu Ser Met Gly Thr Val Thr Arg 10 (2) INFORMATION FOR SEQ ID NO:225: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 34 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:225: Tyr Lys Ala Pro Leu Gly Ala Trp Xaa Xaa Ala Val His Thr Gin Tyr 1 5 10 15 Pro Gin Met Val Val Asn Gly Thr His Gin Thr Ser Ser Gin Xaa Leu 20 25 30 Arg Leu (2) INFORMATION FOR SEQ ID NO:226: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 18 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:226: Pro Pro Leu Arg Leu Arg Ala Xaa Gly Ala Gin Pro Arg Xaa Val Trp 1 5 10 15 Leu Met (2) INFORMATION FOR SEQ ID NO:227: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 106 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:227: Arg Pro Val Lys Leu Glu Pro Cys Trp Leu Thr Xaa Arg Val Leu Arg 1 5 10 15 Gly Arg Leu Gly Leu Gin Thr Thr Leu Cys Leu His Gin His His Thr 20 25 30 Gin Leu Pro Cys Xaa Arg Ala Trp Xaa Leu Arg Ser Leu Gin Leu Gly 35 40 45 He Ala Cys Ser Leu Thr Ala Val Pro Cys Leu Leu Gly Ser Gin Leu 50 55 60 Leu Thr Ala Leu Gly Gly Thr His Arg Trp Ala Ser Glu Pro Leu Ser 65 70 75 80 Cys Trp Ala Cys His Arg Ala Xaa Xaa Leu Thr Ser Aep Leu Leu Leu 85 90 95 Arg Cyβ Ser Ser Ala Ser Gly Val Pro Ser 100 105 (2) INFORMATION FOR SEQ ID NO:228: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 23 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:228: Ala Arg Leu Leu Leu Gly Leu Leu Trp Arg Val Pro Thr Ser Xaa Gly 1 5 10 15 Ala Ala Leu Pro Leu Thr Gly 20 (2) INFORMATION FOR SEQ ID NO:229: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 5 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:229: Val Ser Leu Trp Leu 1 5 (2) INFORMATION FOR SEQ ID NO:230: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 65 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:230: Ser Glu Ala Gly Arg Gly Xaa Xaa Thr Gin Pro His Ser Pro Ser Xaa 1 5 10 15 Ser Trp Xaa Gly Ser Tyr Lys Xaa Xaa Xaa Leu Gly Ala Xaa Ser Xaa 20 25 30 Xaa Trp Pro Leu Arg Gly Leu Arg Trp Xaa Val Trp Xaa Xaa Xaa Xaa 35 40 45 Cys Xaa Gly Leu Ser Xaa Arg Val Trp Xaa Xaa Xaa Gly Leu Thr Xaa 50 55 60 Cys 65 (2) INFORMATION FOR SEQ ID NO:231: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 5 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:231: Cys His Ala Val Arg 1 5 (2) INFORMATION FOR SEQ ID NO:232: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:232: Cye Leu Thr He Ser Ser Ser Lye Met Ser Ser Ser Pro Arg Cyβ Leu 1 5 10 15 20 (2) INFORMATION FOR SEQ ID NO:233: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 7 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:233: Cyβ Hiβ Cyβ Gin Aep Gly Ser 1 5 (2) INFORMATION FOR SEQ ID NO:234: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 72 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:234: Leu Leu Trp Thr Ser Gly Arg Trp Arg Trp Arg Xaa Pro Leu Leu Arg 1 5 10 15 Leu Phe Gly Thr Cyβ Leu Thr Gly Ala Ser Gly Xaa Val Gly Ser Cyβ 20 25 30 Thr He Aβn Xaa Cyβ Leu Leu Ser Leu Gly Cye Ala Cyβ Arg Leu Ser 35 40 45 Val Ala Val Pro Val Gly Val Ala Arg Gly Arg Ala Met Val He Trp 50 55 60 Lye Gin Gly Val Leu Val Ala Val 65 70 (2) INFORMATION FOR SEQ ID NO:235: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 78 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:235: Leu Pro Val He Phe Thr Met Val Tyr Cyβ Thr Thr Tyr He He Pro 10 IS Pro Tyr Cys Ala Asp He Thr Thr Arg Gly Gin Cys Leu Leu Ala Ser 20 25 30 Trp Ala Met Leu Arg Glu Gin Ser Pro Leu Cys Leu Leu Ala Val Glu 35 40 45 Ser Gly Leu Thr Lys Leu Gly Leu Leu Thr Gly Leu Arg Leu Trp Ser 50 55 60 Cys Met Gly Gin Ser Arg Cys Thr Pro Pro Val Ala Met Ser 65 70 75 (2) INFORMATION FOR SEQ ID NO;236: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 35 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:236: Lys Leu Leu Thr Phe Gly Gly Arg Cyβ Glu Pro Ala Arg Leu Thr Leu 1 5 10 15 Val Ala Tyr Leu Ala Ala Gly Ala Arg Arg Val Leu Arg Leu Arg Ser 20 25 30 Phe Thr Gly 35 (2) INFORMATION FOR SEQ ID NO:237: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 16 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:237: Ala Arg Ala Ser Lys Ser Met Glu Arg Ala Aep Cye Cyβ Pro Val Thr 1 5 10 15 (2) INFORMATION FOR SEQ ID NO:238: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 52 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:238: Hiβ Arg Glu Arg Ala Thr Pro Arg Tyr Leu Ala Val Leu Pro Val Val 1 5 10 15 Val Gly Gin Met Arg Thr Arg Gly Thr Trp Trp Lye Pro Arg Leu Pro 20 25 30 Pro Ser Arg Pro Leu Gly Arg Pro Cyβ Thr Ser Leu Hiβ Arg Arg Leu 35 40 45 Leu Arg Pro Leu 50 (2) INFORMATION FOR SEQ ID NO:239: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 38 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:239: Arg Leu Trp Arg Arg Leu Pro Cyβ Pro Cyβ Cyβ Pro Met Cys Pro Ser 1 5 10 15 Leu Trp Val Met Thr Val Hiβ Ala Gly Met Arg Arg Ser Lys Ala Thr 20 25 30 35 (2) INFORMATION FOR SEQ ID NO:240: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:240: Gin Arg Tyr Pro Leu Ser Pro Arg Ser Glu Thr Trp Arg Hiβ Ser Ser 1 5 10 15 Cye Gly Leu Gin Thr 20 (2) INFORMATION FOR SEQ ID NO:241: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 50 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:241: Pro Pro Gly Cys Lys Thr Trp Arg Pro Trp Leu Ser Pro Ala Leu Ser 1 5 10 15 Gin Ser Arg Met Leu Ala Gin Leu Arg Cyβ Leu Arg Ser Pro Arg Trp 20 25 30 Thr Gin Cye Hiβ Hie Trp Ser Arg Ala Leu Ala Pro Pro Leu Aβn Lye 35 40 45 Ser Leu 50 (2) INFORMATION FOR SEQ ID NO:242: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 17 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:242: Leu Lys Val Thr Leu Arg Leu Ser Ser Arg Leu Ala Tyr Pro Trp Ser 1 5 10 15 Ser (2) INFORMATION FOR SEQ ID NO:243: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 25 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:243: Thr Pro Thr Pro Gly Arg Leu Arg Leu Gly Gly Leu Ser Glu Ser Asp 1 5 10 15 Arg Leu Ala Val Val Thr Asp Pro Gin 20 25 (2) INFORMATION FOR SEQ ID NO:244: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:244: Arg Pro Cyβ Arg Cyβ Arg Ser Leu Ser Gly Ser Ala Ser Ser Leu Leu 1 5 10 15 Ala Met Thr Arg Thr Val Thr Aβn Cys Leu Thr Ser Glu Val Arg 20 25 30 (2) INFORMATION FOR SEQ ID NO:245: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:245: Arg Tyr Leu Leu Leu Tyr Val Lys 1 5 (2) INFORMATION FOR SEQ ID NO:246: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 36 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:246: Leu Gly Thr Ser Gly Phe Ser Val Thr Lys Leu Arg Lye Leu Gin Hie 1 5 10 15 Leu Thr Leu Thr Ser Gly Gin Gly Arg Pro Trp Val Leu Gly Glu Val 20 25 30 Ser Pro Asn Pro 35 (2) INFORMATION FOR SEQ ID NO:247: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 42 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:247: Leu Val Thr Leu Pro Lys Phe Met Leu Leu Thr Leu He Gly Pro Leu 1 5 10 15 Ser Gly Pro Arg Arg Leu Gin Ser Gly Gly Val He Gly Ser Met Thr 20 25 30 Ser He Met Arg Leu Ser Leu Arg Leu Ser 35 40 (2) INFORMATION FOR SEQ ID NO:248: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 16 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:248: Lye Arg Gin Pro Arg Arg Ser Leu Met Ala Gly Pro He Pro Arg Leu 1 5 10 15 (2) INFORMATION FOR SEQ ID NO:249: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 14 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:249: Leu Lye Leu Gly Ala Glu Gin Pro Leu Aep Thr Ala Ala Arg 1 5 10 (2) INFORMATION FOR SEQ ID NO:250: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 18 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:250: Pro Pro Pro His Trp Pro Leu Val Gly Leu Thr Trp Arg Arg Cys Trp 1 5 10 15 Thr Lys (2) INFORMATION FOR SEQ ID NO:251: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 10 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:251: Pro Gly Aep Arg Lys Phe Leu Ser Leu Leu 1 5 10 (2) INFORMATION FOR SEQ ID NO:252: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 17 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:252: Pro Ser Glu Arg Phe Ser Ser Pro Lye Leu Pro Val Ser Pro Gin Aep 1 5 10 15 Ser (2) INFORMATION FOR SEQ ID NO:253: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:253: Phe Ser His Leu Trp Thr Ser Gly 1 5 (2) INFORMATION FOR SEQ ID NO:254: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 111 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:254: Phe Trp Val Thr Pro Ala Ser Leu Gin Ser Gin Phe Trp Val Thr Leu 1 5 10 15 He Cys Ser Ser Thr Arg Pro He Arg Gly Ser Lys Leu Trp Leu Arg 20 25 30 Arg Gly Arg Gly Ser Cys He Pro Leu Arg Ser Leu Trp Thr Pro Leu 35 40 45 Val Ser Thr Hiβ Arg Leu Met Ser Thr Thr Cyβ Arg Trp Arg Leu Arg 50 55 60 Cye Leu Arg Arg Leu Val Thr Thr Pro Gin Trp Tyr Met Leu Cys Ala 65 70 75 80 Ser Thr Thr Leu Val Ala Leu Trp Phe Pro Gin Met Gly Phe Pro Trp 85 90 95 Gly Thr Ala Ser Val Gly Arg Arg Ala Cys 100 110 (2) INFORMATION FOR SEQ ID NO:255: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 29 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:255: Gin Leu Ala Arg Arg Thr Ala Ser Leu Val Thr Leu Arg Ser Ala Arg 1 5 10 15 Pro Ala Gly Gly Trp Gly Leu Arg His Hiβ Hie Ser Leu 20 25 (2) INFORMATION FOR SEQ ID NO:256: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 5 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:256: Leu Glu Met He Ala 1 5 (2) INFORMATION FOR SEQ ID NO:257: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 46 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:257: Ser Ser Met Lye Met Met Glu Leu He Pro Ala Leu Leu Leu Arg Leu 1 5 10 15 Pro Trp Pro Thr Met Aep Thr Gly Val Aβn Gin Gin Ser Met Leu Hiβ 20 25 30 Trp Thr Gin Leu Ser Val Ala Arg Pro Thr Trp Leu Ser Ala 35 40 45 (2) INFORMATION FOR SEQ ID NO:258: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:258: Leu Gly Val Pro Ser Ala Gly Gly 1 5 (2) INFORMATION FOR SEQ ID NO:259: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 18 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:259: Gly Ser Arg Ser Gin Gly Arg Leu Pro Asn He Arg Thr Gin Ser Ala 1 5 10 15 Val Leu (2) INFORMATION FOR SEQ ID NO:260: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 10 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:260: Cys He Pro Gly He Gin Ser Cys Gly Met Phe 1 5 10 (2) INFORMATION FOR SEQ ID NO:261: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE : protein (xi) SEQUENCE DESCRIPTION : SEQ ID NO : 261 : Tyr His Thr Tyr 1 (2) INFORMATION FOR SEQ ID NO:262: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 61 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:262: Trp Leu Thr Gly Val Ala Ala His Arg Met Ser Trp Leu Cys Val Arg 1 5 10 15 Phe Arg Glu He He Thr Leu Ser Arg Cys Gly Cys Cys Leu Ala Ser 20 25 30 Trp Ser Leu Tyr Met Val Arg Gly Ala Tyr Lys Ser Pro Arg Thr Val 35 40 45 Arg Arg Leu Gly Trp Arg Gin Ala Gin Xaa Cys Gly He 50 55 60 (2) INFORMATION FOR SEQ ID NO:263: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 14 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:263: Pro Gly Thr Ala Aep Val Pro Glu Met Cye Ala Leu Ala Ser 1 5 10 (2) INFORMATION FOR SEQ ID NO:264: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 18 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE : protein (xi) SEQUENCE DESCRIPTION : SEQ ID NO : 264 : Gly Glu Ala Arg Ser Gly Gly Thr Trp Pro Glu Pro Ser Ser Gly Xaa 1 5 10 15 Gin Xaa (2) INFORMATION FOR SEQ ID NO:265: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 6 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:265: Arg Ser Xaa Pro Xaa Pro 1 5 (2) INFORMATION FOR SEQ ID NO:266: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 18 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:266: He Hie Phe Gin Val Phe Ser Trp Arg Arg Leu Thr Aβn Thr Met Lye 1 5 10 15 Arg Ser (2) INFORMATION FOR SEQ ID NO:267: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:267: Ser Arg Ser Arg Val Aep Hiβ Leu Gly (2) INFORMATION FOR SEQ ID NO:268: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 27 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:268: Gly Gly Phe Leu Val Leu Val Ser Arg Cys Trp Pro Pro Cys Cys Glu 1 5 10 15 Phe Ala Pro Gly Ser Arg Thr Phe Gly Ser Gly 20 25 (2) INFORMATION FOR SEQ ID NO:269: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9493 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 2..9493 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:269: C GTG GGA GTC CGG GGC CCC GGA CCT CCC ACC GAG GTG GGG GGA AAG 46 Val Gly Val Arg Gly Pro Gly Pro Pro Thr Glu Val Gly Gly Lye 1 5 10 15 GGG CCC TGG ACC GGC CGG GTG GAA GGC CCG GAA CCG GTC CAT CTT CCT 94 Gly Pro Trp Thr Gly Arg Val Glu Gly Pro Glu Pro Val Hiβ Leu Pro 20 25 30 CAA GGT TGA GGA AGG GGT ACG TCT ATC GGT CCG GTC GGT CCG AAA GGC 142 Gin Gly * Gly Arg Gly Thr Ser He Gly Pro Val Gly Pro Lys Gly 35 40 45 GTC TGG ATG CCT AGT GTT AGG GTT CGT AGG TGG TAA ATC CCA GCT AGG 190 Val Trp Met Pro Ser Val Arg Val Arg Arg Trp * He Pro Ala Arg 50 55 60 CGT GAA AGC GCT ATA GGA TAG GCT TAT CCC GGT GAC CGC TGC CCC GGA 238 Arg Glu Ser Ala He Gly * Ala Tyr Pro Gly Asp Arg Cys Pro Gly 65 70 75 ACC AGC CCC GCG GKT CTT TGG ACA CGG TCC ACA GGT TGG GGG TAC CGG 286 Thr Ser Pro Ala Xaa Leu Trp Thr Arg Ser Thr Gly Trp Gly Tyr Arg 80 85 90 95 TGT GAA TAA CCC CCC GAC TGA AGC GTC AGT CGT TAA ACG GAG ACG GTC 334 Cys Glu * Pro Pro Asp * Ser Val Ser Arg * Thr Glu Thr Val 100 105 110 TCC TGA GAT CGC AAC GAC GCC CCA CGT ACG GGA ACG CCG CCA AAA CCT 382 Ser * Asp Arg Asn Aep Ala Pro Arg Thr Gly Thr Pro Pro Lys Pro 115 120 125 TCG GGA CAG CTA TGC GGG TTG ACA ATC CCA GTG GGG GGC CGG GGA CCA 430 Ser Gly Gin Leu Cys Gly Leu Thr He Pro Val Gly Gly Arg Gly Pro 130 135 140 GCT GAT TAC TTG TCC TGC GAG TTC CTC TTG AGA CTG GCC GAA AGG CAG 478 Ala Asp Tyr Leu Ser Cys Glu Phe Leu Leu Arg Leu Ala Glu Arg Gin 145 150 155 CCA CGG GGC CAC CAA GGC GGC GCA GCG CTG CAT GCG GCA AGG GGA AAA 526 Pro Arg Gly His Gin Gly Gly Ala Ala Leu Hie Ala Ala Arg Gly Lye 160 165 170 175 ATC CTT CGG GTG ACC CCT GGT GGC AAT CCC TTC CCT TAG GAG CAT GAG 574 He Leu Arg Val Thr Pro Gly Gly Aen Pro Phe Pro * Glu Hie Glu 180 185 190 TGT GGT CGA CAC ATT CAC CAT GGC TTG GCT GTG GTT GCT GGT TTG CTT 622 Cyβ Gly Arg Hiβ He His Hiβ Gly Leu Ala Val Val Ala Gly Leu Leu 195 200 205 CCC CCT CGC GGG GGG GGT GCT CTT CAA CTC GCG GCA CCA GTG CTT CAA 670 Pro Pro Arg Gly Gly Gly Ala Leu Gin Leu Ala Ala Pro Val Leu Gin 210 215 220 TGG GGA CCA TTA TGT GCT TTC CAA TTG TTG TTC CCG AGA CGA GGT TTA 718 Trp Gly Pro Leu Cyβ Ala Phe Gin Leu Leu Phe Pro Arg Arg Gly Leu 225 230 235 CTT CTG TTT CGG GGA CGG ATG TCT GGT GGC TTA TGG CTG TAC TGT TTG 766 Leu Leu Phe Arg Gly Arg Met Ser Gly Gly Leu Trp Leu Tyr Cys Leu 240 245 250 255 CAC ACA GTC TTG CTG GAA GCT CTA CCG GCC TGG GGT GGC TAC TCG GCC 814 His Thr Val Leu Leu Glu Ala Leu Pro Ala Trp Gly Gly Tyr Ser Ala 260 265 270 CGG GTC CGA ACC AGG TGA GCT GCT GGG GAG ATT TGG GAG TGT AAT TGG 862 Arg Val Arg Thr Arg * Ala Ala Gly Glu He Trp Glu Cys Asn Trp 275 280 285 TCC GGT GTC GGC TTC GGC TTA CAC CGC TGG AGT CCT CGG GTT GGG TGA 91TJ Ser Gly Val Gly Phe Gly Leu Hiβ Arg Trp Ser Pro Arg Val Gly * 290 295 300 ACC TTA CAG TTT GGC CTT CTT GGG GAC GTT CCT CAC CAG TCG CCT CTC 958 Thr Leu Gin Phe Gly Leu Leu Gly Aep Val Pro Hiβ Gin Ser Pro Leu 305 310 315 ACG GAT TCC CAA CGT CAC CTG CGT GAA GGC TTG TGA CCT TGA GTT TAC 1006 Thr Asp Ser Gin Arg His Leu Arg Glu Gly Leu * Pro * Val Tyr 320 325 330 335 CTA CCC AGG CTT GTC CAT CGA TTT TGA CTG GGC GTT TAC CAA GAT CTT 1054 Leu Pro Arg Leu Val His Arg Phe * Leu Gly Val Tyr Gin Aep Leu 340 345 350 GCA GTT GCC GGC CAA GCT GTG GCG AGG CCT AAC GGC RGC WCC GGT CTT 1102 Ala Val Ala Gly Gin Ala Val Ala Arg Pro Asn Gly Xaa Xaa Gly Leu 355 360 365 GAG CCT CCT CGT GAT CCT CAT GCT GGT CCT CGA GCA GCG CCT CCT GAT 1150 Glu Pro Pro Arg Aep Pro His Ala Gly Pro Arg Ala Ala Pro Pro Aep 370 375 380 AGC CTT CCT ACT GCT TTT GGT AGT GGG CGA GGC TCA GAG GGG GAT GTT 1198 Ser Leu Pro Thr Ala Phe Gly Ser Gly Arg Gly Ser Glu Gly Aep Val 385 390 395 CGA CAA CTG CGT GTG TGG TTA CTG GGG GGG CAA GAG GCC CCC GTC GGT 1246 Arg Gin Leu Arg Val Trp Leu Leu Gly Gly Gin Glu Ala Pro Val Gly 400 405 410 415 GAC CCC GCT GTA CCG TGG CAA CGG TAC TGT GGT GTG TGA CTG TGA TTT 1294 Aep Pro Ala Val Pro Trp Gin Arg Tyr Cye Gly Val * Leu * Phe 420 425 430 TGG AAA AAT GCA TTG GGC CCC CCC CTT GTG TTC CGG YCT GGT GTG GCG 1342 Trp Lys Aβn Ala Leu Gly Pro Pro Leu Val Phe Arg Xaa Gly Val Ala 435 440 445 GGA CGG TCA TAG GAG GGG CAC CGT GCG CGA CCT CCC CCC GGT TTG CCC 1390 Gly Arg Ser * Glu Gly Hiβ Arg Ala Arg Pro Pro Pro Gly Leu Pro 450 455 460 CCG GGA GGT TCT CGG CAC GGT GAC AGT CAT GTG TCA GTG GGG TTC TGC 1438 Pro Gly Gly Ser Arg His Gly Aep Ser Hie Val Ser Val Gly Phe Cyβ 465 470 475 CTA CTG GAT TTG GAG ATT TGG GGA CTG GGT TGC ATT GTA CGA CGA GCT 1486 Leu Leu Aep Leu Glu He Trp Gly Leu Gly Cyβ He Val Arg Arg Ala 480 485 490 495 ACC ACG ATC AGC TCT CTG TAC TTT CTT CTC AGG TCA TGG TCC ACA ACC 1534 Thr Thr He Ser Ser Leu Tyr Phe Leu Leu Arg Ser Trp Ser Thr Thr 500 505 510 TAA AGA TCT CTC AGT CTT GAA TCC ATC CGG GGC ACC TTG TGC TTC TTG 1582 * Arg Ser Leu Ser Leu Glu Ser He Arg Gly Thr Leu Cyβ Phe Leu 515 520 525 CGT CGT TGA CCA GAG GCC GCT GAA ATG TGG TTC CTG CGT CCG CGA CTG 1630 Arg Arg * Pro Glu Ala Ala Glu Met Trp Phe Leu Arg Pro -Arg -Leu 530 535 540 CTG GGA GAC GGG GGG TCC TGG GTT CGA TGA GTG CGG TGT CGG TAC TCG 1678 Leu Gly Aep Gly Gly Ser Trp Val Arg * Val Arg Cye Arg Tyr Ser 545 550 555 GAT GAC GAA GCA CCT CGA GGC CGT CCT GGT TGA TGG AGG TGT GGA GTC 1726 Asp Asp Glu Ala Pro Arg Gly Arg Pro Gly * Trp Arg Cys Gly Val 560 565 570 575 CAA GGT GAC AAC GCC CAA GGG TGA GCG CCC CAA ATA CAT AGG TCA GCA 1774 Gin Gly Aep Aβn Ala Gin Gly * Ala Pro Gin He Hiβ Arg Ser Ala 580 585 590 CGG TGT GGG AAC CTA CTA CGG CGC TGT CCG TAG CCT CAA CAT CAG TTA 1822 Arg Cyβ Gly Aβn Leu Leu Arg Arg Cys Pro * Pro Gin His Gin Leu 595 600 605 CCT AGT GAC TGA GGT GGG GGG CTA TTG GCA TGC GCT GAA GTG CCC GTG 1870 Pro Ser Asp * Gly Gly Gly Leu Leu Ala Cys Ala Glu Val Pro Val 610 615 620 CGA CTT TGT GCC CCG AGT GCT CCC AGA AAG AAT TCC AGG TAG GCC TGT 1918 Arg Leu Cys Ala Pro Ser Ala Pro Arg Lys Asn Ser Arg * Ala Cys 625 630 635 GAA TGC ATG TCT AGC TGG GAA GTC TCC GCA CCC GTT CGC AAG TTG GGC 1966 Glu Cys Met Ser Ser Trp Glu Val Ser Ala Pro Val Arg Lys Leu Gly 640 645 650 655 TCC CGG TGG GTT TTA CGC CCC CGT GTT CAC CAA GTG CAA CTG GCC GAA 2014 Ser Arg Trp Val Leu Arg Pro Arg Val His Gin Val Gin Leu Ala Glu 660 665 670 GAC CTC CGG AGT GGA TGT GTG TCC TGG GTT TGC TTT CGA TTT CCC TGG 2062 Asp Leu Arg Ser Gly Cys Val Ser Trp Val Cys Phe Arg Phe Pro Trp 675 680 685 TGA TCA CAA CGG CTT CAT CCA TGT TAA AGG CAA CAG ACA GCA GGT TTA 2110 * Ser Gin Arg Leu Hiβ Pro Cye * Arg Gin Gin Thr Ala Gly Leu 690 695 700 CAG TGG TCA GCG AAG GTC TTC GCC GGC TTG GTT GCT TAC TGA CAT GGT 2158 Gin Trp Ser Ala Lys Val Phe Ala Gly Leu Val Ala Tyr * His Gly 705 710 715 CCT GGC CCT GTT GGT GGT GAT GAA GTT GGC TGA GGC TAG AGT TGT CCC 2206 Pro Gly Pro Val Gly Gly Asp Glu Val Gly * Gly * Ser Cys Pro 720 725 730 735 CCT GTT TAT GCT GGC AAT GTG GTG GTG GTT GAA TGG AGC ATC TGC TGC 2254 Pro Val Tyr Ala Gly Aβn Val Val Val Val Glu Trp Ser He Cyβ Cyβ 740 745 750 CAC TAT TGT CAT CAT ACA CCC TAC TGT CAC GAA GTC CAC TGA AAG TGT 2302 Hiβ Tyr Cyβ Hie Hiβ Thr Pro Tyr Cye His Glu Val His * Lye Cys 755 760 765 TCC ATT GTG GAC TCC GCC CAC TGT TCC AAC TCC ATC TTG CCC GAA TTC 2350 Ser He Val Asp Ser Ala His Cys Ser Asn Ser He Leu Pro Glu Phe 770 775 780 TAC CAC CGG AGT CGC GGA CTC TAC CTA CAA TGC TGG TTG CTA CAT GGT 2398 Tyr Hiβ Arg Ser Arg Gly Leu Tyr Leu Gin Cyβ Trp Leu Leu Hiβ Gly 785 790 795 GGC AGG CCT GGC GGC CGG GGC TCA GGC GGT CTG GGG TGC TGC CAA TGA 2446 Gly Arg Pro Gly Gly Arg Gly Ser Gly Gly Leu Gly Cye Cye Gin * 800 805 810 815 TGG TGC TCA GGC CGT CGT TGG TGG CAT CTG GCC CGC GTG GCT CAA GCT 2494 Trp Cye Ser Gly Arg Arg Trp Trp Hiβ Leu Ala Arg Val Ala Gin Ala 820 825 830 GCG AAG CTT CGC TGC CGG TCT GGC CTG GTT GTC AAA TGT TGG GGC TTA 2542 Ala Lye Leu Arg Cyβ Arg Ser Gly Leu Val Val Lye Cyβ Trp Gly Leu 835 840 845 CTT GCC GGT CGT CGA GGC CGC VCT GGC TCC CGA GCT GGT GTG CAC CCC 2590 Leu Ala Gly Arg Arg Gly Arg Xaa Gly Ser Arg Ala Gly Val Hie Pro 850 855 860 GGT GGT CGG CTG GGC AGC CCA GGA GTG GTG GTT CAC TGG TTG TCT GGG 2638 Gly Gly Arg Leu Gly Ser Pro Gly Val Val Val His Trp Leu Ser Gly 865 870 875 TGT GAT GTG TGT CGT GGC GTA CCT GAA TGT CCT GGG CTC TGT RAG GGC 2686 Cyβ Aep Val Cys Arg Gly Val Pro Glu Cys Pro Gly Leu Cys Xaa Gly 880 885 890 895 TGC CGT GCT TGT GGC GAT GCA CTT CGC AAG GGG TGC TCT GCC GCT GGT 2734 Cys Arg Ala Cys Gly Asp Ala Leu Arg Lye Gly Cyβ Ser Ala Ala Gly 900 905 910 ATT GGT GGT AGC TGC CGG GGT RAC CCG GGA GCG GCA CAG CGT CTT AGG 2782 He Gly Gly Ser Cys Arg Gly Xaa Pro Gly Ala Ala Gin Arg Leu Arg 915 920 925 GCT TGA GGT GTG CTT CGA TCT GGA TGG TGG AGA CTG GCC RGA CGC CAG 2830 Ala * Gly Val Leu Arg Ser Gly Trp Trp Arg Leu Ala Xaa Arg Gin 930 935 940 TTG GTC TTG GGG TTT AGC AGG CGT GGT GAG CTG GGC CCT CCT GGT GGG 2878 Leu Val Leu Gly Phe Ser Arg Arg Gly Glu Leu Gly Pro Pro Gly Gly 945 950 955 GGG TCT GAT GAC CCA CGG TGG CCG ATC AGC CAG AYT GAC TTG GTA YGC 2926 Gly Ser Asp Asp Pro Arg Trp Pro He Ser Gin Xaa Aep Leu Val Xaa 960 965 970 975 CAG GTG GGC CGT CAA TTA YCA GAG GGT TCG YCG GTG GGT GAA CAA CTC 2974 Gin Val Gly Arg Gin Leu Xaa Glu Gly Ser Xaa Val Gly Glu Gin Leu 980 985 990 ACC GGT TGG AGC YTT TGG YCG TTG GMG GCG YGC CTG GAA AGC YTG GTT 3022 Thr Gly Trp Ser Xaa Trp Xaa Leu Xaa Ala Xaa Leu Glu Ser Xaa Val 34J3 9*5 ϊOfJO 1005 RGT KGT GGC TTG GTT CTT CCC CCA GAC AGT TGC CAC AGT YTC CGT CAT 3070 Xaa Xaa Gly Leu Val Leu Pro Pro Asp Ser Cys His Ser Xaa Arg His 1010 1015 1020 CTT CAT ACT CTG TTT GAG CAG TTT AGA TGT CAT TGA TTT CAT CTT GGA 3118 Leu His Thr Leu Phe Glu Gin Phe Arg Cye His * Phe Hie Leu Gly 1025 1030 1035 RGT ACT CTT GGT TAA CTC ACC AAA TCT CGC GCG CTT GGC GCG RGT GCT 3166 Xaa Thr Leu Gly * Leu Thr Lye Ser Arg Ala Leu Gly Ala Xaa Ala 1040 1045 1050 1055 GGA CTC CTT AGC TCT HGC TGA GGA GCG GCT GGC CTG CTC TTG GCT GGT 3214 Gly Leu Leu Ser Ser Xaa * Gly Ala Ala Gly Leu Leu Leu Ala Gly 1060 1065 1070 GGG CGT CCT GCG CAA GCG GGG CGT CCT CCT CTA CGA GCA CGC YGG TCA 3262 Gly Arg Pro Ala Gin Ala Gly Arg Pro Pro Leu Arg Ala Arg Xaa Ser 1075 1080 1085 CAC TAG CAG GCG CGG TGC TGC CCG CTT GCG AGA GTG GGG YTT TGC GCT 3310 Hie * Gin Ala Arg Cye Cye Pro Leu Ala Arg Val Gly Xaa Cyβ Ala 1090 1095 1100 YGA GCC KGT TAG YAT AAC CAA GGA AGA TTG YGC YAT TGT TCG GGA CTC 3358 Xaa Ala Xaa * Xaa Aβn Gin Gly Arg Leu Xaa Xaa Cys Ser Gly Leu 1105 1110 1115 TGC TCG TGT GTT GGG CTG TGG ACA ATT GGT CCA TGG GAA ACC AGT GGT 3406 Cyβ Ser Cyβ Val Gly Leu Trp Thr He Gly Pro Trp Glu Thr Ser Gly 1120 1125 1130 1135 CGC GAG GCG AGG CGA CGA GGT GTT GAT CGG CTG TGT GAA CAG TCG GTT 3454 Arg Glu Ala Arg Arg Arg Gly Val Asp Arg Leu Cys Glu Gin Ser Val 1140 1145 1150 CGA CCT TCC GCC TGG CTT TGT TCC CAC TGC TCC CGT GGT SCT TCA TCA 3502 Arg Pro Ser Ala Trp Leu Cye Ser Hiβ Cys Ser Arg Gly Xaa Ser Ser 1155 1160 1165 RGC WGG CAA RGG RTT YTT YGG GGT TGT GAA GAC MTC CAT GAC AGG CAA 3550 Xaa Xaa Gin Xaa Xaa Xaa Xaa Gly Cyβ Glu Asp Xaa Hiβ Asp Arg Gin 1170 1175 1180 GGA CCC GTC CGA ACA CCA CGG RAA CGT GGT GGT CCT WGG GAC TTC AAC 3598 Gly Pro Val Arg Thr Pro Arg Xaa Arg Gly Gly Pro Xaa Asp Phe Asn 1185 1190 1195 AAC KCG TTC CAT GGG CTG CTG CGT GAA CGG AGT AGT GTA CAC RAC ATA 3646 Aβn Xaa Phe Hiβ Gly Leu Leu Arg Glu Arg Ser Ser Val His Xaa He 1200 1205 1210 1215 CCA TGG YAC CAA CGC CCG RCC KAT GGC GGG GCC KTT TGG KCC YGT CAA 3694 Pro Trp Xaa Gin Arg Pro Xaa Xaa Gly Gly Ala Xaa Trp Xaa Xaa Gin 1220 - 1225 1230 YGC TCG GTG GTG GTC WGC GAG YGA CGA CGT CAC GGT YTA CCC GCT CCC 3742 Xaa Ser Val Val Val Xaa Glu Xaa Arg Arg Hiβ Gly Xaa Pro Ala Pro 1235 1240 1245 WAA TGG YGC TTC TTG CCT YCA RGC WTG YAA GTG CCA ACC AAC TGG GGT 3790 Xaa Trp Xaa Phe Leu Pro Xaa Xaa Xaa Xaa Val Pro Thr Aβn Trp Gly 1250 1255 1260 GTG GGT GAT CCG GAA TGA CGG AGC TCT TTG CCA TGG AAC TCT CGG CAA 3838 Val Gly Aep Pro Glu * Arg Ser Ser Leu Pro Trp Aβn Ser Arg Gin 1265 1270 1275 GGT GGT GGA TTT AGA TAT GCC CGC TGA GTT GTC AGA CTT TCG CGG GTC 3886 Gly Gly Gly Phe Arg Tyr Ala Arg * Val Val Arg Leu Ser Arg Val 1280 1285 1290 1295 TTC TGG ATC ACC AAT CTT GTG CGA TGA GGG TCA TGC TGT TGG CAT GCT 3934 Phe Trp He Thr Asn Leu Val Arg * Gly Ser Cys Cyβ Trp Hiβ Ala 1300 1305 1310 GAT TTC GGT GCT TCA TAG GGG GAG TAG GGT TTC CTC GGT GCG GTA TAC 3982 Asp Phe Gly Ala Ser * Gly Glu * Gly Phe Leu Gly Ala Val Tyr 1315 1320 1325 CAA ACC TTG GGA AAC TCT CCC TCG GGA GAT TGA GGC TCG ATC GGA GGC 4030 Gin Thr Leu Gly Aβn Ser Pro Ser Gly Aep * Gly Ser He Gly Gly 1330 1335 1340 CCC CCC TGT GCC AGG AAC CAC TGG ATA CAG GGA GGC GCC ACT GTT CCT 4078 Pro Pro Cys Ala Arg Aβn Hiβ Trp He Gin Gly Gly Ala Thr Val Pro 1345 1350 1355 GCC CAC CGG AGC TGG CAA GTC GAC GCG CGT GCC GAA TGA GTA CGT CAA 4126 Ala His Arg Ser Trp Gin Val Asp Ala Arg Ala Glu * Val Arg Gin 1360 1365 1370 1375 GGC TGG ACA CAA RGT GCT TGT ACT AAA CCC ATC CAT TGC CAC AGT GAG 4174 Gly Trp Thr Gin Xaa Ala Cys Thr Lye Pro He Hie Cys His Ser Glu 1380 1385 1390 GGC CAT GGG CCC TTA CAT GGA AAA GTT AAC CGG CAA ACA TCC GTC GGT 4222 Gly Hie Gly Pro Leu Hie Gly Lye Val Aβn Arg Gin Thr Ser Val Gly 1395 1400 1405 GTA CTG TGG CCA TGA CAC TAC TGC ATA TTC CAG GAC TAC TGA CTC ATC 4270 Val Leu Trp Pro * Hiβ Tyr Cyβ He Phe Gin Aep Tyr * Leu He 1410 1415 1420 TTT GAC CTA CTG TAC ATA CGG CAG GTT TAT GGC CAA TCC CAG GAA ATA 4318 Phe Asp Leu Leu Tyr He Arg Gin Val Tyr Gly Gin Ser Gin Glu He 1425 1430 1435 CTT GCG GGG GAA CGA CGT CGT AAT TTG CGA CGA GTT GCA CGT CAC CGA 4366 Leu Ala Gly Glu Arg Arg Arg Aβn Leu Arg Arg Val Ala Arg Hiβ Arg 1440 1445 1450 1455 CCC GAC CTC AAT TTT GGG GAT GGG TCG GGC GAG GTT ACT CGC TCG CGA 4414 Pro Aep Leu Aβn Phe Gly Asp Gly Ser Gly Glu Val Thr Arg Ser Arg 1460 1465 1470 GTG CGG CGT ACG CCT CCT GCT TTT CGC TAC GGC GAC CCC ACC GGT CTC 4462 Val Arg Arg Thr Pro Pro Ala Phe Arg Tyr Gly Asp Pro Thr Gly Leu 1475 1480 1485 TCC GAT GGC GAA GCA TGA ATC TAT TCA TGA GGA GAT GTT GGG CAG TGA 4510 Ser Asp Gly Glu Ala * He Tyr Ser * Gly Asp Val Gly Gin * 1490 1495 1500 GGG GGA GGT CCC CTT CTA TTG CCA ATT CCT CCC ACT GAG TAG GTA TGC 4558 Gly Gly Gly Pro Leu Leu Leu Pro He Pro Pro Thr Glu * Val Cyβ 1505 1510 1515 TAC TGG GAG ACA CCT GCT GTT TTG TCA TTC CAA GGT AGA RTG CAC TAG 4606 Tyr Trp Glu Thr Pro Ala Val Leu Ser Phe Gin Gly Arg Xaa Hiβ * 1520 1525 1530 1535 GTT ATC CTC AGC TTT GGC CAG CTT TGG TGT CAA CAC CGT TGT GTA CTT 4654 Val He Leu Ser Phe Gly Gin Leu Trp Cye Gin Hie Arg Cyβ Val Leu 1540 1545 1550 CAG AGG CAA AGA AAC TGA CAT TCC AAC TGG TGA CGT GTG CGT TTG CGC 4702 Gin Arg Gin Arg Aen * Hie Ser Aβn Trp * Arg Val Arg Leu Arg 1555 1560 1565 CAC AGA CGC ACT TTC CAC TGG TTA CAC TGG CAA TTT TGA CAC CGT AAC 4750 Hiβ Arg Arg Thr Phe His Trp Leu His Trp Gin Phe * Hiβ Arg Asn 1570 1575 1580 AGA CTG TGG TTT AAT GGT TGA GGA GGT AGT GGA AGT GAC CCT GGA CCC 4798 Arg Leu Trp Phe Aβn Gly * Gly Gly Ser Gly Ser Asp Pro Gly Pro 1585 1590 1595 GAC CAT CAC TAT CGG TGT GAA GAC CGT CCC GGC CCC TGC CGA ACT GAG 4846 Asp Hiβ Hie Tyr Arg Cyβ Glu Aep Arg Pro Gly Pro Cye Arg Thr Glu 1600 1605 1610 1615 GGC TCA GAG GCG TGG TAG GTG TGG CCG TGG GAA AGC GGG CAC TTA CTA 4894 Gly Ser Glu Ala Trp * Val Trp Pro Trp Glu Ser Gly His Leu Leu 1620 1625 1630 TCA GGC ATT GAT GTC TTC GGC GCC GGC GGG AAC SGT TCG GTC TGG GGC 4942 Ser Gly He Aep Val Phe Gly Ala Gly Gly Aen Xaa Ser Val Trp Gly 1635 1640 1645 TCT CTG GGC AGC TGT TGA GGC TGG HGT CTC GTG GTA TGG CCT AGA GCC 4990 Ser Leu Gly Ser Cys * Gly Trp Xaa Leu Val Val Trp Pro Arg Ala 1650 1655 1660 CGA TGC TAT TGG AGA CCT GCT TAG GGC CTA CGA CTC GTG TCC TTA TAC 5038 Arg Cyβ Tyr Trp Arg Pro Ala * Gly Leu Arg Leu Val Ser Leu Tyr 1665 1670 1675 TGC TGC CAT CAG TGC GTC CAT CGG AGA GGC CAT TGC CTT TTT TAC TGG 5086 Cyβ Cyβ Hiβ Gin Cyβ Val Hiβ Arg Arg Gly His Cyβ Leu Phe Tyr Trp 1680 1685 1690 169Ϊ YCT AGT GCC AAT GAG GAA TTA TCC TCA GGT GGT TTG GGC CAA GCA GAA 5134 Xaa Ser Ala Aen Glu Glu Leu Ser Ser Gly Gly Leu Gly Gin Ala Glu 1700 1705 1710 k " f GGG RCA CAA CTG GCC ACT CTT GGT GGG TGT GCA GAG GCA CAT GTG TGA 5182 Gly Xaa Gin Leu Ala Thr Leu Gly Gly Cye Ala Glu Ala Hiβ Val * 1715 1720 1725 GGA CGC GGG CTG TGG TCC KCC CGC TAA TGG TCC CGA ATG GAG CGG CAT 5230 Gly Arg Gly Leu Trp Ser Xaa Arg * Trp Ser Arg Met Glu Arg Hie 1730 1735 1740 CAG GGG AAA AGG GCC TGT TCC CCT GTT GTG CCG ATG GGG TGG TGA CTT 5278 Gin Gly Lye Arg Ala Cyβ Ser Pro Val Val Pro Met Gly Trp * Leu 1745 1750 1755 GCC TGA GTC GGT GGC TCC GCA TCA CTG GGT TGA TGA CCT ACA GGC CCG 5326 Ala * Val Gly Gly Ser Ala Ser Leu Gly * * Pro Thr Gly Pro 1760 1765 1770 1775 GCT CGG TGT GGC CGA GGG TTA CAC TCC CTG CAT TGC TGG ACC GGT GCT 5374 Ala Arg Cyβ Gly Arg Gly Leu Hiβ Ser Leu Hiβ Cye Trp Thr Gly Ala 1780 1785 1790 TTT GGT CGG TTT GGC GAT GGC GGG GGG GGC TAT CCT GGC ACA CTG GAC 5422 Phe Gly Arg Phe Gly Aep Gly Gly Gly Gly Tyr Pro Gly Thr Leu Asp 1795 1800 1805 GGG GTC TCT GGT TGT AGT GAC CAG TTG GGT TGT CAA TGG GAA CGG TAA 5470 Gly Val Ser Gly Cys Ser Asp Gin Leu Gly Cys Gin Trp Glu Arg * 1810 1815 1820 CCC GCT GAT ACA AAG CGC CTC TAG GGG CGT GGC KAC YAG CGG TCC ATA 5518 Pro Ala Asp Thr Lys Arg Leu * Gly Arg Gly Xaa Xaa Arg Ser He 1825 1830 1835 CCC AGT ACC CCC AGA TGG TGG TGA ACG GTA CCC ATC AGA CAT CAA GCC 5566 Pro Ser Thr Pro Arg Trp Trp * Thr Val Pro He Arg His Gin Ala 1840 1845 1850 1855 AAT YAC TGA GGC TGT GAC CAC CCT TGA GAC TGC GTG CGG YTG GGG CCC 5614 Asn Xaa * Gly Cys Aep His Pro * Aep Cys Val Arg Xaa Gly Pro 1860 1865 1870 AGC CGC GGC BAG TCT GGC TTA TGT GAA GGC CTG TGA AAC TGG AAC CAT 5662 Ser Arg Gly Xaa Ser Gly Leu Cys Glu Gly Leu * Asn Trp Aβn His 1875 1880 1885 GTT GGC TGA CAA RGC GAG TGC TGC GTG GCA GGC TTG GGC TGC AAA CAA 5710 Val Gly * Gin Xaa Glu Cys Cys Val Ala Gly Leu Gly Cyβ Lys Gin 1890 1895 1900 CTT TGT GCC TCC ACC AGC ATC ACA CTC AAC TTC CTT GTT RCA GAG CTT 5758 Leu Cye Ala Ser Thr Ser He Thr Leu Aβn Phe Leu Val Xaa Glu Leu 1905 1910 1915 GGA YGC TGC GTT CAC TTC AGC TTG GGA TAG CGT GTT CAC TCA CGG CCG "~ 5806 Gly Xaa Cye Val Hie Phe Ser Leu Gly * Arg Val Hiβ Ser Arg Pro 1920 1925 1930 1935 TTC CTT GCT TGT TGG GTT CAC AGC TGC TTA CGG CGC TCG GCG GAA CCC 5854 Phe Leu Ala Cye Trp Val Hiβ Ser Cys Leu Arg Arg Ser Ala Glu Pro 1940 1945 1950 ACC GCT GGG CGT CGG AGC CTC TTT CTT GCT GGG CAT GTC ATC GAG CCA 5902 Thr Ala Gly Arg Arg Ser Leu Phe Leu Ala Gly His Val He Glu Pro 1955 1960 1965 CYT RAC TCA CGT CAG ACT TGC TGC TGC GTT GCT CCT CGG CGT CGG GGG 5950 Xaa Xaa Ser Arg Gin Thr Cyβ Cys Cyβ Val Ala Pro Arg Arg Arg Gly 1970 1975 1980 TAC CGT CCT AGG CAC GCC TGC TAC TGG GCT TGC TAT GGC GGG TGC CTA 5998 Tyr Arg Pro Arg Hie Ala Cyβ Tyr Trp Ala Cyβ Tyr Gly Gly Cyβ Leu 1985 1990 1995 CTT CGC KGG GGG CAG CGT TAC CGC TAA CTG GCT GAG TAT CAT TGT GGC 6046 Leu Arg Xaa Gly Gin Arg Tyr Arg * Leu Ala Glu Tyr Hie Cye Gly 2000 2005 2010 2015 TCT AAT CGG AGG CTG GGA GGG GGC RGT KAA CGC AGC CTC ACT CAC CTT 6094 Ser Aβn Arg Arg Leu Gly Gly Gly Xaa Xaa Arg Ser Leu Thr Hiβ Leu 2020 2025 2030 CGA YCT CCT GGC KGG GAA GTT ACA AGC KAG YGA YGC TTG GTG CCT RGT 6142 Arg Xaa Pro Gly Xaa Glu Val Thr Ser Xaa Xaa Xaa Leu Val Pro Xaa 2035 2040 2045 CAG YTG CYT GGC CTC TCC GGG GGC TTC GGT GGC YGG TGT GGC DCT VGG 6190 Gin Xaa Xaa Gly Leu Ser Gly Gly Phe Gly Gly Xaa Cys Gly Xaa Xaa 2050 2055 2060 YCT DYT GCT VTG GTC TGT CAA RAA GGG TGT GGG WCA RGA YTG GGT TAA 6238 Xaa Xaa Ala Xaa Val Cys Gin Xaa Gly Cys Gly Xaa Xaa Xaa Gly * 2065 2070 2075 CAG AYT GTT GAC GAT GAT GCC ACG CAG TTC GGT GAT GCC TGA CGA TTT 6286 Gin Xaa Val Asp Asp Aep Ala Thr Gin Phe Gly Asp Ala * Arg Phe 2080 2085 2090 2095 CTT CCT CAA AGA TGA GTT CGT CAC CAA GGT GTC TAC TGT CCT GCG AAA 6334 Leu Pro Gin Arg * Val Arg Hie Gin Gly Val Tyr Cys Pro Ala Lys 2100 2105 2110 GTT GTC ATT GTC AAG ATG GAT CAT GAC TCT TGT GGA CAA GCG GGA GAT 6382 Val Val He Val Lys Met Asp His Asp Ser Cyβ Gly Gin Ala Gly Asp 2115 2120 2125 GGA GAT GGA GAC MCC CGC TTC TCA GAT TGT TTG GGA CTT GCT TGA CTG 6430 Gly Asp Gly Asp Xaa Arg Phe Ser Aep Cyβ Leu Gly Leu Ala * Leu 2130 2135 2140 GTG CAT CCG GCT RGG TCG GTT CCT GTA CAA TAA ACT YAT GTT TGC TCT 6478 Val Hiβ Pro Ala Xaa Ser Val Pro Val Gin * Thr Xaa Val Cyβ Ser 2145 2150 2155 CCC TAG GTT GCG CCT GCC GCT TAT CGG TTG CAG TAC CGG TTG GGG TGG 6526 Pro * Val Ala Pro Ala Ala Tyr Arg Leu Gin Tyr Arg Leu Gly Trp 2160 2165 2170 2175 CCC GTG GGA GGG CAA TGG TCA TTT GGA AAC AAG GTG TAC TTG TGG CTG 6574 Pro Val Gly Gly Gin Trp Ser Phe Gly Aen Lye Val Tyr Leu Trp Leu 2180 2185 2190 TGT GAT TAC CGG TGA TAT TCA CGA TGG TAT ATT GCA CGA CCT ACA TTA 6622 Cyβ Aep Tyr Arg * Tyr Ser Arg Trp Tyr He Ala Arg Pro Thr Leu 2195 2200 2205 TAC CTC CCT ACT GTG CAG ACA TTA CTA CAA GAG GAC AGT GCC TGT TGG 6670 Tyr Leu Pro Thr Val Gin Thr Leu Leu Gin Glu Aep Ser Ala Cye Trp 2210 2215 2220 CGT CAT GGG CAA TGC TGA GGG AGC AGT CCC CCT TGT GCC TAC TGG CGG 6718 Arg Hiβ Gly Gin Cyβ * Gly Ser Ser Pro Pro Cys Ala Tyr Trp Arg 2225 2230 2235 TGG AAT CAG GAC TTA CCA AAT TGG GAC TTC TGA CTG GTT TGA GGC TGT 6766 Trp Aβn Gin Aep Leu Pro Aβn Trp Asp Phe * Leu Val * Gly Cys 2240 2245 2250 2255 GGT CGT GCA TGG GAC AAT CAC GGT GCA CGC CAC CAG TTG CTA TGA GTT 6814 Gly Arg Ala Trp Asp Asn His Gly Ala Arg His Gin Leu Leu * Val 2260 2265 2270 GAA AGC TGC TGA CGT TCG GAG GGC GGT GCG AGC CGG CCC GAC TTA CGT 6862 Glu Ser Cys * Arg Ser Glu Gly Gly Ala Ser Arg Pro Asp Leu Arg 2275 2280 2285 TGG TGG CGT ACC TTG CAG CTG GAG CGC GCC GTG TAC TGC GCC TGC GCT 6910 Trp Trp Arg Thr Leu Gin Leu Glu Arg Ala Val Tyr Cys Ala Cys Ala 2290 2295 2300 CGT TTA CAG GCT AGG CCA GGG CAT CAA AAT CGA TGG AGC GCG CCG ACT 6958 Arg Leu Gin Ala Arg Pro Gly His Gin Asn Arg Trp Ser Ala Pro Thr 2305 2310 2315 GTT GCC CTG TGA CTT AGC ACA GGG AGC GCG CCA CCC CCC GGT ATC TGG 7006 Val Ala Leu * Leu Ser Thr Gly Ser Ala Pro Pro Pro Gly He Trp 2320 2325 2330 2335 CAG TGT TGC CGG TAG TGG TTG GAC AGA TGA GGA CGA GAG GGA CTT GGT 7054 Gin Cys Cys Arg * Trp Leu Asp Arg * Gly Arg Glu Gly Leu Gly 2340 2345 2350 GGA AAC CAA GGC TGC CGC CAT CGA GGC CAT TGG GGC GGC CTT GCA CCT 7102 Gly Asn Gin Gly Cys Arg His Arg Gly His Trp Gly Gly Leu Ala Pro 2355 2360 2365 CCC TTC ACC GGA GGC TGC TCA GGC CGC TCT AGA GGC TTT GGA GGA GGC 7150 Pro Phe Thr Gly Gly Cys Ser Gly Arg Ser Arg Gly Phe Gly Gly Gly 2370 2375 2380 TGC CGT GTC CCT GTT GCC CCA TGT GCC CGT CAT TAT GGG TGA TGA CTG 7198 Cyβ Arg Val Pro Val Ala Pro Cyβ Ala Arg Hiβ Tyr Gly * * Leu 2385 2390 2395 TTC ATG CCG GGA TGA GGC GTT CCA AGG CCA CTT CAT CCC AGA ACC CAA 7246 Phe Met Pro Gly * Gly Val Pro Arg Pro Leu His Pro Arg Thr Gin 2400 2405 2410 2415 TGT GAC AGA GGT ACC CAT TGA GCC CAC GGT CGG AGA CGT GGA GGC ACT 7294 Cyβ Aep Arg Gly Thr Hie * Ala Hiβ Gly Arg Arg Arg Gly Gly Thr 2420 2425 2430 CAA GCT GCG GGC TGC AGA CCT GAC CGC CAG GTT GCA AGA CTT GGA GGC 7342 Gin Ala Ala Gly Cys Arg Pro Asp Arg Gin Val Ala Arg Leu Gly Gly 2435 2440 2445 CAT GGC TCT CGC CCG CGC TGA GTC AAT CGA GGA TGC TCG CGC AGC TTC 7390 Hiβ Gly Ser Arg Pro Arg * Val Asn Arg Gly Cyβ Ser Arg Ser Phe 2450 2455 2460 GAT GCC TTC GCT CAC CGA GGT GGA CTC AAT GCC ATC ATT GGA GTC GAG 7438 Aep Ala Phe Ala His Arg Gly Gly Leu Asn Ala He He Gly Val Glu 2465 2470 2475 CCC TTG CTC CTC CTT TGA ACA AAT CTC TTT AAC TGA AAG TGA CCC TGA 7486 Pro Leu Leu Leu Leu * Thr Asn Leu Phe Asn * Lys * Pro * 2480 2485 2490 2495 GAC TGT CGT CGA GGC TGG CTT ACC CTT GGA GTT CGT GAA CTC CAA CAC 7534 Asp Cye Arg Arg Gly Trp Leu Thr Leu Gly Val Arg Glu Leu Gin His 2500 2505 2510 CGG GCC GTC TCC GGC TCG GAG GAT TGT CAG AAT CCG ACA GGC TTG CTG 7582 Arg Ala Val Ser Gly Ser Glu Aep Cye Gin Aen Pro Thr Gly Leu Leu 2515 2520 2525 TTG TGA CAG ATC CAC AAT GAA GGC CAT GCC GTT GTC GTT CAC TGT CGG 7630 Leu * Gin He Hiβ Aβn Glu Gly Hiβ Ala Val Val Val Hiβ Cyβ Arg 2530 2535 2540 GGA GTG CCT CTT CGT TAC TCG CTA TGA CCC GGA CGG TCA CCA ACT GTT 7678 Gly Val Pro Leu Arg Tyr Ser Leu * Pro Gly Arg Ser Pro Thr Val 2545 2550 2555 TGA CGA GCG AGG TCC GAT AGA GGT ATC TAC TCC TAT ATG TGA AGT GAT 7726 * Arg Ala Arg Ser Aep Arg Gly He Tyr Ser Tyr Met * Ser Aep 2560 2565 2570 2575 TGG GGA CAT CAG GCT TCA GTG TGA CCA AAT TGA GGA AAC TCC AAC ATC 7774 Trp Gly His Gin Ala Ser Val * Pro Asn * Gly Asn Ser Asn He 2580 2585 2590 TTA CTC TTA CAT CTG GTC AGG GGC GCC CTT GGG TAC TGG GAG AAG TGT 7822 Leu Leu Leu His Leu Val Arg Gly Ala Leu Gly Tyr Trp Glu Lys Cyβ 2595 2600 2605 CCC CCA ACC CAT GAC GCG CCC TAT AGG GAC CCA TCT GAC TTG TGA CAC 7870 Pro Pro Thr His Aep Ala Pro Tyr Arg Aep Pro Ser Aep Leu * Hie 2610 2615 2620 357 GGG GCA CCT GGC CAG AGC CCT CCT CTG GCA YCC AGG KTT GAA GGA GCA 9310 Gly Ala Pro Gly Gin Ser Pro Pro Leu Ala Xaa Arg Xaa Glu Gly Ala 3090 3095 3100 YCC CCC RCC CAT AAA TTC ACT TCC AGG TTT TCA GCT GGC GAC GCC TTA 9358 Xaa Pro Xaa Hie Lye Phe Thr Ser Arg Phe Ser Ala Gly Aep Ala Leu 3105 3110 3115 CGA ACA CCA TGA AGA GGT CTT GAT CTC GAT CAA GAG TCG ACC ACC TTG 9406 Arg Thr Pro * Arg Gly Leu Aep Leu Aep Gin Glu Ser Thr Thr Leu 3120 3125 3130 3135 GAT AAG GTG GAT TCT TGG TGC TTG TCT CTC GTT GCT GGC CGC CTT GCT 9454 Aep Lye Val Aep Ser Trp Cyβ Leu Ser Leu Val Ala Gly Arg Leu Ala 3140 3145 3150 GTG AAT TCG CTC CAG GCA GTA GGA CCT TCG GGT CGG GGG 9493 Val Aβn Ser Leu Gin Ala Val Gly Pro Ser Gly Arg Gly 3155 3160 (2) INFORMATION FOR SEQ ID NO:270: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 33 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (Xi) SEQUENCE DESCRIPTION: SEQ ID NO:270: Val Gly Val Arg Gly Pro Gly Pro Pro Thr Glu Val Gly Gly Lye Gly 1 5 10 15 Pro Trp Thr Gly Arg Val Glu Gly Pro Glu Pro Val Hie Leu Pro Gin 20 25 30 Gly (2) INFORMATION FOR SEQ ID NO:271: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:271: Gly Arg Gly Thr Ser He Gly Pro Val Gly Pro Lye Gly Val Trp Met 1 5 10 15 Pro Ser Val Arg Val Arg Arg Trp 20 (2) INFORMATION FOR SEQ ID NO:272: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 10 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:272: He Pro Ala Arg Arg Glu Ser Ala He Gly 1 5 10 (2) INFORMATION FOR SEQ ID NO:273: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 27 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:273; Ala Tyr Pro Gly Aep Arg Cyβ Pro Gly Thr Ser Pro Ala Xaa Leu Trp 1 5 10 15 Thr Arg Ser Thr Gly Trp Gly Tyr Arg Cyβ Glu 20 25 (2) INFORMATION FOR SEQ ID NO:274: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:274: Ser Val Ser Arg 1 (2) INFORMATION FOR SEQ ID NO:275: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 5 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear 359 (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:275: Thr Glu Thr Val Ser 1 5 (2) INFORMATION FOR SEQ ID NO:276: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 74 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:276: Asp Arg Asn Asp Ala Pro Arg Thr Gly Thr Pro Pro Lye Pro Ser Gly 1 5 10 15 Gin Leu Cys Gly Leu Thr He Pro Val Gly Gly Arg Gly Pro Ala Asp 20 25 30 Tyr Leu Ser Cys Glu Phe Leu Leu Arg Leu Ala Glu Arg Gin Pro Arg 35 40 45 Gly His Gin Gly Gly Ala Ala Leu His Ala Ala Arg Gly Lys He Leu 50 55 60 Arg Val Thr Pro Gly Gly Asn Pro Phe Pro 65 70 (2) INFORMATION FOR SEQ ID NO:277: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 88 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:277: Glu Hiβ Glu Cys Gly Arg His He His His Gly Leu Ala Val Val Ala 1 5 10 15 Gly Leu Leu Pro Pro Arg Gly Gly Gly Ala Leu Gin Leu Ala Ala Pro 20 25 30 Val Leu Gin Trp Gly Pro Leu Cyβ Ala Phe Gin Leu Leu Phe Pro Arg 35 40 45 Arg Gly Leu Leu Leu Phe Arg Gly Arg Met Ser Gly Gly Leu Trp Leu 360 50 55 60 Tyr Cys Leu His Thr Val Leu Leu Glu Ala Leu Pro Ala Trp Gly Gly 65 70 75 80 Tyr Ser Ala Arg Val Arg Thr Arg 85 (2) INFORMATION FOR SEQ ID NO:278: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 25amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:278: Ala Ala Gly Glu He Trp Glu Cys Aen Trp Ser Gly Val Gly Phe Gly 1 5 10 15 Leu Hiβ Arg Trp Ser Pro Arg Val Gly 20 25 (2) INFORMATION FOR SEQ ID NO:279: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 27 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:279: Thr Leu Gin Phe Gly Leu Leu Gly Aep Val Pro Hie Gin Ser Pro Leu 1 5 10 15 Thr Aep Ser Gin Arg Hiβ Leu Arg Glu Gly Leu 20 25 (2) INFORMATION FOR SEQ ID NO:280: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 10 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear 361 (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:280: Val Tyr Leu Pro Arg Leu Val Hiβ Arg Phe 1 5 10 (2) INFORMATION FOR SEQ ID NO:281: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 83 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:281: Leu Gly Val Tyr Gin Aep Leu Ala Val Ala Gly Gin Ala Val Ala Arg 1 5 10 16 Pro Aen Gly Xaa Xaa Gly Leu Glu Pro Pro Arg Aep Pro His Ala Gly 20 25 30 Pro Arg Ala Ala Pro Pro Asp Ser Leu Pro Thr Ala Phe Gly Ser Gly 35 40 45 Arg Gly Ser Glu Gly Asp Val Arg Gin Leu Arg Val Trp Leu Leu Gly 50 55 60 Gly Gin Glu Ala Pro Val Gly Asp Pro Ala Val Pro Trp Gin Arg Tyr 65 70 75 80 Cys Gly Val (2) INFORMATION FOR SEQ ID NO:282: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:282: Phe Trp Lys Asn Ala Leu Gly Pro Pro Leu Val Phe Arg Xaa Gly Val 1 5 10 15 362 Ala Gly Arg Ser 20 (2) INFORMATION FOR SEQ ID NO:283: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 65 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:283: Glu Gly Hiβ Arg Ala Arg Pro Pro Pro Gly Leu Pro Pro Gly Gly Ser 1 5 10 15 Arg His Gly Asp Ser His Val Ser Val Gly Phe Cyβ Leu Leu Aep Leu 20 25 30 Glu He Trp Gly Leu Gly Cys He Val Arg Arg Ala Thr Thr He Ser 35 40 45 Ser Leu Tyr Phe Leu Leu Arg Ser Trp Ser Thr Thr 50 60 65 (2) INFORMATION FOR SEQ ID NO:284: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 16 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:284; Arg Ser Leu Ser Leu Glu Ser He Arg Gly Thr Leu Cye Phe Leu Arg 1 5 10 15 Arg (2) INFORMATION FOR SEQ ID NO:285: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 22 amino acidβ 363 ' (B) TYPE : aπrirro- όrc-±dr (D) TOPOLOGY : linear Cii) MOLECULE TYPK: protein <χi) SEQUENCE DESCRIPTION : SEQ ID NO?2&5 f Pro <31u Ala Ala Glu Met Trp Phe Leu Arg Pro Arg Leu Leu Gly Asp 1 5 10 15 Gly Gly Ser Trp Val Arg 20 (2) INFORMATION FOR SEQ ID NO:286: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 16 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:286: Val Arg Cyβ Arg Tyr Ser Asp Asp Glu Ala Pro Arg Gly Arg Pro Gly 1 5 10 15 (2) INFORMATION FOR SEQ ID NO:287: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 12 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:287: Trp Arg Cys Gly Val Gin Gly Asp Asn Ala Gin Gly 1 5 10 (2) INFORMATION FOR SEQ ID NO:288: (i) SEQUENCE CHARACTERISTICS: 364 (A) LENGTH: 18 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:288: Ala Pro Gin He Hiβ Arg Ser Ala Arg Cyβ Gly Aβn Leu Leu Arg Arg 1 5 10 15 (2) INFORMATION FOR SEQ ID NO:289: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:289: Pro Gin Hiβ Gin Leu Pro Ser Aep 1 5 (2) INFORMATION FOR SEQ ID NO:290: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 25 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:290: Gly Gly Gly Leu Leu Ala Cyβ Ala Glu Val Pro Val Arg Leu Cyβ Ale 1 5 10 15 Pro Ser Ala Pro Arg Lye Aen Ser Arg 20 25 365 (2) INFORMATION FOR SEQ ID NO:291: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 50 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:291: Ala Cyβ Glu Cyβ Met Ser Ser Trp Glu Val Ser Ala Pro Val Arg Lye 1 5 10 15 Leu Gly Ser Arg Trp Val Leu Arg Pro Arg Val Hiβ Gin Val Gin Leu 20 25 30 Ala Glu Asp Leu Arg Ser Gly Cys Val Ser Trp Val Cys Phe Arg Phe 35 40 45 Pro Trp 50 (2) INFORMATION FOR SEQ ID NO:292: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:292: Ser Gin Arg Leu Hiβ Pro Cyβ 1 5 (2) INFORMATION FOR SEQ ID NO:293: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein 366 ( i) SEQUENCE DESCRIPTION: SEQ ID NO:293: Arg Gin Gin Thr Ala Gly Leu Gin Trp Ser Ala Lys Val Phe Ala Gly 1 5 10 15 Leu Val Ala Tyr 20 (2) INFORMATION FOR SEQ ID NO:294: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 12 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:294: His Gly Pro Gly Pro Val Gly Gly Asp Glu Val Gly 1 5 10 (2) INFORMATION FOR SEQ ID NO:295: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 32 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:295: Ser Cyβ Pro Pro Val Tyr Ala Gly Aen Val Val Val Val Glu Trp Ser 1 5 10 15 He Cyβ Cyβ Hiβ Tyr Cyβ Hiβ Hiβ Thr Pro Tyr Cyβ Hiβ Glu Val Hiβ 20 25 30 (2) INFORMATION FOR SEQ ID NO:296: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 45 amino acidβ (B) TYPE: amino acid 367 (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:296: Lys Cys Ser He Val Asp Ser Ala Hie Cys Ser Aβn Ser He Leu Pro 1 5 10 15 Glu Phe Tyr Hiβ Arg Ser Arg Gly Leu Tyr Leu Gin Cyβ Trp Leu Leu 20 25 30 Hiβ Gly Gly Arg Pro Gly Gly Arg Gly Ser Gly Gly Leu Gly Cyβ Cyβ 35 40 45 Gin (2) INFORMATION FOR SEQ ID NO:297: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 104 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:297: Trp Cyβ Ser Gly Arg Arg Trp Trp His Leu Ala Arg Val Ala Gin Ala 1 5 10 15 Ala Lys Leu Arg Cys Arg Ser Gly Leu Val Val Lys Cys Trp Gly Leu 20 25 30 Leu Ala Gly Arg Arg Gly Arg Xaa Gly Ser Arg Ala Gly Val His Pro 35 40 45 Gly Gly Arg Leu Gly Ser Pro Gly Val Val Val Hiβ Trp Leu Ser Gly 50 55 60 Cys Aep Val Cye Arg Gly Val Pro Glu Cye Pro Gly Leu Cye Xaa Gly 65 70 75 80 Cys Arg Ala Cys Gly Asp Ala Leu Arg Lys Gly Cys Ser Ala Ala Gly 85 90 95 He Gly Gly Ser Cys Arg Gly Xaa Pro Gly Ala Ala Gin Arg Leu Arg 100 105 110 Ala 368 (2) INFORMATION FOR SEQ ID NO:298: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 105 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:298: Gly Val Leu Arg Ser Gly Trp Trp Arg Leu Ala Xaa Arg Gin Leu Val 1 5 10 15 Leu Gly Phe Ser Arg Arg Gly Glu Leu Gly Pro Pro Gly Gly Gly Ser 20 25 30 Asp Asp Pro Arg Trp Pro He Ser Gin Xaa Asp Leu Val Xaa Gin Val 35 40 45 Gly Arg Gin Leu Xaa Glu Gly Ser Xaa Val Gly Glu Gin Leu Thr Gly 50 55 60 Trp Ser Xaa Trp Xaa Leu Xaa Ala Xaa Leu Glu Ser Xaa Val Xaa Xaa 65 70 75 80 Gly Leu Val Leu Pro Pro Aep Ser Cyβ His Ser Xaa Arg His Leu His 85 90 95 Thr Leu Phe Glu Gin Phe Arg Cys 100 105 (2) INFORMATION FOR SEQ ID NO:299: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 7 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:299: Phe Hie Leu Gly Xaa Thr Leu Gly 1 5 (2) INFORMATION FOR SEQ ID NO:300: (i) SEQUENCE CHARACTERISTICS: 369 (A) LENGTH: 16 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:300: Leu Thr Lye Ser Arg Ala Leu Gly Ala Xaa Ala Gly Leu Leu Ser Ser 1 5 10 15 Xaa (2) INFORMATION FOR SEQ ID NO:301: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:301: Gly Ala Ala Gly Leu Leu Leu Ala Gly Gly Arg Pro Ala Gin Ala Gly 1 5 10 15 Arg Pro Pro Leu Arg Ala Arg Xaa Ser His 20 25 (2) INFORMATION FOR SEQ ID NO:302: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 17 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:302: Gin Ala Arg Cyβ Cyβ Pro Leu Ala Arg Val Gly Xaa Cyβ Ala Xaa Ala 1 5 10 15 Xaa 370 (2) INFORMATION FOR SEQ ID NO:303: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 163 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:303: Xaa Aβn Gin Gly Arg Leu Xaa Xaa Cyβ Ser Gly Leu Cye Ser Cys Val 1 5 10 15 Gly Leu Trp Thr He Gly Pro Trp Glu Thr Ser Gly Arg Glu Ala Arg 20 25 30 Arg Arg Gly Val Aep Arg Leu Cyβ Glu Gin Ser Val Arg Pro Ser Ala 35 40 45 Trp Leu Cye Ser Hie Cye Ser Arg Gly Xaa Ser Ser Xaa Xaa Gin Xaa 50 55 60 Xaa Xaa Xaa Gly Cyβ Glu Asp Xaa Hiβ Aep Arg Gin Gly Pro Val Arg 65 70 75 80 Thr Pro Arg Xaa Arg Gly Gly Pro Xaa Aep Phe Asn Asn Xaa Phe His 85 90 95 Gly Leu Leu Arg Glu Arg Ser Ser Val Hiβ Xaa He Pro Trp Xaa Gin 100 105 110 Arg Pro Xaa Xaa Gly Gly Ala Xaa Trp Xaa Xaa Gin Xaa Ser Val Val 115 120 125 Val Xaa Glu Xaa Arg Arg Hiβ Gly Xaa Pro Ala Pro Xaa Trp Xaa Phe 130 135 140 145 Leu Pro Xaa Xaa Xaa Xaa Val Pro Thr Asn Trp Gly Val Gly Aep Pro 150 155 160 Glu (2) INFORMATION FOR SEQ ID NO:304: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 18 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein 371 (xi) SEQUENCE DESCRIPTION: SEQ ID NO : 304 : Arg Ser Ser Leu Pro Trp Aβn Ser Arg Gin Gly Gly Gly Phe Arg Tyr 1 5 10 15 Ala Arg (2) INFORMATION FOR SEQ ID NO:305: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:305: Val Val Arg Leu Ser Arg Val Phe Trp He Thr Aβn Leu Val Arg 1 5 10 15 (2) INFORMATION FOR SEQ ID NO:306: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:12 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:306: Gly Ser Cye Cyβ Trp Hiβ Ala Aep Phe Gly Ala Ser 1 5 10 (2) INFORMATION FOR SEQ ID NO:307: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 17 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein 372 (xi) SEQUENCE DESCRIPTION : SEQ ID NO: 307 : Gly Phe Leu Gly Ala Val Tyr Gin Thr Leu Gly Asn Ser Pro Ser Gly 1 5 10 15 Asp (2) INFORMATION FOR SEQ ID NO:308: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 33 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:308: Gly Ser He Gly Gly Pro Pro Cyβ Ala Arg Aβn His Trp He Gin Gly 1 5 10 15 Gly Ala Thr Val Pro Ala His Arg Ser Trp Gin Val Asp Ala Arg Ala 20 25 30 Glu (2) INFORMATION FOR SEQ ID NO:309: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 39 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:309: Val Arg Gin Gly Trp Thr Gin Xaa Ala Cys Thr Lys Pro He His Cys 1 5 10 15 His Ser Glu Gly Hie Gly Pro Leu Hiβ Gly Lye Val Aβn Arg Gin Thr 20 25 30 373 Ser Val Gly Val Leu Trp Pro 35 (2) INFORMATION FOR SEQ ID NO:310: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:310: His Tyr Cys He Phe Gin Asp Tyr 1 5 (2) INFORMATION FOR SEQ ID NO:311: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 71 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:311: Leu He Phe Aep Leu Leu Tyr He Arg Gin Val Tyr Gly Gin Ser Gin 1 5 10 15 Glu He Leu Ala Gly Glu Arg Arg Arg Asn Leu Arg Arg Val Ala Arg 20 25 30 His Arg Pro Asp Leu Asn Phe Gly Asp Gly Ser Gly Glu Val Thr Arg 35 40 45 Ser Arg Val Arg Arg Thr Pro Pro Ala Phe Arg Tyr Gly Asp Pro Thr 50 55 60 Gly Leu Ser Asp Gly Glu Ala 65 70 (2) INFORMATION FOR SEQ ID NO:312; 374 (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 5 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:312: Gly Asp Val Gly Gin 1 5 (2) INFORMATION FOR SEQ ID NO:313: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 13 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:313: Gly Gly Gly Pro Leu Leu Leu Pro He Pro Pro Thr Glu 1 5 10 (2) INFORMATION FOR SEQ ID NO:314: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 17 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:314: Val Cye Tyr Trp Glu Thr Pro Ala Val Leu Ser Phe Gin Gly Arg Xaa 1 5 10 15 (2) INFORMATION FOR SEQ ID NO:315: 375 ( i) SEQUENCE CHARACTERISTICS : (A) LENGTH : 22 amino acidβ (B) TYPE : amino acid (D) TOPOLOGY : linear ( ii) MOLECULE TYPE : protein (xi) SEQUENCE DESCRIPTION : SEQ ID NO : 315 : Val He Leu Ser Phe Gly Gin Leu Trp Cys Gin His Arg Cys Val Leu 1 5 10 15 Gin Arg Gin Arg Asn 21 (2) INFORMATION FOR SEQ ID NO:316: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:316: 1 (2) INFORMATION FOR SEQ ID NO:317: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 16 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:317: Arg Val Arg Leu Arg Hiβ Arg Arg Thr Phe Hiβ Trp Leu Hiβ Trp Gin Phe 1 5 10 15 (2) INFORMATION -FOR SEQ ID NO:318: 376 (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:9 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:318; Hiβ Arg Aβn Arg Leu Trp Phe Aβn Gly 1 5 (2) INFORMATION FOR SEQ ID NO:319: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 30 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:319: Gly Gly Ser Gly Ser Aep Pro Gly Pro Aep Hiβ Hiβ Tyr Arg Cyβ Glu 1 5 10 15 Aep Arg Pro Gly Pro Cyβ Arg Thr Glu Gly Ser Glu Ala Trp 20 25 30 (2) INFORMATION FOR SEQ ID NO:320: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:320: Val Trp Pro Trp Glu Ser Gly Hiβ Leu Leu Ser Gly He Aep Val Phe 1 5 10 15 Gly Ala Gly Gly Aβn Xaa Ser Val Trp Gly Ser Leu Gly Ser Cye 20 25 30 377 (2) INFORMATION FOR SEQ ID NO:321: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 17 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:321: Gly Trp Xaa Leu Val Val Trp Pro Arg Ala Arg Cys Tyr Trp Arg Pro 1 5 10 15 Ala (2) INFORMATION FOR SEQ ID NO:322: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 56 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:322: Gly Leu Arg Leu Val Ser Leu Tyr Cys Cys Hiβ Gin Cyβ Val Hie Arg 1 5 10 15 Arg Gly Hie Cye Leu Phe Tyr Trp Xaa Ser Ala Aen Glu Glu Leu Ser 20 25 ~ 30 Ser Gly Gly Leu Gly Gin Ala Glu Gly Xaa Gin Leu Ala Thr Leu Gly 35 40 45 Gly Cye Ala Glu Ala Hie Val 50 55 (2) INFORMATION FOR SEQ ID NO:323: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:8 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear 378 (ii) MOLECULE TYPE : protein (xi) SEQUENCE DESCRIPTION : SEQ ID NO : 323 ; Gly Arg Gly Leu Trp Ser Xaa Arg 1 5 (2) INFORMATION FOR SEQ ID NO:324: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:324; Trp Ser Arg Met Glu Arg Hie Gin Gly Lys Arg Ala Cye Ser Pro Val 1 5 10 15 Val Pro Met Gly Trp 20 (2) INFORMATION FOR SEQ ID NO:325: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:325: Val Gly Gly Ser Ala Ser Leu Gly 1 5 (2) INFORMATION FOR SEQ ID NO:326: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 51 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear 379 (ii) MOLECULE TYPE : protein (xi) SEQUENCE DESCRIPTION : SEQ ID NO -.326 : Pro Thr Gly Pro Ala Arg Cyβ Gly Arg Gly Leu His Ser Leu Hie Cyβ 1 5 10 15 Trp Thr Gly Ala Phe Gly Arg Phe Gly Asp Gly Gly Gly Gly Tyr Pro 20 25 30 Gly Thr Leu Aep Gly Val Ser Gly Cyβ Ser Asp Gin Leu Gly Cys Gin 35 40 45 Trp Glu Arg 50 (2) INFORMATION FOR SEQ ID NO:327: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 7 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:327: Pro Ala Asp Thr Lys Arg Leu 1 5 (2) INFORMATION FOR SEQ ID NO:328: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 15 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:328: Gly Arg Gly Xaa Xaa Arg Ser He Pro Ser Thr Pro Arg Trp Trp 1 5 10 15 (2) INFORMATION FOR SEQ ID NO:329: 380 (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 10 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:329: Thr Val Pro He Arg His Gin Ala Asn Xaa 1 5 10 (2) INFORMATION FOR SEQ ID NO:330: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:330: Gly Cys Asp His Pro 1 5 (2) INFORMATION FOR SEQ ID NO:331: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 18 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:331: Asp Cyβ Val Arg Xaa Gly Pro Ser Arg Gly Xaa Ser Gly Leu Cys Glu 1 5 10 15 Gly Leu (2) INFORMATION FOR SEQ ID NO:332: 381 (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 6 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:332: 1 5 (2) INFORMATION FOR SEQ ID NO:333: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 38 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:333: Gin Xaa Glu Cye Cyβ Val Ala Gly Leu Gly Cyβ Lye Gin Leu Cyβ Ala 1 5 10 15 Ser Thr Ser He Thr Leu Aen Phe Leu Val Xaa Glu Leu Gly Xaa Cyβ 20 25 30 Val His Phe Ser Leu Gly 35 (2) INFORMATION FOR SEQ ID NO:334: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 78 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:334: Arg Val Hiβ Ser Arg Pro Phe Leu Ala Cyβ Trp Val Hiβ Ser Cyβ Leu 1 5 10 15 382 Arg Arg Ser Ala Glu Pro Thr Ala Gly Arg Arg Ser Leu Phe Leu Ala 20 25 30 Gly Hiβ Val He Glu Pro Xaa Xaa Ser Arg Gin Thr Cyβ Cys Cye Val 35 40 45 Ala Pro Arg Arg Arg Gly Tyr Arg Pro Arg His Ala Cys Tyr Trp Ala 50 55 60 Cys Tyr Gly Gly Cys Leu LeuArg Xaa Gly Gin Arg Tyr Arg 65 70 75 (2) INFORMATION FOR SEQ ID NO:335: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 70 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:335: Leu Ala Glu Tyr His Cys Gly Ser Asn Arg Arg Leu Gly Gly Gly Xaa 1 5 10 15 Xaa Arg Ser Leu Thr His Leu Arg Xaa Pro Gly Xaa Glu Val Thr Ser 20 25 30 Xaa Xaa Xaa Leu Val Pro Xaa Gin Xaa Xaa Gly Leu Ser Gly Gly Phe 35 40 45 Gly Gly Xaa Cyβ Gly Xaa Xaa Xaa Xaa Ala Xaa Val Cys Gin Xaa Gly 50 55 60 65 70 (2) INFORMATION FOR SEQ ID NO:336: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 18 amino acids (B) TYPE: arαino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein 383 (Xi) SEQUENCE DESCRIPTION : SEQ ID NO : 336 : Gin Xaa Val Asp Asp Aep Ala Thr Gin Phe Gly Aep Ala 1 5 10 (2) INFORMATION FOR SEQ ID NO:337: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:6 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:337: Arg Phe Leu Pro Gin Arg 1 5 (2) INFORMATION FOR SEQ ID NO:338: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:338: Val Arg His Gin Gly Val Tyr Cys Pro Ala Lye Val Val He Val Lye 1 5 10 15 Met Aep His Asp Ser Cyβ Gly Gin Ala Gly Aep Gly Aep Gly Aep Xaa 20 25 30 Arg Phe Ser Aep Cyβ Leu Gly Leu Ala 35 40 (2) INFORMATION FOR SEQ ID NO:339: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 11 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear 384 ( ii) MOLECULE TYPE : protein (xi) SEQUENCE DESCRIPTION : SEQ ID NO : 339 ; Leu Val Hiβ Pro Ala Xaa Ser Val Pro Val Gin 1 5 10 (2) INFORMATION FOR SEQ ID NO:340: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 6 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:340 Thr Xaa Val Cye Ser Pro 1 5 (2) INFORMATION FOR SEQ ID NO:341: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 34 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:341: Val Ala Pro Ala Ala Tyr Arg Leu Gin Tyr Arg Leu Gly Trp Pro Val 1 5 10 15 Gly Gly Gin Trp Ser Phe Gly Aβn Lye Val Tyr Leu Trp Leu Cye Aep 20 25 30 Tyr Arg (2) INFORMATION FOR SEQ ID NO:342: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 32 amino acidβ (B) TYPE: amino acid 385 (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:342: Tyr Ser Arg Trp Tyr He Ala Arg Pro Thr Leu Tyr Leu Pro Thr Val 1 5 10 15 Gin Thr Leu Leu Gin Glu Asp Ser Ala Cys Trp Arg His Gly Gin Cys 20 25 30 (2) INFORMATION FOR SEQ ID NO:343: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:343: Gly Ser Ser Pro Pro Cyβ Ala Tyr Trp Arg Trp Asn Gin Asp Leu Pro 1 5 10 15 Asn Trp Asp Phe 20 (2) INFORMATION FOR SEQ ID NO:344: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 16 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:344: Gly Cys Gly Arg Ala Trp Asp Asn Hiβ Gly Ala Arg Hiβ Gin Leu Leu 1 5 10 15 (2) INFORMATION FOR SEQ ID NO:345: 386 (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:345; Val Glu Ser Cys 1 (2) INFORMATION FOR SEQ ID NO:346: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 47 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:346: Arg Ser Glu Gly Gly Ala Ser Arg Pro Aep Leu Arg Trp Trp Arg Thr 1 5 10 15 Leu Gin Leu Glu Arg Ala Val Tyr Cys Ala Cys Ala Arg Leu Gin Ala 20 25 30 Arg Pro Gly Hiβ Gin Aβn Arg Trp Ser Ala Pro Thr Val Ala Leu 35 40 45 (2) INFORMATION FOR SEQ ID NO:347: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 16 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:347: Leu Ser Thr Gly Ser Ala Pro Pro Pro Gly He Trp Gin Cye Cye Arg 1 5 10 15 387 (2) INFORMATION FOR SEQ ID NO:3 8: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:348: Trp Leu Asp Arg 1 (2) INFORMATION FOR SEQ ID NO:349: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 51 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:349: Gly Arg Glu Gly Leu Gly Gly Aen Gin Gly Cys Arg Hie Arg Gly His 1 5 10 15 Trp Gly Gly Leu Ala Pro Pro Phe Thr Gly Gly Cys Ser Gly Arg Ser 20 25 30 Arg Gly Phe Gly Gly Gly Cye Arg Val Pro Val Ala Pro Cyβ Ala Arg 35 40 45 50 (2) INFORMATION FOR SEQ ID NO:350: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 5 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear 388 (ii) MOLECULE TYPE : protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO : 350 ; Leu Phe Met Pro Gly 1 5 (2) INFORMATION FOR SEQ ID NO:351: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 17 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:351: Gly Val Pro Arg Pro Leu Hie Pro Arg Thr Gin Cyβ Asp Arg Gly Thr 1 5 10 15 (2) INFORMATION FOR SEQ ID NO:352: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 30 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:352: Ala Hiβ Gly Arg Arg Arg Gly Gly Thr GlnAla Ala Gly Cye Arg Pro Aep 1 5 10 15 Arg Gin Val Ala Arg Leu Gly Gly Hiβ Gly Ser Arg Pro Arg 20 25 30 (2) INFORMATION FOR SEQ ID NO:353; 389 (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 30 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:353: Val Asn Arg Gly Cys Ser Arg- Ser Phe Asp Ala Phe Ala Hiβ Arg Gly 1 5 10 15 Gly Leu Asn Ala He He Gly Val Glu Pro Leu Leu Leu Leu 20 25 30 (2) INFORMATION FOR SEQ ID NO:354: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 5 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:354: Thr Asn Leu Phe Asn 1 5 (2) INFORMATION FOR SEQ ID NO:355: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 33 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:355: Asp Cyβ Arg Arg Gly Trp Leu Thr Leu Gly Val Arg Glu Leu Gin Hiβ 1 5 10 15 Arg Ala Val Ser Gly Ser Glu Aep Cye Gin Aβn Pro Thr Gly Leu Leu 20 25 30 390 Leu (2) INFORMATION FOR SEQ ID NO:356: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 22 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:356: Gin He Hie Aβn Glu Gly His Ala Val Val Val His Cys Arg Gly Val 1 5 10 15 Pro Leu Arg Tyr Ser Leu 20 (2) INFORMATION FOR SEQ ID NO:357: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 7 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:357: Pro Gly Arg Ser Pro Thr Val 1 5 (2) INFORMATION FOR SEQ ID NO:358: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 12 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:358: 39Ϊ Arg Ala Arg Ser Aep Arg <31y He Tyr Se Tyr" Met 1 5 10 (2) INFORMATION FOR SEQ ID NO:359: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:359: Ser Aap Trp Gly His Gin Ala Ser Val 1 5 (2) INFORMATION FOR SEQ ID NO:360: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 35 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:360: Gly Aβn Ser Aen He Leu Leu Leu Hiβ Leu Val Arg Gly Ala Leu Gly 1 5 10 15 Tyr Trp Glu Lye Cyβ Pro Pro Thr Hiβ Aep Ala Pro Tyr Arg Aep Pro 20 25 30 Ser Aep Leu 35 (2) INFORMATION FOR SEQ ID NO:361: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 7 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein 392 (xi) SEQUENCE DESCRIPTION : SEQ ID NO : 361 : His Tyr Gin Ser Leu Cys Tyr 1 5 (2) INFORMATION FOR SEQ ID NO:362: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 10 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:362: Ala Gly Arg Glu Gly Tyr Asn Leu Glu Gly 1 5 10 (2) INFORMATION FOR SEQ ID NO:363: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:363: Gly Cyβ Pro Glu Lye Gly Ser Arg Asp Glu Val Ser Trp Leu Asp Leu 1 5 10 15 Phe Pro Gly Tyr Ser 20 (2) INFORMATION FOR SEQ ID NO:364: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 53 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear 393 (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:364: Ala Pro Ser Ser Arg Trp He Arg Gin Gin Gly Asp Arg Leu His He 1 5 10 15 Gly Hiβ Trp Leu Ala Ser Arg Gly Gly Aep Ala Gly Gin Aβn Ser Gin 20 25 30 Gly Thr Gly Ser Ser Phe His Phe Cyβ Asp Gin Ala Arg Gly Phe Leu 35 40 45 50 (2) INFORMATION FOR SEQ ID NO:365: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 15 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:365: Ala Pro Lye He Hiβ Ser Phe Pro Thr Phe Gly Leu Gin Aep Ser 1 5 10 15 (2) INFORMATION FOR SEQ ID NO:366: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 5 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:366: 394 Lye Asp Asp Ser Gly 1 5 (2) INFORMATION FOR SEQ ID NO:367: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 10 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:367; Pro Arg Hiβ Arg Cyβ Lye Val Aβn Ser Gly 1 5 10 (2) INFORMATION FOR SEQ ID NO:368: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 16 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:368: Arg Leu Ser Val Pro Val Hiβ Ala Gin Ser Glu Gly Gin Ser Ser Gly 1 5 10 15 (2) INFORMATION FOR SEQ ID NO:369: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:369; Gly Val Gly Gly Glu Val Ala Ser Arg Cyβ Aep Hie Cys Gly Arg His 395 1 5 10 15 Leu Phe Arg Leu He 20 (2) INFORMATION FOR SEQ ID NO:370: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:13 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:370: Ala Arg Hiβ Ala Gly Gly Gly Phe Gly Val Cys Gly Gly 1 5 10 (2) INFORMATION FOR SEQ ID NO:371: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 30 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:371: Gin Pro Leu Asn Gly Thr Cys Phe Val Gin Val Leu Leu Trp Trp Pro 1 5 10 15 Tyr Gly Phe Pro Arg Trp Gly Ser Leu Gly Val Pro Pro Val 20 25 30 (2) INFORMATION FOR SEQ ID NO:372: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:7 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear 396 (ii) MOLECULE TYPE : protein (xi) SEQUENCE DESCRIPTION : SEQ ID NO : 372 ; Val Val Gly Arg Val Asn Asn 1 5 (2) INFORMATION FOR SEQ ID NO:373: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:373: Leu Gly Glu Gin Hie Hie Leu Leu Hie 1 5 (2) INFORMATION FOR SEQ ID NO:374: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 10 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:374: Gly Gin Arg Gly Leu Gin Ala Gly Gly Aep 1 5 10 (2) INFORMATION FOR SEQ ID NO:375: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear 397 (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:375: Gly Thr He He Leu Tyr Ser Trp Arg 1 5 (2) INFORMATION FOR SEQ ID NO:376: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 5 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:376: Leu Leu Aep Hie Leu 1 5 (2) INFORMATION FOR SEQ ID NO:377: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:377: 1 5 (2) INFORMATION FOR SEQ ID NO:378: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 10 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear 398 (ii) MOLECULE TYPE : protein (xi) SEQUENCE DESCRIPTION : SEQ ID NO: 378 : Gly Cyβ Pro Gly Gin Leu Trp He Gin Val 1 5 10 (2) INFORMATION FOR SEQ ID NO:379: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 15 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:379: Thr Aβn Lye Ala Cyβ Phe Thr Gly Hiβ Ser 1 5 10 (2) INFORMATION FOR SEQ ID NO:380: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 7 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:380: Val Leu Leu Gly Leu Leu Gly 1 5 (2) INFORMATION FOR SEQ ID NO:381: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 66 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein 399 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:381: Val Arg Ser Trp Gly Cys Gin Ala Leu Val Val Glu His Gly His Glu 1 5 10 15 Glu Ala Ala Arg Lys Gly Val Phe Arg He Phe Gly Pro Asn Arg Gin 20 25 30 Cys Phe Arg Asp His Leu Aep Val Ser Pro Ala Ser Aβn Arg Ala Val 35 40 45 Cyβ Ser Aen Thr Thr Arg Thr Asn Asn Gly Leu Gin Glu Trp Gin Hie 50 55 60 Thr Gly 65 (2) INFORMATION FOR SEQ ID NO:382: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 39 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:382: Val Gly Tyr Val Ser Gly Ser Gly Lye Ser Leu Leu Phe Pro Ala Ala 1 5 10 15 Ala Ala Ala Ser Arg Leu Gly Leu Ser Thr Trp Ser Val Val Pro Thr 20 25 30 Ser Hiβ Hiβ Gly Gin Tyr Glu 35 (2) INFORMATION FOR SEQ ID NO:383: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 61 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:383: 400 Asp Gly Gly Arg Leu Ser Xaa Ala Gly Phe Arg Asn Glu He Pro Ser 1 5 10 15 Leu Ala Pro Pro Thr Cyβ Arg Lys Cys Ala His Ser Pro Pro Glu Gly 20 25 30 Arg Gin Gly Val Gly Ala Pro Gly Gin Ser Pro Pro Leu Ala Xaa Arg 35 40 .45 Xaa Glu Gly Ala Xaa Pro Xaa Hiβ Lye Phe Thr Ser Arg Phe Ser Ala 40 45 50 Gly Aep Ala Leu Arg Thr Pro 55 60 (2) INFORMATION FOR SEQ ID NO:384: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:41 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:384: Arg Gly Leu Aep Leu Aep Gin Glu Ser Thr Thr Leu Aep Lye Val Aep 1 5 10 15 Ser Trp Cys Leu Ser Leu Val Ala Gly Arg Leu Ala Val Aen Ser Leu 20 25 30 Gin Ala Val Gly Pro Ser Gly Arg Gly 355 40 (2) INFORMATION FOR SEQ ID NO:385: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9493 base paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (ix) FEATURE: (A) NAME/KEY: CDS 401 (B) LOCATION: 3..9493 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:385: CG TGG GAG TCC GGG GCC CCG GAC CTC CCA CCG AGG TGG GGG GAA AGG 47 Trp Glu Ser Gly Ala Pro Asp Leu Pro Pro Arg Trp Gly Glu Arg 1 5 10 15 GGC CCT GGA CCG GCC GGG TGG AAG GCC CGG AAC CGG TCC ATC TTC CTC 95 Gly Pro Gly Pro Ala Gly Trp Lys Ala Arg Asn Arg Ser He Phe Leu 20 25 30 AAG GTT GAG GAA GGG GTA CGT CTA TCG GTC CGG TCG GTC CGA AAG GCG 143 Lys Val Glu Glu Gly Val Arg Leu Ser Val Arg Ser Val Arg Lys Ala 35 40 45 TCT GGA TGC CTA GTG TTA GGG TTC GTA GGT GGT AAA TCC CAG CTA GGC 191 Ser Gly Cys Leu Val Leu Gly Phe Val Gly Gly Lys Ser Gin Leu Gly 50 55 60 GTG AAA GCG CTA TAG GAT AGG CTT ATC CCG GTG ACC GCT GCC CCG GAA 239 Val Lys Ala Leu * Asp Arg Leu He Pro Val Thr Ala Ala Pro Glu 65 70 75 CCA GCC CCG CGG KTC TTT GGA CAC GGT CCA CAG GTT GGG GGT ACC GGT 287 Pro Ala Pro Arg Xaa Phe Gly His Gly Pro Gin Val Gly Gly Thr Gly 80 85 90 95 GTG AAT AAC CCC CCG ACT GAA GCG TCA GTC GTT AAA CGG AGA CGG TCT 335 Val Asn Asn Pro Pro Thr Glu Ala Ser Val Val Lys Arg Arg Arg Ser 100 105 110 CCT GAG ATC GCA ACG ACG CCC CAC GTA CGG GAA CGC CGC CAA AAC CTT 383 Pro Glu He Ala Thr Thr Pro His Val Arg Glu Arg Arg Gin Asn Leu 115 120 125 CGG GAC AGC TAT GCG GGT TGA CAA TCC CAG TGG GGG GCC GGG GAC CAG 431 Arg Asp Ser Tyr Ala Gly * Gin Ser Gin Trp Gly Ala Gly Asp Gin 130 135 140 CTG ATT ACT TGT CCT GCG AGT TCC TCT TGA GAC TGG CCG AAA GGC AGC 479 Leu He Thr Cys Pro Ala Ser Ser Ser * Asp Trp Pro Lys Gly Ser 145 150 155 CAC GGG GCC ACC AAG GCG GCG CAG CGC TGC ATG CGG CAA GGG GAA AAA 527 His Gly Ala Thr Lys Ala Ala Gin Arg Cys Met Arg Gin Gly Glu Lys 160 165 170 175 TCC TTC GGG TGA CCC CTG GTG GCA ATC CCT TCC CTT AGG AGC ATG AGT 575 Ser Phe Gly * Pro Leu Val Ala He Pro Ser Leu Arg Ser Met Ser 180 185 190 GTG GTC GAC ACA TTC ACC ATG GCT TGG CTG TGG TTG CTG GTT TGC TTC 623 Val Val Aεp Thr Phe Thr Met Ala Trp Leu Trp Leu Leu Val Cye Phe 195 200 205 402 CCC CTC GCG GGG GGG GTG CTC TTC AAC TCG CGG CAC CAG TGC TTC AAT 671 Pro Leu Ala Gly Gly Val Leu Phe Aβn Ser Arg His Gin Cys Phe Asn 210 215 220 GGG GAC CAT TAT GTG CTT TCC AAT TGT TGT TCC CGA GAC GAG GTT TAC 719 Gly Asp His Tyr Val Leu Ser Asn Cys Cys Ser Arg Asp Glu Val Tyr 225 230 235 TTC TGT TTC GGG GAC GGA TGT CTG ' GTG GCT TAT GGC TGT ACT GTT TGC 767 Phe Cys Phe Gly Asp Gly Cys Leu Val Ala Tyr Gly Cys Thr Val Cys 240 245 250 255 ACA CAG TCT TGC TGG AAG CTC TAC CGG CCT GGG GTG GCT ACT CGG CCC 815 Thr Gin Ser Cys Trp Lys Leu Tyr Arg Pro Gly Val Ala Thr Arg Pro 260 265 270 GGG TCC GAA CCA GGT GAG CTG CTG GGG AGA TTT GGG AGT GTA ATT GGT 863 Gly Ser Glu Pro Gly Glu Leu Leu Gly Arg Phe Gly Ser Val He Gly 275 280 285 CCG GTG TCG GCT TCG GCT TAC ACC GCT GGA GTC CTC GGG TTG GGT GAA 911 Pro Val Ser Ala Ser Ala Tyr Thr Ala Gly Val Leu Gly Leu Gly Glu 290 295 300 CCT TAC AGT TTG GCC TTC TTG GGG ACG TTC CTC ACC AGT CGC CTC TCA 959 Pro Tyr Ser Leu Ala Phe Leu Gly Thr Phe Leu Thr Ser Arg Leu Ser 305 310 315 CGG ATT CCC AAC GTC ACC TGC GTG AAG GCT TGT GAC CTT GAG TTT ACC 1007 Arg He Pro Asn Val Thr Cys Val Lys Ala Cys Asp Leu Glu Phe Thr 320 325 330 335 TAC CCA GGC TTG TCC ATC GAT TTT GAC TGG GCG TTT ACC AAG ATC TTG 1055 Tyr Pro Gly Leu Ser He Asp Phe Asp Trp Ala Phe Thr Lys He Leu 340 345 350 CAG TTG CCG GCC AAG CTG TGG CGA GGC CTA ACG GCR GCW CCG GTC TTG 1103 Gin Leu Pro Ala Lys Leu Trp Arg Gly Leu Thr Xaa Xaa Pro Val Leu 355 360 365 AGC CTC CTC GTG ATC CTC ATG CTG GTC CTC GAG CAG CGC CTC CTG ATA 1151 Ser Leu Leu Val He Leu Met Leu Val Leu Glu Gin Arg Leu Leu He 370 375 380 GCC TTC CTA CTG CTT TTG GTA GTG GGC GAG GCT CAG AGG GGG ATG TTC 1199 Ala Phe Leu Leu Leu Leu Val Val Gly Glu Ala Gin Arg Gly Met Phe 385 390 395 GAC AAC TGC GTG TGT GGT TAC TGG GGG GGC AAG AGG CCC CCG TCG GTG 1247 Asp Asn Cys Val Cys Gly Tyr Trp Gly Gly Lys Arg Pro Pro Ser Val 400 405 410 415 ACC CCG CTG TAC CGT GGC AAC GGT ACT GTG GTG TGT GAC TGT GAT TTT 1295 Thr Pro Leu Tyr Arg Gly Asn Gly Thr Val Val Cys Asp Cys Asp Phe 420 425 430 GGA AAA ATG CAT TGG GCC CCC CCC TTG TGT TCC GGY CTG GTG TGG CGG 1343 403 Gly Lys Met His Trp Ala Pro Pro Leu Cys Ser Xaa Leu Val Trp Arg 435 ' 440 445 GAC GGT CAT AGG AGG GGC ACC GTG CGC GAC CTC CCC CCG GTT TGC CCC 1391 Asp Gly His Arg Arg Gly Thr Val Arg Asp Leu Pro Pro Val Cys Pro 450 455 460 CGG GAG GTT CTC GGC ACG GTG ACA GTC ATG TGT CAG TGG GGT TCT GCC 1439 Arg Glu Val Leu Gly Thr Val Thr Val Met Cys Gin Trp Gly Ser Ala 465 470 475 TAC TGG ATT TGG AGA TTT GGG GAC TGG GTT GCA TTG TAC GAC GAG CTA 1487 Tyr Trp He Trp Arg Phe Gly Asp Trp Val Ala Leu Tyr Asp Glu Leu 480 485 490 495 CCA CGA TCA GCT CTC TGT ACT TTC TTC TCA GGT CAT GGT CCA CAA CCT 1535 Pro Arg Ser Ala Leu Cys Thr Phe Phe Ser Gly His Gly Pro Gin Pro 500 505 510 AAA GAT CTC TCA GTC TTG AAT CCA TCC GGG GCA CCT TGT GCT TCT TGC 1583 Lys Asp Leu Ser Val Leu Asn Pro Ser Gly Ala Pro Cys Ala Ser Cys 515 520 525 GTC GTT GAC CAG AGG CCG CTG AAA TGT GGT TCC TGC GTC CGC GAC TGC 1631 Val Val Asp Gin Arg Pro Leu Lys Cys Gly Ser Cys Val Arg Asp Cys 530 535 540 TGG GAG ACG GGG GGT CCT GGG TTC GAT GAG TGC GGT GTC GGT ACT CGG 1679 Trp Glu Thr Gly Gly Pro Gly Phe Asp Glu Cys Gly Val Gly Thr Arg 545 550 555 ATG ACG AAG CAC CTC GAG GCC GTC CTG GTT GAT GGA GGT GTG GAG TCC 1727 Met Thr Lys His Leu Glu Ala Val Leu Val Asp Gly Gly Val Glu Ser 560 565 570 575 AAG GTG ACA ACG CCC AAG GGT GAG CGC CCC AAA TAC ATA GGT CAG CAC 1775 Lys Val Thr Thr Pro Lys Gly Glu Arg Pro Lys Tyr He Gly Gin Hie 580 585 590 GGT GTG GGA ACC TAC TAC GGC GCT GTC CGT AGC CTC AAC ATC AGT TAC 1823 Gly Val Gly Thr Tyr Tyr Gly Ala Val Arg Ser Leu Asn He Ser Tyr 595 600 605 CTA GTG ACT GAG GTG GGG GGC TAT TGG CAT GCG CTG AAG TGC CCG TGC 1871 Leu Val Thr' Glu Val Gly Gly Tyr Trp His Ala Leu Lys Cys Pro Cys 610 615 620 GAC TTT GTG CCC CGA GTG CTC CCA GAA AGA ATT CCA GGT AGG CCT GTG 1919 Asp Phe Val Pro Arg Val Leu Pro Glu Arg He Pro Gly Arg Pro Val 625 630 635 AAT GCA TGT CTA GCT GGG AAG TCT CCG CAC CCG TTC GCA AGT TGG GCT 1967 Aen Ala Cyβ Leu Ala Gly Lye Ser Pro Hie Pro Phe Ala Ser Trp Ala 640 645 650 655 CCC GGT GGG TTT TAC GCC CCC GTG TTC ACC AAG TGC AAC TGG CCG AAG 2015 Pro Gly Gly Phe Tyr Ala Pro Val Phe Thr Lye Cye Aβn Trp Pro Lye 404 660 665 670 ACC TCC GGA GTG GAT GTG TGT CCT GGG TTT GCT TTC GAT TTC CCT GGT 2063 Thr Ser Gly Val Asp Val Cys Pro Gly Phe Ala Phe Asp Phe Pro Gly 675 680 685 GAT CAC AAC GGC TTC ATC CAT GTT AAA GGC AAC AGA CAG CAG GTT TAC 2111 Asp His Asn Gly Phe He His Val Lys Gly Asn Arg Gin Gin Val Tyr 690 695 700 AGT GGT CAG CGA AGG TCT TCG CCG GCT TGG TTG CTT ACT GAC ATG GTC 2159 Ser Gly Gin Arg Arg Ser Ser Pro Ala Trp Leu Leu Thr Asp Met Val 705 710 715 CTG GCC CTG TTG GTG GTG ATG AAG TTG GCT GAG GCT AGA GTT GTC CCC 2207 Leu Ala Leu Leu Val Val Met Lys Leu Ala Glu Ala Arg Val Val Pro 720 725 730 735 CTG TTT ATG CTG GCA ATG TGG TGG TGG TTG AAT GGA GCA TCT GCT GCC 2255 Leu Phe Met Leu Ala Met Trp Trp Trp Leu Asn Gly Ala Ser Ala Ala 740 745 750 ACT ATT GTC ATC ATA CAC CCT ACT GTC ACG AAG TCC ACT GAA AGT GTT 2303 Thr He Val He He Hie Pro Thr Val Thr Lye Ser Thr Glu Ser Val 755 760 765 CCA TTG TGG ACT CCG CCC ACT GTT CCA ACT CCA TCT TGC CCG AAT TCT 2351 Pro Leu Trp Thr Pro Pro Thr Val Pro Thr Pro Ser Cye Pro Asn Ser 770 775 780 ACC ACC GGA GTC GCG GAC TCT ACC TAC AAT GCT GGT TGC TAC ATG GTG 2399 Thr Thr Gly Val Ala Asp Ser Thr Tyr Asn Ala Gly Cys Tyr Met Val 785 790 795 GCA GGC CTG GCG GCC GGG GCT CAG GCG GTC TGG GGT GCT GCC AAT GAT 2447 Ala Gly Leu Ala Ala Gly Ala Gin Ala Val Trp Gly Ala Ala Asn Asp 800 805 810 815 GGT GCT CAG GCC GTC GTT GGT GGC ATC TGG CCC GCG TGG CTC AAG CTG 2495 Gly Ala Gin Ala Val Val Gly Gly He Trp Pro Ala Trp Leu Lys Leu 820 825 830 CGA AGC TTC GCT GCC GGT CTG GCC TGG TTG TCA AAT GTT GGG GCT TAC 2543 Arg Ser Phe Ala Ala Gly Leu Ala Trp Leu Ser Asn Val Gly Ala Tyr 835 840 845 TTG CCG GTC GTC GAG GCC GCV CTG GCT CCC GAG CTG GTG TGC ACC CCG 2591 Leu Pro Val Val Glu Ala Xaa Leu Ala Pro Glu Leu Val Cys Thr Pro 850 855 860 GTG GTC GGC TGG GCA GCC CAG GAG TGG TGG TTC ACT GGT TGT CTG GGT 2639 Val Val Gly Trp Ala Ala Gin Glu Trp Trp Phe Thr Gly Cys Leu Gly 865 870 875 GTG ATG TGT GTC GTG GCG TAC CTG AAT GTC CTG GGC TCT GTR AGG GCT 2687 Val Met Cyβ Val Val Ala Tyr Leu Aen Val Leu Gly Ser Xaa Arg Ala 880 885 890 895 405 GCC GTG CTT GTG GCG ATG CAC TTC GCA AGG GGT GCT CTG CCG CTG GTA 2735 Ala Val Leu Val Ala Met Hie Phe Ala Arg Gly Ala Leu Pro Leu Val 900 905 910 TTG GTG GTA GCT GCC GGG GTR ACC CGG GAG CGG CAC AGC GTC TTA GGG 2783 Leu Val Val Ala Ala Gly Xaa Thr Arg Glu Arg Hiβ Ser Val Leu Gly 915 920 925 CTT GAG GTG TGC TTC GAT CTG GAT GGT GGA GAC TGG CCR GAC GCC AGT 2831 Leu Glu Val Cyβ Phe Aep Leu Asp Gly Gly Asp Trp Xaa Asp Ala Ser 930 935 940 TGG TCT TGG GGT TTA GCA GGC GTG GTG AGC TGG GCC CTC CTG GTG GGG 2879 Trp Ser Trp Gly Leu Ala Gly Val Val Ser Trp Ala Leu Leu Val Gly 945 950 955 GGT CTG ATG ACC CAC GGT GGC CGA TCA GCC AGA YTG ACT TGG TAY GCC 2927 Gly Leu Met Thr His Gly Gly Arg Ser Ala Arg Xaa Thr Trp Xaa Ala 960 965 970 975 AGG TGG GCC GTC AAT TAY CAG AGG GTT CGY CGG TGG GTG AAC AAC TCA 2975 Arg Trp Ala Val Asn Xaa Gin Arg Val Xaa Arg Trp Val Asn Asn Ser 980 985 990 CCG GTT GGA GCY TTT GGY CGT TGG MGG CGY GCC TGG AAA GCY TGG TTR 3023 Pro Val Gly Xaa Phe Xaa Arg Trp Xaa Xaa Ala Trp Lys Xaa Trp Xaa 995 1000 1005 GTK GTG GCT TGG TTC TTC CCC CAG ACA GTT GCC ACA GTY TCC GTC ATC 3071 Xaa Val Ala Trp Phe Phe Pro Gin Thr Val Ala Thr Xaa Ser Val He 1010 1015 1020 TTC ATA CTC TGT TTG AGC AGT TTA GAT GTC ATT GAT TTC ATC TTG GAR 3119 Phe He Leu Cys Leu Ser Ser Leu Asp Val He Asp Phe He Leu Xaa 1025 1030 1035 GTA CTC TTG GTT AAC TCA CCA AAT CTC GCG CGC TTG GCG CGR GTG CTG 3167 Val Leu Leu Val Aen Ser Pro Aen Leu Ala Arg Leu Ala Xaa Val Leu 1040 1045 1050 1055 GAC TCC TTA GCT CTH GCT GAG GAG CGG CTG GCC TGC TCT TGG CTG GTG 3215 Aep Ser Leu Ala Xaa Ala Glu Glu Arg Leu Ala Cye Ser Trp Leu Val 1060 1065 1070 GGC GTC CTG CGC AAG CGG GGC GTC CTC CTC TAC GAG CAC GCY GGT CAC 3263 Gly Val Leu Arg Lye Arg Gly Val Leu Leu Tyr Glu Hiβ Xaa Gly Hiβ 1075 1080 1085 ACT AGC AGG CGC GGT GCT GCC CGC TTG CGA GAG TGG GGY TTT GCG CTY 3311 Thr Ser Arg Arg Gly Ala Ala Arg Leu Arg Glu Trp Xaa Phe Ala Xaa 1090 1095 1100 GAG CCK GTT AGY ATA ACC AAG GAA GAT TGY GCY ATT GTT CGG GAC TCT 3359 Glu Xaa Val Xaa He Thr Lye Glu Asp Xaa Xaa He Val Arg Aep Ser 1105 1110 1115 GCT CGT GTG TTG GGC TGT GGA CAA TTG GTC CAT GGG AAA CCA GTG GTC 3407 406 Ala Arg Val Leu Gly Cyβ Gly Gin Leu Val His Gly Lys Pro Val Val 1120 1125 1130 1135 GCG AGG CGA GGC GAC GAG GTG TTG ATC GGC TGT GTG AAC AGT CGG TTC 3455 Ala Arg Arg Gly Asp Glu Val Leu He Gly Cys Val Asn Ser Arg Phe 1140 1145 1150 GAC CTT CCG CCT GGC TTT GTT CCC ACT GCT CCC GTG GTS CTT CAT CAR 3503 Asp Leu Pro Pro Gly Phe Val Pro Thr Ala Pro Val Xaa Leu His Xaa 1155 1160 1165 GCW GGC AAR GGR TTY TTY GGG GTT GTG AAG ACM TCC ATG ACA GGC AAG 3551 Xaa Gly Xaa Xaa Xaa Xaa Gly Val Val Lye Xaa Ser Met Thr Gly Lye 1170 1175 1180 GAC CCG TCC GAA CAC CAC GGR AAC GTG GTG GTC CTW GGG ACT TCA ACA 3599 Asp Pro Ser Glu His His Xaa Asn Val Val Val Xaa Gly Thr Ser Thr 1185 1190 1195 ACK CGT TCC ATG GGC TGC TGC GTG AAC GGA GTA GTG TAC ACR ACA TAC 3647 Xaa Arg Ser Met Gly Cyβ Cyβ Val Aen Gly Val Val Tyr Xaa Thr Tyr 1200 1205 1210 1215 CAT GGY ACC AAC GCC CGR CCK ATG GCG GGG CCK TTT GGK CCY GTC AAY 3695 Hie Xaa Thr Aβn Ala Xaa Xaa Met Ala Gly Xaa Phe Xaa Xaa Val Xaa 1220 1225 1230 GCT CGG TGG TGG TCW GCG AGY GAC GAC GTC ACG GTY TAC CCG CTC CCW 3743 Ala Arg Trp Trp Xaa Ala Xaa Aep Aep Val Thr Xaa Tyr Pro Leu Xaa 1235 1240 1245 AAT GGY GCT TCT TGC CTY CAR GCW TGY AAG TGC CAA CCA ACT GGG GTG 3791 Aβn Xaa Ala Ser Cyβ Xaa Xaa Xaa Xaa Lye Cye Gin Pro Thr Gly Val 1250 1255 1260 TGG GTG ATC CGG AAT GAC GGA GCT CTT TGC CAT GGA ACT CTC GGC AAG 3839 Trp Val He Arg Aβn Aep Gly Ala Leu Cyβ Hiβ Gly Thr Leu Gly Lye 1265 1270 1275 GTG GTG GAT TTA GAT ATG CCC GCT GAG TTG TCA GAC TTT CGC GGG TCT 3887 Val Val Aep Leu Aep Met Pro Ala Glu Leu Ser Aep Phe Arg Gly Ser 1280 1285 1290 1295 TCT GGA TCA CCA ATC TTG TGC GAT GAG GGT CAT GCT GTT GGC ATG CTG 3935 Ser Gly Ser Pro He Leu Cyβ Aep Glu Gly Hiβ Ala Val Gly Met Leu 1300 1305 1310 ATT TCG GTG CTT CAT AGG GGG AGT AGG GTT TCC TCG GTG CGG TAT ACC 3983 He Ser Val Leu Hiβ Arg Gly Ser Arg Val Ser Ser Val Arg Tyr Thr 1315 1320 1325 AAA CCT TGG GAA ACT CTC CCT CGG GAG ATT GAG GCT CGA TCG GAG GCC 4031 Lye Pro Trp Glu Thr Leu Pro Arg Glu He Glu Ala Arg Ser Glu Ala 1330 1335 1340 CCC CCT GTG CCA GGA ACC ACT GGA TAC AGG GAG GCG CCA CTG TTC CTG 4079 Pro Pro Val Pro Gly Thr Thr Gly Tyr Arg Glu Ala Pro Leu Phe Leu 407 1345 1350 1355 CCC ACC GGA GCT GGC AAG TCG ACG CGC GTG CCG AAT GAG TAC GTC AAG 4127 Pro Thr Gly Ala Gly Lys Ser Thr Arg Val Pro Asn Glu Tyr Val Lys 1360 1365 1370 1375 GCT GGA CAC AAR GTG CTT GTA CTA AAC CCA TCC ATT GCC ACA GTG AGG 4175 Ala Gly His Xaa Val Leu Val Leu Asn Pro Ser He Ala Thr Val Arg 1380 1385 1390 GCC ATG GGC CCT TAC ATG GAA AAG TTA ACC GGC AAA CAT CCG TCG GTG 4223 Ala Met Gly Pro Tyr Met Glu Lys Leu Thr Gly Lys His Pro Ser Val 1395 1400 1405 TAC TGT GGC CAT GAC ACT ACT GCA TAT TCC AGG ACT ACT GAC TCA TCT 4271 Tyr Cys Gly His Asp Thr Thr Ala Tyr Ser Arg Thr Thr Asp Ser Ser 1410 1415 1420 TTG ACC TAC TGT ACA TAC GGC AGG TTT ATG GCC AAT CCC AGG AAA TAC 4319 Leu Thr Tyr Cys Thr Tyr Gly Arg Phe Met Ala Asn Pro Arg Lys Tyr 1425 1430 1435 TTG CGG GGG AAC GAC GTC GTA ATT TGC GAC GAG TTG CAC GTC ACC GAC 4367 Leu Arg Gly Asn Asp Val Val He Cys Asp Glu Leu His Val Thr Asp 1440 1445 1450 1455 CCG ACC TCA ATT TTG GGG ATG GGT CGG GCG AGG TTA CTC GCT CGC GAG 4415 Pro Thr Ser He Leu Gly Met Gly Arg Ala Arg Leu Leu Ala Arg Glu 1460 1465 1470 TGC GGC GTA CGC CTC CTG CTT TTC GCT ACG GCG ACC CCA CCG GTC TCT 4463 Cye Gly Val Arg Leu Leu Leu Phe Ala Thr Ala Thr Pro Pro Val Ser 1475 1480 1485 CCG ATG GCG AAG CAT GAA TCT ATT CAT GAG GAG ATG TTG GGC AGT GAG 4511 Pro Met Ala Lye Hie Glu Ser He Hiβ Glu Glu Met Leu Gly Ser Glu 1490 1495 1500 GGG GAG GTC CCC TTC TAT TGC CAA TTC CTC CCA CTG AGT AGG TAT GCT 4559 Gly Glu Val Pro Phe Tyr Cyβ Gin Phe Leu Pro Leu Ser Arg Tyr Ala 1505 1510 1515 ACT GGG AGA CAC CTG CTG TTT TGT CAT TCC AAG GTA GAR TGC ACT AGG 4607 Thr Gly Arg Hie Leu Leu Phe Cyβ Hie Ser Lye Val Xaa Cyβ Thr Arg 1520 1525 1530 1535 TTA TCC TCA GCT TTG GCC AGC TTT GGT GTC AAC ACC GTT GTG TAC TTC 4655 Leu Ser Ser Ala Leu Ala Ser Phe Gly Val Aβn Thr Val Val Tyr Phe 1540 1545 1550 AGA GGC AAA GAA ACT GAC ATT CCA ACT GGT GAC GTG TGC GTT TGC GCC 4703 Arg Gly Lye Glu Thr Aep He Pro Thr Gly Aep Val Cyβ Val Cyβ Ala 1555 1560 1565 ACA GAC GCA CTT TCC ACT GGT TAC ACT GGC AAT TTT GAC ACC GTA ACA 4751 Thr Aep Ala Leu Ser Thr Gly Tyr Thr Gly Aβn Phe Aep Thr Val Thr 1570 1575 1580 408 GAC TGT GGT TTA ATG GTT GAG GAG GTA GTG GAA GTG ACC CTG GAC CCG 4799 Aep Cye Gly Leu Met Val Glu Glu Val Val Glu Val Thr Leu Aep Pro 1585 1590 1595 ACC ATC ACT ATC GGT GTG AAG ACC GTC CCG GCC CCT GCC GAA CTG AGG 4847 Thr He Thr He Gly Val Lys Thr Val Pro Ala Pro Ala Glu Leu Arg 1600 1605 1610 1615 GCT CAG AGG CGT GGT AGG TGT GGC CGT GGG AAA GCG GGC ACT TAC TAT 4895 Ala Gin Arg Arg Gly Arg Cye Gly Arg Gly Lye Ala Gly Thr Tyr Tyr 1620 1625 1630 CAG GCA TTG ATG TCT TCG GCG CCG GCG GGA ACS GTT CGG TCT GGG GCT 4943 Gin Ala Leu Met Ser Ser Ala Pro Ala Gly Xaa Val Arg Ser Gly Ala 1635 1640 1645 CTC TGG GCA GCT GTT GAG GCT GGH GTC TCG TGG TAT GGC CTA GAG CCC 4991 Leu Trp Ala Ala Val Glu Ala Xaa Val Ser Trp Tyr Gly Leu Glu Pro 1650 1655 1660 GAT GCT ATT GGA GAC CTG CTT AGG GCC TAC GAC TCG TGT CCT TAT ACT 5039 Aep Ala He Gly Aep Leu Leu Arg Ala Tyr Aep Ser Cye Pro Tyr Thr 1665 1670 1675 GCT GCC ATC AGT GCG TCC ATC GGA GAG GCC ATT GCC TTT TTT ACT GGY 5087 Ala Ala He Ser Ala Ser He Gly Glu Ala He Ala Phe Phe Thr Xaa 1680 1685 1690 1695 CTA GTG CCA ATG AGG AAT TAT CCT CAG GTG GTT TGG GCC AAG CAG AAG 5135 Leu Val Pro Met Arg Aβn Tyr Pro Gin Val Val Trp Ala Lys Gin Lys 1700 1705 1710 GGR CAC AAC TGG CCA CTC TTG GTG GGT GTG CAG AGG CAC ATG TGT GAG 5183 Xaa His Asn Trp Pro Leu Leu Val Gly Val Gin Arg Hie Met Cys Glu 1715 1720 1725 GAC GCG GGC TGT GGT CCK CCC GCT AAT GGT CCC GAA TGG AGC GGC ATC 5231 Asp Ala Gly Cys Gly Xaa Pro Ala Asn Gly Pro Glu Trp Ser Gly He 1730 1735 1740 AGG GGA AAA GGG CCT GTT CCC CTG TTG TGC CGA TGG GGT GGT GAC TTG 5279 Arg Gly Lys Gly Pro Val Pro Leu Leu Cys Arg Trp Gly Gly Asp Leu 1745 1750 1755 CCT GAG TCG GTG GCT CCG CAT CAC TGG GTT GAT GAC CTA CAG GCC CGG 5327 Pro Glu Ser Val Ala Pro Hiβ Hie Trp Val Aep Aep Leu Gin Ala Arg 1760 1765 1770 1775 CTC GGT GTG GCC GAG GGT TAC ACT CCC TGC ATT GCT GGA CCG GTG CTT 5375 Leu Gly Val Ala Glu Gly Tyr Thr Pro Cyβ He Ala Gly Pro Val Leu 1780 1785 1790 TTG GTC GGT TTG GCG ATG GCG GGG GGG GCT ATC CTG GCA CAC TGG ACG 5423 Leu Val Gly Leu Ala Met Ala Gly Gly Ala He Leu Ala Hiβ Trp Thr 1795 1800 1805 GGG TCT CTG GTT GTA GTG ACC AGT TGG GTT GTC AAT GGG AAC GGT AAC 5471 409 Gly Ser Leu Val Val Val Thr Ser Trp Val Val Aen Gly Aβn Gly Aβn 1810 1815 1820 CCG CTG ATA CAA AGC GCC TCT AGG GGC GTG GCK ACY AGC GGT CCA TAC 5519 Pro Leu He Gin Ser Ala Ser Arg Gly Val Xaa Xaa Ser Gly Pro Tyr 1825 1830 1835 CCA GTA CCC CCA GAT GGT GGT GAA CGG TAC CCA TCA GAC ATC AAG CCA 5567 Pro Val Pro Pro Aep Gly Gly Glu Arg Tyr Pro Ser Asp He Lys Pro 1840 1845 1850 1855 ATY ACT GAG GCT GTG ACC ACC CTT GAG ACT GCG TGC GGY TGG GGC CCA 5615 Xaa Thr Glu Ala Val Thr Thr Leu Glu Thr Ala Cys Xaa Trp Gly Pro 1860 1865 1870 GCC GCG GCB AGT CTG GCT TAT GTG AAG GCC TGT GAA ACT GGA ACC ATG 5663 Ala Ala Xaa Ser Leu Ala Tyr Val Lys Ala Cys Glu Thr Gly Thr Met 1875 1880 1885 TTG GCT GAC AAR GCG AGT GCT GCG TGG CAG GCT TGG GCT GCA AAC AAC 5711 Leu Ala Asp Xaa Ala Ser Ala Ala Trp Gin Ala Trp Ala Ala Asn Asn 1890 1895 1900 TTT GTG CCT CCA CCA GCA TCA CAC TCA ACT TCC TTG TTR CAG AGC TTG 5759 Phe Val Pro Pro Pro Ala Ser His Ser Thr Ser Leu Xaa Gin Ser Leu 1905 1910 1915 GAY GCT GCG TTC ACT TCA GCT TGG GAT AGC GTG TTC ACT CAC GGC CGT 5807 Xaa Ala Ala Phe Thr Ser Ala Trp Asp Ser Val Phe Thr Hie Gly Arg 1920 1925 1930 1935 TCC TTG CTT GTT GGG TTC ACA GCT GCT TAC GGC GCT CGG CGG AAC CCA 5855 Ser Leu Leu Val Gly Phe Thr Ala Ala Tyr Gly Ala Arg Arg Aβn Pro 1940 1945 1950 CCG CTG GGC GTC GGA GCC TCT TTC TTG CTG GGC ATG TCA TCG AGC CAC 5903 Pro Leu Gly Val Gly Ala Ser Phe Leu Leu Gly Met Ser Ser Ser His 1955 1960 1965 YTR ACT CAC GTC AGA CTT GCT GCT GCG TTG CTC CTC GGC GTC GGG GGT 5951 Xaa Thr Hiβ Val Arg Leu Ala Ala Ala Leu Leu Leu Gly Val Gly Gly 1970 1975 1980 ACC GTC CTA GGC ACG CCT GCT ACT GGG CTT GCT ATG GCG GGT GCC TAC 5999 Thr Val Leu Gly Thr Pro Ala Thr Gly Leu Ala Met Ala Gly Ala Tyr 1985 1990 1995 TTC GCK GGG GGC AGC GTT ACC GCT AAC TGG CTG AGT ATC ATT GTG GCT 6047 Phe Xaa Gly Gly Ser Val Thr Ala Aβn Trp Leu Ser He He Val Ala 2000 2005 2010 2015 CTA ATC GGA GGC TGG GAG GGG GCR GTK AAC GCA GCC TCA CTC ACC TTC 6095 Leu He Gly Gly Trp Glu Gly Xaa Xaa Aen Ala Ala Ser Leu Thr Phe 2020 2025 2030 GAY CTC CTG GCK GGG AAG TTA CAA GCK AGY GAY GCT TGG TGC CTR GTC 6143 Xaa Leu Leu Xaa Gly Lye Leu Gin Xaa Xaa Xaa Ala Trp Cyβ Xaa Val 410 2035 2040 2045 AGY TGC YTG GCC TCT CCG GGG GCT TCG GTG GCY GGT GTG GCD CTV GGY 6191 Xaa Cyβ Xaa Ala Ser Pro Gly Ala Ser Val Xaa Gly Val Xaa Xaa Xaa 2050 2055 2060 CTD YTG CTV TGG TCT GTC AAR AAG GGT GTG GGW CAR GAY TGG GTT AAC 6239 Xaa Xaa Xaa Trp Ser Val Xaa Lye Gly Val Xaa Xaa Xaa Trp Val Asn 2065 2070 2075 AGA YTG TTG ACG ATG ATG CCA CGC AGT TCG GTG ATG CCT GAC GAT TTC 6287 Arg Xaa Leu Thr Met Met Pro Arg Ser Ser Val Met Pro Aep Asp Phe 2080 2085 2090 2095 TTC CTC AAA GAT GAG TTC GTC ACC AAG GTG TCT ACT GTC CTG CGA AAG 6335 Phe Leu Lye Asp Glu Phe Val Thr Lys Val Ser Thr Val Leu Arg Lys 2100 2105 2110 TTG TCA TTG TCA AGA TGG ATC ATG ACT CTT GTG GAC AAG CGG GAG ATG 6383 Leu Ser Leu Ser Arg Trp He Met Thr Leu Val Asp Lys Arg Glu Met 2115 2120 2125 GAG ATG GAG ACM CCC GCT TCT CAG ATT GTT TGG GAC TTG CTT GAC TGG 6431 Glu Met Glu Xaa Pro Ala Ser Gin He Val Trp Asp Leu Leu Asp Trp 2130 2135 2140 TGC ATC CGG CTR GGT CGG TTC CTG TAC AAT AAA CTY ATG TTT GCT CTC 6479 Cys He Arg Xaa Gly Arg Phe Leu Tyr Asn Lys Xaa Met Phe Ala Leu 2145 2150 2155 CCT AGG TTG CGC CTG CCG CTT ATC GGT TGC AGT ACC GGT TGG GGT GGC 6527 Pro Arg Leu Arg Leu Pro Leu He Gly Cys Ser Thr Gly Trp Gly Gly 2160 2165 2170 2175 CCG TGG GAG GGC AAT GGT CAT TTG GAA ACA AGG TGT ACT TGT GGC TGT 6575 Pro Trp Glu Gly Asn Gly Hie Leu Glu Thr Arg Cys Thr Cys Gly Cys 2180 2185 2190 GTG ATT ACC GGT GAT ATT CAC GAT GGT ATA TTG CAC GAC CTA CAT TAT 6623 Val He Thr Gly Asp He His Aep Gly He Leu Hiβ Aep Leu Hiβ Tyr 2195 2200 2205 ACC TCC CTA CTG TGC AGA CAT TAC TAC AAG AGG ACA GTG CCT GTT GGC 6671 Thr Ser Leu Leu Cyβ Arg Hie Tyr Tyr Lye Arg Thr Val Pro Val Gly 2210 2215 2220 GTC ATG GGC AAT GCT GAG GGA GCA GTC CCC CTT GTG CCT ACT GGC GGT 6719 Val Met Gly Aβn Ala Glu Gly Ala Val Pro Leu Val Pro Thr Gly Gly 2225 2230 2235 GGA ATC AGG ACT TAC CAA ATT GGG ACT TCT GAC TGG TTT GAG GCT GTG 6767 Gly He Arg Thr Tyr Gin He Gly Thr Ser Aep Trp Phe Glu Ala Val 2240 2245 2250 2255 GTC GTG CAT GGG ACA ATC ACG GTG CAC GCC ACC AGT TGC TAT GAG TTG 6815 Val Val His Gly Thr He Thr Val Hie Ala Thr Ser Cyβ Tyr Glu Leu 2260 2265 2270 411 AAA GCT GCT GAC GTT CGG AGG GCG GTG CGA GCC GGC CCG ACT TAC GTT 6863 Lys Ala Ala Aep Val Arg Arg Ala Val Arg Ala Gly Pro Thr Tyr Val 2275 2280 2285 GGT GGC GTA CCT TGC AGC TGG AGC GCG CCG TGT ACT GCG CCT GCG CTC 6911 Gly Gly Val Pro Cye Ser Trp Ser Ala Pro Cyβ Thr Ala Pro Ala Leu 2290 2295 2300 GTT TAC AGG CTA GGC CAG GGC ATC AAA ATC GAT GGA GCG CGC CGA CTG 6959 Val Tyr Arg Leu Gly Gin Gly He Lye He Aep Gly Ala Arg Arg Leu 2305 2310 2315 TTG CCC TGT GAC TTA GCA CAG GGA GCG CGC CAC CCC CCG GTA TCT GGC 7007 Leu Pro Cyβ Aep Leu Ala Gin Gly Ala Arg Hiβ Pro Pro Val Ser Gly 2320 2325 2330 2335 AGT GTT GCC GGT AGT GGT TGG ACA GAT GAG GAC GAG AGG GAC TTG GTG 7055 Ser Val Ala Gly Ser Gly Trp Thr Aep Glu Aep Glu Arg Aep Leu Val 2340 2345 2350 GAA ACC AAG GCT GCC GCC ATC GAG GCC ATT GGG GCG GCC TTG CAC CTC 7103 Glu Thr Lye Ala Ala Ala He Glu Ala He Gly Ala Ala Leu Hiβ Leu 2355 2360 2365 CCT TCA CCG GAG GCT GCT CAG GCC GCT CTA GAG GCT TTG GAG GAG GCT 7151 Pro Ser Pro Glu Ala Ala Gin Ala Ala Leu Glu Ala Leu Glu Glu Ala 2370 2375 2380 GCC GTG TCC CTG TTG CCC CAT GTG CCC GTC ATT ATG GGT GAT GAC TGT 7199 Ala Val Ser Leu Leu Pro Hiβ Val Pro Val He Met Gly Aep Aep Cyβ 2385 2390 2395 TCA TGC CGG GAT GAG GCG TTC CAA GGC CAC TTC ATC CCA GAA CCC AAT 7247 Ser Cyβ Arg Asp Glu Ala Phe Gin Gly Hie Phe He Pro Glu Pro Aen 2400 2405 2410 2415 GTG ACA GAG GTA CCC ATT GAG CCC ACG GTC GGA GAC GTG GAG GCA CTC 7295 Val Thr Glu Val Pro He Glu Pro Thr Val Gly Asp Val Glu Ala Leu 2420 2425 2430 AAG CTG CGG GCT GCA GAC CTG ACC GCC AGG TTG CAA GAC TTG GAG GCC 7343 Lye Leu Arg Ala Ala Aep Leu Thr Ala Arg Leu Gin Aep Leu Glu Ala 2435 2440 2445 ATG GCT CTC GCC CGC GCT GAG TCA ATC GAG GAT GCT CGC GCA GCT TCG ' 7391 Met Ala Leu Ala Arg Ala Glu Ser He Glu Aep Ala Arg Ala Ala Ser 2450 2455 2460 ATG CCT TCG CTC ACC GAG GTG GAC TCA ATG CCA TCA TTG GAG TCG AGC 7439 Met Pro Ser Leu Thr Glu Val Aep Ser Met Pro Ser Leu Glu Ser Ser 2465 2470 2475 CCT TGC TCC TCC TTT GAA CAA ATC TCT TTA ACT GAA AGT GAC CCT GAG 7487 Pro Cyβ Ser Ser Phe Glu Gin He Ser Leu Thr Glu Ser Asp Pro Glu 2480 2485 2490 2495 ACT GTC GTC GAG GCT GGC TTA CCC TTG GAG TTC GTG AAC TCC AAC ACC 7535 412 Thr Val Val Glu Ala Gly Leu Pro Leu Glu Phe Val Asn Ser Asn Thr 2500 2505 2510 GGG CCG TCT CCG GCT CGG AGG ATT GTC AGA ATC CGA CAG GCT TGC TGT 7583 Gly Pro Ser Pro Ala Arg Arg He Val Arg He Arg Gin Ala Cys Cye 2515 2520 2525 TGT GAC AGA TCC ACA ATG AAG GCC ATG CCG TTG TCG TTC ACT GTC GGG 7631 Cys Asp Arg Ser Thr Met Lys Ala Met Pro Leu Ser Phe Thr Val Gly 2530 2535 2540 GAG TGC CTC TTC GTT ACT CGC TAT GAC CCG GAC GGT CAC CAA CTG TTT 7679 Glu Cys Leu Phe Val Thr Arg Tyr Aep Pro Aep Gly Hiβ Gin Leu Phe 2545 2550 2555 GAC GAG CGA GGT CCG ATA GAG GTA TCT ACT CCT ATA TGT GAA GTG ATT 7727 Aep Glu Arg Gly Pro He Glu Val Ser Thr Pro He Cye Glu Val He 2560 2565 2570 2575 GGG GAC ATC AGG CTT CAG TGT GAC CAA ATT GAG GAA ACT CCA ACA TCT 7775 Gly Aep He Arg Leu Gin Cyβ Aep Gin He Glu Glu Thr Pro Thr Ser 2580 2585 2590 TAC TCT TAC ATC TGG TCA GGG GCG CCC TTG GGT ACT GGG AGA AGT GTC 7823 Tyr Ser Tyr He Trp Ser Gly Ala Pro Leu Gly Thr Gly Arg Ser Val 2595 2600 2605 CCC CAA CCC ATG ACG CGC CCT ATA GGG ACC CAT CTG ACT TGT GAC ACT 7871 Pro Gin Pro Met Thr Arg Pro He Gly Thr Hiβ Leu Thr Cyβ Aep Thr 2610 2615 2620 ACC AAA GTT TAT GTT ACT GAC CCT GAT CGG GCC GCT GAG CGG GCC GAG 7919 Thr Lye Val Tyr Val Thr Aep Pro Aep Arg Ala Ala Glu Arg Ala Glu 2625 2630 2635 AAG GTT ACA ATC TGG AGG GGT GAT AGG AAG TAT GAC AAG CAT TAT GAG 7967 Lye Val Thr He Trp Arg Gly Aep Arg Lye Tyr Aep Lye Hiβ Tyr Glu 2640 2645 2650 2655 GCT GTC GTT GAG GCT GTC CTG AAA AAG GCA GCC GCG ACG AAG TCT CAT 8015 Ala Val Val Glu Ala Val Leu Lye Lye Ala Ala Ala Thr Lye Ser Hiβ 2660 2665 2670 GGC TGG ACC TAT TCC CAG GCT ATA GCT AAA GTT AGG CGC CGA GCA GCC 8063 Gly Trp Thr Tyr Ser Gin Ala He Ala Lye Val Arg Arg Arg Ala Ala 2675 2680 2685 GCT GGA TAC GGC AGC AAG GTG ACC GCC TCC ACA TTG GCC ACT GGT TGG 8111 Ala Gly Tyr Gly Ser Lye Val Thr Ala Ser Thr Leu Ala Thr Gly Trp 2690 2695 2700 CCT CAC GTG GAG GAG ATG CTG GAC AAA ATA GCC AGG GGA CAG GAA GTT 8159 Pro Hie Val Glu Glu Met Leu Aep Lye He Ala Arg Gly Gin Glu Val 2705 2710 2715 CCT TTC ACT TTT GTG ACC AAG CGA GAG GTT TTC TTC TCC AAA ACT ACC 8207 Pro Phe Thr Phe Val Thr Lye Arg Glu Val Phe Phe Ser Lye Thr Thr 413 2720 2725 2730 2735 CGT AAG CCC CCA AGA TTC ATA GTT TTC CCA CCT TTG GAC TTC AGG ATA 8255 Arg Lys Pro Pro Arg Phe He Val Phe Pro Pro Leu Aep Phe Arg He 2740 2745 2750 GCT GAA AAG ATG ATT CTG GGT GAC CCC GGC ATC GTT GCA AAG TCA ATT 8303 Ala Glu Lye Met He Leu Gly Aep Pro Gly He Val Ala Lye Ser He 2755 2760 2765 CTG GGT GAC GCT TAT CTG TTC CAG TAC ACG CCC AAT CAG AGG GTC AAA 8351 Leu Gly Aep Ala Tyr Leu Phe Gin Tyr Thr Pro Asn Gin Arg Val Lys 2770 2775 2780 GCT CTG GTT AAG GCG TGG GAG GGG AAG TTG CAT CCC GCT GCG ATC ACT 8399 Ala Leu Val Lys Ala Trp Glu Gly Lys Leu His Pro Ala Ala He Thr 2785 2790 2795 GTG GAC GCC ACT TGT TTC GAC TCA TCG ATT GAT GAG CAC GAC ATG CAG 8447 Val Asp Ala Thr Cys Phe Asp Ser Ser He Asp Glu His Asp Met Gin 2800 2805 2810 2815 GTG GAG GCT TCG GTG TTT GCG GCG GCT AGT GAC AAC CCC TCA ATG GTA 8495 Val Glu Ala Ser Val Phe Ala Ala Ala Ser Asp Asn Pro Ser Met Val 2820 2825 2830 CAT GCT TTG TGC AAG TAC TAC TCT GGT GGC CCT ATG GTT TCC CCA GAT 8543 His Ala Leu Cys Lys Tyr Tyr Ser Gly Gly Pro Met Val Ser Pro Asp 2835 2840 2845 GGG GTT CCC TTG GGG TAC CGC CAG TGT AGG TCG TCG GGC GTG TTA ACA 8591 Gly Val Pro Leu Gly Tyr Arg Gin Cye Arg Ser Ser Gly Val Leu Thr 2850 2855 2860 ACT AGC TCG GCG AAC AGC ATC ACT TGT TAC ATT AAG GTC AGC GCG GCC 8639 Thr Ser Ser Ala Aβn Ser He Thr Cyβ Tyr He Lye Val Ser Ala Ala 2865 2870 2875 TGC AGG CGG GTG GGG ATT AAG GCA CCA TCA TTC TTT ATA GCT GGA GAT 8687 Cys Arg Arg Val Gly He Lye Ala Pro Ser Phe Phe He Ala Gly Aep 2880 2885 2890 2895 GAT TGC TTG ATC ATC TAT GAA AAT GAT GGA ACT GAT CCC TGC CCT GCT 8735 Aep Cyβ Leu He He Tyr Glu Aβn Aep Gly Thr Aep Pro Cyβ Pro Ala 2900 2905 2910 CTT AAG GCT GCC CTG GCC AAC TAT GGA TAC AGG TGT GAA CCA ACA AAG 8783 Leu Lye Ala Ala Leu Ala Aβn Tyr Gly Tyr Arg Cyβ Glu Pro Thr Lye 2915 2920 2925 CAT GCT TCA CTG GAC ACA GCT GAG TGT TGC TCG GCC TAC TTG GCT GAG 8831 His Ala Ser Leu Asp Thr Ala Glu Cys Cye Ser Ala Tyr Leu Ala Glu 2930 2935 2940 TGC GTA GCT GGG GGT GCC AAG CGC TGG TGG TTG AGC ACG GAC ATG AGG 8879 Cys Val Ala Gly Gly Ala Lys Arg Trp Trp Leu Ser Thr Asp Met Arg 2945 2950 2955 414 AAG CCG CTC GCA AGG GCG TCT TCC GAA TAT TCG GAC CCA ATC GGC AGT 8927 Lye Pro Leu Ala Arg Ala Ser Ser Glu Tyr Ser Aep Pro He Gly Ser 2960 2965 2970 2975 GCT TTA GGG ACC ATC TTG ATG TAT CCC CGG CAT CCA ATC GTG CGG TAT 8975 Ala Leu Gly Thr He Leu Met Tyr Pro Arg His Pro He yal Arg Tyr 2980 2985 2990 GTT CTA ATA CCA CAC GTA CTA ATA ATG GCT TAC AGG AGT GGC AGC ACA 9023 Val Leu He Pro His Val Leu He Met Ala Tyr Arg Ser Gly Ser Thr 2995 3000 3005 CCG GAT GAG TTG GTT ATG TGT CAG GTT CAG GGA AAT CAT TAC TCT TTC 9071 Pro Aep Glu Leu Val Met Cys Gin Val Gin Gly Asn His Tyr Ser Phe 3010 3015 3020 CCG CTG CGG CTG CTG CCT CGC GTC TTG GTC TCT CTA CAT GGT CCG TGG 9119 Pro Leu Arg Leu Leu Pro Arg Val Leu Val Ser Leu His Gly Pro Trp 3025 3030 3035 TGC CTA CAA GTC ACC ACG GAC AGT ACG AAG ACT AGG ATG GAG GCA GGC 9167 Cys Leu Gin Val Thr Thr Asp Ser Thr Lye Thr Arg Met Glu Ala Gly 3040 3045 3050 3055 TCA GCS TTG CGG GAT TTA GGA ATG AAA TCC CTA GCC TGG CAC CGC CGA 9215 Ser Xaa Leu Arg Asp Leu Gly Met Lys Ser Leu Ala Trp His Arg Arg 3060 3065 3070 CGT GCC GGA AAT GTG CGC ACT CGC CTC CTG AGG GGA GGC AAG GAG TGG 9263 Arg Ala Gly Aen Val Arg Thr Arg Leu Leu Arg Gly Gly Lye Glu Trp 3075 3080 3085 GGG CAC CTG GCC AGA GCC CTC CTC TGG CAY CCA GGK TTG AAG GAG CAY 9311 Gly Hie Leu Ala Arg Ala Leu Leu Trp Xaa Pro Xaa Leu Lye Glu Xaa 3090 3095 3100 CCC CCR CCC ATA AAT TCA CTT CCA GGT TTT CAG CTG GCG ACG CCT TAC 9359 Pro Xaa Pro He Aβn Ser Leu Pro Gly Phe Gin Leu Ala Thr Pro Tyr 3105 3110 3115 GAA CAC CAT GAA GAG GTC TTG ATC TCG ATC AAG AGT CGA CCA CCT TGG 9407 Glu Hie Hie Glu Glu Val Leu He Ser He Lye Ser Arg Pro Pro Trp 3120 3125 3130 3135 ATA AGG TGG ATT CTT GGT GCT TGT CTC TCG TTG CTG GCC GCC TTG CTG 9455 He Arg Trp He Leu Gly Ala Cys Leu Ser Leu Leu Ala Ala Leu Leu 3140 3145 3150 TGA ATT CGC TCC AGG CAG TAG GAC CTT CGG GTC GGG GG 9493 * He Arg Ser Arg Gin * Asp Leu Arg Val Gly 3155 3160 (2) INFORMATION FOR SEQ ID NO:386: 415 (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 67 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:386: Trp Glu Ser Gly Ala Pro Asp Leu Pro Pro Arg Trp Gly Glu Arg Gly 1 5 10 15 Pro Gly Pro Ala Gly Trp Lys Ala Arg Asn Arg Ser He Phe Leu Lys 20 25 30 Val Glu Glu Gly Val Arg Leu Ser Val Arg Ser Val Arg Lys Ala Ser 35 40 45 Gly Cys Leu Val Leu Gly Phe Val Gly Gly Lys Ser Gin Leu Gly Val 50 55 60 Lys Ala Leu 65 (2) INFORMATION FOR SEQ ID NO:387: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2972 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:387: Asp Arg Leu He Pro Val Thr Ala Ala Pro Glu Pro Ala Pro Arg Xaa 1 5 10 15 Phe Gly His Gly Pro Gin Val Gly Gly Thr Gly Val Asn Asn Pro Pro 20 25 30 Thr Glu Ala Ser Val Val Lys Arg Arg Arg Ser Pro Glu He Ala Thr 35 40 45 Thr Pro His Val Arg Glu Arg Arg Gin Asn Leu Arg Asp Ser Tyr Ala 50 55 60 (2) INFORMATION FOR SEQ ID NO-:388: 416 (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 18 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:388: Gin Ser Gin Trp Gly Ala Gly Asp Gin Leu He Thr Cys Pro Ala Ser 1 5 10 15 Ser Ser (2) INFORMATION FOR SEQ ID NO:389: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 25 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:389: Asp Trp Pro Lys Gly Ser His Gly Ala Thr Lys Ala Ala Gin Arg Cys 1 5 10 15 Met Arg Gin Gly Glu Lys Ser Phe Gly 20 25 (2) INFORMATION FOR SEQ ID NO:390: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2973 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:390: Pro Leu Val Ala He Pro Ser Leu Arg Ser Met Ser Val Val Asp Thr 1 5 10 15 Phe Thr Met Ala Trp Leu Trp Leu Leu Val Cys Phe Pro Leu Ala Gly 20 25 30 Gly Val Leu Phe Asn Ser Arg His Gin Cys Phe Asn Gly Asp His Tyr 35 40 45 417 Val Leu Ser Asn Cys Cys Ser Arg Asp Glu Val Tyr Phe Cys Phe Gly 50 55 60 Asp Gly Cyβ Leu Val Ala Tyr Gly Cyβ Thr Val Cye Thr Gin Ser Cyβ 65 70 75 80 Trp Lye Leu Tyr Arg Pro Gly Val Ala Thr Arg Pro Gly Ser Glu Pro 85 90 95 Gly Glu Leu Leu Gly Arg Phe Gly Ser Val He Gly Pro Val Ser Ala 100 105 110 Ser Ala Tyr Thr Ala Gly Val Leu Gly Leu Gly Glu Pro Tyr Ser Leu 115 120 125 Ala Phe Leu Gly Thr Phe Leu Thr Ser Arg Leu Ser Arg He Pro Aen 130 135 140 Val Thr Cyβ Val Lye Ala Cye Aep Leu Glu Phe Thr Tyr Pro Gly Leu 145 150 155 160 Ser He Aep Phe Asp Trp Ala Phe Thr Lys He Leu Gin Leu Pro Ala 165 170 175 Lys Leu Trp Arg Gly Leu Thr Xaa Xaa Pro Val Leu Ser Leu Leu Val 180 185 190 He Leu Met Leu Val Leu Glu Gin Arg Leu Leu He Ala Phe Leu Leu 195 200 205 Leu Leu Val Val Gly Glu Ala Gin Arg Gly Met Phe Asp Aβn Cye Val 210 215 220 Cye Gly Tyr Trp Gly Gly Lye Arg Pro Pro Ser Val Thr Pro Leu Tyr 225 230 235 240 Arg Gly Aen Gly Thr Val Val Cys Asp Cys Asp Phe Gly Lys Met His 245 250 255 Trp Ala Pro Pro Leu Cys Ser Xaa Leu Val Trp Arg Asp Gly His Arg 260 265 270 Arg Gly Thr Val Arg Asp Leu Pro Pro Val Cys Pro Arg Glu Val Leu 275 280 285 Gly Thr Val Thr Val Met Cys Gin Trp Gly Ser Ala Tyr Trp He Trp 290 295 300 Arg Phe Gly Asp Trp Val Ala Leu Tyr Asp Glu Leu Pro Arg Ser Ala 305 310 315 320 Leu Cys Thr Phe Phe Ser Gly His Gly Pro Gin Pro Lys Asp Leu Ser 325 330 335 Val Leu Asn Pro Ser Gly Ala Pro Cys Ala Ser Cys Val Val Asp Gin 340 345 " 350 418 Arg Pro Leu Lys Cys Gly Ser Cyβ Val Arg Aep Cys Trp Glu Thr Gly 355 360 365 Gly Pro Gly Phe Asp Glu Cyβ Gly Val Gly Thr Arg Met Thr Lye His 370 375 380 Leu Glu Ala Val Leu Val Aep Gly Gly Val Glu Ser Lye Val Thr Thr 385 390 395 400 Pro Lye Gly Glu Arg Pro Lye Tyr He Gly Gin His Gly Val Gly Thr 405 410 415 Tyr Tyr Gly Ala Val Arg Ser Leu Aen He Ser Tyr Leu Val Thr Glu 420 425 430 Val Gly Gly Tyr Trp Hiβ Ala Leu Lye Cyβ Pro Cyβ Aep Phe Val Pro 435 440 445 Arg Val Leu Pro Glu Arg He Pro Gly Arg Pro Val Aβn Ala Cye Leu 450 455 460 Ala Gly Lye Ser Pro His Pro Phe Ala Ser Trp Ala Pro Gly Gly Phe 465 470 475 480 Tyr Ala Pro Val Phe Thr Lys Cys Asn Trp Pro Lys Thr Ser Gly Val 485 490 495 Asp Val Cys Pro Gly Phe Ala Phe Asp Phe Pro Gly Asp His Aβn Gly 500 505 510 Phe He Hiβ Val Lye Gly Asn Arg Gin Gin Val Tyr Ser Gly Gin Arg 515 520 525 Arg Ser Ser Pro Ala Trp Leu Leu Thr Asp Met Val Leu Ala Leu Leu 530 535 540 Val Val Met Lys Leu Ala Glu Ala Arg Val Val Pro Leu Phe Met Leu 545 550 555 560 Ala Met Trp Trp Trp Leu Asn Gly Ala Ser Ala Ala Thr He Val lie 565 570 575 He Hiβ Pro Thr Val Thr Lys Ser Thr Glu Ser Val Pro Leu Trp Thr 580 585 590 Pro Pro Thr Val Pro Thr Pro Ser Cys Pro Asn Ser Thr Thr Gly Val 595 600 605 Ala Asp Ser Thr Tyr Aβn Ala Gly Cye Tyr Met Val Ala Gly Leu Ala 610 615 620 Ala Gly Ala Gin Ala Val Trp Gly Ala Ala Aen Asp Gly Ala Gin Ala 625 630 635 640 Val Val Gly Gly He Trp Pro Ala Trp Leu Lys Leu Arg Ser Phe Ala 645 650 655 419 Ala Gly Leu Ala Trp Leu Ser Asn Val Gly Ala Tyr Leu Pro Val Val 660 665 670 Glu Ala Xaa Leu Ala Pro Glu Leu Val Cye Thr Pro Val Val Gly Trp 675 680 685 Ala Ala Gin Glu Trp Trp Phe Thr Gly Cye Leu Gly Val Met Cyβ Val 690 695 700 Val Ala Tyr Leu Asn Val Leu Gly Ser Xaa Arg Ala Ala Val Leu Val 705 710 715 720 Ala Met His Phe Ala Arg Gly Ala Leu Pro Leu Val Leu Val Val Ala 725 730 735 Ala Gly Xaa Thr Arg Glu Arg Hiβ Ser Val Leu Gly Leu Glu Val Cyβ 740 745 750 Phe Aep Leu Aep Gly Gly Aep Trp Xaa Aep Ala Ser Trp Ser Trp Gly 755 760 765 Leu Ala Gly Val Val Ser Trp Ala Leu Leu Val Gly Gly Leu Met Thr 770 775 780 His Gly Gly Arg Ser Ala Arg Xaa Thr Trp Xaa Ala Arg Trp Ala Val 785 790 795 800 Aβn Xaa Gin Arg Val Xaa Arg Trp Val Aβn Aβn Ser Pro Val Gly Xaa 805 810 815 Phe Xaa Arg Trp Xaa Xaa Ala Trp Lye Xaa Trp Xaa Xaa Val Ala Trp 820 825 830 Phe Phe Pro Gin Thr Val Ala Thr Xaa Ser Val He Phe He Leu Cyβ 835 840 845 Leu Ser Ser Leu Aep Val He Aep Phe He Leu Xaa Val Leu Leu Val 850 855 860 Aβn Ser Pro Aβn Leu Ala Arg Leu Ala Xaa Val Leu Aep Ser Leu Ala 865 870 875 880 Xaa Ala Glu Glu Arg Leu Ala Cye Ser Trp Leu Val Gly Val Leu Arg 885 890 895 Lys Arg Gly Val Leu Leu Tyr Glu Hiβ Xaa Gly Hie Thr Ser Arg Arg 900 905 910 Gly Ala Ala Arg Leu Arg Glu Trp Xaa Phe Ala Xaa Glu Xaa Val Xaa 915 920 925 He Thr Lye Glu Aep Xaa Xaa He Val Arg Aep Ser Ala Arg Val Leu 930 935 940 Gly Cys Gly Gin Leu Val His Gly Lys Pro Val Val Ala Arg Arg Gly 945 950 955 960 420 Asp Glu Val Leu He Gly Cyβ Val Aβn Ser Arg Phe Aep Leu Pro Pro 965 970 975 Gly Phe Val Pro Thr Ala Pro Val Xaa Leu Hie Xaa Xaa Gly Xaa Xaa 980 985 990 Xaa Xaa Gly Val Val Lye Xaa Ser Met Thr Gly Lye Aep Pro Ser Glu 995 1000 1005 Hiβ Hiβ Xaa Aen Val Val Val Xaa Gly Thr Ser Thr Xaa Arg Ser Met 1010 1015 1020 Gly Cye Cye Val Aβn Gly Val Val Tyr Xaa Thr Tyr Hie Xaa Thr Aen 1025 1030 1035 1040 Ala Xaa Xaa Met Ala Gly Xaa Phe Xaa Xaa Val Xaa Ala Arg Trp Trp 1045 1050 1055 Xaa Ala Xaa Asp Asp Val Thr Xaa Tyr Pro Leu Xaa Asn Xaa Ala Ser 1060 1065 1070 Cyβ Xaa Xaa Xaa Xaa Lye Cye Gin Pro Thr Gly Val Trp Val He Arg 1075 1080 1085 Aβn Asp Gly Ala Leu Cyβ Hiβ Gly Thr Leu Gly Lye Val Val Aep Leu 1090 1095 1100 Aep Met Pro Ala Glu Leu Ser Aep Phe Arg Gly Ser Ser Gly Ser Pro 1105 1110 1115 1120 He Leu Cye Asp Glu Gly His Ala Val Gly Met Leu He Ser Val Leu 1125 1130 1135 His Arg Gly Ser Arg Val Ser Ser Val Arg Tyr Thr Lys Pro Trp Glu 1140 1145 1150 Thr Leu Pro Arg Glu He Glu Ala Arg Ser Glu Ala Pro Pro Val Pro 1155 1160 1165 Gly Thr Thr Gly Tyr Arg Glu Ala Pro Leu Phe Leu Pro Thr Gly Ala 1170 1175 1180 Gly Lye Ser Thr Arg Val Pro Aβn Glu Tyr Val Lye Ala Gly Hiβ Xaa 1185 1190 1195 1200 Val Leu Val Leu Asn Pro Ser He Ala Thr Val Arg Ala Met Gly Pro 1205 1210 1215 Tyr Met Glu Lys Leu Thr Gly Lys His Pro Ser Val Tyr Cys Gly His 1220 1225 1230 Aep Thr Thr Ala Tyr Ser Arg Thr Thr Aep Ser Ser Leu Thr Tyr Cys 1235 1240 1245 Thr Tyr Gly Arg Phe Met Ala Asn Pro Arg Lye Tyr Leu Arg Gly Aβn 1250 1255 1260 421 Aep Val Val He Cye Aep Glu Leu Hiβ Val Thr Aep Pro Thr Ser He 1265 1270 1275 1280 Leu Gly Met Gly Arg Ala Arg Leu Leu Ala Arg Glu Cys Gly Val Arg 1285 1290 1295 Leu Leu Leu Phe Ala Thr Ala Thr Pro Pro Val Ser Pro Met Ala Lye 1300 1305 1310 Hiβ Glu Ser He Hiβ Glu Glu Met Leu Gly Ser Glu Gly Glu Val Pro 1315 1320 1325 Phe Tyr Cye Gin Phe Leu Pro Leu Ser Arg Tyr Ala Thr Gly Arg Hie 1330 1335 1340 Leu Leu Phe Cyβ Hie Ser Lye Val Xaa Cys Thr Arg Leu Ser Ser Ala 1345 1350 1355 1360 Leu Ala Ser Phe Gly Val Aβn Thr Val Val Tyr Phe Arg Gly Lye Glu 1365 1370 1375 Thr Aep He Pro Thr Gly Asp Val Cys Val Cys Ala Thr Asp Ala Leu 1380 1385 1390 Ser Thr Gly Tyr Thr Gly Asn Phe Aep Thr Val Thr Asp Cys Gly Leu 1395 1400 1405 Met Val Glu Glu Val Val Glu Val Thr Leu Asp Pro Thr He Thr He 1410 1415 1420 Gly Val Lye Thr Val Pro Ala Pro Ala Glu Leu Arg Ala Gin Arg Arg 1425 1430 1435 1440 Gly Arg Cyβ Gly Arg Gly Lye Ala Gly Thr Tyr Tyr Gin Ala Leu Met 1445 1450 1455 Ser Ser Ala Pro Ala Gly Xaa Val Arg Ser Gly Ala Leu Trp Ala Ala 1460 1465 1470 Val Glu Ala Xaa Val Ser Trp Tyr Gly Leu Glu Pro Aep Ala He Gly 1475 1480 1485 Aep Leu Leu Arg Ala Tyr Asp Ser Cys Pro Tyr Thr Ala Ala He Ser 1490 1495 1500 Ala Ser He Gly Glu Ala He Ala Phe Phe Thr Xaa Leu Val Pro Met 1505 1510 1515 1520 Arg Aβn Tyr Pro Gin Val Val Trp Ala Lye Gin Lye Xaa His Asn Trp 1525 1530 1535 Pro Leu Leu Val Gly Val Gin Arg His Met Cys Glu Asp Ala Gly Cyβ 1540 1545 1550 Gly Xaa Pro Ala Asn Gly Pro Glu Trp Ser Gly He Arg Gly Lys Gly 1555 1560 1565 422 Pro Val Pro Leu Leu Cyβ Arg Trp Gly Gly Aep Leu Pro Glu Ser Val 1570 1575 1580 Ala Pro His Hie Trp Val Aep Aep Leu Gin Ala Arg Leu Gly Val Ala 1585 1590 1595 1600 Glu Gly Tyr Thr Pro Cyβ He Ala Gly Pro Val Leu Leu Val Gly Leu 1605 1610 1615 Ala Met Ala Gly Gly Ala He Leu Ala His Trp Thr Gly Ser Leu Val 1620 1625 1630 Val Val Thr Ser Trp Val Val Asn Gly Aβn Gly Aβn Pro Leu He Gin 1635 1640 1645 Ser Ala Ser Arg Gly Val Xaa Xaa Ser Gly Pro Tyr Pro Val Pro Pro 1650 1655 1660 Aep Gly Gly Glu Arg Tyr Pro Ser Asp He Lys Pro Xaa Thr Glu Ala 1665 1670 1675 1680 Val Thr Thr Leu Glu Thr Ala Cys Xaa Trp Gly Pro Ala Ala Xaa Ser 1685 1690 1695 Leu Ala Tyr Val Lye Ala Cys Glu Thr Gly Thr Met Leu Ala Asp Xaa 1700 1705 1710 Ala Ser Ala Ala Trp Gin Ala Trp Ala Ala Aβn Asn Phe Val Pro Pro 1715 1720 1725 Pro Ala Ser Hiβ Ser Thr Ser Leu Xaa Gin Ser Leu Xaa Ala Ala Phe 1730 1735 1740 Thr Ser Ala Trp Aep Ser Val Phe Thr Hiβ Gly Arg Ser Leu Leu Val 1745 1750 1755 1760 Gly Phe Thr Ala Ala Tyr Gly Ala Arg Arg Aen Pro Pro Leu Gly Val 1765 1770 1775 Gly Ala Ser Phe Leu Leu Gly Met Ser Ser Ser Hie Xaa Thr Hiβ Val 1780 1785 1790 Arg Leu Ala Ala Ala Leu Leu Leu Gly Val Gly Gly Thr Val Leu Gly 1795 1800 1805 Thr Pro Ala Thr Gly Leu Ala Met Ala Gly Ala Tyr Phe Xaa Gly Gly 1810 1815 1820 Ser Val Thr Ala Aen Trp Leu Ser He He Val Ala Leu He Gly Gly 1825 1830 1835 1840 Trp Glu Gly Xaa Xaa Aβn Ala Ala Ser Leu Thr Phe Xaa Leu Leu Xaa 1845 1850 1855 Gly Lye Leu Gin Xaa Xaa Xaa Ala Trp Cyβ Xaa Val Xaa Cyβ Xaa Ala 1860 1865 1870 423 Ser Pro Gly Ala Ser Val Xaa Gly Val Xaa Xaa Xaa Xaa Xaa Xaa Trp 1875 1880 1885 Ser Val Xaa Lye Gly Val Xaa Xaa Xaa Trp Val Asn Arg Xaa Leu Thr 1890 1895 1900 Met Met Pro Arg Ser Ser Val Met Pro Aep Aep Phe Phe Leu Lye Aep 1905 1910 1915 1920 Glu Phe Val Thr Lye Val Ser Thr Val Leu Arg Lye Leu Ser Leu Ser 1925 1930 1935 Arg Trp He Met Thr Leu Val Asp Lys Arg Glu Met Glu Met Glu Xaa 1940 1945 1950 Pro Ala Ser Gin He Val Trp Asp Leu Leu Aep Trp Cyβ He Arg Xaa 1955 1960 1965 Gly Arg Phe Leu Tyr Aen Lye Xaa Met Phe Ala Leu Pro Arg Leu Arg 1970 1975 1980 Leu Pro Leu He Gly Cys Ser Thr Gly Trp Gly Gly Pro Trp Glu Gly 1985 1990 1995 2000 Asn Gly His Leu Glu Thr Arg Cys Thr Cys Gly Cys Val He Thr Gly 2005 2010 2015 Aep He Hie Aep Gly He Leu Hie Aep Leu Hiβ Tyr Thr Ser Leu Leu 2020 2025 2030 Cye Arg Hie Tyr Tyr Lye Arg Thr Val Pro Val Gly Val Met Gly Aβn 2035 2040 2045 Ala Glu Gly Ala Val Pro Leu Val Pro Thr Gly Gly Gly He Arg Thr 2050 2055 2060 Tyr Gin He Gly Thr Ser Aep Trp Phe Glu Ala Val Val Val Hie Gly 2065 2070 2075 2080 Thr He Thr Val His Ala Thr Ser Cys Tyr Glu Leu Lys Ala Ala Asp 2085 2090 2095 Val Arg Arg Ala Val Arg Ala Gly Pro Thr Tyr Val Gly Gly Val Pro 2100 2105 2110 Cys Ser Trp Ser Ala Pro Cys Thr Ala Pro Ala Leu Val Tyr Arg Leu 2115 2120 2125 Gly Gin Gly He Lys He Asp Gly Ala Arg Arg Leu Leu Pro Cys Asp 2130 2135 2140 Leu Ala Gin Gly Ala Arg His Pro Pro Val Ser Gly Ser Val Ala Gly 2145 2150 2155 2160 Ser Gly Trp Thr Asp Glu Asp Glu Arg Asp Leu Val Glu Thr Lys Ala 2165 2170 2175 424 Ala Ala He Glu Ala He Gly Ala Ala Leu His Leu Pro Ser Pro Glu 2180 2185 2190 Ala Ala Gin Ala Ala Leu Glu Ala Leu Glu Glu Ala Ala Val Ser Leu 2195 2200 2205 Leu Pro His Val Pro Val He Met Gly Asp Aep Cyβ Ser Cyβ Arg Asp 2210 2215 2220 Glu Ala Phe Gin Gly His Phe He Pro Glu Pro Aen Val Thr Glu Val 2225 2230 2235 2240 Pro He Glu Pro Thr Val Gly Aep Val Glu Ala Leu Lye Leu Arg Ala 2245 2250 2255 Ala Aep Leu Thr Ala Arg Leu Gin Aep Leu Glu Ala Met Ala Leu Ala 2260 2265 2270 Arg Ala Glu Ser He Glu Asp Ala Arg Ala Ala Ser Met Pro Ser Leu 2275 2280 2285 Thr Glu Val Asp Ser Met Pro Ser Leu Glu Ser Ser Pro Cye Ser Ser 2290 2295 2300 Phe Glu Gin He Ser Leu Thr Glu Ser Aep Pro Glu Thr Val Val Glu 2305 2310 2315 2320 Ala Gly Leu Pro Leu Glu Phe Val Aβn Ser Aβn Thr Gly Pro Ser Pro 2325 2330 2335 Ala Arg Arg He Val Arg He Arg Gin Ala Cyβ Cyβ Cyβ Aep Arg Ser 2340 2345 2350 Thr Met Lye Ala Met Pro Leu Ser Phe Thr Val Gly Glu Cyβ Leu Phe 2355 2360 2365 Val Thr Arg Tyr Aep Pro Asp Gly Hie Gin Leu Phe Aep Glu Arg Gly 2370 2375 2380 Pro He Glu Val Ser Thr Pro He Cye Glu Val He Gly Aep He Arg 2385 2390 2395 2400 Leu Gin Cye Aep Gin He Glu Glu Thr Pro Thr Ser Tyr Ser Tyr He 2405 2410 2415 Trp Ser Gly Ala Pro Leu Gly Thr Gly Arg Ser Val Pro Gin Pro Met 2420 2425 2430 Thr Arg Pro He Gly Thr Hiβ Leu Thr Cye Aep Thr Thr Lye Val Tyr 2435 2440 2445 Val Thr Aep Pro Aep Arg Ala Ala Glu Arg Ala Glu Lye Val Thr He 2450 2455 2460 Trp Arg Gly Aep Arg Lye Tyr Aep Lye His Tyr Glu Ala Val Val Glu 2465 2470 2475 2480 425 Ala Val Leu Lys Lye Ala Ala Ala Thr Lye Ser Hiβ Gly Trp Thr Tyr 2485 2490 2495 Ser Gin Ala He Ala Lys Val Arg Arg Arg Ala Ala Ala Gly Tyr Gly 2500 2505 2510 Ser Lye Val Thr Ala Ser Thr Leu Ala Thr Gly Trp Pro Hiβ Val Glu 2515 2520 2525 Glu Met Leu Aep Lye He Ala Arg Gly Gin Glu Val Pro Phe Thr Phe 2530 2535 2540 Val Thr Lye Arg Glu Val Phe Phe Ser Lye Thr Thr Arg Lye Pro Pro 2545 2550 2555 2560 Arg Phe He Val Phe Pro Pro Leu Aep Phe Arg He Ala Glu Lye Met 2565 2570 2575 He Leu Gly Aep Pro Gly He Val Ala Lye Ser He Leu Gly Aep Ala 2580 2585 2590 Tyr Leu Phe Gin Tyr Thr Pro Aβn Gin Arg Val Lys Ala Leu Val Lys 2595 2600 2605 Ala Trp Glu Gly Lye Leu His Pro Ala Ala He Thr Val Asp Ala Thr 2610 2615 2620 Cys Phe Asp Ser Ser He Asp Glu His Asp Met Gin Val Glu Ala Ser 2625 2630 2635 2640 Val Phe Ala Ala Ala Ser Aep Aen Pro Ser Met Val Hiβ Ala Leu Cyβ 2645 2650 2655 Lye Tyr Tyr Ser Gly Gly Pro Met Val Ser Pro Aep Gly Val Pro Leu 2660 2665 2670 Gly Tyr Arg Gin Cys Arg Ser Ser Gly Val Leu Thr Thr Ser Ser Ala 2675 2680 2685 Asn Ser He Thr Cys Tyr He Lys Val Ser Ala Ala Cys Arg Arg Val 2690 2695 2700 Gly He Lys Ala Pro Ser Phe Phe He Ala Gly Asp Asp Cys Leu He 2705 2710 2715 2720 He Tyr Glu Aβn Asp Gly Thr Aep Pro Cyβ Pro Ala Leu Lye Ala Ala 2725 2730 2735 Leu Ala Aen Tyr Gly Tyr Arg Cyβ Glu Pro Thr Lye Hiβ Ala Ser Leu 2740 2745 2750 Aep Thr Ala Glu Cyβ Cyβ Ser Ala Tyr Leu Ala Glu Cyβ Val Ala Gly 2755 2760 2765 Gly Ala Lye Arg Trp Trp Leu Ser Thr Aep Met Arg Lye Pro Leu Ala 2770 2775 2780 426 Arg Ala Ser Ser Glu Tyr Ser Asp Pro He Gly Ser Ala Leu Gly Thr 2785 2790 2795 2800 He Leu Met Tyr Pro Arg His Pro He Val Arg Tyr Val Leu He Pro 2805 2810 2815 Hiβ Val Leu He Met Ala Tyr Arg Ser Gly Ser Thr Pro Aep Glu Leu 2820 2825 2830 Val Met Cye Gin Val Gin Gly Asn His Tyr Ser Phe Pro Leu Arg Leu 2835 2840 2845 Leu Pro Arg Val Leu Val Ser Leu His Gly Pro Trp Cys Leu Gin Val 2850 2855 2860 Thr Thr Asp Ser Thr Lys Thr Arg Met Glu Ala Gly Ser Xaa Leu Arg 2865 2870 2875 2880 Asp Leu Gly Met Lye Ser Leu Ala Trp Hiβ Arg Arg Arg Ala Gly Aen 2885 2890 2895 Val Arg Thr Arg Leu Leu Arg Gly Gly Lys Glu Trp Gly His Leu Ala 2900 2905 2910 Arg Ala Leu Leu Trp Xaa Pro Xaa Leu Lys Glu Xaa Pro Xaa Pro He 2915 2920 2925 Asn Ser Leu Pro Gly Phe Gin Leu Ala Thr Pro Tyr Glu Hiβ Hie Glu 2930 2935 2940 Glu Val Leu He Ser He Lye Ser Arg Pro Pro Trp He Arg Trp He 2945 2950 2955 2960 Leu Gly Ala Cyβ Leu Ser Leu Leu Ala Ala Leu Leu 2965 2970 (2) INFORMATION FOR SEQ ID NO:391: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 5 amino acide (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:391: He Arg Ser Arg Gin 1 5 427 (2) INFORMATION FOR SEQ ID NO:392: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 5 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:392; Asp Leu Arg Val Gly 1 5 (2) INFORMATION FOR SEQ ID NO:393: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9143 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:393: ACCACAAACA CTCCAGTTTG TTACACTCCG CTAGGAATGC TCCTGGAGCA CCCCCCCTAG 60 CAGGGCGTGG GGGATTTCCC CTGCCCGTCT GCAGAAGGGT GGAGCCAACC ACCTTAGTAT 120 GTAGGCGGCG GGACTCATGA CGCTCGCGTG ATGACAAGCG CCAAGCTTGA CTTGGATGGC 180 CCTGATGGGC GTTCATGGGT TCGGTGGTGG TGGCGCTTTA GGCAGCCTCC ACGCCCACCA 240 CCTCCCAGAT AGAGCGGCGG CACTGTAGGG AAGACCGGGG ACCGGTCACT ACCAAGGACG 300 CAGACCTCTT TTTGAGTATC ACGCCTCCGG AAGTAGTTGG GCAAGCCCAC CTATATGTGT 360 TGGGATGGTT GGGGTTAGCC ATCCATACCG TACTGCCTGA TAGGGTCCTT GCGAGGGGAT 420 CTGGGAGTCT CGTAGACCGT AGCACATGCC TGTTATTTCT ACTCAAACAA GTCCTGTACC 480 TGCGCCCAGA ACGCGCAAGA ACAAGCAGAC GCAGGCTTCA TATCCTGTGT CCATTAAAAC 540 ATCTGTTGAA AGGGGACAAC GAGCAAAGCG CAAAGTCCAG CGCGATGCTC GGCCTCGTAA 600 TTACAAAATT GCTGGTATCC ATGATGGCTT GCAGACATTG GCTCAGGCTG CTTTGCCAGC 660 428 TCATGGTTGG GGACGCCAAG ACCCTCGCCA TAAGTCTCGC AATCTTGGAA TCCTTCTGGA 720 TTACCCTTTG GGGTGGATTG GTGATGTTAC AACTCACACA CCTCTAGTAG GCCCGCTGGT 780 GGCAGGAGCG GTCGTTCGAC CAGTCTGCCA GATAGTACGC TTGCTGGAGG ATGGAGTCAA 840 CTGGGCTACT GGTTGGTTCG GTGTCCACCT TTTTGTGGTA TGTCTGCTAT CTTTGGCCTG 900 TCCCTGTAGT GGGGCGCGGG TCACTGACCC AGACACAAAT ACCACAATCC TGACCAATTG 960 CTGCCAGCGT AATCAGGTTA TCTATTGTTC TCCTTCCACT TGCCTACACG AGCCTGGTTG 1020 TGTGATCTGC GCGGACGAGT GCTGGGTTCC CGCCAATCCG TACATCTCAC ACCCTTCCAA 1080 TTGGACTGGC ACGGACTCCT TCTTGGCTGA CCACATTGAT TTTGTTATGG GCGCTCTTGT 1140 GACCTGTGAC GCCCTTGACA TTGGTGAGTT GTGTGGTGCG TGTGTATTAG TCGGTGACTG 1200 GCTTGTCAGG CACTGGCTTA TTCACATAGA CCTCAATGAA ACTGGTACTT GTTACCTGGA 1260 AGTGCCCACT GGAATAGATC CTGGGTTCCT AGGGTTTATC GGGTGGATGG CCGGCAAGGT 1320 CGAGGCTGTC ATCTTCTTGA CCAAACTGGC TTCACAAGTA CCATACGCTA TTGCGACTAT 1380 GTTTAGCAGT GTACACTACC TGGCGGTTGG CGCTCTGATC TACTATGCCT CTCGGGGCAA 1440 GTGGTATCAG TTGCTCCTAG CGCTTATGCT TTACATAGAA GCGACCTCTG GAAACCCTAT 1500 CAGGGTGCCC ACTGGATGCT CAATAGCTGA GTTTTGCTCG CCTTTGATGA TACCATGTCC 1560 TTGCCACTCT TATTTGAGTG AGAATGTGTC AGAAGTCATT TGTTACAGTC CAAAGTGGAC 1620 CAGGCCTGTC ACTCTAGAGT ATAACAACTC CATATCTTGG TACCCCTATA CAATCCCTGG 1680 TGCGAGGGGA TGTATGGTTA AATTCAAAAA TAACACATGG GGTTGCTGCC GTATTCGCAA 1740 TGTGCCATCG TACTGCACTA TGGGCACTGA TGCAGTGTGG AACGACACTC GCAACACTTA 1800 CGAAGCATGC GGTGTAACAC CATGGCTAAC AACCGCATGG CACAACGGCT CAGCCCTGAA 1860 ATTGGCTATA TTACAATACC CTGGGTCTAA AGAAATGTTT AAACCTCATA ATTGGATGTC 1920 AGGCCATTTG TATTTTGAGG GATCAGATAC CCCTATAGTT TACTTTTATG ACCCTGTGAA 1980 TTCCACTCTC CTACCACCGG AGAGGTGGGC TAGGTTGCCC GGTACCCCAC CTGTGGTACG 2040 TGGTTCTTGG TTACAGGTTC CGCAAGGGTT TTACAGTGAT GTGAAAGACC TAGCCACAGG 2100 ATTGATCACC AAAGACAAAG CCTGGAAAAA TTATCAGGTC TTATATTCCG CCACGGGTGC 2160 TTTGTCTCTT ACGGGAGTTA CCACCAAGGC CGTGGTGCTA ATTCTGTTGG GGTTGTGTGG 2220 CAGCAAGTAT CTTATTTTAG CCTACCTCTG TTACTTGTCC CTTTGTTTTG GGCGCGCTTC 2280 TGGTTACCCT TTGCGTCCTG TGCTCCCATC CCAGTCGTAT CTCCAAGCTG GCTGGGATGT 2340 TTTGTCTAAA GCTCAAGTAG CTCCTTTTGC TTTGATTTTC TTCATCTGTT GCTATCTCCG 2400 O95/21922 429 CTGCAGGCTA CGTTATGCTG CCCTTTTAGG GTTTGTGCCC ATGGCTGCGG GCTTGCCCCT 2460 AACTTTCTTT GTTGCAGCAG CTGCTGCCCA ACCAGATTAT GACTGGTGGG TGCGACTGCT 2520 AGTGGCAGGG TTAGTTTTGT GGGCCGGCCG TGACCGTGGT CCACGTATAG CTCTGCTTGT 2580 AGGTCCTTGG CCTCTGGTAG CGCTTTTAAC CCTCTTGCAT TTGGCTACGC CTGCTTCAGC 2640 TTTTGACACC GAGATAATTG GAGGGCTGAC AATACCACCT GTAGTAGCAT TAGTTGTCAT 2700 GTCTCGTTTT GGCTTCTTTG CTCACTTGTT ACCTCGCTGT GCTTTAGTTA ACTCCTATCT 2760 TTGGCAACGT TGGGAGAATT GGTTTTGGAA CGTTACACTA AGACCGGAGA GGTTTCTCCT 2820 TGTGCTGGTT TGTTTCCCCG GTGCGACATA TGACACGCTG GTGACTTTCT GTGTGTGTCA 2880 CGTAGCTCTT CTATGTTTAA CATCCAGTGC AGCATCGTTC TTTGGGACTG ACTCTAGGGT 2940 TAGGGCCCAT AGAATGTTGG TGCGTCTCGG AAAGTGTCAT GCTTGGTATT CTCATTATGT 3000 TCTTAAGTTT TTCCTCTTAG TGTTTGGTGA GAATGGTGTG TTTTTCTATA AGCACTTGCA 3060 TGGTGATGTC TTGCCTAATG ATTTTGCCTC GAAACTACCA TTGCAAGAGC CATTTTTCCC 3120 TTTTGAAGGC AAGGCAAGGG TCTATAGGAA TGAAGGAAGA CGCTTGGCGT GTGGGGACAC 3180 GGTTGATGGT TTGCCCGTTG TTGCGCGTCT CGGCGACCTT GTTTTCGCAG GGTTAGCTAT 3240 GCCGCCAGAT GGGTGGGCCA TTACCGCACC TTTTACGCTG CAGTGTCTCT CTGAACGTGG 3300 CACGCTGTCA GCGATGGCAG TGGTCATGAC TGGTATAGAC CCCCGAACTT GGACTGGAAC 3360 TATCTTCAGA TTAGGATCTC TGGCCACTAG CTACATGGGA TTTGTTTGTG ACAACGTGTT 3420 GTATACTGCT CACCATGGCA GCAAGGGGCG CCGGTTGGCT CATCCCACAG GCTCCATACA 3480 CCCAATAACC GTTGACGCGG CTAATGACCA GGACATCTAT CAACCACCAT GTGGAGCTGG 3540 GTCCCTTACT CGGTGCTCTT GCGGGGAGAC CAAGGGGTAT CTGGTAACAC GACTGGGGTC 3600 ATTGGTTGAG GTCAACAAAT CCGATGACCC TTATTGGTGT GTGTGCGGGG CCCTTCCCAT 3660 GGCTGTTGCC AAGGGTTCTT CAGGTGCCCC GATTCTGTGC TCCTCCGGGC ATGTTATTGG 3720 GATGTTCACC GCTGCTAGAA ATTCTGGCGG TTCAGTCAGC CAGATTAGGG TTAGGCCGTT 3780 GGTGTGTGCT GGATACCATC CCCAGTACAC AGCACATGCC ACTCTTGATA CAAAACCTAC 3840 TGTGCCTAAC GAGTATTCAG TGCAAATTTT AATTGCCCCC ACTGGCAGCG GCAAGTCAAC 3900 CAAATTACCA CTTTCTTACA TGCAGGAGAA GTATGAGGTC TTGGTCCTAA ATCCCAGTGT 3960 GGCTACAACA GCATCAATGC CAAAGTACAT GCACGCGACG TACGGCGTGA ATCCAAATTG 4020 CTATTTTAAT GGCAAATGTA CCAACACAGG GGCTTCACTT ACGTACAGCA CATATGGCAT 4080 GTACCTGACC GGAGCATGTT CCCGGAACTA TGACGTCATC ATTTGTGACG AATGCCATGC 4140 430 TACCGATGCA ACCACCGTGT TGGGCATTGG AAAGGTTCTA ACCGAAGCTC CATCCAAAAA 4200 TGTTAGGCTA GTGGTTCTTG CCACGGCTAC CCCCCCTGGA GTAATCCCTA CACCACATGC 4260 CAACATAACT GAGATTCAAT TAACCGATGA AGGCACTATC CCCTTTCATG GAAAAAAGAT 4320 TAAGGAGGAA AATCTGAAGA AAGGGAGACA CCTTATCTTT GAGGCTACCA AAAAACACTG 4380 TGATGAGCTT GCTAACGAGT TAGCTCGAAA GGGAATAACA GCTGTCTCTT ACTATAGGGG 4440 ATGTGACATC TCAAAAATCC CTGAGGGCGA CTGTGTAGTA GTTGCCACTG ATGCCTTGTG 4500 TACAGGGTAC ACTGGTGACT TTGATTCCGT GTATGACTGC AGCCTCATGG TAGAAGGCAC 4560 ATGCCATGTT GACCTTGACC CTACTTTCAC CATGGGTGTT CGTGTGTGCG GGGTCTCAGC 4620 AATAGTTAAA GGCCAGCGTA GGGGCCGCAC AGGCCGTGGG AGAGCTGGCA TATACTACTA 4680 TGTAGACGGG AGTTGTACCC CTTCGGGTAT GGTTCCTGAA TGCAACATTG TTGAAGCCTT 4740 CGACGCAGCC AAGGCATGGT ATGGTTTGTC ATCAACAGAA GCTCAAACTA TTCTGGACAC 4800 CTATCGCACC CAACCTGGGT TACCTGCGAT AGGAGCAAAT TTGGACGAGT GGGCTGATCT 4860 CTTTTCTATG GTCAACCCCG AACCTTCATT TGTCAATACT GCAAAAAGAA CTGCTGACAA 4920 TTATGTTTTG TTGACTGCAG CCCAACTACA ACTGTGTCAT CAGTATGGCT ATGCTGCTCC 4980 CAATGACGCA CCACGGTGGC AGGGAGCCCG GCTTGGGAAA AAACCTTGTG GGGTTCTGTG 5040 GCGCTTGGAC GGCGCTGACG CCTGTCCTGG CCCAGAGCCC AGCGAGGTGA CCAGATACCA 5100 AATGTGCTTC ACTGAAGTCA ATACTTCTGG GACAGCCGCA CTCGCTGTTG GCGTTGGAGT 5160 GGCTATGGCT TATCTAGCCA TTGACACTTT TGGCGCCACT TGTGTGCGGC GTTGCTGGTC 5220 TATTACATCA GTCCCTACCG GTGCTACTGT CGCCCCAGTG GTTGACGAAG AAGAAATCGT 5280 GGAGGAGTGT GCATCATTCA TTCCCTTGGA GGCCATGGTT GCTGCAATCG ATAAGCTGAA 5340 GAGTACAATA ACCACAACTA GTCCTTTCAC ATTGGAAACC GCCCTTGAAA AACTTAACAC 5400 CTTTCTTGGG CCTCATGCAG CTACAATCCT TGCTATCATA GAGTATTGCT GTGGCTTAGT 5460 CACTTTACCT GACAATCCCT TTGCATCATG CGTGTTTGCT TTCATTGCGG GTATTACTAC 5520 CCCACTACCT CACAAGATCA AAATGTTCCT GTCATTATTT GGAGGCGCAA TTGCGTCCAA 5580 GCTTACAGAC GCTAGAGGCG CACTGGCGTT CATGATGGCC GGGGCTGCGG GAACAGCTCT 5640 TGGTACATGG ACATCGGTGG GTTTTGTCTT TGACATGCTA GGCGGCTATG CTGCCGCCTC 5700 ATCCACTGCT TGCTTGACAT TTAAATGCTT GATGGGTGAG TGGCCCACTA TGGATCAGCT 5760 TGCTGGTTTA GTCTACTCCG CGTTCAATCC GGCCGCAGGA GTTGTGGGCG TCTTGTCAGC 5820 TTGTGCAATG TTTGCTTTGA CAACAGCAGG GCCAGATCAC TGGCCCAACA GACTTCTTAC 5880 O95/21922 431 TATGCTTGCT AGGAGCAACA CTGTATGTAA TGAGTACTTT ATTGCCACTC GTGACATCCG 5940 CAGGAAGATA CTGGGCATTC TGGAGGCATC TACCCCCTGG AGTGTCATAT CAGCTTGCAT 6000 CCGTTGGCTC CACACCCCGA CGGAGGATGA TTGCGGCCTC ATTGCTTGGG GTCTAGAGAT 6060 TTGGCAGTAT GTGTGCAATT TCTTTGTGAT TTGCTTTAAT GTCCTTAAAG CTGGAGTTCA 6120 GAGCATGGTT AACATTCCTG GTTGTCCTTT CTACAGCTGC CAGAAGGGGT ACAAGGGCCC 6180 CTGGATTGGA TCAGGTATGC TCCAAGCACG CTGTCCATGC GGTGCTGAAC TCATCTTTTC 6240 TGTTGAGAAT GGTTTTGCAA AACTTTACAA AGGACCCAGA ACTTGTTCAA ATTACTGGAG 6300 AGGGGCTGTT CCAGTCAACG CTAGGCTGTG TGGGTCGGCT AGACCGGACC CAACTGATTG 6360 GACTAGTCTT GTCGTCAATT ATGGCGTTAG GGACTACTGT AAATATGAGA AATTGGGAGA 6420 TCACATTTTT GTTACAGCAG TATCCTCTCC AAATGTCTGT TTCACCCAGG TGCCCCCAAC 6480 CTTGAGAGCT GCAGTGGCCG TGGACGGCGT ACAGGTTCAG TGTTATCTAG GTGAGCCCAA 6540 AACTCCTTGG ACGACATCTG CTTGCTGTTA CGGTCCGGAC GGTAAGGGTA AAACTGTTAA 6600 GCTTCCCTTC CGCGTTGACG GTCACACACC TGGTGTGCGC ATGCAACTTA ATTTGCGTGA 6660 TGCACTTGAG ACAAATGACT GTAATTCCAT AAACAACACT CCTAGTGATG AAGCCGCAGT 6720 GTCCGCTCTT GTTTTCAAAC AGGAGTTGCG GCGTACAAAC CAATTGCTTG AGGCAATTTC 6780 AGCTGGCGTT GACACCACCA AACTGCCAGC CCCCTCCATC GAAGAGGTAG TGGTAAGAAA 6840 GCGCCAGTTC CGGGCAAGAA CTGGTTCGCT TACCTTGCCT CCCCCTCCGA GATCCGTCCC 6900 AGGAGTGTCA TGTCCTGAAA GCCTGCAACG AAGTGACCCG TTAGAAGGTC CTTCAAACCT 6960 CCCTTCTTCA CCACCTGTTC TACAGTTGGC CATGCCGATG CCCCTGTTGG GAGCAGGTGA 7020 GTGTAACCCT TTCACTGCAA TTGGATGTGC AATGACCGAA ACAGGCGGAG GCCCTGATGA 7080 TTTACCCAGT TACCCTCCCA AAAAGGAGGT CTCTGAATGG TCAGACGGAA GTTGGTCAAC 7140 GACTACAACC GCTTCCAGCT ACGTTACTGG CCCCCCGTAC CCTAAGATAC GGGGAAAGGA 7200 TTCCACTCAG TCAGCCCCCG CCAAACGGCC TACAAAAAAG AAGTTGGGAA AGAGTGAGTT 7260 TTCGTGCAGC ATGAGCTACA CTTGGACCGA CGTGATTAGC TTCAAAACTG CTTCTAAAGT 7320 TCTGTCTGCA ACTCGGGCCA TCACTAGTGG TTTCCTCAAA CAAAGATCAT TGGTGTATGT 7380 GACTGAGCCG CGGGATGCGG AGCTTAGAAA ACAAAAAGTC ACTATTAATA GACAACCTCT 7440 GTTCCCCCCA TCATACCACA AGCAAGTGAG ATTGGCTAAG GAAAAAGCTT CAAAAGTTGT 7500 CGGTGTCATG TGGGACTATG ATGAAGTAGC AGCTCACACG CCCTCTAAGT CTGCTAAGTC 7560 CCACATCACT GGCCTTCGGG GCACTGATGT TCGTTCTGGA GCAGCCCGCA AGGCTGTTCT 7620 432 GGACTTGCAG AAGTGTGTCG AGGCAGGTGA GATACCGAGT CATTATCGGC AAACTGTGAT 7680 AGTTCCAAAG GAGGAGGTCT TCGTGAAGAC CCCCCAGAAA CCAACAAAGA AACCCCCAAG 7740 GCTTATCTCG TACCCCCACC TTGAAATGAG ATGTGTTGAG AAGATGTACT ACGGTCAGGT 7800 TGCTCCTGAC GTAGTTAAAG CTGTCATGGG AGATGCGTAC GGGTTTGTCG ACCCACGTAC 7860 CCGTGTCAAG CGTCTGTTGT CGATGTGGTC ACCCGATGCA GTCGGAGCCA CATGCGATAC 7920 AGTGTGTTTT GACAGTACCA TCACACCCGA GGATATCATG GTGGAGACAG ACATCTACTC 7980 AGCAGCTAAA CTCAGTGACC AACACCGAGC TGGCATTCAC ACCATTGCGA GGCAGTTATA 8040 CGCTGGAGGA CCGATGATCG CTTATGATGG CCGAGAGATC GGATATCGTA GGTGTAGGTC 8100 TTCCGGCGTC TATACTACCT CAAGTTCCAA CAGTTTGACC TGCTGGCTGA AGGTAAATGC 8160 TGCAGCCGAA CAGGCTGGCA TGAAGAACCC TCGCTTCCTT ATTTGCGGCG ATGATTGCAC 8220 CGTAATTTGG AAGAGCGCCG GAGCAGATGC AGACAAACAA GCAATGCGTG TCTTTGCTAG 8280 CTGGATGAAG GTGATGGGTG CACCACAAGA TTGTGTGCCT CAACCCAAAT ACAGTTTGGA 8340 AGAATTAACA TCATGCTCAT CAAATGTTAC CTCTGGAATT ACCAAAAGTG GCAAGCCTTA 8400 CTACTTTCTT ACAAGAGATC CTCGTATCCC CCTTGGCAGG TGCTCTGCCG AGGGTCTGGG 8460 ATACAACCCC AGTGCTGCGT GGATTGGGTA TCTAATACAT CACTACCCAT GTTTGTGGGT 8520 TAGCCGTGTG TTGGCTGTCC ATTTCATGGA GCAGATGCTC TTTGAGGACA AACTTCCCGA 8580 GACTGTGACC TTTGACTGGT ATGGGAAAAA TTATACGGTG CCTGTAGAAG ATCTGCCCAG 8640 CATCATTGCT GGTGTGCACG GTATTGAGGC TTTCTCGGTG GTGCGCTACA CCAACGCTGA 8700 GATCCTCAGA GTTTCCCAAT CACTAACAGA CATGACCATG CCCCCCCTGC GAGCCTGGCG 8760 AAAGAAAGCC AGGGCGGTCC TCGCCAGCGC CAAGAGGCGT GGCGGAGCAC ACGCAAAATT 8820 GGCTCGCTTC CTTCTCTGGC ATGCTACATC TAGACCTCTA CCAGATTTGG ATAAGACGAG 8880 CGTGGCTCGG TACACCACTT TCAATTATTG TGATGTTTAC TCCCCGGAGG GGGATGTGTT 8940 TGTTACACCA CAGAGAAGAT TGCAGAAGTT TCTTGTGAAG TATTTGGCTG TCATTGTTTT 9000 TGCCCTAGGG CTCATTGCTG TTGGACTAGC CATCAGCTGA ACCCCCAAAT TCAAAATTAA 9060 TTAACAGTTT TTTTTTTTTT TTTTTTTTTT TTTTAGGGCA GCGGCAACAG GGGAGACCCC 9120 GGGCTTAACG ACCCCGCGAT GTG 9143 (2) INFORMATION FOR SEQ ID NO:394: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 234 base paire (B) TYPE: nucleic acid 433 (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:394: GATCAGGTAT GCTCCAAGCA CGCTGTCCAT GCGGTGCTGA ACTCATCTTT TCTGTTGAGA 60 ATGGTTTTGC AAAACTTTAC AAAGGACCCA GAACTTGTTC AAATTACTGG AGAGGGGCTG 120 TTCCAGTCAA CGCTAGGCTG TGTGGGTCGG CTAGACCGGA CCCAACTGAT TGGACTAGTC 180 TTGTCGTCAA TTATGGCGTT AGGGACTACT GTAAATATGA GAAATTGGGA GATC 234 (2) INFORMATION FOR SEQ ID NO:395: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 479 baβe pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:395: GATCACATTT TTGTTACAGC AGTATCCTCT CCAAATGTCT GTTTCACCCA GGTGCCCCCA 60 ACCTTGAGAG CTGCAGTGGC CGTGGACCGC GTACAGGTTC AGYGTTATCT AGGTGAGCCC 120 AAAACTCCTT GGACGACATC TGCTTGCTGT TACGGTCCTG ACGGTAAGGG TAAAACTGTT 180 AAGCTTCCCT TCCGCGTTGA CGGACACACA CCTGGTGGTC GCATGCAACT TAATTTGCGT 240 GATCGACTTG AGGCAAATGA CTGTAATTCC ATAAACAACA CTCCTAGTGA TGAAGCCGCA 300 GTGTCCGCTC TTGTTTTCAA ACAGGAGTTG CGGCGTACAA ACCAATTGCT TGAGGCAATT 360 TCAGCTGGCG TTGACACCAC CAAACTGCCA GCCCCCTCCC AGATCGAAGA GGTAGTGGTA 420 AGAAAGCGCC AGTTCCGGGC AAGAACTGGT TCGCTTACCT TGCCTCCCCC TCCGAGATC 479 (2) INFORMATION FOR SEQ ID NO:396: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9143 baee paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear 434 (ii) MOLECULE TYPE : DNA (genomic) (ix) FEATURE : (A) NAME/KEY: 5 ' UTR (B) LOCATION : 1 . .445 (ix) FEATURE : (A) NAME/KEY: CDS (B) LOCATION : 446 . . 9037 (ix) FEATURE: (A) NAME/KEY: 3'UTR (B) LOCATION: 9038..9143 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:396: ACCACAAACA CTCCAGTTTG TTACACTCCG CTAGGAATGC TCCTGGAGCA CCCCCCCTAG 60 CAGGGCGTGG GGGATTTCCC CTGCCCGTCT GCAGAAGGGT GGAGCCAACC ACCTTAGTAT 120 GTAGGCGGCG GGACTCATGA CGCTCGCGTG ATGACAAGCG CCAAGCTTGA CTTGGATGGC 180 CCTGATGGGC GTTCATGGGT TCGGTGGTGG TGGCGCTTTA GGCAGCCTCC ACGCCCACCA 240 CCTCCCAGAT AGAGCGGCGG CACTGTAGGG AAGACCGGGG ACCGGTCACT ACCAAGGACG 300 CAGACCTCTT TTTGAGTATC ACGCCTCCGG AAGTAGTTGG GCAAGCCCAC CTATATGTGT 360 TGGGATGGTT GGGGTTAGCC ATCCATACCG TACTGCCTGA TAGGGTCCTT GCGAGGGGAT 420 CTGGGAGTCT CGTAGACCGT AGCAC ATG CCT GTT ATT TCT ACT CAA ACA AGT 472 Met Pro Val He Ser Thr Gin Thr Ser 1 5 CCT GTA CCT GCG CCC AGA ACG CGC AAG AAC AAG CAG ACG CAG GCT TCA 520 Pro Val Pro Ala Pro Arg Thr Arg Lye Asn Lys Gin Thr Gin Ala Ser 10 15 20 25 TAT CCT GTG TCC ATT AAA ACA TCT GTT GAA AGG GGA CAA CGA GCA AAG 568 Tyr Pro Val Ser He Lys Thr Ser Val Glu Arg Gly Gin Arg Ala Lye 30 35 40 CGC AAA GTC CAG CGC GAT GCT CGG CCT CGT AAT TAC AAA ATT GCT GGT 616 Arg Lye Val Gin Arg Aep Ala Arg Pro Arg Aβn Tyr Lys He Ala Gly 45 50 55 ATC CAT GAT GGC TTG CAG ACA TTG GCT CAG GCT GCT TTG CCA GCT CAT 664 He His Asp Gly Leu Gin Thr Leu Ala Gin Ala Ala Leu Pro Ala His 60 65 70 GGT TGG GGA CGC CAA GAC CCT CGC CAT AAG TCT CGC AAT CTT GGA ATC 712 Gly Trp Gly Arg Gin Asp Pro Arg His Lys Ser Arg Asn Leu Gly He 75 80 85 CTT CTG GAT TAC CCT TTG GGG TGG ATT GGT GAT GTT ACA ACT CAC ACA 760 435 Leu Leu Aep Tyr Pro Leu Gly Trp He Gly Aep Val Thr Thr Hiβ Thr 90 95 100 105 CCT CTA GTA GGC CCG CTG GTG GCA GGA GCG GTC GTT CGA CCA GTC TGC 808 Pro Leu Val Gly Pro Leu Val Ala Gly Ala Val Val Arg Pro Val Cyβ 110 115 120 CAG ATA GTA CGC TTG CTG GAG GAT GGA GTC AAC TGG GCT ACT GGT TGG 856 Gin He Val Arg Leu Leu Glu Aep Gly Val Aβn Trp Ala Thr Gly Trp 125 130 135 TTC GGT GTC CAC CTT TTT GTG GTA TGT CTG CTA TCT TTG GCC TGT CCC 904 Phe Gly Val Hiβ Leu Phe Val Val Cys Leu Leu Ser Leu Ala Cyβ Pro 140 145 150 TGT AGT GGG GCG CGG GTC ACT GAC CCA GAC ACA AAT ACC ACA ATC CTG 952 Cyβ Ser Gly Ala Arg Val Thr Aep Pro Aep Thr Aβn Thr Thr He Leu 155 160 165 ACC AAT TGC TGC CAG CGT AAT CAG GTT ATC TAT TGT TCT CCT TCC ACT 1000 Thr Asn Cys Cys Gin Arg Asn Gin Val He Tyr Cys Ser Pro Ser Thr 170 175 180 185 TGC CTA CAC GAG CCT GGT TGT GTG ATC TGC GCG GAC GAG TGC TGG GTT 1048 Cye Leu Hie Glu Pro Gly Cye Val He Cyβ Ala Aep Glu Cys Trp Val 190 195 200 CCC GCC AAT CCG TAC ATC TCA CAC CCT TCC AAT TGG ACT GGC ACG GAC 1096 Pro Ala Asn Pro Tyr He Ser His Pro Ser Aβn Trp Thr Gly Thr Aep 205 210 215 TCC TTC TTG GCT GAC CAC ATT GAT TTT GTT ATG GGC GCT CTT GTG ACC 1144 Ser Phe Leu Ala Aep Hiβ He Asp Phe Val Met Gly Ala Leu Val Thr 220 225 230 TGT GAC GCC CTT GAC ATT GGT GAG TTG TGT GGT GCG TGT GTA TTA GTC 1192 Cys Asp Ala Leu Aep He Gly Glu Leu Cys Gly Ala Cyβ Val Leu Val 235 240 245 GGT GAC TGG CTT GTC AGG CAC TGG CTT ATT CAC ATA GAC CTC AAT GAA 1240 Gly Aep Trp Leu Val Arg Hiβ Trp Leu He Hiβ He Asp Leu Aβn Glu 250 255 260 265 ACT GGT ACT TGT TAC CTG GAA GTG CCC ACT GGA ATA GAT CCT GGG TTC 1288 Thr Gly Thr Cyβ Tyr Leu Glu Val Pro Thr Gly He Aep Pro Gly Phe 270 275 280 CTA GGG TTT ATC GGG TGG ATG GCC GGC AAG GTC GAG GCT GTC ATC TTC 1336 Leu Gly Phe He Gly Trp Met Ala Gly Lye Val Glu Ala Val He Phe 285 290 295 TTG ACC AAA CTG GCT TCA CAA GTA CCA TAC GCT ATT GCG ACT ATG TTT 1384 Leu Thr Lye Leu Ala Ser Gin Val Pro Tyr Ala He Ala Thr Met Phe 300 305 310 AGC AGT GTA CAC TAC CTG GCG GTT GGC GCT CTG ATC TAC TAT GCC TCT 1432 Ser Ser Val His Tyr Leu Ala Val Gly Ala Leu He Tyr Tyr Ala Ser 436 315 320 325 CGG GGC AAG TGG TAT CAG TTG CTC CTA GCG CTT ATG CTT TAC ATA GAA 1480 Arg Gly Lye Trp Tyr Gin Leu Leu Leu Ala Leu Met Leu Tyr He Glu 330 335 340 345 GCG ACC TCT GGA AAC CCT ATC AGG GTG CCC ACT GGA TGC TCA ATA GCT 1528 Ala Thr Ser Gly Aβn Pro He Arg Val Pro Thr Gly Cyβ Ser He Ala 350 355 360 GAG TTT TGC TCG CCT TTG ATG ATA CCA TGT CCT TGC CAC TCT TAT TTG 1576 Glu Phe Cyβ Ser Pro Leu Met He Pro Cyβ Pro Cyβ Hiβ Ser Tyr Leu 365 370 375 AGT GAG AAT GTG TCA GAA GTC ATT TGT TAC AGT CCA AAG TGG ACC AGG 1624 Ser Glu Aβn Val Ser Glu Val He Cyβ Tyr Ser Pro Lye Trp Thr Arg 380 385 390 CCT GTC ACT CTA GAG TAT AAC AAC TCC ATA TCT TGG TAC CCC TAT ACA 1672 Pro Val Thr Leu Glu Tyr Aβn Aen Ser He Ser Trp Tyr Pro Tyr Thr 395 400 405 ATC CCT GGT GCG AGG GGA TGT ATG GTT AAA TTC AAA AAT AAC ACA TGG 1720 He Pro Gly Ala Arg Gly Cys Met Val Lys Phe Lys Asn Asn Thr Trp 410 415 420 425 GGT TGC TGC CGT ATT CGC AAT GTG CCA TCG TAC TGC ACT ATG GGC ACT 1768 Gly Cys Cys Arg He Arg Asn Val Pro Ser Tyr Cyβ Thr Met Gly Thr 430 435 440 GAT GCA GTG TGG AAC GAC ACT CGC AAC ACT TAC GAA GCA TGC GGT GTA 1816 Aep Ala Val Trp Aen Asp Thr Arg Asn Thr Tyr Glu Ala Cyβ Gly Val 445 450 455 ACA CCA TGG CTA ACA ACC GCA TGG CAC AAC GGC TCA GCC CTG AAA TTG 1864 Thr Pro Trp Leu Thr Thr Ala Trp Hiβ Aβn Gly Ser Ala Leu Lye Leu 460 465 470 GCT ATA TTA CAA TAC CCT GGG TCT AAA GAA ATG TTT AAA CCT CAT AAT 1912 Ala He Leu Gin Tyr Pro Gly Ser Lye Glu Met Phe Lye Pro Hie Aβn 475 480 485 TGG ATG TCA GGC CAT TTG TAT TTT GAG GGA TCA GAT ACC CCT ATA GTT 1960 Trp Met Ser Gly Hiβ Leu Tyr Phe Glu Gly Ser Aep Thr Pro He Val 490 495 500 • 505 TAC TTT TAT GAC CCT GTG AAT TCC ACT CTC CTA CCA CCG GAG AGG TGG 2008 Tyr Phe Tyr Aep Pro Val Asn Ser Thr Leu Leu Pro Pro Glu Arg Trp 510 515 520 GCT AGG TTG CCC GGT ACC CCA CCT GTG GTA CGT GGT TCT TGG TTA CAG 2056 Ala Arg Leu Pro Gly Thr Pro Pro Val Val Arg Gly Ser Trp Leu Gin 525 530 535 GTT CCG CAA GGG TTT TAC AGT GAT GTG AAA GAC CTA GCC ACA GGA TTG 2104 Val Pro Gin Gly Phe Tyr Ser Asp Val Lys Asp Leu Ala Thr Gly Leu 540 545 550 437 ATC ACC AAA GAC AAA GCC TGG AAA AAT TAT CAG GTC TTA TAT TCC GCC 2152 He Thr Lys Asp Lye Ala Trp Lye Aβn Tyr Gin Val Leu Tyr Ser Ala 555 560 565 ACG GGT GCT TTG TCT CTT ACG GGA GTT ACC ACC AAG GCC GTG GTG CTA 2200 Thr Gly Ala Leu Ser Leu Thr Gly Val Thr Thr Lye Ala Val Val Leu 570 575 580 585 ATT CTG TTG GGG TTG TGT GGC AGC AAG TAT CTT ATT TTA GCC TAC CTC 2248 He Leu Leu Gly Leu Cys Gly Ser Lye Tyr Leu He Leu Ala Tyr Leu 590 595 600 TGT TAC TTG TCC CTT TGT TTT GGG CGC GCT TCT GGT TAC CCT TTG CGT 2296 Cys Tyr Leu Ser Leu Cys Phe Gly Arg Ala Ser Gly Tyr Pro Leu Arg 605 610 615 CCT GTG CTC CCA TCC CAG TCG TAT CTC CAA GCT GGC TGG GAT GTT TTG 2344 Pro Val Leu Pro Ser Gin Ser Tyr Leu Gin Ala Gly Trp Asp Val Leu 620 625 630 TCT AAA GCT CAA GTA GCT CCT TTT GCT TTG ATT TTC TTC ATC TGT TGC 2392 Ser Lys Ala Gin Val Ala Pro Phe Ala Leu He Phe Phe He Cys Cys 635 640 645 TAT CTC CGC TGC AGG CTA CGT TAT GCT GCC CTT TTA GGG TTT GTG CCC 2440 Tyr Leu Arg Cye Arg Leu Arg Tyr Ala Ala Leu Leu Gly Phe Val Pro 650 655 660 665 ATG GCT GCG GGC TTG CCC CTA ACT TTC TTT GTT GCA GCA GCT GCT GCC 2488 Met Ala Ala Gly Leu Pro Leu Thr Phe Phe Val Ala Ala Ala Ala Ala 670 675 680 CAA CCA GAT TAT GAC TGG TGG GTG CGA CTG CTA GTG GCA GGG TTA GTT 2536 Gin Pro Aep Tyr Asp Trp Trp Val Arg Leu Leu Val Ala Gly Leu Val 685 690 695 TTG TGG GCC GGC CGT GAC CGT GGT CCA CGT ATA GCT CTG CTT GTA GGT 2584 Leu Trp Ala Gly Arg Asp Arg Gly Pro Arg He Ala Leu Leu Val Gly 700 705 710 CCT TGG CCT CTG GTA GCG CTT TTA ACC CTC TTG CAT TTG GCT ACG CCT 2632 Pro Trp Pro Leu Val Ala Leu Leu Thr Leu Leu His Leu Ala Thr Pro 715 720 725 GCT TCA GCT TTT GAC ACC GAG ATA ATT GGA GGG CTG ACA ATA CCA CCT 2680 Ala Ser Ala Phe Asp Thr Glu He He Gly Gly Leu Thr He Pro Pro 730 735 740 745 GTA GTA GCA TTA GTT GTC ATG TCT CGT TTT GGC TTC TTT GCT CAC TTG 2728 Val Val Ala Leu Val Val Met Ser Arg Phe Gly Phe Phe Ala His Leu 750 755 760 TTA CCT CGC TGT GCT TTA GTT AAC TCC TAT CTT TGG CAA CGT TGG GAG 2776 Leu Pro Arg Cys Ala Leu Val Aen Ser Tyr Leu Trp Gin Arg Trp Glu 765 770 775 AAT TGG TTT TGG AAC GTT ACA CTA AGA CCG GAG AGG TTT CTC CTT GTG 2824 438 Aβn Trp Phe Trp Asn Val Thr Leu Arg Pro Glu Arg Phe Leu Leu Val 780 785 790 CTG GTT TGT TTC CCC GGT GCG ACA TAT GAC ACG CTG GTG ACT TTC TGT 2872 Leu Val Cys Phe Pro Gly Ala Thr Tyr Aep Thr Leu Val Thr Phe Cyβ 795 800 805 GTG TGT CAC GTA GCT CTT CTA TGT TTA ACA TCC AGT GCA GCA TCG TTC 2920 Val Cye Hiβ Val Ala Leu Leu Cyβ Leu Thr Ser Ser Ala Ala Ser Phe 810 815 820 825 TTT GGG ACT GAC TCT AGG GTT AGG GCC CAT AGA ATG TTG GTG CGT CTC 2968 Phe Gly Thr Aep Ser Arg Val Arg Ala Hiβ Arg Met Leu Val Arg Leu 830 835 840 GGA AAG TGT CAT GCT TGG TAT TCT CAT TAT GTT CTT AAG TTT TTC CTC 3016 Gly Lye Cye Hie Ala Trp Tyr Ser Hie Tyr Val Leu Lye Phe Phe Leu 845 850 855 TTA GTG TTT GGT GAG AAT GGT GTG TTT TTC TAT AAG CAC TTG CAT GGT 3064 Leu Val Phe Gly Glu Aβn Gly Val Phe Phe Tyr Lye Hiβ Leu Hiβ Gly 860 865 870 GAT GTC TTG CCT AAT GAT TTT GCC TCG AAA CTA CCA TTG CAA GAG CCA 3112 Asp Val Leu Pro Asn Asp Phe Ala Ser Lys Leu Pro Leu Gin Glu Pro 875 880 885 TTT TTC CCT TTT GAA GGC AAG GCA AGG GTC TAT AGG AAT GAA GGA AGA 3160 Phe Phe Pro Phe Glu Gly Lys Ala Arg Val Tyr Arg Asn Glu Gly Arg 890 895 900 905 CGC TTG GCG TGT GGG GAC ACG GTT GAT GGT TTG CCC GTT GTT GCG CGT 3208 Arg Leu Ala Cys Gly Asp Thr Val Aep Gly Leu Pro Val Val Ala Arg 910 915 920 CTC GGC GAC CTT GTT TTC GCA GGG TTA GCT ATG CCG CCA GAT GGG TGG 3256 Leu Gly Aep Leu Val Phe Ala Gly Leu Ala Met Pro Pro Aep Gly Trp 925 930 935 GCC ATT ACC GCA CCT TTT ACG CTG CAG TGT CTC TCT GAA CGT GGC ACG 3304 Ala He Thr Ala Pro Phe Thr Leu Gin Cye Leu Ser Glu Arg Gly Thr 940 945 950 CTG TCA GCG ATG GCA GTG GTC ATG ACT GGT ATA GAC CCC CGA ACT TGG 3352 Leu Ser Ala Met Ala Val Val Met Thr Gly He Aep Pro Arg Thr Trp 955 960 965 ACT GGA ACT ATC TTC AGA TTA GGA TCT CTG GCC ACT AGC TAC ATG GGA 3400 Thr Gly Thr He Phe Arg Leu Gly Ser Leu Ala Thr Ser Tyr Met Gly 970 975 980 985 TTT GTT TGT GAC AAC GTG TTG TAT ACT GCT CAC CAT GGC AGC AAG GGG 3448 Phe Val Cyβ Aep Aβn Val Leu Tyr Thr Ala Hiβ His Gly Ser Lye Gly 990 995 1000 CGC CGG TTG GCT CAT CCC ACA GGC TCC ATA CAC CCA ATA ACC GTT GAC 3496 Arg Arg Leu Ala Hiβ Pro Thr Gly Ser He Hiβ Pro He Thr Val Aep 439 1005 1010 1015 GCG GCT AAT GAC CAG GAC ATC TAT CAA CCA CCA TGT GGA GCT GGG TCC 3544 Ala Ala Asn Aep Gin Aep He Tyr Gin Pro Pro Cyβ Gly Ala Gly Ser 1020 1025 1030 CTT ACT CGG TGC TCT TGC GGG GAG ACC AAG GGG TAT CTG GTA ACA CGA 3592 Leu Thr Arg Cye Ser Cye Gly Glu Thr Lye Gly Tyr Leu Val Thr Arg 1035 1040 1045 CTG GGG TCA TTG GTT GAG GTC AAC AAA TCC GAT GAC CCT TAT TGG TGT 3640 Leu Gly Ser Leu Val Glu Val Aβn Lye Ser Aep Asp Pro Tyr Trp Cys 1050 1055 1060 1065 GTG TGC GGG GCC CTT CCC ATG GCT GTT GCC AAG GGT TCT TCA GGT GCC 3688 Val Cys Gly Ala Leu Pro Met Ala Val Ala Lys Gly Ser Ser Gly Ala 1070 1075 1080 CCG ATT CTG TGC TCC TCC GGG CAT GTT ATT GGG ATG TTC ACC GCT GCT 3736 Pro He Leu Cys Ser Ser Gly His Val He Gly Met Phe Thr Ala Ala 1085 1090 1095 AGA AAT TCT GGC GGT TCA GTC AGC CAG ATT AGG GTT AGG CCG TTG GTG 3784 Arg Aβn Ser Gly Gly Ser Val Ser Gin He Arg Val Arg Pro Leu Val 1100 1105 1110 TGT GCT GGA TAC CAT CCC CAG TAC ACA GCA CAT GCC ACT CTT GAT ACA 3832 Cyβ Ala Gly Tyr His Pro Gin Tyr Thr Ala Hiβ Ala Thr Leu Aep Thr 1115 1120 1125 AAA CCT ACT GTG CCT AAC GAG TAT TCA GTG CAA ATT TTA ATT GCC CCC 3880 Lye Pro Thr Val Pro Aen Glu Tyr Ser Val Gin He Leu He Ala Pro 1130 1135 1140 H45 ACT GGC AGC GGC AAG TCA ACC AAA TTA CCA CTT TCT TAC ATG CAG GAG 3928 Thr Gly Ser Gly Lye Ser Thr Lys Leu Pro Leu Ser Tyr Met Gin Glu 1150 1155 1160 AAG TAT GAG GTC TTG GTC CTA AAT CCC AGT GTG GCT ACA ACA GCA TCA 3976 Lys Tyr Glu Val Leu Val Leu Asn Pro Ser Val Ala Thr Thr Ala Ser 1165 1170 1175 ATG CCA AAG TAC ATG CAC GCG ACG TAC GGC GTG AAT CCA AAT TGC TAT 4024 Met Pro Lye Tyr Met Hie Ala Thr Tyr Gly Val Aβn Pro Aβn Cyβ Tyr 1180 1185 1190 TTT AAT GGC AAA TGT ACC AAC ACA GGG GCT TCA CTT ACG TAC AGC ACA 4072 Phe Aβn Gly Lys Cys Thr Asn Thr Gly Ala Ser Leu Thr Tyr Ser Thr 1195 1200 1205 TAT GGC ATG TAC CTG ACC GGA GCA TGT TCC CGG AAC TAT GAC GTC ATC 4120 Tyr Gly Met Tyr Leu Thr Gly Ala Cye Ser Arg Aen Tyr Aep Val He 1210 1215 1220 1225 ATT TGT GAC GAA TGC CAT GCT ACC GAT GCA ACC ACC GTG TTG GGC ATT 4168 He Cyβ Aep Glu Cyβ His Ala Thr Aep Ala Thr Thr Val Leu Gly He 1230 1235 1240 440 GGA AAG GTT CTA ACC GAA GCT CCA TCC AAA AAT GTT AGG CTA GTG GTT 4216 Gly Lys Val Leu Thr Glu Ala Pro Ser Lys Asn Val Arg Leu Val Val 1245 1250 1255 CTT GCC ACG GCT ACC CCC CCT GGA GTA ATC CCT ACA CCA CAT GCC AAC 4264 Leu Ala Thr Ala Thr Pro Pro Gly Val He Pro Thr Pro His Ala Asn 1260 1265 1270 ATA ACT GAG ATT CAA TTA ACC GAT GAA GGC ACT ATC CCC TTT CAT GGA 4312 He Thr Glu He Gin Leu Thr Asp Glu Gly Thr He Pro Phe His Gly 1275 1280 1285 AAA AAG ATT AAG GAG GAA AAT CTG AAG AAA GGG AGA CAC CTT ATC TTT 4360 Lys Lys He Lys Glu Glu Asn Leu Lys Lys Gly Arg His Leu He Phe 1290 1295 1300 1305 GAG GCT ACC AAA AAA CAC TGT GAT GAG CTT GCT AAC GAG TTA GCT CGA 4408 Glu Ala Thr Lys Lys Hie Cye Asp Glu Leu Ala Asn Glu Leu Ala Arg 1310 1315 1320 AAG GGA ATA ACA GCT GTC TCT TAC TAT AGG GGA TGT GAC ATC TCA AAA 4456 Lys Gly He Thr Ala Val Ser Tyr Tyr Arg Gly Cys Asp He Ser Lye 1325 1330 1335 ATC CCT GAG GGC GAC TGT GTA GTA GTT GCC ACT GAT GCC TTG TGT ACA 4504 He Pro Glu Gly Aep Cyβ Val Val Val Ala Thr Asp Ala Leu Cys Thr 1340 1345 1350 GGG TAC ACT GGT GAC TTT GAT TCC GTG TAT GAC TGC AGC CTC ATG GTA 4552 Gly Tyr Thr Gly Aep Phe Aep Ser Val Tyr Asp Cys Ser Leu Met Val 1355 1360 1365 GAA GGC ACA TGC CAT GTT GAC CTT GAC CCT ACT TTC ACC ATG GGT GTT 4600 Glu Gly Thr Cys His Val Asp Leu Asp Pro Thr Phe Thr Met Gly Val 1370 1375 1380 1385 CGT GTG TGC GGG GTC TCA GCA ATA GTT AAA GGC CAG CGT AGG GGC CGC 4648 Arg Val Cys Gly Val Ser Ala He Val Lys Gly Gin Arg Arg Gly Arg 1390 1395 1400 ACA GGC CGT GGG AGA GCT GGC ATA TAC TAC TAT GTA GAC GGG AGT TGT 4696 Thr Gly Arg Gly Arg Ala Gly He Tyr Tyr Tyr Val Aep Gly Ser Cye 1405 1410 1415 ACC CCT TCG GGT ATG GTT CCT GAA TGC AAC ATT GTT GAA GCC TTC GAC 4744 Thr Pro Ser Gly Met Val Pro Glu Cyβ Aen He Val Glu Ala Phe Asp 1420 1425 1430 GCA GCC AAG GCA TGG TAT GGT TTG TCA TCA ACA GAA GCT CAA ACT ATT 4792 Ala Ala Lys Ala Trp Tyr Gly Leu Ser Ser Thr Glu Ala Gin Thr He 1435 1440 1445 CTG GAC ACC TAT CGC ACC CAA CCT GGG TTA CCT GCG ATA GGA GCA AAT 4840 Leu Asp Thr Tyr Arg Thr Gin Pro Gly Leu Pro Ala He Gly Ala Aen 1450 1455 1460 1465 TTG GAC GAG TGG GCT GAT CTC TTT TCT ATG GTC AAC CCC GAA CCT TCA 4888 441 Leu Asp Glu Trp Ala Asp Leu Phe Ser Met Val Asn Pro Glu Pro Ser 1470 1475 1480 TTT GTC AAT ACT GCA AAA AGA ACT GCT GAC AAT TAT GTT TTG TTG ACT 4936 Phe Val Asn Thr Ala Lys Arg Thr Ala Asp Aen Tyr Val Leu Leu Thr 1485 1490 1495 GCA GCC CAA CTA CAA CTG TGT CAT CAG TAT GGC TAT GCT GCT CCC AAT 4984 Ala Ala Gin Leu Gin Leu Cyβ Hiβ Gin Tyr Gly Tyr Ala Ala Pro Aβn 1500 1505 1510 GAC GCA CCA CGG TGG CAG GGA GCC CGG CTT GGG AAA AAA CCT TGT GGG 5032 Aep Ala Pro Arg Trp Gin Gly Ala Arg Leu Gly Lye Lye Pro Cys Gly 1515 1520 1525 GTT CTG TGG CGC TTG GAC GGC GCT GAC GCC TGT CCT GGC CCA GAG CCC 5080 Val Leu Trp Arg Leu Asp Gly Ala Asp Ala Cys Pro Gly Pro Glu Pro 1530 1535 1540 1545 AGC GAG GTG ACC AGA TAC CAA ATG TGC TTC ACT GAA GTC AAT ACT TCT 5128 Ser Glu Val Thr Arg Tyr Gin Met Cyβ Phe Thr Glu Val Aβn Thr Ser 1550 1555 1560 GGG ACA GCC GCA CTC GCT GTT GGC GTT GGA GTG GCT ATG GCT TAT CTA 5176 Gly Thr Ala Ala Leu Ala Val Gly Val Gly Val Ala Met Ala Tyr Leu 1565 1570 1575 GCC ATT GAC ACT TTT GGC GCC ACT TGT GTG CGG CGT TGC TGG TCT ATT 5224 Ala He Aep Thr Phe Gly Ala Thr Cyβ Val Arg Arg Cyβ Trp Ser He 1580 1585 1590 ACA TCA GTC CCT ACC GGT GCT ACT GTC GCC CCA GTG GTT GAC GAA GAA 5272 Thr Ser Val Pro Thr Gly Ala Thr Val Ala Pro Val Val Aep Glu Glu 1595 1600 1605 GAA ATC GTG GAG GAG TGT GCA TCA TTC ATT CCC TTG GAG GCC ATG GTT 5320 Glu He Val Glu Glu Cys Ala Ser Phe He Pro Leu Glu Ala Met Val 1610 1615 1620 1625 GCT GCA ATC GAT AAG CTG AAG AGT ACA ATA ACC ACA ACT AGT CCT TTC 5368 Ala Ala He Asp Lys Leu Lys Ser Thr He Thr Thr Thr Ser Pro Phe 1630 1635 1640 ACA TTG GAA ACC GCC CTT GAA AAA CTT AAC ACC TTT CTT GGG CCT CAT 5416 Thr Leu Glu Thr Ala Leu Glu Lys Leu Asn Thr Phe Leu Gly Pro His 1645 1650 1655 GCA GCT ACA ATC CTT GCT ATC ATA GAG TAT TGC TGT GGC TTA GTC ACT 5464 Ala Ala Thr He Leu Ala He He Glu Tyr Cys Cys Gly Leu Val Thr 1660 1665 1670 TTA CCT GAC AAT CCC TTT GCA TCA TGC GTG TTT GCT TTC ATT GCG GGT 5512 Leu Pro Asp Asn Pro Phe Ala Ser Cys Val Phe Ala Phe He Ala Gly 1675 1680 1685 ATT ACT ACC CCA CTA CCT CAC AAG ATC AAA ATG TTC CTG TCA TTA TTT 5560 He Thr Thr Pro Leu Pro Hiβ Lye He Lye Met Phe Leu Ser Leu Phe 442 1690 1695 1700 1705 GGA GGC GCA ATT GCG TCC AAG CTT ACA GAC GCT AGA GGC GCA CTG GCG 5608 Gly Gly Ala He Ala Ser Lye Leu Thr Asp Ala Arg Gly Ala Leu Ala 1710 1715 1720 TTC ATG ATG GCC GGG GCT GCG GGA ACA GCT CTT GGT ACA TGG ACA TCG 5656 Phe Met Met Ala Gly Ala Ala Gly Thr Ala Leu Gly Thr Trp Thr Ser 1725 1730 1735 GTG GGT TTT GTC TTT GAC ATG CTA GGC GGC TAT GCT GCC GCC TCA TCC 5704 Val Gly Phe Val Phe Aep Met Leu Gly Gly Tyr Ala Ala Ala Ser Ser 1740 1745 1750 ACT GCT TGC TTG ACA TTT AAA TGC TTG ATG GGT GAG TGG CCC ACT ATG 5752 Thr Ala Cye Leu Thr Phe Lye Cyβ Leu Met Gly Glu Trp Pro Thr Met 1755 1760 1765 GAT CAG CTT GCT GGT TTA GTC TAC TCC GCG TTC AAT CCG GCC GCA GGA 5800 Aep Gin Leu Ala Gly Leu Val Tyr Ser Ala Phe Asn Pro Ala Ala Gly 1770 1775 1780 1785 GTT GTG GGC GTC TTG TCA GCT TGT GCA ATG TTT GCT TTG ACA ACA GCA 5848 Val Val Gly Val Leu Ser Ala Cys Ala Met Phe Ala Leu Thr Thr Ala 1790 1795 1800 GGG CCA GAT CAC TGG CCC AAC AGA CTT CTT ACT ATG CTT GCT AGG AGC 5896 Gly Pro Asp His Trp Pro Aβn Arg Leu Leu Thr Met Leu Ala Arg Ser 1805 1810 1815 AAC ACT GTA TGT AAT GAG TAC TTT ATT GCC ACT CGT GAC ATC CGC AGG 5944 Aβn Thr Val Cyβ Aen Glu Tyr Phe He Ala Thr Arg Asp He Arg Arg 1820 1825 1830 AAG ATA CTG GGC ATT CTG GAG GCA TCT ACC CCC TGG AGT GTC ATA TCA 5992 Lys He Leu Gly He Leu Glu Ala Ser Thr Pro Trp Ser Val He Ser 1835 1840 1845 GCT TGC ATC CGT TGG CTC CAC ACC CCG ACG GAG GAT GAT TGC GGC CTC 6040 Ala Cys " He Arg Trp Leu Hiβ Thr Pro Thr Glu Aep Aep Cyβ Gly Leu 1850 1855 1860 1865 ATT GCT TGG GGT CTA GAG ATT TGG CAG TAT GTG TGC AAT TTC TTT GTG 6088 He Ala Trp Gly Leu Glu He Trp Gin Tyr Val Cye Aβn Phe Phe Val 1870 1875 1880 ATT TGC TTT AAT GTC CTT AAA GCT GGA GTT CAG AGC ATG GTT AAC ATT 6136 He Cyε Phe Aen Val Leu Lye Ala Gly Val Gin Ser Met Val Aβn He 1885 1890 1895 CCT GGT TGT CCT TTC TAC AGC TGC CAG AAG GGG TAC AAG GGC CCC TGG 6184 Pro Gly Cye Pro Phe Tyr Ser Cye Gin Lye Gly Tyr Lys Gly Pro Trp 1900 1905 1910 ATT GGA TCA GGT ATG CTC CAA GCA CGC TGT CCA TGC GGT GCT GAA CTC 6232 He Gly Ser Gly Met Leu Gin Ala Arg Cyβ Pro Cyβ Gly Ala Glu Leu 1915 1920 1925 443 ATC TTT TCT GTT GAG AAT GGT TTT GCA AAA CTT TAC AAA GGA CCC AGA 6280 He Phe Ser Val Glu Aβn Gly Phe Ala Lye Leu Tyr Lye Gly Pro Arg 1930 1935 1940 1945 ACT TGT TCA AAT TAC TGG AGA GGG GCT GTT CCA GTC AAC GCT AGG CTG 6328 Thr Cye Ser Aen Tyr Trp Arg Gly Ala Val Pro Val Aβn Ala Arg Leu 1950 1955 1960 TGT GGG TCG GCT AGA CCG GAC CCA ACT GAT TGG ACT AGT CTT GTC GTC 6376 Cye Gly Ser Ala Arg Pro Aep Pro Thr Aep Trp Thr Ser Leu Val Val 1965 1970 1975 AAT TAT GGC GTT AGG GAC TAC TGT AAA TAT GAG AAA TTG GGA GAT CAC 6424 Aβn Tyr Gly Val Arg Asp Tyr Cys Lys Tyr Glu Lys Leu Gly Aep Hiβ 1980 1985 1990 ATT TTT GTT ACA GCA GTA TCC TCT CCA AAT GTC TGT TTC ACC CAG GTG 6472 He Phe Val Thr Ala Val Ser Ser Pro Aβn Val Cyβ Phe Thr Gin Val 1995 2000 2005 CCC CCA ACC TTG AGA GCT GCA GTG GCC GTG GAC GGC GTA CAG GTT CAG 6520 Pro Pro Thr Leu Arg Ala Ala Val Ala Val Asp Gly Val Gin Val Gin 2010 2015 2020 2025 TGT TAT CTA GGT GAG CCC AAA ACT CCT TGG ACG ACA TCT GCT TGC TGT 6568 Cys Tyr Leu Gly Glu Pro Lys Thr Pro Trp Thr Thr Ser Ala Cys Cys 2030 2035 2040 TAC GGT CCG GAC GGT AAG GGT AAA ACT GTT AAG CTT CCC TTC CGC GTT 6616 Tyr Gly Pro Aep Gly Lye Gly Lye Thr Val Lye Leu Pro Phe Arg Val 2045 2050 2055 GAC GGT CAC ACA CCT GGT GTG CGC ATG CAA CTT AAT TTG CGT GAT GCA 6664 Aep Gly His Thr Pro Gly Val Arg Met Gin Leu Asn Leu Arg Asp Ala 2060 2065 2070 CTT GAG ACA AAT GAC TGT AAT TCC ATA AAC AAC ACT CCT AGT GAT GAA 6712 Leu Glu Thr Asn Asp Cys Asn Ser He Asn Asn Thr Pro Ser Aep Glu 2075 2080 2085 GCC GCA GTG TCC GCT CTT GTT TTC AAA CAG GAG TTG CGG CGT ACA AAC 6760 Ala Ala Val Ser Ala Leu Val Phe Lys Gin Glu Leu Arg Arg Thr Asn 2090 2095 2100 2105 CAA TTG CTT GAG GCA ATT TCA GCT GGC GTT GAC ACC ACC AAA CTG CCA 6808 Gin Leu Leu Glu Ala He Ser Ala Gly Val Asp Thr Thr Lys Leu Pro 2110 2115 2120 GCC CCC TCC ATC GAA GAG GTA GTG GTA AGA AAG CGC CAG TTC CGG GCA 6856 Ala Pro Ser He Glu Glu Val Val Val Arg Lys Arg Gin Phe Arg Ala 2125 2130 2135 AGA ACT GGT TCG CTT ACC TTG CCT CCC CCT CCG AGA TCC GTC CCA GGA 6904 Arg Thr Gly Ser Leu Thr Leu Pro Pro Pro Pro Arg Ser Val Pro Gly 2140 2145 2150 GTG TCA TGT CCT GAA AGC CTG CAA CGA AGT GAC CCG TTA GAA GGT CCT 6952 444 Val Ser Cys Pro Glu Ser Leu Gin Arg Ser Asp Pro Leu Glu Gly Pro 2155 2160 2165 TCA AAC CTC CCT TCT TCA CCA CCT GTT CTA CAG TTG GCC ATG CCG ATG 7000 Ser Asn Leu Pro Ser Ser Pro Pro Val Leu Gin Leu Ala Met Pro Met 2170 2175 2180 2185 CCC CTG TTG GGA GCA GGT GAG TGT AAC CCT TTC ACT GCA ATT GGA TGT 7048 Pro Leu Leu Gly Ala Gly Glu Cyβ Aen Pro Phe Thr Ala He Gly Cyβ 2190 2195 2200 GCA ATG ACC GAA ACA GGC GGA GGC CCT GAT GAT TTA CCC AGT TAC CCT 7096 Ala Met Thr Glu Thr Gly Gly Gly Pro Aep Aep Leu Pro Ser Tyr Pro 2205 2210 2215 CCC AAA AAG GAG GTC TCT GAA TGG TCA GAC GGA AGT TGG TCA ACG ACT 7144 Pro Lye Lye Glu Val Ser Glu Trp Ser Aep Gly Ser Trp Ser Thr Thr 2220 2225 2230 ACA ACC GCT TCC AGC TAC GTT ACT GGC CCC CCG TAC CCT AAG ATA CGG 7192 Thr Thr Ala Ser Ser Tyr Val Thr Gly Pro Pro Tyr Pro Lye He Arg 2235 2240 2245 GGA AAG GAT TCC ACT CAG TCA GCC CCC GCC AAA CGG CCT ACA AAA AAG 7240 Gly Lye Aep Ser Thr Gin Ser Ala Pro Ala Lye Arg Pro Thr Lys Lye 2250 2255 2260 2265 AAG TTG GGA AAG AGT GAG TTT TCG TGC AGC ATG AGC TAC ACT TGG ACC 7288 Lys Leu Gly Lys Ser Glu Phe Ser Cys Ser Met Ser Tyr Thr Trp Thr 2270 2275 2280 GAC GTG ATT AGC TTC AAA ACT GCT TCT AAA GTT CTG TCT GCA ACT CGG 7336 Asp Val He Ser Phe Lye Thr Ala Ser Lye Val Leu Ser Ala Thr Arg 2285 2290 2295 GCC ATC ACT AGT GGT TTC CTC AAA CAA AGA TCA TTG GTG TAT GTG ACT 7384 Ala He Thr Ser Gly Phe Leu Lye Gin Arg Ser Leu Val Tyr Val Thr 2300 2305 2310 GAG CCG CGG GAT GCG GAG CTT AGA AAA CAA AAA GTC ACT ATT AAT AGA 7432 Glu Pro Arg Aep Ala Glu Leu Arg Lye Gin Lye Val Thr He Asn Arg 2315 2320 2325 CAA CCT CTG TTC CCC CCA TCA TAC CAC AAG CAA GTG AGA TTG GCT AAG 7480 Gin Pro Leu Phe Pro Pro Ser Tyr His Lys Gin Val Arg Leu Ala Lys 2330 2335 2340 2345 GAA AAA GCT TCA AAA GTT GTC GGT GTC ATG TGG GAC TAT GAT GAA GTA 7528 Glu Lys Ala Ser Lys Val Val Gly Val Met Trp Asp Tyr Asp Glu Val 2350 2355 2360 GCA GCT CAC ACG CCC TCT AAG TCT GCT AAG TCC CAC ATC ACT GGC CTT 7576 Ala Ala His Thr Pro Ser Lys Ser Ala Lys Ser Hiβ He Thr Gly Leu 2365 2370 2375 CGG GGC ACT GAT GTT CGT TCT GGA GCA GCC CGC AAG GCT GTT CTG GAC - 7624 Arg Gly Thr Aep Val Arg Ser Gly Ala Ala Arg Lye Ala Val Leu Aep 445 2380 2385 2390 TTG CAG AAG TGT GTC GAG GCA GGT GAG ATA CCG AGT CAT TAT CGG CAA 7672 Leu Gin Lys Cyβ Val Glu Ala Gly Glu He Pro Ser Hie Tyr Arg Gin 2395 2400 2405 ACT GTG ATA GTT CCA AAG GAG GAG GTC TTC GTG AAG ACC CCC CAG AAA 7720 Thr Val He Val Pro Lye Glu Glu Val Phe Val Lye Thr Pro Gin Lye 2410 2415 2420 2425 CCA ACA AAG AAA CCC CCA AGG CTT ATC TCG TAC CCC CAC CTT GAA ATG 7768 Pro Thr Lye Lye Pro Pro Arg Leu He Ser Tyr Pro Hiβ Leu Glu Met 2430 2435 2440 AGA TGT GTT GAG AAG ATG TAC TAC GGT CAG GTT GCT CCT GAC GTA GTT 7816 Arg Cye Val Glu Lys Met Tyr Tyr Gly Gin Val Ala Pro Aep Val Val 2445 2450 2455 AAA GCT GTC ATG GGA GAT GCG TAC GGG TTT GTC GAC CCA CGT ACC CGT 7864 Lye Ala Val Met Gly Asp Ala Tyr Gly Phe Val Asp Pro Arg Thr Arg 2460 2465 2470 GTC AAG CGT CTG TTG TCG ATG TGG TCA CCC GAT GCA GTC GGA GCC ACA 7912 Val Lys Arg Leu Leu Ser Met Trp Ser Pro Asp Ala Val Gly Ala Thr 2475 2480 2485 TGC GAT ACA GTG TGT TTT GAC AGT ACC ATC ACA CCC GAG GAT ATC ATG 7960 Cys Asp Thr Val Cys Phe Asp Ser Thr He Thr Pro Glu Aep He Met 2490 2495 2500 2505 GTG GAG ACA GAC ATC TAC TCA GCA GCT AAA CTC AGT GAC CAA CAC CGA 8008 Val Glu Thr Aep He Tyr Ser Ala Ala Lye Leu Ser Asp Gin His Arg 2510 2515 2520 GCT GGC ATT CAC ACC ATT GCG AGG CAG TTA TAC GCT GGA GGA CCG ATG 8056 Ala Gly He His Thr He Ala Arg Gin Leu Tyr Ala Gly Gly Pro Met 2525 2530 2535 ATC GCT TAT GAT GGC CGA GAG ATC GGA TAT CGT AGG TGT AGG TCT TCC 8104 He Ala Tyr Asp Gly Arg Glu He Gly Tyr Arg Arg Cyβ Arg Ser Ser 2540 2545 2550 GGC GTC TAT ACT ACC TCA AGT TCC AAC AGT TTG ACC TGC TGG CTG AAG 8152 Gly Val Tyr Thr Thr Ser Ser Ser Aen Ser Leu Thr Cye Trp Leu Lys 2555 2560 2565 GTA AAT GCT GCA GCC GAA CAG GCT GGC ATG AAG AAC CCT CGC TTC CTT 8200 Val Asn Ala Ala Ala Glu Gin Ala Gly Met Lye Asn Pro Arg Phe Leu 2570 2575 2580 2585 ATT TGC GGC GAT GAT TGC ACC GTA ATT TGG AAG AGC GCC GGA GCA GAT 8248 He Cys Gly Asp Asp Cys Thr Val He Trp Lys Ser Ala Gly Ala Asp 2590 2595 2600 GCA GAC AAA CAA GCA ATG CGT GTC TTT GCT AGC TGG ATG AAG GTG ATG 8296 Ala Asp Lys Gin Ala Met Arg Val Phe Ala Ser Trp Met Lys Val Met 2605 2610 2615 446 GGT GCA CCA CAA GAT TGT GTG CCT CAA CCC AAA TAC AGT TTG GAA GAA 8344 Gly Ala Pro Gin Asp Cys Val Pro Gin Pro Lys Tyr Ser Leu Glu Glu 2620 2625 2630 TTA ACA TCA TGC TCA TCA AAT GTT ACC TCT GGA ATT ACC AAA AGT GGC 8392 Leu Thr Ser Cys Ser Ser Asn Val Thr Ser Gly He Thr Lys Ser Gly 2635 2640 2645 AAG CCT TAC TAC TTT CTT ACA AGA GAT CCT CGT ATC CCC CTT GGC AGG 8440 Lys Pro Tyr Tyr Phe Leu Thr Arg Asp Pro Arg He Pro Leu Gly Arg 2650 2655 2660 2665 TGC TCT GCC GAG GGT CTG GGA TAC AAC CCC AGT GCT GCG TGG ATT GGG 8488 Cys Ser Ala Glu Gly Leu Gly Tyr Asn Pro Ser Ala Ala Trp He Gly 2670 2675 2680 TAT CTA ATA CAT CAC TAC CCA TGT TTG TGG GTT AGC CGT GTG TTG GCT 8536 Tyr Leu He Hiβ Hiβ Tyr Pro Cys Leu Trp Val Ser Arg Val Leu Ala 2685 2690 2695 GTC CAT TTC ATG GAG CAG ATG CTC TTT GAG GAC AAA CTT CCC GAG ACT 8584 Val His Phe Met Glu Gin Met Leu Phe Glu Asp Lys Leu Pro Glu Thr 2700 2705 2710 GTG ACC TTT GAC TGG TAT GGG AAA AAT TAT ACG GTG CCT GTA GAA GAT 8632 Val Thr Phe Asp Trp Tyr Gly Lys Asn Tyr Thr Val Pro Val Glu Aep 2715 2720 2725 CTG CCC AGC ATC ATT GCT GGT GTG CAC GGT ATT GAG GCT TTC TCG GTG 8680 Leu Pro Ser He He Ala Gly Val Hie Gly He Glu Ala Phe Ser Val 2730 2735 2740 2745 GTG CGC TAC ACC AAC GCT GAG ATC CTC AGA GTT TCC CAA TCA CTA ACA 8728 Val Arg Tyr Thr Aen Ala Glu He Leu Arg Val Ser Gin Ser Leu Thr 2750 2755 2760 GAC ATG ACC ATG CCC CCC CTG CGA GCC TGG CGA AAG AAA GCC AGG GCG 8776 Aep Met Thr Met Pro Pro Leu Arg Ala Trp Arg Lys Lys Ala Arg Ala 2765 2770 2775 GTC CTC GCC AGC GCC AAG AGG CGT GGC GGA GCA CAC GCA AAA TTG GCT 8824 Val Leu Ala Ser Ala Lys Arg Arg Gly Gly Ala His Ala Lys Leu Ala 2780 2785 2790 CGC TTC CTT CTC TGG CAT GCT ACA TCT AGA CCT CTA CCA GAT TTG GAT 8872 Arg Phe Leu Leu Trp Hie Ala Thr Ser Arg Pro Leu Pro Aep Leu Aep 2795 2800 2805 AAG ACG AGC GTG GCT CGG TAC ACC ACT TTC AAT TAT TGT GAT GTT TAC 8920 Lye Thr Ser Val Ala Arg Tyr Thr Thr Phe Aβn Tyr Cyβ Aep Val Tyr 2810 2815 2820 2825 TCC CCG GAG GGG GAT GTG TTT GTT ACA CCA CAG AGA AGA TTG CAG AAG 8968 Ser Pro Glu Gly Aep Val Phe Val Thr Pro Gin Arg Arg Leu Gin Lye 2830 2835 2840 TTT CTT GTG AAG TAT TTG GCT GTC ATT GTT TTT GCC CTA GGG CTC ATT 9016 447 Phe Leu Val Lys Tyr Leu Ala Val He Val Phe Ala Leu Gly Leu He 2845 2850 2855 GCT GTT GGA CTA GCC ATC AGC TGAACCCCCA AATTCAAAAT TAATTAACAG 9067 Ala Val Gly Leu Ala He Ser 2860 TTTTTTTTTT TTTTTTTTTT TTTTTTTAGG GCAGCGGCAA CAGGGGAGAC CCCGGGCTTA 9127 ACGACCCCGC GATGTG 9143 (2) INFORMATION FOR SEQ ID NO:397: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2864 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:397: Met Pro Val He Ser Thr Gin Thr Ser Pro Val Pro Ala Pro Arg Thr 1 5 10 15 Arg Lye Aen Lye Gin Thr Gin Ala Ser Tyr Pro Val Ser He Lye Thr 20 25 30 Ser Val Glu Arg Gly Gin Arg Ala Lye Arg Lys Val Gin Arg Asp Ala 35 40 45 Arg Pro Arg Asn Tyr Lys He Ala Gly He His Asp Gly Leu Gin Thr 50 55 60 Leu Ala Gin Ala Ala Leu Pro Ala Hiβ Gly Trp Gly Arg Gin Asp Pro 65 70 75 80 Arg His Lye Ser Arg Aen Leu Gly He Leu Leu Aep Tyr Pro Leu Gly 85 90 95 Trp He Gly Aep Val Thr Thr Hie Thr Pro Leu Val Gly Pro Leu Val 100 105 110 Ala Gly Ala Val Val Arg Pro Val Cyβ Gin He Val Arg Leu Leu Glu 115 120 125 Aep Gly Val Aβn Trp Ala Thr Gly Trp Phe Gly Val Hiβ Leu Phe Val 130 135 140 Val Cyβ Leu Leu Ser Leu Ala Cye Pro Cye Ser Gly Ala Arg Val Thr 145 150 155 160 Aep Pro Aep Thr Aβn Thr Thr He Leu Thr Aβn Cys Cyβ Gin Arg Aβn 165 170 175 Gin Val He Tyr Cyβ Ser Pro Ser Thr Cye Leu His Glu Pro Gly Cyβ 448 180 185 190 Val He Cys Ala Asp Glu Cyβ Trp Val Pro Ala Asn Pro Tyr He Ser 195 200 205 His Pro Ser Asn Trp Thr Gly Thr Asp Ser Phe Leu Ala Asp His He 210 215 220 Asp Phe Val Met Gly Ala Leu Val Thr Cys Asp Ala Leu Asp He Gly 225 230 235 240 Glu Leu Cyβ Gly Ala Cye Val Leu Val Gly Aep Trp Leu Val Arg His 245 250 255 Trp Leu He His He Asp Leu Aβn Glu Thr Gly Thr Cyβ Tyr Leu Glu 260 265 270 Val Pro Thr Gly He Aep Pro Gly Phe Leu Gly Phe He Gly Trp Met 275 280 285 Ala Gly Lye Val Glu Ala Val He Phe Leu Thr Lye Leu Ala Ser Gin 290 295 300 Val Pro Tyr Ala He Ala Thr Met Phe Ser Ser Val Hie Tyr Leu Ala 305 310 315 320 Val Gly Ala Leu He Tyr Tyr Ala Ser Arg Gly Lys Trp Tyr Gin Leu 325 330 335 Leu Leu Ala Leu Met Leu Tyr He Glu Ala Thr Ser Gly Asn Pro He 340 345 350 Arg Val Pro Thr Gly Cys Ser He Ala Glu Phe Cys Ser Pro Leu Met 355 360 365 He Pro Cys Pro Cys His Ser Tyr Leu Ser Glu Asn Val Ser Glu Val 370 375 380 He Cys Tyr Ser Pro Lys Trp Thr Arg Pro Val Thr Leu Glu Tyr Asn 385 390 395 400 Asn Ser He Ser Trp Tyr Pro Tyr Thr He Pro Gly Ala Arg Gly Cyβ 405 410 415 Met Val Lys Phe Lys Asn Aen Thr Trp Gly Cyβ Cye Arg He Arg Aen 420 425 430 Val Pro Ser Tyr Cyβ Thr Met Gly Thr Aep Ala Val Trp Aβn Aep Thr 435 440 445 Arg Aen Thr Tyr Glu Ala Cyβ Gly Val Thr Pro Trp Leu Thr Thr Ala 450 455 460 Trp Hiβ Aβn Gly Ser Ala Leu Lye Leu Ala He Leu Gin Tyr Pro Gly 465 470 475 480 Ser Lye Glu Met Phe Lye Pro Hiβ Aen Trp Met Ser Gly Hiβ Leu Tyr 449 485 490 495 Phe Glu Gly Ser Asp Thr Pro He Val Tyr Phe Tyr Aep Pro Val Asn 500 505 510 Ser Thr Leu Leu Pro Pro Glu Arg Trp Ala Arg Leu Pro Gly Thr Pro 515 520 525 Pro Val Val Arg Gly Ser Trp Leu Gin Val Pro Gin Gly Phe Tyr Ser 530 535 540 Aep Val Lye Aep Leu Ala Thr Gly Leu He Thr Lys Asp Lys Ala Trp 545 550 555 560 Lys Asn Tyr Gin Val Leu Tyr Ser Ala Thr Gly Ala Leu Ser Leu Thr 565 570 575 Gly Val Thr Thr Lys Ala Val Val Leu He Leu Leu Gly Leu Cys Gly 580 585 590 Ser Lye Tyr Leu He Leu Ala Tyr Leu Cyβ Tyr Leu Ser Leu Cye Phe 595 600 605 Gly Arg Ala Ser Gly Tyr Pro Leu Arg Pro Val Leu Pro Ser Gin Ser 610 615 620 Tyr Leu Gin Ala Gly Trp Aep Val Leu Ser Lye Ala Gin Val Ala Pro 625 630 635 640 Phe Ala Leu He Phe Phe He Cyβ Cyβ Tyr Leu Arg Cyβ Arg Leu Arg 645 650 655 Tyr Ala Ala Leu Leu Gly Phe Val Pro Met Ala Ala Gly Leu Pro Leu 660 665 670 Thr Phe Phe Val Ala Ala Ala Ala Ala Gin Pro Asp Tyr Asp Trp Trp 675 680 685 Val Arg Leu Leu Val Ala Gly Leu Val Leu Trp Ala Gly Arg Asp Arg 690 695 700 Gly Pro Arg He Ala Leu Leu Val Gly Pro Trp Pro Leu Val Ala Leu 705 710 715 720 Leu Thr Leu Leu His Leu Ala Thr Pro Ala Ser Ala Phe Aep Thr Glu 725 730 735 He He Gly Gly Leu Thr He Pro Pro Val Val Ala Leu Val Val Met 740 745 750 Ser Arg Phe Gly Phe Phe Ala His Leu Leu Pro Arg Cyβ Ala Leu Val 755 760 765 Aen Ser Tyr Leu Trp Gin Arg Trp Glu Aen Trp Phe Trp Aen Val Thr 770 775 780 Leu Arg Pro Glu Arg Phe Leu Leu Val Leu Val Cyβ Phe Pro Gly Ala 450 785 790 795 800 Thr Tyr Asp Thr Leu Val Thr Phe Cys Val Cys Hiβ Val Ala Leu Leu 805 810 815 Cyβ Leu Thr Ser Ser Ala Ala Ser Phe Phe Gly Thr Aep Ser Arg Val 820 825 830 Arg Ala Hiβ Arg Met Leu Val Arg Leu Gly Lye Cys His Ala Trp Tyr 835 840 845 Ser His Tyr Val Leu Lye Phe Phe Leu Leu Val Phe Gly Glu Aen Gly 850 855 860 Val Phe Phe Tyr Lye Hiβ Leu His Gly Aep Val Leu Pro Aen Asp Phe 865 870 875 880 Ala Ser Lys Leu Pro Leu Gin Glu Pro Phe Phe Pro Phe Glu Gly Lys 885 890 895 Ala Arg Val Tyr Arg Asn Glu Gly Arg Arg Leu Ala Cys Gly Asp Thr 900 905 910 Val Asp Gly Leu Pro Val Val Ala Arg Leu Gly Asp Leu Val Phe Ala 915 920 925 Gly Leu Ala Met Pro Pro Asp Gly Trp Ala He Thr Ala Pro Phe Thr 930 935 940 Leu Gin Cys Leu Ser Glu Arg Gly Thr Leu Ser Ala Met Ala Val Val 945 950 955 960 Met Thr Gly He Asp Pro Arg Thr Trp Thr Gly Thr He Phe Arg Leu 965 970 975 Gly Ser Leu Ala Thr Ser Tyr Met Gly Phe Val Cys Asp Asn Val Leu 980 985 990 Tyr Thr Ala His His Gly Ser Lys Gly Arg Arg Leu Ala His Pro Thr 995 1000 1005 Gly Ser He Hie Pro He Thr Val Aep Ala Ala Aβn Aep Gin Aep He 1010 1015 1020 Tyr Gin Pro Pro Cye Giy Ala Gly Ser Leu Thr Arg Cyβ Ser Cye Gly 1025 1030 1035 1040 Glu Thr Lye Gly Tyr Leu Val Thr Arg Leu Gly Ser Leu Val Glu Val 1045 1050 1055 Asn Lye Ser Aep Aep Pro Tyr Trp Cyβ Val Cyβ Gly Ala Leu Pro Met 1060 1065 1070 Ala Val Ala Lye Gly Ser Ser Gly Ala Pro He Leu Cye Ser Ser Gly 1075 1080 1085 Hiβ Val He Gly Met Phe Thr Ala Ala Arg Aβn Ser Gly Gly Ser Val 451 1090 1095 1100 Ser Gin He Arg Val Arg Pro Leu Val Cyβ Ala Gly Tyr Hie Pro Gin 1105 1110 1115 1120 Tyr Thr Ala Hiβ Ala Thr Leu Aep Thr Lye Pro Thr Val Pro Asn Glu 1125 1130 1135 Tyr Ser Val Gin He Leu He Ala Pro Thr Gly Ser Gly Lys Ser Thr 1140 1145 1150 Lys Leu Pro Leu Ser Tyr Met Gin Glu Lye Tyr Glu Val Leu Val Leu 1155 1160 1165 Aβn Pro Ser Val Ala Thr Thr Ala Ser Met Pro Lye Tyr Met His Ala 1170 1175 1180 Thr Tyr Gly Val Asn Pro Asn Cys Tyr Phe Asn Gly Lys Cys Thr Asn 1185 1190 1195 1200 Thr Gly Ala Ser Leu Thr Tyr Ser Thr Tyr Gly Met Tyr Leu Thr Gly 1205 1210 1215 Ala Cys Ser Arg Asn Tyr Asp Val He He Cye Aep Glu Cye His Ala 1220 1225 1230 Thr Asp Ala Thr Thr Val Leu Gly He Gly Lys Val Leu Thr Glu Ala 1235 1240 1245 Pro Ser Lye Asn Val Arg Leu Val Val Leu Ala Thr Ala Thr Pro Pro 1250 1255 1260 Gly Val He Pro Thr Pro His Ala Asn He Thr Glu He Gin Leu Thr 1265 1270 1275 1280 Asp Glu Gly Thr He Pro Phe His Gly Lys Lys He Lys Glu Glu Asn 1285 1290 1295 Leu Lys Lys Gly Arg His Leu He Phe Glu Ala Thr Lye Lye Hie Cys 1300 1305 1310 Asp Glu Leu Ala Aβn Glu Leu Ala Arg Lys Gly He Thr Ala Val Ser 1315 1320 1325 Tyr Tyr Arg Gly Cys Aep He Ser Lye He Pro Glu Gly Aep Cyβ Val 1330 1335 1340 Val Val Ala Thr Aep Ala Leu Cyβ Thr Gly Tyr Thr Gly Asp Phe Asp 1345 1350 1355 1360 Ser Val Tyr Asp Cys Ser Leu Met Val Glu Gly Thr Cys His Val Asp 1365 1370 1375 Leu Asp Pro Thr Phe Thr Met Gly Val Arg Val Cys Gly Val Ser Ala 1380 1385 1390 He Val Lye Gly Gin Arg Arg Gly Arg Thr Gly Arg Gly Arg Ala Gly 452 1395 1400 1405 He Tyr Tyr Tyr Val Asp Gly Ser Cys Thr Pro Ser Gly Met Val Pro 1410 1415 1420 Glu Cys Aβn He Val Glu Ala Phe Asp Ala Ala Lye Ala Trp Tyr Gly 1425 1430 1435 1440 Leu Ser Ser Thr Glu Ala Gin Thr He Leu Asp Thr Tyr Arg Thr Gin 1445 1450 1455 Pro Gly Leu Pro Ala He Gly Ala Aen Leu Asp Glu Trp Ala Asp Leu 1460 1465 1470 Phe Ser Met Val Asn Pro Glu Pro Ser Phe Val Asn Thr Ala Lys Arg 1475 1480 1485 Thr Ala Asp Asn Tyr Val Leu Leu Thr Ala Ala Gin Leu Gin Leu Cys 1490 1495 1500 His Gin Tyr Gly Tyr Ala Ala Pro Asn Aep Ala Pro Arg Trp Gin Gly 1505 1510 1515 1520 Ala Arg Leu Gly Lye Lye Pro Cys Gly Val Leu Trp Arg Leu Aep Gly 1525 1530 1535 Ala Asp Ala Cye Pro Gly Pro Glu Pro Ser Glu Val Thr Arg Tyr Gin 1540 1545 1550 Met Cys Phe Thr Glu Val Asn Thr Ser Gly Thr Ala Ala Leu Ala Val 1555 1560 1565 Gly Val Gly Val Ala Met Ala Tyr Leu Ala He Asp Thr Phe Gly Ala 1570 1575 1580 Thr Cys Val Arg Arg Cys Trp Ser He Thr Ser Val Pro Thr Gly Ala 1585 1590 1595 1600 Thr Val Ala Pro Val Val Asp Glu Glu Glu He Val Glu Glu Cyβ Ala 1605 1610 1615 Ser Phe He Pro Leu Glu Ala Met Val Ala Ala He Aep Lye Leu Lye 1620 1625 1630 Ser Thr He Thr Thr Thr Ser Pro Phe Thr Leu Glu Thr Ala Leu Glu 1635 1640 1645 Lye Leu Aen Thr Phe Leu Gly Pro Hiβ Ala Ala Thr He Leu Ala He 1650 1655 1660 He Glu Tyr Cye Cyβ Gly Leu Val Thr Leu Pro Aep Aen Pro Phe Ala 1665 1670 1675 1680 Ser Cye Val Phe Ala Phe He Ala Gly He Thr Thr Pro Leu Pro Hie 1685 1690 1695 Lye He Lye Met Phe Leu Ser Leu Phe Gly Gly Ala He Ala Ser Lye 453 1700 1705 1710 Leu Thr Asp Ala Arg Gly Ala Leu Ala Phe Met Met Ala Gly Ala Ala 1715 1720 1725 Gly Thr Ala Leu Gly Thr Trp Thr Ser Val Gly Phe Val Phe Asp Met 1730 1735 1740 Leu Gly Gly Tyr Ala Ala Ala Ser Ser Thr Ala Cys Leu Thr Phe Lye 1745 1750 1755 1760 Cyβ Leu Met Gly Glu Trp Pro Thr Met Aep Gin Leu Ala Gly Leu Val 1765 1770 1775 Tyr Ser Ala Phe Aβn Pro Ala Ala Gly Val.Val Gly Val Leu Ser Ala 1780 1785 1790 Cyβ Ala Met Phe Ala Leu Thr Thr Ala Gly Pro Aep His Trp Pro Asn 1795 1800 1805 Arg Leu Leu Thr Met Leu Ala Arg Ser Asn Thr Val Cys Asn Glu Tyr 1810 1815 1820 Phe He Ala Thr Arg Asp He Arg Arg Lye He Leu Gly He Leu Glu 1825 1830 1835 1840 Ala Ser Thr Pro Trp Ser Val He Ser Ala Cyβ He Arg Trp Leu Hie 1845 1850 1855 Thr Pro Thr Glu Aep Asp Cys Gly Leu He Ala Trp Gly Leu Glu He 1860 1865 1870 Trp Gin Tyr Val Cys Aβn Phe Phe Val He Cys Phe Asn Val Leu Lys 1875 1880 1885 Ala Gly Val Gin Ser Met Val Asn He Pro Gly Cys Pro Phe Tyr Ser 1890 1895 1900 Cyβ Gin Lys Gly Tyr Lys Gly Pro Trp He Gly Ser Gly Met Leu Gin 1905 " 1910 1915 1920 Ala Arg Cys Pro Cys Gly Ala Glu Leu He Phe Ser Val Glu Asn Gly 1925 1930 1935 Phe Ala Lys Leu Tyr Lye Gly Pro Arg Thr Cyβ Ser Aβn Tyr Trp Arg 1940 1945 1950 Gly Ala Val Pro Val Asn Ala Arg Leu Cye Gly Ser Ala Arg Pro Asp 1955 1960 1965 Pro Thr Asp Trp Thr Ser Leu Val Val Aβn Tyr Gly Val Arg Aep Tyr 1970 1975 1980 Cys Lys Tyr Glu Lys Leu Gly Aep His He Phe Val Thr Ala Val Ser 1985 1990 1995 2000 Ser Pro Aβn Val Cys Phe Thr Gin Val Pro Pro Thr Leu Arg Ala Ala 454 2005 2010 2015 Val Ala Val Asp Gly Val Gin Val Gin Cyβ Tyr Leu Gly Glu Pro Lys 2020 2025 2030 Thr Pro Trp Thr Thr Ser Ala Cyβ Cys Tyr Gly Pro Asp Gly Lys Gly 2035 2040 2045 Lye Thr Val Lye Leu Pro Phe Arg Val Aep Gly Hiβ Thr Pro Gly Val 2050 2055 2060 Arg Met Gin Leu Aen Leu Arg Aep Ala Leu Glu Thr Aen Aep Cyβ Asn 2065 2070 2075 2080 Ser He Aβn Aβn Thr Pro Ser Aep Glu Ala Ala Val Ser Ala Leu Val 2085 2090 2095 Phe Lye Gin Glu Leu Arg Arg Thr Asn Gin Leu Leu Glu Ala He Ser 2100 2105 2110 Ala Gly Val Asp Thr Thr Lye Leu Pro Ala Pro Ser He Glu Glu Val 2115 2120 2125 Val Val Arg Lye Arg Gin Phe Arg Ala Arg Thr Gly Ser Leu Thr Leu 2130 2135 2140 Pro Pro Pro Pro Arg Ser Val Pro Gly Val Ser Cyβ Pro Glu Ser Leu 2145 2150 2155 2160 Gin Arg Ser Aep Pro Leu Glu Gly Pro Ser Aen Leu Pro Ser Ser Pro 2165 2170 2175 Pro Val Leu Gin Leu Ala Met Pro Met Pro Leu Leu Gly Ala Gly Glu 2180 2185 2190 Cyβ Asn Pro Phe Thr Ala He Gly Cye Ala Met Thr Glu Thr Gly Gly 2195 2200 2205 Gly Pro Aep Aep Leu Pro Ser Tyr Pro Pro Lye Lye Glu Val Ser Glu 2210 2215 2220 Trp Ser Aep Gly Ser Trp Ser Thr Thr Thr Thr Ala Ser Ser Tyr Val 2225 2230 2235 2240 Thr Gly Pro Pro Tyr Pro Lye He Arg Gly Lye Aep Ser Thr Gin Ser 2245 2250 2255 Ala Pro Ala Lye Arg Pro Thr Lye Lye Lye Leu Gly Lye Ser Glu Phe 2260 2265 2270 Ser Cyβ Ser Met Ser Tyr Thr Trp Thr Asp Val He Ser Phe Lys Thr 2275 2280 2285 Ala Ser Lys Val Leu Ser Ala Thr Arg Ala He Thr Ser Gly Phe Leu 2290 2295 2300 Lys Gin Arg Ser Leu Val Tyr Val Thr Glu Pro Arg Asp Ala Glu Leu 455 2305 2310 2315 2320 Arg Lys Gin Lye Val Thr He Asn Arg Gin Pro Leu Phe Pro Pro Ser 2325 2330 2335 Tyr His Lye Gin Val Arg Leu Ala Lys Glu Lye Ala Ser Lye Val Val 2340 2345 2350 Gly Val Met Trp Aep Tyr Aep Glu Val Ala Ala Hiβ Thr Pro Ser Lye 2355 2360 2365 Ser Ala Lye Ser Hie He Thr Gly Leu Arg Gly Thr Aep Val Arg Ser 2370 2375 2380 Gly Ala Ala Arg Lys Ala Val Leu Asp Leu Gin Lys Cys Val Glu Ala 2385 2390 2395 2400 Gly Glu He Pro Ser His Tyr Arg Gin Thr Val He Val Pro Lye Glu 2405 2410 2415 Glu Val Phe Val Lye Thr Pro Gin Lye Pro Thr Lye Lys Pro Pro Arg 2420 2425 2430 Leu He Ser Tyr Pro Hiβ Leu Glu Met Arg Cyβ Val Glu Lye Met Tyr 2435 2440 2445 Tyr Gly Gin Val Ala Pro Aep Val Val Lye Ala Val Met Gly Aep Ala 2450 2455 2460 Tyr Gly Phe Val Aep Pro Arg Thr Arg Val Lye Arg Leu Leu Ser Met 2465 2470 2475 2480 Trp Ser Pro Aep Ala Val Gly Ala Thr Cyβ Aep Thr Val Cye Phe Aep 2485 2490 2495 Ser Thr He Thr Pro Glu Aep He Met Val Glu Thr Asp He Tyr Ser 2500 2505 2510 Ala Ala Lys Leu Ser Asp Gin Hiβ Arg Ala Gly He Hiβ Thr He Ala 2515 2520 2525 Arg Gin Leu Tyr Ala Gly Gly Pro Met He Ala Tyr Aep Gly Arg Glu 2530 2535 2540 He Gly Tyr Arg Arg Cyβ Arg Ser Ser Gly Val Tyr Thr Thr Ser Ser 2545 2550 2555 2560 Ser Aen Ser Leu Thr Cye Trp Leu Lye Val Aβn Ala Ala Ala Glu Gin 2565 2570 2575 Ala Gly Met Lye Aβn Pro Arg Phe Leu He Cys Gly Asp Asp Cys Thr 2580 2585 2590 Val He Trp Lye Ser Ala Gly Ala Aep Ala Asp Lys Gin Ala Met Arg 2595 2600 2605 Val Phe Ala Ser Trp Met Lys Val Met Gly Ala Pro Gin Asp Cyβ Val 456 2610 2615 2620 Pro Gin Pro Lys Tyr Ser Leu Glu Glu Leu Thr Ser Cyβ Ser Ser Aβn 2625 2630 2635 2640 Val Thr Ser Gly He Thr Lys Ser Gly Lys Pro Tyr Tyr Phe Leu Thr 2645 2650 2655 Arg Asp Pro Arg He Pro Leu Gly Arg Cys Ser Ala Glu Gly Leu Gly 2660 2665 2670 Tyr Aen Pro Ser Ala Ala Trp He Gly Tyr Leu He Hie Hiβ Tyr Pro 2675 2680 2685 Cye Leu Trp Val Ser Arg Val Leu Ala Val Hiβ Phe Met Glu Gin Met 2690 2695 2700 Leu Phe Glu Aep Lye Leu Pro Glu Thr Val Thr Phe Asp Trp Tyr Gly 2705 2710 2715 2720 Lye Aβn Tyr Thr Val Pro Val Glu Asp Leu Pro Ser He He Ala Gly 2725 2730 2735 Val His Gly He Glu Ala Phe Ser Val Val Arg Tyr Thr Asn Ala Glu 2740 2745 2750 He Leu Arg Val Ser Gin Ser Leu Thr Asp Met Thr Met Pro Pro Leu 2755 2760 2765 Arg Ala Trp Arg Lys Lys Ala Arg Ala Val Leu Ala Ser Ala Lys Arg 2770 2775 2780 Arg Gly Gly Ala His Ala Lys Leu Ala Arg Phe Leu Leu Trp His Ala 2785 2790 2795 2800 Thr Ser Arg Pro Leu Pro Asp Leu Asp Lys Thr Ser Val Ala Arg Tyr 2805 2810 2815 Thr Thr Phe Aen Tyr Cyβ Aep Val Tyr Ser Pro Glu Gly Aep Val Phe 2820 2825 2830 Val Thr Pro Gin Arg Arg Leu Gin Lye Phe Leu Val Lye Tyr Leu Ala 2835 2840 2845 Val He Val Phe Ala Leu Gly Leu He Ala Val Gly Leu Ala He Ser 2850 2855 2860 (2) INFORMATION FOR SEQ ID NO:398: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 200 amino acidβ (B) TYPE: amino acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear 457 (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:398: Lys Phe Leu Ala Aep Gly Gly Cyβ Ser Gly Gly Ala Tyr Asp He He 1 5 10 15 He Cyβ Aep Glu Cys His Ser Thr Asp Ala Thr Ser He Leu Gly He 20 25 30 Gly Thr Val Leu Asp Gin Ala Glu Thr Ala Gly Ala Arg Leu Val Val 35 40 45 Leu Ala Thr Ala Thr Pro Pro Gly Ser Val Thr Val Pro His Pro Asn 50 55 60 He Glu Glu Val Ala Leu Ser Thr Thr Gly Glu He Pro Phe Tyr Gly 65 70 75 80 Lys Ala He Pro Leu Glu Val He Lys Gly Gly Arg His Leu He Phe 85 90 95 Cys His Ser Lys Lye Lye Cys Asp Glu Leu Ala Ala Lye Leu Val Ala 100 105 110 Leu Gly He Asn Ala Val Ala Tyr Tyr Arg Gly Leu Aep Val Ser Val 115 120 125 He Pro Thr Ser Gly Aep Val Val Val Val Ala Thr Aep Ala Leu Met 130 135 140 Thr Gly Tyr Thr Gly Aep Phe Aep Ser Val He Aep Cyβ Aen Thr Cyβ 145 150 155 160 Val Thr Gin Thr Val Aep Phe Ser Leu Aep Pro Thr Phe Thr He Glu 165 170 175 Thr He Thr Leu Pro Gin Asp Ala Val Ser Arg Thr Gin Arg Arg Gly 180 185 190 Arg Thr Gly Arg Gly Lys Pro Gly 195 200 (2) INFORMATION FOR SEQ ID NO:399: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 100 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein 458 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:399; Cys Cys Asp Leu Asp Pro Gin Ala Arg Val Ala He Lys Ser Leu Thr 1 5 10 15 Glu Arg Leu Tyr Val Gly Gly Pro Leu Thr Asn Ser Arg Gly Glu Asn 20 25 30 Cyβ Gly Tyr Arg Arg Cys Arg Ala Ser Gly Val Leu Thr Thr Ser Cyβ 35 40 45 Gly Aβn Thr Leu Thr Cyβ Tyr He Lys Ala Arg Ala Ala Cys Arg Ala 50 55 60 Ala Gly Leu Gin Asp Cys Thr Met Leu Val Cys Gly Aep Aep Leu Val 65 70 75 80 Val He Cys Glu Ser Ala Gly Val Gin Glu Asp Ala Ala Ser Leu Arg 85 90 95 Ala Phe Thr Glu 100 (2) INFORMATION FOR SEQ ID NO:400: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9034 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 1..9034 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:400: AAA GGT GGT GGA TGG GTG ATG ACA GGG TTG GTA GGT CGT AAA TCC CGG 48 Lys Gly Gly Gly Trp Val Met Thr Gly Leu Val Gly Arg Lys Ser Arg 1 5 10 15 TCA TCC TGG TAG CCA CTA TAG GTG GGT CTT AAG GGG AGG CTA CGG TCC 96 Ser Ser Trp * Pro Leu * Val Gly Leu Lys Gly Arg Leu Arg Ser 20 25 30 CTC TTG CGC ATA TGG AGG AAA AGC GCA CGG TCC ACA GGT GTT GGT CCT 144 Leu Leu Arg He Trp Arg Lys Ser Ala Arg Ser Thr Gly Val Gly Pro 35 40 45 ACC GGT GTA ATA AGG ACC CGG CGC TAG GCA CGC CGT TAA ACC GAG CCC 192 459 Thr Gly Val He Arg Thr Arg Arg * Ala Arg Arg * Thr Glu Pro 50 55 60 GTT ACT CCC CTG GGC AAA CGA CGC CCA CGT ACG GTC CAC GTC GCC CTT 240 Val Thr Pro Leu Gly Lys Arg Arg Pro Arg Thr Val His Val Ala Leu 65 70 75 80 CAA TGT CTC TCT TGA CCA ATA GGC GTA CGG CGA GTT GAC AAG GAC CAG 288 Gin Cys Leu Ser * Pro He Gly Val Arg Arg Val Asp Lys Asp Gin 85 90 95 TGG GGG CCG GGC GGG AGG GGG AAG GAC CCC CAC CGC TGC CCT TCC CGG 336 Trp Gly Pro Gly Gly Arg Gly Lys Asp Pro His Arg Cys Pro Ser Arg 100 105 110 GGA GGC GGG AAA TGC ATG GGG CCA CCC AGC TCC GCG GCG GCC TAC AGC 384 Gly Gly Gly Lys Cys Met Gly Pro Pro Ser Ser Ala Ala Ala Tyr Ser 115 120 125 CGG GGT AGC CCA AGA ACT TCG GGT GAG GGC GGG TGG CAT TTC TTT TCC 432 Arg Gly Ser Pro Arg Thr Ser Gly Glu Gly Gly Trp His Phe Phe Ser 130 135 140 TAT ACC GAT CAT GGC AGT CCT TCT GCT CCT ACT CGT GGT GGA GCC GGG 480 Tyr Thr Asp His Gly Ser Pro Ser Ala Pro Thr Arg Gly Gly Ala Gly 145 150 155 160 GCT ATT TTA GCC CCG GCC ACC CAT GCT TGT AGC GCG AAA GGG CAA TAT 528 Ala He Leu Ala Pro Ala Thr His Ala Cys Ser Ala Lys Gly Gin Tyr 165 170 175 TTS CTC ACA AAC TGT TGC GCC CTG GAG GAC ATA GGC TTC TGC CTG GAG 576 Xaa Leu Thr Asn Cys Cys Ala Leu Glu Aep He Gly Phe Cyβ Leu Glu 180 185 190 GGC GGA TGC CTG GTG GCT CTG GGG TGC ACC ATT TGC ACC GAC CGC TGC 624 Gly Gly Cyβ Leu Val Ala Leu Gly Cyβ Thr He Cyβ Thr Aep Arg Cye 195 200 205 TGG CCA CTG TAT" CAG GCG GGT TTG GCC GTG CGG CCC GGC AAG TCC GCC 672 Trp Pro Leu Tyr Gin Ala Gly Leu Ala Val Arg Pro Gly Lys Ser Ala 210 215 220 GCC CAG TTG GTG GGG GAA CTC GGT AGT CTC TAC GGG CCC TTG TCG GTC 720 Ala Gin Leu Val Gly Glu Leu Gly Ser Leu Tyr Gly Pro Leu Ser Val 225 230 235 240 TCG GCT TAT GTG GCC GGG ATC CTG GGG CTT GGG GAG GTC TAC TCG GGG 768 Ser Ala Tyr Val Ala Gly He Leu Gly Leu Gly Glu Val Tyr Ser Gly 245 250 255 GTC CTC ACC GTC GGG GTG GCG TTG ACG CGC AGG GTC TAC CCG GTC CCG 816 Val Leu Thr Val Gly Val Ala Leu Thr Arg Arg Val Tyr Pro Val Pro 260 265 270 AAC CTG ACG TGT GCA GTA GAG TGT- GAG TTG AAG TGG GAA AGT GAG TTT 864 Aen Leu Thr Cys Ala Val Glu Cys Glu Leu Lys Trp Glu Ser Glu Phe 460 275 280 285 TGG AGA TGG ACT GAA CAG CTG GCC TCA AAC TAC TGG ATT CTG GAA TAC 912 Trp Arg Trp Thr Glu Gin Leu Ala Ser Asn Tyr Trp He Leu Glu Tyr 290 295 300 CTC TGG AAG GTG CCT TTC GAC TTT TGG CGG GGA GTG ATG AGC CTT ACT 960 Leu Trp Lys Val Pro Phe Asp Phe Trp Arg Gly Val Met Ser Leu Thr 305 310 315 320 CCT CTC TTG GTG TGC GTG GCG GCC CTC CTC CTG CTG GAG CAG CGT ATT 1008 Pro Leu Leu Val Cys Val Ala Ala Leu Leu Leu Leu Glu Gin Arg He 325 330 335 GTC ATG GTC TTC CTC CTG GTC ACT ATG GCG GGC ATG TCG CAA GGC GCG 1056 Val Met Val Phe Leu Leu Val Thr Met Ala Gly Met Ser Gin Gly Ala 340 345 350 CCC GCC TCA AGT GTT GGG GTC ACG GCC TTT CGA GGC GGG TTT GAC TTG 1104 Pro Ala Ser Ser Val Gly Val Thr Ala Phe Arg Gly Gly Phe Asp Leu 355 360 365 GCA GTC TTG TTC TTG CAG GTC GAA CGG GTC CCG CGT GCC GAC AGG GAG 1152 Ala Val Leu Phe Leu Gin Val Glu Arg Val Pro Arg Ala Asp Arg Glu 370 375 380 AGG GTT TGG GAA CGT GGG AAC GTC ACA CTT TTG TGT GAC TGC CCC AAC 1200 Arg Val Trp Glu Arg Gly Asn Val Thr Leu Leu Cys Asp Cys Pro Asn 385 390 395 400 GGT CCT TGG GTG TGG GTC CCG GCC CTT TGC CAG GCA ATC GGA TGG GGC 1248 Gly Pro Trp Val Trp Val Pro Ala Leu Cys Gin Ala He Gly Trp Gly 405 410 415 GAC CCT ATC ACT CAT TGG AGC CAC GGA CAA AAT CAG TGG CCC CTT TCT 1296 Asp Pro He Thr Hiβ Trp Ser Hie Gly Gin Aen Gin Trp Pro Leu Ser 420 425 430 TGT CCC CAA TTT GTC TAC GGC GCC GTT TCA GTG ACC TGC GTG TGG GGT 1344 Cys Pro Gin Phe Val Tyr Gly Ala Val Ser Val Thr Cys Val Trp Gly 435 440 445 TCT GTG TCT TGG TTT GCT TCC ACT GGG GGT CGC GAC TCC AAG GTT GAT 1392 Ser Val Ser Trp Phe Ala Ser Thr Gly Gly Arg Asp Ser Lys Val Asp 450 455 460 GTG TGG AGT TTG GTT CCA GTT GGC TCT GCC AGC TGC ACC ATA GCC GCA 1440 Val Trp Ser Leu Val Pro Val Gly Ser Ala Ser Cye Thr He Ala Ala 465 470 475 480 CTG GGA TCT TCG GAT CGC GAC ACA GTG GTT GAG CTC TCC GAG TGG GGA 1488 Leu Gly Ser Ser Asp Arg Asp Thr Val Val Glu Leu Ser Glu Trp Gly 485 490 495 ATT CCC TGC GCC ACT TGT ATC CTG GAC AGG CGG CCT GCC TCG TGT GGC 1536 He Pro Cys Ala Thr Cys He Leu Asp Arg Arg Pro Ala Ser Cys Gly 500 505 510 461 ACC TGT GTG AGG GAC TGC TGG CCC GAG ACC GGG TCG GTA CGT TTC CCA 1584 Thr Cys Val Arg Aep Cys Trp Pro Glu Thr Gly Ser Val Arg Phe Pro 515 520 525 TTC CAC AGG TGT GGC GCG GGA CCG AGG CTG ACC AGA GAC CTT GAG GCT 1632 Phe His Arg Cye Gly Ala Gly Pro Arg Leu Thr Arg Aep Leu Glu Ala 530 535 540 GTG CCC TTC GTC AAT AGG ACA ACT CCC TTC ACC ATA AGG GGG CCC CTG 1680 Val Pro Phe Val Aen Arg Thr Thr Pro Phe Thr He Arg Gly Pro Leu 545 550 555 560 GGC AAC CAG GGG CGA GGC AAC CCG GTG CGG TCG CCC TTG GGT TTT GGG 1728 Gly Aen Gin Gly Arg Gly Aβn Pro Val Arg Ser Pro Leu Gly Phe Gly 565 570 575 TCC TAC ACC ATG ACC AAG ATC CGA GAC TCC TTA CAC TTG GTG AAA TGT 1776 Ser Tyr Thr Met Thr Lye He Arg Asp Ser Leu His Leu Val Lys Cys 580 585 590 CCC ACC CCA GCC ATT GAG CCT CCC ACC GGA ACG TTT GGG TTC TTC CCA 1824 Pro Thr Pro Ala He Glu Pro Pro Thr Gly Thr Phe Gly Phe Phe Pro 595 600 605 GGA GTC CCC CCC CTT AAC AAC TGC ATG CTT CTC GGC ACT GAG GTG TCA 1872 Gly Val Pro Pro Leu Asn Asn Cys Met Leu Leu Gly Thr Glu Val Ser 610 615 620 GAG GTA TTG GGT GGG GCG GGC CTC ACT GGG GGG TTT TAC GAA CCT CTG 1920 Glu Val Leu Gly Gly Ala Gly Leu Thr Gly Gly Phe Tyr Glu Pro Leu 625 630 635 640 GTG CGG CGG TGT TCA GAG CTG ATG GGT CGG CGG AAT CCG GTC TGC CCG 1968 Val Arg Arg Cys Ser Glu Leu Met Gly Arg Arg Asn Pro Val Cyβ Pro 645 650 655 GGG TTT GCA TGG CTC TCT TCG GGA CGG CCT GAT GGG TTC ATA CAT GTT 2016 Gly Phe Ala Trp Leu Ser Ser Gly Arg Pro Aep Gly Phe He His Val 660 665 670 CAG GGC CAC TTG CAG GAG GTG GAT GCG GGC AAC TTC ATT CCG CCC CCA 2064 Gin Gly His Leu Gin Glu Val Asp Ala Gly Asn Phe He Pro Pro Pro 675 680 685 CGC TGG TTG CTC TTG GAC TTT GTA TTT GTC CTG TTA TAC CTG ATG AAG 2112 Arg Trp Leu Leu Leu Asp Phe Val Phe Val Leu Leu Tyr Leu Met Lys 690 695 700 CTG GCA GAG GCA CGG TTG GTC CCG CTG ATC CTC CTC CTG CTA TGG TGG 2160 Leu Ala Glu Ala Arg Leu Val Pro Leu He Leu Leu Leu Leu Trp Trp 705 710 715 720 TGG GTG AAC CAG TTG GCG GTC CTT GKT GTG SCG GCT GCK CRC GCC GCC 2208 Trp Val Asn Gin Leu Ala Val Leu Xaa Val Xaa Ala Xaa Xaa Ala Ala 725 730 735 GTG GCT GGA GAG GTG TTT GCG GGC CCT GCC TTG TCC TGG TGT CTG GGC 2256 462 Val Ala Gly Glu Val Phe Ala Gly Pro Ala Leu Ser Trp Cys Leu Gly 740 745 750 CTA CCC TTC GTG AGT ATG ATC CTG GGG CTA GCA AAC CTG GTG TTG TAC 2304 Leu Pro Phe Val Ser Met He Leu Gly Leu Ala Aβn Leu Val Leu Tyr 755 760 765 TTC CGC TGG ATG GGT CCT CAA CGC CTG ATG TTC CTC GTG TTG TGG AAG 2352 Phe Arg Trp Met Gly Pro Gin Arg Leu Met Phe Leu Val Leu Trp Lye 770 775 780 CTC GCT CGG GGG GCT TTC CCG CTG GCA TTA CTG ATG GGG ATT TCC GCC 2400 Leu Ala Arg Gly Ala Phe Pro Leu Ala Leu Leu Met Gly He Ser Ala 785 790 795 800 ACT CGC GGC CGC ACC TCT GTG CTT GGC GCC GAA TTC TGC TTT GAT GTC 2448 Thr Arg Gly Arg Thr Ser Val Leu Gly Ala Glu Phe Cyβ Phe Aep Val 805 810 815 ACC TTT GAA GTG GAC ACG TCA GTC TTG GGT TGG GTG GTT GCT AGT GTG 2496 Thr Phe Glu Val Asp Thr Ser Val Leu Gly Trp Val Val Ala Ser Val 820 825 830 GTG GCT TGG GCC ATA GCG CTC CTG AGC TCT ATG AGC GCG GGG GGG TGG 2544 Val Ala Trp Ala He Ala Leu Leu Ser Ser Met Ser Ala Gly Gly Trp 835 840 845 AAG CAC AAA GCC ATA ATC TAT AGG ACG TGG TGT AAA GGG TAC CAG GCY 2592 Lys His Lys Ala He He Tyr Arg Thr Trp Cyβ Lys Gly Tyr Gin Xaa 850 855 860 CTT CGC CAG CGC GTG GTG CGT AGC CCC CTC GGG GAG GGG CGG CCC ACC 2640 Leu Arg Gin Arg Val Val Arg Ser Pro Leu Gly Glu Gly Arg Pro Thr 865 870 875 880 AAG CCG CTG ACG ATA GCC TGG TGT CTG GCC TCT TAC ATC TGG CCG GAC 2688 Lys Pro Leu Thr He Ala Trp Cys Leu Ala Ser Tyr He Trp Pro Asp 885 890 895 GCT GTG ATG TTG GTG GTT GTG GCC ATG GTC CTC CTC TTC GGC CTT TTC 2736 Ala Val Met Leu Val Val Val Ala Met Val Leu Leu Phe Gly Leu Phe 900 905 910 GAC GCG CTC GAT TGG GCC TTG GAG GAG CTC CTT GTG TCG CGG CCT TCG 2784 Asp Ala Leu Asp Trp Ala Leu Glu Glu Leu Leu Val Ser Arg Pro Ser 915 920 925 TTG CGT CGT TTG GCA AGG GTG GTG GAG TGT TGT GTG ATG GCG GGC GAG 2832 Leu Arg Arg Leu Ala Arg Val Val Glu Cys Cys Val Met Ala Gly Glu 930 935 940 AAG GCC ACT ACC GTC CGG CTT GTG TCC AAG ATG TGC GCG AGA GGG GCC 2880 Lys Ala Thr Thr Val Arg Leu Val Ser Lys Met Cys Ala Arg Gly Ala 945 950 955 960 TAC CTG TTT GAC CAC ATG GGG TCG TTC TCG CGC GCG GTC AAG GAG CGC 292 Tyr Leu Phe Asp Hie Met Gly Ser Phe Ser Arg Ala Val Lys Glu Arg O 95/21922 463 965 970 975 TTG CTG GAG TGG GAC GCG GCT TTG GAG MCC CTG TCA TTC ACT AGG ACG 2976 Leu Leu Glu Trp Aep Ala Ala Leu Glu Xaa Leu Ser Phe Thr Arg Thr 980 985 990 GAC TGT CGC ATC ATA CGA GAC GCC GCC AGG ACC CTG AGC TGC GGC CAA 3024 Aep Cyβ Arg He He Arg Aep Ala Ala Arg Thr Leu Ser Cye Gly Gin 995 1000 1005 TGC GTC ATG GGC TTG CCC GTG GTG GCT AGG CGC GGC GAT GAG GTC CTG 3072 Cys Val Met Gly Leu Pro Val Val Ala Arg Arg Gly Aep Glu Val Leu 1010 1015 1020 ATT GGG GTC TTT CAG GAT GTG AAC CAC TTG CCT CCG GGG TTT GYT CCT 3120 He Gly Val Phe Gin Aep Val Asn Hie Leu Pro Pro Gly Phe Xaa Pro 1025 1030 1035 1040 ACA GCG CCT GTT GTC ATC CGT CGG TGC GGA AAG GGC TTC CTC GGG GTC 3168 Thr Ala Pro Val Val He Arg Arg Cyβ Gly Lye Gly Phe Leu Gly Val 1045 1050 1055 ACT AAG GCT GCC TTG ACT GGT CGG GAT CCT GAC TTA CAC CCA GGA AAC 3216 Thr Lye Ala Ala Leu Thr Gly Arg Aep Pro Asp Leu His Pro Gly Aβn 1060 1065 1070 GTC ATG GTT TTG GGG ACG GCT ACC TCG CGC AGC ATG GGA ACG TGC TTA 3264 Val Met Val Leu Gly Thr Ala Thr Ser Arg Ser Met Gly Thr Cyβ Leu 1075 1080 1085 AAC GGG TTG CTG TTC ACG ACA TTC CAT GGG GCT TCT TCC CGA ACC ATT 3312 Aβn Gly Leu Leu Phe Thr Thr Phe Hiβ Gly Ala Ser Ser Arg Thr He 1090 1095 1100 GCG ACA CCT GTG GGG GCC CTT AAC CCA AGG TGG TGG TCG GCC AGT GAT 3360 Ala Thr Pro Val Gly Ala Leu Asn Pro Arg Trp Trp Ser Ala Ser Asp 1105 1110 1115 1120 GAC GTC ACG GTC TAT CCC CTC CCC GAT GGA GCT AAC TCG TTG GTT CCC 3408 Aep Val Thr Val Tyr Pro Leu Pro Aep Gly Ala Asn Ser Leu Val Pro 1125 1130 1135 TGC TCG TGT CAG GCT GAG TCC TGT TGG GTC ATY CGA TCC GAT GGG GCT 3456 Cys Ser Cys Gin Ala Glu Ser Cye Trp Val Xaa Arg Ser Aep Gly Ala 1140 1145 1150 CTT TGC CAT GGC TTG AGC AAG GGG GAC AAG GTA GAA CTG GAC GTG GCC 3504 Leu Cye Hie Gly Leu Ser Lys Gly Asp Lys Val Glu Leu Asp Val Ala 1155 1160 1165 ATG GAG GTT GCT GAC TTT CGT GGG TCG TCT GGG TCT CCT GTC CTA TGC 3552 Met Glu Val Ala Asp Phe Arg Gly Ser Ser Gly Ser Pro Val Leu Cyβ 1170 1175 1180 GAC GAG GGG CAC GCT GTA GGA ATG CTC GTG TCC GTC CTT CAT TCG GGG 3600 Aep Glu Gly Hiβ Ala Val Gly Met Leu Val Ser Val Leu Hiβ Ser Gly 1185 1190 1195 1200 O 95/21922 464 GGG AGG GTG ACC GCG GCT CGA TTC ACT CGG CCG TGG ACC CAA GTC CCA 3648 Gly Arg Val Thr Ala Ala Arg Phe Thr Arg Pro Trp Thr Gin Val Pro 1205 1210 1215 ACA GAC GCC AAG ACT ACC ACT GAG CCA CCC CCG GTG CCA GCT AAA GGG 3696 Thr Asp Ala Lys Thr Thr Thr Glu Pro Pro Pro Val Pro Ala Lye Gly 1220 1225 1230 GTT TTC AAA GAG GCT CCT CTT TTC ATG CCA ACA GGG GCG GGG AAA AGC 3744 Val Phe Lye Glu Ala Pro Leu Phe Met Pro Thr Gly Ala Gly Lye Ser 1235 1240 1245 ACA CGC GTC CCT TTG GAG TAT GGA AAC ATG GGG CAC AAG GTC CTG ATT 3792 Thr Arg Val Pro Leu Glu Tyr Gly Aβn Met Gly Hiβ Lys Val Leu He 1250 1255 1260 CTC AAC CCG TCG GTT GCC ACT GTG AGG GCC ATG GGC CCT TAC ATG GAG 3840 Leu Asn Pro Ser Val Ala Thr Val Arg Ala Met Gly Pro Tyr Met Glu 1265 1270 1275 1280 AGG CTG GCG GGG AAA CAT CCT AGC ATT TTC TGT GGA CAC GAC ACA ACA 3888 Arg Leu Ala Gly Lys Hie Pro Ser He Phe Cye Gly Hiβ Aep Thr Thr 1285 1290 1295 GCT TTC ACA CGG ATC ACG GAC TCT CCA TTG ACG TAC TCT ACC TAT GGG 3936 Ala Phe Thr Arg He Thr Aep Ser Pro Leu Thr Tyr Ser Thr Tyr Gly 1300 1305 1310 AGG TTT CTG GCC AAC CCG AGG CAG ATG CTG AGG GGA GTT TCC GTG GTC 3984 Arg Phe Leu Ala Aβn Pro Arg Gin Met Leu Arg Gly Val Ser Val Val 1315 1320 1325 ATC TGT GAT GAG TGC CAC AGT CAT GAC TCA ACT GTG TTG CTG GGT ATA 4032 He Cyβ Aep Glu Cyβ His Ser His Aep Ser Thr Val Leu Leu Gly He 1330 1335 1340 GGC AGG GTC AGG GAC GTG GCG CGG GGG TGT GGA GTG CAA TTA GTG CTC 4080 Gly Arg Val Arg Aep Val Ala Arg Gly Cyβ Gly Val Gin Leu Val Leu 1345 1350 1355 1360 TAC GCT ACT GCG ACT CCC CCG GGC TCG CCT ATG ACT CAG CAT CCA TCC 4128 Tyr Ala Thr Ala Thr Pro Pro Gly Ser Pro Met Thr Gin Hiβ Pro Ser 1365 1370 1375 ATA ATT GAG ACA AAG CTG GAC GTT GGT GAG ATC CCC TTT TAT GGG CAT 4176 He He Glu Thr Lye Leu Aep Val Gly Glu He Pro Phe Tyr Gly Hiβ 1380 1385 1390 GGT ATC CCC CTC GAG CGT ATG AGG ACT GGT CGC CAC CTT GTA TTC TGC 4224 Gly He Pro Leu Glu Arg Met Arg Thr Gly Arg His Leu Val Phe Cys 1395 1400 1405 CAT TCC AAG GCG GAG TGC GAG AGA TTG GCC GGC CAG TTC TCC GCG CGG 4272 His Ser Lye Ala Glu Cyβ Glu Arg Leu Ala Gly Gin Phe Ser Ala Arg 1410 1415 1420 GGG GTT AAT GCC ATC GCC TAT TAT AGG GGT AAG GAC AGT TCC ATC ATC 4320 465 Gly Val Asn Ala He Ala Tyr Tyr Arg Gly Lye Asp Ser Ser He He 1425 1430 1435 1440 AAA GAC GGA GAC CTG GTG GTT TGT GCG ACA GAC GCG CTC TCT ACC GGG 4368 Lys Asp Gly Asp Leu Val Val Cys Ala Thr Aep Ala Leu Ser Thr Gly 1445 1450 1455 TAC ACA GGA AAC TTC GAT TCT GTC ACC GAC TGT GGG TTG GTG GTG GAG 4416 Tyr Thr Gly Aen Phe Aep Ser Val Thr Aep Cyβ Gly Leu Val Val Glu 1460 1465 1470 GAG GTC GTT GAG GTG ACC CTT GAT CCC ACC ATT ACC ATT TCC TTG CGG 4464 Glu Val Val Glu Val Thr Leu Aep Pro Thr He Thr He Ser Leu Arg 1475 1480 1485 ACT GTC CCT GCT TCG GCT GAA TTG TCG ATG CAG CGG CGC GGA CGC ACG 4512 Thr Val Pro Ala Ser Ala Glu Leu Ser Met Gin Arg Arg Gly Arg Thr 1490 1495 1500 GGG AGA GGT CGG TCG GGC CGC TAC TAC TAC GCT GGG GTC GGT AAG GCT 4560 Gly Arg Gly Arg Ser Gly Arg Tyr Tyr Tyr Ala Gly Val Gly Lye Ala 1505 1510 1515 1520 CCC GCG GGG GTG GTG CGG TCT GGT CCG GTC TGG TCG GCA GTG GAA GCT 4608 Pro Ala Gly Val Val Arg Ser Gly Pro Val Trp Ser Ala Val Glu Ala 1525 1530 1535 GGA GTG ACC TGG TAT GGA ATG GAA CCT GAC TTG ACA GCA AAC CTT CTG 4656 Gly Val Thr Trp Tyr Gly Met Glu Pro Asp Leu Thr Ala Aβn Leu Leu 1540 1545 1550 AGA CTT TAC GAC GAC TGC CCT TAC ACC GCA GCC GTC GCA GCT GAC ATT 4704 Arg Leu Tyr Aep Asp Cys Pro Tyr Thr Ala Ala Val Ala Ala Asp He 1555 1560 1565 GGT GAA GCC GCG GTG TTC TTT GCG GGC CTC GCG CCC CTC AGG ATG CAT 4752 Gly Glu Ala Ala Val Phe Phe Ala Gly Leu Ala Pro Leu Arg Met His 1570 1575 1580 CCC GAT GTT AGC TGG GCA AAA GTT CGC GGC GTC AAT TGG CCC CTC CTG 4800 Pro Asp Val Ser Trp Ala Lys Val Arg Gly Val Asn Trp Pro Leu Leu 1585 1590 1595 1600 GTG GGT GTT CAG CGG ACG ATG TGT CGG GAA ACA CTG TCT CCC GGC CCG 4848 Val Gly Val Gin Arg Thr Met Cys Arg Glu Thr Leu Ser Pro Gly Pro 1605 1610 1615 TCG GAC GAC CCT CAG TGG GCA GGT CTG AAA GGC CCG AAT CCT GTC CCA 4896 Ser Asp Aep Pro Gin Trp Ala Gly Leu Lys Gly Pro Asn Pro Val Pro 1620 1625 1630 CTA CTG CTG AGG TGG GGC AAT GAT TTG CCA TCA AAA GTG GCC GGC CAC 4944 Leu Leu Leu Arg Trp Gly Aβn Aep Leu Pro Ser Lye Val Ala Gly Hie 1635 1640 1645 CAC ATA GTT GAC GAT CTG GTC CGT CGG--CTC GGT GTG GCG GAG GGA TAC 4992 Hiβ He Val Asp Aep Leu Val Arg Arg Leu Gly Val Ala Glu Gly Tyr O 95/21922 466 1650 1655 1660 GTG CGC TGT GAT GCT GGR CCC ATC CTC ATG GTG GGC TTG GCC ATA GCG 5040 Val Arg Cys Aep Ala Xaa Pro He Leu Met Val Gly Leu Ala He Ala 1665 1670 1675 1680 GGC GGC ATG ATC TAC GCC TCT TAC ACT GGG TCG CTA GTG GTG GTA ACA 5088 Gly Gly Met He Tyr Ala Ser Tyr Thr Gly Ser Leu Val Val Val Thr 1685 1690 1695 GAC TGG GAT GTG AAG GGA GGT GGC AAT CCC CTT TAT AGG AGT GGT GAC 5136 Aep Trp Aep Val Lye Gly Gly Gly Aβn Pro Leu Tyr Arg Ser Gly Asp 1700 1705 1710 CAG GCC ACC CCT CAA CCC GTG GTG CAG GTC CCC CCG GTA GAC CAT CGG 5184 Gin Ala Thr Pro Gin Pro Val Val Gin Val Pro Pro Val Aep Hie Arg 1715 1720 1725 CCG GGG GGG GAG TCT GCG CCA CGG GAT GCC AAG ACA GTG ACA GAT GCG 5232 Pro Gly Gly Glu Ser Ala Pro Arg Aep Ala Lys Thr Val Thr Asp Ala 1730 1735 1740 GTG GCA GCC ATC CAG GTG AAC TGC GAT TGG TCT GTG ATG ACC CTG TCG 5280 Val Ala Ala He Gin Val Asn Cys Asp Trp Ser Val Met Thr Leu Ser 1745 1750 1755 1760 ATC GGG GAA GTC CTC ACC TTG GCT CAG GCT AAG ACA GCC GAG GCC TAC 5328 He Gly Glu Val Leu Thr Leu Ala Gin Ala Lys Thr Ala Glu Ala Tyr 1765 1770 1775 GCA GCT ACT TCC AGG TGG CTC GCT GGC TGC TAC ACG GGG ACG CGG GCC 5376 Ala Ala Thr Ser Arg Trp Leu Ala Gly Cys Tyr Thr Gly Thr Arg Ala 1780 1785 1790 GTC CCC ACT GTA TCA ATT GTT GAC AAG CTC TTC GCC GGG GGT TGG GCC 5424 Val Pro Thr Val Ser He Val Asp Lys Leu Phe Ala Gly Gly Trp Ala 1795 1800 1805 GCC GTG GTG GGT CAC TGT CAC AGC GTC ATT GCT GCG GCG GTG GCT GCC 5472 Ala Val Val Gly His Cys His Ser Val He Ala Ala Ala Val Ala Ala 1810 1815 1820 TAT GGA GCT TCT CGA AGT CCT CCA CTG GCC GCG GCG GCG TCC TAC CTC 5520 Tyr Gly Ala Ser Arg Ser Pro Pro Leu Ala Ala Ala Ala Ser Tyr Leu 1825 1830 1835 1840 ATG GGG TTG GGC GTC GGA GGC AAC GCA CAG GCG CGC TTG GCT TCA GCT 5568 Met Gly Leu Gly Val Gly Gly Asn Ala Gin Ala Arg Leu Ala Ser Ala 1845 1850 1855 CTT CTA CTG GGG GCT GCT GGT ACG GCT CTG GGG ACC CCT GTC GTG GGA 5616 Leu Leu Leu Gly Ala Ala Gly Thr Ala Leu Gly Thr Pro Val Val Gly 1860 1865 1870 CTC ACC ATG GCG GGG GCC TTC ATG GGC GGT GCC AGC GTG TCC CCC TCC 5664 Leu Thr Met Ala Gly Ala Phe Met Gly Gly Ala Ser Val Ser Pro Ser 1875 1880 1885 PCΪY O 95/21922 467 CTC GTC ACT GTC CTA CTT GGG GCT GTG GGA GGT TGG GAG GGC GTT GTC 5712 Leu Val Thr Val Leu Leu Gly Ala Val Gly Gly Trp Glu Gly Val Val 1890 1895 1900 AAC GCT GCC AGT CTC GTC TTC GAC TTC ATG GCT GGG AAA CTT TCA ACA 5760 Aβn Ala Ala Ser Leu Val Phe Asp Phe Met Ala Gly Lys Leu Ser Thr 1905 1910 1915 1920 GAA GAC CTT TGG TAT GCC ATC CCG GTA CTC ACT AGT CCT GGR GCG GGC 5808 Glu Aep Leu Trp Tyr Ala He Pro Val Leu Thr Ser Pro Xaa Ala Gly 1925 1930 1935 CTC GCG GGG ATT GCC CTT GGT CTG GTT TTG TAC TCA GCA AAC AAC TCT 5856 Leu Ala Gly He Ala Leu Gly Leu Val Leu Tyr Ser Ala Aen Aβn Ser 1940 1945 1950 GGC ACT ACC ACA TGG CTG AAC CGT CTG CTG ACG ACG TTG CCA CGG TCA 5904 Gly Thr Thr Thr Trp Leu Aβn Arg Leu Leu Thr Thr Leu Pro Arg Ser 1955 1960 1965 TCT TGC ATA CCC GAC AGC TAC TTC CAA CAG GCT GAC TAC TGC GAC AAG 5952 Ser Cys He Pro Aep Ser Tyr Phe Gin Gin Ala Asp Tyr Cys Asp Lye 1970 1975 1980 GTC TCG GCA ATC GTG CGC CGC CTG AGC CTT ACT CGC ACC GTG GTG GCC 6000 Val Ser Ala He Val Arg Arg Leu Ser Leu Thr Arg Thr Val Val Ala 1985 1990 1995 2000 CTG GTC AAC AGG GAG CCT AAG GTG GAT GAG GTC CAG GTG GGG TAC GTC 6048 Leu Val Asn Arg Glu Pro Lys Val Aep Glu Val Gin Val Gly Tyr Val 2005 2010 2015 TGG GAT CTG TGG GAG TGG GTG ATG CGC CAG GTG CGC ATG GTG ATG TCT 6096 Trp Aep Leu Trp Glu Trp Val Met Arg Gin Val Arg Met Val Met Ser 2020 2025 2030 AGA CTC CGG GCC CTC TGC CCT GTG GTG TCA CTC CCC TTG TGG CAC TGC 6144 Arg Leu Arg Ala Leu Cyβ Pro Val Val Ser Leu Pro Leu Trp Hie Cys 2035 2040 2045 GGG GAG GGG TGG TCC GGT GAA TGG CTT CTC GAT GGG CAC GTG GAG AGT 6192 Gly Glu Gly Trp Ser Gly Glu Trp Leu Leu Asp Gly His Val Glu Ser 2050 2055 2060 CGT TGT CTG TGC GGG TGT GTA ATC ACC GGC GAC GTC CTC AAT GGG CAA 6240 Arg Cys Leu Cyβ Gly Cyβ Val He Thr Gly Asp Val Leu Aβn Gly Gin 2065 2070 2075 2080 CTC AAA GAT CCA GTT TAC TCT ACC AAG CTG TGC AGG CAC TAC TGG ATG 6288 Leu Lys Aep Pro Val Tyr Ser Thr Lye Leu Cys Arg Hiβ Tyr Trp Met 2085 2090 2095 GGA ACT GTG CCG GTC AAC ATG CTG GGC TAC GGG GAA ACC TCA CCT CTT 6336 Gly Thr Val Pro Val Aβn Met Leu Gly Tyr Gly Glu Thr Ser Pro Leu 2100 2105 2110 CTC GCC TCT GAC ACC CCG AAG GTG GTA CCC TTC GGG ACG TCG GGG TGG 6384 95/21922 468 Leu Ala Ser Asp Thr Pro Lys Val Val Pro Phe Gly Thr Ser Gly Trp 2115 2120 2125 GCT GAG GTG GTG GTG ACC CCT ACC CAC GTG GTG ATC AGG CGC ACG TCC 6432 Ala Glu Val Val Val Thr Pro Thr Hiβ Val Val He Arg Arg Thr Ser 2130 2135 2140 TGT TAC AAA CTG CTT CGC CAG CAA ATT CTT TCA GCA GCT GTA GCT GAG 6480 Cye Tyr Lye Leu Leu Arg Gin Gin He Leu Ser Ala Ala Val Ala Glu 2145 2150 2155 2160 CCC TAC TAC GTT GAT GGC ATT CCG GTC TCT TGG GAG GCT GAC GCG AGA 6528 Pro Tyr Tyr Val Asp Gly He Pro Val Ser Trp Glu Ala Asp Ala Arg 2165 2170 2175 GCG CCG GCC ATG GTC TAC GGT CCG GGC CAA AGT GTT ACC ATT GAT GGG 6576 Ala Pro Ala Met Val Tyr Gly Pro Gly Gin Ser Val Thr He Asp Gly 2180 2185 2190 GAG CGC TAC ACC CTT CCG CAC CAG TTG CGG ATG CGG AAT GTG GCG CCC 6624 Glu Arg Tyr Thr Leu Pro His Gin Leu Arg Met Arg Asn Val Ala Pro 2195 2200 2205 TCT GAG GTT TCA TCT GAG GTC AGC ATC GAG ATC GGG ACG GAG ACT GAA 6672 Ser Glu Val Ser Ser Glu Val Ser He Glu He Gly Thr Glu Thr Glu 2210 2215 2220 GAC TCA GAA CTG ACT GAG GCC GAT TTG CCA CCA GCG GCT GCT GCC CTC 6720 Aep Ser Glu Leu Thr Glu Ala Aep Leu Pro Pro Ala Ala Ala Ala Leu 2225 2230 2235 2240 CAA GCG ATA GAG AAT GCT GCG AGA ATT CTC GAA CCG CAC ATC GAT GTC 6768 Gin Ala He Glu Aβn Ala Ala Arg He Leu Glu Pro Hiβ He Asp Val 2245 2250 2255 AYC ATG GAG GAT TGC AGT ACA CCC TCT CTC TGT GGT AGT AGC CGA GAG 6816 Xaa Met Glu Asp Cys Ser Thr Pro Ser Leu Cye Gly Ser Ser Arg Glu 2260 2265 2270 ATG CCT GTG TGG GGA GAA GAC ATA CCC CGC ACT CCA TCG CCT GCA CTT 6864 Met Pro Val Trp Gly Glu Asp He Pro Arg Thr Pro Ser Pro Ala Leu 2275 2280 2285 ATC TCG GTT ACG GAG AGC AGC TCA GAT GAG AAG ACC CTG TCG GTG ACC 6912 He Ser Val Thr Glu Ser Ser Ser Asp Glu Lye Thr Leu Ser Val Thr 2290 2295 2300 TCC TCG CAG GAG GAC ACC CCG TCC TCA GAC TCA TTT GAA GTC ATC CAA 6960 Ser Ser Gin Glu Aep Thr Pro Ser Ser Aep Ser Phe Glu Val He Gin 2305 2310 2315 2320 GAG TCT GAT ACT GCT GAA TCA GAG GAA AGC GTC TTC AAC GTG GCT CTT 7008 Glu Ser Aep Thr Ala Glu Ser Glu Glu Ser Val Phe Aen Val Ala Leu 2325 2330 2335 TCC GTA CTA AAA GCC TTA TTT CCA CAG AGC GAT GCC ACA CGA AAG CTA 7056 Ser Val Leu Lye Ala Leu Phe Pro Gin Ser Aep Ala Thr Arg Lye Leu O 95/21922 469 2340 2345 2350 ACG GTT AAG ATG TCT TGC TGT GTT GAG AAG AGC GTA ACA CGC TTC TTT 7104 Thr Val Lye Met Ser Cyβ Cyβ Val Glu Lye Ser Val Thr Arg Phe Phe 2355 2360 2365 TCT TTA GGG TTG ACC GTG GCT GAC GTG GCT AGC CTG TGT GAG ATG GAG 7152 Ser Leu Gly Leu Thr Val Ala Asp Val Ala Ser Leu Cys Glu Met Glu 2370 2375 2380 ATC CAG AAC CAT ACA GCC TAT TGT GAC AAG GTG CGC ACT CCG CTC GAA 7200 He Gin Asn His Thr Ala Tyr Cys Asp Lye Val Arg Thr Pro Leu Glu 2385 2390 2395 2400 TTG CAA GTT GGG TGC TTG GTG GGC AAT GAA CTT ACC TTT GAA TGT GAC 7248 Leu Gin Val Gly Cys Leu Val Gly Asn Glu Leu Thr Phe Glu Cys Asp 2405 2410 2415 AAG TGT GAG GCA CGC CAA GAG ACC CTT GCC TCC TTC TCC TAC ATA TGG 7296 Lys Cys Glu Ala Arg Gin Glu Thr Leu Ala Ser Phe Ser Tyr He Trp 2420 2425 2430 TCC GGG GTC CCA CTT ACT CGG GCC ACT CCG GCC AAA CCA CCA GTG GTG 7344 Ser Gly Val Pro Leu Thr Arg Ala Thr Pro Ala Lys Pro Pro Val Val 2435 2440 2445 AGG CCG GTG GGG TCC TTG TTG GTG GCA GAC ACC ACC AAG GTC TAC GTG 7392 Arg Pro Val Gly Ser Leu Leu Val Ala Asp Thr Thr Lys Val Tyr Val 2450 2455 2460 ACC AAT CCG GAC AAT GTT GGG AGG AGG GTT GAC AAG GTG ACT TTC TGG 7440 Thr Asn Pro Asp Asn Val Gly Arg Arg Val Asp Lye Val Thr Phe Trp 2465 2470 2475 2480 CGC GCT CCT CGG GTA CAC GAC AAG TTC CTC GTG GAC TCG ATC GAG CGC 7488 Arg Ala Pro Arg Val His Asp Lys Phe Leu Val Asp Ser He Glu Arg 2485 2490 2495 GCT CGG AGA GCT GCT CAA GGC TGC CTA AGC ATG GGT TAC ACT TAT GAG 7536 Ala Arg Arg Ala Ala Gin Gly Cye Leu Ser Met Gly Tyr Thr Tyr Glu 2500 2505 2510 GAG GCA ATA AGG ACT GTT AGG CCG CAT GCT GCC ATG GGC TGG GGA TCT 7584 Glu Ala He Arg Thr Val Arg Pro Hie Ala Ala Met Gly Trp Gly Ser 2515 2520 2525 AAG GTG TCG GTC AAG GAC TTG GCC ACC CCT GCG GGG AAG ATG GCT GTT 7632 Lye Val Ser Val Lye Asp Leu Ala Thr Pro Ala Gly Lys Met Ala Val 2530 2535 2540 CAT GAC CGG CTT CAG GAG ATA CTT GAA GGG ACT CCG GTC CCT TTT ACC 7680 His Aep Arg Leu Gin Glu He Leu Glu Gly Thr Pro Val Pro Phe Thr 2545 2550 2555 2560 CTG ACT GTC AAA AAG GAG GTG TTC TTC AAA GAT CGT AAG GAG GAG AAG 7728 Leu Thr Val Lys Lye Glu Val Phe Phe Lys Asp Arg Lye Glu Glu Lye 2565 2570 2575 O 95/2 470 GCC CCC CGC CTC ATT GTG TTC CCC CCC CTG GAC TTC CGG ATA GCT GAA 7776 Ala Pro Arg Leu He Val Phe Pro Pro Leu Aep Phe Arg He Ala Glu 2580 2585 2590 AAG CTC ATT CTG GGA GAC CCG GGG CGG GTT GCA AAG GCC GGT GTT GGG 7824 Lye Leu He Leu Gly Asp Pro Gly Arg Val Ala Lye Ala Gly Val Gly 2595 2600 2605 GGG GCT TAC GCC TTC CAG TAC ACC CCC AAC CAG CGG GTT AAG GAG ATG 7872 Gly Ala Tyr Ala Phe Gin Tyr Thr Pro Aβn Gin Arg Val Lye Glu Met 2610 2615 2620 CTA AAG CTG TGG GAA TCA AAG AAG ACC CCG TGC GCC ATC TGT GTG GAT 7920 Leu Lye Leu Trp Glu Ser Lye Lye Thr Pro Cyβ Ala He Cyβ Val Aep 2625 2630 2635 2640 GCC ACT TGC TTC GAC AGT AGC ATT ACT GAR GAG GAC GTG GCA CTA GAG 7968 Ala Thr Cyβ Phe Aep Ser Ser He Thr Xaa Glu Aep Val Ala Leu Glu 2645 2650 2655 ACA GAG CTT TAC GCC CTG GCC TCG GAC CAT CCA GAA TGG GTG CGC GCC 8016 Thr Glu Leu Tyr Ala Leu Ala Ser Aep Hie Pro Glu Trp Val Arg Ala 2660 2665 2670 CTG GGG AAA TAC TRT GCC TCT GGC ACA ATG GTG ACC CCG GAA GGG GTG 8064 Leu Gly Lye Tyr Xaa Ala Ser Gly Thr Met Val Thr Pro Glu Gly Val 2675 2680 2685 CCA GTG GGC GAG AGG TAT TGT AGG TCC TCG GGT GTG TTG ACC ACA AGT 8112 Pro Val Gly Glu Arg Tyr Cye Arg Ser Ser Gly Val Leu Thr Thr Ser 2690 2695 2700 GCT AGC AAC TGT TTG ACC TGC TAC ATC AAA GTG AGA GCC GCC TGT GAG 8160 Ala Ser Aen Cyβ Leu Thr Cye Tyr He Lye Val Arg Ala Ala Cyβ Glu 2705 2710 2715 2720 AGG ATC GGA CTG AAA AAT GTC TCG CTT CTC ATC GCG GGC GAT GAC TGC 8208 Arg He Gly Leu Lye Aβn Val Ser Leu Leu He Ala Gly Aep Aep Cyβ 2725 2730 2735 TTA ATT GTG TGC GAG AGG CCT GTA TGC GAC CCT TGC GAG GCC CTG GGC 8256 Leu He Val Cyβ Glu Arg Pro Val Cye Aep Pro Cye Glu Ala Leu Gly 2740 2745 2750 CGA ACC CTG GCT TCG TAC GGG TAC GCG TGT GAG CCC TCG TAT CAC GCT 8304 Arg Thr Leu Ala Ser Tyr Gly Tyr Ala Cye Glu Pro Ser Tyr Hiβ Ala 2755 2760 2765 TCA CTG GAC ACA GCC CCC TTC TGC TCC ACT TGG CTC GCT GAG TGC AAT 8352 Ser Leu Aep Thr Ala Pro Phe Cye Ser Thr Trp Leu Ala Glu Cyβ Aβn 2770 2775 2780 GCG GAT GGG RAA AGG CAT TTC TTC CTG ACC ACG GAC TTT CGG AGA CCA 8400 Ala Aep Gly Xaa Arg Hie Phe Phe Leu Thr Thr Aep Phe Arg Arg Pro 2785 2790 2795 2800 CTC GCT CGC ATG TCG AGC GAG TAC AGT GAC CCT ATG GCT TCG GCC ATT 8448 95/21922 471 Leu Ala Arg Met Ser Ser Glu Tyr Ser Asp Pro Met Ala Ser Ala He 2805 2810 2815 GGT TAC ATT CTC CTC TAC CCC TGG CRT CCC ATC ACA CGG TGG GTC ATC 8496 Gly Tyr He Leu Leu Tyr Pro Trp Xaa Pro He Thr Arg Trp Val He 2820 2825 2830 ATC CCG CAT GTG CTA ACA TGC GCT TCT TCC CGG GGT GGT GGC ACA CSG 8544 He Pro His Val Leu Thr Cys Ala Ser Ser Arg Gly Gly Gly Thr Xaa 2835 2840 2845 TCT GAT CCG GTT TGG TGT CAG GTT CAT GGT AAC TAC TAC AAG TTT CCC 8592 Ser Asp Pro Val Trp Cye Gin Val Hiβ Gly Aβn Tyr Tyr Lys Phe Pro 2850 2855 2860 CTG GAC AAA CTG CCT AAC ATC ATC GTG GCC CTC CAC GGA CCA GCA GCG 86 0 Leu Aep Lye Leu Pro Asn He He Val Ala Leu His Gly Pro Ala Ala 2865 2870 2875 2880 TTG AGG GTT ACC GCA GAC ACA ACC AAA ACA AAG ATG GAG GCT GGG AAG 8688 Leu Arg Val Thr Ala Asp Thr Thr Lys Thr Lys Met Glu Ala Gly Lys 2885 2890 2895 GTT CTG AGC GAC CTC AAG CTC CCT GGT CTA GCC GTC CAC CGC AAG AAG 8736 Val Leu Ser Asp Leu Lye Leu Pro Gly Leu Ala Val Hiβ Arg Lye Lye 2900 2905 2910 GCC GGG GCA TTG CGA ACA CGC ATG CTC CGG TCG CGC GGT TGG GCG GAG 8784 Ala Gly Ala Leu Arg Thr Arg Met Leu Arg Ser Arg Gly Trp Ala Glu 2915 2920 2925 TTG GCT AGG GGC CTG TTG TGG CAT CCA GGA CTC CGG CTT CCT CCC CCT 8832 Leu Ala Arg Gly Leu Leu Trp Hie Pro Gly Leu Arg Leu Pro Pro Pro 2930 2935 2940 GAG ATT GCT GGT ATC CCA GGG GGT TTC CCT CTG TCC CCC CCC TAC ATG 8880 Glu He Ala Gly He Pro Gly Gly Phe Pro Leu Ser Pro Pro Tyr Met 2945 2950 2955 2960 GGG GTG GTT CAT CAA TTG GAT TTC ACA GCS CAG CGG AGT CGC TGG CGG 8928 Gly Val Val Hiβ Gin Leu Aep Phe Thr Xaa Gin Arg Ser Arg Trp Arg 2965 2970 2975 TGG TTG GGG TTC TTA GCC CTG CTC ATC GTA GCG CTC TTT GGG TGA ACT 8976 Trp Leu Gly Phe Leu Ala Leu Leu He Val Ala Leu Phe Gly * Thr 2980 2985 2990 AAA TTC ATC TGT TGC GGC CGG AGT CAG ACC TGA GCC CCG TTC AAA AGG 9024 Lye Phe He Cye Cys Gly Arg Ser Gin Thr * Ala Pro Phe Lye Arg 2995 3000 3005 GGA TTG AGA C 9034 Gly Leu Arg 3010 (2) INFORMATION FOR SEQ ID NO:401: 472 (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 19 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:401: Lys Gly Gly Gly Trp Val Met Thr Gly Leu Val Gly Arg Lys Ser Arg 1 5 10 15 Ser Ser Trp (2) INFORMATION FOR SEQ ID NO:402: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 33 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:402: Val Gly Leu Lye Gly Arg Leu Arg Ser Leu Leu Arg He Trp Arg Lye 1 5 10 15 Ser Ala Arg Ser Thr Gly Val Gly Pro Thr Gly Val He Arg Thr Arg 20 25 30 Arg (2) INFORMATION FOR SEQ ID NO:403: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 23 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:403: Thr Glu Pro Val Thr Pro Leu Gly Lye Arg Arg Pro Arg Thr Val His 1 5 10 15 Val Ala Leu Gin Cys Leu Ser 20 (2) INFORMATION FOR SEQ ID NO:404: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2905 amino acids (B) TYPE: amino acid 473 (D) TOPOLOGY: linear (ii) MOLECULE TYPE : protein (xi) SEQUENCE DESCRIPTION : SEQ ID NO : 404 : Pro He Gly Val Arg Arg Val Asp Lys Aep Gin Trp Gly Pro Gly Gly 1 5 10 15 Arg Gly Lye Aep Pro Hiβ Arg Cye Pro Ser Arg Gly Gly Gly Lys Cyβ 20 25 30 Met Gly Pro Pro Ser Ser Ala Ala Ala Tyr Ser Arg Gly Ser Pro Arg 35 40 45 Thr Ser Gly Glu Gly Gly Trp Hiβ Phe Phe Ser Tyr Thr Aep His Gly 50 55 60 Ser Pro Ser Ala Pro Thr Arg Gly Gly Ala Gly Ala He Leu Ala Pro 65 70 75 80 Ala Thr His Ala Cys Ser Ala Lys Gly Gin Tyr Xaa Leu Thr Asn Cye 85 90 95 Cys Ala Leu Glu Asp He Gly Phe Cye Leu Glu Gly Gly Cys Leu Val 100 105 110 Ala Leu Gly Cys Thr He Cys Thr Asp Arg Cys Trp Pro Leu Tyr Gin 115 120 125 Ala Gly Leu Ala Val Arg Pro Gly Lys Ser Ala Ala Gin Leu Val Gly 130 135 140 Glu Leu Gly Ser Leu Tyr Gly Pro Leu Ser Val Ser Ala Tyr Val Ala 145 150 155 160 Gly He Leu Gly Leu Gly Glu Val Tyr Ser Gly Val Leu Thr Val Gly 165 170 175 Val Ala Leu Thr Arg Arg Val Tyr Pro Val Pro Asn Leu Thr Cys Ala 180 185 190 Val Glu Cys Glu Leu Lys Trp Glu Ser Glu Phe Trp Arg Trp Thr Glu 195 200 205 Gin Leu Ala Ser Asn Tyr Trp He Leu Glu Tyr Leu Trp Lys Val Pro 210 215 220 Phe Asp Phe Trp Arg Gly Val Met Ser Leu Thr Pro Leu Leu Val Cys 225 230 235 240 Val Ala Ala Leu Leu Leu Leu Glu Gin Arg He Val Met Val Phe Leu 245 250 255 Leu Val Thr Met Ala Gly Met Ser Gin Gly Ala Pro Ala Ser Ser Val 260 265 270 474 Gly Val Thr Ala Phe Arg Gly Gly Phe Aep Leu Ala Val Leu Phe Leu 275 280 285 Gin Val Glu Arg Val Pro Arg Ala Asp Arg Glu Arg Val Trp Glu Arg 290 295 300 Gly Asn Val Thr Leu Leu Cys Asp Cyβ Pro Aβn Gly Pro Trp Val Trp 305 310 315 320 Val Pro Ala Leu Cyβ Gin Ala He Gly Trp Gly Aep Pro He Thr Hiβ 325 330 335 Trp Ser Hiβ Gly Gin Aen Gin Trp Pro Leu Ser Cys Pro Gin Phe Val 340 345 350 Tyr Gly Ala Val Ser Val Thr Cye Val Trp Gly Ser Val Ser Trp Phe 355 360 365 Ala Ser Thr Gly Gly Arg Asp Ser Lye Val Aep Val Trp Ser Leu Val 370 375 380 Pro Val Gly Ser Ala Ser Cyβ Thr He Ala Ala Leu Gly Ser Ser Aep 385 390 395 400 Arg Asp Thr Val Val Glu Leu Ser Glu Trp Gly He Pro Cys Ala Thr 405 410 415 Cys He Leu Asp Arg Arg Pro Ala Ser Cys Gly Thr Cys Val Arg Aep 420 425 430 Cyβ Trp Pro Glu Thr Gly Ser Val Arg Phe Pro Phe Hie Arg Cyβ Gly 435 440 445 Ala Gly Pro Arg Leu Thr Arg Asp Leu Glu Ala Val Pro Phe Val Asn 450 455 460 Arg Thr Thr Pro Phe Thr He Arg Gly Pro Leu Gly Asn Gin Gly Arg 465 470 475 480 Gly Asn Pro Val Arg Ser Pro Leu Gly Phe Gly Ser Tyr Thr Met Thr 485 490 495 Lys He Arg Asp Ser Leu His Leu Val Lys Cys Pro Thr Pro Ala He 500 505 510 Glu Pro Pro Thr Gly Thr Phe Gly Phe Phe Pro Gly Val Pro Pro Leu 515 520 525 Asn Asn Cyβ Met Leu Leu Gly Thr Glu Val Ser Glu Val Leu Gly Gly 530 535 540 Ala Gly Leu Thr Gly Gly Phe Tyr Glu Pro Leu Val Arg Arg Cye Ser 545 550 555 560 Glu Leu Met Gly Arg Arg Aen Pro Val Cyβ Pro Gly Phe Ala Trp Leu 565 570 575 O 95/21922 475 Ser Ser Gly Arg Pro Aep Gly Phe He His Val Gin Gly His Leu Gin 580 585 590 Glu Val Asp Ala Gly Asn Phe He Pro Pro Pro Arg Trp Leu Leu Leu 595 600 605 Aep Phe Val Phe Val Leu Leu Tyr Leu Met Lye Leu Ala Glu Ala Arg 610 615 620 Leu Val Pro Leu He Leu Leu Leu Leu Trp Trp Trp Val Aβn Gin Leu 625 630 635 640 Ala Val Leu Xaa Val Xaa Ala Xaa Xaa Ala Ala Val Ala Gly Glu Val 645 650 655 Phe Ala Gly Pro Ala Leu Ser Trp Cye Leu Gly Leu Pro Phe Val Ser 660 665 670 Met He Leu Gly Leu Ala Aen Leu Val Leu Tyr Phe Arg Trp Met Gly 675 680 685 Pro Gin Arg Leu Met Phe Leu Val Leu Trp Lye Leu Ala Arg Gly Ala 690 695 700 Phe Pro Leu Ala Leu Leu Met Gly He Ser Ala Thr Arg Gly Arg Thr 705 710 715 720 Ser Val Leu Gly Ala Glu Phe Cys Phe Asp Val Thr Phe Glu Val Asp 725 730 735 Thr Ser Val Leu Gly Trp Val Val Ala Ser Val Val Ala Trp Ala He 740 745 750 Ala Leu Leu Ser Ser Met Ser Ala Gly Gly Trp Lye His Lys Ala He 755 760 765 He Tyr Arg Thr Trp Cys Lys Gly Tyr Gin Xaa Leu Arg Gin Arg Val 770 775 780 Val Arg Ser Pro Leu Gly Glu Gly Arg Pro Thr Lys Pro Leu Thr He 785 790 795 800 Ala Trp Cys Leu Ala Ser Tyr He Trp Pro Asp Ala Val Met Leu Val 805 810 815 Val Val Ala Met Val Leu Leu Phe Gly Leu Phe Asp Ala Leu Aep Trp 820 825 830 Ala Leu Glu Glu Leu Leu Val Ser Arg Pro Ser Leu Arg Arg Leu Ala 835 840 845 Arg Val Val Glu Cys Cys Val Met Ala Gly Glu Lye Ala Thr Thr Val 850 855 860 Arg Leu Val Ser Lye Met Cyβ Ala Arg Gly Ala Tyr Leu Phe Aep Hiβ 865 870 875 880 476 Met Gly Ser Phe Ser Arg Ala Val Lys Glu Arg Leu Leu Glu Trp Aep 885 890 895 Ala Ala Leu Glu Xaa Leu Ser Phe Thr Arg Thr Aep Cys Arg He He 900 905 910 Arg Aep Ala Ala Arg Thr Leu Ser Cyβ Gly Gin Cye Val Met Gly Leu 915 920 925 Pro Val Val Ala Arg Arg Gly Aep Glu Val Leu He Gly Val Phe Gin 930 935 940 Aep Val Aβn Hiβ Leu Pro Pro Gly Phe Xaa Pro Thr Ala Pro Val Val 945 950 955 960 He Arg Arg Cyβ Gly Lye Gly Phe Leu Gly Val Thr Lye Ala Ala Leu 965 970 975 Thr Gly Arg Asp Pro Aep Leu Hiβ Pro Gly Asn Val Met Val Leu Gly 980 985 990 Thr Ala Thr Ser Arg Ser Met Gly Thr Cys Leu Asn Gly Leu Leu Phe 995 1000 1005 Thr Thr Phe His Gly Ala Ser Ser Arg Thr He Ala Thr Pro Val Gly 1010 1015 1020 Ala Leu Aβn Pro Arg Trp Trp Ser Ala Ser Asp Aep Val Thr Val Tyr 1025 1030 1035 1040 Pro Leu Pro Aep Gly Ala Asn Ser Leu Val Pro Cyβ Ser Cyβ Gin Ala 1045 1050 1055 Glu Ser Cyβ Trp Val Xaa Arg Ser Aep Gly Ala Leu Cye Hie Gly Leu 1060 1065 1070 Ser Lye Gly Aep Lys Val Glu Leu Asp Val Ala Met Glu Val Ala Asp 1075 1080 1085 Phe Arg Gly Ser Ser Gly Ser Pro Val Leu Cys Asp Glu Gly His Ala 1090 1095 1100 Val Gly Met Leu Val Ser Val Leu His Ser Gly Gly Arg Val Thr Ala 1105 1110 1115 1120 Ala Arg Phe Thr Arg Pro Trp Thr Gin Val Pro Thr Asp Ala Lye Thr 1125 1130 1135 Thr Thr Glu Pro Pro Pro Val Pro Ala Lye Gly Val Phe Lye Glu Ala 1140 1145 1150 Pro Leu Phe Met Pro Thr Gly Ala Gly Lye Ser Thr Arg Val Pro Leu 1155 1160 1165 Glu Tyr Gly Aβn Met Gly Hiβ Lye Val Leu He Leu Aen Pro Ser Val 1170 1175 1180 477 Ala Thr Val Arg Ala Met Gly Pro Tyr Met Glu Arg Leu Ala Gly Lys 1185 1190 1195 1200 His Pro Ser He Phe Cys Gly His Asp Thr Thr Ala Phe Thr Arg He 1205 1210 1215 Thr Aep Ser Pro Leu Thr Tyr Ser Thr Tyr Gly Arg Phe Leu Ala Aβn 1220 1225 1230 Pro Arg Gin Met Leu Arg Gly Val Ser Val Val He Cys Asp Glu Cyβ 1235 1240 1245 His Ser His Asp Ser Thr Val Leu Leu Gly He Gly Arg Val Arg Asp 1250 1255 1260 Val Ala Arg Gly Cys Gly Val Gin Leu Val Leu Tyr Ala Thr Ala Thr 1265 1270 1275 1280 Pro Pro Gly Ser Pro Met Thr Gin His Pro Ser He He Glu Thr Lys 1285 1290 1295 Leu Asp Val Gly Glu He Pro Phe Tyr Gly Hiβ Gly He Pro Leu Glu 1300 1305 1310 Arg Met Arg Thr Gly Arg Hie Leu Val Phe Cys His Ser Lys Ala Glu 1315 1320 1325 Cys Glu Arg Leu Ala Gly Gin Phe Ser Ala Arg Gly Val Aβn Ala He 1330 1335 1340 Ala Tyr Tyr Arg Gly Lye Aep Ser Ser He He Lys Asp Gly Asp Leu 1345 1350 1355 1360 Val Val Cyβ Ala Thr Aep Ala Leu Ser Thr Gly Tyr Thr Gly Asn Phe 1365 1370 1375 Asp Ser Val Thr Asp Cys Gly Leu Val Val Glu Glu Val Val Glu Val 1380 1385 1390 Thr Leu Aep Pro Thr He Thr He Ser Leu Arg Thr Val Pro Ala Ser 1395 1400 1405 Ala Glu Leu Ser Met Gin Arg Arg Gly Arg Thr Gly Arg Gly Arg Ser 1410 1415 1420 Gly Arg Tyr Tyr Tyr Ala Gly Val Gly Lye Ala Pro Ala Gly Val Val 1425 1430 1435 1440 Arg Ser Gly Pro Val Trp Ser Ala Val Glu Ala Gly Val Thr Trp Tyr 1445 1450 1455 Gly Met Glu Pro Aep Leu Thr Ala Aβn Leu Leu Arg Leu Tyr Aep Aep 1460 1465 1470 Cyβ Pro Tyr Thr Ala Ala Val Ala Ala Aep He Gly Glu Ala Ala Val 1475 1480 1485 478 Phe Phe Ala Gly Leu Ala Pro Leu Arg Met Hie Pro Aep Val Ser Trp 1490 1495 1500 Ala Lye Val Arg Gly Val Aen Trp Pro Leu Leu Val Gly Val Gin Arg 1505 1510 1515 1520 Thr Met Cyβ Arg Glu Thr Leu Ser Pro Gly Pro Ser Aep Aep Pro Gin 1525 1530 1535 Trp Ala Gly Leu Lye Gly Pro Aen Pro Val Pro Leu Leu Leu Arg Trp 1540 1545 1550 Gly Aβn Aep Leu Pro Ser Lye Val Ala Gly Hie Hie He Val Aep Aep 1555 1560 1565 Leu Val Arg Arg Leu Gly Val Ala Glu Gly Tyr Val Arg Cyβ Aep Ala 1570 1575 1580 Xaa Pro He Leu Met Val Gly Leu Ala He Ala Gly Gly Met He Tyr 1585 1590 1595 1600 Ala Ser Tyr Thr Gly Ser Leu Val Val Val Thr Aep Trp Aep Val Lye 1605 1610 1615 Gly Gly Gly Aβn Pro Leu Tyr Arg Ser Gly Asp Gin Ala Thr Pro Gin 1620 1625 1630 Pro Val Val Gin Val Pro Pro Val Asp His Arg Pro Gly Gly Glu Ser 1635 1640 1645 Ala Pro Arg Asp Ala Lye Thr Val Thr Aep Ala Val Ala Ala He Gin 1650 1655 1660 Val Asn Cys Asp Trp Ser Val Met Thr Leu Ser He Gly Glu Val Leu 1665 1670 1675 1680 Thr Leu Ala Gin Ala Lys Thr Ala Glu Ala Tyr Ala Ala Thr Ser Arg 1685 1690 1695 Trp Leu Ala Gly Cys Tyr Thr Gly Thr Arg Ala Val Pro Thr Val Ser 1700 1705 1710 He Val Asp Lys Leu Phe Ala Gly Gly Trp Ala Ala Val Val Gly His 1715 1720 1725 Cys Hie Ser Val He Ala Ala Ala Val Ala Ala Tyr Gly Ala Ser Arg 1730 1735 1740 Ser Pro Pro Leu Ala Ala Ala Ala Ser Tyr Leu Met Gly Leu Gly Val 1745 1750 1755 1760 Gly Gly Aen Ala Gin Ala Arg Leu Ala Ser Ala Leu Leu Leu Gly Ala 1765 1770 1775 Ala Gly Thr Ala Leu Gly Thr Pro Val Val Gly Leu Thr Met Ala Gly 1780 1785 1790 479 Ala Phe Met Gly Gly Ala Ser Val Ser Pro Ser Leu Val Thr Val Leu 1795 1800 1805 Leu Gly Ala Val Gly Gly Trp Glu Gly Val Val Asn Ala Ala Ser Leu 1810 1815 1820 Val Phe Asp Phe Met Ala Gly Lys Leu Ser Thr Glu Asp Leu Trp Tyr 1825 1830 1835 1840 Ala He Pro Val Leu Thr Ser Pro Xaa Ala Gly Leu Ala Gly He Ala 1845 1850 1855 Leu Gly Leu Val Leu Tyr Ser Ala Asn Asn Ser Gly Thr Thr Thr Trp 1860 1865 1870 Leu Asn Arg Leu Leu Thr Thr Leu Pro Arg Ser Ser Cyβ He Pro Asp 1875 1880 1885 Ser Tyr Phe Gin Gin Ala Aep Tyr Cyβ Asp Lys Val Ser Ala He Val 1890 1895 1900 Arg Arg Leu Ser Leu Thr Arg Thr Val Val Ala Leu Val Asn Arg Glu 1905 1910 1915 1920 Pro Lys Val Aep Glu Val Gin Val Gly Tyr Val Trp Aep Leu Trp Glu 1925 1930 1935 Trp Val Met Arg Gin Val Arg Met Val Met Ser Arg Leu Arg Ala Leu 1940 1945 1950 Cys Pro Val Val Ser Leu Pro Leu Trp Hiβ Cye Gly Glu Gly Trp Ser 1955 1960 1965 Gly Glu Trp Leu Leu Aep Gly His Val Glu Ser Arg Cys Leu Cyβ Gly 1970 1975 1980 Cys Val He Thr Gly Asp Val Leu Asn Gly Gin Leu Lys Asp Pro Val 1985 1990 1995 2000 Tyr Ser Thr Lys Leu Cys Arg His Tyr Trp Met Gly Thr Val Pro Val 2005 2010 2015 Asn Met Leu Gly Tyr Gly Glu Thr Ser Pro Leu Leu Ala Ser Asp Thr 2020 2025 2030 Pro Lys Val Val Pro Phe Gly Thr Ser Gly Trp Ala Glu Val Val Val 2035 2040 2045 Thr Pro Thr His Val Val He Arg Arg Thr Ser Cys Tyr Lys Leu Leu 2050 2055 2060 Arg Gin Gin He Leu Ser Ala Ala Val Ala Glu Pro Tyr Tyr Val Asp 2065 2070 2075 2080 Gly He Pro Val Ser Trp Glu Ala Asp Ala Arg Ala Pro Ala Met Val 2085 2090 2095 480 Tyr Gly Pro Gly Gin Ser Val Thr He Asp Gly Glu Arg Tyr Thr Leu 2100 2105 2110 Pro His Gin Leu Arg Met Arg Asn Val Ala Pro Ser Glu Val Ser Ser 2115 2120 2125 Glu Val Ser He Glu He Gly Thr Glu Thr Glu Asp Ser Glu Leu Thr 2130 2135 2140 Glu Ala Asp Leu Pro Pro Ala Ala Ala Ala Leu Gin Ala He Glu Asn 2145 2150 2155 2160 Ala Ala Arg He Leu Glu Pro His He Asp Val Xaa Met Glu Asp Cyβ 2165 2170 2175 Ser Thr Pro Ser Leu Cyβ Gly Ser Ser Arg Glu Met Pro Val Trp Gly 2180 2185 2190 Glu Aep He Pro Arg Thr Pro Ser Pro Ala Leu He Ser Val Thr Glu 2195 2200 2205 Ser Ser Ser Aep Glu Lye Thr Leu Ser Val Thr Ser Ser Gin Glu Aep 2210 2215 2220 Thr Pro Ser Ser Asp Ser Phe Glu Val He Gin Glu Ser Asp Thr Ala 2225 2230 2235 2240 Glu Ser Glu Glu Ser Val Phe Aen Val Ala Leu Ser Val Leu Lys Ala 2245 2250 2255 Leu Phe Pro Gin Ser Asp Ala Thr Arg Lys Leu Thr Val Lys Met Ser 2260 2265 2270 Cys Cys Val Glu Lye Ser Val Thr Arg Phe Phe Ser Leu Gly Leu Thr 2275 2280. 2285 Val Ala Aep Val Ala Ser Leu Cye Glu Met Glu He Gin Aβn Hie Thr 2290 2295 2300 Ala Tyr Cyβ Aep Lye Val Arg Thr Pro Leu Glu Leu Gin Val Gly Cye 2305 2310 2315 2320 Leu Val Gly Aβn Glu Leu Thr Phe Glu Cyβ Aep Lye Cye Glu Ala Arg 2325 2330 2335 Gin Glu Thr Leu Ala Ser Phe Ser Tyr He Trp Ser Gly Val Pro Leu 2340 2345 2350 Thr Arg Ala Thr Pro Ala Lye Pro Pro Val Val Arg Pro Val Gly Ser 2355 2360 2365 Leu Leu Val Ala Aep Thr Thr Lye Val Tyr Val Thr Aβn Pro Aep Asn 2370 2375 2380 Val Gly Arg Arg Val Aep Lye Val Thr Phe Trp Arg Ala Pro Arg Val 2385 2390 2395 2400 481 His Asp Lye Phe Leu Val Aep Ser He Glu Arg Ala Arg Arg Ala Ala 2405 2410 2415 Gin Gly Cyβ Leu Ser Met Gly Tyr Thr Tyr Glu Glu Ala He Arg Thr 2420 2425 2430 Val Arg Pro Hiβ Ala Ala Met Gly Trp Gly Ser Lye Val Ser Val Lys 2435 2440 2445 Aep Leu Ala Thr Pro Ala Gly Lye Met Ala Val Hie Aep Arg Leu Gin 2450 2455 2460 Glu He Leu Glu Gly Thr Pro Val Pro Phe Thr Leu Thr Val Lye Lys 2465 2470 2475 2480 Glu Val Phe Phe Lys Asp Arg Lye Glu Glu Lye Ala Pro Arg Leu He 2485 2490 2495 Val Phe Pro Pro Leu Aep Phe Arg He Ala Glu Lys Leu He Leu Gly 2500 2505 2510 Aep Pro Gly Arg Val Ala Lys Ala Gly Val Gly Gly Ala Tyr Ala Phe 2515 2520 2525 Gin Tyr Thr Pro Asn Gin Arg Val Lye Glu Met Leu Lye Leu Trp Glu 2530 2535 2540 Ser Lye Lye Thr Pro Cyβ Ala He Cye Val Asp Ala Thr Cys Phe Asp 2545 2550 2555 2560 Ser Ser He Thr Xaa Glu Asp Val Ala Leu Glu Thr Glu Leu Tyr Ala 2565 2570 2575 Leu Ala Ser Asp His Pro Glu Trp Val Arg Ala Leu Gly Lys Tyr Xaa 2580 2585 2590 Ala Ser Gly Thr Met Val Thr Pro Glu Gly Val Pro Val Gly Glu Arg 2595 2600 2605 Tyr Cys Arg Ser Ser Gly Val Leu Thr Thr Ser Ala Ser Asn Cys Leu 2610 2615 2620 Thr Cys Tyr He Lys Val Arg Ala Ala Cys Glu Arg He Gly Leu Lys 2625 2630 2635 2640 Asn Val Ser Leu Leu He Ala Gly Asp Asp Cys Leu He Val Cys Glu 2645 2650 2655 Arg Pro Val Cys Asp Pro Cys Glu Ala Leu Gly Arg Thr Leu Ala Ser 2660 2665 2670 Tyr Gly Tyr Ala Cys Glu Pro Ser Tyr His Ala Ser Leu Aep Thr Ala 2675 2680 2685 Pro Phe Cyβ Ser Thr Trp Leu Ala Glu Cys Asn Ala Asp Gly Xaa Arg 2690 2695 2700 482 His Phe Phe Leu Thr Thr Aep Phe Arg Arg Pro Leu Ala Arg Met Ser 2705 2710 2715 2720 Ser Glu Tyr Ser Aep Pro Met Ala Ser Ala He Gly Tyr He Leu Leu 2725 2730 2735 Tyr Pro Trp Xaa Pro He Thr Arg Trp Val He He Pro Hiβ Val Leu 2740 2745 2750 Thr Cyβ Ala Ser Ser Arg Gly Gly Gly Thr Xaa Ser Aep Pro Val Trp 2755 2760 2765 Cyβ Gin Val Hiβ Gly Aβn Tyr Tyr Lye Phe Pro Leu Aep Lye Leu Pro 2770 2775 2780 Aen He He Val Ala Leu Hiβ Gly Pro Ala Ala Leu Arg Val Thr Ala 2785 2790 2795 2800 Aep Thr Thr Lys Thr Lys Met Glu Ala Gly Lys Val Leu Ser Asp Leu 2805 2810 2815 Lys Leu Pro Gly Leu Ala Val His Arg Lys Lys Ala Gly Ala Leu Arg 2820 2825 2830 Thr Arg Met Leu Arg Ser Arg Gly Trp Ala Glu Leu Ala Arg Gly Leu 2835 2840 2845 Leu Trp His Pro Gly Leu Arg Leu Pro Pro Pro Glu He Ala Gly He 2850 2855 2860 Pro Gly Gly Phe Pro Leu Ser Pro Pro Tyr Met Gly Val Val Hiβ Gin 2865 2870 2875 2880 Leu Aep Phe Thr Xaa Gin Arg Ser Arg Trp Arg Trp Leu Gly Phe Leu 2885 2890 2895 Ala Leu Leu He Val Ala Leu Phe Gly 2900 2905 (2) INFORMATION FOR SEQ ID NO:405: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 11 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:405: Thr Lys Phe He Cys Cys Gly Arg Ser Gin Thr 1 5 10 483 (2) INFORMATION FOR SEQ ID NO: 06: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO.-406: Ala Pro Phe Lys Arg Gly Leu Arg 1 5 (2) INFORMATION FOR SEQ ID NO:407: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9034 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 2..9034 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:407: AAG GTG GTG GAT GGG TGA TGA CAG GGT TGG TAG GTC GTA AAT CCC GGT 48 Lys Val Val Asp Gly * * Gin Gly Trp * Val Val Asn Pro Gly 1 5 10 15 CAT CCT GGT AGC CAC TAT AGG TGG GTC TTA AGG GGA GGC TAC GGT CCC 96 His Pro Gly Ser Hiβ Tyr Arg Trp Val Leu Arg Gly Gly Tyr Gly Pro 20 25 30 TCT TGC GCA TAT GGA GGA AAA GCG CAC GGT CCA CAG GTG TTG GTC CTA 144 Ser Cye Ala Tyr Gly Gly Lye Ala His Gly Pro Gin Val Leu Val Leu 35 40 45 CCG GTG TAA TAA GGA CCC GGC GCT AGG CAC GCC GTT AAA CCG AGC CCG 192 Pro Val * * Gly Pro Gly Ala Arg His Ala Val Lys Pro Ser Pro 50 55 60 TTA CTC CCC TGG GCA AAC GAC GCC CAC GTA CGG TCC ACG TCG CCC TTC 240 Leu Leu Pro Trp Ala Asn Asp Ala His Val Arg Ser Thr Ser Pro Phe 65 70 75 80 484 AAT GTC TCT CTT GAC CAA TAG GCG TAC GGC GAG TTG ACA AGG ACC AGT 288 Asn Val Ser Leu Asp Gin * Ala Tyr Gly Glu Leu Thr Arg Thr Ser 85 90 95 GGG GGC CGG GCG GGA GGG GGA AGG ACC CCC ACC GCT GCC CTT CCC GGG 336 Gly Gly Arg Ala Gly Gly Gly Arg Thr Pro Thr Ala Ala Leu Pro Gly 100 105 110 GAG GCG GGA AAT GCA TGG GGC CAC CCA GCT CCG CGG CGG CCT ACA GCC 384 Glu Ala Gly Asn Ala Trp Gly His Pro Ala Pro Arg Arg Pro Thr Ala 115 120 125 GGG GTA GCC CAA GAA CTT CGG GTG AGG GCG GGT GGC ATT TCT TTT CCT 432 Gly Val Ala Gin Glu Leu Arg Val Arg Ala Gly Gly He Ser Phe Pro 130 135 140 ATA CCG ATC ATG GCA GTC CTT CTG CTC CTA CTC GTG GTG GAG CCG GGG 480 He Pro He Met Ala Val Leu Leu Leu Leu Leu Val Val Glu Pro Gly 145 150 155 160 CTA TTT TAG CCC CGG CCA CCC ATG CTT GTA GCG CGA AAG GGC AAT ATT 528 Leu Phe * Pro Arg Pro Pro Met Leu Val Ala Arg Lye Gly Aen He 165 170 175 TSC TCA CAA ACT GTT GCG CCC TGG AGG ACA TAG GCT TCT GCC TGG AGG 576 Xaa Ser Gin Thr Val Ala Pro Trp Arg Thr * Ala Ser Ala Trp Arg 180 185 190 GCG GAT GCC TGG TGG CTC TGG GGT GCA CCA TTT GCA CCG ACC GCT GCT 624 Ala Asp Ala Trp Trp Leu Trp Gly Ala Pro Phe Ala Pro Thr Ala Ala 195 200 205 GGC CAC TGT ATC AGG CGG GTT TGG CCG TGC GGC CCG GCA AGT CCG CCG 672 Gly His Cys He Arg Arg Val Trp Pro Cys Gly Pro Ala Ser Pro Pro 210 215 220 CCC AGT TGG TGG GGG AAC TCG GTA GTC TCT ACG GGC CCT TGT CGG TCT 720 Pro Ser Trp Trp Gly Asn Ser Val Val Ser Thr Gly Pro Cys Arg Ser 225 230 235 240 CGG CTT ATG TGG CCG GGA TCC TGG GGC TTG GGG AGG TCT ACT CGG GGG 768 Arg Leu Met Trp Pro Gly Ser Trp Gly Leu Gly Arg Ser Thr Arg Gly 245 250 255 TCC TCA CCG TCG GGG TGG CGT TGA CGC GCA GGG TCT ACC CGG TCC CGA 816 Ser Ser Pro Ser Gly Trp Arg * Arg Ala Gly Ser Thr Arg Ser Arg 260 265 270 ACC TGA CGT GTG CAG TAG AGT GTG AGT TGA AGT GGG AAA GTG AGT TTT 864 Thr * Arg Val Gin * Ser Val Ser * Ser Gly Lys Val Ser Phe 275 280 285 GGA GAT GGA CTG AAC AGC TGG CCT CAA ACT ACT GGA TTC TGG AAT ACC 912 Gly Asp Gly Leu Asn Ser Trp Pro Gin Thr Thr Gly Phe Trp Asn Thr 290 295 300 TCT GGA AGG TGC CTT TCG ACT TTT GGC GGG GAG TGA TGA GCC TTA CTC 960 485 Ser Gly Arg Cye Leu Ser Thr Phe Gly Gly Glu * * Ala Leu Leu 305 310 315 320 CTC TCT TGG TGT GCG TGG CGG CCC TCC TCC TGC TGG AGC AGC GTA TTG 1008 Leu Ser Trp Cys Ala Trp Arg Pro Ser Ser Cyβ Trp Ser Ser Val Leu 325 330 335 TCA TGG TCT TCC TCC TGG TCA CTA TGG CGG GCA TGT CGC AAG GCG CGC 1056 Ser Trp Ser Ser Ser Trp Ser Leu Trp Arg Ala Cyβ Arg Lye Ala Arg 340 345 350 CCG CCT CAA GTG TTG GGG TCA CGG CCT TTC GAG GCG GGT TTG ACT TGG 1104 Pro Pro Gin Val Leu Gly Ser Arg Pro Phe Glu Ala Gly Leu Thr Trp 355 360 365 CAG TCT TGT TCT TGC AGG TCG AAC GGG TCC CGC GTG CCG ACA GGG AGA 1152 Gin Ser Cys Ser Cyβ Arg Ser Aβn Gly Ser Arg Val Pro Thr Gly Arg 370 375 380 GGG TTT GGG AAC GTG GGA ACG TCA CAC TTT TGT GTG ACT GCC CCA ACG 1200 Gly Phe Gly Aβn Val Gly Thr Ser Hiβ Phe Cyβ Val Thr Ala Pro Thr 385 390 395 400 GTC CTT GGG TGT GGG TCC CGG CCC TTT GCC AGG CAA TCG GAT GGG GCG 1248 Val Leu Gly Cyβ Gly Ser Arg Pro Phe Ala Arg Gin Ser Aep Gly Ala 405 410 415 ACC CTA TCA CTC ATT GGA GCC ACG GAC AAA ATC AGT GGC CCC TTT CTT 1296 Thr Leu Ser Leu He Gly Ala Thr Aep Lys He Ser Gly Pro Phe Leu 420 425 430 GTC CCC AAT TTG TCT ACG GCG CCG TTT CAG TGA CCT GCG TGT GGG GTT 1344 Val Pro Asn Leu Ser Thr Ala Pro Phe Gin * Pro Ala Cys Gly Val 435 440 445 CTG TGT CTT GGT TTG CTT CCA CTG GGG GTC GCG ACT CCA AGG TTG ATG 1392 Leu Cys Leu Gly Leu Leu Pro Leu Gly Val Ala Thr Pro Arg Leu Met 450 455 460 TGT GGA GTT TGG TTC CAG TTG GCT CTG CCA GCT GCA CCA TAG CCG CAC 1440 Cys Gly Val Trp Phe Gin Leu Ala Leu Pro Ala Ala Pro * Pro His 465 470 475 480 TGG GAT CTT CGG ATC GCG ACA CAG TGG TTG AGC TCT CCG AGT GGG GAA 1488 Trp Asp Leu Arg He Ala Thr Gin Trp Leu Ser Ser Pro Ser Gly Glu 485 490 495 TTC CCT GCG CCA CTT GTA TCC TGG ACA GGC GGC CTG CCT CGT GTG GCA 1536 Phe Pro Ala Pro Leu Val Ser Trp Thr Gly Gly Leu Pro Arg Val Ala 500 505 510 CCT GTG TGA GGG ACT GCT GGC CCG AGA CCG GGT CGG TAC GTT TCC CAT 1584 Pro Val * Gly Thr Ala Gly Pro Arg Pro Gly Arg Tyr Val Ser His 515 520 525 TCC ACA GGT GTG GCG CGG GAC CGA GGC TGA CCA GAG ACC TTG AGG CTG 1632 Ser Thr Gly Val Ala Arg Asp Arg Gly * Pro Glu Thr Leu Arg Leu 486 530 535 540 TGC CCT TCG TCA ATA GGA CAA CTC CCT TCA CCA TAA GGG GGC CCC TGG 1680 Cyβ Pro Ser Ser He Gly Gin Leu Pro Ser Pro * Gly Gly Pro Trp 545 550 555 560 GCA ACC AGG GGC GAG GCA ACC CGG TGC GGT CGC CCT TGG GTT TTG GGT 1728 Ala Thr Arg Gly Glu Ala Thr Arg Cye Gly Arg Pro Trp Val Leu Gly 565 570 575 CCT ACA CCA TGA CCA AGA TCC GAG ACT CCT TAC ACT TGG TGA AAT GTC 1776 Pro Thr Pro * Pro Arg Ser Glu Thr Pro Tyr Thr Trp * Aβn Val 580 585 590 CCA CCC CAG CCA TTG AGC CTC CCA CCG GAA CGT TTG GGT TCT TCC CAG 1824 Pro Pro Gin Pro Leu Ser Leu Pro Pro Glu Arg Leu Gly Ser Ser Gin 595 600 605 GAG TCC CCC CCC TTA ACA ACT GCA TGC TTC TCG GCA CTG AGG TGT CAG 1872 Glu Ser Pro Pro Leu Thr Thr Ala Cyβ Phe Ser Ala Leu Arg Cye Gin 610 615 620 AGG TAT TGG GTG GGG CGG GCC TCA CTG GGG GGT TTT ACG AAC CTC TGG 1920 Arg Tyr Trp Val Gly Arg Ala Ser Leu Gly Gly Phe Thr Aen Leu Trp 625 630 635 640 TGC GGC GGT GTT CAG AGC TGA TGG GTC GGC GGA ATC CGG TCT GCC CGG 1968 Cye Gly Gly Val Gin Ser * Trp Val Gly Gly He Arg Ser Ala Arg 645 650 655 GGT TTG CAT GGC TCT CTT CGG GAC GGC CTG ATG GGT TCA TAC ATG TTC 2016 Gly Leu Hiβ Gly Ser Leu Arg Aep Gly Leu Met Gly Ser Tyr Met Phe 660 665 670 AGG GCC ACT TGC AGG AGG TGG ATG CGG GCA ACT TCA TTC CGC CCC CAC 2064 Arg Ala Thr Cye Arg Arg Trp Met Arg Ala Thr Ser Phe Arg Pro His 675 680 685 GCT GGT TGC TCT TGG ACT TTG TAT TTG TCC TGT TAT ACC TGA TGA AGC 2112 Ala Gly Cys Ser Trp Thr Leu Tyr Leu Ser Cys Tyr Thr * * Ser 690 695 700 TGG CAG AGG CAC GGT TGG TCC CGC TGA TCC TCC TCC TGC TAT GGT GGT 2160 Trp Gin Arg His Gly Trp Ser Arg * Ser Ser Ser Cys Tyr Gly Gly 705 710 715 720 GGG TGA ACC AGT TGG CGG TCC TTG KTG TGS CGG CTG CKC RCG CCG CCG 2208 Gly * Thr Ser Trp Arg Ser Leu Xaa Xaa Arg Leu Xaa Xaa Pro Pro 725 730 735 TGG CTG GAG AGG TGT TTG CGG GCC CTG CCT TGT CCT GGT GTC TGG GCC 2256 Trp Leu Glu Arg Cys Leu Arg Ala Leu Pro Cys Pro Gly Val Trp Ala 740 745 750 TAC CCT TCG TGA GTA TGA TCC TGG GGC TAG CAA ACC TGG TGT TGT ACT 2304 Tyr Pro Ser * Val * Ser Trp Gly * Gin Thr Trp Cye Cye Thr 755 760 765 487 TCC GCT GGA TGG GTC CTC AAC GCC TGA TGT TCC TCG TGT TGT GGA AGC 2352 Ser Ala Gly Trp Val Leu Aen Ala * Cyβ Ser Ser Cys Cys Gly Ser 770 775 780 TCG CTC GGG GGG CTT TCC CGC TGG CAT TAC TGA TGG GGA TTT CCG CCA 2400 Ser Leu Gly Gly Leu Ser Arg Trp Hiβ Tyr * Trp Gly Phe Pro Pro 785 790 795 800 CTC GCG GCC GCA CCT CTG TGC TTG GCG CCG AAT TCT GCT TTG ATG TCA 2448 Leu Ala Ala Ala Pro Leu Cyβ Leu Ala Pro Asn Ser Ala Leu Met Ser 805 810 815 CCT TTG AAG TGG ACA CGT CAG TCT TGG GTT GGG TGG TTG CTA GTG TGG 2496 Pro Leu Lys Trp Thr Arg Gin Ser Trp Val Gly Trp Leu Leu Val Trp 820 825 830 TGG CTT GGG CCA TAG CGC TCC TGA GCT CTA TGA GCG CGG GGG GGT GGA 2544 Trp Leu Gly Pro * Arg Ser * Ala Leu * Ala Arg Gly Gly Gly 835 840 845 AGC ACA AAG CCA TAA TCT ATA GGA CGT GGT GTA AAG GGT ACC AGG CYC 2592 Ser Thr Lys Pro * Ser He Gly Arg Gly Val Lys Gly Thr Arg Xaa 850 855 860 TTC GCC AGC GCG TGG TGC GTA GCC CCC TCG GGG AGG GGC GGC CCA CCA 2640 Phe Ala Ser Ala Trp Cys Val Ala Pro Ser Gly Arg Gly Gly Pro Pro 865 870 875 880 AGC CGC TGA CGA TAG CCT GGT GTC TGG CCT CTT ACA TCT GGC CGG ACG 2688 Ser Arg * Arg * Pro Gly Val Trp Pro Leu Thr Ser Gly Arg Thr 885 890 895 CTG TGA TGT TGG TGG TTG TGG CCA TGG TCC TCC TCT TCG GCC TTT TCG 2736 Leu * Cys Trp Trp Leu Trp Pro Trp Ser Ser Ser Ser Ala Phe Ser 900 905 910 ACG CGC TCG ATT GGG CCT TGG AGG AGC TCC TTG TGT CGC GGC CTT CGT 2784 Thr Arg Ser He Gly Pro Trp Arg Ser Ser Leu Cye Arg Gly Leu Arg 915 920 925 TGC GTC GTT TGG CAA GGG TGG TGG AGT GTT GTG TGA TGG CGG GCG AGA 2832 Cyβ Val Val Trp Gin Gly Trp Trp Ser Val Val * Trp Arg Ala Arg 930 935 940 AGG CCA CTA CCG TCC GGC TTG TGT CCA AGA TGT GCG CGA GAG GGG CCT 2880 Arg Pro Leu Pro Ser Gly Leu Cys Pro Arg Cyβ Ala Arg Glu Gly Pro 945 950 955 960 ACC TGT TTG ACC ACA TGG GGT CGT TCT CGC GCG CGG TCA AGG AGC GCT 2928 Thr Cyβ Leu Thr Thr Trp Gly Arg Ser Arg Ala Arg Ser Arg Ser Ala 965 970 975 TGC TGG AGT GGG ACG CGG CTT TGG AGM CCC TGT CAT TCA CTA GGA CGG 2976 Cyβ Trp Ser Gly Thr Arg Leu Trp Xaa Pro Cyβ Hie Ser Leu Gly Arg 980 985 990 ACT GTC GCA TCA TAC GAG ACG CCG CCA GGA CCC TGA GCT GCG GCC AAT 3024 488 Thr Val Ala Ser Tyr Glu Thr Pro Pro Gly Pro * Ala Ala Ala Aβn 995 1000 1005 GCG TCA TGG GCT TGC CCG TGG TGG CTA GGC GCG GCG ATG AGG TCC TGA 3072 Ala Ser Trp Ala Cyβ Pro Trp Trp Leu Gly Ala Ala Met Arg Ser * 1010 1015 1020 TTG GGG TCT TTC AGG ATG TGA ACC ACT TGC CTC CGG GGT TTG YTC CTA 3120 Leu Gly Ser Phe Arg Met * Thr Thr Cyβ Leu Arg Gly Leu Xaa Leu 1025 1030 1035 1040 CAG CGC CTG TTG TCA TCC GTC GGT GCG GAA AGG GCT TCC TCG GGG TCA 3168 Gin Arg Leu Leu Ser Ser Val Gly Ala Glu Arg Ala Ser Ser Gly Ser 1045 1050 1055 CTA AGG CTG CCT TGA CTG GTC GGG ATC CTG ACT TAC ACC CAG GAA ACG 3216 Leu Arg Leu Pro * Leu Val Gly He Leu Thr Tyr Thr Gin Glu Thr 1060 1065 1070 TCA TGG TTT TGG GGA CGG CTA CCT CGC GCA GCA TGG GAA CGT GCT TAA 3264 Ser Trp Phe Trp Gly Arg Leu Pro Arg Ala Ala Trp Glu Arg Ala * 1075 1080 1085 ACG GGT TGC TGT TCA CGA CAT TCC ATG GGG CTT CTT CCC GAA CCA TTG 3312 Thr Gly Cyβ Cye Ser Arg Hie Ser Met Gly Leu Leu Pro Glu Pro Leu 1090 1095 1100 CGA CAC CTG TGG GGG CCC TTA ACC CAA GGT GGT GGT CGG CCA GTG ATG 3360 Arg Hiβ Leu Trp Gly Pro Leu Thr Gin Gly Gly Gly Arg Pro Val Met 1105 1110 1115 1120 ACG TCA CGG TCT ATC CCC TCC CCG ATG GAG CTA ACT CGT TGG TTC CCT 3408 Thr Ser Arg Ser He Pro Ser Pro Met Glu Leu Thr Arg Trp Phe Pro 1125 1130 1135 GCT CGT GTC AGG CTG AGT CCT GTT GGG TCA TYC GAT CCG ATG GGG CTC 3456 Ala Arg Val Arg Leu Ser Pro Val Gly Ser Xaa Aep Pro Met Gly Leu 1140 1145 1150 TTT GCC ATG GCT TGA GCA AGG GGG ACA AGG TAG AAC TGG ACG TGG CCA 3504 Phe Ala Met Ala * Ala Arg Gly Thr Arg * Aβn Trp Thr Trp Pro 1155 1160 1165 TGG AGG TTG CTG ACT TTC GTG GGT CGT CTG GGT CTC CTG TCC TAT GCG 3552 Trp Arg Leu Leu Thr Phe Val Gly Arg Leu Gly Leu Leu Ser Tyr Ala 1170 1175 1180 ACG AGG GGC ACG CTG TAG GAA TGC TCG TGT CCG TCC TTC ATT CGG GGG 3600 Thr Arg Gly Thr Leu * Glu Cyβ Ser Cye Pro Ser Phe He Arg Gly 1185 1190 1195 1200 GGA GGG TGA CCG CGG CTC GAT TCA CTC GGC CGT GGA CCC AAG TCC CAA 3648 Gly Gly * Pro Arg Leu Aep Ser Leu Gly Arg Gly Pro Lys Ser Gin 1205 1210 1215 CAG ACG CCA AGA CTA CCA CTG AGC CAC CCC CGG TGC CAG CTA AAG GGG 3696 Gin Thr Pro Arg Leu Pro Leu Ser His Pro Arg Cys Gin Leu Lys Gly 489 1220 1225 1230 TTT TCA AAG AGG CTC CTC TTT TCA TGC CAA CAG GGG CGG GGA AAA GCA 3744 Phe Ser Lye Arg Leu Leu Phe Ser Cyβ Gin Gin Gly Arg Gly Lye Ala 1235 1240 1245 CAC GCG TCC CTT TGG AGT ATG GAA ACA TGG GGC ACA AGG TCC TGA TTC 3792 Hie Ala Ser Leu Trp Ser Met Glu. Thr Trp Gly Thr Arg Ser * Phe 1250 1255 1260 TCA ACC CGT CGG TTG CCA CTG TGA GGG CCA TGG GCC CTT ACA TGG AGA 3840 Ser Thr Arg Arg Leu Pro Leu * Gly Pro Trp Ala Leu Thr Trp Arg 1265 1270 1275 1280 GGC TGG CGG GGA AAC ATC CTA GCA TTT TCT GTG GAC ACG ACA CAA CAG 3888 Gly Trp Arg Gly Asn He Leu Ala Phe Ser Val Asp Thr Thr Gin Gin 1285 1290 1295 CTT TCA CAC GGA TCA CGG ACT CTC CAT TGA CGT ACT CTA CCT ATG GGA 3936 Leu Ser His Gly Ser Arg Thr Leu His * Arg Thr Leu Pro Met Gly 1300 1305 1310 GGT TTC TGG CCA ACC CGA GGC AGA TGC TGA GGG GAG TTT CCG TGG TCA 3984 Gly Phe Trp Pro Thr Arg Gly Arg Cys * Gly Glu Phe Pro Trp Ser 1315 1320 1325 TCT GTG ATG AGT GCC ACA GTC ATG ACT CAA CTG TGT TGC TGG GTA TAG 4032 Ser Val Met Ser Ala Thr Val Met Thr Gin Leu Cys Cys Trp Val * 1330 1335 1340 GCA GGG TCA GGG ACG TGG CGC GGG GGT GTG GAG TGC AAT TAG TGC TCT 4080 Ala Gly Ser Gly Thr Trp Arg Gly Gly Val Glu Cys Asn * Cys Ser 1345 1350 1355 1360 ACG CTA CTG CGA CTC CCC CGG GCT CGC CTA TGA CTC AGC ATC CAT CCA 4128 Thr Leu Leu Arg Leu Pro Arg Ala Arg Leu * Leu Ser He His Pro 1365 1370 1375 TAA TTG AGA CAA AGC TGG ACG TTG GTG AGA TCC CCT TTT ATG GGC ATG 4176 * Leu Arg Gin Ser Trp Thr Leu Val Arg Ser Pro Phe Met Gly Met 1380 1385 1390 GTA TCC CCC TCG AGC GTA TGA GGA CTG GTC GCC ACC TTG TAT TCT GCC 4224 Val Ser Pro Ser Ser Val * Gly Leu Val Ala Thr Leu Tyr Ser Ala 1395 1400 1405 ATT CCA AGG CGG AGT GCG AGA GAT TGG CCG GCC AGT TCT CCG CGC GGG 4272 He Pro Arg Arg Ser Ala Arg Aep Trp Pro Ala Ser Ser Pro Arg Gly 1410 1415 1420 GGG TTA ATG CCA TCG CCT ATT ATA GGG GTA AGG ACA GTT CCA TCA TCA 4320 Gly Leu Met Pro Ser Pro He He Gly Val Arg Thr Val Pro Ser Ser 1425 1430 1435 1440 AAG ACG GAG ACC TGG TGG TTT GTG CGA CAG ACG CGC TCT CTA CCG GGT 4368 Lye Thr Glu Thr Trp Trp Phe Val Arg Gin Thr Arg Ser Leu Pro Gly 1445 1450 1455 490 ACA CAG GAA ACT TCG ATT CTG TCA CCG ACT GTG GGT TGG TGG TGG AGG 4416 Thr Gin Glu Thr Ser He Leu Ser Pro Thr Val Gly Trp Trp Trp Arg 1460 1465 1470 AGG TCG TTG AGG TGA CCC TTG ATC CCA CCA TTA CCA TTT CCT TGC GGA 4464 Arg Ser Leu Arg * Pro Leu He Pro Pro Leu Pro Phe Pro Cye Gly 1475 1480 1485 CTG TCC CTG CTT CGG CTG AAT TGT CGA TGC AGC GGC GCG GAC GCA CGG 4512 Leu Ser Leu Leu Arg Leu Aβn Cye Arg Cye Ser Gly Ala Aep Ala Arg 1490 1495 1500 GGA GAG GTC GGT CGG GCC GCT ACT ACT ACG CTG GGG TCG GTA AGG CTC 4560 Gly Glu Val Gly Arg Ala Ala Thr Thr Thr Leu Gly Ser Val Arg Leu 1505 1510 1515 1520 CCG CGG GGG TGG TGC GGT CTG GTC CGG TCT GGT CGG CAG TGG AAG CTG 4608 Pro Arg Gly Trp Cyβ Gly Leu Val Arg Ser Gly Arg Gin Trp Lye Leu 1525 1530 1535 GAG TGA CCT GGT ATG GAA TGG AAC CTG ACT TGA CAG CAA ACC TTC TGA 4656 Glu * Pro Gly Met Glu Trp Aβn Leu Thr * Gin Gin Thr Phe * 1540 1545 1550 GAC TTT ACG ACG ACT GCC CTT ACA CCG CAG CCG TCG CAG CTG ACA TTG 4704 Aep Phe Thr Thr Thr Ala Leu Thr Pro Gin Pro Ser Gin Leu Thr Leu 1555 1560 1565 GTG AAG CCG CGG TGT TCT TTG CGG GCC TCG CGC CCC TCA GGA TGC ATC 4752 Val Lye Pro Arg Cye Ser Leu Arg Ala Ser Arg Pro Ser Gly Cyβ He 1570 1575 1580 CCG ATG TTA GCT GGG CAA AAG TTC GCG GCG TCA ATT GGC CCC TCC TGG 4800 Pro Met Leu Ala Gly Gin Lye Phe Ala Ala Ser He Gly Pro Ser Trp 1585 1590 1595 1600 TGG GTG TTC AGC GGA CGA TGT GTC GGG AAA CAC TGT CTC CCG GCC CGT 4848 Trp Val Phe Ser Gly Arg Cye Val Gly Lye Hiβ Cys Leu Pro Ala Arg 1605 1610 1615 CGG ACG ACC CTC AGT GGG CAG GTC TGA AAG GCC CGA ATC CTG TCC CAC 4896 Arg Thr Thr Leu Ser Gly Gin Val * Lys Ala Arg He Leu Ser His 1620 1625 1630 TAC TGC TGA GGT GGG GCA ATG ATT TGC CAT CAA AAG TGG CCG GCC ACC 4944 Tyr Cys * Gly Gly Ala Met He Cys His Gin Lys Trp Pro Ala Thr 1635 1640 1645 ACA TAG TTG ACG ATC TGG TCC GTC GGC TCG GTG TGG CGG AGG GAT ACG 4992 Thr * Leu Thr He Trp Ser Val Gly Ser Val Trp Arg Arg Asp Thr 1650 1655 1660 TGC GCT GTG ATG CTG GRC CCA TCC TCA TGG TGG GCT TGG CCA TAG CGG 5040 Cys Ala Val Met Leu Xaa Pro Ser Ser Trp Trp Ala Trp Pro * Arg 1665 1670 1675 1680 GCG GCA TGA TCT ACG CCT CTT ACA CTG GGT CGC TAG TGG TGG TAA CAG 5088 491 Ala Ala * Ser Thr Pro Leu Thr Leu Gly Arg * Trp Trp * Gin 1685 1690 1695 ACT GGG ATG TGA AGG GAG GTG GCA ATC CCC TTT ATA GGA GTG GTG ACC 5136 Thr Gly Met * Arg Glu Val Ala He Pro Phe He Gly Val Val Thr 1700 1705 1710 AGG CCA CCC CTC AAC CCG TGG TGC AGG TCC CCC CGG TAG ACC ATC GGC 5184 Arg Pro Pro Leu Asn Pro Trp Cyβ Arg Ser Pro Arg * Thr He Gly 1715 1720 1725 CGG GGG GGG AGT CTG CGC CAC GGG ATG CCA AGA CAG TGA CAG ATG CGG 5232 Arg Gly Gly Ser Leu Arg Hiβ Gly Met Pro Arg Gin * Gin Met Arg 1730 1735 1740 TGG CAG CCA TCC AGG TGA ACT GCG ATT GGT CTG TGA TGA CCC TGT CGA 5280 Trp Gin Pro Ser Arg * Thr Ala He Gly Leu * * Pro Cys Arg 1745 1750 1755 1760 TCG GGG AAG TCC TCA CCT TGG CTC AGG CTA AGA CAG CCG AGG CCT ACG 5328 Ser Gly Lys Ser Ser Pro Trp Leu Arg Leu Arg Gin Pro Arg Pro Thr 1765 1770 1775 CAG CTA CTT CCA GGT GGC TCG CTG GCT GCT ACA CGG GGA CGC GGG CCG 5376 Gin Leu Leu Pro Gly Gly Ser Leu Ala Ala Thr Arg Gly Arg Gly Pro 1780 1785 1790 TCC CCA CTG TAT CAA TTG TTG ACA AGC TCT TCG CCG GGG GTT GGG CCG 5424 Ser Pro Leu Tyr Gin Leu Leu Thr Ser Ser Ser Pro Gly Val Gly Pro 1795 1800 1805 CCG TGG TGG GTC ACT GTC ACA GCG TCA TTG CTG CGG CGG TGG CTG CCT 5472 Pro Trp Trp Val Thr Val Thr Ala Ser Leu Leu Arg Arg Trp Leu Pro 1810 1815 1820 ATG GAG CTT CTC GAA GTC CTC CAC TGG CCG CGG CGG CGT CCT ACC TCA 5520 Met Glu Leu Leu Glu Val Leu His Trp Pro Arg Arg Arg Pro Thr Ser 1825 1830 1835 1840 TGG GGT TGG GCG TCG GAG GCA ACG CAC AGG CGC GCT TGG CTT CAG CTC 5568 Trp Gly Trp Ala Ser Glu Ala Thr His Arg Arg Ala Trp Leu Gin Leu 1845 1850 1855 TTC TAC TGG GGG CTG CTG GTA CGG CTC TGG GGA CCC CTG TCG TGG GAC 5616 Phe Tyr Trp Gly Leu Leu Val Arg Leu Trp Gly Pro Leu Ser Trp Asp 1860 1865 1870 TCA CCA TGG CGG GGG CCT TCA TGG GCG GTG CCA GCG TGT CCC CCT CCC 5664 Ser Pro Trp Arg Gly Pro Ser Trp Ala Val Pro Ala Cys Pro Pro Pro 1875 1880 1885 TCG TCA CTG TCC TAC TTG GGG CTG TGG GAG GTT GGG AGG GCG TTG TCA 5712 Ser Ser Leu Ser Tyr Leu Gly Leu Trp Glu Val Gly Arg Ala Leu Ser 1890 1895 1900 ACG CTG CCA GTC TCG TCT TCG ACT TCA TGG CTG GGA AAC TTT CAA CAG 5760 Thr Leu Pro Val Ser Ser Ser Thr Ser Trp Leu Gly Asn Phe Gin Gin 492 1905 1910 1915 1920 AAG ACC TTT GGT ATG CCA TCC CGG TAC TCA CTA GTC CTG GRG CGG GCC 5808 Lys Thr Phe Gly Met Pro Ser Arg Tyr Ser Leu Val Leu Xaa Arg Ala 1925 1930 1935 TCG CGG GGA TTG CCC TTG GTC TGG TTT TGT ACT CAG CAA ACA ACT CTG 5856 Ser Arg Gly Leu Pro Leu Val Trp Phe Cyβ Thr Gin Gin Thr Thr Leu 1940 1945 1950 GCA CTA CCA CAT GGC TGA ACC GTC TGC TGA CGA CGT TGC CAC GGT CAT 5904 Ala Leu Pro His Gly * Thr Val Cyβ * Arg Arg Cye Hiβ Gly Hiβ 1955 1960 1965 CTT GCA TAC CCG ACA GCT ACT TCC AAC AGG CTG ACT ACT GCG ACA AGG 5952 Leu Ala Tyr Pro Thr Ala Thr Ser Aβn Arg Leu Thr Thr Ala Thr Arg 1970 1975 1980 TCT CGG CAA TCG TGC GCC GCC TGA GCC TTA CTC GCA CCG TGG TGG CCC 6000 Ser Arg Gin Ser Cye Ala Ala * Ala Leu Leu Ala Pro Trp Trp Pro 1985 1990 1995 2000 TGG TCA ACA GGG AGC CTA AGG TGG ATG AGG TCC AGG TGG GGT ACG TCT 6048 Trp Ser Thr Gly Ser Leu Arg Trp Met Arg Ser Arg Trp Gly Thr Ser 2005 2010 2015 GGG ATC TGT GGG AGT GGG TGA TGC GCC AGG TGC GCA TGG TGA TGT CTA 6096 Gly He Cyβ Gly Ser Gly * Cyβ Ala Arg Cyβ Ala Trp * Cye Leu 2020 2025 2030 GAC TCC GGG CCC TCT GCC CTG TGG TGT CAC TCC CCT TGT GGC ACT GCG 6144 Aep Ser Gly Pro Ser Ala Leu Trp Cys Hiβ Ser Pro Cye Gly Thr Ala 2035 2040 2045 GGG AGG GGT GGT CCG GTG AAT GGC TTC TCG ATG GGC ACG TGG AGA GTC 6192 Gly Arg Gly Gly Pro Val Asn Gly Phe Ser Met Gly Thr Trp Arg Val 2050 2055 2060 GTT GTC TGT GCG GGT GTG TAA TCA CCG GCG ACG TCC TCA ATG GGC AAC 6240 Val Val Cys Ala Gly Val * Ser Pro Ala Thr Ser Ser Met Gly Asn 2065 2070 2075 2080 TCA AAG ATC CAG TTT ACT CTA CCA AGC TGT GCA GGC ACT ACT GGA TGG 6288 Ser Lys He Gin Phe Thr Leu Pro Ser Cye Ala Gly Thr Thr Gly Trp 2085 2090 2095 GAA CTG TGC CGG TCA ACA TGC TGG GCT ACG GGG AAA CCT CAC CTC TTC 6336 Glu Leu Cyβ Arg Ser Thr Cyβ Trp Ala Thr Gly Lys Pro His Leu Phe 2100 2105 2110 TCG CCT CTG ACA CCC CGA AGG TGG TAC CCT TCG GGA CGT CGG GGT GGG 6384 Ser Pro Leu Thr Pro Arg Arg Trp Tyr Pro Ser Gly Arg Arg Gly Gly 2115 2120 2125 CTG AGG TGG TGG TGA CCC CTA CCC ACG TGG TGA TCA GGC GCA CGT CCT 6432 Leu Arg Trp Trp * Pro Leu Pro Thr Trp * Ser Gly Ala Arg Pro 2130 2135 2140 493 GTT ACA AAC TGC TTC GCC AGC AAA TTC TTT CAG CAG CTG TAG CTG AGC 6480 Val Thr Aen Cye Phe Ala Ser Lye Phe Phe Gin Gin Leu * Leu Ser 2145 2150 2155 2160 CCT ACT ACG TTG ATG GCA TTC CGG TCT CTT GGG AGG CTG ACG CGA GAG 6528 Pro Thr Thr Leu Met Ala Phe Arg Ser Leu Gly Arg Leu Thr Arg Glu 2165 2170 2175 CGC CGG CCA TGG TCT ACG GTC CGG GCC AAA GTG TTA CCA TTG ATG GGG 6576 Arg Arg Pro Trp Ser Thr Val Arg Ala Lye Val Leu Pro Leu Met Gly 2180 2185 2190 AGC GCT ACA CCC TTC CGC ACC AGT TGC GGA TGC GGA ATG TGG CGC CCT 6624 Ser Ala Thr Pro Phe Arg Thr Ser Cys Gly Cys Gly Met Trp Arg Pro 2195 2200 2205 CTG AGG TTT CAT CTG AGG TCA GCA TCG AGA TCG GGA CGG AGA CTG AAG 6672 Leu Arg Phe His Leu Arg Ser Ala Ser Arg Ser Gly Arg Arg Leu Lys 2210 2215 2220 ACT CAG AAC TGA CTG AGG CCG ATT TGC CAC CAG CGG CTG CTG CCC TCC 6720 Thr Gin Asn * Leu Arg Pro He Cys His Gin Arg Leu Leu Pro Ser 2225 2230 2235 2240 AAG CGA TAG AGA ATG CTG CGA GAA TTC TCG AAC CGC ACA TCG ATG TCA 6768 Lys Arg * Arg Met Leu Arg Glu Phe Ser Asn Arg Thr Ser Met Ser 2245 2250 2255 YCA TGG AGG ATT GCA GTA CAC CCT CTC TCT GTG GTA GTA GCC GAG AGA 6816 Xaa Trp Arg He Ala Val His Pro Leu Ser Val Val Val Ala Glu Arg 2260 2265 2270 TGC CTG TGT GGG GAG AAG ACA TAC CCC GCA CTC CAT CGC CTG CAC TTA 6864 Cys Leu Cys Gly Glu Lys Thr Tyr Pro Ala Leu His Arg Leu His Leu 2275 2280 2285 TCT CGG TTA CGG AGA GCA GCT CAG ATG AGA AGA CCC TGT CGG TGA CCT 6912 Ser Arg Leu Arg Arg Ala Ala Gin Met Arg Arg Pro Cyβ Arg * Pro 2290 2295 2300 CCT CGC AGG AGG ACA CCC CGT CCT CAG ACT CAT TTG AAG TCA TCC AAG 6960 Pro Arg Arg Arg Thr Pro Arg Pro Gin Thr Hie Leu Lye Ser Ser Lys 2305 2310 2315 2320 AGT CTG ATA CTG CTG AAT CAG AGG AAA GCG TCT TCA ACG TGG CTC TTT 7008 Ser Leu He Leu Leu Asn Gin Arg Lys Ala Ser Ser Thr Trp Leu Phe 2325 2330 2335 CCG TAC TAA AAG CCT TAT TTC CAC AGA GCG ATG CCA CAC GAA AGC TAA 7056 Pro Tyr * Lys Pro Tyr Phe Hiβ Arg Ala Met Pro Hie Glu Ser * 2340 2345 2350 CGG TTA AGA TGT CTT GCT GTG TTG AGA AGA GCG TAA CAC GCT TCT TTT 7104 Arg Leu Arg Cyβ Leu Ala Val Leu Arg Arg Ala * His Ala Ser Phe 2355 2360 2365 CTT TAG GGT TGA CCG TGG CTG ACG TGG CTA GCC TGT GTG AGA TGG AGA 7152 494 Leu * Gly * Pro Trp Leu Thr Trp Leu Ala Cys Val Arg Trp Arg 2370 2375 2380 TCC AGA ACC ATA CAG CCT ATT GTG ACA AGG TGC GCA CTC CGC TCG AAT 7200 Ser Arg Thr He Gin Pro He Val Thr Arg Cys Ala Leu Arg Ser Asn 2385 2390 2395 2400 TGC AAG TTG GGT GCT TGG TGG GCA ATG AAC TTA CCT TTG AAT GTG ACA 7248 Cys Lys Leu Gly Ala Trp Trp Ala Met Asn Leu Pro Leu Asn Val Thr 2405 2410 2415 AGT GTG AGG CAC GCC AAG AGA CCC TTG CCT CCT TCT CCT ACA TAT GGT 7296 Ser Val Arg His Ala Lys Arg Pro Leu Pro Pro Ser Pro Thr Tyr Gly 2420 2425 2430 CCG GGG TCC CAC TTA CTC GGG CCA CTC CGG CCA AAC CAC CAG TGG TGA 7344 Pro Gly Ser His Leu Leu Gly Pro Leu Arg Pro Asn His Gin Trp * 2435 2440 2445 GGC CGG TGG GGT CCT TGT TGG TGG CAG ACA CCA CCA AGG TCT ACG TGA 7392 Gly Arg Trp Gly Pro Cys Trp Trp Gin Thr Pro Pro Arg Ser Thr * 2450 2455 2460 CCA ATC CGG ACA ATG TTG GGA GGA GGG TTG ACA AGG TGA CTT TCT GGC 7440 Pro He Arg Thr Met Leu Gly Gly Gly Leu Thr Arg * Leu Ser Gly 2465 2470 2475 2480 GCG CTC CTC GGG TAC ACG ACA AGT TCC TCG TGG ACT CGA TCG AGC GCG 7488 Ala Leu Leu Gly Tyr Thr Thr Ser Ser Ser Trp Thr Arg Ser Ser Ala 2485 2490 2495 CTC GGA GAG CTG CTC AAG GCT GCC TAA GCA TGG GTT ACA CTT ATG AGG 7536 Leu Gly Glu Leu Leu Lys Ala Ala * Ala Trp Val Thr Leu Met Arg 2500 2505 2510 AGG CAA TAA GGA CTG TTA GGC CGC ATG CTG CCA TGG GCT GGG GAT CTA 7584 Arg Gin * Gly Leu Leu Gly Arg Met Leu Pro Trp Ala Gly Asp Leu 2515 2520 2525 AGG TGT CGG TCA AGG ACT TGG CCA CCC CTG CGG GGA AGA TGG CTG TTC 7632 Arg Cys Arg Ser Arg Thr Trp Pro Pro Leu Arg Gly Arg Trp Leu Phe 2530 2535 2540 ATG ACC GGC TTC AGG AGA TAC TTG AAG GGA CTC CGG TCC CTT TTA CCC 7680 Met Thr Gly Phe Arg Arg Tyr Leu Lys Gly Leu Arg Ser Leu Leu Pro 2545 2550 2555 2560 TGA CTG TCA AAA AGG AGG TGT TCT TCA AAG ATC GTA AGG AGG AGA AGG 7728 * Leu Ser Lys Arg Arg Cys Ser Ser Lys He Val Arg Arg Arg Arg 2565 2570 2575 CCC CCC GCC TCA TTG TGT TCC CCC CCC TGG ACT TCC GGA TAG CTG AAA 7776 Pro Pro Ala Ser Leu Cys Ser Pro Pro Trp Thr Ser Gly * Leu Lys 2580 2585 2590 AGC TCA TTC TGG GAG ACC CGG GGC GGG TTG CAA AGG CCG GTG TTG GGG 7824 Ser Ser Phe Trp Glu Thr Arg Gly Gly Leu Gin Arg Pro Val Leu Gly 495 2595 2600 2605 GGG CTT ACG CCT TCC AGT ACA CCC CCA ACC AGC GGG TTA AGG AGA TGC 7872 Gly Leu Thr Pro Ser Ser Thr Pro Pro Thr Ser Gly Leu Arg Arg Cys 2610 2615 2620 TAA AGC TGT GGG AAT CAA AGA AGA CCC CGT GCG CCA TCT GTG TGG ATG 7920 * Ser Cyβ Gly Aβn Gin Arg Arg. Pro Arg Ala Pro Ser Val Trp Met 2625 2630 2635 2640 CCA CTT GCT TCG ACA GTA GCA TTA CTG ARG AGG ACG TGG CAC TAG AGA 7968 Pro Leu Ala Ser Thr Val Ala Leu Leu Xaa Arg Thr Trp Hiβ * Arg 2645 2650 2655 CAG AGC TTT ACG CCC TGG CCT CGG ACC ATC CAG AAT GGG TGC GCG CCC 8016 Gin Ser Phe Thr Pro Trp Pro Arg Thr He Gin Asn Gly Cys Ala Pro 2660 2665 2670 TGG GGA AAT ACT RTG CCT CTG GCA CAA TGG TGA CCC CGG AAG GGG TGC 8064 Trp Gly Asn Thr Xaa Pro Leu Ala Gin Trp * Pro Arg Lys Gly Cys 2675 2680 2685 CAG TGG GCG AGA GGT ATT GTA GGT CCT CGG GTG TGT TGA CCA CAA GTG 8112 Gin Trp Ala Arg Gly He Val Gly Pro Arg Val Cys * Pro Gin Val 2690 2695 2700 CTA GCA ACT GTT TGA CCT GCT ACA TCA AAG TGA GAG CCG CCT GTG AGA 8160 Leu Ala Thr Val * Pro Ala Thr Ser Lys * Glu Pro Pro Val Arg 2705 2710 2715 2720 GGA TCG GAC TGA AAA ATG TCT CGC TTC TCA TCG CGG GCG ATG ACT GCT 8208 Gly Ser Asp * Lye Met Ser Arg Phe Ser Ser Arg Ala Met Thr Ala 2725 2730 2735 TAA TTG TGT GCG AGA GGC CTG TAT GCG ACC CTT GCG AGG CCC TGG GCC 8256 * Leu Cye Ala Arg Gly Leu Tyr Ala Thr Leu Ala Arg Pro Trp Ala 2740 2745 2750 GAA CCC TGG CTT CGT ACG GGT ACG CGT GTG AGC CCT CGT ATC ACG CTT 8304 Glu Pro Trp Leu Arg Thr Gly Thr Arg Val Ser Pro Arg He Thr Leu 2755 2760 2765 CAC TGG ACA CAG CCC CCT TCT GCT CCA CTT GGC TCG CTG AGT GCA ATG 8352 Hiβ Trp Thr Gin Pro Pro Ser Ala Pro Leu Gly Ser Leu Ser Ala Met 2770 2775 2780 CGG ATG GGR AAA GGC ATT TCT TCC TGA CCA CGG ACT TTC GGA GAC CAC 8400 Arg Met Xaa Lye Gly He Ser Ser * Pro Arg Thr Phe Gly Asp Hiβ 2785 2790 2795 2800 TCG CTC GCA TGT CGA GCG AGT ACA GTG ACC CTA TGG CTT CGG CCA TTG 8448 Ser Leu Ala Cye Arg Ala Ser Thr Val Thr Leu Trp Leu Arg Pro Leu 2805 2810 2815 GTT ACA TTC TCC TCT ACC CCT GGC RTC CCA TCA CAC GGT GGG TCA TCA 8496 Val Thr Phe Ser Ser Thr Pro Gly Xaa Pro Ser Hie Gly Gly Ser Ser 2820 2825 2830 496 TCC CGC ATG TGC TAA CAT GCG CTT CTT CCC GGG GTG GTG GCA CAC SGT 8544 Ser Arg Met Cye * Hiβ Ala Leu Leu Pro Gly Val Val Ala Hiβ Xaa 2835 2840 2845 CTG ATC CGG TTT GGT GTC AGG TTC ATG GTA ACT ACT ACA AGT TTC CCC 8592 Leu He Arg Phe Gly Val Arg Phe Met Val Thr Thr Thr Ser Phe Pro 2850 2855 2860 TGG ACA AAC TGC CTA ACA TCA TCG TGG CCC TCC ACG GAC CAG CAG CGT 8640 Trp Thr Aβn Cye Leu Thr Ser Ser Trp Pro Ser Thr Asp Gin Gin Arg 2865 2870 2875 2880 TGA GGG TTA CCG CAG ACA CAA CCA AAA CAA AGA TGG AGG CTG GGA AGG 8688 * Gly Leu Pro Gin Thr Gin Pro Lys Gin Arg Trp Arg Leu Gly Arg 2885 2890 2895 TTC TGA GCG ACC TCA AGC TCC CTG GTC TAG CCG TCC ACC GCA AGA AGG 8736 Phe * Ala Thr Ser Ser Ser Leu Val * Pro Ser Thr Ala Arg Arg 2900 2905 2910 CCG GGG CAT TGC GAA CAC GCA TGC TCC GGT CGC GCG GTT GGG CGG AGT 8784 Pro Gly Hiβ Cyβ Glu Hie Ala Cye Ser Gly Arg Ala Val Gly Arg Ser 2915 2920 2925 TGG CTA GGG GCC TGT TGT GGC ATC CAG GAC TCC GGC TTC CTC CCC CTG 8832 Trp Leu Gly Ala Cyβ Cys Gly He Gin Asp Ser Gly Phe Leu Pro Leu 2930 2935 2940 AGA TTG CTG GTA TCC CAG GGG GTT TCC CTC TGT CCC CCC CCT ACA TGG 8880 Arg Leu Leu Val Ser Gin Gly Val Ser Leu Cys Pro Pro Pro Thr Trp 2945 2950 2955 2960 GGG TGG TTC ATC AAT TGG ATT TCA CAG CSC AGC GGA GTC GCT GGC GGT 8928 Gly Trp Phe He Asn Trp He Ser Gin Xaa Ser Gly Val Ala Gly Gly 2965 2970 2975 GGT TGG GGT TCT TAG CCC TGC TCA TCG TAG CGC TCT TTG GGT GAA CTA 8976 Gly Trp Gly Ser * Pro Cys Ser Ser * Arg Ser Leu Gly Glu Leu 2980 . 2985 2990 AAT TCA TCT GTT GCG GCC GGA GTC AGA CCT GAG CCC CGT TCA AAA GGG 9024 Asn Ser Ser Val Ala Ala Gly Val Arg Pro Glu Pro Arg Ser Lys Gly 2995 3000 3005 GAT TGA GAC 9033 Aep * Aep 3010 (2) INFORMATION FOR SEQ ID NO:408: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 5 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear 497 (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:408: Lys Val Val Asp Gly 1 5 (2) INFORMATION FOR SEQ ID NO:409: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 39 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:409: Val Val Aβn Pro Gly Hie Pro Gly Ser Hie Tyr Arg Trp Val Leu Arg 1 5 10 15 Gly Gly Tyr Gly Pro Ser Cys Ala Tyr Gly Gly Lys Ala Hie Gly Pro 20 25 30 Gin Val Leu Val Leu Pro Val 35 (2) INFORMATION FOR SEQ ID NO:410: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 34 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:410: Gly Pro Gly Ala Arg Hiβ Ala Val Lye Pro Ser Pro Leu Leu Pro Trp 1 5 10 15 Ala Asn Asp Ala His Val Arg Ser Thr Ser Pro Phe Asn Val Ser Leu 20 25 30 Asp Gin (2) INFORMATION FOR SEQ ID NO:411: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 75 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:411: 498 Ala Tyr Gly Glu Leu Thr Arg Thr Ser Gly Gly Arg Ala Gly Gly Gly 1 5 10 15 Arg Thr Pro Thr Ala Ala Leu Pro Gly Glu Ala Gly Aen Ala Trp Gly 20 25 30 Hiβ Pro Ala Pro Arg Arg Pro Thr Ala Gly Val Ala Gin Glu Leu Arg 35 40 45 Val Arg Ala Gly Gly He Ser Phe Pro He Pro He Met Ala Val Leu 50 55 60 Leu Leu Leu Leu Val Val Glu Pro Gly Leu Phe 65 70 75 (2) INFORMATION FOR SEQ ID NO:412: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 23 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:412: Pro Arg Pro Pro Met Leu Val Ala Arg Lye Gly Asn He Xaa Ser Gin 1 5 10 15 Thr Val Ala Pro Trp Arg Thr 20 (2) INFORMATION FOR SEQ ID NO:413: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 76 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:413: Ala Ser Ala Trp Arg Ala Asp Ala Trp Trp Leu Trp Gly Ala Pro Phe 1 5 10 15 Ala Pro Thr Ala Ala Gly Hie Cys He Arg Arg Val Trp Pro Cys Gly 20 25 30 Pro Ala Ser Pro Pro Pro Ser Trp Trp Gly Asn Ser Val Val Ser Thr 35 40 45 Gly Pro Cys Arg Ser Arg Leu Met Trp Pro Gly Ser Trp Gly Leu Gly 50 55 60 Arg Ser Thr Arg Gly Ser Ser Pro Ser Gly Trp Arg 65 70 75 (2) INFORMATION FOR SEQ ID NO:414: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9 amino acids 499 (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:414: Arg Ala Gly Ser Thr Arg Ser Arg Thr 1 5 (2) INFORMATION FOR SEQ ID NO:415: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 33 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:415: Ser Gly Lys Val Ser Phe Gly Aep Gly Leu Asn Ser Trp Pro Gin Thr 1 5 10 15 Thr Gly Phe Trp Asn Thr Ser Gly Arg Cys Leu Ser Thr Phe Gly Gly 20 25 30 Glu (2) INFORMATION FOR SEQ ID NO:416: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 125 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:416: 500 115 120 125 (2) INFORMATION FOR SEQ ID NO:417: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 34 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:417: Pro Ala Cys Gly Val Leu Cys Leu Gly Leu Leu Pro Leu Gly Val Ala 1 5 10 15 Thr Pro Arg Leu Met Cys Gly Val Trp Phe Gin Leu Ala Leu Pro Ala 20 25 30 Ala Pro (2) INFORMATION FOR SEQ ID NO:418: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 36 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:418: Pro His Trp Asp Leu Arg He Ala Thr Gin Trp Leu Ser Ser Pro Ser 1 5 10 15 Gly Glu Phe Pro Ala Pro Leu Val Ser Trp Thr Gly Gly Leu Pro Arg 20 25 30 Val Ala Pro Val 35 (2) INFORMATION FOR SEQ ID NO:419: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 22 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:419: 501 Gly Thr Ala Gly Pro Arg Pro Gly Arg Tyr Val Ser Hie Ser Thr Gly 1 5 10 15 Val Ala Arg Aep Arg Gly 20 (2) INFORMATION FOR SEQ ID NO:420: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 17 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID N0:420: Pro Glu Thr Leu Arg Leu Cye Pro Ser Ser He Gly Gin Leu Pro Ser 1 5 10 15 Pro (2) INFORMATION FOR SEQ ID NO:421: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 23 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:421: Gly Gly Pro Trp Ala Thr Arg Gly Glu Ala Thr Arg Cye Gly Arg Pro 1 5 10 15 Trp Val Leu Gly Pro Thr Pro 20 (2) INFORMATION FOR SEQ ID NO:422: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:422: Pro Arg Ser Glu Thr Pro Tyr Thr Trp 1 5 (2) INFORMATION FOR SEQ ID NO:423: 502 (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 56 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:423: Aβn Val Pro Pro Gin Pro Leu Ser Leu Pro Pro Glu Arg Leu Gly Ser 1 5 10 15 Ser Gin Glu Ser Pro Pro Leu Thr Thr Ala Cyβ Phe Ser Ala Leu Arg 20 25 30 Cyβ Gin Arg Tyr Trp Val Gly Arg Ala Ser Leu Gly Gly Phe Thr Aen 35 40 45 Leu Trp Cys Gly Gly Val Gin Ser 50 55 (2) INFORMATION FOR SEQ ID NO:424: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 54 amino acide (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:424: Trp Val Gly Gly He Arg Ser Ala Arg Gly Leu His Gly Ser Leu Arg 1 5 10 15 Aep Gly Leu Met Gly Ser Tyr Met Phe Arg Ala Thr Cyβ Arg Arg Trp 20 25 30 Met Arg Ala Thr Ser Phe Arg Pro His Ala Gly Cys Ser Trp Thr Leu 35 40 45 Tyr Leu Ser Cys Tyr Thr 50 (2) INFORMATION FOR SEQ ID NO.-425: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:425: Ser Trp Gin Arg Hie Gly Trp Ser Arg 1 5 503 (2) INFORMATION FOR SEQ ID NO:426: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:426: Ser Ser Ser Cye Tyr Gly Gly Gly 1 5 (2) INFORMATION FOR SEQ ID NO:427: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 33 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:427: Thr Ser Trp Arg Ser Leu Xaa Xaa Arg Leu Xaa Xaa Pro Pro Trp Leu 1 5 10 15 Glu Arg Cye Leu Arg Ala Leu Pro Cyβ Pro Gly Val Trp Ala Tyr Pro 20 25 30 Ser (2) INFORMATION FOR SEQ ID NO:428: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 14 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:428: Gin Thr Trp Cyβ Cyβ Thr Ser Ala Gly Trp Val Leu Aβn Ala 1 5 10 (2) INFORMATION FOR SEQ ID NO:429: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 17 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein 504 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:429: Cye Ser Ser Cyβ Cyβ Gly Ser Ser Leu Gly Gly Leu Ser Arg Trp His 1 5 10 15 Tyr (2) INFORMATION FOR SEQ ID NO:430: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 41 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:430: Trp Gly Phe Pro Pro Leu Ala Ala Ala Pro Leu Cye Leu Ala Pro Asn 1 5 10 15 Ser Ala Leu Met Ser Pro Leu Lys Trp Thr Arg Gin Ser Trp Val Gly 20 25 30 Trp Leu Leu Val Trp Trp Leu Gly Pro 35 40 (2) INFORMATION FOR SEQ ID NO:431: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:431: Ala Arg Gly Gly Gly Ser Thr Lye Pro 1 5 (2) INFORMATION FOR SEQ ID NO:432: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 29 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:432: Ser He Gly Arg Gly Val Lye Gly Thr Arg Xaa Phe Ala Ser Ala Trp 1 5 10 15 Cye Val Ala Pro Ser Gly Arg Gly Gly Pro Pro Ser Arg 20 25 505 <2) INFORMATION FOR SEQ ID NO: 33: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 12 amino acids <B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:433: Pro Gly Val Trp Pro Leu Thr Ser Gly Arg Thr Leu 1 5 10 (2) INFORMATION FOR SEQ ID NO:434: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 41 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:434: Cyβ Trp Trp Leu Trp Pro Trp Ser Ser Ser Ser Ala Phe Ser Thr Arg 1 5 10 15 Ser He Gly Pro Trp Arg Ser Ser Leu Cyβ Arg Gly Leu Arg Cyβ Val 20 25 30 Val Trp Gin Gly Trp Trp Ser Val Val 35 40 (2) INFORMATION FOR SEQ ID NO:435: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 63 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:435: Trp Arg Ala Arg Arg Pro Leu Pro Ser Gly Leu Cyβ Pro Arg Cyβ Ala 1 5 10 15 Arg Glu Gly Pro Thr Cyβ Leu Thr Thr Trp Gly Arg Ser Arg Ala Arg 20 25 30 Ser Arg Ser Ala Cyβ Trp Ser Gly Thr Arg Leu Trp Xaa Pro Cyβ Hie 35 40 45 Ser Leu Gly Arg Thr Val Ala Ser Tyr Glu Thr Pro Pro Gly Pro 50 55 60 506 (2) INFORMATION FOR SEQ ID NO:436: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 19 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:436: Ala Ala Ala Asn Ala Ser Trp Ala Cys Pro Trp Trp Leu Gly Ala Ala 1 5 10 15 Met Arg Ser (2) INFORMATION FOR SEQ ID NO:437: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 6 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:437: Leu Gly Ser Phe Arg Met 1 5 (2) INFORMATION FOR SEQ ID NO:438: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 29 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:438: Thr Thr Cys Leu Arg Gly Leu Xaa Leu Gin Arg Leu Leu Ser Ser Val 1 5 10 15 Gly Ala Glu Arg Ala Ser Ser Gly Ser Leu Arg Leu Pro 20 25 (2) INFORMATION FOR SEQ ID NO:439: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 26 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein 507 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:439: Leu Val Gly He Leu Thr Tyr Thr Gin Glu Thr Ser Trp Phe Trp Gly 1 5 10 15 Arg Leu Pro Arg Ala Ala Trp Glu Arg Ala 20 25 (2) INFORMATION FOR SEQ ID NO:440: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 68 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:440: Thr Gly Cyβ Cys Ser Arg His Ser Met Gly Leu Leu Pro Glu Pro Leu 1 5 10 15 Arg His Leu Trp Gly Pro Leu Thr Gin Gly Gly Gly Arg Pro Val Met 20 25 30 Thr Ser Arg Ser He Pro Ser Pro Met Glu Leu Thr Arg Trp Phe Pro 35 40 45 Ala Arg Val Arg Leu Ser Pro Val Gly Ser Xaa Asp Pro Met Gly Leu 50 55 60 Phe Ala Met Ala 65 (2) INFORMATION FOR SEQ ID NO:441: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 5 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:441: Ala Arg Gly Thr Arg 1 5 (2) INFORMATION FOR SEQ ID NO:442: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 26 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:442: Aen Trp Thr Trp Pro Trp Arg Leu Leu Thr Phe Val Gly Arg Leu Gly 1 5 10 15 Leu Leu Ser Tyr Ala Thr Arg Gly Thr Leu 508 20 25 (2) INFORMATION FOR SEQ ID NO:443: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 12 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:443: Glu Cys Ser Cyβ Pro Ser Phe He Arg Gly Gly Gly 1 5 10 (2) INFORMATION FOR SEQ ID NO:444: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 59 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:444: Pro Arg Leu Aep Ser Leu Gly Arg Gly Pro Lye Ser Gin Gin Thr Pro 1 5 10 15 Arg Leu Pro Leu Ser Hiβ Pro Arg Cyβ Gin Leu Lye Gly Phe Ser Lye 20 25 30 Arg Leu Leu Phe Ser Cyβ Gin Gin Gly Arg Gly Lys Ala His Ala Ser 35 40 45 Leu Trp Ser Met Glu Thr Trp Gly Thr Arg Ser 50 55 (2) INFORMATION FOR SEQ ID NO:445: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:445: Phe Ser Thr Arg Arg Leu Pro Leu 1 5 (2) INFORMATION FOR SEQ ID NO:446: 509 (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 33 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:446: Gly Pro Trp Ala Leu Thr Trp Arg Gly Trp Arg Gly Aβn He Leu Ala 1 5 10 15 Phe Ser Val Aep Thr Thr Gin Gin Leu Ser Hie Gly Ser Arg Thr Leu 20 25 30 His (2) INFORMATION FOR SEQ ID NO:447: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 15 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:447; Arg Thr Leu Pro Met Gly Gly Phe Trp Pro Thr Arg Gly Arg Cyβ 1 5 10 15 (2) INFORMATION FOR SEQ ID NO:448: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:448: Gly Glu Phe Pro Trp Ser Ser Val Met Ser Ala Thr Val Met Thr Gin 1 5 10 15 20 (2) INFORMATION FOR SEQ ID NO:449: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 13 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein 510 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:449: Ala Gly Ser Gly Thr Trp Arg Gly Gly Val Glu Cyβ Aβn 1 5 10 (2) INFORMATION FOR SEQ ID NO:450: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 12 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:450: Cyβ Ser Thr Leu Leu Arg Leu Pro Arg Ala Arg Leu 1 5 10 (2) INFORMATION FOR SEQ ID NO:451: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 5 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:451: 1 5 (2) INFORMATION FOR SEQ ID NO:452: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:452: Leu Arg Gin Ser Trp Thr Leu Val Arg Ser Pro Phe Met Gly Met Val 1 5 10 15 Ser Pro Ser Ser Val 20 (2) INFORMATION FOR SEQ ID NO:453: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 77 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear 511 (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:453: Gly Leu Val Ala Thr Leu Tyr Ser Ala He Pro Arg Arg Ser Ala Arg 1 5 10 15 Asp Trp Pro Ala Ser Ser Pro Arg Gly Gly Leu Met Pro Ser Pro He 20 25 30 He Gly Val Arg Thr Val Pro Ser Ser Lys Thr Glu Thr Trp Trp Phe 35 40 45 Val Arg Gin Thr Arg Ser Leu Pro Gly Thr Gin Glu Thr Ser He Leu 50 55 60 Ser Pro Thr Val Gly Trp Trp Trp Arg Arg Ser Leu Arg 65 70 75 (2) INFORMATION FOR SEQ ID NO:454: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 60 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:454: Pro Leu He Pro Pro Leu Pro Phe Pro Cyβ Gly Leu Ser Leu Leu Arg 1 5 10 15 Leu Aen Cye Arg Cys Ser Gly Ala Asp Ala Arg Gly Glu Val Gly Arg 20 25 30 Ala Ala Thr Thr Thr Leu Gly Ser Val Arg Leu Pro Arg Gly Trp Cys 35 40 45 Gly Leu Val Arg Ser Gly Arg Gin Trp Lye Leu Glu 50 55 60 (2) INFORMATION FOR SEQ ID NO:455: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:455: Pro Gly Met Glu Trp Aen Leu Thr 1 5 (2) INFORMATION FOR SEQ ID NO:456: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acidβ (B) TYPE: amino acid 512 (D) TOPOLOGY : linear ( ii) MOLECULE TYPE : protein (xi) SEQUENCE DESCRIPTION : SEQ ID NO : 456 : Gin Gin Thr Phe 1 (2) INFORMATION FOR SEQ ID NO:457: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 72 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:457: Asp Phe Thr Thr Thr Ala Leu Thr Pro Gin Pro Ser Gin Leu Thr Leu 1 5 10 15 Val Lys Pro Arg Cys Ser Leu Arg Ala Ser Arg Pro Ser Gly Cys He 20 25 30 Pro Met Leu Ala Gly Gin Lys Phe Ala Ala Ser He Gly Pro Ser Trp 35 40 45 Trp Val Phe Ser Gly Arg Cys Val Gly Lye Hie Cyβ Leu Pro Ala Arg 50 55 60 Arg Thr Thr Leu Ser Gly Gin Val 65 70 (2) INFORMATION FOR SEQ ID NO:458: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:458: Lye Ala Arg He Leu Ser Hiβ Tyr Cyβ 1 5 (2) INFORMATION FOR SEQ ID NO:459: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 14 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein 513 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:459: Gly Gly Ala Met He Cys His Gin Lys Trp Pro Ala Thr Thr 1 5 10 (2) INFORMATION FOR SEQ ID NO:460: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 28 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:460: Leu Thr He Trp Ser Val Gly Ser Val Trp Arg Arg Asp Thr Cys Ala 1 5 10 15 Val Met Leu Xaa Pro Ser Ser Trp Trp Ala Trp Pro 20 25 (2) INFORMATION FOR SEQ ID NO:461: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:461: Ser Thr Pro Leu Thr Leu Gly Arg 1 5 (2) INFORMATION FOR SEQ ID NO:462: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:462: Gin Thr Gly Met 1 (2) INFORMATION FOR SEQ ID NO:463: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 amino acidβ (B) TYPE: amino acid 514 (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:463: Arg Glu Val Ala He Pro Phe He Gly Val Val Thr Arg Pro Pro Leu 1 5 10 15 Aβn Pro Trp Cye Arg Ser Pro Arg 20 (2) INFORMATION FOR SEQ ID NO:464: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 15 amino acidε (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:464: Thr He Gly Arg Gly Gly Ser Leu Arg Hie Gly Met Pro Arg Gin 1 5 10 15 (2) INFORMATION FOR SEQ ID NO:465: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:465: Gin Met Arg Trp Gin Pro Ser Arg 1 5 (2) INFORMATION FOR SEQ ID NO:466: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 5 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:466: Thr Ala He Gly Leu 515 1 5 (2) INFORMATION FOR SEQ ID NO:467: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 200 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:467: Pro Cys Arg Ser Gly Lys Ser Ser Pro Trp Leu Arg Leu Arg Gin Pro 1 5 10 15 Arg Pro Thr Gin Leu Leu Pro Gly Gly Ser Leu Ala Ala Thr Arg Gly 20 25 30 Arg Gly Pro Ser Pro Leu Tyr Gin Leu Leu Thr Ser Ser Ser Pro Gly 35 40 45 Val Gly Pro Pro Trp Trp Val Thr Val Thr Ala Ser Leu Leu Arg Arg 50 55 60 Trp Leu Pro Met Glu Leu Leu Glu Val Leu His Trp Pro Arg Arg Arg 65 70 75 80 Pro Thr Ser Trp Gly Trp Ala Ser Glu Ala Thr His Arg Arg Ala Trp 85 90 95 Leu Gin Leu Phe Tyr Trp Gly Leu Leu Val Arg Leu Trp Gly Pro Leu 100 105 110 Ser Trp Asp Ser Pro Trp Arg Gly Pro Ser Trp Ala Val Pro Ala Cyβ 115 120 125 Pro Pro Pro Ser Ser Leu Ser Tyr Leu Gly Leu Trp Glu Val Gly Arg 130 135 140 Ala Leu Ser Thr Leu Pro Val Ser Ser Ser Thr Ser Trp Leu Gly Aβn 145 150 155 160 Phe Gin Gin Lye Thr Phe Gly Met Pro Ser Arg Tyr Ser Leu Val Leu 165 170 175 Xaa Arg Ala Ser Arg Gly Leu Pro Leu Val Trp Phe Cyβ Thr Gin Gin 180 185 190 Thr Thr Leu Ala Leu Pro Hie Gly 195 200 (2) INFORMATION FOR SEQ ID NO:468: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 29 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:468: Arg Arg Cyβ His Gly Hie Leu Ala Tyr Pro Thr Ala Thr Ser Aβn Arg 1 5 10 15 Leu Thr Thr Ala Thr Arg Ser Arg Gin Ser Cys Ala Ala 20 25 516 (2) INFORMATION FOR SEQ ID NO:469: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 30 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:469: Ala Leu Leu Ala Pro Trp Trp Pro Trp Ser Thr Gly Ser Leu Arg Trp 1 5 10 15 Met Arg Ser Arg Trp Gly Thr Ser Gly He Cys Gly Ser Gly 20 25 30 (2) INFORMATION FOR SEQ ID NO:470: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 6 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:470: 1 5 (2) INFORMATION FOR SEQ ID NO:471: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 40 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:471: Cys Leu Asp Ser Gly Pro Ser Ala Leu Trp Cys Hiβ Ser Pro Cyβ Gly 1 5 10 15 Thr Ala Gly Arg Gly Gly Pro Val Aβn Gly Phe Ser Met Gly Thr Trp 20 25 30 Arg Val Val Val Cyβ Ala Gly Val 35 40 (2) INFORMATION FOR SEQ ID NO:472: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 61 amino acidβ (B) TYPE: amino acid 517 (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:472: Ser Pro Ala Thr Ser Ser Met Gly Aen Ser Lye He Gin Phe Thr Leu 1 5 10 15 Pro Ser Cyβ Ala Gly Thr Thr Gly Trp Glu Leu Cye Arg Ser Thr Cys 20 25 30 Trp Ala Thr Gly Lye Pro Hie Leu Phe Ser Pro Leu Thr Pro Arg Arg 35 40 45 Trp Tyr Pro Ser Gly Arg Arg Gly Gly Leu Arg Trp Trp 50 55 60 (2) INFORMATION FOR SEQ ID NO:473: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 5 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:473: Pro Leu Pro Thr Trp 1 5 (2) INFORMATION FOR SEQ ID NO:474: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 18 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:474: Ser Gly Ala Arg Pro Val Thr Asn Cys Phe Ala Ser Lys Phe Phe Gin 1 5 10 15 Gin Leu (2) INFORMATION FOR SEQ ID NO:475: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 69 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:475: 518 Leu Ser Pro Thr Thr Leu Met Ala Phe Arg Ser Leu Gly Arg Leu Thr 1 5 10 15 Arg Glu Arg Arg Pro Trp Ser Thr Val Arg Ala Lys Val Leu Pro Leu 20 25 30 Met Gly Ser Ala Thr Pro Phe Arg Thr Ser Cyβ Gly Cyβ Gly Met Trp 35 40 45 Arg Pro Leu Arg Phe Hiβ Leu Arg Ser Ala Ser Arg Ser Gly Arg Arg 50 55 60 Leu Lye Thr Gin Aen 65 (2) INFORMATION FOR SEQ ID NO:476: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 14 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:476: Leu Arg Pro He Cyβ Hiβ Gin Arg Leu Leu Pro Ser Lye Arg 1 5 10 (2) INFORMATION FOR SEQ ID NO:477: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 59 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:477: Arg Met Leu Arg Glu Phe Ser Asn Arg Thr Ser Met Ser Xaa Trp Arg 1 5 10 15 He Ala Val His Pro Leu Ser Val Val Val Ala Glu Arg Cys Leu Cys 20 25 30 Gly Glu Lye Thr Tyr Pro Ala Leu His Arg Leu Hiβ Leu Ser Arg Leu 35 40 45 Arg Arg Ala Ala Gin Met Arg Arg Pro Cys Arg 50 55 (2) INFORMATION FOR SEQ ID NO:478: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 35 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein 519 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:478: Pro Pro Arg Arg Arg Thr Pro Arg Pro Gin Thr His Leu Lye Ser Ser 1 5 10 15 Lye Ser Leu He Leu Leu Aen Gin Arg Lye Ala Ser Ser Thr Trp Leu 20 25 30 Phe Pro Tyr 35 (2) INFORMATION FOR SEQ ID NO:479: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 12 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:479: Lys Pro Tyr Phe His Arg Ala Met Pro Hie Glu Ser 1 5 10 (2) INFORMATION FOR SEQ ID NO:480: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 11 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:480: Arg Leu Arg Cyβ Leu Ala Val Leu Arg Arg Ala 1 5 10 (2) INFORMATION FOR SEQ ID NO:481: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 5 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:481: 1 5 (2) INFORMATION FOR SEQ ID NO:482: (i) SBQUENCE CHARACTERISTICS: 520 (A) LENGTH: 75 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:482: Pro Trp Leu Thr Trp Leu Ala Cyβ Val Arg Trp Arg Ser Arg Thr He 1 5 10 15 Gin Pro He Val Thr Arg Cye Ala Leu Arg Ser Aβn Cyβ Lys Leu Gly 20 25 30 Ala Trp Trp Ala Met Asn Leu Pro Leu Aβn Val Thr Ser Val Arg Hiβ 35 40 45 Ala Lye Arg Pro Leu Pro Pro Ser Pro Thr Tyr Gly Pro Gly Ser His 50 55 60 Leu Leu Gly Pro Leu Arg Pro Asn His Gin Trp 65 70 75 (2) INFORMATION FOR SEQ ID NO:483: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 15 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:483: Gly Arg Trp Gly Pro Cys Trp Trp Gin Thr Pro Pro Arg Ser Thr 1 5 10 15 (2) INFORMATION FOR SEQ ID NO:484: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 12 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:484: Pro He Arg Thr Met Leu Gly Gly Gly Leu Thr Arg 1 5 10 (2) INFORMATION FOR SEQ ID NO:485: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 27 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:485: 521 Leu Ser Gly Ala Leu Leu Gly Tyr Thr Thr Ser Ser Ser Trp Thr Arg 1 5 10 15 Ser Ser Ala Leu Gly Glu Leu Leu Lys Ala Ala 20 25 (2) INFORMATION FOR SEQ ID NO:486: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:486: Ala Trp Val Thr Leu Met Arg Arg Gin 1 5 (2) INFORMATION FOR SEQ ID NO:487: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 45 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:487: Gly Leu Leu Gly Arg Met Leu Pro Trp Ala Gly Aep Leu Arg Cye Arg 1 5 10 15 Ser Arg Thr Trp Pro Pro Leu Arg Gly Arg Trp Leu Phe Met Thr Gly 20 25 30 Phe Arg Arg Tyr Leu Lye Gly Leu Arg Ser Leu Leu Pro 35 40 45 (2) INFORMATION FOR SEQ ID NO:488: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 28 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:488: Leu Ser Lys Arg Arg Cys Ser Ser Lye He Val Arg Arg Arg Arg Pro 1 5 10 15 Pro Ala Ser Leu Cye Ser Pro Pro Trp Thr Ser Gly 20 25 (2) INFORMATION FOR SEQ ID NO:489: 522 (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 34 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:489: Leu Lys Ser Ser Phe Trp Glu Thr Arg Gly Gly Leu Gin Arg Pro Val 1 5 10 15 Leu Gly Gly Leu Thr Pro Ser Ser Thr Pro Pro Thr Ser Gly Leu Arg 20 25 30 Arg Cys (2) INFORMATION FOR SEQ ID NO:490: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 29 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:490: Ser Cys Gly Asn Gin Arg Arg Pro Arg Ala Pro Ser Val Trp Met Pro 1 5 10 15 Leu Ala Ser Thr Val Ala Leu Leu Xaa Arg Thr Trp His 20 25 (2) INFORMATION FOR SEQ ID NO:491: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 27 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:491: Arg Gin Ser Phe Thr Pro Trp Pro Arg Thr He Gin Aβn Gly Cyβ Ala 1 5 10 15 Pro Trp Gly Aen Thr Xaa Pro Leu Ala Gin Trp 20 25 (2) INFORMATION FOR SEQ ID NO:492: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 17 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein 523 (xi) SEQUENCE DESCRIPTION : SEQ ID NO : 492 : Pro Arg Lys Gly Cys Gin Trp Ala Arg Gly He Val Gly Pro Arg Val 1 5 10 15 Cys (2) INFORMATION FOR SEQ ID NO:493: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 7 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:493: Pro Gin Val Leu Ala Thr Val 1 5 (2) INFORMATION FOR SEQ ID NO:494: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 5 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:494: Pro Ala Thr Ser Lys 1 5 (2) INFORMATION FOR SEQ ID NO:495: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:495: Glu Pro Pro Val Arg Gly Ser Asp 1 5 (2) INFORMATION FOR SEQ ID NO:496: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 13 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear 524 (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:496: Lye Met Ser Arg Phe Ser Ser Arg Ala Met Thr Ala 1 5 10 (2) INFORMATION FOR SEQ ID NO: 97: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 55 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:497: Leu Cyβ Ala Arg Gly Leu Tyr Ala Thr Leu Ala Arg Pro Trp Ala Glu 1 5 10 15 Pro Trp Leu Arg Thr Gly Thr Arg Val Ser Pro Arg He Thr Leu His 20 25 30 Trp Thr Gin Pro Pro Ser Ala Pro Leu Gly Ser Leu Ser Ala Met Arg 35 40 45 Met Xaa Lys Gly He Ser Ser 50 55 (2) INFORMATION FOR SEQ ID NO:498: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 43 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:498: Pro Arg Thr Phe Gly Asp His Ser Leu Ala Cys Arg Ala Ser Thr Val 1 5 10 15 Thr Leu Trp Leu Arg Pro Leu Val Thr Phe Ser Ser Thr Pro Gly Xaa 20 25 30 Pro Ser Hie Gly Gly Ser Ser Ser Arg Met Cye 35 40 (2) INFORMATION FOR SEQ ID NO:499: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 43 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:499: Hiβ Ala Leu Leu Pro Gly Val Val Ala Hiβ Xaa Leu He Arg Phe Gly 525 1 5 10 15 Val Arg Phe Met Val Thr Thr Thr Ser Phe Pro Trp Thr Aβn Cyβ Leu 20 25 30 Thr Ser Ser Trp Pro Ser Thr Asp Gin Gin Arg 35 40 (2) INFORMATION FOR SEQ ID NO:500: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 16 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:500: Gly Leu Pro Gin Thr Gin Pro Lys Gin Arg Trp Arg Leu Gly Arg Phe 1 5 10 15 (2) INFORMATION FOR SEQ ID NO:501: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 7 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:501: Ala Thr Ser Ser Ser Leu Val 1 5 (2) INFORMATION FOR SEQ ID NO:502: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 74 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:502: Pro Ser Thr Ala Arg Arg Pro Gly Hiβ Cyβ Glu Hie Ala Cye Ser Gly 1 5 10 15 Arg Ala Val Gly Arg Ser Trp Leu Gly Ala Cyβ Cye Gly He Gin Aep 20 25 30 Ser Gly Phe Leu Pro Leu Arg Leu Leu Val Ser Gin Gly Val Ser Leu 35 40 45 Cye Pro Pro Pro Thr Trp Gly Trp Phe He Aen Trp He Ser Gin Xaa 50 55 60 Ser Gly Val Ala Gly Gly Gly Trp Gly Ser 65 70 526 (2) INFORMATION FOR SEQ ID NO:503: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:503: 1 (2) INFORMATION FOR SEQ ID NO:504: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 23 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:504: Arg Ser Leu Gly Glu Leu Aβn Ser Ser Val Ala Ala Gly Val Arg Pro 1 5 10 15 Glu Pro Arg Ser Lys Gly Asp 20 (2) INFORMATION FOR SEQ ID NO:505: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9034 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 3..9034 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:505; AGG TGG TGG ATG GGT GAT GAC AGG GTT GGT AGG TCG TAA ATC CCG GTC 48 Arg Trp Trp Met Gly Aep Aep Arg Val Gly Arg Ser * He Pro Val 1 5 10 15 ATC CTG GTA GCC ACT ATA GGT GGG TCT TAA GGG GAG GCT ACG GTC CCT 96 He Leu Val Ala Thr He Gly Gly Ser * Gly Glu Ala Thr Val Pro 527 20 25 30 CTT GCG CAT ATG GAG GAA AAG CGC ACG GTC CAC AGG TGT TGG TCC TAC 144 Leu Ala Hie Met Glu Glu Lye Arg Thr Val Hiβ Arg Cys Trp Ser Tyr 35 40 45 CGG TGT AAT AAG GAC CCG GCG CTA GGC ACG CCG TTA AAC CGA GCC CGT 192 Arg Cyβ Asn Lye Aep Pro Ala Leu Gly Thr Pro Leu Aβn Arg Ala Arg 50 55 60 TAC TCC CCT GGG CAA ACG ACG CCC ACG TAC GGT CCA CGT CGC CCT TCA 240 Tyr Ser Pro Gly Gin Thr Thr Pro Thr Tyr Gly Pro Arg Arg Pro Ser 65 70 75 80 ATG TCT CTC TTG ACC AAT AGG CGT ACG GCG AGT TGA CAA GGA CCA GTG 288 Met Ser Leu Leu Thr Aen Arg Arg Thr Ala Ser * Gin Gly Pro Val 85 90 95 GGG GCC GGG CGG GAG GGG GAA GGA CCC CCA CCG CTG CCC TTC CCG GGG 336 Gly Ala Gly Arg Glu Gly Glu Gly Pro Pro Pro Leu Pro Phe Pro Gly 100 105 110 AGG CGG GAA ATG CAT GGG GCC ACC CAG CTC CGC GGC GGC CTA CAG CCG 384 Arg Arg Glu Met Hie Gly Ala Thr Gin Leu Arg Gly Gly Leu Gin Pro 115 120 125 GGG TAG CCC AAG AAC TTC GGG TGA GGG CGG GTG GCA TTT CTT TTC CTA 432 Gly * Pro Lye Aβn Phe Gly * Gly Arg Val Ala Phe Leu Phe Leu 130 135 140 TAC CGA TCA TGG CAG TCC TTC TGC TCC TAC TCG TGG TGG AGC CGG GGC 480 Tyr Arg Ser Trp Gin Ser Phe Cye Ser Tyr Ser Trp Trp Ser Arg Gly 145 150 155 160 TAT TTT AGC CCC GGC CAC CCA TGC TTG TAG CGC GAA AGG GCA ATA TTT 528 Tyr Phe Ser Pro Gly His Pro Cys Leu * Arg Glu Arg Ala He Phe 165 170 175 SCT CAC AAA CTG TTG CGC CCT GGA GGA CAT AGG CTT CTG CCT GGA GGG 576 Xaa His Lys Leu Leu Arg Pro Gly Gly His Arg Leu Leu Pro Gly Gly 180 185 190 CGG ATG CCT GGT GGC TCT GGG GTG CAC CAT TTG CAC CGA CCG CTG CTG 624 Arg Met Pro Gly Gly Ser Gly Val Hiβ Hie Leu Hie Arg Pro Leu Leu 195 200 205 GCC ACT GTA TCA GGC GGG TTT GGC CGT GCG GCC CGG CAA GTC CGC CGC 672 Ala Thr Val Ser Gly Gly Phe Gly Arg Ala Ala Arg Gin Val Arg Arg 210 215 220 CCA GTT GGT GGG GGA ACT CGG TAG TCT CTA CGG GCC CTT GTC GGT CTC 720 Pro Val Gly Gly Gly Thr Arg * Ser Leu Arg Ala Leu Val Gly Leu 225 230 235 240 GGC TTA TGT GGC CGG GAT CCT GGG GCT TGG GGA GGT CTA CTC GGG GGT 768 Gly Leu Cye Gly Arg Aep Pro Gly Ala Trp Gly Gly Leu Leu Gly Gly 245 250 255 528 CCT CAC CGT CGG GGT GGC GTT GAC GCG CAG GGT CTA CCC GGT CCC GAA 816 Pro Hie Arg Arg Gly Gly Val Aep Ala Gin Gly Leu Pro Gly Pro Glu 260 265 270 CCT GAC GTG TGC AGT AGA GTG TGA GTT GAA GTG GGA AAG TGA GTT TTG 864 Pro Asp Val Cys Ser Arg Val * Val Glu Val Gly Lys * Val Leu 275 280 285 GAG ATG GAC TGA ACA GCT GGC CTC AAA CTA CTG GAT TCT GGA ATA CCT 912 Glu Met Aep * Thr Ala Gly Leu Lye Leu Leu Aep Ser Gly He Pro 290 295 300 CTG GAA GGT GCC TTT CGA CTT TTG GCG GGG AGT GAT GAG CCT TAC TCC 960 Leu Glu Gly Ala Phe Arg Leu Leu Ala Gly Ser Aep Glu Pro Tyr Ser 305 310 315 320 TCT CTT GGT GTG CGT GGC GGC CCT CCT CCT GCT GGA GCA GCG TAT TGT 1008 Ser Leu Gly Val Arg Gly Gly Pro Pro Pro Ala Gly Ala Ala Tyr Cyβ 325 330 335 CAT GGT CTT CCT CCT GGT CAC TAT GGC GGG CAT GTC GCA AGG CGC GCC 1056 His Gly Leu Pro Pro Gly His Tyr Gly Gly Hiβ Val Ala Arg Arg Ala 340 345 350 CGC CTC AAG TGT TGG GGT CAC GGC CTT TCG AGG CGG GTT TGA CTT GGC 1104 Arg Leu Lys Cyβ Trp Gly Hiβ Gly Leu Ser Arg Arg Val * Leu Gly 355 360 365 AGT CTT GTT CTT GCA GGT CGA ACG GGT CCC GCG TGC CGA CAG GGA GAG 1152 Ser Leu Val Leu Ala Gly Arg Thr Gly Pro Ala Cyβ Arg Gin Gly Glu 370 375 380 GGT TTG GGA ACG TGG GAA CGT CAC ACT TTT GTG TGA CTG CCC CAA CGG 1200 Gly Leu Gly Thr Trp Glu Arg Hie Thr Phe Val * Leu Pro Gin Arg 385 390 395 400 TCC TTG GGT GTG GGT CCC GGC CCT TTG CCA GGC AAT CGG ATG GGG CGA 1248 Ser Leu Gly Val Gly Pro Gly Pro Leu Pro Gly Aβn Arg Met Gly Arg 405 410 415 CCC TAT CAC TCA TTG GAG CCA CGG ACA AAA TCA GTG GCC CCT TTC TTG 1296 Pro Tyr Hiβ Ser Leu Glu Pro Arg Thr Lye Ser Val Ala Pro Phe Leu 420 425 430 TCC CCA ATT TGT CTA CGG CGC CGT TTC AGT GAC CTG CGT GTG GGG TTC 1344 Ser Pro He Cye Leu Arg Arg Arg Phe Ser Aep Leu Arg Val Gly Phe 435 440 445 TGT GTC TTG GTT TGC TTC CAC TGG GGG TCG CGA CTC CAA GGT TGA TGT 1392 Cyβ Val Leu Val Cyβ Phe Hiβ Trp Gly Ser Arg Leu Gin Gly * Cyβ 450 455 460 GTG GAG TTT GGT TCC AGT TGG CTC TGC CAG CTG CAC CAT AGC CGC ACT 1440 Val Glu Phe Gly Ser Ser Trp Leu Cye Gin Leu His His Ser Arg Thr 465 470 475 480 GGG ATC TTC GGA TCG CGA CAC AGT GGT TGA GCT CTC CGA GTG GGG AAT 1488 529 Gly He Phe Gly Ser Arg Hiβ Ser Gly * Ala Leu Arg Val Gly Asn 485 490 495 TCC CTG CGC CAC TTG TAT CCT GGA CAG GCG GCC TGC CTC GTG TGG CAC 1536 Ser Leu Arg His Leu Tyr Pro Gly Gin Ala Ala Cys Leu Val Trp Hiβ 500 505 510 CTG TGT GAG GGA CTG CTG GCC CGA GAC CGG GTC GGT ACG TTT CCC ATT 1584 Leu Cyβ Glu Gly Leu Leu Ala Arg Aep Arg Val Gly Thr Phe Pro He 515 520 525 CCA CAG GTG TGG CGC GGG ACC GAG GCT GAC CAG AGA CCT TGA GGC TGT 1632 Pro Gin Val Trp Arg Gly Thr Glu Ala Aep Gin Arg Pro * Gly Cyβ 530 535 540 GCC CTT CGT CAA TAG GAC AAC TCC CTT CAC CAT AAG GGG GCC CCT GGG 1680 Ala Leu Arg Gin * Aep Asn Ser Leu His His Lys Gly Ala Pro Gly 545 550 555 560 CAA CCA GGG GCG AGG CAA CCC GGT GCG GTC GCC CTT GGG TTT TGG GTC 1728 Gin Pro Gly Ala Arg Gin Pro Gly Ala Val Ala Leu Gly Phe Trp Val 565 570 575 CTA CAC CAT GAC CAA GAT CCG AGA CTC CTT ACA CTT GGT GAA ATG TCC 1776 Leu His His Asp Gin Asp Pro Arg Leu Leu Thr Leu Gly Glu Met Ser 580 585 590 CAC CCC AGC CAT TGA GCC TCC CAC CGG AAC GTT TGG GTT CTT CCC AGG 1824 His Pro Ser His * Ala Ser Hiβ Arg Aβn Val Trp Val Leu Pro Arg 595 600 605 AGT CCC CCC CCT TAA CAA CTG CAT GCT TCT CGG CAC TGA GGT GTC AGA 1872 Ser Pro Pro Pro * Gin Leu Hiβ Ala Ser Arg Hie * Gly Val Arg 610 615 620 GGT ATT GGG TGG GGC GGG CCT CAC TGG GGG GTT TTA CGA ACC TCT GGT 1920 Gly He Gly Trp Gly Gly Pro Hiβ Trp Gly Val Leu Arg Thr Ser Gly 625 630 635 640 GCG GCG GTG TTC AGA GCT GAT GGG TCG GCG GAA TCC GGT CTG CCC GGG 1968 Ala Ala Val Phe Arg Ala Aep Gly Ser Ala Glu Ser Gly Leu Pro Gly 645 650 655 GTT TGC ATG GCT CTC TTC GGG ACG GCC TGA TGG GTT CAT ACA TGT TCA 2016 Val Cyβ Met Ala Leu Phe Gly Thr Ala * Trp Val Hiβ Thr Cyβ Ser 660 665 670 GGG CCA CTT GCA GGA GGT GGA TGC GGG CAA CTT CAT TCC GCC CCC ACG 2064 Gly Pro Leu Ala Gly Gly Gly Cys Gly Gin Leu Hiβ Ser Ala Pro Thr 675 680 685 CTG GTT GCT CTT GGA CTT TGT ATT TGT CCT GTT ATA CCT GAT GAA GCT 2112 Leu Val Ala Leu Gly Leu Cyβ He Cys Pro Val He Pro Asp Glu Ala 690 695 700 GGC AGA GGC ACG GTT GGT CCC GCT GAT CCT CCT CCT GCT ATG GTG GTG - -• 2160 Gly Arg Gly Thr Val Gly Pro Ala Aep Pro Pro Pro Ala Met Val Val 530 705 710 715 720 GGT GAA CCA GTT GGC GGT CCT TGK TGT GSC GGC TGC KCR CGC CGC CGT 2208 Gly Glu Pro Val Gly Gly Pro Xaa Cys Xaa Gly Cys Xaa Arg Arg Arg 725 730 735 GGC TGG AGA GGT GTT TGC GGG CCC TGC CTT GTC CTG GTG TCT GGG CCT 2256 Gly Trp Arg Gly Val Cys Gly Pro Cye Leu Val Leu Val Ser Gly Pro 740 745 750 ACC CTT CGT GAG TAT GAT CCT GGG GCT AGC AAA CCT GGT GTT GTA CTT 2304 Thr Leu Arg Glu Tyr Aep Pro Gly Ala Ser Lye Pro Gly Val Val Leu 755 760 765 CCG CTG GAT GGG TCC TCA ACG CCT GAT GTT CCT CGT GTT GTG GAA GCT 2352 Pro Leu Aep Gly Ser Ser Thr Pro Aep Val Pro Arg Val Val Glu Ala 770 775 780 CGC TCG GGG GGC TTT CCC GCT GGC ATT ACT GAT GGG GAT TTC CGC CAC 2400 Arg Ser Gly Gly Phe Pro Ala Gly He Thr Aep Gly Asp Phe Arg His 785 790 795 800 TCG CGG CCG CAC CTC TGT GCT TGG CGC CGA ATT CTG CTT TGA TGT CAC 2448 Ser Arg Pro Hie Leu Cye Ala Trp Arg Arg He Leu Leu * Cye Hiβ 805 810 815 CTT TGA AGT GGA CAC GTC AGT CTT GGG TTG GGT GGT TGC TAG TGT GGT 2496 Leu * Ser Gly Hie Val Ser Leu Gly Leu Gly Gly Cye * Cyβ Gly 820 825 830 GGC TTG GGC CAT AGC GCT CCT GAG CTC TAT GAG CGC GGG GGG GTG GAA 2544 Gly Leu Gly Hie Ser Ala Pro Glu Leu Tyr Glu Arg Gly Gly Val Glu 835 840 845 GCA CAA AGC CAT AAT CTA TAG GAC GTG GTG TAA AGG GTA CCA GGC YCT 2592 Ala Gin Ser Hiβ Asn Leu * Asp Val Val * Arg Val Pro Gly Xaa 850 855 860 TCG CCA GCG CGT GGT GCG TAG CCC CCT CGG GGA GGG GCG GCC CAC CAA 2640 Ser Pro Ala Arg Gly Ala * Pro Pro Arg Gly Gly Ala Ala His Gin 865 870 875 880 GCC GCT GAC GAT AGC CTG GTG TCT GGC CTC TTA CAT CTG GCC GGA CGC 2688 Ala Ala Asp Asp Ser Leu Val Ser Gly Leu Leu His Leu Ala Gly Arg 885 890 895 TGT GAT GTT GGT GGT TGT GGC CAT GGT CCT CCT CTT CGG CCT TTT CGA 2736 Cys Asp Val Gly Gly Cys Gly His Gly Pro Pro Leu Arg Pro Phe Arg 900 905 910 CGC GCT CGA TTG GGC CTT GGA GGA GCT CCT TGT GTC GCG GCC TTC GTT 2784 Arg Ala Arg Leu Gly Leu Gly Gly Ala Pro Cys Val Ala Ala Phe Val 915 920 925 GCG TCG TTT GGC AAG GGT GGT GGA GTG TTG TGT GAT GGC GGG CGA GAA 2832 Ala Ser Phe Gly Lys Gly Gly Gly Val Leu Cys Asp Gly Gly Arg Glu 930 935 940 531 GGC CAC TAC CGT CCG GCT TGT GTC CAA GAT GTG CGC GAG AGG GGC CTA 2880 Gly His Tyr Arg Pro Ala Cys Val Gin Aep Val Arg Glu Arg Gly Leu 945 950 955 960 CCT GTT TGA CCA CAT GGG GTC GTT CTC GCG CGC GGT CAA GGA GCG CTT 2928 Pro Val * Pro Hie Gly Val Val Leu Ala Arg Gly Gin Gly Ala Leu 965 970 975 GCT GGA GTG GGA CGC GGC TTT GGA GMC CCT GTC ATT CAC TAG GAC GGA 2976 Ala Gly Val Gly Arg Gly Phe Gly Xaa Pro Val He Hiβ * Aep Gly 980 985 990 CTG TCG CAT CAT ACG AGA CGC CGC CAG GAC CCT GAG CTG CGG CCA ATG 3024 Leu Ser Hie Hiβ Thr Arg Arg Arg Gin Aep Pro Glu Leu Arg Pro Met 995 1000 1005 CGT CAT GGG CTT GCC CGT GGT GGC TAG GCG CGG CGA TGA GGT CCT GAT 3072 Arg His Gly Leu Ala Arg Gly Gly * Ala Arg Arg * Gly Pro Asp 1010 1015 1020 TGG GGT CTT TCA GGA TGT GAA CCA CTT GCC TCC GGG GTT TGY TCC TAC 3120 Trp Gly Leu Ser Gly Cys Glu Pro Leu Ala Ser Gly Val Xaa Ser Tyr 1025 1030 1035 1040 AGC GCC TGT TGT CAT CCG TCG GTG CGG AAA GGG CTT CCT CGG GGT CAC 3168 Ser Ala Cys Cys His Pro Ser Val Arg Lye Gly Leu Pro Arg Gly Hiβ 1045 1050 1055 TAA GGC TGC CTT GAC TGG TCG GGA TCC TGA CTT ACA CCC AGG AAA CGT 3216 * Gly Cyβ Leu Aep Trp Ser Gly Ser * Leu Thr Pro Arg Lye Arg 1060 1065 1070 CAT GGT TTT GGG GAC GGC TAC CTC GCG CAG CAT GGG AAC GTG CTT AAA 3264 Hiβ Gly Phe Gly Aep Gly Tyr Leu Ala Gin Hiβ Gly Asn Val Leu Lye 1075 1080 1085 CGG GTT GCT GTT CAC GAC ATT CCA TGG GGC TTC TTC CCG AAC CAT TGC 3312 Arg Val Ala Val Hiβ Aep He Pro Trp Gly Phe Phe Pro Asn His Cyβ 1090 1095 1100 GAC ACC TGT GGG GGC CCT TAA CCC AAG GTG GTG GTC GGC CAG TGA TGA 3360 Asp Thr Cys Gly Gly Pro * Pro Lys Val Val Val Gly Gin * * 1105 1110 1115 1120 CGT CAC GGT CTA TCC CCT CCC CGA TGG AGC TAA CTC GTT GGT TCC CTG 3408 Arg His Gly Leu Ser Pro Pro Arg Trp Ser * Leu Val Gly Ser Leu 1125 1130 1135 CTC GTG TCA GGC TGA GTC CTG TTG GGT CAT YCG ATC CGA TGG GGC TCT 3456 Leu Val Ser Gly * Val Leu Leu Gly His Xaa He Arg Trp Gly Ser 1140 1145 1150 TTG CCA TGG CTT GAG CAA GGG GGA CAA GGT AGA ACT GGA CGT GGC CAT 3504 Leu Pro Trp Leu Glu Gin Gly Gly Gin Gly Arg Thr Gly Arg Gly Hiβ 1155 1160 1165 GGA GGT TGC TGA CTT TCG TGG GTC GTC TGG GTC TCC TGT CCT ATG CGA 3552 532 Gly Gly Cyβ * Leu Ser Trp Val Val Trp Val Ser Cyβ Pro Met Arg 1170 1175 1180 CGA GGG GCA CGC TGT AGG AAT GCT CGT GTC CGT CCT TCA TTC GGG GGG 3600 Arg Gly Ala Arg Cyβ Arg Aβn Ala Arg Val Arg Pro Ser Phe Gly Gly 1185 1190 1195 1200 GAG GGT GAC CGC GGC TCG ATT CAC TCG GCC GTG GAC CCA AGT CCC AAC 3648 Glu Gly Aep Arg Gly Ser He His Ser Ala Val Asp Pro Ser Pro Asn 1205 1210 1215 AGA CGC CAA GAC TAC CAC TGA GCC ACC CCC GGT GCC AGC TAA AGG GGT 3696 Arg Arg Gin Asp Tyr His * Ala Thr Pro Gly Ala Ser * Arg Gly 1220 1225 1230 TTT CAA AGA GGC TCC TCT TTT CAT GCC AAC AGG GGC GGG GAA AAG CAC 3744 Phe Gin Arg Gly Ser Ser Phe His Ala Asn Arg Gly Gly Glu Lys Hiβ 1235 1240 1245 ACG CGT CCC TTT GGA GTA TGG AAA CAT GGG GCA CAA GGT CCT GAT TCT 3792 Thr Arg Pro Phe Gly Val Trp Lye Hiβ Gly Ala Gin Gly Pro Aep Ser 1250 1255 1260 CAA CCC GTC GGT TGC CAC TGT GAG GGC CAT GGG CCC TTA CAT GGA GAG 3840 Gin Pro Val Gly Cyβ Hiβ Cyβ Glu Gly Hiβ Gly Pro Leu Hiβ Gly Glu 1265 1270 1275 1280 GCT GGC GGG GAA ACA TCC TAG CAT TTT CTG TGG ACA CGA CAC AAC AGC 3888 Ala Gly Gly Glu Thr Ser * His Phe Leu Trp Thr Arg Hiβ Aβn Ser 1285 1290 1295 TTT CAC ACG GAT CAC GGA CTC TCC ATT GAC GTA CTC TAC CTA TGG GAG 3936 Phe Hiβ Thr Aep Hiβ Gly Leu Ser He Aep Val Leu Tyr Leu Trp Glu 1300 1305 1310 GTT TCT GGC CAA CCC GAG GCA GAT GCT GAG GGG AGT TTC CGT GGT CAT 3984 Val Ser Gly Gin Pro Glu Ala Aep Ala Glu Gly Ser Phe Arg Gly Hiβ 1315 1320 1325 CTG TGA TGA GTG CCA CAG TCA TGA CTC AAC TGT GTT GCT GGG TAT AGG 4032 Leu * * Val Pro Gin Ser * Leu Aβn Cyβ Val Ala Gly Tyr Arg 1330 1335 1340 CAG GGT CAG GGA CGT GGC GCG GGG GTG TGG AGT GCA ATT AGT GCT CTA 4080 Gin Gly Gin Gly Arg Gly Ala Gly Val Trp Ser Ala He Ser Ala Leu 1345 1350 1355 1360 CGC TAC TGC GAC TCC CCC GGG CTC GCC TAT GAC TCA GCA TCC ATC CAT 4128 Arg Tyr Cyβ Aep Ser Pro Gly Leu Ala Tyr Aep Ser Ala Ser He Hie 1365 1370 1375 AAT TGA GAC AAA GCT GGA CGT TGG TGA GAT CCC CTT TTA TGG GCA TGG 4176 Aβn * Asp Lys Ala Gly Arg Trp * Asp Pro Leu Leu Trp Ala Trp 1380 1385 1390 TAT CCC CCT CGA GCG TAT GAG-GAC TGG TCG CCA CCT TGT ATT CTG CCA 4224 Tyr Pro Pro Arg Ala Tyr Glu Asp Trp Ser Pro Pro Cys He Leu Pro 533 1395 1400 1405 TTC CAA GGC GGA GTG CGA GAG ATT GGC CGG CCA GTT CTC CGC GCG GGG 4272 Phe Gin Gly Gly Val Arg Glu He Gly Arg Pro Val Leu Arg Ala Gly 1410 1415 1420 GGT TAA TGC CAT CGC CTA TTA TAG GGG TAA GGA CAG TTC CAT CAT CAA 4320 Gly * Cyβ Hiβ Arg Leu Leu * Gly * Gly Gin Phe Hiβ Hie Gin 1425 1430 1435 1440 AGA CGG AGA CCT GGT GGT TTG TGC GAC AGA CGC GCT CTC TAC CGG GTA 4368 Arg Arg Arg Pro Gly Gly Leu Cyβ Aep Arg Arg Ala Leu Tyr Arg Val 1445 1450 1455 CAC AGG AAA CTT CGA TTC TGT CAC CGA CTG TGG GTT GGT GGT GGA GGA 4416 His Arg Lys Leu Arg Phe Cys Hie Arg Leu Trp Val Gly Gly Gly Gly 1460 1465 1470 GGT CGT TGA GGT GAC CCT TGA TCC CAC CAT TAC CAT TTC CTT GCG GAC 4464 Gly Arg * Gly Aep Pro * Ser Hie Hie Tyr His Phe Leu Ala Asp 1475 1480 1485 TGT CCC TGC TTC GGC TGA ATT GTC GAT GCA GCG GCG CGG ACG CAC GGG 4512 Cyβ Pro Cye Phe Gly * He Val Aep Ala Ala Ala Arg Thr Hiβ Gly 1490 1495 1500 GAG AGG TCG GTC GGG CCG CTA CTA CTA CGC TGG GGT CGG TAA GGC TCC 4560 Glu Arg Ser Val Gly Pro Leu Leu Leu Arg Trp Gly Arg * Gly Ser 1505 1510 1515 1520 CGC GGG GGT GGT GCG GTC TGG TCC GGT CTG GTC GGC AGT GGA AGC TGG 4608 Arg Gly Gly Gly Ala Val Trp Ser Gly Leu Val Gly Ser Gly Ser Trp 1525 1530 1535 AGT GAC CTG GTA TGG AAT GGA ACC TGA CTT GAC AGC AAA CCT TCT GAG 4656 Ser Asp Leu Val Trp Asn Gly Thr * Leu Asp Ser Lys Pro Ser Glu 1540 1545 1550 ACT TTA CGA CGA CTG CCC TTA CAC CGC AGC CGT CGC AGC TGA CAT TGG 4704 Thr Leu Arg Arg Leu Pro Leu His Arg Ser Arg Arg Ser * His Trp 1555 1560 1565 TGA AGC CGC GGT GTT CTT TGC GGG CCT CGC GCC CCT CAG GAT GCA TCC 4752 * Ser Arg Gly Val Leu Cys Gly Pro Arg Ala Pro Gin Asp Ala Ser 1570 1575 1580 CGA TGT TAG CTG GGC AAA AGT TCG CGG CGT CAA TTG GCC CCT CCT GGT 4800 Arg Cyβ * Leu Gly Lye Ser Ser Arg Arg Gin Leu Ala Pro Pro Gly 1585 1590 1595 1600 GGG TGT TCA GCG GAC GAT GTG TCG GGA AAC ACT GTC TCC CGG CCC GTC 4848 Gly Cys Ser Ala Asp Aep Val Ser Gly Aβn Thr Val Ser Arg Pro Val 1605 1610 1615 GGA CGA CCC TCA GTG GGC AGG TCT GAA AGG CCC GAA TCC TGT CCC ACT 4896 Gly Arg Pro Ser Val Gly Arg Ser Glu Arg Pro Glu Ser Cye Pro Thr 1620 1625 1630 534 ACT GCT GAG GTG GGG CAA TGA TTT GCC ATC AAA AGT GGC CGG CCA CCA 4944 Thr Ala Glu Val Gly Gin * Phe Ala He Lys Ser Gly Arg Pro Pro 1635 1640 1645 CAT AGT TGA CGA TCT GGT CCG TCG GCT CGG TGT GGC GGA GGG ATA CGT 992 His Ser * Arg Ser Gly Pro Ser Ala Arg Cys Gly Gly Gly He Arg 1650 1655 1660 GCG CTG TGA TGC TGG RCC CAT CCT CAT GGT GGG CTT GGC CAT AGC GGG 5040 Ala Leu * Cye Trp Xaa Hiβ Pro Hiβ Gly Gly Leu Gly Hiβ Ser Gly 1665 1670 1675 1680 CGG CAT GAT CTA CGC CTC TTA CAC TGG GTC GCT AGT GGT GGT AAC AGA 5088 Arg Hiβ Aep Leu Arg Leu Leu Hiβ Trp Val Ala Ser Gly Gly Aβn Arg 1685 1690 1695 CTG GGA TGT GAA GGG AGG TGG CAA TCC CCT TTA TAG GAG TGG TGA CCA 5136 Leu Gly Cye Glu Gly Arg Trp Gin Ser Pro Leu * Glu Trp * Pro 1700 1705 1710 GGC CAC CCC TCA ACC CGT GGT GCA GGT CCC CCC GGT AGA CCA TCG GCC 5184 Gly Hiβ Pro Ser Thr Arg Gly Ala Gly Pro Pro Gly Arg Pro Ser Ala 1715 1720 1725 GGG GGG GGA GTC TGC GCC ACG GGA TGC CAA GAC AGT GAC AGA TGC GGT 5232 Gly Gly Gly Val Cyβ Ala Thr Gly Cyβ Gin Asp Ser Asp Arg Cys Gly 1730 1735 1740 GGC AGC CAT CCA GGT GAA CTG CGA TTG GTC TGT GAT GAC CCT GTC GAT 5280 Gly Ser His Pro Gly Glu Leu Arg Leu Val Cys Asp Asp Pro Val Asp 1745 1750 1755 1760 CGG GGA AGT CCT CAC CTT GGC TCA GGC TAA GAC AGC CGA GGC CTA CGC 5328 Arg Gly Ser Pro Hiβ Leu Gly Ser Gly * Aep Ser Arg Gly Leu Arg 1765 1770 1775 AGC TAC TTC CAG GTG GCT CGC TGG CTG CTA CAC GGG GAC GCG GGC CGT 5376 Ser Tyr Phe Gin Val Ala Arg Trp Leu Leu Hie Gly Aep Ala Gly Arg 1780 1785 1790 CCC CAC TGT ATC AAT TGT TGA CAA GCT CTT CGC CGG GGG TTG GGC CGC 5424 Pro Hiβ Cyβ He Aβn Cye * Gin Ala Leu Arg Arg Gly Leu Gly Arg 1795 1800 1805 CGT GGT GGG TCA CTG TCA CAG CGT CAT TGC TGC GGC GGT GGC TGC CTA 5472 Arg Gly Gly Ser Leu Ser Gin Arg His Cys Cys Gly Gly Gly Cys Leu 1810 1815 1820 TGG AGC TTC TCG AAG TCC TCC ACT GGC CGC GGC GGC GTC CTA CCT CAT 5520 Trp Ser Phe Ser Lye Ser Ser Thr Gly Arg Gly Gly Val Leu Pro Hie 1825 1830 1835 1840 GGG GTT GGG CGT CGG AGG CAA CGC ACA GGC GCG CTT GGC TTC AGC TCT 5568 Gly Val Gly Arg Arg Arg Gin Arg Thr Gly Ala Leu Gly Phe Ser Ser 1845 1850 1855 TCT ACT GGG GGC TGC TGG TAC GGC TCT GGG GAC CCC TGT CGT GGG ACT 5616 535 Ser Thr Gly Gly Cys Trp Tyr Gly Ser Gly Asp Pro Cye Arg Gly Thr 1860 1865 1870 CAC CAT GGC GGG GGC CTT CAT GGG CGG TGC CAG CGT GTC CCC CTC CCT 5664 Hiβ Hiβ Gly Gly Gly Leu Hiβ Gly Arg Cys Gin Arg Val Pro Leu Pro 1875 1880 1885 CGT CAC TGT CCT ACT TGG GGC TGT GGG AGG TTG GGA GGG CGT TGT CAA 5712 Arg Hiβ Cyβ Pro Thr Trp Gly Cyβ Gly Arg Leu Gly Gly Arg Cyβ Gin 1890 1895 1900 CGC TGC CAG TCT CGT CTT CGA CTT CAT GGC TGG GAA ACT TTC AAC AGA 5760 Arg Cye Gin Ser Arg Leu Arg Leu Hiβ Gly Trp Glu Thr Phe Aβn Arg 1905 1910 1915 1920 AGA CCT TTG GTA TGC CAT CCC GGT ACT CAC TAG TCC TGG RGC GGG CCT 5808 Arg Pro Leu Val Cyβ His Pro Gly Thr His * Ser Trp Xaa Gly Pro 1925 1930 1935 CGC GGG GAT TGC CCT TGG TCT GGT TTT GTA CTC AGC AAA CAA CTC TGG 5856 Arg Gly Asp Cys Pro Trp Ser Gly Phe Val Leu Ser Lys Gin Leu Trp 1940 1945 1950 CAC TAC CAC ATG GCT GAA CCG TCT GCT GAC GAC GTT GCC ACG GTC ATC 5904 His Tyr His Met Ala Glu Pro Ser Ala Asp Asp Val Ala Thr Val He 1955 1960 1965 TTG CAT ACC CGA CAG CTA CTT CCA ACA GGC TGA CTA CTG CGA CAA GGT 5952 Leu His Thr Arg Gin Leu Leu Pro Thr Gly * Leu Leu Arg Gin Gly 1970 1975 1980 CTC GGC AAT CGT GCG CCG CCT GAG CCT TAC TCG CAC CGT GGT GGC CCT 6000 Leu Gly Asn Arg Ala Pro Pro Glu Pro Tyr Ser His Arg Gly Gly Pro 1985 1990 1995 2000 GGT CAA CAG GGA GCC TAA GGT GGA TGA GGT CCA GGT GGG GTA CGT CTG 6048 Gly Gin Gin Gly Ala * Gly Gly * Gly Pro Gly Gly Val Arg Leu 2005 2010 2015 GGA TCT GTG GGA GTG GGT GAT GCG CCA GGT GCG CAT GGT GAT GTC TAG 6096 Gly Ser Val Gly Val Gly Aep Ala Pro Gly Ala His Gly Aep Val * 2020 2025 2030 ACT CCG GGC CCT CTG CCC TGT GGT GTC ACT CCC CTT GTG GCA CTG CGG 6144 Thr Pro Gly Pro Leu Pro Cyβ Gly Val Thr Pro Leu Val Ala Leu Arg 2035 2040 2045 GGA GGG GTG GTC CGG TGA ATG GCT TCT CGA TGG GCA CGT GGA GAG TCG 6192 Gly Gly Val Val Arg * Met Ala Ser Arg Trp Ala Arg Gly Glu Ser 2050 2055 2060 TTG TCT GTG CGG GTG TGT AAT CAC CGG CGA CGT CCT CAA TGG GCA ACT 6240 Leu Ser Val Arg Val Cye Aβn Hiβ Arg Arg Arg Pro Gin Trp Ala Thr 2065 2070 2075 2080 CAA AGA TCC AGT TTA CTC TAC CAA GCT GTG CAG GCA CTA CTG GAT GGG -6288 Gin Arg Ser Ser Leu Leu Tyr Gin Ala Val Gin Ala Leu Leu Aep Gly 536 2085 2090 2095 AAC TGT GCC GGT CAA CAT GCT GGG CTA CGG GGA AAC CTC ACC TCT TCT 6336 Asn Cyβ Ala Gly Gin Hiβ Ala Gly Leu Arg Gly Aβn Leu Thr Ser Ser 2100 2105 2110 CGC CTC TGA CAC CCC GAA GGT GGT ACC CTT CGG GAC GTC GGG GTG GGC 6384 Arg Leu * Hiβ Pro Glu Gly Gly Thr Leu Arg Aep Val Gly Val Gly 2115 2120 2125 TGA GGT GGT GGT GAC CCC TAC CCA CGT GGT GAT CAG GCG CAC GTC CTG 6432 * Gly Gly Gly Aep Pro Tyr Pro Arg Gly Aep Gin Ala Hie Val Leu 2130 2135 2140 TTA CAA ACT GCT TCG CCA GCA AAT TCT TTC AGC AGC TGT AGC TGA GCC 6480 Leu Gin Thr Ala Ser Pro Ala Aβn Ser Phe Ser Ser Cyβ Ser * Ala 2145 2150 2155 2160 CTA CTA CGT TGA TGG CAT TCC GGT CTC TTG GGA GGC TGA CGC GAG AGC 6528 Leu Leu Arg * Trp Hie Ser Gly Leu Leu Gly Gly * Arg Glu Ser 2165 2170 2175 GCC GGC CAT GGT CTA CGG TCC GGG CCA AAG TGT TAC CAT TGA TGG GGA 6576 Ala Gly His Gly Leu Arg Ser Gly Pro Lys Cys Tyr Hiβ * Trp Gly 2180 2185 2190 GCG CTA CAC CCT TCC GCA CCA GTT GCG GAT GCG GAA TGT GGC GCC CTC 6624 Ala Leu Hiβ Pro Ser Ala Pro Val Ala Aep Ala Glu Cyβ Gly Ala Leu 2195 2200 2205 TGA GGT TTC ATC TGA GGT CAG CAT CGA GAT CGG GAC GGA GAC TGA AGA 6672 * Gly Phe He * Gly Gin His Arg Asp Arg Asp Gly Asp * Arg 2210 2215 2220 CTC AGA ACT GAC TGA GGC CGA TTT GCC ACC AGC GGC TGC TGC CCT CCA 6720 Leu Arg Thr Asp * Gly Arg Phe Ala Thr Ser Gly Cys Cys Pro Pro 2225 2230 2235 2240 AGC GAT AGA GAA TGC TGC GAG AAT TCT CGA ACC GCA CAT CGA TGT CAY 6768 Ser Asp Arg Glu Cys Cys Glu Aβn Ser Arg Thr Ala Hie Arg Cys Xaa 2245 2250 2255 CAT GGA GGA TTG CAG TAC ACC CTC TCT CTG TGG TAG TAG CCG AGA GAT 6816 His Gly Gly Leu Gin Tyr Thr Leu Ser Leu Trp * * Pro Arg Aep 2260 2265 2270 GCC TGT GTG GGG AGA AGA CAT ACC CCG CAC TCC ATC GCC TGC ACT TAT 6864 Ala Cyβ Val Gly Arg Arg Hiβ Thr Pro Hie Ser He Ala Cyβ Thr Tyr 2275 2280 2285 CTC GGT TAC GGA GAG CAG CTC AGA TGA GAA GAC CCT GTC GGT GAC CTC 6912 Leu Gly Tyr Gly Glu Gin Leu Arg * Glu Aep Pro Val Gly Aep Leu 2290 2295 2300 CTC GCA GGA GGA CAC CCC GTC CTC AGA CTC ATT TGA AGT CAT CCA AGA 6960 Leu Ala Gly Gly Hiβ Pro Val Leu Arg Leu He * Ser Hiβ Pro Arg 2305 2310 2315 2320 537 GTC TGA TAC TGC TGA ATC AGA GGA AAG CGT CTT CAA CGT GGC TCT TTC 7008 Val * Tyr Cys * He Arg Gly Lys Arg Leu Gin Arg Gly Ser Phe 2325 2330 2335 CGT ACT AAA AGC CTT ATT TCC ACA GAG CGA TGC CAC ACG AAA GCT AAC 7056 Arg Thr Lye Ser Leu He Ser Thr Glu Arg Cys Hiβ Thr Lye Ala Asn 2340 2345 2350 GGT TAA GAT GTC TTG CTG TGT TGA GAA GAG CGT AAC ACG CTT CTT TTC 7104 Gly * Aep Val Leu Leu Cyβ * Glu Glu Arg Aβn Thr Leu Leu Phe 2355 2360 2365 TTT AGG GTT GAC CGT GGC TGA CGT GGC TAG CCT GTG TGA GAT GGA GAT 7152 Phe Arg Val Aep Arg Gly * Arg Gly * Pro Val * Aep Gly Asp 2370 2375 2380 CCA GAA CCA TAC AGC CTA TTG TGA CAA GGT GCG CAC TCC GCT CGA ATT 7200 Pro Glu Pro Tyr Ser Leu Leu * Gin Gly Ala Hiβ Ser Ala Arg He 2385 2390 2395 2400 GCA AGT TGG GTG CTT GGT GGG CAA TGA ACT TAC CTT TGA ATG TGA CAA 7248 Ala Ser Trp Val Leu Gly Gly Gin * Thr Tyr Leu * Met * Gin 2405 2410 2415 GTG TGA GGC ACG CCA AGA GAC CCT TGC CTC CTT CTC CTA CAT ATG GTC 7296 Val * Gly Thr Pro Arg Aep Pro Cyβ Leu Leu Leu Leu Hiβ Met Val 2420 2425 2430 CGG GGT CCC ACT TAC TCG GGC CAC TCC GGC CAA ACC ACC AGT GGT GAG 7344 Arg Gly Pro Thr Tyr Ser Gly Hiβ Ser Gly Gin Thr Thr Ser Gly Glu 2435 2440 2445 GCC GGT GGG GTC CTT GTT GGT GGC AGA CAC CAC CAA GGT CTA CGT GAC 7392 Ala Gly Gly Val Leu Val Gly Gly Arg Hiβ Hiβ Gin Gly Leu Arg Aep 2450 2455 2460 CAA TCC GGA CAA TGT TGG GAG GAG GGT TGA CAA GGT GAC TTT CTG GCG 7440 Gin Ser Gly Gin Cyβ Trp Glu Glu Gly * Gin Gly Aep Phe Leu Ala 2465 2470 2475 2480 CGC TCC TCG GGT ACA CGA CAA GTT CCT CGT GGA CTC GAT CGA GCG CGC 7488 Arg Ser Ser Gly Thr Arg Gin Val Pro Arg Gly Leu Aep Arg Ala Arg 2485 2490 2495 TCG GAG AGC TGC TCA AGG CTG CCT AAG CAT GGG TTA CAC TTA TGA GGA 7536 Ser Glu Ser Cyβ Ser Arg Leu Pro Lye His Gly Leu Hie Leu * Gly 2500 2505 2510 GGC AAT AAG GAC TGT TAG GCC GCA TGC TGC CAT GGG CTG GGG ATC TAA 7584 Gly Aen Lys Aep Cyβ * Ala Ala Cye Cyβ Hiβ Gly Leu Gly He * 2515 2520 2525 GGT GTC GGT CAA GGA CTT GGC CAC CCC TGC GGG GAA GAT GGC TGT TCA 7632 Gly Val Gly Gin Gly Leu Gly Hiβ Pro Cyβ Gly Glu Aep Gly Cye Ser 2530 2535 2540 TGA CCG GCT TCA GGA GAT ACT TGA AGG GAC TCC GGT CCC TTT TAC CCT 7680 538 * Pro Ala Ser Gly Asp Thr * Arg Asp Ser Gly Pro Phe Tyr Pro 2545 2550 2555 2560 GAC TGT CAA AAA GGA GGT GTT CTT CAA AGA TCG TAA GGA GGA GAA GGC 7728 Asp Cys Gin Lye Gly Gly Val Leu Gin Arg Ser * Gly Gly Glu Gly 2565 2570 2575 CCC CCG CCT CAT TGT GTT CCC CCC CCT GGA CTT CCG GAT AGC TGA AAA 7776 Pro Pro Pro Hiβ Cye Val Pro Pro Pro Gly Leu Pro Aep Ser * Lye 2580 2585 2590 GCT CAT TCT GGG AGA CCC GGG GCG GGT TGC AAA GGC CGG TGT TGG GGG 7824 Ala Hiβ Ser Gly Arg Pro Gly Ala Gly Cyβ Lys Gly Arg Cys Trp Gly 2595 2600 2605 GGC TTA CGC CTT CCA GTA CAC CCC CAA CCA GCG GGT TAA GGA GAT GCT 7872 Gly Leu Arg Leu Pro Val Hie Pro Gin Pro Ala Gly * Gly Aep Ala 2610 2615 2620 AAA GCT GTG GGA ATC AAA GAA GAC CCC GTG CGC CAT CTG TGT GGA TGC 7920 Lys Ala Val Gly He Lys Glu Asp Pro Val Arg Hiβ Leu Cyβ Gly Cyβ 2625 2630 2635 2640 CAC TTG CTT CGA CAG TAG CAT TAC TGA RGA GGA CGT GGC ACT AGA GAC 7968 Hiβ Leu Leu Arg Gin * Hie Tyr * Xaa Gly Arg Gly Thr Arg Aep 2645 2650 2655 AGA GCT TTA CGC CCT GGC CTC GGA CCA TCC AGA ATG GGT GCG CGC CCT 8016 Arg Ala Leu Arg Pro Gly Leu Gly Pro Ser Arg Met Gly Ala Arg Pro 2660 2665 2670 GGG GAA ATA CTR TGC CTC TGG CAC AAT GGT GAC CCC GGA AGG GGT GCC 8064 Gly Glu He Xaa Cye Leu Trp Hiβ Aβn Gly Aep Pro Gly Arg Gly Ala 2675 2680 2685 AGT GGG CGA GAG GTA TTG TAG GTC CTC GGG TGT GTT GAC CAC AAG TGC 8112 Ser Gly Arg Glu Val Leu * Val Leu Gly Cye Val Aep Hiβ Lye Cye 2690 2695 2700 TAG CAA CTG TTT GAC CTG CTA CAT CAA AGT GAG AGC CGC CTG TGA GAG 8160 * Gin Leu Phe Aep Leu Leu Hiβ Gin Ser Glu Ser Arg Leu * Glu 2705 2710 2715 2720 GAT CGG ACT GAA AAA TGT CTC GCT TCT CAT CGC GGG CGA TGA CTG CTT 8208 Aep Arg Thr Glu Lye Cye Leu Ala Ser Hiβ Arg Gly Arg * Leu Leu 2725 2730 2735 AAT TGT GTG CGA GAG GCC TGT ATG CGA CCC TTG CGA GGC CCT GGG CCG 8256 Aβn Cyβ Val Arg Glu Ala Cyβ Met Arg Pro Leu Arg Gly Pro Gly Pro 2740 2745 2750 AAC CCT GGC TTC GTA CGG GTA CGC GTG TGA GCC CTC GTA TCA CGC TTC 8304 Aβn Pro Gly Phe Val Arg Val Arg Val * Ala Leu Val Ser Arg Phe 2755 2760 2765 ACT GGA CAC AGC CCC CTT CTG CTC CAC TTG GCT CGC TGA GTG CAA TGC 8352 Thr Gly Hiβ Ser Pro Leu Leu Leu Hiβ Leu Ala Arg * Val Gin Cyβ 539 2770 2775 2780 GGA TGG GRA AAG GCA TTT CTT CCT GAC CAC GGA CTT TCG GAG ACC ACT 8400 Gly Trp Xaa Lye Ala Phe Leu Pro Aep Hiβ Gly Leu Ser Glu Thr Thr 2785 2790 2795 2800 CGC TCG CAT GTC GAG CGA GTA CAG TGA CCC TAT GGC TTC GGC CAT TGG 8448 Arg Ser Hiβ Val Glu Arg Val Gin * Pro Tyr Gly Phe Gly Hiβ Trp 2805 2810 2815 TTA CAT TCT CCT CTA CCC CTG GCR TCC CAT CAC ACG GTG GGT CAT CAT 8496 Leu Hiβ Ser Pro Leu Pro Leu Xaa Ser Hiβ Hiβ Thr Val Gly Hie Hiβ 2820 2825 2830 CCC GCA TGT GCT AAC ATG CGC TTC TTC CCG GGG TGG TGG CAC ACS GTC 8544 Pro Ala Cyβ Ala Aen Met Arg Phe Phe Pro Gly Trp Trp Hie Xaa Val 2835 2840 2845 TGA TCC GGT TTG GTG TCA GGT TCA TGG TAA CTA CTA CAA GTT TCC CCT 8592 * Ser Gly Leu Val Ser Gly Ser Trp * Leu Leu Gin Val Ser Pro 2850 2855 2860 GGA CAA ACT GCC TAA CAT CAT CGT GGC CCT CCA CGG ACC AGC AGC GTT 8640 Gly Gin Thr Ala * Hiβ Hie Arg Gly Pro Pro Arg Thr Ser Ser Val 2865 2870 2875 2880 GAG GGT TAC CGC AGA CAC AAC CAA AAC AAA GAT GGA GGC TGG GAA GGT 8688 Glu Gly Tyr Arg Arg Hiβ Asn Gin Asn Lys Asp Gly Gly Trp Glu Gly 2885 2890 2895 TCT GAG CGA CCT CAA GCT CCC TGG TCT AGC CGT CCA CCG CAA GAA GGC 8736 Ser Glu Arg Pro Gin Ala Pro Trp Ser Ser Arg Pro Pro Gin Glu Gly 2900 2905 2910 CGG GGC ATT GCG AAC ACG CAT GCT CCG GTC GCG CGG TTG GGC GGA GTT 8784 Arg Gly He Ala Asn Thr His Ala Pro Val Ala Arg Leu Gly Gly Val 2915 2920 2925 GGC TAG GGG CCT GTT GTG GCA TCC AGG ACT CCG GCT TCC TCC CCC TGA 8832 Gly * Gly Pro Val Val Ala Ser Arg Thr Pro Ala Ser Ser Pro * 2930 2935 2940 GAT TGC TGG TAT CCC AGG GGG TTT CCC TCT GTC CCC CCC CTA CAT GGG 8880 Aep Cye Trp Tyr Pro Arg Gly Phe Pro Ser Val Pro Pro Leu Hiβ Gly 2945 2950 2955 2960 GGT GGT TCA TCA ATT GGA TTT CAC AGC SCA GCG GAG TCG CTG GCG GTG 8928 Gly Gly Ser Ser He Gly Phe Hiβ Ser Xaa Ala Glu Ser Leu Ala Val 2965 2970 2975 GTT GGG GTT CTT AGC CCT GCT CAT CGT AGC GCT CTT TGG GTG AAC TAA 8976 Val Gly Val Leu Ser Pro Ala Hiβ Arg Ser Ala Leu Trp Val Aβn * 2980 2985 2990 ATT CAT CTG TTG CGG CCG GAG TCA GAC CTG AGC CCC GTT CAA AAG GGG 9024 He Hiβ Leu Leu Arg Pro Glu Ser Aep Leu Ser Pro Val Gin Lye Gly 2995 3000 3005 540 ATT GAG AC 9032 He Glu 3010 (2) INFORMATION FOR SEQ ID NO:506: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 12 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:506: Arg Trp Trp Met Gly Asp Asp Arg Val Gly Arg Ser 1 5 10 (2) INFORMATION FOR SEQ ID NO:507: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 12 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:507: He Pro Val He Leu Val Ala Thr He Gly Gly Ser 1 5 10 (2) INFORMATION FOR SEQ ID NO:508: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 65 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:508: Gly Glu Ala Thr Val Pro Leu Ala Hie Met Glu Glu Lye Arg Thr Val 1 5 10 15 Hie Arg Cye Trp Ser Tyr Arg Cye Asn Lye Asp Pro Ala Leu Gly Thr 20 25 30 Pro Leu Asn Arg Ala Arg Tyr Ser Pro Gly Gin Thr Thr Pro Thr Tyr 35 40 45 Gly Pro Arg Arg Pro Ser Met Ser Leu Leu Thr Asn Arg Arg Thr Ala 50 55 60 Ser 65 (2) INFORMATION FOR SEQ ID NO:509: 541 (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 37 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:509: Gin Gly Pro Val Gly Ala Gly Arg Glu Gly Glu Gly Pro Pro Pro Leu 1 5 10 15 Pro Phe Pro Gly Arg Arg Glu Met Hiβ Gly Ala Thr Gin Leu Arg Gly 20 25 30 Gly Leu Gin Pro Gly 35 (2) INFORMATION FOR SEQ ID NO:510: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 5 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:510: Pro Lys Aen Phe Gly 1 5 (2) INFORMATION FOR SEQ ID NO:511: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 33 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:511: Gly Arg Val Ala Phe Leu Phe Leu Tyr Arg Ser Trp Gin Ser Phe Cys 1 5 10 15 Ser Tyr Ser Trp Trp Ser Arg Gly Tyr Phe Ser Pro Gly His Pro Cys 20 25 30 Leu (2) INFORMATION FOR SEQ ID NO:512: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 61 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein 542 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:512: Arg Glu Arg Ala He Phe Xaa His Lys Leu Leu Arg Pro Gly Gly His 1 5 10 15 Arg Leu Leu Pro Gly Gly Arg Met Pro Gly Gly Ser Gly Val His Hiβ 20 25 30 Leu His Arg Pro Leu Leu Ala Thr Val Ser Gly Gly Phe Gly Arg Ala 35 40 45 Ala Arg Gin Val Arg Arg Pro Val Gly Gly Gly Thr Arg 50 55 60 (2) INFORMATION FOR SEQ ID NO:513: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 47 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:513: Ser Leu Arg Ala Leu Val Gly Leu Gly Leu Cys Gly Arg Aep Pro Gly 1 5 10 15 Ala Trp Gly Gly Leu Leu Gly Gly Pro Hiβ Arg Arg Gly Gly Val Asp 20 25 30 Ala Gin Gly Leu Pro Gly Pro Glu Pro Aep Val Cyβ Ser Arg Val 35 40 45 (2) INFORMATION FOR SEQ ID NO:514: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 5 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:514: Val Glu Val Gly Lys 1 5 (2) INFORMATION FOR SEQ ID NO:514: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 5 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:514: 543 Val Leu Glu Met Asp 1 5 (2) INFORMATION FOR SEQ ID NO:515: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 73 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:515: Thr Ala Gly Leu Lye Leu Leu Aep Ser Gly He Pro Leu Glu Gly Ala 1 5 10 15 Phe Arg Leu Leu Ala Gly Ser Asp Glu Pro Tyr Ser Ser Leu Gly Val 20 25 30 Arg Gly Gly Pro Pro Pro Ala Gly Ala Ala Tyr Cyβ Hiβ Gly Leu Pro 35 40 45 Pro Gly His Tyr Gly Gly His Val Ala Arg Arg Ala Arg Leu Lys Cyβ 50 55 60 Trp Gly His Gly Leu Ser Arg Arg Val 65 70 (2) INFORMATION FOR SEQ ID NO:516: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 29 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:516: Leu Gly Ser Leu Val Leu Ala Gly Arg Thr Gly Pro Ala Cye Arg Gin 1 5 10 15 Gly Glu Gly Leu Gly Thr Trp Glu Arg His Thr Phe Val 20 25 (2) INFORMATION FOR SEQ ID NO:517: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 66 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:517: Leu Pro Gin Arg Ser Leu Gly Val Gly Pro Gly Pro Leu Pro Gly Asn 1 - 5 10 15 Arg Met Gly Arg Pro Tyr His Ser Leu Glu Pro Arg Thr Lye Ser Val 544 20 25 30 Ala Pro Phe Leu Ser Pro He Cys Leu Arg Arg Arg Phe Ser Asr Leu 35 40 45 Arg Val Gly Phe Cys Val Leu Val Cyβ Phe Hiβ Trp Gly Ser Arg Leu 50 55 60 Gin Gly 65 (2) INFORMATION FOR SEQ ID NO:518: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 26 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:518: Cyβ Val Glu Phe Gly Ser Ser Trp Leu Cye Gin Leu Hiβ Hie Ser Arg 1 5 10 15 Thr Gly He Phe Gly Ser Arg Hie Ser Gly 20 25 (2) INFORMATION FOR SEQ ID NO:519: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 51 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:519: Ala Leu Arg Val Gly Asn Ser Leu Arg Hiβ Leu Tyr Pro Gly Gin Ala 1 5 10 15 Ala Cye Leu Val Trp Hiβ Leu Cye Glu Gly Leu Leu Ala Arg Aep Arg 20 25 30 Val Gly Thr Phe Pro He Pro Gin Val Trp Arg Gly Thr Glu Ala Aep 35 40 45 Gin Arg Pro 50 (2) INFORMATION FOR SEQ ID NO:520: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 6 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION; SEQ ID NO:520: 545 Gly Cye Ala Leu Arg Gin 1 5 (2) INFORMATION FOR SEQ ID NO:521: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 47 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:521: Asp Asn Ser Leu His Hiβ Lys Gly Ala Pro Gly Gin Pro Gly Ala Arg 1 5 10 15 Gin Pro Gly Ala Val Ala Leu Gly Phe Trp Val Leu His His Asp Gin 20 25 30 Asp Pro Arg Leu Leu Thr Leu Gly Glu Met Ser His Pro Ser Hiβ 35 40 45 (2) INFORMATION FOR SEQ ID NO:522: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 15 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:522: Ala Ser Hie Arg Aen Val Trp Val Leu Pro Arg Ser Pro Pro Pro 1 5 10 15 (2) INFORMATION FOR SEQ ID NO:523: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 7 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:523: Gin Leu Hiβ Ala Ser Arg Hiβ 1 5 (2) INFORMATION FOR SEQ ID NO:524: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 44 amino acide 546 (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:524: Gly Val Arg Gly He Gly Trp Gly Gly Pro Hiβ Trp Gly Val Leu Arg 1 5 10 15 Thr Ser Gly Ala Ala Val Phe Arg Ala Asp Gly Ser Ala Glu Ser Gly 20 25 30 Leu Pro Gly Val Cyβ Met Ala Leu Phe Gly Thr Ala 35 40 (2) INFORMATION FOR SEQ ID NO:525: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 147 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:525: Trp Val Hiβ Thr Cye Ser Gly Pro Leu Ala Gly Gly Gly Cye Gly Gin 1 5 10 15 Leu His Ser Ala Pro Thr Leu Val Ala Leu Gly Leu Cys He Cye Pro 20 25 30 Val He Pro Aep Glu Ala Gly Arg Gly Thr Val Gly Pro Ala Aep Pro 35 40 45 Pro Pro Ala Met Val Val Gly Glu Pro Val Gly Gly Pro Xaa Cyε Xaa 50 55 60 Gly Cye Xaa Arg Arg Arg Gly Trp Arg Gly Val Cyβ Gly Pro Cyβ Leu 65 70 75 80 Val Leu Val Ser Gly Pro Thr Leu Arg Glu Tyr Aep Pro Gly Ala Ser 85 90 95 Lye Pro Gly Val Val Leu Pro Leu Aep Gly Ser Ser Thr Pro Aep Val 100 105 110 Pro Arg Val Val Glu Ala Arg Ser Gly Gly Phe Pro Ala Gly He Thr 115 120 125 Aep Gly Asp Phe Arg His Ser Arg Pro His Leu Cys Ala Trp Arg Arg 130 135 140 He Leu Leu 145 (2) INFORMATION FOR SEQ ID NO:526: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 11 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:526: 547 Ser Gly Hiβ Val Ser Leu Gly Leu Gly Gly Cyβ 1 5 10 (2) INFORMATION FOR SEQ ID NO:527: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:527: Cyβ Gly Gly Leu Gly Hiβ Ser Ala Pro Glu Leu Tyr Glu Arg Gly Gly 1 5 10 15 Val Glu Ala Gin Ser His Asn Leu 20 (2) INFORMATION FOR SEQ ID NO:528: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 11 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:528: Arg Val Pro Gly Xaa Ser Pro Ala Arg Gly Ala 1 5 10 (2) INFORMATION FOR SEQ ID NO:529: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 91 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:529: Pro Pro Arg Gly Gly Ala Ala Hie Gin Ala Ala Aep Aep Ser Leu Val 1 5 10 15 Ser Gly Leu Leu Hie Leu Ala Gly Arg Cye Aep Val Gly Gly Cyβ Gly 20 25 30 Hiβ Gly Pro Pro Leu Arg Pro Phe Arg Arg Ala Arg Leu Gly Leu Gly 35 40 45 Gly Ala Pro Cyβ Val Ala Ala Phe Val Ala Ser Phe Gly Lye Gly Gly 50 55 60 Gly Val Leu Cye Aep Gly Gly Arg Glu Gly Hie Tyr Arg Pro Ala Cyβ 65 70 75 80 548 Val Gin Asp Val Arg Glu Arg Gly Leu Pro Val 85 90 (2) INFORMATION FOR SEQ ID NO:530: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 26 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:530: Pro His Gly Val Val Leu Ala Arg Gly Gin Gly Ala Leu Ala Gly Val 1 5 10 15 Gly Arg Gly Phe Gly Xaa Pro Val He His 20 25 (2) INFORMATION FOR SEQ ID NO:531: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 26 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:531: Asp Gly Leu Ser His His Thr Arg Arg Arg Gin Aep Pro Glu Leu Arg 1 5 10 15 Pro Met Arg His Gly Leu Ala Arg Gly Gly 20 25 (2) INFORMATION FOR SEQ ID NO:532: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 35 amino acids (B)- TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (Xi) SEQUENCE DESCRIPTION: SEQ ID NO:532: Gly Pro Asp Trp Gly Leu Ser Gly Cys Glu Pro Leu Ala Ser Gly Val 1 5 10 15 Xaa Ser Tyr Ser Ala Cyβ Cye Hie Pro Ser Val Arg Lye Gly Leu Pro 20 25 30 Arg Gly Hie 35 (2) INFORMATION FOR SEQ ID NO:533: 549 (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:533: Gly Cye Leu Aep Trp Ser Gly Ser 1 5 (2) INFORMATION FOR SEQ ID NO:534: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 44 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:534: Leu Thr Pro Arg Lys Arg His Gly Phe Gly Asp Gly Tyr Leu Ala Gin 1 5 10 15 His Gly Asn Val Leu Lye Arg Val Ala Val Hie Aep He Pro Trp Gly 20 25 30 Phe Phe Pro Asn His Cys Aep Thr Cys Gly Gly Pro 35 40 (2) INFORMATION FOR SEQ ID NO:535: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 7 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:535: Pro Lye Val Val Val Gly Gin 1 5 (2) INFORMATION FOR SEQ ID NO:536: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 10 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:536: Arg Hiβ Gly Leu Ser Pro Pro Arg Trp Ser 550 1 5 10 (2) INFORMATION FOR SEQ ID NO : 537 : (i) SEQUENCE CHARACTERISTICS : (A) LENGTH : 9 amino acidβ (B) TYPE : amino acid (D) TOPOLOGY: linear ( ii) MOLECULE TYPE : protein (xi) SEQUENCE DESCRIPTION : SEQ ID NO : 537 : Leu Val Gly Ser Leu Leu Val Ser Gly 1 5 (2) INFORMATION FOR SEQ ID NO:538: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 30 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:538: Val Leu Leu Gly His Xaa He Arg Trp Gly Ser Leu Pro Trp Leu Glu 1 5 10 15 Gin Gly Gly Gin Gly Arg Thr Gly Arg Gly His Gly Gly Cys 20 25 30 (2) INFORMATION FOR SEQ ID NO:539: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 50 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:539: Leu Ser Trp Val Val Trp Val Ser Cys Pro Met Arg Arg Gly Ala Arg 1 5 10 15 Cys Arg Asn Ala Arg Val Arg Pro Ser Phe Gly Gly Glu Gly Asp Arg 20 25 30 Gly Ser He His Ser Ala Val Aep Pro Ser Pro Aen Arg Arg Gin Aep 35 40 45 Tyr Hie 50 (2) INFORMATION FOR SEQ ID NO:540: 551 (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 6 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:540: Ala Thr Pro Gly Ala Ser 1 5 (2) INFORMATION FOR SEQ ID NO:541: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 56 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:541: Arg Gly Phe Gin Arg Gly Ser Ser Phe His Ala Asn Arg Gly Gly Glu 1 5 10 15 Lys His Thr Arg Pro Phe Gly Val Trp Lys His Gly Ala Gin Gly Pro 20 25 30 Asp Ser Gin Pro Val Gly Cys His Cys Glu Gly His Gly Pro Leu Hiβ 35 40 45 Gly Glu Ala Gly Gly Glu Thr Ser 50 55 (2) INFORMATION FOR SEQ ID NO:542: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 42 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:542: Hiβ Phe Leu Trp Thr Arg His Asn Ser Phe Hiβ Thr Aep Hie Gly Leu 1 5 10 15 Ser He Aep Val Leu Tyr Leu Trp Glu Val Ser Gly Gin Pro Glu Ala 20 25 30 Aep Ala Glu Gly Ser Phe Arg Gly Hie Leu 35 40 (2) INFORMATION FOR SEQ ID NO:543: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acidβ 552 (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:543: Val Pro Gin Ser 1 (2) INFORMATION FOR SEQ ID NO:544: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 41 amino acide (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:544: Leu Asn Cye Val Ala Gly Tyr Arg Gin Gly Gin Gly Arg Gly Ala Gly 1 5 10 15 Val Trp Ser Ala He Ser Ala Leu Arg Tyr Cyβ Asp Ser Pro Gly Leu 20 25 30 Ala Tyr Asp Ser Ala Ser He His Aen 35 40 (2) INFORMATION FOR SEQ ID NO:545: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 6 amino acide (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:545: Aep Lye Ala Gly Arg Trp 1 5 (2) INFORMATION FOR SEQ ID NO:546: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 40 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:546: Asp Pro Leu Leu Trp Ala Trp Tyr Pro Pro Arg Ala Tyr Glu Asp Trp 1 5 10 15 Ser Pro Pro Cys He Leu Pro Phe Gin Gly Gly Val Arg Glu He Gly 553 20 25 30 Arg Pro Val Leu Arg Ala Gly Gly 35 40 (2) INFORMATION FOR SEQ ID NO:547: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 5 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:547: Cys His Arg Leu Leu 1 5 (2) INFORMATION FOR SEQ ID NO:548: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 40 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:548: Gly Gin Phe Hie Hiβ Gin Arg Arg Arg Pro Gly Gly Leu Cyβ Aep Arg 1 5 10 15 Arg Ala Leu Tyr Arg Val Hie Arg Lye Leu Arg Phe Cys His Arg Leu 20 25 30 Trp Val Gly Gly Gly Gly Gly Arg 35 40 (2) INFORMATION FOR SEQ ID NO:549: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 14 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:549: Ser His His Tyr His Phe Leu Ala Aep Cye Pro Cys Phe Gly 1 5 10 (2) INFORMATION FOR SEQ ID NO:550: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 23 amino acidβ 554 (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:550: He Val Asp Ala Ala Ala Arg Thr His Gly Glu Arg Ser Val Gly Pro 1 5 10 15 Leu Leu Leu Arg Trp Gly Arg 20 (2) INFORMATION FOR SEQ ID NO:551: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 26 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:551: Gly Ser Arg Gly Gly Gly Ala Val Trp Ser Gly Leu Val Gly Ser Gly 1 5 10 15 Ser Trp Ser Aep Leu Val Trp Aβn Gly Thr 20 25 (2) INFORMATION FOR SEQ ID NO:552: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:552: Leu Asp Ser Lys Pro Ser Glu Thr Leu Arg Arg Leu Pro Leu Hiβ Arg 1 5 10 15 Ser Arg Arg Ser 20 (2) INFORMATION FOR SEQ ID NO:553: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 17 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:553: Ser Arg Gly Val Leu Cys Gly Pro Arg Ala Pro Gin Asp Ala Ser Arg 1 5 10 15 555 Cys (2) INFORMATION FOR SEQ ID NO:554: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 51 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:554: Leu Gly Lys Ser Ser Arg Arg Gin Leu Ala Pro Pro Gly Gly Cye Ser 1 5 10 15 Ala Asp Asp Val Ser Gly Asn Thr Val Ser Arg Pro Val Gly Arg Pro 20 25 30 Ser Val Gly Arg Ser Glu Arg Pro Glu Ser Cys Pro Thr Thr Ala Glu 35 40 45 Val Gly Gin 50 (2) INFORMATION FOR SEQ ID NO:555: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 11 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:555: Phe Ala He Lys Ser Gly Arg Pro Pro His Ser 1 5 10 (2) INFORMATION FOR SEQ ID NO:556: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 15 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:556: Arg Ser Gly Pro Ser Ala Arg Cys Gly Gly Gly He Arg Ala Leu 1 5 10 15 (2) INFORMATION FOR SEQ ID NO:557: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 40 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear 556 (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:557: Cyβ Trp Xaa Hiβ Pro Hiβ Gly Gly Leu Gly Hiβ Ser Gly Arg Hiβ Aep 1 5 10 15 Leu Arg Leu Leu Hiβ Trp Val Ala Ser Gly Gly Aβn Arg Leu Gly Cyβ 20 25 30 Glu Gly Arg Trp Gin Ser Pro Leu 35 40 (2) INFORMATION FOR SEQ ID NO:558: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 58 amino acide (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:558: Pro Gly Hiβ Pro Ser Thr Arg Gly Ala Gly Pro Pro Gly Arg Pro Ser 1 5 10 15 Ala Gly Gly Gly Val Cye Ala Thr Gly Cys Gin Asp Ser Asp Arg Cys 20 25 30 Gly Gly Ser Hiβ Pro Gly Glu Leu Arg Leu Val Cye Aep Aep Pro Val 35 40 45 Aep Arg Gly Ser Pro Hiβ Leu Gly Ser Gly 50 55 (2) INFORMATION FOR SEQ ID NO:559: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 28 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:559: Aep Ser Arg Gly Leu Arg Ser Tyr Phe Gin Val Ala Arg Trp Leu Leu 1 5 10 15 Hie Gly Aep Ala Gly Arg Pro Hie Cye He Asn Cys 20 25 (2) INFORMATION FOR SEQ ID NO:560: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 131 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear 557 (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:560: Gin Ala Leu Arg Arg Gly Leu Gly Arg Arg Gly Gly Ser Leu Ser Gin 1 5 10 15 Arg His Cyβ Cyβ Gly Gly Gly Cyβ Leu Trp Ser Phe Ser Lys Ser Ser 20 25 30 Thr Gly Arg Gly Gly Val Leu Pro Hiβ Gly Val Gly Arg Arg Arg Gin 35 40 45 Arg Thr Gly Ala Leu Gly Phe Ser Ser Ser Thr Gly Gly Cyβ Trp Tyr 50 55 60 Gly Ser Gly Aep Pro Cye Arg Gly Thr His His Gly Gly Gly Leu His 65 70 75 80 Gly Arg Cys Gin Arg Val Pro Leu Pro Arg His Cys Pro Thr Trp Gly 85 90 95 Cys Gly Arg Leu Gly Gly Arg Cys Gin Arg Cys Gin Ser Arg Leu Arg 100 105 110 Leu His Gly Trp Glu Thr Phe Asn Arg Arg Pro Leu Val Cys His Pro 115 120 125 Gly Thr His 130 (2) INFORMATION FOR SEQ ID NO:561: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 47 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:561: Ser Trp Xaa Gly Pro Arg Gly Asp Cys Pro Trp Ser Gly Phe Val Leu 1 5 10 15 Ser Lys Gin Leu Trp His Tyr His Met Ala Glu Pro Ser Ala Asp Asp 20 25 30 Val Ala Thr Val He Leu His Thr Arg Gin Leu Leu Pro Thr Gly 35 40 45 (2) INFORMATION FOR SEQ ID NO:562: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 26 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:562: Leu Leu Arg Gin Gly Leu Gly Asn Arg Ala Pro Pro Glu Pro Tyr Ser 1 5 10 15 Hie Arg Gly Gly Pro Gly Gin Gin Gly Ala 20 25 558 (2) INFORMATION FOR SEQ ID NO:563: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 22 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:563: Gly Pro Gly Gly Val Arg Leu Gly Ser Val Gly Val Gly Asp Ala Pro 1 5 10 15 Gly Ala His Gly Asp Val 20 (2) INFORMATION FOR SEQ ID NO:564: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:564: Thr Pro Gly Pro Leu Pro Cys Gly Val Thr Pro Leu Val Ala Leu Arg 1 5 10 15 Gly Gly Val Val Arg 20 (2) INFORMATION FOR SEQ ID NO:565: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 60 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:565: Met Ala Ser Arg Trp Ala Arg Gly Glu Ser Leu Ser Val Arg Val Cys 1 5 10 15 Asn His Arg Arg Arg Pro Gin Trp Ala Thr Gin Arg Ser Ser Leu Leu 20 25 30 Tyr Gin Ala Val Gin Ala Leu Leu Aep Gly Aβn Cye Ala Gly Gin Hie 35 40 45 Ala Gly Leu Arg Gly Asn Leu Thr Ser Ser Arg Leu 50 55 60 (2) INFORMATION FOR SEQ ID NO:566: (i) SEQUENCE CHARACTERISTICS: 559 (A) LENGTH: 13 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:566: Hiβ Pro Glu Gly Gly Thr Leu Arg Aep Val Gly Val Gly 1 5 10 (2) INFORMATION FOR SEQ ID NO:567: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 29 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:567: Gly Gly Gly Aep Pro Tyr Pro Arg Gly Aep Gin Ala Hie Val Leu Leu 1 5 10 15 Gin Thr Ala Ser Pro Ala Aen Ser Phe Ser Ser Cyβ Ser 20 25 (2) INFORMATION FOR SEQ ID NO:568: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:568: Ala Leu Leu Arg 1 (2) INFORMATION FOR SEQ ID NO:569: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:569: Trp Hiβ Ser Gly Leu Leu Gly Gly 1 5 (2) INFORMATION FOR SEQ ID NO:570: 560 (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 16 amino acide (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:570: Arg Glu Ser Ala Gly Hiβ Gly Leu Arg Ser Gly Pro Lye Cye Tyr Hiβ 1 5 10 15 (2) INFORMATION FOR SEQ ID NO:571: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 18 amino acide (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:571: Trp Gly Ala Leu Hie Pro Ser Ala Pro Val Ala Aep Ala Glu Cyβ Gly 1 5 10 15 Ala Leu (2) INFORMATION FOR SEQ ID NO:572: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:572: Gly Gin His Arg Aep Arg Asp Gly Aep 1 5 (2) INFORMATION FOR SEQ ID NO:573: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 5 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:573: Arg Leu Arg Thr Asp 1 5 561 (2) INFORMATION FOR SEQ ID NO:574: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 38 amino acide (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:574: Gly Arg Phe Ala Thr Ser Gly Cye Cyβ Pro Pro Ser Aep Arg Glu Cyβ 1 5 10 15 Cyβ Glu Aβn Ser Arg Thr Ala Hiβ Arg Cys Xaa Hiβ Gly Gly Leu Gin 20 25 30 Tyr Thr Leu Ser Leu Trp 35 (2) INFORMATION FOR SEQ ID NO:575: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 27 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:575: Pro Arg Aep Ala Cyβ Val Gly Arg Arg Hiβ Thr Pro Hiβ Ser He Ala 1 5 10 15 Cyβ Thr Tyr Leu Gly Tyr Gly Glu Gin Leu Arg 20 25 (2) INFORMATION FOR SEQ ID NO:576: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 18 amino acide (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:576: Glu Aep Pro Val Gly Aep Leu Leu Ala Gly Gly Hie Pro Val Leu Arg 1 5 10 15 Leu He (2) INFORMATION FOR SEQ ID NO:577: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 5 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear 562 (ii) MOLECULE TYPE : protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 577 : Ser His Pro Arg Val 1 5 (2) INFORMATION FOR SEQ ID NO:578: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 28 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:578: He Arg Gly Lye Arg Leu Gin Arg Gly Ser Phe Arg Thr Lye Ser Leu 1 5 10 15 He Ser Thr Glu Arg Cys His Thr Lye Ala Aen Gly 20 25 (2) INFORMATION FOR SEQ ID NO:579: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 5 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:579: 1 5 (2) INFORMATION FOR SEQ ID NO:580: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 14 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:580: Glu Glu Arg Aβn Thr Leu Leu Phe Phe Arg Val Aep Arg Gly 1 5 10 (2) INFORMATION FOR SEQ ID NO:581: (i) SEQUENCE CHARACTERISTICS: 563 (A) LENGTH: 10 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:581: Asp Gly Aep Pro Glu Pro Tyr Ser Leu Leu 1 5 10 (2) INFORMATION FOR SEQ ID NO:582: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 16 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:582: Gin Gly Ala Hiβ Ser Ala Arg He Ala Ser Trp Val Leu Gly Gly Gin 1 5 10 15 (2) INFORMATION FOR SEQ ID NO:583: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 55 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:583: Gly Thr Pro Arg Asp Pro Cys Leu Leu Leu Leu His Met Val Arg Gly 1 5 10 15 Pro Thr Tyr Ser Gly Hiβ Ser Gly Gin Thr Thr Ser Gly Glu Ala Gly 20 25 30 Gly Val Leu Val Gly Gly Arg Hiβ Hie Gin Gly Leu Arg Aep Gin Ser 35 40 45 Gly Gin Cye Trp Glu Glu Gly 50 55 (2) INFORMATION FOR SEQ ID NO:584: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 36 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein 564 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:584: Gin Gly Asp Phe Leu Ala Arg Ser Ser Gly Thr Arg Gin Val Pro Arg 1 5 10 15 Gly Leu Asp Arg Ala Arg Ser Glu Ser Cye Ser Arg Leu Pro Lye Hiβ 20 25 30 Gly Leu Hie Leu 35 (2) INFORMATION FOR SEQ ID NO:585: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 6 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:585: 1 5 (2) INFORMATION FOR SEQ ID NO:586: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9 amino acide (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:586: Ala Ala Cyβ Cys His Gly Leu Gly He 1 5 (2) INFORMATION FOR SEQ ID NO:587: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 16 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:587: Gly Val Gly Gin Gly Leu Gly Hie Pro Cyβ Gly Glu Aep Gly Cye Ser 1 5 10 15 565 (2) INFORMATION FOR SEQ ID NO:588: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 6 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:588: Pro Ala Ser Gly Asp Thr 1 5 (2) INFORMATION FOR SEQ ID NO:589: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 19 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:589: Arg Aep Ser Gly Pro Phe Tyr Pro Aep Cyβ Gin Lye Gly Gly Val Leu 1 5 10 15 Gin Arg Ser (2) INFORMATION FOR SEQ ID NO:590: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 18 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:590: Gly Gly Glu Gly Pro Pro Pro Hiβ Cyβ Val Pro Pro Pro Gly Leu Pro 1 5 10 15 Aep Ser (2) INFORMATION FOR SEQ ID NO:591: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 29 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:591: 566 Lye Ala Hie Ser Gly Arg Pro Gly Ala Gly Cyβ Lye Gly Arg Cye Trp 1 5 10 15 Gly Gly Leu Arg Leu Pro Val Hiβ Pro Gin Pro Ala Gly 20 25 (2) INFORMATION FOR SEQ ID NO:592: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 amino acide (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:592: Gly Asp Ala Lye Ala Val Gly He Lye Glu Aep Pro Val Arg Hiβ Leu 1 5 10 15 Cyβ Gly Cyβ Hie Leu Leu Arg Gin 20 (2) INFORMATION FOR SEQ ID NO:593: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 45 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:593: Xaa Gly Arg Gly Thr Arg Asp Arg Ala Leu Arg Pro Gly Leu Gly Pro 1 5 10 15 Ser Arg Met Gly Ala Arg Pro Gly Glu He Xaa Cys Leu Trp His Asn 20 25 30 Gly Asp Pro Gly Arg Gly Ala Ser Gly Arg Glu Val Leu 35 40 45 (2) INFORMATION FOR SEQ ID NO:594: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:594: Val Leu Gly Cys Val Asp Hiβ Lye Cys 567 1 5 (2) INFORMATION FOR SEQ ID NO:595: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 13 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:595: Gin Leu Phe Asp Leu Leu Hie Gin Ser Glu Ser Arg Leu 1 5 10 (2) INFORMATION FOR SEQ ID NO:596: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 14 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:596: Glu Aep Arg Thr Glu Lye Cye Leu Ala Ser Hiβ Arg Gly Arg 1 5 10 (2) INFORMATION FOR SEQ ID NO:597: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 27 amino acide (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:597: Leu Leu Aen Cyβ Val Arg Glu Ala Cyβ Met Arg Pro Leu Arg Gly Pro 1 5 10 15 Gly Pro Aβn Pro Gly Phe Val Arg Val Arg Val 20 25 (2) INFORMATION FOR SEQ ID NO:598: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 18 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear 568 (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:598: Ala Leu Val Ser Arg Phe Thr Gly His Ser Pro Leu Leu Leu His Leu 1 5 10 15 Ala Arg (2) INFORMATION FOR SEQ ID NO:599: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 27 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:599: Val Gin Cyβ Gly Trp Xaa Lye Ala Phe Leu Pro Aep Hiβ Gly Leu Ser 1 5 10 15 Glu Thr Thr Arg Ser Hie Val Glu Arg Val Gin 20 25 (2) INFORMATION FOR SEQ ID NO:600: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 39 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:600: Pro Tyr Gly Phe Gly Hiβ Trp Leu Hiβ Ser Pro Leu Pro Leu Xaa Ser 1 5 10 15 His His Thr Val Gly His Hiβ Pro Ala Cyβ Ala Aβn Met Arg Phe Phe 20 25 30 Pro Gly Trp Trp Hiβ Xaa Val 35 (2) INFORMATION FOR SEQ ID NO:601: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:601: Ser Gly Leu Val Ser Gly Ser Trp 1 5 569 (2) INFORMATION FOR SEQ ID NO:602: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 10 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:602: Leu Leu Gin Val Ser Pro Gly Gin Thr Ala 1 5 10 (2) INFORMATION FOR SEQ ID NO:603: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 60 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:603: His Hiβ Arg Gly Pro Pro Arg Thr Ser Ser Val Glu Gly Tyr Arg Arg 1 5 10 15 Hie Aβn Gin Asn Lys Asp Gly Gly Trp Glu Gly Ser Glu Arg Pro Gin 20 25 30 Ala Pro Trp Ser Ser Arg Pro Pro Gin Glu Gly Arg Gly He Ala Asn 35 40 45 Thr His Ala Pro Val Ala Arg Leu Gly Gly Val Gly 50 55 60 (2) INFORMATION FOR SEQ ID NO:604: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 13 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:604: Gly Pro Val Val Ala Ser Arg Thr Pro Ala Ser Ser Pro 1 5 10 (2) INFORMATION FOR SEQ ID NO:605: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 47 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear 570 (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:605: Asp Cys Trp Tyr Pro Arg Gly Phe Pro Ser Val Pro Pro Leu His Gly 1 5 10 15 Gly Gly Ser Ser He Gly Phe His Ser Xaa Ala Glu Ser Leu Ala Val 20 25 30 Val Gly Val Leu Ser Pro Ala Hiβ Arg Ser Ala Leu Trp Val Aβn 35 40 45 (2) INFORMATION FOR SEQ ID NO:606: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 18 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:606: He Hiβ Leu Leu Arg Pro Glu Ser Aep Leu Ser Pro Val Gin Lye Gly 1 5 10 15 He Glu (2) INFORMATION FOR SEQ ID NO:607: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 36 baee pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:607: GCCGCTGAAT TCATGCCTTG TTATTTCTAC TCAAAC 36 (2) INFORMATION FOR SEQ ID NO:608: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 33 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:608: 571 GCCGCAGGAT CCTCGAACGA CCGCTCCTGC CAC 33 (2) INFORMATION FOR SEQ ID NO:609: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 34 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:609: GCCGCAGGAA TTCATGGCTT GGCTGTGGTT GCTG 34 (2) INFORMATION FOR SEQ ID NO:610: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 507 amino acidβ (B) TYPE: amino acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:610: Tyr Ser Thr Tyr Gly Met Tyr Leu Thr Gly Arg Cys Ser Arg Asn Tyr 1 5 10 15 Asp Val He He Cys Asp Glu Cys His Ala Thr Asp Arg Thr Thr Val 20 25 30 Leu Gly He Gly Lys Val Leu Thr Glu Ala Pro Ser Lye Asn Val Arg 35 40 45 Leu Val Val Leu Ala Thr Ala Thr Pro Pro Gly Val He Pro Thr Pro 50 55 60 Hie Ala Aβn He Thr Glu He Gin Leu Thr Aep Glu Gly Thr He Pro 65 70 75 80 Phe Hiβ Gly Lye Lye He Lye Glu Glu Aβn Leu Lye Lye Gly Arg Hie 85 90 95 Leu He Phe Glu Ala Thr Lye Lys His Cys Asp Glu Leu Ala Asn Glu 100 105 110 Leu Ala Arg Lys Gly He Thr Ala Val Ser Tyr Tyr Arg Gly Cys Aep 572 115 120 125 He Ser Lys Met Pro Glu Gly Asp Cys Val Val Val Ala Thr Asp Ala 130 135 140 Leu Cyβ Thr Gly Tyr Thr Gly Aep Phe Aep Ser Val Tyr Aep Cyβ Ser 145 150 155 160 Leu Met Val Glu Gly Thr Cye His Val Aep Leu Aep Pro Thr Phe Thr 165 170 175 Met Gly Val Arg Val Cys Gly Val Ser Ala He Val Lye Gly Gin Arg 180 185 190 Arg Gly Arg Thr Gly Arg Gly Arg Ala Gly He Tyr Tyr Tyr Val Aep 195 200 205 Gly Ser Cyβ Thr Pro Ser Gly Met Val Pro Glu Cyβ Aen He Val Glu 210 215 220 Ala Phe Aep Ala Ala Lye Ala Trp Tyr Gly Leu Ser Ser Thr Glu Ala 225 230 235 240 Gin Thr He Leu Aep Thr Tyr Arg Thr Gin Pro Gly Leu Pro Ala He 245 250 255 Gly Ala Asn Leu Asp Glu Trp Ala Asp Leu Phe Ser Met Val Aβn Pro 260 265 270 Glu Pro Ser Phe Val Aβn Thr Ala Lye Arg Thr Ala Asp Asn Tyr Val 275 280 285 Leu Leu Thr Ala Ala Gin Leu Gin Leu Cyβ Hiβ Gin Tyr Gly Tyr Ala 290 295 300 Ala Pro Asn Asp Ala Pro Arg Trp Gin Gly Ala Arg Leu Gly Lys Lys 305 310 315 320 Pro Cys Gly Val Leu Trp Arg Leu Asp Gly Cys Asp Ala Cyβ Pro Gly 325 330 335 Pro Glu Pro Ser Glu Val Thr Arg Tyr Gin Met Cys Phe Thr Glu Val 340 345 350 Asn Thr Ser Gly Thr Ala Ala Leu Ala Val Gly Val Gly Val Ala Met 355 360 365 Ala Tyr Leu Ala He Aep Thr Phe Gly Ala Thr Cye Val Arg Arg Cye 370 375 380 Trp Ser He Thr Ser Val Pro Thr Gly Ala Thr Val Ala Pro Val Val 385 390 395 400 Aep Glu Glu Glu He Val Glu Glu Cyβ Ala Ser Phe He Pro Leu Glu 405 410 415 Ala Met Val Ala Ala He Aep Lye Leu Lye Ser Thr He Thr Thr Thr 573 420 425 430 Ser Pro Phe Thr Leu Glu Thr Ala Leu Glu Lye Leu Aβn Thr Phe Leu 435 440 445 Gly Pro Hiβ Ala Ala Thr He Leu Ala He He Glu Tyr Cys Cys Gly 450 455 460 Leu Val Thr Leu Pro Aep Aen Pro Phe Ala Ser Cyβ Val Phe Ala Phe 465 470 475 480 He Ala Gly He Thr Thr Pro Leu Pro Hiβ Lye He Lye Met Phe Leu 485 490 495 Ser Leu Phe Gly Gly Ala He Ala Ser Lys Leu 500 505 (2) INFORMATION FOR SEQ ID NO:611: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 522 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:611: Cyβ Gin Lye Gly Tyr Lye Gly Pro Trp He Gly Ser Gly Met Leu Gin 1 5 10 15 Ala Arg Cys Pro Cys Gly Ala Glu Leu He Phe Ser Val Glu Aβn Gly 20 25 30 Phe Ala Lys Leu Tyr Lye Gly Pro Arg Thr Cyβ Ser Asn Tyr Trp Arg 35 40 45 Gly Ala Val Pro Val Asn Ala Arg Leu Cys Gly Ser Ala Arg Pro Asp 50 55 60 Pro Thr Asp Trp Thr Ser Leu Val Val Asn Tyr Gly Val Arg Aep Tyr 65 70 75 80 Cys Lys Tyr Glu Lye Leu Gly Aep Hiβ He Phe Val Thr Ala Val Ser 85 90 95 Ser Pro Aβn Val Cyβ Phe Thr Gin Val Pro Pro Thr Leu Arg Ala Ala 100 105 110 Val Ala Val Aep Arg Val Gin Val Gin Xaa Tyr Leu Gly Glu Pro Lye 115 120 125 Thr Fro Trp Thr Thr Ser Ala Cyβ Cyβ Tyr Gly Pro Aep Gly Lys Gly 130 135 140 574 Lye Thr Val Lye Leu Pro Phe Arg Val Aep Gly Hie Thr Pro Gly Gly 145 150 155 160 Arg Met Gin Leu Aβn Leu Arg Aep Arg Leu Glu Ala Aen Aep Cye Aβn 165 170 175 Ser He Aen Aβn Thr Pro Ser Aep Glu Ala Ala Val Ser Ala Leu Val 180 185 190 Phe Lye Gin Glu Leu Arg Arg Thr Aen Gin Leu Leu Glu Ala He Ser 195 200 205 Ala Gly Val Aep Thr Thr Lye Leu Pro Ala Pro Ser Gin He Glu Glu 210 215 220 Val Val Val Arg Lye Arg Gin Phe Arg Ala Arg Thr Gly Ser Leu Thr 225 230 235 240 Leu Pro Pro Pro Pro Arg Ser Val Pro Gly Val Ser Cyβ Pro Glu Ser 245 250 255 Leu Gin Arg Ser Aep Pro Leu Glu Gly Pro Ser Xaa Leu Pro Ser Ser 260 265 270 Pro Pro Val Leu Gin Leu Ala Met Pro Met Pro Leu Leu Gly Ala Gly 275 280 285 Glu Cye Aen Pro Phe Thr Ala He Gly Cye Ala Met Thr Glu Thr Xaa 290 295 300 Gly Xaa Pro Xaa Xaa Leu Pro Ser Tyr Pro Pro Lye Lye Glu Val Ser 305 310 315 320 Glu Trp Ser Aep Glu Ser Trp Ser Thr Thr Thr Thr Ala Ser Ser Tyr 325 330 335 Val Thr Gly Pro Pro Tyr Pro Lye He Arg Gly Lye Aep Ser Thr Gin 340 345 350 Ser Ala Thr Ala Lye Arg Pro Thr Lye Lys Lye Leu Gly Lye Ser Glu 355 360 365 Phe Ser Cye Ser Met Ser Tyr Thr Trp Thr Aep Val He Ser Phe Lye 370 375 380 Thr Ala Ser Lye Val Leu Ser Ala Thr Arg Ala He Thr Ser Gly Phe 385 390 395 400 Leu Lye Gin Arg Ser Leu Val Tyr Val Thr Glu Pro Arg Aep Ala Glu 405 410 415 Leu Arg Lye Gin Lye Val Thr He Aβn Arg Gin Pro Leu Phe Pro Pro 420 425 430 Ser Tyr Hiβ Lye Gin Val Arg Leu Ala Lye Glu Lye Ala Ser Lye Val 435 - 440 445 575 Val Gly Val Met Trp Aep Tyr Aep Glu Val Ala Ala Hiβ Thr Pro Ser 450 455 460 Lye Ser Ala Lye Ser Hie He Thr Gly Leu Arg Gly Thr Aep Val Leu 465 470 475 480 Aep Leu Gin Lye Cyβ Val Glu Ala Gly Glu He Pro Ser Hiβ Tyr Arg 485 490 495 Gin Thr Val He Val Pro Lye Glu Glu Val Phe Val Lye Thr Pro Gin 500 505 510 Lye Pro Thr Lye Lys Pro Pro Arg Leu He 515 520 (2) INFORMATION FOR SEQ ID NO:612: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 118 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:612: Met Pro Val He Ser Thr Gin Thr Ser Pro Val Pro Ala Pro Arg Thr 1 5 10 15 Arg Lys Aen Lye Gin Thr Gin Ala Ser Tyr Pro Val Ser He Lye Thr 20 25 30 Ser Val Glu Arg Gly Gin Arg Ala Xaa Arg Lye Val Gin Arg Aep Ala 35 40 45 Arg Pro Arg Aβn Tyr Lye He Ala Gly He Hie Aep Gly Leu Gin Thr 50 55 60 Leu Ala Gin Ala Ala Leu Pro Ala Hie Gly Trp Gly Arg Gin Aep Pro 65 70 75 80 Arg Hiβ Lye Ser Arg Aβn Leu Gly He Leu Leu Aep Tyr Pro Leu Gly 85 90 95 Trp He Gly Aep Val Thr Thr Hiβ Thr Pro Leu Val Gly Pro Leu Val 100 105 110 Ala Gly Ala Val Val Arg 115 (2) INFORMATION FOR SEQ ID NO:613: (i) SEQUENCE CHARACTERISTICS:^ " - (A) LENGTH: 118 amino acidβ 576 (B) TYPE: amino acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:613: Gly Ser Gly Trp Thr Asp Glu Asp Glu Arg Asp Leu Val Glu 1 5 10 15 Thr Lys Ala Ala Ala He Glu Ala He Gly Ala Ala Leu Hiβ Leu Pro 20 25 30 Ser Pro Glu Ala Ala Gin Ala Ala Leu Glu Ala Leu Glu Glu Ala Ala 35 40 45 50 Val Ser Leu Leu Pro Hie Val Pro Val He Met Gly Aep Aep Cyβ Ser 55 60 65 70 Cyβ Arg Aep Glu Ala Phe Gin Gly Hie Phe He Pro Glu Pro Aen Val 75 80 85 Thr Glu Val Pro He Glu Pro Thr Val Gly Aep Val Glu Ala Leu Lye 90 95 100 Leu Arg Ala Ala Aep Leu Thr Ala Arg Leu Gin Aep Leu Glu Ala Met 105 110 115 Ala Leu Ala Arg Ala Glu Ser He Glu Aep Ala Arg Ala Ala Ser Met 120 125 130 Pro Ser Leu Thr Glu Val Aep Ser Met Pro Ser Leu Glu Ser Ser Pro 135 140 145 150 Cyβ Ser Ser Phe Glu Gin He Ser Leu Thr Glu Ser Aep Pro Glu Thr 155 160 165 Val Val Glu Ala Gly Xaa Pro Leu Glu Phe Val Aβn Ser Aβn Thr Gly 170 175 180 Xaa Ser Pro Ala Arg Arg He Val Arg He Arg Gin Ala Cyβ Cyβ Cyβ 185 190 195 Aep Arg Ser Thr Met Lye Ala Met Pro Leu Ser Phe Thr Val Gly Glu 200 205 210 215 Cyβ Leu Phe Val Thr Arg Tyr Aep Pro Aep Gly Hiβ Gin Leu Phe Aep 220 225 230 Glu Arg Gly Pro He Glu Val Ser Thr Pro He Cyβ Glu Val He Gly 235 240 245 Aep He Arg Leu Gin Cye Aep Gin He Glu Glu Thr Pro Thr Ser Tyr 250 255 260 577 Ser Tyr He Trp Ser Gly Ala Pro Leu Gly Thr Gly Arg Ser Val Pro 265 270 275 Gin Pro Met Thr Arg Pro He Gly Thr His Leu Thr Cyβ Aep Thr Thr 280 285 290 295 Lye Val Tyr Val Thr Aep Pro Asp Arg Ala Ala Glu Arg Ala Glu Lys 300 305 310 Val Thr He Trp Arg Gly Asp Arg Lye Tyr Aep Lye Hiβ Tyr Glu Ala 315 320 325 Val Val Glu Ala Val Leu Lye Lye Ala Ala Ala Thr Lys Ser His Gly 330 335 340 Trp Thr Tyr Ser Gin Ala He Ala Lys 345 350 (2) INFORMATION FOR SEQ ID NO:614: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 222 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO:614: Tyr Ser Gin Ala He Ala Lye Val Arg Arg Arg Ala Ala Ala Gly Tyr 1 5 10 15 Gly Ser Lye Val Thr Ala Ser Thr Leu Ala Thr Gly Trp Pro Hiβ Val 20 25 30 Glu Glu Met Leu Aep Lye He Ala Arg Gly Gin Glu Val Pro Phe Thr 35 40 45 Phe Val Thr Lye Arg Glu Val Phe Phe Ser Lye Thr Thr Arg Lye Pro 50 55 60 Pro Arg Phe He Val Phe Pro Pro Leu Aep Phe Arg He Ala Glu Lye 65 70 75 80 Met He Leu Gly Aep Pro Gly He Val Ala Lye Ser He Leu Gly Aep 85 90 95 Ala Tyr Leu Phe Gin Tyr Thr Pro Aen Gin Arg Val Lye Ala Leu Val 100 105 HO Lye Ala Trp Glu Gly Lye Leu Hiβ Pro Ala Ala He Thr Val Xaa Ala 115 120 125 Thr Cyβ Phe Aep Ser Ser He Asp Glu His Asp Met Gin Val Glu Ala 578 130 135 140 Ser Val Phe Ala Ala Ala Ser Asp Asn Pro Ser Met Val His Ala Leu 145 150 155 160 Cys Lys Tyr Tyr Ser Gly Gly Pro Met Val Ser Pro Asp Gly Val Pro 165 170 175 Leu Gly Tyr Arg Gin Cys Arg Ser Ser Gly Val Leu Thr Thr Ser Ser 180 185 190 Ala Asn Ser He Thr Cyβ Tyr He Lye Val Ser Ala Ala Cyβ Arg Arg 195 200 205 Val Gly He Lye Ala Pro Ser Phe Phe He Ala Gly Aep Asp 210 215 220 (2) INFORMATION FOR SEQ ID NO:615: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 34 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:615: GGGGCCGAAT TCTACAGCAC ATATGGCATG TAC 33 (2) INFORMATION FOR SEQ ID' NO:616: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH:38 base paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:616: GGGGAAAAGC TTATTAGTGT TTTTTGGTAG CCTCAAAG 38 (2) INFORMATION FOR SEQ ID NO:617: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH:34 baee paire (B) TYPE: nucleic acid 579 (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID N0:617: GGGGCCGAAT TCATCTTTGA GGCTACCAAA AAAC 34 (2) INFORMATION FOR SEQ ID NO:618: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 38 baee paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:618: GGGGAAAAGC TTATTAATAG TAGTATATGC CAGCTCTC 38 (2) INFORMATION FOR SEQ ID NO:619: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 33 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:619: GGGGCCGAAT TCGGGAGAGC TGGCATATAC TAC 33 (2) INFORMATION FOR SEQ ID NO:620: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 35 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) 580 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:620: GGGGAAAAGC TTATTAGTCAT TGGGAGCAGCA TAGCC 35 (2) INFORMATION FOR SEQ ID NO:621: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 34 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:621: GGGGCCGAAT TCTATGGCTA TGCTGCTCCC AATG 34 (2) INFORMATION FOR SEQ ID NO:622: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 36 baee pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:622: GGGGAAAAGC TTATTATGCAC ACTCCTCCAC GATTTC 36 (2) INFORMATION FOR SEQ ID NO:623: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 33 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:623: GGGGCCGAAT TCGAGGAAAT CGTGGAGGAG TGT 33 (2) INFORMATION FOR SEQ ID NO:624: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 37 base pairs (B) TYPE: nucleic acid 581 (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:624: GGGGAAAAGC TTATTACTTG GACGCAATTG CGCCTCC 37 (2) INFORMATION FOR SEQ ID NO:6.25: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 33 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:625: GGGGCCGAAT TCTCAGCAAT AGTTAAAGGC CAG 33 (2) INFORMATION FOR SEQ ID NO:626: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 38 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:626: GGGGAAAAGC TTATTAATTT GCTCCTATCG CAGGTAAC 38 (2) INFORMATION FOR SEQ ID NO:627: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 32 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:627: 582 GGGGCCGAAT TCCCTGGGTTA CCTGCGATAG GA 32 (2) INFORMATION FOR SEQ ID NO:628: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 38 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:628: GGGGAAAAGC TTATTACAGA ACCCCACAAG GTTTTTTC 38 (2) INFORMATION FOR SEQ ID NO:629: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 33 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:629: GGGGAAGAAT TCTGCCAGAA GGGGTACAAG GGC 33 (2) INFORMATION FOR SEQ ID NO:630: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 36 base paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:630: GGAAAAGGAT CCTTAACAGC AAGCAGATGT CGTCCA 36 (2) INFORMATION FOR SEQ ID NO:631: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 32 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear 583 (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:631: GGGGAAGAAT TCACTCCTTG GACGACATCTG CT 32 (2) INFORMATION FOR SEQ ID NO:632: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 36 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:632: GGAAAAGGAT CCTTAACCTT CTAACGGGTC ACTTCG 36 (2) INFORMATION FOR SEQ ID NO:633: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 33 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:633: GGGGAAGAAT TCCTGCAACG AAGTGACCCG TTA 33 (2) INFORMATION FOR SEQ ID NO:634: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 36 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:634: GGGGAAGGAT CCTTAAGTTG CAGACAGAAC TTTAGA 36 (2) INFORMATION FOR SEQ ID NO:635: 584 (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 33 baee paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:635: GGGGCCGAAT TCACTGCTTC TAAAGTTCTG TCT 33 (2) INFORMATION FOR SEQ ID NO:636: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 36 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:636: GGAAAAGGAT CCTTAGATAA GCCTTGGGGG TTTCTT 36 (2) INFORMATION FOR SEQ ID NO:637: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 32 baβe pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:637: GGGGAAGAAT TCTACGGTCC TGACGGTAAGG GT 32 (2) INFORMATION FOR SEQ ID NO:638: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 35 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) 585 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:638: GGAAAAGGAT CCTTAGTCAA CGCCAGCTGAA ATTGC 35 (2) INFORMATION FOR SEQ ID NO:639: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 32 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:639: GGGGAAGAATT CCTTGAGGCA ATTTCAGCTG GC 32 (2) INFORMATION FOR SEQ ID NO:640: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 36 baβe pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:640: GGAAAAGGAT CCTTACAACT GCAGAACAGG TGGTGA 36 (2) INFORMATION FOR SEQ ID NO:641: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 33 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:641: GGAAAAGGAT CCAGTGACGC TTGGTGCCTG GTC 33 (2) INFORMATION FOR SEQ ID NO:642: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 34 base paire (B) TYPE: nucleic acid 586 (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:642: GGGGAAAAGC TTAAAGTTTA TTGTACAGGA ACCG 34 (2) INFORMATION FOR SEQ ID NO:643: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 33 base paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:643: GGGGAAGAAT TCCGGCTAGG TCGGTTCCTG TAC 33 (2) INFORMATION FOR SEQ ID NO:644: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 36 baee paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:644: GGAAAAGGAT CCTTATGTCC CATGCACGAC CACAGC 36 (2) INFORMATION FOR SEQ ID NO:645: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 33 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:645: 587 GGGGAAGAAT TCTGGTTTGA GGCTGTGGTC GTG 33 (2) INFORMATION FOR SEQ ID NO:646: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 35 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:646: GGAAAAGGAT CCTTACAAGGC CGCCCCAATG GCCTC 35 (2) INFORMATION FOR SEQ ID NO:647: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 32 baee pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:647: GGGGAAGAAT TCGCCGCCAT CGAGGCCATTG GG 32 (2) INFORMATION FOR SEQ ID NO:648: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 37 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:648: GGAAAAGGAT CCTTACACCT CGGTGAGCGA AGGCATC 3 (2) INFORMATION FOR SEQ ID NO:649: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 33 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear 588 (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:649; GGGGAAGAAT TCGCAGCTTC GATGCCTTCG CTC 33 (2) INFORMATION FOR SEQ ID NO:650: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 38 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:650: GGAAAAGGAT CCTTAAATCA CTTCACATAT AGGAGTAG 38 (2) INFORMATION FOR SEQ ID NO:651: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 33 baβe pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:651: GGGGAAGAAT TCGAGGTATC TACTCCTATAT GTG 33 (2) INFORMATION FOR SEQ ID NO:652: (I) SEQUENCE CHARACTERISTICS: (A) LENGTH: 36 baβe pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:652: GGAAAAGGAT CCTTATTTAGC TATAGCCTGG GAATAG 36 589 (2) INFORMATION FOR SEQ ID NO:653: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:653: CATCAGCTCT GAACACCGCC GCAC 24 (2) INFORMATION FOR SEQ ID NO:654: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 25 baee pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:654: GCCGAGAAGC ATGCAGTTGT TAAGG 25 (2) INFORMATION FOR SEQ ID NO:655: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 22 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:655: GCCAGCTGTT CAGTCCATCT CC 22 (2) INFORMATION FOR SEQ ID NO:656: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 base paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) 590 (xi) SEQUENCE DESCRIPTION : SEQ ID NO: 656 : CTCTACTGCA CACGTCAGGT TCGG 24 (2) INFORMATION FOR SEQ ID NO:657: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 baee paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:657; CCAGAGCCAC CAGGCATCCG C 21 (2) INFORMATION FOR SEQ ID NO:658: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 25 baβe pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:658: CAGGCAGAAG CCTATGTCCT CCAGG 25 (2) INFORMATION FOR SEQ ID NO:659: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:659: GTGGTAGTAG CCGAGAGATG CCTG 24 (2) INFORMATION FOR SEQ ID NO:660: (i) SEQUENCE CHARACTERISTICS: 591 (A) LENGTH: 25 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:660: CACTCCATCG CCTGCACTTA TCTCG 25 (2) INFORMATION FOR SEQ ID NO:661: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 25 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:661: CTCGAATTGC AAGTTGGGTG CTTGG 25 (2) INFORMATION FOR SEQ ID NO:662: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 23 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:662: GAATGTGACA AGTGTGAGGC ACG 23 (2) INFORMATION FOR SEQ ID NO:663: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:663: 592 GGAGATGCTA AAGCTGTGGG AATC 24 (2) INFORMATION FOR SEQ ID NO:664: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:664: GAGGACGTGG CACTAGAGAC AGAG 24 (2) INFORMATION FOR SEQ ID NO:665: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 34 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:665: CAGTTCAAGC TTGTCCAGGA ATTCNNNNNG CGCA 34 (2) INFORMATION FOR SEQ ID NO:666: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 25 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:666: GCTTCGGCCA TTGGTTACAT TCTCC 666 (2) INFORMATION FOR SEQ ID NO:667: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 baee paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double 593 (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:667: GGTCATCATC CCGCATGTGC TAAC 24 (2) INFORMATION FOR SEQ ID NO:668: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:668: GGGATTTAGG ACCAAGACCT C 21 (2) INFORMATION FOR SEQ ID NO:669: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 23 base paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:669: CCAAAAGTCG AAAGGCACCT TCC 23 (2) INFORMATION FOR SEQ ID NO:670: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 22 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:670: CAACCGTGCC TCTGCCAGCT TC 22 (2) INFORMATION FOR SEO ID NO:671: 594 (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (Xi) SEQUENCE DESCRIPTION: SEQ ID NO:671: TYGCYACKGC KACCCCHCCK G 21 (2) INFORMATION FOR SEQ ID NO:672: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 19 baee paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:672: TGCCMGCTYT CCCMCKGCC 19 (2) INFORMATION FOR SEQ ID NO:673: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 5091 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:673: TACGTTTGGG TTCTTCCCAG GAGTCCCCCC CCTTAACAAC TGCATGCTTC GGTGTCAGAG GTATTGGGTG GGGCGGGCCT CACTGGGGGG TTTTACGAAC GCGGTGTTCA GAGCTGATGG GTCGGCGGAA TCCGGTCTGC CCGGGGTTTG TTCGGGACGG CCTGATGGGT TCATACATGT TCAGGGCCAC TTGCAGGAGG CAACTTCATT CCGCCCCCAC GCTGGTTGCT CTTGGACTTT GTATTTGTCC GATGAAGCTG GCAGAGGCAC GGTTGGTCCC GCTGATCCTC CTCCTGCTAT 595 GAACCAGTTG GCGGTCCTTG KTGTGSCGGC TGCKCRCGCC GCCGTGGCTG GAGAGGTGTT 420 TGCGGGCCCT GCCTTGTCCT GGTGTCTGGG CCTACCCTTC GTGAGTATGA TCCTGGGGCT 480 AGCAAACCTG GTGTTGTACT TCCGCTGGAT GGGTCCTCAA CGCCTGATGT TCCTCGTGTT 540 GTGGAAGCTC GCTCGGGGGG CTTTCCCGCT GGCATTACTG ATGGGGATTT CCGCCACTCG 600 CGGCCGCACC TCTGTGCTTG GCGCCGAATT CTGCTTTGAT GTCACCTTTG AAGTGGACAC 660 GTCAGTCTTG GGTTGGGTGG TTGCTAGTGT GGTGGCTTGG GCCATAGCGC TCCTGAGCTC 720 TATGAGCGCG GGGGGGTGGA AGCACAAAGC CATAATCTAT AGGACGTGGT GTAAAGGGTA 780 CCAGGCYCTT CGCCAGCGCG TGGTGCGTAG CCCCCTCGGG AGGGGCGGCC CACCAAGCCG 840 CTGACGATAR GCCTGGTGTC TGGCCTCTTA CATCTGGCCG GACGCTGTGA TGTTGGTGGT 900 TGTGGCCATG GTCCTCCTCT TCGGCCTTTT CGACGCGCTC GATTGGGCCT TGGAGGAGCT 960 CCTTGTGTCG CGGCCTTCGT TGCGTCGTTT GGCAAGGGTG GTGGAGTGTT GTGTGATGGC 1020 GGGCGAGAAG GCCACTACCG TCCGGCTTGT GTCCAAGATG TGCGCGAGAG GGGCCTACCT 1080 GTTTGACCAC ATGGGGTCGT TCTCGCGCGC GGTCAAGGAG CGCTTGCTGG AGTGGGACGC 1140 GGCTTTGGAG MCCCTGTCAT TCACTAGGAC GGACTGTCGC ATCATACGAG ACGCCGCCAG 1200 ACCCTGAGCT GCGGCCAATG CGTCATGGGC TTGCGTGGTG GCTAGGCGCG GCGATGAGGT 1260 CCTGATTGGG GTCTTTCAGG ATGTGAACCA CTTGCCTCCG GGGTTTGYTC CTACAGCGCC 1320 TGTTGTCATC CGTCGGTGCG GAAAGGGCTT CCTCGGGGTC ACTAAGGCTG CCTTGACTGG 1380 TCGGGATCCT GACTTACACC CAGGAAACGT CATGGTTTTG GGGACGGCTA CCTCGCGCAG 1440 CATGGGAACG TGCTTAAACG GGTTGCTGTT CACGACATTC CATGGGGCTT CTTCCCGAAC 1500 CATTGCGACA CCTGTGGGGG CCCTTAACCC AAGGTGGTGG TCGGCCAGTG ATGACGTCAC 1560 GGTCTATCCC CTCCCCGATG GAGCTAACTC GTTGGTTCCC TGCTCGTGTC AGGCTGAGTC 1620 CTGTTGGGTC ATYCGATCCG ATGGGGCTCT TTGCCATGGC TTGAGCAAGG GGGACAAGGT 1680 AGAACTGGAC GTGGCCATGG AGGTTGCTGA CTTTCGTGGG TCGTCTGGGT CTCCTGTCCT 1740 ATGCGACGAG GGGCACGCTG TAGGAATGCT CGTGTCCGTC CTTCATTCGG GGGGGAGGGT 1800 GACCGCGGCT CGATTCACTC GGCCGTGGAC CCAAGTCCCA ACAGACGCCA AGACTACCAC 1860 TGAGCCACCC CCGGTGCCAG CTAAAGGGGT TTTCAAAGAG GCTCCTCTTT TCATGCCAAC 1920 AGGGGCGGGG AAAAGCACAC GCGTCCCTTT GGAGTATGGA AACATGGGGC ACAAGGTCCT 1980 GATTCTCAAC CCGTCGGTTG CCACTGTGAG GGCCATGGGC CCTTACATGG AGAGGCTGGC 2040 GGGGAAACAT CCTAGCATTT TCTGTGGACA CGACACAACA GCTTTCACAC GGATCACGGA 2100 596 CTCTCCATTG ACGTACTCTA CCTATGGGAG GTTTCTGGCC AACCCGAGGC AGATGCTGAG 2160 GGGAGTTTCC GTGGTCATCT GTGATGAGTG CCACAGTCAT GACTCAACTG TGTTGCTGGG 2220 TATAGGCAGG GTCAGGGACG TGGCGCGGGG GTGTGGAGTG CAATTAGTGC TCTAGCCTAC 2280 TGCGACTCCC CCGGGCTCGC CTATGACTCA GCATCCATCC ATAATTGAGA CAAAGCTGGA 2340 CGTTGGTGAG ATCCCCTTTT ATGGGCATGG TATCCCCCTC GAGCGTATGA GGACTGGTCG 2400 CCACCTTGTA TTCTGCCATT CCAAGGCGGA GTGCGAGAGA TTGGCCGGCC AGTTCTCCGC 2460 GCGGGGGGTT AATGCCATCG CCTATTATAG GGGTAAGGAC AGTTCCATCA TCAAAGACGG 2520 AGACCTGGTG GTTTGTGCGA CAGACGCGCT CTCTACCGGG TACACAGGAA ACTTCGATTC 2580 TGTCACCGAC TGTGGGTTGG TGGTGGAGGA GGTCGTTGAG GTGACCCTTG ATCCCACCAT 2640 TACCATTTCC TTGCGGACTG TCCCTGCTTC GGCTGAATTG TCGATGCAGC GGCGCGGACG 2700 CACGGGGAGA GGTCGGTCGG GCCGCTACTA CTACGCTGGG GTCGGTAAGG CTCCCGCGGG 2760 GGTGGTGCGG TCTGGTCCGG TCTGGTCGGC AGTGGAAGCT GGAGTGACCT GGTATGGAAT 2820 GGAACCTGAC TTGACAGCAA ACCTTCTGAG ACTTTACGAC GACTGCCCTT ACACCGCAGC 2880 CGTCGCAGCT GACATTGGTG AAGCCGCGGT GTTCTTTGCG GGCCTCGCGC CCCTCAGGAT 2940 GCATCCCGAT GTTAGCTGGG CAAAAGTTCG CGGCGTCAAT TGGCCCCTCC TGGTGGGTGT 3000 TCAGCGGACG ATGTGTCGGG AAACACTGTC TCCCGGCCCG TCGGACGACC CTCAGTGGGC 3060 AGGTCTGAAA GGCCCGAATC CTGTCCCACT ACTGCTGAGG TGGGGCAATG ATTTGCCATC 3120 AAAAGTGGCC GGCCACCACA TAGTTGACGA TCTGGTCCGT CGGCTCGGTG TGGCGGAGGG 3180 ATACGTGCGC TGTGATGCTG GRCCCATCCT CATGGTGGGC TTGGCCATAG CGGGCGGCAT 3240 GATCTACGCC TCTTACACTG GGTCGCTAGT GGTGGTAACA GACTGGGATG TGAAGGGAGG 3300 TGGCAATCCC CTTTATAGGA GTGGTGACCA GGCCACCCCT CAACCCGTGG TGCAGGTCCC 3360 CCCGGTAGAC CATCGGCCGG GGGGGGAGTC TGCGCCACGG GATGCCAAGA CAGTGACAGA 3420 TGCGGTGGCA GCCATCCAGG TGAACTGCGA TTGGTCTGTG ATGACCCTGT CGATCGGGGA 3480 AGTCCTCACC TTGGCTCAGG CTAAGACAGC CGAGGCCTAC GCAGCTACTT CCAGGTGGCT 3540 CGCTGGCTGC TACACGGGGA CGCGGGCCGT CCCCACTGTA TCAATTGTTG ACAAGCTCTT 3600 CGCCGGGGGT TGGGCCGCCG TGGTGGGTCA CTGTCACAGC GTCATTGCTG CGGCGGTGGC 3660 TGCCTATGGA GCTTCTCGAA GTCCTCCACT GGCCGCGGCG GCGTCCTACC TCATGGGGTT 3720 GGGCGTCGGA GGCAACGCAC AGGCGCGCTT GGCTTCAGCT CTTCTACTGG GGGCTGCTGG 3780 GTACGGCTCT GGGGGACCCC TGTCAGTGGG ACTCACCATG GCGGGGGCCT TCATGGGACA 3840 597 GGTGCCAGCG TGTCCCCTCC CTCGTCACTG TCCTACTTGG GGCTGTGGGA GGTTGGGAGG 3900 GCGTTGTCAA CGCTGCCAGT CTCGTCTTCG ACTTCATGGC TGGGAAACTT TCAACAGAAG 3960 ACCTTTGGTA TGCCATCCCG GTACTCACTA GTCCTGGRGC GGGCCTCGCG GGGATTGCCC 4020 TTGGTCTGGT TTTGTACTCA GCAAACAACT CTGGCACTAC CACATGGCTG AACCGTCTGC 4080 TGACGACGTT GCCACGGTCA TCTTGCATAC CCGACAGCTA CTTCCAACAG GCTGACTACT 4140 GCGACAAGGT CTCGGCAATC GTGCGCCGCC TGAGCCTTAC TCGCACCGTG GTGGCCCTGG 4200 TCAACAGGGA GCCTAAGGTG GATGAGGTCC AGGTGGGGTA CGTCTGGGAT CTGTGGGAGT 4260 GGGTGATGCG CCAGGTGCGC ATGGTGATGT CTAGACTCCG GGCCCTCTGC CCTGTGGTGT 4320 CACTCCCCTT GTGGCACTGC GGGGAGGGGT GGTCCGGTGA ATGGCTTCTC GATGGGCACG 4380 TGGAGAGTCG TTGTCTGTGC GGGTGTGTAA TCACCGGCGA CGTCCTCAAT GGGCAACTCA 4440 AAGATCCAGT TTACTCTACC AAGCTGTGCA GGCACTACTG GATGGGAACT GTGCCGGTCA 4500 ACATGCTGGG CTACGGGGAA ACCTCACCTC TTCTCGCCTC TGACACCCCG AAGGTGGTAC 4560 CCTTCGGGAC GTCGGGGTGG GCTGAGGTGG TGGTGACCCC TACCCACGTG GTGATCAGGC 4620 GCACGTCCTG TTACAAACTG CTTCGCCAGC AAATTCTTTC AGCAGCTGTA GCTGAGCCCT 4680 ACTACGTTGA TGGCATTCCG GTCTCTTGGG AGGCTGACGC GAGAGCGCCG GCCATGGTCT 4740 ACGGTCCGGG CCAAAGTGTT ACCATTGATG GGGAGCGCTA CACCCTTCCG CACCAGTTGC 4800 GGATGCGGAA TGTGGCGCCC TCTGAGGTTT CATCTGAGGT CAGCATCGAG ATCGGGACGG 4860 AGACTGAAGA CTCAGAACTG ACTGAGGCCG ATTTGCCACC AGCGGCTGCT GCCCTCCAAG 4920 CGATAGAGAA TGCTGCGAGA ATTCTCGAAC CGCACATCGA TGTCAYCATG GAGGATTGCA 4980 GTACACCCTC TCTCTGTGGT AGTAGCCGAG AGATGCCTGT GTGGGGAGAA GACATACCCC 5040 GCACTCCATC GCCTGCACTT ATCTCGGTTA CGGAGAGCAG CTCAGATGAG A 5091 (2) INFORMATION FOR SEQ ID NO:674: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 373 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:674: TCGCCACTGC TACCCCTCCG GGCTCCGTCA CTGTGTCCCA TCCTAACATC GAGGAGGTTG 60 598 CTCTGTCCAC CACCGGAGAG ATCCCCTTTT ACGGCAAGGC TATCCCCCTC GAGGTGATCA 120 AGGGGGGAAG ACATCTCATC TTCTGCCACT CAAAGAAGAA GTGCGACGAG CTCGCCGCGA 180 AGCTGGTCGC ATTGGGCATC AATGCCGTGG CCTACTACCG CGGTCTTGAC GTGTCTGTCA 240 TCCCGACCAG CGGCGATGTT GTCGTCGTGT CGACCGATGC TCTCATGACT GGCTTTACCG 300 GCGACTTCGA CTCTGTGATA GACTGCAACA CGTGTGTCAC TCAGACAGTC GATTTTAGCC 360 TTGACCCTAC CTT 373 (2) INFORMATION FOR SEQ ID NO:675: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:675: GACGTTGGTG AGATCCCCTT 20 (2) INFORMATION FOR SEQ ID NO:676: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 19 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:676: CGAAGTTTCC TGTGTACCC 19 (2) INFORMATION FOR SEQ ID NO:677: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 156 baβe pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) 599 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:677: ATCCCCTTTT ATGGGCATGG CATACCCCTG GAGAGGATGC GGACCGGCAG GCACCTCGTA 60 ATCCCCTTTT ATGGGCATGG CATACCCCTG GAGAGGATGC GGACCGGCAG GCACCTCGTA 120 AATGCCATTG CCTATTATAG GGGGAAAGAC AGTTCT 156 (2) INFORMATION FOR SEQ ID NO:678: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 156 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:678: ATCCCCTTTT ATGGGCATGG AATCCCCCTC GAGCGGATGC GGACCGGGCG CCACCTCGTG 60 TTCTGCCATT CAAAGGCGGA GTGCGAGCGG TTGGCTGGCC AGTTCTCTTC GCGGGGGGTG 120 AATGCCATTG CCTATTACAG GGGGAAAGAC AGTTCC 156 (2) INFORMATION FOR SEQ ID NO:679: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 23 baβe pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:679: CCAATCTCTC GCACTCCGCC TTG 23 (2) INFORMATION FOR SEQ ID NO:680: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) 600 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:680: CTCACCAACG TCCAGCTTTG TCTC 24 (2) INFORMATION FOR SEQ ID NO:681: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 baee paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:681: CTCGTATGAT GCGACAGTCC GTCC 24 (2) INFORMATION FOR SEQ ID NO:682: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 baee paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:682: GTAGTGGCCT TCTCGCCCGC CATC 24 (2) INFORMATION FOR SEQ ID NO:683: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 23 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear ' (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:683: CACTCCACCA CCCTTGCCAA ACG 23 (2) INFORMATION FOR SEQ ID NO:684: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 baβe paire (B) TYPE: nucleic acid 601 (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:684: CCTGGTACCC TTTACACCAC GTCC 24 (2) INFORMATION FOR SEQ ID NO:685: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 25 baee paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:685: GATTATGGCC TTTGTGCTTC CACCC 25 (2) INFORMATION FOR SEQ ID NO:686: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 25 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:686: CTCCAAAGCC GCGTCCCACT CCAGC 25 (2) INFORMATION FOR SEQ ID NO:687: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 26 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:687: 602 CATCATCAAA GACGGAGACC TGGTGG 26 (2) INFORMATION FOR SEQ ID NO:688: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 25 baee pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (Xi) SEQUENCE DESCRIPTION: SEQ ID NO:688: GCATGATCTA CGCCTCTTAC ACTGG 25 (2) INFORMATION FOR SEQ ID NO:689: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 25 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (Xi) SEQUENCE DESCRIPTION: SEQ ID NO:689: GTCGCTAGTG GTGGTAACAG ACTGG 25 (2) INFORMATION FOR SEQ ID NO:690: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 25 base paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:690: GGTGCGCATG GTGATGTCTA GACTC 25 (2) INFORMATION FOR SEQ ID NO:691: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 25 baee paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear 603 (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:691: GGTCCGGTGA ATGGCTTCTC GATGG 25 (2) INFORMATION FOR SEQ ID NO:692: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 23 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:692: ACCAGTTGCG GATGCGGAAT GTG 23 (2) INFORMATION FOR SEQ ID NO:693: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:693: GCATCGAGAT CGGGACGGAG ACTG 24 (2) INFORMATION FOR SEQ ID NO:694: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 34 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:694: CAGTTCAAGC TTGTCCAGGA ATTCNNNNNG GCCA 34 (2) INFORMATION FOR SEQ ID NO:695: 604 (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 34 baβe pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:695: CAGTTCAAGC TTGTCCAGGA ATTCNNNNNC CGGA 34 (2) INFORMATION FOR SEQ ID NO:696: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 baβe pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:696: CATCAGCTCT GAACACCGCC GCAC 24 (2) INFORMATION FOR SEQ ID NO:697: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 25 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:697: GCCGAGAAGC ATGCAGTTGT TAAGG 25 (2) INFORMATION FOR SEQ ID NO:698: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 22 base paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:698: 605 GCCAGCTGTT CAGTCCATCT CC 22 (2) INFORMATION FOR SEQ ID NO:699: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 baee paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:699: CTCTACTGCA CACGTCAGGT TCGG 24 (2) INFORMATION FOR SEQ ID NO:700: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 baee paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:700: CCAGAGCCAC CAGGCATCCG C 21 (2) INFORMATION FOR SEQ ID NO:701: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 25 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:701: CAGGCAGAAG CCTATGTCCT CCAGG 25 (2) INFORMATION FOR SEQ ID NO:702: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 base paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double 606 (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:702: GTGGTAGTAG CCGAGAGATG CCTG 24 (2) INFORMATION FOR SEQ ID NO:703: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 25 baee paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:703: CACTCCATCG CCTGCACTTA TCTCG 25 (2) INFORMATION FOR SEQ ID NO:704: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 25 baee pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:704: CTCGAATTGC AAGTTGGGTG CTTGG 25 (2) INFORMATION FOR SEQ ID NO:705: ' (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 23 baee paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:705: GAATGTGACA AGTGTGAGGC ACG 23 607 (2) INFORMATION FOR SEQ ID NO:706: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO-.706: GGAGATGCTA AAGCTGTGGG AATC 24 (2) INFORMATION FOR SEQ ID NO:707: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 baee pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:707: GAGGACGTGG CACTAGAGAC AGAG 24 (2) INFORMATION FOR SEQ ID NO:708: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 36 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:708: GCCGCTGAAT TCATGCCTTG TTATTTCTAC TCAAAC 36 (2) INFORMATION FOR SEQ ID NO:709: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 33 baβe pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear 608 (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:709: GCCGCAGGAT CCTCGAACGA CCGCTCCTGC CAC 33 (2) INFORMATION FOR SEQ ID NO:710: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 34 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:710: GCCGCAGGAA TTCATGGCTT GGCTGTGGTT GCTG 34 (2) INFORMATION FOR SEQ ID NO:711: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:711: GCIACIGCIA CNCCNCCNGG 20 (2) INFORMATION FOR SEQ ID NO:712: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:712: ATGGTIAIIG TNGGRTCHAR R 21 609 (2) INFORMATION FOR SEQ ID NO:713: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 22 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:713: ATGGGCATGG CATCCCCCTG GA 22 (2) INFORMATION FOR SEQ ID NO:714: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 base paire (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:714: TCCTTGATGA TTGAACTGTC (2) INFORMATION FOR SEQ ID NO:714: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 19 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:714: GGCACCTCGT GTTCTGCCA 19 (2) INFORMATION FOR SEQ ID NO:715: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 18 baβe paire (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) 610 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:715: GGCACCTCGTG TTCTGCCA (2) INFORMATION FOR SEQ ID NO:716: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 20 baβe pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: βingle (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:716: AGGTCTCCGT CCTTGATGAT 20 (2) INFORMATION FOR SEQ ID NO:717: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 199 baβe pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:717: TTATGGGCAT GGCATCCCCC TGGAGCGGAT GAGGACCGGT AGGCACCTGG TATTCTGCCA 60 CTCAAAGGCG GAGTGTGAGA GGCTGGCCGG CCAATTCTCC TCACGGGGGG TTAATGCTGT 120 TGCCTATTAT AGGGGTAAGG ACAGTTCAAT CATCAAGGAT GGTGACCTGG TGGTGTGCGC 180 TACTGACGCG CTATCTACC 199 (2) INFORMATION FOR SEQ ID NO:718: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 199 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) 611 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:718: TTATGGGCAT GGCATACCTC TCGAACGGAT GCGGACCGGA AGGCACCTCG TGTTCTGCCA 60 TTCAAAGGCG GAGTGCGAGC GGCTCGCTGG TCAGTTTTCT GCGAGGGGGG TAAACGCCAT 120 TGCTTATTAT AGGGGCAAAG ACAGTTCCAT CATCAAGGAC GGAGACCTAG TGGTGTGCGC 180 CACAGACGCG CTATCCACG 199 (2) INFORMATION FOR SEQ ID NO:719: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 199 baee pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:719: TTATGGGCAT GGCATTCCTC TGGAGCGGAT GCAGACCGGT AGACATCTTG TGTTCCGCCA 60 CTCGAAGGCG GAGTGCGAGC GGCTTGCCGG CCAGTTCTCC TCTAGGGGGG TCAACGCCAT 120 TGCCTATTAC AGGGGTAAGG ACAGCTCCAT CATCAAGGAC GGAGACCTCG TTGTGTGCGC 180 CACTGATGCG CTCTCTACG 199 (2) INFORMATION FOR SEQ ID NO:720: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 199 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:720: TTATGGGCAT GGCATACCCC TCGAACGGAT GCGAACCGGA GGGCACCTCG TGTTCTGTCA 60 TTCCAAGGCG GAGTGCGAGC GGCTTGCTGG CCAGTTCTCT GCGAGGGGGG TGAATGCCAT 120 TGCCTATTAT AGGGGCAAAG ACAGTTCCAT CATCAAGGAT GGCGACCTGG TGGTGTGCGC 180 612 TACGCACGCG CTATCCACC 199 613 WHAT IS CLAIMED IS: 1 . A purified polynucleotide or fragment thereof derived from hepatitis GB virus (HGBN) capable of selectively hybridizing to the genome of HGBN or the complement thereof. 2. The purified polynucleotide or fragment thereof of claim 1 wherein said polynucleotide is characterized by a positive stranded RΝA genome wherein said genome comprises an open reading frame (ORF) encoding a polyprotein wherein said polyprotein comprises an amino acid sequence having at least 35% identity to an amino acid sequence selected from the group consisting of HGBN- A, HGBN-B and HGBN-C. 3. The purified polynucleotide or fragment thereof of claim 1 wherein said polynucleotide is characterized by a positive stranded RΝA genome wherein said genome comprises an open reading frame (ORF) encoding a polyprotein wherein said polyprotein comprises an amino acid sequence having at least 40% identity to an amino acid sequence selected from the group consisting of HGBN- A, HGBN-B and HGBN-C. 4. The purified polynucleotide or fragment thereof of claim 1 wherein said polynucleotide is characterized by a positive stranded RΝA genome wherein said genome comprises an open reading frame (ORF) encoding a polyprotein wherein said polyprotein comprises an amino acid sequence having at least 60% identity to an amino acid sequence selected from the group consisting of HGBN- A, HGBN-B and HGBN-C. 5. A recombinant polynucleotide or fragment therof derived from hepatitis GB virus (HGBN) capable of selectively hybridizing to the genome of HGBN or the complement thereof. 6. The recombinant polynucleotide of claim 5 wherein said nucleotide comprises a sequence that encodes at least one epitope of HGBN. 7. The recombinant polynucleotide of claim 6 wherein said recombinant nucleotide is characterized by a positive stranded RΝA genome wherein said genome comprises an open reading frame (ORF) encoding a polyprotein wherein said polyprotein comprises an amino acid sequence having at 614 least 35% identity to an amino acid sequence selected from the group consisting of HGBN- A, HGBV-B and HGBN-C. 8. The recombinant polynucleotide of claim 5 wherein said polynucleotide is contained within a recombinant vector. 9. The polynucleotide of claim 8 further comprising a host cell transformed with said vector. 10. A hepatitis GB virus (HGBN) recombinant polynucleotide or fragment thereof comprising a nucleotide sequence derived from an HGBN genome. 1 1. The HGBN recombinant polynucleotide of claim 10 wherein said polynucleotide is contained within a recombinant vector. 12. The HGBN recombinant polynucleotide of claim 10 further comprising a host cell transformed with said vector. 13. The HGBV recombinant polynucleotide of claim 10, wherein said sequence encodes an epitope of HGBV. 14. The HGBV recombinant polynucleotide of claim 13, wherein said sequence is characterized by a positive stranded RΝA genome wherein said genome comprises an open reading frame (ORF) encoding a polyprotein wherein said polyprotein comprises an amino acid sequence having at least 35% identity to an amino acid sequence selected from the group consisting of HGBV-A, HGBV-B and HGBV-C. 15. The HGBV recombinant polynucleotide of claim 13 wherein said polynucleotide is contained within a recombinant vector. 16. The HGBV recombinant polynucleotide of claim 15 further comprising a host cell transformed with said vector. 17. A recombinant expression system comprising an open reading frame of DΝA or RΝA derived from hepatitis GB virus (HGBV) wherein said

Claims: 615 open reading frame comprises a sequence of HGBV genome or cDNA and wherein said open reading frame is operably linked to a control sequence compatible with a desired host. 18. The expression system of claim 17 further comprising a cell transformed with said recombinant expression system. 19. The expression system of claim 18 further comprising a polypeptide of at least about eight amino acids in length produced by said cell. 20. Purified hepatitis GB virus (HGBV). 21. The purified virus of claim 20 further comprising a preparation of HGBV polypeptide or fragment thereof. 22. A purified polypeptide derived from hepatitis GB virus (HGBV) comprising an amino acid sequence or fragment thereof wherein said sequence is characterized by a positive stranded RNA genome wherein said genome comprises an open reading frame (ORF) encoding a polyprotein wherein said polyprotein comprises an amino acid sequence having at least 35% identity to an amino acid sequence selected from the group consisting of HGBV-A, HGBV-B and HGB V- C. 23. A recombinant polypeptide comprising an amino acid sequence or fragment thereof wherein said sequence is characterized by a positive stranded RNA genome wherein said genome comprises an open reading frame (ORF) encoding a polyprotein wherein said polyprotein comprises an amino acid sequence having at least 35% identity to an amino acid sequence selected from the group consisting of HGBV-A, HGBV-B and HGBV-C. 24. A recombinant polypeptide comprising an amino acid sequence or fragment thereof characterized by a positive stranded RNA genome wherein said genome comprises an open reading frame (ORF) encoding a polyprotein wherein said polyprotein comprises an amino acid sequence having at least 35% identity to an amino acid sequence selected from the group consisting of HGBV-A, HGBV-B and HGBV-C. 616 25. An antibody directed against at least one hepatitis GB virus (HGBV) epitope. 26. The antibody of claim 25 wherein said antibody is polyclonal. 27. The antibody of claim 25 wherein said antibody is monoclonal. 28. A fusion polypeptide comprising at least one hepatitis GB virus (HGBV) polypeptide or fragment thereof . 29. A particle that is immunogenic against hepatitis GB virus (HGBV) infection, comprising a non-HGBV polypeptide having an amino acid sequence capable of forming a particle when said sequence is produced in a eukaryotic or prokaryotic host, and at least one HGBV epitope. 30. A polynucleotide probe for hepatitis GB virus (HGBV) wherein said polynucleotide probe is characterized by a positive stranded RNA genome wherein said genome comprises an open reading frame (ORF) encoding a polyprotein wherein said polyprotein comprises an amino acid sequence having at least 35% identity to an amino acid sequence selected from the group consisting of HGBV-A, HGBV-B and HGBV-C. 31. An assay kit for determining the presence of hepatitis GB virus (HGBV) antigen or antibody in a test sample comprising a container containing a polypeptide possessing at least one HGBV epitope present in an HGBV antigen. 32. The assay kit of claim 31 , wherein said polypeptide is characterized by a positive stranded RNA genome wherein said genome comprises an open reading frame (ORF) encoding a polyprotein wherein said polyprotein comprises an amino acid sequence having at least 35% identity to an amino acid sequence selected from the group consisting of HGBV-A, HGBV-B and HGBV-C. 33. The assay kit of claim 32 wherein said polypeptide is attached to a solid phase. 34. A kit for determining the presence of hepatitis GB virus (HGBV) antigen or antibody in a test sample comprising a container containing an antibody 617 which specifically binds to an HGBV antigen, wherein said antigen comprises an HGBV epitope encoded by a sequence having at least about 60% sequence similarity to a sequence of HGBV. 35. The kit of claim 34 wherein said antibody is attached to a solid phase. 36. A kit for determining the presence of hepatitis GB virus (HGBV) polynucleotides in a test sample suspected of containing said polynucleotides, comprising a container containing a polynucleotide probe wherein said polynucleotide probe comprises a nucleotide sequence characterized by a positive stranded RNA genome wherein said genome comprises an open reading frame (ORF) encoding a polyprotein wherein said polyprotein comprises an amino acid sequence having at least 35% identity to an amino acid sequence selected from the group consisting of HGBN- A, HGBN-B and HGBN-C. 37. A method for producing a polypeptide containing at least one hepatitis GB virus (HGBN) epitope comprising incubating host cells transformed with an expression vector comprising a sequence encoding a polypeptide characterized by a positive stranded RΝA genome wherein said genome comprises an open reading frame (ORF) encoding a polyprotein wherein said polyprotein comprises an amino acid sequence having at least 35% identity to an amino acid sequence selected from the group consisting of HGBV-A, HGBV-B and HGB V- C. 38. A method for detecting hepatitis GB virus (HGBV) nucleic acid in a test sample suspected of containing HGBV comprising: a. reacting the test sample with a probe for an HGBV polynucleotide encoded by a sequence of HGBV or fragment thereof wherein said sequence is characterized by a positive stranded RΝA genome wherein said genome comprises an open reading frame (ORF) encoding a polyprotein wherein said polyprotein comprises an amino acid sequence having at least 35% identity to an amino acid sequence selected from the group consisting of HGBV-A, HGBV-B and HGB V- C, under conditions and for a time which allows the formation of a complex between the probe and the HGBV nucleic acid in the test sample; b . detecting the complex which contains the probe. 618 39. The method of claim 38 further comprising the step of amplifying the probe of step (a) by the polymerase chain reaction (PCR) technique. 40. The method of claim 38 further comprising the step of amplifying the probe of step (a) by the ligase chain reaction (LCR) technique. 41. A method for detecting hepatitis GB virus (HGBV) antigen in a test sample suspected of containing HGBV comprising: a. contacting the test sample with an antibody or fragment thereof which specifically binds to at least one HGBV antigen, for a time and under conditions sufficient to allow the formation of antibody/antigen complexes; b . detecting said complex containing the antibody. 42. The method of claim 41 wherein said antibody is attached to a solid phase. 43. The method of claim 41 wherein said antibody is a monoclonal or polyclonal antibody. 44. A method for detecting hepatitis GB virus (HGBV) antibodies in a test sample suspected of containing said antibodies, comprising: a. contacting the test sample with a probe polypeptide wherein said polypeptide contains at least one HGBV epitope comprising an amino acid sequence or fragment thereof is characterized by a positive stranded RNA genome wherein said genome comprises an open reading frame (ORF) encoding a polyprotein wherein said polyprotein comprises an amino acid sequence having at least 35% identity to an amino acid sequence selected from the group consisting of HGBV-A, HGBV-B and HGBV-C, for a time and under conditions sufficient to allow antigen/antibody complexes to form; b . detecting said complexes which contain the probe polypeptide. 45. The method of claim 42 wherein said probe polypeptide is attached to a solid phase. 46. The method of claim 42 wherein said solid phase is selected from the group consisting of beads, microtiter wells, walls of test tube, nitrocellulose strips, magnetic beads and non-magnetic beads. 619 47. The method of claim 44 wherein said polypeptide is a recombinant protein or a synthetic peptide which encodes at least one epitope of HGBV is characterized by a positive stranded RNA genome wherein said genome comprises an open reading frame (ORF) encoding a polyprotein wherein said polyprotein comprises an amino acid sequence having at least 35% identity to an amino acid sequence selected from the group consisting of HGBV-A, HGBV-B and HGB V- C. 48. The method of claim 44 wherein said sequence is characterized by a positive stranded RNA genome wherein said genome comprises an open reading frame (ORF) encoding a polyprotein wherein said polyprotein comprises an amino acid sequence having at least 35% identity to an amino acid sequence selected from the group consisting of HGBV-A, HGBV-B and HGBV-C. 49. A vaccine for treatment of hepatitis GB virus (HGBV) infection comprising a pharmacologically effective dose of an immunogenic HGBV polypeptide or fragment thereof which polypeptide is characterized by a positive stranded RNA genome wherein said genome comprises an open reading frame (ORF) encoding a polyprotein wherein said polyprotein comprises an amino acid sequence having at least 35% identity to an amino acid sequence selected from the group consisting of HGBV-A, HGBV-B and HGBV-C, in a pharmaceutically acceptable excipient. 50. A vaccine for treatment of hepatitis GB virus (HGBV) infection comprising an inactivated or attenuated HGBV in a pharmacologically effective dose in an pharmaceutically acceptable excipient. 51. A tissue culture grown cell infected with hepatitis GB virus (HGBV). 52. The tissue culture grown cell of claim 51 wherein said HGBV is transfected into a cell. 53. The tissue culture grown cell of claim 51 wherein said HGBV comprises a subgenomic fragment of the HGBV gene. 620 54. A method for producing antibodies to hepatitis GB virus (HGBV) comprising administering to an individual an isolated immunogenic polypeptide or fragment thereof comprising at least one HGBV epitope in an amount sufficient to produce an immune response. 55. A synthetic peptide encoding an epitope of hepatitis GB virus (HGBV) comprising a sequence of HGBV or fragment thereof is characterized by a positive stranded RNA genome wherein said genome comprises an open reading frame (ORF) encoding a polyprotein wherein said polyprotein comprises an amino acid sequence having at least 35% identity to an amino acid sequence selected from the group consisting of HGBV-A, HGBV-B and HGBV-C. 56. The synthetic polypeptide of claim 55 attached to a solid support. 57. A diagnostic reagent comprising a polynucleotide derived from hepatitis GB virus (HGBV), wherein said polynucleotide or fragment thereof encodes at least one epitope of HGBV and is characterized by a positive stranded RNA genome wherein said genome comprises an open reading frame (ORF) encoding a polyprotein wherein said polyprotein comprises an amino acid sequence having at least 35% identity to an amino acid sequence selected from the group consisting of HGBV-A, HGBV-B and HGBV-C. 58. A diagnostic reagent comprising a polypeptide or fragment thereof derived from hepatitis GB virus (HGBV), wherein said polypeptide or fragment thereof encodes at least one epitope of HGBV and is characterized by a positive stranded RNA genome wherein said genome comprises an open reading frame (ORF) encoding a polyprotein wherein said polyprotein comprises an amino acid sequence having at least 35% identity to an amino acid sequence selected from the group consisting of HGBV-A, HGBV-B and HGBV-C. 1/39 FIGURfe 1 WEEKS POST INOCULATION FIGURE 2 WEEKS POST INOCULATION

Inventors: BUIJK SHERI L, DAWSON GEORGE J, DESAI SURESH M, ERKER JAMES CARL, LEARY THOMAS P, MUERHOFF ANTHONY SCOTT, MUSHAHWAR ISA K, PILOT-MATIAS TAMI J, SCHLAUDER GEORGE G, SIMONS JOHN N, BUIJK, SHERI, L., DAWSON, GEORGE, J., DESAI, SURESH, M., ERKER, JAMES, CARL, LEARY, THOMAS, P., MUERHOFF, ANTHONY, SCOTT, MUSHAHWAR, ISA, K., PILOT-MATIAS, TAMI, J., SCHLAUDER, GEORGE, G., SIMONS, JOHN, N.
Applicants: ABBOTT LAB, BUIJK SHERI L, DAWSON GEORGE J, DESAI SURESH M, ERKER JAMES CARL, LEARY THOMAS P, MUERHOFF ANTHONY SCOTT, MUSHAHWAR ISA K, PILOT MATIAS TAMI J, SCHLAUDER GEORGE G, SIMONS JOHN N, ABBOTT LABORATORIES, BUIJK, SHERI, L., DAWSON, GEORGE, J., DESAI, SURESH, M., ERKER, JAMES, CARL, LEARY, THOMAS, P., MUERHOFF, ANTHONY, SCOTT, MUSHAHWAR, ISA, K., PILOT-MATIAS, TAMI, J., SCHLAUDER, GEORGE, G., SIMONS, JOHN, N.
Application year: 1995
Main classification: C12N15
IPC codes: A61K39, C07K14, C07K16, C12N7, C12N15, C12Q1, G01N33