Patent Publication Number: US-2003224379-A1

Title: Novel nucleic acids and polypeptides

Description:
Cross Reference to Related Applications  
     [0001] This application is a continuation-in-part application of PCT application Ser. No. PCT/US00/35017 filed Dec. 22, 2000 entitled “Novel Contigs Obtained from Various Libraries”, Attorney Docket No. 784CIP3A/PCT, which in turn is a continuation-in-part application of U.S. application Ser. No. 09/552,317 filed Apr. 25, 2000 entitled “Novel Contigs Obtained from Various Libraries”, Attorney Docket No. 784CIP, which in turn is a continuation-in-part application of U.S. application Ser. No. 09/488,725 filed Jan. 21, 2000 entitled “Novel Contigs Obtained from Various Libraries”, Attorney Docket No. 784; PCT application Ser. No. PCT/US01/02623 filed Jan. 25, 2001 entitled “Novel Contigs Obtained from Various Libraries”, Attorney Docket No. 785CIP3/PCT, which in turn is a continuation-in-part application of U.S. application Ser. No. 09/491,404 filed Jan. 25, 2000 entitled “Novel Contigs Obtained from Various Libraries”, Attorney Docket No. 785; PCT application Ser. No. PCT/US01/03800 filed Feb. 5, 2001 entitled “Novel Contigs Obtained from Various Libraries”, Attorney Docket No. 787CIP3/PCT, which in turn is a continuation-in-part application of U.S. application Ser. No. 09/560,875 filed Apr. 27, 2000 entitled “Novel Contigs Obtained from Various Libraries”, Attorney Docket No. 787CIP, which in turn is a continuation-in-part application of U.S. application Ser. No. 09/496,914 filed Feb. 03, 2000 entitled “Novel Contigs Obtained from Various Libraries”, Attorney Docket No. 787; PCT application Ser. No. PCT/US01/04927 filed Feb. 26, 2001 entitled “Novel Contigs Obtained from Various Libraries”, Attorney Docket No. 788CIP3/PCT, which in turn is a continuation-in-part application of U.S. application Ser. No. 09/577,409 filed May 18, 2000 entitled “Novel Contigs Obtained from Various Libraries”, Attorney Docket No. 788CIP, which in turn is a continuation-in-part application of U.S. application Ser. No. 09/515,126 filed Feb. 28, 2000 entitled “Novel Contigs Obtained from Various Libraries”, Attorney Docket No. 788; PCT application Ser. No. PCT/US01/04941 filed Mar. 5, 2001 entitled “Novel Contigs Obtained from Various Libraries”, Attorney Docket No. 789CIP3/PCT, which in turn is a continuation-in-part application of U.S. application Ser. No. 09/574,454 filed May 19, 2000 entitled “Novel Contigs Obtained from Various Libraries”, Attorney Docket No. 789CIP, which in turn is a continuation-in-part application of U.S. application Ser. No. 09/519,705 filed Mar. 07, 2000 entitled “Novel Contigs Obtained from Various Libraries”, Attorney Docket No. 789; PCT application Ser. No. PCT/US01/08631 filed Mar. 30, 2001 entitled “Novel Contigs Obtained from Various Libraries”, Attorney Docket No. 790CIP3/PCT, which in turn is a continuation-in-part application of U.S. application Ser. No. 09/649,167 filed Aug. 23, 2000 entitled “Novel Contigs Obtained from Various Libraries”, Attorney Docket No. 790CIP, which in turn is a continuation-in-part application of U.S. application Ser. No. 09/540,217 filed Mar. 31, 2000 entitled “Novel Contigs Obtained from Various Libraries”, Attorney Docket No. 790; PCT application Ser. No. PCT/US01/08656 filed Apr. 18, 2001 entitled “Novel Contigs Obtained from Various Libraries”, Attorney Docket No. 791CIP3/PCT, which in turn is a continuation-in-part application of U.S. application Ser. No. 09/770,160 filed Jan. 26, 2001 entitled “Novel Contigs Obtained from Various Libraries”, Attorney Docket No. 791CIP, which is in turn a continuation-in-part application of U.S. application Ser. No. 09/552,929 filed Apr. 18, 2000 entitled “Novel Contigs Obtained from Various Libraries”, Attorney Docket No. 791; and PCT application Ser. No. PCT/US01/14827 filed May 16, 2001 entitled “Novel Contigs Obtained from Various Libraries”, Attorney Docket No. 792CIP3/PCT, which in turn is a continuation-in-part application of U.S. application Ser. No. 09/577,408 filed May 18, 2000 entitled “Novel Contigs Obtained from Various Libraries”, Attorney Docket No. 792; all of which are incorporated herein by reference in their entirety. 
    
    
     
       BACKGROUND OF THE INVENTION  
       [0002] 1. Technical Field  
       [0003] The present invention provides novel polynucleotides and proteins encoded by such polynucleotides, along with uses for these polynucleotides and proteins, for example in therapeutic, diagnostic and research methods.  
       [0004] 2. Background  
       [0005] Technology aimed at the discovery of protein factors (including e.g., cytokines, such as lymphokines, interferons, circulating soluble factors, chemokines, and interleukins) has matured rapidly over the past decade. The now routine hybridization cloning and expression cloning techniques clone novel polynucleotides “directly” in the sense that they rely on information directly related to the discovered protein (i.e., partial DNA/amino acid sequence of the protein in the case of hybridization cloning; activity of the protein in the case of expression cloning). More recent “indirect” cloning techniques such as signal sequence cloning, which isolates DNA sequences based on the presence of a now well-recognized secretory leader sequence motif, as well as various PCR-based or low stringency hybridization-based cloning techniques, have advanced the state of the art by making available large numbers of DNA/amino acid sequences for proteins that are known to have biological activity, for example, by virtue of their secreted nature in the case of leader sequence cloning, by virtue of their cell or tissue source in the case of PCR-based techniques, or by virtue of structural similarity to other genes of known biological activity.  
       [0006] Identified polynucleotide and polypeptide sequences have numerous applications in, for example, diagnostics, forensics, gene mapping; identification of mutations responsible for genetic disorders or other traits, to assess biodiversity, and to produce many other types of data and products dependent on DNA and amino acid sequences.  
       SUMMARY OF THE INVENTION  
       [0007] The compositions of the present invention include novel isolated polypeptides, novel isolated polynucleotides encoding such polypeptides, including recombinant DNA molecules, cloned genes or degenerate variants thereof, especially naturally occurring variants such as allelic variants, antisense polynucleotide molecules, and antibodies that specifically recognize one or more epitopes present on such polypeptides, as well as hybridomas producing such antibodies.  
       [0008] The compositions of the present invention additionally include vectors, including expression vectors, containing the polynucleotides of the invention, cells genetically engineered to contain such polynucleotides and cells genetically engineered to express such polynucleotides.  
       [0009] The present invention relates to a collection or library of at least one novel nucleic acid sequence assembled from expressed sequence tags (ESTs) isolated mainly by sequencing by hybridization (SBH), and in some cases, sequences obtained from one or more public databases. The invention relates also to the proteins encoded by such polynucleotides, along with therapeutic, diagnostic and research utilities for these polynucleotides and proteins. These nucleic acid sequences are designated as SEQ ID NO: 1-337, or 675-836 and are provided in the Sequence Listing. In the nucleic acids provided in the Sequence Listing, A is adenine; C is cytosine; G is guanine; T is thymine; and N is any of the four bases or unknown. In the amino acids provided in the Sequence Listing, * corresponds to the stop codon.  
       [0010] The nucleic acid sequences of the present invention also include, nucleic acid sequences that hybridize to the complement of SEQ ID NO: 1-337, or 675-836 under stringent hybridization conditions; nucleic acid sequences which are allelic variants or species homologues of any of the nucleic acid sequences recited above, or nucleic acid sequences that encode a peptide comprising a specific domain or truncation of the peptides encoded by SEQ ID NO: 1-337, or 675-836. A polynucleotide comprising a nucleotide sequence having at least 90% identity to an identifying sequence of SEQ ID NO: 1-337, or 675-836 or a degenerate variant or fragment thereof. The identifying sequence can be 100 base pairs in length.  
       [0011] The nucleic acid sequences of the present invention also include the sequence information from the nucleic acid sequences of SEQ ID NO: 1-337, or 675-836. The sequence information can be a segment of any one of SEQ ID NO: 1-337, or 675-836 that uniquely identifies or represents the sequence information of SEQ ID NO: 1-337, or 675-836.  
       [0012] A collection as used in this application can be a collection of only one polynucleotide. The collection of sequence information or identifying information of each sequence can be provided on a nucleic acid array. In one embodiment, segments of sequence information are provided on a nucleic acid array to detect the polynucleotide that contains the segment. The array can be designed to detect full-match or mismatch to the polynucleotide that contains the segment. The collection can also be provided in a computer-readable format.  
       [0013] This invention also includes the reverse or direct complement of any of the nucleic acid sequences recited above; cloning or expression vectors containing the nucleic acid sequences; and host cells or organisms transformed with these expression vectors. Nucleic acid sequences (or their reverse or direct complements) according to the invention have numerous applications in a variety of techniques known to those skilled in the art of molecular biology, such as use as hybridization probes, use as primers for PCR, use in an array, use in computer-readable media, use in sequencing full-length genes, use for chromosome and gene mapping, use in the recombinant production of protein, and use in the generation of anti-sense DNA or RNA, their chemical analogs and the like.  
       [0014] In a preferred embodiment, the nucleic acid sequences of SEQ ID NO: 1-337, or 675-836 or novel segments or parts of the nucleic acids of the invention are used as primers in expression assays that are well known in the art. In a particularly preferred embodiment, the nucleic acid sequences of SEQ ID NO: 1-337, or 675-836 or novel segments or parts of the nucleic acids provided herein are used in diagnostics for identifying expressed genes or, as well known in the art and exemplified by Vollrath et al., Science 258:52-59 (1992), as expressed sequence tags for physical mapping of the human genome.  
       [0015] The isolated polynucleotides of the invention include, but are not limited to, a polynucleotide comprising any one of the nucleotide sequences set forth in SEQ ID NO: 1-337, or 675-836; a polynucleotide comprising any of the full length protein coding sequences of SEQ ID NO: 1-337, or 675-836; and a polynucleotide comprising any of the nucleotide sequences of the mature protein coding sequences of SEQ ID NO: 1-337, or 675-836. The polynucleotides of the present invention also include, but are not limited to, a polynucleotide that hybridizes under stringent hybridization conditions to (a) the complement of any one of the nucleotide sequences set forth in SEQ ID NO: 1-337, or 675-836; (b) a nucleotide sequence encoding any one of the amino acid sequences set forth in SEQ ID NO: 1-337, or 675-836; (c) a polynucleotide which is an allelic variant of any polynucleotides recited above; (d) a polynucleotide which encodes a species homologue (e.g. orthologs) of any of the proteins recited above; or (e) a polynucleotide that encodes a polypeptide comprising a specific domain or truncation of any of the polypeptides comprising an amino acid sequence set forth in SEQ ID NO: 338-674, or 837-998, or Tables 3, 5, 6, 8, or 9.  
       [0016] The isolated polypeptides of the invention include, but are not limited to, a polypeptide comprising any of the amino acid sequences set forth in the Sequence Listing; or the corresponding full length or mature protein. Polypeptides of the invention also include polypeptides with biological activity that are encoded by (a) any of the polynucleotides having a nucleotide sequence set forth in SEQ ID NO: 1-337, or 675-836; or (b) polynucleotides that hybridize to the complement of the polynucleotides of (a) under stringent hybridization conditions. Biologically active variants of any of the polypeptide sequences in the Sequence Listing, and “substantial equivalents” thereof (e.g., with at least about 65%, 70%, 75%, 80%, 85%, 90%, 95%, 98% or 99% amino acid sequence identity) that preferably retain biological activity are also contemplated. The polypeptides of the invention may be wholly or partially chemically synthesized but are preferably produced by recombinant means using the genetically engineered cells (e.g. host cells) of the invention.  
       [0017] The invention also provides compositions comprising a polypeptide of the invention. Polypeptide compositions of the invention may further comprise an acceptable carrier, such as a hydrophilic, e.g., pharmaceutically acceptable, carrier.  
       [0018] The invention also provides host cells transformed or transfected with a polynucleotide of the invention.  
       [0019] The invention also relates to methods for producing a polypeptide of the invention comprising growing a culture of the host cells of the invention in a suitable culture medium under conditions permitting expression of the desired polypeptide, and purifying the polypeptide from the culture or from the host cells. Preferred embodiments include those in which the protein produced by such processes is a mature form of the protein.  
       [0020] Polynucleotides according to the invention have numerous applications in a variety of techniques Known to those skilled in the art of molecular biology. These techniques include use as hybridization probes, use as oligomers, or primers, for PCR, use for chromosome and gene mapping, use in the recombinant production of protein, and use in generation of anti-sense DNA or RNA, their chemical analogs and the like. For example, when the expression of an mRNA is largely restricted to a particular cell or tissue type, polynucleotides of the invention can be used as hybridization probes to detect the presence of the particular cell or tissue mRNA in a sample using, e.g., in situ hybridization.  
       [0021] In other exemplary embodiments, the polynucleotides are used in diagnostics as expressed sequence tags for identifying expressed genes or, as well known in the art and exemplified by Vollrath et al., Science 258:52-59 (1992), as expressed sequence tags for physical mapping of the human genome.  
       [0022] The polypeptides according to the invention can be used in a variety of conventional procedures and methods that are currently applied to other proteins. For example, a polypeptide of the invention can be used to generate an antibody that specifically binds the polypeptide. Such antibodies, particularly monoclonal antibodies, are useful for detecting or quantitating the polypeptide in tissue. The polypeptides of the invention can also be used as molecular weight markers, and as a food supplement.  
       [0023] Methods are also provided for preventing, treating, or ameliorating a medical condition which comprises the step of administering to a mammalian subject a therapeutically effective amount of a composition comprising a polypeptide of the present invention and a pharmaceutically acceptable carrier.  
       [0024] In particular, the polypeptides and polynucleotides of the invention can be utilized, for example, in methods for the prevention and/or treatment of disorders involving aberrant protein expression or biological activity.  
       [0025] The present invention further relates to methods for detecting the presence of the polynucleotides or polypeptides of the invention in a sample. Such methods can, for example, be utilized as part of prognostic and diagnostic evaluation of disorders as recited herein and for the identification of subjects exhibiting a predisposition to such conditions. The invention provides a method for detecting the polynucleotides of the invention in a sample, comprising contacting the sample with a compound that binds to and forms a complex with the polynucleotide of interest for a period sufficient to form the complex and under conditions sufficient to form a complex and detecting the complex such that if a complex is detected, the polynucleotide of interest is detected. The invention also provides a method for detecting the polypeptides of the invention in a sample comprising contacting the sample with a compound that binds to and forms a complex with the polypeptide under conditions and for a period sufficient to form the complex and detecting the formation of the complex such that if a complex is formed, the polypeptide is detected.  
       [0026] The invention also provides kits comprising polynucleotide probes and/or monoclonal antibodies, and optionally quantitative standards, for carrying out methods of the invention. Furthermore, the invention provides methods for evaluating the efficacy of drugs, and monitoring the progress of patients, involved in clinical trials for the treatment of disorders as recited above.  
       [0027] The invention also provides methods for the identification of compounds that modulate (i.e., increase or decrease) the expression or activity of the polynucleotides and/or polypeptides of the invention. Such methods can be utilized, for example, for the identification of compounds that can ameliorate symptoms of disorders as recited herein. Such methods can include, but are not limited to, assays for identifying compounds and other substances that interact with (e.g., bind to) the polypeptides of the invention. The invention provides a method for identifying a compound that binds to the polypeptides of the invention comprising contacting the compound with a polypeptide of the invention in a cell for a time sufficient to form a polypeptide/compound complex, wherein the complex drives expression of a reporter gene sequence in the cell; and detecting the complex by detecting the reporter gene sequence expression such that if expression of the reporter gene is detected the compound that binds to a polypeptide of the invention is identified.  
       [0028] The methods of the invention also provide methods for treatment which involve the administration of the polynucleotides or polypeptides of the invention to individuals exhibiting symptoms or tendencies. In addition, the invention encompasses methods for treating diseases or disorders as recited herein comprising administering compounds and other substances that modulate the overall activity of the target gene products. Compounds and other substances can affect such modulation either on the level of target gene/protein expression or target protein activity.  
       [0029] The polypeptides of the present invention and the polynucleotides encoding them are also useful for the same functions known to one of skill in the art as the polypeptides and polynucleotides to which they have homology (set forth in Table 2); for which they have a signature region (as set forth in Table 3); or for which they have homology to a gene family (as set forth in Table 4). If no homology is set forth for a sequence, then the polypeptides and polynucleotides of the present invention are useful for a variety of applications, as described herein, including use in arrays for detection.  
       DETAILED DESCRIPTION OF THE INVENTION  
       Definitions  
       [0030] It must be noted that as used herein and in the appended claims, the singular forms “a”, “an” and “the” include plural references unless the context clearly dictates otherwise.  
       [0031] The term “active” refers to those forms of the polypeptide which retain the biologic and/or immunologic activities of any naturally occurring polypeptide. According to the invention, the terms “biologically active” or “biological activity” refer to a protein or peptide having structural, regulatory or biochemical functions of a naturally occurring molecule. Likewise “immunologically active” or “immunological activity” refers to the capability of the natural, recombinant or synthetic polypeptide to induce a specific immune response in appropriate animals or cells and to bind with specific antibodies.  
       [0032] The term “activated cells” as used in this application are those cells which are engaged in extracellular or intracellular membrane trafficking, including the export of secretory or enzymatic molecules as part of a normal or disease process.  
       [0033] The terms “complementary” or “complementary” refer to the natural binding of polynucleotides by base pairing. For example, the sequence 5′-AGT-3′ binds to the complementary sequence 3′-TCA-5′. Complementary between two single-stranded molecules may be “partial” such that only certain portion(s) of the nucleic acids bind or it may be “complete” such that total complementarity exists between the single stranded molecules. The degree of complementarity between the nucleic acid strands has significant effects on the efficiency and strength of the hybridization between the nucleic acid strands.  
       [0034] The term “embryonic stem cells (ES)” refers to a cell that can give rise to many differentiated cell types in an embryo or an adult, including the germ cells. The term “germ line stem cells (GSCs)” refers to stem cells derived from primordial stem cells that provide a steady and continuous source of germ cells for the production of gametes. The term “primordial germ cells (PGCs)” refers to a small population of cells set aside from other cell lineages particularly from the yolk sac, mesenteries, or gonadal ridges during embryogenesis that have the potential to differentiate into germ cells and other cells. PGCs are the source from which GSCs and ES cells are derived. The PGCs, the GSCs and the ES cells are capable of self-renewal. Thus these cells not only populate the germ line and give rise to a plurality of terminally differentiated cells that comprise the adult specialized organs, but are able to regenerate themselves.  
       [0035] The term “expression modulating fragment,” EMF, means a series of nucleotides which modulates the expression of an operably linked ORF or another EMF.  
       [0036] As used herein, a sequence is said to “modulate the expression of an operably linked sequence” when the expression of the sequence is altered by the presence of the EMF. EMFs include, but are not limited to, promoters, and promoter modulating sequences (inducible elements). One class of EMFs are nucleic acid fragments which induce the expression of an operably linked ORF in response to a specific regulatory factor or physiological event.  
       [0037] The terms “nucleotide sequence” or “nucleic acid” or “polynucleotide” or “oligonucleotide” are used interchangeably and refer to a heteropolymer of nucleotides or the sequence of these nucleotides. These phrases also refer to DNA or RNA of genomic or synthetic origin which may be single-stranded or double-stranded and may represent the sense or the antisense strand, to peptide nucleic acid (PNA) or to any DNA-like or RNA-like material. In the sequences herein A is adenine, C is cytosine, T is thymine, G is guanine and N is A, C, G, or T (U) or unknown. It is contemplated that where the polynucleotide is RNA, the T (thymine) in the sequences provided herein is substituted with U (uracil). Generally, nucleic acid segments provided by this invention may be assembled from fragments of the genome and short oligonucleotide linkers, or from a series of oligonucleotides, or from individual nucleotides, to provide a synthetic nucleic acid which is capable of being expressed in a recombinant transcriptional unit comprising regulatory elements derived from a microbial or viral operon, or a eukaryotic gene.  
       [0038] The terms “oligonucleotide fragment” or a “polynucleotide fragment”, “portion,” or “segment” or “probe” or “primer” are used interchangeably and refer to a sequence of nucleotide residues which are at least about 5 nucleotides, more preferably at least about 7 nucleotides, more preferably at least about 9 nucleotides, more preferably at least about 11 nucleotides and most preferably at least about 17 nucleotides. The fragment is preferably less than about 500 nucleotides, preferably less than about 200 nucleotides, more preferably less than about 100 nucleotides, more preferably less than about 50 nucleotides and most preferably less than 30 nucleotides. Preferably the probe is from about 6 nucleotides to about 200 nucleotides, preferably from about 15 to about 50 nucleotides, more preferably from about 17 to 30 nucleotides and most preferably from about 20 to 25 nucleotides. Preferably the fragments can be used in polymerase chain reaction (PCR), various hybridization procedures or microarray procedures to identify or amplify identical or related parts of mRNA or DNA molecules. A fragment or segment may uniquely identify each polynucleotide sequence of the present invention. Preferably the fragment comprises a sequence substantially similar to any one of SEQ ID NO: 1-337, or 675-836.  
       [0039] Probes may, for example, be used to determine whether specific mRNA molecules are present in a cell or tissue or to isolate similar nucleic acid sequences from chromosomal DNA as described by Walsh et al. (Walsh, P. S. et al., 1992, PCR Methods Appl 1:241-250). They may be labeled by nick translation, Klenow fill-in reaction, PCR, or other methods well known in the art. Probes of the present invention, their preparation and/or labeling are elaborated in Sambrook, J. et al., 1989, Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory, NY; or Ausubel, F. M. et al., 1989, Current Protocols in Molecular Biology, John Wiley &amp; Sons, New York N.Y., both of which are incorporated herein by reference in their entirety.  
       [0040] The nucleic acid sequences of the present invention also include the sequence information from the nucleic acid sequences of SEQ ID NO: 1-337, or 675-836. The sequence information can be a segment of any one of SEQ ID NO: 1-337, or 675-836 that uniquely identifies or represents the sequence information of that sequence of SEQ ID NO: 1-337, or 675-836, or those segments identified in Tables 3, 5, 6, 8, or 9. One such segment can be a twenty-mer nucleic acid sequence because the probability that a twenty-mer is fully matched in the human genome is 1 in 300. In the human genome, there are three billion base pairs in one set of chromosomes. Because 4 20  possible twenty-mers exist, there are 300 times more twenty-mers than there are base pairs in a set of human chromosomes. Using the same analysis, the probability for a seventeen-mer to be fully matched in the human genome is approximately 1 in 5. When these segments are used in arrays for expression studies, fifteen-mer segments can be used. The probability that the fifteen-mer is fully matched in the expressed sequences is also approximately one in five because expressed sequences comprise less than approximately 5% of the entire genome sequence.  
       [0041] Similarly, when using sequence information for detecting a single mismatch, a segment can be a twenty-five mer. The probability that the twenty-five mer would appear in a human genome with a single mismatch is calculated by multiplying the probability for a full match (1÷4 25 ) times the increased probability for mismatch at each nucleotide position (3×25). The probability that an eighteen mer with a single mismatch can be detected in an array for expression studies is approximately one in five. The probability that a twenty-mer with a single mismatch can be detected in a human genome is approximately one in five.  
       [0042] The term “open reading frame,” ORF, means a series of nucleotide triplets coding for amino acids without any termination codons and is a sequence translatable into protein.  
       [0043] The terms “operably linked” or “operably associated” refer to functionally related nucleic acid sequences. For example, a promoter is operably associated or operably linked with a coding sequence if the promoter controls the transcription of the coding sequence. While operably linked nucleic acid sequences can be contiguous and in the same reading frame, certain genetic elements e.g. repressor genes are not contiguously linked to the coding sequence but still control transcription/translation of the coding sequence.  
       [0044] The term “pluripotent” refers to the capability of a cell to differentiate into a number of differentiated cell types that are present in an adult organism. A pluripotent cell is restricted in its differentiation capability in comparison to a totipotent cell.  
       [0045] The terms “polypeptide” or “peptide” or “amino acid sequence” refer to an oligopeptide, peptide, polypeptide or protein sequence or fragment thereof and to naturally occurring or synthetic molecules. A polypeptide “fragment,” “portion,” or “segment” is a stretch of amino acid residues of at least about 5 amino acids, preferably at least about 7 amino acids, more preferably at least about 9 amino acids and most preferably at least about 17 or more amino acids. The peptide preferably is not greater than about 200 amino acids, more preferably less than 150 amino acids and most preferably less than 100 amino acids. Preferably the peptide is from about 5 to about 200 amino acids. To be active, any polypeptide must have sufficient length to display biological and/or immunological activity.  
       [0046] The term “naturally occurring polypeptide” refers to polypeptides produced by cells that have not been genetically engineered and specifically contemplates various polypeptides arising from post-translational modifications of the polypeptide including. but not limited to, acetylation, carboxylation, glycosylation, phosphorylation, lipidation and acylation.  
       [0047] The term “translated protein coding portion” means a sequence which encodes for the full-length protein which may include any leader sequence or any processing sequence.  
       [0048] The term “mature protein coding sequence” means a sequence which encodes a peptide or protein without a signal or leader sequence. The “mature protein portion” means that portion of the protein which does not include a signal or leader sequence. The peptide may have been produced by processing in the cell which removes any leader/signal sequence. The mature protein portion may or may not include the initial methionine residue. The methionine residue may be removed from the protein during processing in the cell. The peptide may be produced synthetically or the protein may have been produced using a polynucleotide only encoding for the mature protein coding sequence.  
       [0049] The term “derivative” refers to polypeptides chemically modified by such techniques as ubiquitination, labeling (e.g., with radionuclides or various enzymes), covalent polymer attachment such as pegylation (derivatization with polyethylene glycol) and insertion or substitution by chemical synthesis of amino acids such as ornithine, which do not normally occur in human proteins.  
       [0050] The term “variant” (or “analog”) refers to any polypeptide differing from naturally occurring polypeptides by amino acid insertions, deletions, and substitutions, created using, e g., recombinant DNA techniques. Guidance in determining which amino acid residues may be replaced, added or deleted without abolishing activities of interest, may be found by comparing the sequence of the particular polypeptide with that of homologous peptides and minimizing the number of amino acid sequence changes made in regions of high homology (conserved regions) or by replacing amino acids with consensus sequence.  
       [0051] Alternatively, recombinant variants encoding these same or similar polypeptides may be synthesized or selected by making use of the “redundancy” in the genetic code. Various codon substitutions, such as the silent changes which produce various restriction sites, may be introduced to optimize cloning into a plasmid or viral vector or expression in a particular prokaryotic or eukaryotic system. Mutations in the polynucleotide sequence may be reflected in the polypeptide or domains of other peptides added to the polypeptide to modify the properties of any part of the polypeptide, to change characteristics such as ligand-binding, affinities, interchain affinities, or degradation/turnover rate.  
       [0052] Preferably, amino acid “substitutions” are the result of replacing one amino acid with another amino acid having similar structural and/or chemical properties, i.e., conservative amino acid replacements. “Conservative” amino acid substitutions may be made on the basis of similarity in polarity, charge, solubility, hydrophobicity, hydrophilicity, and/or the amphipathic nature of the residues involved. For example, nonpolar (hydrophobic) amino acids include alanine, leucine, isoleucine, valine, proline, phenylalanine, tlyptophan, and methionine; polar neutral amino acids include glycine, serine, threonine, cysteine, tyrosine, asparagine, and glutamine; positively charged (basic) amino acids include arginine, lysine, and histidine; and negatively charged (acidic) amino acids include aspartic acid and glutamic acid. “Insertions” or “deletions” are preferably in the range of about 1 to 20 amino acids, more preferably 1 to 10 amino acids. The variation allowed may be experimentally determined by systematically making insertions, deletions, or substitutions of amino acids in a polypeptide molecule using recombinant DNA techniques and assaying the resulting recombinant variants for activity.  
       [0053] Alternatively, where alteration of function is desired, insertions, deletions or non-conservative alterations can be engineered to produce altered polypeptides. Such alterations can, for example, alter one or more of the biological functions or biochemical characteristics of the polypeptides of the invention. For example, such alterations may change polypeptide characteristics such as ligand-binding affinities, interchain affinities, or degradation/turnover rate. Further, such alterations can be selected so as to generate polypeptides that are better suited for expression, scale up and the like in the host cells chosen for expression. For example, cysteine residues can be deleted or substituted with another amino acid residue in order to eliminate disulfide bridges.  
       [0054] The terms “purified” or “substantially purified” as used herein denotes that the indicated nucleic acid or polypeptide is present in the substantial absence of other biological macromolecules, e.g., polynucleotides, proteins, and the like. In one embodiment, the polynucleotide or polypeptide is purified such that it constitutes at least 95% by weight, more preferably at least 99% by weight, of the indicated biological macromolecules present (but water, buffers, and other small molecules, especially molecules having a molecular weight of less than 1000 daltons, can be present).  
       [0055] The term “isolated” as used herein refers to a nucleic acid or polypeptide separated from at least one other component (e.g., nucleic acid or polypeptide) present with the nucleic acid or polypeptide in its natural source. In one embodiment, the nucleic acid or polypeptide is found in the presence of (if anything) only a solvent, buffer, ion, or other component normally present in a solution of the same. The terms “isolated” and “purified” do not encompass nucleic acids or polypeptides present in their natural source.  
       [0056] The term “recombinant,” when used herein to refer to a polypeptide or protein, means that a polypeptide or protein is derived from recombinant (e.g., microbial, insect, or mammalian) expression systems. “Microbial” refers to recombinant polypeptides or proteins made in bacterial or fungal (e.g., yeast) expression systems. As a product, “recombinant microbial” defines a polypeptide or protein essentially free of native endogenous substances and unaccompanied by associated native glycosylation. Polypeptides or proteins expressed in most bacterial cultures, e.g.,  E. coli , will be free of glycosylation modifications; polypeptides or proteins expressed in yeast will have a glycosylation pattern in general different from those expressed in mammalian cells.  
       [0057] The term “recombinant expression vehicle or vector” refers to a plasmid or phage or virus or vector, for expressing a polypeptide from a DNA (RNA) sequence. An expression vehicle can comprise a transcriptional unit comprising an assembly of (1) a genetic element or elements having a regulatory role in gene expression, for example, promoters or enhancers, (2) a structural or coding sequence which is transcribed into mRNA and translated into protein, and (3) appropriate transcription initiation and termination sequences. Structural units intended for use in yeast or eukaryotic expression systems preferably include a leader sequence enabling extracellular secretion of translated protein by a host cell. Alternatively, where recombinant protein is expressed without a leader or transport sequence, it may include an amino terminal methionine residue. This residue may or may not be subsequently cleaved from the expressed recombinant protein to provide a final product.  
       [0058] The term “recombinant expression system” means host cells which have stably integrated a recombinant transcriptional unit into chromosomal DNA or caney the recombinant transcriptional unit extrachromosomally. Recombinant expression systems as defined herein will express heterologous polypeptides or proteins upon induction of the regulatory elements linked to the DNA segment or synthetic gene to be expressed. This term also means host cells which have stably integrated a recombinant genetic element or elements having a regulatory role in gene expression, for example, promoters or enhancers. Recombinant expression systems as defined herein will express polypeptides or proteins endogenous to the cell upon induction of the regulatory elements linked to the endogenous DNA segment or gene to be expressed. The cells can be prokaryotic or eukaryotic.  
       [0059] The term “secreted” includes a protein that is transported across or through a membrane, including transport as a result of signal sequences in its amino acid sequence when it is expressed in a suitable host cell. “Secreted” proteins include without limitation proteins secreted wholly (e.g., soluble proteins) or partially (e.g., receptors) from the cell in which they are expressed. “Secreted” proteins also include without limitation proteins that are transported across the membrane of the endoplasmic reticulum. “Secreted” proteins are also intended to include proteins containing non-typical signal sequences (e.g. Interleukin-1 Beta, see Krasney, P. A. and Young, P. R. (1992) Cytokine 4(2): 134-143) and factors released from damaged cells (e.g. Interleukin-1 Receptor Antagonist. see Arend, W. P. et. al. (1998) Annu. Rev. Immunol. 16:27-55)  
       [0060] Where desired, an expression vector may be designed to contain a “signal or leader sequence” which will direct the polypeptide through the membrane of a cell. Such a sequence may be naturally present on the polypeptides of the present invention or provided from heterologous protein sources by recombinant DNA techniques.  
       [0061] The term “stringent” is used to refer to conditions that are commonly understood in the art as stringent. Stringent conditions can include highly stringent conditions (i.e., hybridization to filter-bound DNA in 0.5 M NaHPO 4 , 7% sodium dodecyl sulfate (SDS), 1 mM EDTA at 65° C., and washing in 0.1×SSC/0.1% SDS at 68° C.), and moderately stringent conditions (i.e., washing in 0.2×SSC/0.1% SDS at 42° C.). Other exemplary hybridization conditions are described herein in the examples.  
       [0062] In instances of hybridization of deoxyoligonucleotides, additional exemplary stringent hybridization conditions include washing in 6×SSC/0.05% sodium pyrophosphate at 37° C. (for 14-base oligonucleotides), 48° C. (for 17-base oligonucleotides), 55° C. (for 20-base oligonucleotides), and 60° C. (for 23-base oligonucleotides).  
       [0063] As used herein, “substantially equivalent” or “substantially similar” can refer both to nucleotide and amino acid sequences, for example a mutant sequence, that varies from a reference sequence by one or more substitutions, deletions, or additions, the net effect of which does not result in an adverse functional dissimilarity between the reference and subject sequences. Typically, such a substantially equivalent sequence varies from one of those listed herein by no more than about 35% (i.e., the number of individual residue substitutions, additions, and/or deletions in a substantially equivalent sequence, as compared to the corresponding reference sequence, divided by the total number of residues in the substantially equivalent sequence is about 0.35 or less). Such a sequence is said to have 65% sequence identity to the listed sequence. In one embodiment, a substantially equivalent, e.g., mutant, sequence of the invention varies from a listed sequence by no more than 30% (70% sequence identity); in a variation of this embodiment, by no more than 25% (75% sequence identity); and in a further variation of this embodiment, by no more than 20% (80% sequence identity) and in a further variation of this embodiment, by no more than 10% (90% sequence identity) and in a further variation of this embodiment, by no more that 5% (95% sequence identity). Substantially equivalent, e.g., mutant, amino acid sequences according to the invention preferably have at least 80% sequence identity with a listed amino acid sequence, more preferably at least 85% sequence identity, more preferably at least 90% sequence identity, more preferably at least 95% sequence identity, more preferably at least 98% sequence identity, and most preferably at least 99% sequence identity. Substantially equivalent nucleotide sequence of the invention can have lower percent sequence identities, taking into account, for example, the redundancy or degeneracy of the genetic code. Preferably, the nucleotide sequence has at least about 65% identity, more preferably at least about 75% identity, more preferably at least about 80% sequence identity, more preferably at least 85% sequence identity, more preferably at least 90% sequence identity, more preferably at least about 95% sequence identity, more preferably at least 98% sequence identity, and most preferably at least 99% sequence identity. For the purposes of the present invention, sequences having substantially equivalent biological activity and substantially equivalent expression characteristics are considered substantially equivalent. For the purposes of determining equivalence, truncation of the mature sequence (e.g., via a mutation which creates a new stop codon) should be disregarded. Sequence identity may be determined, e.g., using the Jotun Hein method (Hein, J. (1990) Methods Enzymol. 183:626-645). Identity between sequences can also be determined by other methods known in the art, e.g. by varying hybridization conditions.  
       [0064] The term “totipotent” refers to the capability of a cell to differentiate into all of the cell types of an adult organism.  
       [0065] The term “transformation” means introducing DNA into a suitable host cell so that the DNA is replicable, either as an extrachromosomal element, or by chromosomal integration. The term “transfection” refers to the taking up of an expression vector by a suitable host cell, whether or not any coding sequences are in fact expressed. The term “infection” refers to the introduction of nucleic acids into a suitable host cell by use of a virus or viral vector.  
       [0066] As used herein, an “uptake modulating fragment,” UMF, means a series of nucleotides which mediate the uptake of a linked DNA fragment into a cell. UMFs can be readily identified using known UMFs as a target sequence or target motif with the computer-based systems described below. The presence and activity of a UMF can be confirmed by attaching the suspected UMF to a marker sequence. The resulting nucleic acid molecule is then incubated with an appropriate host under appropriate conditions and the uptake of the marker sequence is determined. As described above, a UMF will increase the frequency of uptake of a linked marker sequence.  
       [0067] Each of the above terms is meant to encompass all that is described for each, unless the context dictates otherwise.  
       NUCLEIC ACIDS OF THE INVENTION  
       [0068] Nucleotide sequences of the invention are set forth in the Sequence Listing.  
       [0069] The isolated polynucleotides of the invention include a polynucleotide comprising the nucleotide sequences of SEQ ID NO: 1-337, or 675-836; a polynucleotide encoding any one of the peptide sequences of SEQ ID NO: 1-337, or 675-836; and a polynucleotide comprising the nucleotide sequence encoding the mature protein coding sequence of the polynucleotides of any one of SEQ ID NO: 1-337, or 675-836. The polynucleotides of the present invention also include, but are not limited to, a polynucleotide that hybridizes under stringent conditions to (a) the complement of any of the nucleotides sequences of SEQ ID NO: 1-337, or 675-836; (b) nucleotide sequences encoding any one of the amino acid sequences set forth in the Sequence Listing, or Table 8; (c) a polynucleotide which is an allelic variant of any polynucleotide recited above; (d) a polynucleotide which encodes a species homologue of any of the proteins recited above; or (e) a polynucleotide that encodes a polypeptide comprising a specific domain or truncation of the polypeptides of SEQ ID NO: 338-674, or 837-998 (for example, as set forth in Tables 3, 5, 6, 8, or 9). Domains of interest may depend on the nature of the encoded polypeptide; e.g., domains in receptor-like polypeptides include ligand-binding, extracellular, transmembrane, or cytoplasmic domains, or combinations thereof; domains in immunoglobulin-like proteins include the variable immunoglobulin-like domains; domains in enzyme-like polypeptides include catalytic and substrate binding domains; and domains in ligand polypeptides include receptor-binding domains.  
       [0070] The polynucleotides of the invention include naturally occurring or wholly or partially synthetic DNA, e.g., cDNA and genomic DNA, and RNA, e.g., mRNA. The polynucleotides may include entire coding region of the cDNA or may represent a portion of the coding region of the cDNA.  
       [0071] The present invention also provides genes corresponding to the cDNA sequences disclosed herein. The corresponding genes can be isolated in accordance with known methods using the sequence information disclosed herein. Such methods include the preparation of probes or primers from the disclosed sequence information for identification and/or amplification of genes in appropriate genomic libraries or other sources of genomic materials. Further 5′ and 3′ sequence can be obtained using methods known in the art. For example, full length cDNA or genomic DNA that corresponds to any of the polynucleotides of SEQ ID NO: 1-337, or 675-836 can be obtained by screening appropriate cDNA or genomic DNA libraries under suitable hybridization conditions using any of the polynucleotides of SEQ ID NO: 1-337, or 675-836 or a portion thereof as a probe. Alternatively, the polynucleotides of SEQ ID NO: 1-337, or 675-836 may be used as the basis for suitable primer(s) that allow identification and/or amplification of genes in appropriate genomic DNA or cDNA libraries.  
       [0072] The nucleic acid sequences of the invention can be assembled from ESTs and sequences (including cDNA and genomic sequences) obtained from one or more public databases, such as dbEST, gbpri, and UniGene. The EST sequences can provide identifying sequence information, representative fragment or segment information, or novel segment information for the full-length gene.  
       [0073] The polynucleotides of the invention also provide polynucleotides including nucleotide sequences that are substantially equivalent to the polynucleotides recited above. Polynucleotides according to the invention can have, e.g., at least about 65%, at least about 70%, at least about 75%, at least about 80%, 81%, 82%, 83%, 84%, more typically at least about 85%, 86%, 87%, 88%, 89%, more typically at least about 90%, 91%, 92%, 93%, 94%, and even more typically at least about 95%, 96%, 97%, 98%, 99% sequence identity to a polynucleotide recited above.  
       [0074] Included within the scope of the nucleic acid sequences of the invention are nucleic acid sequence fragments that hybridize under stringent conditions to any of the nucleotide sequences of SEQ ID NO: 1-337, or 675-836, or complements thereof, which fragment is greater than about 5 nucleotides, preferably 7 nucleotides, more preferably greater than 9 nucleotides and most preferably greater than 17 nucleotides. Fragments of, e.g. 15, 17, or 20 nucleotides or more that are selective for (i.e. specifically hybridize to) any one of the polynucleotides of the invention are contemplated. Probes capable of specifically hybridizing to a polynucleotide can differentiate polynucleotide sequences of the invention from other polynucleotide sequences in the same family of genes or can differentiate human genes from genes of other species, and are preferably based on unique nucleotide sequences.  
       [0075] The sequences falling within the scope of the present invention are not limited to these specific sequences, but also include allelic and species variations thereof. Allelic and species variations can be routinely determined by comparing the sequence provided in SEQ ID NO: 1-337, or 675-836, a representative fragment thereof, or a nucleotide sequence at least 90% identical, preferably 95% identical, to SEQ ID NO: 1-337, or 675-836 with a sequence from another isolate of the same species. Furthermore, to accommodate codon variability, the invention includes nucleic acid molecules coding for the same amino acid sequences as do the specific ORFs disclosed herein. In other words, in the coding region of an ORF, substitution of one codon for another codon that encodes the same amino acid is expressly contemplated.  
       [0076] The nearest neighbor or homology results for the nucleic acids of the present invention, including SEQ ID NO: 1-337, or 675-836 can be obtained by searching a database using an algorithm or a program. Preferably, a BLAST (Basic Local Alignment Search Tool) program is used to search for local sequence alignments (Altshul, S. F. J Mol. Evol. 36 290-300 (1993) and Altschul S. F. et al. J. Mol. Biol. 21:403-410 (1990)). Alternatively a FASTA version 3 search against Genpept, using FASTXY algorithm may be performed.  
       [0077] Species homologs (or orthologs) of the disclosed polynucleotides and proteins are also provided by the present invention. Species homologs may be isolated and identified by making suitable probes or primers from the sequences provided herein and screening a suitable nucleic acid source from the desired species.  
       [0078] The invention also encompasses allelic variants of the disclosed polynucleotides or proteins; that is, naturally-occurring alternative forms of the isolated polynucleotide which also encode proteins which are identical, homologous or related to that encoded by the polynucleotides.  
       [0079] The nucleic acid sequences of the invention are further directed to sequences which encode variants of the described nucleic acids. These amino acid sequence variants may be prepared by methods known in the art by introducing appropriate nucleotide changes into a native or variant polynucleotide. There are two variables in the construction of amino acid sequence variants: the location of the mutation and the nature of the mutation. Nucleic acids encoding the amino acid sequence variants are preferably constructed by mutating the polynucleotide to encode an amino acid sequence that does not occur in nature. These nucleic acid alterations can be made at sites that differ in the nucleic acids from different species (variable positions) or in highly conserved regions (constant regions). Sites at such locations will typically be modified in series, e.g., by substituting first with conservative choices (e.g., hydrophobic amino acid to a different hydrophobic amino acid) and then with more distant choices (e.g., hydrophobic amino acid to a charged amino acid), and then deletions or insertions may be made at the target site. Amino acid sequence deletions generally range from about 1 to 30 residues, preferably about 1 to 10 residues, and are typically contiguous. Amino acid insertions include amino- and/or carboxyl-terminal fusions ranging in length from one to one hundred or more residues, as well as intrasequence insertions of single or multiple amino acid residues. Intrasequence insertions may range generally from about 1 to 10 amino residues, preferably from 1 to 5 residues. Examples of terminal insertions include the heterologous signal sequences necessary for secretion or for intracellular targeting in different host cells and sequences such as FLAG or poly-histidine sequences useful for purifying the expressed protein.  
       [0080] In a preferred method, polynucleotides encoding the novel amino acid sequences are changed via site-directed mutagenesis. This method uses oligonucleotide sequences to alter a polynucleotide to encode the desired amino acid variant, as well as sufficient adjacent nucleotides on both sides of the changed amino acid to form a stable duplex on either side of the site of being changed. In general, the techniques of site-directed mutagenesis are well known to those of skill in the art and this technique is exemplified by publications such as, Edelman et al., DNA 2:183 (1983). A versatile and efficient method for producing site-specific changes in a polynucleotide sequence was published by Zoller and Smith,  Nucleic Acids Res . 10:6487-6500 (1982). PCR may also be used to create amino acid sequence variants of the novel nucleic acids. When small amounts of template DNA are used as starting material, primer(s) that differs slightly in sequence from the corresponding region in the template DNA can generate the desired amino acid variant. PCR amplification results in a population of product DNA fragments that differ from the polynucleotide template encoding the polypeptide at the position specified by the primer. The product DNA fragments replace the corresponding region in the plasmid and this gives a polynucleotide encoding the desired amino acid variant.  
       [0081] A further technique for generating amino acid variants is the cassette mutagenesis technique described in Wells et al.,  Gene  34:315 (1985); and other mutagenesis techniques well known in the art, such as, for example, the techniques in Sambrook et al., supra, and  Current Protocols in Molecular Biology , Ausubel et al. Due to the inherent degeneracy of the genetic code, other DNA sequences which encode substantially the same or a functionally equivalent amino acid sequence may be used in the practice of the invention for the cloning and expression of these novel nucleic acids. Such DNA sequences include those which are capable of hybridizing to the appropriate novel nucleic acid sequence under stringent conditions.  
       [0082] Polynucleotides encoding preferred polypeptide truncations of the invention could be used to generate polynucleotides encoding chimeric or fusion proteins comprising one or more domains of the invention and heterologous protein sequences.  
       [0083] The polynucleotides of the invention additionally include the complement of any of the polynucleotides recited above. The polynucleotide can be DNA (genomic, cDNA, amplified, or synthetic) or RNA. Methods and algorithms for obtaining such polynucleotides are well known to those of skill in the art and can include, for example, methods for determining hybridization conditions that can routinely isolate polynucleotides of the desired sequence identities.  
       [0084] In accordance with the invention, polynucleotide sequences comprising the mature protein coding sequences corresponding to any one of SEQ ID NO: 1-337, or 675-836, or functional equivalents thereof, may be used to generate recombinant DNA molecules that direct the expression of that nucleic acid, or a functional equivalent thereof, in appropriate host cells. Also included are the cDNA inserts of any of the clones identified herein.  
       [0085] A polynucleotide according to the invention can be joined to any of a variety of other nucleotide sequences by well-established recombinant DNA techniques (see Sambrook J et al. (1989) Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory, NY). Useful nucleotide sequences for joining to polynucleotides include an assortment of vectors, e.g., plasmids, cosmids, lambda phage derivatives, phagemids, and the like, that are well known in the art. Accordingly, the invention also provides a vector including a polynucleotide of the invention and a host cell containing the polynucleotide. In general, the vector contains an origin of replication functional in at least one organism, convenient restriction endonuclease sites, and a selectable marker for the host cell. Vectors according to the invention include expression vectors, replication vectors, probe generation vectors, and sequencing vectors. A host cell according to the invention can be a prokaryotic or eukaryotic cell and can be a unicellular organism or part of a multicellular organism.  
       [0086] The present invention further provides recombinant constructs comprising a nucleic acid having any of the nucleotide sequences of SEQ ID NO: 1-337, or 675-836 or a fragment thereof or any other polynucleotides of the invention. In one embodiment, the recombinant constructs of the present invention comprise a vector, such as a plasmid or viral vector, into which a nucleic acid having any of the nucleotide sequences of SEQ ID NO: 1-337, or 675-836 or a fragment thereof is inserted, in a forward or reverse orientation. In the case of a vector comprising one of the ORFs of the present invention, the vector may further comprise regulatory sequences, including for example, a promoter, operably linked to the ORF. Large numbers of suitable vectors and promoters are known to those of skill in the art and are commercially available for generating the recombinant constructs of the present invention. The following vectors are provided by way of example: Bacterial: pBs, phagescript, PsiX174, pBluescript SK, pBs KS, pNH8a, pNH16a, pNH18a, pNH46a (Stratagene), pTrc99A, pKK223-3, pKK233-3, pDR540, pRIT5 (Pharmacia); Eukaryotic: pWLneo, pSV2cat, pOG44, PXTI, pSG (Stratagene) pSVK3, pBPV, pMSG, pSVL (Pharmacia).  
       [0087] The isolated polynucleotide of the invention may be operably linked to an expression control sequence such as the pMT2 or pED expression vectors disclosed in Kaufman et al.,  Nucleic Acids Res . 19, 4485-4490 (1991), in order to produce the protein recombinantly. Many suitable expression control sequences are known in the art. General methods of expressing recombinant proteins are also known and are exemplified in R. Kaufman,  Methods in Enzymology  185, 537-566 (1990). As defined herein “operably linked” means that the isolated polynucleotide of the invention and an expression control sequence are situated within a vector or cell in such a way that the protein is expressed by a host cell which has been transformed (transfected) with the ligated polynucleotide/expression control sequence.  
       [0088] Promoter regions can be selected from any desired gene using CAT (chloramphenicol transferase) vectors or other vectors with selectable markers. Two appropriate vectors are pKK232-8 and pCM7. Particular named bacterial promoters include lacI, lacZ, T3, T7, gpt, lambda PR, and trc. Eukaryotic promoters include CMV immediate early, HSV thymidine kinase, early and late SV40, LTRs from retrovirus, and mouse metallothionein-I. Selection of the appropriate vector and promoter is well within the level of ordinary skill in the art. Generally, recombinant expression vectors will include origins of replication and selectable markers permitting transformation of the host cell, e.g., the ampicillin resistance gene of  E. coli  and  S. cerevisiae  TRP1 gene, and a promoter derived from a highly expressed gene to direct transcription of a downstream structural sequence. Such promoters can be derived from operons encoding lycolytic enzymes such as 3-phosphoglycerate kinase (PGK), a-factor, acid phosphatase, or heat shock proteins, among others. The heterologous structural sequence is assembled in appropriate phase with translation initiation and termination sequences, and preferably, a leader sequence capable of directing secretion of translated protein into the periplasmic space or extracellular medium. Optionally, the heterologous sequence can encode a fusion protein including an amino terminal identification peptide imparting desired characteristics, e.g., stabilization or simplified purification of expressed recombinant product. Useful expression vectors for bacterial use are constructed by inserting a structural DNA sequence encoding a desired protein together with suitable translation initiation and termination signals in operable reading phase with a functional promoter. The vector will comprise one or more phenotypic selectable markers and an origin of replication to ensure maintenance of the vector and to, if desirable, provide amplification within the host. Suitable prokaryotic hosts for transformation include  E. coli, Bacillus subtilis, Salmonella typhimurium  and various species within the genera Pseudomonas, Streptomyces, and Staphylococcus, although others may also be employed as a matter of choice.  
       [0089] As a representative but non-limiting example, useful expression vectors for bacterial use can comprise a selectable marker and bacterial origin of replication derived from commercially available plasmids comprising genetic elements of the well known cloning vector pBR322 (ATCC 37017). Such commercial vectors include, for example, pKK223-3 (Pharmacia Fine Chemicals, Uppsala, Sweden) and GEM 1 (Promega Biotech, Madison, Wis., USA). These pBR322 “backbone” sections are combined with an appropriate promoter and the structural sequence to be expressed. Following transformation of a suitable host strain and growth of the host strain to an appropriate cell density, the selected promoter is induced or derepressed by appropriate means (e.g., temperature shift or chemical induction) and cells are cultured for an additional period. Cells are typically harvested by centrifugation, disrupted by physical or chemical means, and the resulting crude extract retained for further purification.  
       [0090] Polynucleotides of the invention can also be used to induce immune responses. For example, as described in Fan et al., Nat. Biotech 17, 870-872 (1999), incorporated herein by reference, nucleic acid sequences encoding a polypeptide may be used to generate antibodies against the encoded polypeptide following topical administration of naked plasmid DNA or following injection, and preferably intra-muscular injection of the DNA. The nucleic acid sequences are preferably inserted in a recombinant expression vector and may be in the form of naked DNA.  
       Antisense  
       [0091] Another aspect of the invention pertains to isolated antisense nucleic acid molecules that are hybridizable to or complementary to the nucleic acid molecule comprising the nucleotide sequence of SEQ ID NO: 1-337, or 675-836, or fragments, analogs or derivatives thereof. An “antisense” nucleic acid comprises a nucleotide sequence that is complementary to a “sense” nucleic acid encoding a protein, e.g., complementary to the coding strand of a double-stranded cDNA molecule or complementary to an mRNA sequence. In specific aspects, antisense nucleic acid molecules are provided that comprise a sequence complementary to at least about 10, 25, 50, 100, 250 or 500 nucleotides or an entire coding strand, or to only a portion thereof. Nucleic acid molecules encoding fragments, homologs, derivatives and analogs of a protein of any of SEQ ID NO: 1-337, or 675-836 or antisense nucleic acids complementary to a nucleic acid sequence of SEQ ID NO: 1-337, or 675-836 are additionally provided.  
       [0092] In one embodiment, an antisense nucleic acid molecule is antisense to a “coding region” of the coding strand of a nucleotide sequence of the invention. The term “coding region” refers to the region of the nucleotide sequence comprising codons which are translated into amino acid residues. In another embodiment, the antisense nucleic acid molecule is antisense to a “noncoding region” of the coding strand of a nucleotide sequence of the invention. The term “noncoding region” refers to 5′ and 3′ sequences that flank the coding region that are not translated into amino acids (i.e., also referred to as 5′ and 3′ untranslated regions).  
       [0093] Given the coding strand sequences encoding a nucleic acid disclosed herein (e.g., SEQ ID NO: 1-337, or 675-836, antisense nucleic acids of the invention can be designed according to the rules of Watson and Crick or Hoogsteen base pairing. The antisense nucleic acid molecule can be complementary to the entire coding region of an mRNA, but more preferably is an oligonucleotide that is antisense to only a portion of the coding or noncoding region of an mRNA. For example, the antisense oligonucleotide can be complementary to the region surrounding the translation start site of an mRNA. An antisense oligonucleotide can be, for example, about 5, 10, 15, 20, 25, 30, 35, 40, 45 or 50 nucleotides in length. An antisense nucleic acid of the invention can be constructed using chemical synthesis or enzymatic ligation reactions using procedures known in the art. For example, an antisense nucleic acid (e.g., an antisense oligonucleotide) can be chemically synthesized using naturally occurring nucleotides or variously modified nucleotides designed to increase the biological stability of the molecules or to increase the physical stability of the duplex formed between the antisense and sense nucleic acids, e.g., phosphorothioate derivatives and acridine substituted nucleotides can be used.  
       [0094] Examples of modified nucleotides that can be used to generate the antisense nucleic acid include: 5-fluorouracil, 5-bromouracil, 5-chlorouracil, 5-iodouracil, hypoxanthine, xanthine, 4-acetylcytosine, 5-(carboxyhydroxylmethyl) uracil, 5-carboxymethylaminomethyl-2-thiouridine, 5-carboxymethylaminomethyluracil, dihydrouracil, beta-D-galactosylqueosine, inosine, N6-isopentenyladenine, 1-methylguanine, 1-methylinosine, 2,2-dimethylguanine, 2-methyladenine, 2-methylguanine, 3-methylcytosine, 5-methylcytosine, N6-adenine, 7-methylguanine, 5-methylaminomethyluracil, 5-methoxyaminomethyl-2-thiouracil, beta-D-mannosylqueosine, 5′-methoxycarboxymethyluracil, 5-methoxyuracil, 2-methylthio-N6-isopentenyladenine, uracil-5-oxyacetic acid (v), wybutoxosine, pseudouracil, queosine, 2-thiocytosine, 5-methyl-2-thiouracil, 2-thiouracil, 4-thiouracil, 5-methyluracil, uracil-5-oxyacetic acid methylester, uracil-5-oxyacetic acid (v), 5-methyl-2-thiouracil, 3-(3-amino-3-N-2-carboxypropyl) uracil, (acp3)w, and 2,6-diaminopurine. Alternatively, the antisense nucleic acid can be produced biologically using an expression vector into which a nucleic acid has been subcloned in an antisense orientation (i.e., RNA transcribed from the inserted nucleic acid will be of an antisense orientation to a target nucleic acid of interest, described further in the following subsection).  
       [0095] The antisense nucleic acid molecules of the invention are typically administered to a subject or generated in situ such that they hybridize with or bind to cellular mRNA and/or genomic DNA encoding a protein according to the invention to thereby inhibit expression of the protein, e.g., by inhibiting transcription and/or translation. The hybridization can be by conventional nucleotide complementarity to form a stable duplex, or, for example, in the case of an antisense nucleic acid molecule that binds to DNA duplexes, through specific interactions in the major groove of the double helix. An example of a route of administration of antisense nucleic acid molecules of the invention includes direct injection at a tissue site. Alternatively, antisense nucleic acid molecules can be modified to target selected cells and then administered systemically. For example, for systernic administration, antisense molecules can be modified such that they specifically bind to receptors or antigens expressed on a selected cell surface, e.g., by linking the antisense nucleic acid molecules to peptides or antibodies that bind to cell surface receptors or antigens. The antisense nucleic acid molecules can also be delivered to cells using the vectors described herein. To achieve sufficient intracellular concentrations of antisense molecules, vector constructs in which the antisense nucleic acid molecule is placed under the control of a strong pol II or pol III promoter are preferred.  
       [0096] In yet another embodiment, the antisense nucleic acid molecule of the invention is an α-anomeric nucleic acid molecule. An α-anomeric nucleic acid molecule forms specific double-stranded hybrids with complementary RNA in which, contrary to the usual α-units, the strands run parallel to each other (Gaultier et al. (1987)  Nucleic Acids Res  15: 6625-6641). The antisense nucleic acid molecule can also comprise a 2′-o-methylribonucleotide (Inoue et al. (1987)  Nucleic Acids Res  15: 6131-6148) or a chimeric RNA-DNA analogue (Inoue et al. (1987)  FEBS Lett  215: 327-330).  
       Ribozymes and PNA Moieties  
       [0097] In still another embodiment, an antisense nucleic acid of the invention is a ribozyme. Ribozymes are catalytic RNA molecules with ribonuclease activity that are capable of cleaving a single-stranded nucleic acid, such as an mRNA, to which they have a complementary region. Thus, ribozymes (e.g., hammerhead ribozymes (described in Haselhoff and Gerlach (1988)  Nature  334:585-591)) can be used to catalytically cleave mRNA transcripts to thereby inhibit translation of an mRNA. A ribozyme having specificity for a nucleic acid of the invention can be designed based upon the nucleotide sequence of a DNA disclosed herein (i.e., SEQ ID NO: 1-337, or 675-836). For example, a derivative of Tetrahymena L-19 IVS RNA can be constructed in which the nucleotide sequence of the active site is complementary to the nucleotide sequence to be cleaved in a mRNA. See, e.g., Cech et al. U.S. Pat. No. 4,987,071; and Cech et al. U.S. Pat. No. 5,116,742. Alternatively, mRNA of the invention can be used to select a catalytic RNA having a specific ribonuclease activity from a pool of RNA molecules. See, e.g., Bartel et al., (1993)  Science  261:1411-1418.  
       [0098] Alternatively, gene expression can be inhibited by targeting nucleotide sequences complementary to the regulatory region (e.g., promoter and/or enhancers) to form triple helical structures that prevent transcription of the gene in target cells. See generally, Helene. (1991)  Anticancer Drug Des . 6: 569-84; Helene. et al. (1992)  Ann. N.Y. Acad. Sci . 660:27-36; and Maher (1992)  Bioassays  14: 807-15.  
       [0099] In various embodiments, the nucleic acids of the invention can be modified at the base moiety, sugar moiety or phosphate backbone to improve, e.g., the stability, hybridization, or solubility of the molecule. For example, the deoxyribose phosphate backbone of the nucleic acids can be modified to generate peptide nucleic acids (see Hyrup et al. (1996)  Bioorg Med Chem  4: 5-23). As used herein, the terms “peptide nucleic acids” or “PNAs” refer to nucleic acid mimics, e.g., DNA mimics, in which the deoxyribose phosphate backbone is replaced by a pseudopeptide backbone and only the four natural nucleobases are retained. The neutral backbone of PNAs has been shown to allow for specific hybridization to DNA and RNA under conditions of low ionic strength. The synthesis of PNA oligomers can be performed using standard solid phase peptide synthesis protocols as described in Hyrup et al. (1996) above; Perry-O&#39;Keefe et al. (1996)  PNAS  93: 14670-675.  
       [0100] PNAs of the invention can be used in therapeutic and diagnostic applications. For example, PNAs can be used as antisense or antigene agents for sequence-specific modulation of gene expression by, e.g., inducing transcription or translation arrest or inhibiting replication. PNAs of the invention can also be used, e.g., in the analysis of single base pair mutations in a gene by, e.g., PNA directed PCR clamping; as artificial restriction enzymes when used in combination with other enzymes, e.g., S1 nucleases (Hyrup B. (1996) above); or as probes or primers for DNA sequence and hybridization (Hyrup et al. (1996), above; Perry-O&#39;Keefe (1996), above).  
       [0101] In another embodiment, PNAs of the invention can be modified, e.g., to enhance their stability or cellular uptake, by attaching lipophilic or other helper groups to PNA, by the formation of PNA-DNA chimeras, or by the use of liposomes or other techniques of drug delivery known in the art. For example, PNA-DNA chimeras can be generated that may combine the advantageous properties of PNA and DNA. Such chimeras allow DNA recognition enzymes, e.g., RNase H and DNA polymerases, to interact with the DNA portion while the PNA portion would provide high binding affinity and specificity. PNA-DNA chimeras can be linked using linkers of appropriate lengths selected in terms of base stacking, number of bonds between the nucleobases, and orientation (Hyrup (1996) above). The synthesis of PNA-DNA chimeras can be performed as described in Hyrup (1996) above and Finn et al. (1996)  Nucl Acids Res  24: 3357-63. For example, a DNA chain can be synthesized on a solid support using standard phosphoramidite coupling chemistry, and modified nucleoside analogs, e.g., 5′-(4-methoxytrityl)amino-5′-deoxy-thymidine phosphoramidite, can be used between the PNA and the 5′ end of DNA (Mag et al. (1989)  Nucl Acid Res  17: 5973-88). PNA monomers are then coupled in a stepwise manner to produce a chimeric molecule with a 5′ PNA segment and a 3′ DNA segment (Finn et al. (1996) above). Alternatively, chimeric molecules can be synthesized with a 5′ DNA segment and a 3′ PNA segment. See, Petersen et al. (1975)  Bioorg Med Chem Lett  5: 1119-11124.  
       [0102] In other embodiments, the oligonucleotide may include other appended groups such as peptides (e.g., for targeting host cell receptors in vivo), or agents facilitating transport across the cell membrane (see, e.g., Letsinger et al., 1989 , Proc. Natl. Acad. Sci. U.S.A . 86:6553-6556; Lemaitre et al., 1987 , Proc. Natl. Acad. Sci . 84:648-652; PCT Publication No. W088/09810) or the blood-brain barrier (see, e.g., PCT Publication No. W089/10134). In addition, oligonucleotides can be modified with hybridization triggered cleavage agents (See, e.g., Krol et al., 1988 , BioTechniques  6:958-976) or intercalating agents. (See, e.g., Zon, 1988 , Pharm. Res . 5: 539-549). To this end, the oligonucleotide may be conjugated to another molecule, e.g., a peptide, a hybridization triggered cross-linking agent, a transport agent, a hybiidization-triggered cleavage agent, etc.  
       Hosts  
       [0103] The present invention further provides host cells genetically engineered to contain the polynucleotides of the invention. For example, such host cells may contain nucleic acids of the invention introduced into the host cell using known transformation, transfection or infection methods. The present invention still further provides host cells genetically engineered to express the polynucleotides of the invention, wherein such polynucleotides are in operative association with a regulatory sequence heterologous to the host cell which drives expression of the polynucleotides in the cell.  
       [0104] Knowledge of nucleic acid sequences allows for modification of cells to permit, or increase, expression of endogenous polypeptide. Cells can be modified (e.g., by homologous recombination) to provide increased polypeptide expression by replacing, in whole or in part, the naturally occurring promoter with all or part of a heterologous promoter so that the cells express the polypeptide at higher levels. The heterologous promoter is inserted in such a manner that it is operatively linked to the encoding sequences. See, for example, PCT International Publication No. WO94/12650, PCT International Publication No. WO92/20808, and PCT International Publication No. WO91/09955. It is also contemplated that, in addition to heterologous promoter DNA, amplifiable marker DNA (e.g., ada, dhfr, and the multifunctional CAD gene which encodes carbamyl phosphate synthase, aspartate transcarbamylase, and dihydroorotase) and/or intron DNA may be inserted along with the heterologous promoter DNA. If linked to the coding sequence, amplification of the marker DNA by standard selection methods results in co-amplification of the desired protein coding sequences in the cells.  
       [0105] The host cell can be a higher eukaryotic host cell, such as a mammalian cell, a lower eukaryotic host cell, such as a yeast cell, or the host cell can be a prokaryotic cell, such as a bacterial cell. Introduction of the recombinant construct into the host cell can be effected by calcium phosphate transfection, DEAE, dextran mediated transfection, or electroporation (Davis, L. et al.,  Basic Methods in Molecular Biology  (1986)). The host cells containing one of the polynucleotides of the invention, can be used in conventional manners to produce the gene product encoded by the isolated fragment (in the case of an ORF) or can be used to produce a heterologous protein under the control of the EMF.  
       [0106] Any host/vector system can be used to express one or more of the ORFs of the present invention. These include, but are not limited to, eukaryotic hosts such as HeLa cells, Cv-1 cell, COS cells, 293 cells, and Sf9 cells, as well as prokaryotic host such as  E. coli  and  B. subtilis . The most preferred cells are those which do not normally express the particular polypeptide or protein or which expresses the polypeptide or protein at low natural level. Mature proteins can be expressed in mammalian cells, yeast, bacteria, or other cells under the control of appropriate promoters. Cell-free translation systems can also be employed to produce such proteins using RNAs derived from the DNA constructs of the present invention. Appropriate cloning and expression vectors for use with prokaryotic and eukaryotic hosts are described by Sambrook, et al., in Molecular Cloning: A Laboratory Manual, Second Edition, Cold Spring Harbor, N.Y. (1989), the disclosure of which is hereby incorporated by reference.  
       [0107] Various mammalian cell culture systems can also be employed to express recombinant protein. Examples of mammalian expression systems include the COS-7 lines of monkey kidney fibroblasts, described by Gluzman, Cell 23:175 (1981). Other cell lines capable of expressing a compatible vector are, for example, the C127, monkey COS cells, Chinese Hamster Ovary (CHO) cells, human kidney 293 cells, human epidermal A431 cells, human Colo205 cells, 3T3 cells, CV-1 cells, other transformed primate cell lines, normal diploid cells, cell strains derived from in vitro culture of primary tissue, primary explants, HeLa cells, mouse L cells, BHK, EL-60, U937, HaK or Jurkat cells. Mammalian expression vectors will comprise an origin of replication, a suitable promoter and also any necessary ribosome binding sites, polyadenylation site, splice donor and acceptor sites, transcriptional termination sequences, and 5 flanking nontranscribed sequences. DNA sequences derived from the SV40 viral genome, for example, SV40 origin, early promoter, enhancer, splice, and polyadenylation sites may be used to provide the required nontranscribed genetic elements. Recombinant polypeptides and proteins produced in bacterial culture are usually isolated by initial extraction from cell pellets, followed by one or more salting-out, aqueous ion exchange or size exclusion chromatography steps. Protein refolding steps can be used, as necessary, in completing configuration of the mature protein. Finally, high performance liquid chromatography (HPLC) can be employed for final purification steps. Microbial cells employed in expression of proteins can be disrupted by any convenient method, including freeze-thaw cycling, sonication, mechanical disruption, or use of cell lysing agents.  
       [0108] Alternatively, it may be possible to produce the protein in lower eukaryotes such as yeast or insects or in prokaryotes such as bacteria. Potentially suitable yeast strains include  Saccharornyces cerevisiae, Schizosaccharomyces pombe , Kluyveronyces strains, Candida, or any yeast strain capable of expressing heterologous proteins. Potentially suitable bacterial strains include  Escherichia coli, Bacillus subtilis, Salmonella typhimurium , or any bacterial strain capable of expressing heterologous proteins. if the protein is made in yeast or bacteria, it may be necessary to modify the protein produced therein, for example by phosphorylation or glycosylation of the appropriate sites, in order to obtain the functional protein. Such covalent attachments may be accomplished using known chemical or enzymatic methods.  
       [0109] In another embodiment of the present invention, cells and tissues may be engineered to express an endo genous gene comprising the polynucleotides of the invention under the control of inducible regulatory elements, in which case the regulatory sequences of the endogenous gene may be replaced by homologous recombination. As described herein, gene targeting can be used to replace a gene&#39;s existing regulatory region with a regulatory sequence isolated from a different gene or a novel regulatory sequence synthesized by genetic engineering methods. Such regulatory sequences may be comprised of promoters, enhancers, scaffold-attachment regions, negative regulatory elements, transcriptional initiation sites, and regulatory protein binding sites or combinations of said sequences. Alternatively, sequences which affect the structure or stability of the RNA or protein produced may be replaced, removed, added, or otherwise modified by targeting. These sequence include polyadenylation signals, mRNA stability elements, splice sites, leader sequences for enhancing or modifying transport or secretion properties of the protein, or other sequences which alter or improve the function or stability of protein or RNA molecules.  
       [0110] The targeting event may be a simple insertion of the regulatory sequence, placing the gene under the control of the new regulatory sequence, e.g., inserting a new promoter or enhancer or both upstream of a gene. Alternatively, the targeting event may be a simple deletion of a regulatory element, such as the deletion of a tissue-specific negative regulatory element. Alternatively, the targeting event may replace an existing element; for example, a tissue-specific enhancer can be replaced by an enhancer that has broader or different cell-type specificity than the naturally occurring elements. Here, the naturally occurring sequences are deleted and new sequences are added. In all cases, the identification of the targeting event may be facilitated by the use of one or more selectable marker genes that are contiguous with the targeting DNA, allowing for the selection of cells in which the exogenous DNA has integrated into the host cell genome. The identification of the targeting event may also be facilitated by the use of one or more marker genes exhibiting the property of negative selection, such that the negatively selectable marker is linked to the exogenous DNA, but configured such that the negatively selectable marker flanks the targeting sequence, and such that a correct homologous recombination event with sequences in the host cell genome does not result in the stable integration of the negatively selectable marker. Markers useful for this purpose include the Herpes Simplex Virus thymidine kinase (TK) gene or the bacterial xanthine-guanine phosphoribosyl-transferase (gpt) gene.  
       [0111] The gene targeting or gene activation techniques which can be used in accordance with this aspect of the invention are more particularly described in U.S. Pat. No. 5,272,071 to Chappel; U.S. Pat. No. 5,578,461 to Sherwin et al.; International Application No. PCT/US92/09627 (WO93/09222) by Selden et al.; and International Application No. PCT/US90/06436 (WO91/06667) by Skoultchi et al., each of which is incorporated by reference herein in its entirety.  
       Polypeptides of the Invention  
       [0112] The isolated polypeptides of the invention include, but are not limited to, a polypeptide comprising: the amino acid sequences set forth as any one of SEQ ID NO: 338-674, or 837-998 or an amino acid sequence encoded by any one of the nucleotide sequences SEQ ID NO: 1-337, or 675-836 or the corresponding full length or mature protein. Polypeptides of the invention also include polypeptides preferably with biological or immunological activity that are encoded by: (a) a polynucleotide having any one of the nucleotide sequences set forth in SEQ ID NO: 1-337, or 675-836 or (b) polynucleotides encoding any one of the amino acid sequences set forth as SEQ ID NO: 338-674, or 837-998 or (c) polynucleotides that hybridize to the complement of the polynucleotides of either (a) or (b) under stringent hybridization conditions. The invention also provides biologically active or immunologically active variants of any of the amino acid sequences set forth as SEQ ID NO: 338-674, or 837-998 or the corresponding full length or mature protein; and “substantial equivalents” thereof (e.g., with at least about 65%, at least about 70%, at least about 75%, at least about 80%, at least about 85%, 86%, 87%, 88%, 89%, at least about 90%, 91%, 92%, 93%, 94%, typically at least about 95%, 96%, 97%, more typically at least about 98%, or most typically at least about 99% amino acid identity) that retain biological activity. Polypeptides encoded by allelic variants may have a similar, increased, or decreased activity compared to polypeptides comprising SEQ ID NO: 338-674, or 837-998.  
       [0113] Fragments of the proteins of the present invention which are capable of exhibiting biological activity are also encompassed by the present invention. Fragments of the protein may be in linear form or they may be cyclized using known methods, for example, as described in H. U. Saragovi, et al., Bio/Technology 10, 773-778 (1992) and in R. S. McDowell, et al., J. Amer. Chem. Soc. 114, 9245-9253 (1992), both of which are incorporated herein by reference. Such fragments may be fused to carrier molecules such as immunoglobulins for many purposes, including increasing the valency of protein binding sites. Fragments are also identified in Tables 3, 5, 6, 8, or 9.  
       [0114] The present invention also provides both full-length and mature forms (for example, without a signal sequence or precursor sequence) of the disclosed proteins. The protein coding sequence is identified in the sequence listing by translation of the disclosed nucleotide sequences. The predicted signal sequence is set forth in Table 6. The mature form of such protein may be obtained and confirmed by expression of a full-length polynucleotide in a suitable mammalian cell or other host cell and sequencing of the cleaved product. One of skill in the art will recognize that the actual cleavage site may be different than that predicted in Table 6. The sequence of the mature form of the protein is also determinable from the amino acid sequence of the full-length form. Where proteins of the present invention are membrane bound, soluble forms of the proteins are also provided. In such forms, part or all of the regions causing the proteins to be membrane bound are deleted so that the proteins are fully secreted from the cell in which they are expressed (See, e.g., Sakal et al., Prep. Biochem. Biotechnol. (2000), 30(2), pp. 107-23, incorporated herein by reference).  
       [0115] Protein compositions of the present invention may further comprise an acceptable carrier, such as a hydrophilic, e.g., pharmaceutically acceptable, carrier.  
       [0116] The present invention further provides isolated polypeptides encoded by the nucleic acid fragments of the present invention or by degenerate variants of the nucleic acid fragments of the present invention. By “degenerate variant” is intended nucleotide fragments which differ from a nucleic acid fragment of the present invention (e.g., an ORF) by nucleotide sequence but, due to the degeneracy of the genetic code, encode an identical polypeptide sequence. Preferred nucleic acid fragments of the present invention are the ORFs that encode proteins.  
       [0117] A variety of methodologies known in the art can be utilized to obtain any one of the isolated polypeptides or proteins of the present invention. At the simplest level, the amino acid sequence can be synthesized using commercially available peptide synthesizers. The synthetically-constructed protein sequences, by virtue of sharing primary, secondary or tertiary structural and/or conformational characteristics with proteins may possess biological properties in common therewith, including protein activity. This technique is particularly useful in producing small peptides and fragments of larger polypeptides. Fragments are useful, for example, in generating antibodies against the native polypeptide. Thus, they may be employed as biologically active or immunological substitutes for natural, purified proteins in screening of therapeutic compounds and in immunological processes for the development of antibodies.  
       [0118] The polypeptides and proteins of the present invention can alternatively be purified from cells which have been altered to express the desired polypeptide or protein. As used herein, a cell is said to be altered to express a desired polypeptide or protein when the cell, through genetic manipulation, is made to produce a polypeptide or protein which it normally does not produce or which the cell normally produces at a lower level. One skilled in the art can readily adapt procedures for introducing and expressing either recombinant or synthetic sequences into eukaryotic or prokaryotic cells in order to generate a cell which produces one of the polypeptides or proteins of the present invention.  
       [0119] The invention also relates to methods for producing a polypeptide comprising growing a culture of host cells of the invention in a suitable culture medium, and purifying the protein from the cells or the culture in which the cells are grown. For example, the methods of the invention include a process for producing a polypeptide in which a host cell containing a suitable expression vector that includes a polynucleotide of the invention is cultured under conditions that allow expression of the encoded polypeptide. The polypeptide can be recovered from the culture, conveniently from the culture medium, or from a lysate prepared from the host cells and further purified. Preferred embodiments include those in which the protein produced by such process is a full length or mature form of the protein.  
       [0120] In an alternative method, the polypeptide or protein is purified from bacterial cells which naturally produce the polypeptide or protein. One skilled in the art can readily follow known methods for isolating polypeptides and proteins in order to obtain one of the isolated polypeptides or proteins of the present invention. These include, but are not limited to, immunochromatography, HPLC, size-exclusion chromatography, ion-exchange chromatography, and immuno-affinity chromatography. See, e.g., Scopes,  Protein Purification: Principles and Practice , Springer-Verlag (1994); Sambrook, et al., in Molecular Cloning:  A Laboratory Manual ; Ausubel et al.,  Current Protocols in Molecular Biology . Polypeptide fragments that retain biological/immunological activity include fragments comprising greater than about 100 amino acids, or greater than about 200 amino acids, and fragments that encode specific protein domains.  
       [0121] The purified polypeptides can be used in in vitro binding assays which are well known in the art to identify molecules which bind to the polypeptides. These molecules include but are not limited to, for e.g., small molecules, molecules from combinatorial libraries, antibodies or other proteins. The molecules identified in the binding assay are then tested for antagonist or agonist activity in in vivo tissue culture or animal models that are well known in the art. In brief, the molecules are titrated into a plurality of cell cultures or animals and then tested for either cell/animal death or prolonged survival of the animal/cells.  
       [0122] In addition, the peptides of the invention or molecules capable of binding to the peptides may be complexed with toxins, e.g., ricin or cholera, or with other compounds that are toxic to cells. The toxin-binding, molecule complex is then targeted to a tumor or other cell by the specificity of the binding molecule for SEQ ID NO: 338-674, or 837-998.  
       [0123] The protein of the invention may also be expressed as a product of transgenic animals, e.g., as a component of the milk of transgenic cows, goats, pigs, or sheep which are characterized by somatic or germ cells containing a nucleotide sequence encoding the protein.  
       [0124] The proteins provided herein also include proteins characterized by amino acid sequences similar to those of purified proteins but into which modification are naturally provided or deliberately engineered. For example, modifications, in the peptide or DNA sequence, can be made by those skilled in the art using known techniques. Modifications of interest in the protein sequences may include the alteration, substitution, replacement, insertion or deletion of a selected amino acid residue in the coding sequence. For example, one or more of the cysteine residues may be deleted or replaced with another amino acid to alter the conformation of the molecule. Techniques for such alteration, substitution, replacement, insertion or deletion are well known to those skilled in the art (see, e.g., U.S. Pat. No. 4,518,584). Preferably, such alteration, substitution, replacement, insertion or deletion retains the desired activity of the protein. Regions of the protein that are important for the protein function can be determined by various methods known in the art including the alanine-scanning method which involved systematic substitution of single or strings of amino acids with alanine, followed by testing the resulting alanine-containing variant for biological activity. This type of analysis determines the importance of the substituted amino acid(s) in biological activity. Regions of the protein that are important for protein function may be determined by the eMATRIX program.  
       [0125] Other fragments and derivatives of the sequences of proteins which would be expected to retain protein activity in whole or in part and are useful for screening or other immunological methodologies may also be easily made by those skilled in the art given the disclosures herein. Such modifications are encompassed by the present invention.  
       [0126] The protein may also be produced by operably linking the isolated polynucleotide of the invention to suitable control sequences in one or more insect expression vectors, and employing an insect expression system. Materials and methods for baculovirus/insect cell expression systems are commercially available in kit form from, e.g., Invitrogen, San Diego, Calif., U.S.A. (the MaxBat™ kit), and such methods are well known in the art, as described in Summers and Smith, Texas Agricultural Experiment Station Bulletin No. 1555 (1987), incorporated herein by reference. As used herein, an insect cell capable of expressing a polynucleotide of the present invention is “transformed.” 
       [0127] The protein of the invention may be prepared by culturing transformed host cells under culture conditions suitable to express the recombinant protein. The resulting expressed protein may then be purified from such culture (i.e., from culture medium or cell extracts) using known purification processes, such as gel filtration and ion exchange chromatography. The purification of the protein may also include an affinity column containing agents which will bind to the protein; one or more column steps over such affinity resins as concanavalin A-agarose, heparin-toyopearl™ or Cibacrom blue 3GA Sepharose™; one or more steps involving hydrophobic interaction chromatography using such resins as phenyl ether, butyl ether, or propyl ether; or immunoaffinity chromatography.  
       [0128] Alternatively, the protein of the invention may also be expressed in a form which will facilitate purification. For example, it may be expressed as a fusion protein, such as those of maltose binding protein (MBP), glutathione-S-transferase (GST) or thioredoxin (TRX), or as a His tag. Kits for expression and purification of such fusion proteins are commercially available from New England BioLab (Beverly, Mass.), Pharmacia (Piscataway, N.J.) and Invitrogen, respectively. The protein can also be tagged with an epitope and subsequently purified by using a specific antibody directed to such epitope. One such epitope (“FLAG®”) is commercially available from Kodak (New Haven, Conn.).  
       [0129] Finally, one or more reverse-phase high performance liquid chromatography (RP-HPLC) steps employing hydrophobic RP-HPLC media, e.g., silica gel having pendant methyl or other aliphatic groups, can be employed to further purify the protein. Some or all of the foregoing purification steps, in various combinations, can also be employed to provide a substantially homogeneous isolated recombinant protein. The protein thus purified is substantially free of other mammalian proteins and is defined in accordance with the present invention as an “isolated protein.” 
       [0130] The polypeptides of the invention include analogs (variants). This embraces fragments, as well as peptides in which one or more amino acids has been deleted, inserted, or substituted. Also, analogs of the polypeptides of the invention embrace fusions of the polypeptides or modifications of the polypeptides of the invention, wherein the polypeptide or analog is fused to another moiety or moieties, e.g., targeting moiety or another therapeutic agent. Such analogs may exhibit improved properties such as activity and/or stability. Examples of moieties which may be fused to the polypeptide or an analog include, for example, targeting moieties which provide for the delivery of polypeptide to pancreatic cells, e.g., antibodies to pancreatic cells, antibodies to immune cells such as T-cells, monocytes, dendritic cells, granulocytes, etc., as well as receptor and ligands expressed on pancreatic or immune cells. Other moieties which may be fused to the polypeptide include therapeutic agents which are used for treatment, for example, immunosuppressive drugs such as cyclosporin, SK506, azathioprine, CD3 antibodies and steroids. Also, polypeptides may be fused to immune modulators, and other cytokines such as alpha or beta interferon.  
       Determining Polypeptide and Polynucleotide Identity and Similarity  
       [0131] Preferred identity and/or similarity are designed to give the largest match between the sequences tested. Methods to determine identity and similarity are codified in computer programs including, but are not limited to, the GCG program package, including GAP (Devereux, J., et al., Nucleic Acids Research 12(1):387 (1984); Genetics Computer Group, University of Wisconsin, Madison, Wis.), BLASTP, BLASTN, BLASTX, FASTA (Altschul, S. F. et al., J. Molec. Biol. 215:403-410 (1990), PSI-BLAST (Altschul S. F. et al., Nucleic Acids Res. vol. 25, pp. 3389-3402, herein incorporated by reference), eMatrix software (Wu et al., J. Comp. Biol., Vol. 6, pp. 219-235 (1999), herein incorporated by reference), eMotif software (Nevill-Manning et al, ISMB-97, Vol. 4, pp. 202-209, herein incorporated by reference), Pfam software (Sonnhammer et al., Nucleic Acids Res., Vol. 26(1), pp. 320-322 (1998), herein incorporated by reference) and the Kyte-Doolittle hydrophobocity prediction algorithm (J. Mol Biol, 157, pp. 105-31 (1982), the GeneAtlas software (Molecular Simulations Inc. (MSI), San Diego, Calif.) (Sanchez and Sali (1998) Proc. Natl. Acad. Sci., 95, 13597-13602; Kitson DH et al, (2000) “Remote homology detection using structural modeling—an evaluation” Submitted; Fischer and Eisenberg (1996) Protein Sci. 5, 947-955), Neural Network SignalP V1.1 program (from Center for Biological Sequence Analysis, The Technical University of Denmark) incorporated herein by reference). Polypeptide sequences were examined by a proprietary algorithm, SeqLoc that separates the proteins into three sets of locales: intracellular, membrane, or secreted. This prediction is based upon three characteristics of each polypeptide, including percentage of cysteine residues, Kyte-Doolittle scores for the first 20 amino acids of each protein, and Kyte-Doolittle scores to calculate the longest hydrophobic stretch of the said protein. Values of predicted proteins are compared against the values from a set of 592 proteins of known cellular localization from the Swissprot database (http://www.expasv.ch/sprot). Predictions are based upon the maximum likelihood estimation.  
       [0132] Pesence of transmembrane region(s) was detected using the TMpred program (http://www.ch.embnet.org/software/TMPRED form.html).  
       [0133] The BLAST programs are publicly available from the National Center for Biotechnology Information (NCBI) and other sources (BLAST Manual, Altschul, S., et al. NCBI NLM NIH Bethesda, Md. 20894; Altschul, S., et al., J. Mol. Biol. 215:403-410 (1990).  
       Chimeric and Fusion Proteins  
       [0134] The invention also provides chimeric or fusion proteins. As used herein, a “chimeric protein” or “fusion protein” comprises a polypeptide of the invention operatively linked to another polypeptide. Within a fusion protein the polypeptide according to the invention can correspond to all or a portion of a protein according to the invention. In one embodiment, a fusion protein comprises at least one biologically active portion of a protein according to the invention. In another embodiment, a fusion protein comprises at least two biologically active portions of a protein according to the invention. Within the fusion protein, the term “operatively linked” is intended to indicate that the polypeptide according to the invention and the other polypeptide are fused in-frame to each other. The polypeptide can be fused to the N-terminus or C-terminus, or to the middle.  
       [0135] For example, in one embodiment a fusion protein comprises a polypeptide according to the invention operably linked to the extracellular domain of a second protein.  
       [0136] In another embodiment, the fusion protein is a GST-fusion protein in which the polypeptide sequences of the invention are fused to the C-terminus of the GST (i.e., glutathione S-transferase) sequences.  
       [0137] In another embodiment, the fusion protein is an immunoglobulin fusion protein in which the polypeptide sequences according to the invention comprise one or more domains fused to sequences derived from a member of the immunoglobulin protein family. The immunoglobulin fusion proteins of the invention can be incorporated into pharmaceutical compositions and administered to a subject to inhibit an interaction between a ligand and a protein of the invention on the surface of a cell, to thereby suppress signal transduction in vivo. The immunoglobulin fusion proteins can be used to affect the bioavailability of a cognate ligand. Inhibition of the ligand/protein interaction may be useful therapeutically for both the treatment of proliferative and differentiative disorders, e.g., cancer as well as modulating (e.g., promoting or inhibiting) cell survival. Moreover, the immunoglobulin fusion proteins of the invention can be used as immunogens to produce antibodies in a subject, to purify ligands, and in screening assays to identify molecules that inhibit the interaction of a polypeptide of the invention with a ligand.  
       [0138] A chimeric or fusion protein of the invention can be produced by standard recombinant DNA techniques. For example, DNA fragments coding for the different polypeptide sequences are ligated together in-frame in accordance with conventional techniques, e.g., by employing blunt-ended or stagger-ended termini for ligation, restriction enzyme digestion to provide for appropriate termini, filling-in of cohesive ends as appropriate, alkaline phosphatase treatment to avoid undesirable joining, and enzymatic ligation. In another embodiment, the fusion gene can be synthesized by conventional techniques including automated DNA synthesizers. Alternatively, PCR amplification of gene fragments can be carried out using anchor primers that give rise to complementary overhangs between two consecutive gene fragments that can subsequently be annealed and reamplified to generate a chimeric gene sequence (see, for example, Ausubel et al. (eds.) Current Protocols in Molecular Biology, John Wiley &amp; Sons, 1992). Moreover, many expression vectors are commercially available that already encode a fusion moiety (e.g., a GST polypeptide). A nucleic acid encoding a polypeptide of the invention can be cloned into such an expression vector such that the fusion moiety is linked in-frame to the protein of the invention.  
       Gene Therapy  
       [0139] Mutations in the polynucleotides of the invention gene may result in loss of normal function of the encoded protein. The invention thus provides gene therapy to restore normal activity of the polypeptides of the invention; or to treat disease states involving polypeptides of the invention. Delivery of a functional gene encoding polypeptides of the invention to appropriate cells is effected ex vivo, in situ, or in vivo by use of vectors, and more particularly viral vectors (e.g., adenovirus, adeno-associated virus, or a retrovirus), or ex vivo by use of physical DNA transfer methods (e.g., liposomes or chemical treatments). See, for example, Anderson, Nature, supplement to vol. 392, no. 6679, pp.25-20 (1998). For additional reviews of gene therapy technology see Friedmann, Science, 244: 1275-1281 (1989); Verma, Scientific American: 68-84 (1990); and Miller, Nature, 357: 455-460 (1992). Introduction of any one of the nucleotides of the present invention or a gene encoding the polypeptides of the present invention can also be accomplished with extrachromosomal substrates (transient expression) or artificial chromosomes (stable expression). Cells may also be cultured ex vivo in the presence of proteins of the present invention in order to proliferate or to produce a desired effect on or activity in such cells. Treated cells can then be introduced in vivo for therapeutic purposes. Alternatively, it is contemplated that in other human disease states, preventing the expression of or inhibiting the activity of polypeptides of the invention will be useful in treating the disease states. It is contemplated that antisense therapy or gene therapy could be applied to negatively regulate the expression of polypeptides of the invention.  
       [0140] Other methods inhibiting expression of a protein include the introduction of antisense molecules to the nucleic acids of the present invention, their complements, or their translated RNA sequences, by methods known in the art. Further, the polypeptides of the present invention can be inhibited by using targeted deletion methods, or the insertion of a negative regulatory element such as a silencer, which is tissue specific.  
       [0141] The present invention still further provides cells genetically engineered in vivo to express the polynucleotides of the invention, wherein such polynucleotides are in operative association with a regulatory sequence heterologous to the host cell which drives expression of the polynucleotides in the cell. These methods can be used to increase or decrease the expression of the polynucleotides of the present invention.  
       [0142] Knowledge of DNA sequences provided by the invention allows for modification of cells to permit, increase, or decrease, expression of endogenous polypeptide. Cells can be modified (e.g., by homologous recombination) to provide increased polypeptide expression by replacing, in whole or in part, the naturally occurring promoter with all or part of a heterologous promoter so that the cells express the protein at higher levels. The heterologous promoter is inserted in such a manner that it is operatively linked to the desired protein encoding sequences. See, for example, PCT International Publication No. WO 94/12650, PCT International Publication No. WO 92/20808, and PCT International Publication No. WO 91/09955. It is also contemplated that, in addition to heterologous promoter DNA, amplifiable marker DNA (e.g., ada, dhfr, and the multifunctional CAD gene which encodes carbamyl phosphate synthase, aspartate transcarbamylase, and dihydroorotase) and/or intron DNA may be inserted along with the heterologous promoter DNA. If linked to the desired protein coding sequence, amplification of the marker DNA by standard selection methods results in co-amplification of the desired protein coding sequences in the cells.  
       [0143] In another embodiment of the present invention, cells and tissues may be engineered to express an endogenous gene comprising the polynucleotides of the invention under the control of inducible regulatory elements, in which case the regulatory sequences of the endogenous gene may be replaced by homologous recombination. As described herein, gene targeting can be used to replace a gene&#39;s existing regulatory region with a regulatory sequence isolated from a different gene or a novel regulatory sequence synthesized by genetic engineering methods. Such regulatory sequences may be comprised of promoters, enhancers, scaffold-attachment regions, negative regulatory elements, transcriptional initiation sites, regulatory protein binding sites or combinations of said sequences. Alternatively, sequences which affect the structure or stability of the RNA or protein produced may be replaced, removed, added, or otherwise modified by targeting. These sequences include polyadenylation signals, mRNA stability elements, splice sites, leader sequences for enhancing or modifying transport or secretion properties of the protein, or other sequences which alter or improve the function or stability of protein or RNA molecules.  
       [0144] The targeting event may be a simple insertion of the regulatory sequence, placing the gene under the control of the new regulatory sequence, e.g., inserting a new promoter or enhancer or both upstream of a gene. Alternatively, the targeting event may be a simple deletion of a regulatory element, such as the deletion of a tissue-specific negative regulatory element. Alternatively, the targeting event may replace an existing element; for example, a tissue-specific enhancer can be replaced by an enhancer that has broader or different cell-type specificity than the naturally occurring elements. Here, the naturally occurring sequences are deleted and new sequences are added. In all cases, the identification of the targeting event may be facilitated by the use of one or more selectable marker genes that are contiguous with the targeting DNA, allowing for the selection of cells in which the exogenous DNA has integrated into the cell genome. The identification of the targeting event may also be facilitated by the use of one or more marker genes exhibiting the property of negative selection, such that the negatively selectable marker is linked to the exogenous DNA, but configured such that the negatively selectable marker flanks the targeting sequence, and such that a correct homologous recombination event with sequences in the host cell genome does not result in the stable integration of the negatively selectable marker. Markers useful for this purpose include the Herpes Simplex Virus thymidine kinase (TK) gene or the bacterial xanthine-guanine phosphoribosyl-transferase (gpt) gene.  
       [0145] The gene targeting or gene activation techniques which can be used in accordance with this aspect of the invention are more particularly described in U.S. Pat. No. 5,272,071 to Chappel; U.S. Pat. No. 5,578,461 to Sherwin et al.; International Application No. PCT/US92/09627 (WO93/09222) by Selden et al.; and International Application No. PCT/US90/06436 (WO91/06667) by Skoultchi et al., each of which is incorporated by reference herein in its entirety.  
       Transgenic Animals  
       [0146] In preferred methods to determine biological functions of the polypeptides of the invention in vivo, one or more genes provided by the invention are either over expressed or inactivated in the germ line of animals using homologous recombination [Capecchi, Science 244:1288-1292 (1989)]. Animals in which the gene is over expressed, under the regulatory control of exogenous or endogenous promoter elements, are known as transgenic animals. Animals in which an endogenous gene has been inactivated by homologous recombination are referred to as “knockout” animals. Knockout animals, preferably non-human mammals, can be prepared as described in U.S. Pat. No. 5,557,032, incorporated herein by reference. Transgenic animals are useful to determine the roles polypeptides of the invention play in biological processes, and preferably in disease states. Transgenic animals are useful as model systems to identify compounds that modulate lipid metabolism. Transgenic animals, preferably non-human mammals, are produced using methods as described in U.S. Pat. No 5,489,743 and PCT Publication No. WO94/28122, incorporated herein by reference.  
       [0147] Transgenic animals can be prepared wherein all or part of a promoter of the polynucleotides of the invention is either activated or inactivated to alter the level of expression of the polypeptides of the invention. Inactivation can be carried out using homologous recombination methods described above. Activation can be achieved by supplementing or even replacing the homologous promoter to provide for increased protein expression. The homologous promoter can be supplemented by insertion of one or more heterologous enhancer elements known to confer promoter activation in a particular tissue.  
       [0148] The polynucleotides of the present invention also make possible the development, through, e.g., homologous recombination or knock out strategies, of animals that fail to express polypeptides of the invention or that express a variant polypeptide. Such animals are useful as models for studying the in vivo activities of polypeptide as well as for studying modulators of the polypeptides of the invention.  
       [0149] In preferred methods to determine biological functions of the polypeptides of the invention in vivo, one or more genes provided by the invention are either over expressed or inactivated in the germ line of animals using homologous recombination [Capecchi, Science 244:1288-1292 (1989)]. Animals in which the gene is over expressed, under the regulatory control of exogenous or endogenous promoter elements, are known as transgenic animals. Animals in which an endogenous gene has been inactivated by homologous recombination are referred to as “knockout” animals. Knockout animals, preferably non-human mammals, can be prepared as described in U.S. Pat. No. 5,557,032, incorporated herein by reference. Transgenic animals are useful to determine the roles polypeptides of the invention play in biological processes, and preferably in disease states. Transgenic animals are useful as model systems to identify compounds that modulate lipid metabolism. Transgenic animals, preferably non-human mammals, are produced using methods as described in U.S. Pat. No 5,489,743 and PCT Publication No. WO94/28 122, incorporated herein by reference.  
       [0150] Transgenic animals can be prepared wherein all or part of the polynucleotides of the invention promoter is either activated or inactivated to alter the level of expression of the polypeptides of the invention. Inactivation can be carried out using homologous recombination methods described above. Activation can be achieved by supplementing or even replacing the homologous promoter to provide for increased protein expression. The homologous promoter can be supplemented by insertion of one or more heterologous enhancer elements known to confer promoter activation in a particular tissue.  
       Uses and Biological Activity  
       [0151] The polynucleotides and proteins of the present invention are expected to exhibit one or more of the uses or biological activities (including those associated with assays cited herein) identified herein. Uses or activities described for proteins of the present invention may be provided by administration or use of such proteins or of polynucleotides encoding such proteins (such as, for example, in gene therapies or vectors suitable for introduction of DNA). The mechanism underlying the particular condition or pathology will dictate whether the polypeptides of the invention, the polynucleotides of the invention or modulators (activators or inhibitors) thereof would be beneficial to the subject in need of treatment. Thus, “therapeutic compositions of the invention” include compositions comprising isolated polynucleotides (including recombinant DNA molecules, cloned genes and degenerate variants thereof) or polypeptides of the invention (including full length protein, mature protein and truncations or domains thereof), or compounds and other substances that modulate the overall activity of the target gene products, either at the level of target gene/protein expression or target protein activity. Such modulators include polypeptides, analogs, (variants), including fragments and fusion proteins, antibodies and other binding proteins; chemical compounds that directly or indirectly activate or inhibit the polypeptides of the invention (identified, e.g., via drug screening assays as described herein); antisense polynucleotides and polynucleotides suitable for triple helix formation; and in particular antibodies or other binding partners that specifically recognize one or more epitopes of the polypeptides of the invention.  
       [0152] The polypeptides of the present invention may likewise be involved in cellular activation or in one of the other physiological pathways described herein.  
       Research Uses and Utilities  
       [0153] The polynucleotides provided by the present invention can be used by the research community for various purposes. The polynucleotides can be used to express recombinant protein for analysis, characterization or therapeutic use; as markers for tissues in which the corresponding protein is preferentially expressed (either constitutively or at a particular stage of tissue differentiation or development or in disease states); as molecular weight markers on gels; as chromosome markers or tags (when labeled) to identify chromosomes or to map related gene positions; to compare with endogenous DNA sequences in patients to identify potential genetic disorders; as probes to hybridize and thus discover novel, related DNA sequences; as a source of information to derive PCR primers for genetic fingerprinting; as a probe to “subtract-out” known sequences in the process of discovering other novel polynucleotides; for selecting and making oligomers for attachment to a “gene chip” or other support, including for examination of expression patterns; to raise anti-protein antibodies using DNA immunization techniques; and as an antigen to raise anti-DNA antibodies or elicit another immune response. Where the polynucleotide encodes a protein which binds or potentially binds to another protein (such as, for example, in a receptor-ligand interaction), the polynucleotide can also be used in interaction trap assays (such as, for example, that described in Gyuris et al., Cell 75:791-803 (1993)) to identify polynucleotides encoding the other protein with which binding occurs or to identify inhibitors of the binding interaction.  
       [0154] The polypeptides provided by the present invention can similarly be used in assays to determine biological activity, including in a panel of multiple proteins for high-throughput screening; to raise antibodies or to elicit another immune response; as a reagent (including the labeled reagent) in assays designed to quantitatively determine levels of the protein (or its receptor) in biological fluids; as markers for tissues in which the corresponding polypeptide is preferentially expressed (either constitutively or at a particular stage of tissue differentiation or development or in a disease state); and, of course, to isolate correlative receptors or ligands. Proteins involved in these binding interactions can also be used to screen for peptide or small molecule inhibitors or agonists of the binding interaction.  
       [0155] Any or all of these research utilities are capable of being developed into reagent grade or kit format for commercialization as research products.  
       [0156] Methods for performing the uses listed above are well known to those skilled in the art. References disclosing such methods include without limitation “Molecular Cloning: A Laboratory Manual”, 2d ed., Cold Spring Harbor Laboratory Press, Sambrook, J., E. F. Fritsch and T. Maniatis eds., 1989, and “Methods in Enzymology: Guide to Molecular Cloning Techniques”, Academic Press, Berger, S. L. and A. R. Kimmel eds., 1987.  
       Nutritional Uses  
       [0157] Polynucleotides and polypeptides of the present invention can also be used as nutritional sources or supplements. Such uses include without limitation use as a protein or amino acid supplement, use as a carbon source, use as a nitrogen source and use as a source of carbohydrate. In such cases the polypeptide or polynucleotide of the invention can be added to the feed of a particular organism or can be administered as a separate solid or liquid preparation, such as in the form of powder, pills, solutions, suspensions or capsules. In the case of microorganisms, the polypeptide or polynucleotide of the invention can be added to the medium in or on which the microorganism is cultured.  
       Cytokine and Cell Proliferation/Differentiation Activity  
       [0158] A polypeptide of the present invention may exhibit activity relating to cytokine, cell proliferation (either inducing or inhibiting) or cell differentiation (either inducing or inhibiting) activity or may induce production of other cytokines in certain cell populations. A polynucleotide of the invention can encode a polypeptide exhibiting such attributes. Many protein factors discovered to date, including all known cytokines, have exhibited activity in one or more factor-dependent cell proliferation assays, and hence the assays serve as a convenient confirmation of cytokine activity. The activity of therapeutic compositions of the present invention is evidenced by any one of a number of routine factor dependent cell proliferation assays for cell lines including, without limitation, 32D, DA2, DA1G, T10, B9, B9/11, BaF3, MC9/G, M+(preB M+), 2E8, RB5, DA1, 123, T1165, HT2, CTLL2, TF-1, Mo7e, CMK, HUVEC, and Caco. Therapeutic compositions of the invention can be used in the following:  
       [0159] Assays for T-cell or thymocyte proliferation include without limitation those described in: Current Protocols in Immunology, Ed by J. E. Coligan, A. M. Kruisbeek, D. H. Margulies, E. M. Shevach, W. Strober, Pub. Greene Publishing Associates and Wiley-Interscience (Chapter 3, In Vitro assays for Mouse Lymphocyte Function 3.1-3.19; Chapter 7, Immunologic studies in Humans); Takai et al., J. Immunol. 137:3494-3500, 1986; Bertagnolli et al., J. Immunol. 145:1706-1712, 1990; Bertagnolli et al., Cellular Immunology 133:327-341, 1991; Bertagnolli, et al., I. Immunol. 149:3778-3783, 1992; Bowman et al., I. Immunol. 152:1756-1761, 1994.  
       [0160] Assays for cytokine production and/or proliferation of spleen cells, lymph node cells or thymocytes include, without limitation, those described in: Polyclonal T cell stimulation, Kruisbeek, A. M. and Shevach, E. M. In Current Protocols in Immunology. J. E. e.a. Coligan eds. Vol 1 pp. 3.12.1-3.12.14, John Wiley and Sons, Toronto. 1994; and Measurement of mouse and human interleukin-γ, Schreiber, R. D. In Current Protocols in Immunology. J. E. e.a. Coligan eds. Vol 1 pp. 6.8.1-6.8.8, John Wiley and Sons, Toronto. 1994.  
       [0161] Assays for proliferation and differentiation of hematopoietic and lymphopoietic cells include, without limitation, those described in: Measurement of Human and Murine Interleukin 2 and Interleukin 4, Bottomly, K., Davis, L. S. and Lipsky, P. E. In Current Protocols in Immunology. J. E. e.a. Coligan eds. Vol 1 pp. 6.3.1-6.3.12, John Wiley and Sons, Toronto. 1991; deVries et al., J. Exp. Med. 173:1205-1211, 1991; Moreau et al., Nature 336:690-692, 1988; Greenberger et al., Proc. Natl. Acad. Sci. U.S.A. 80:2931-2938, 1983; Measurement of mouse and human interleukin 6-Nordan, R. In Current Protocols in Immunology. J. E. Coligan eds. Vol 1 pp. 6.6.1-6.6.5, John Wiley and Sons, Toronto. 1991; Smith et al., Proc. Natl. Aced. Sci. U.S.A. 83:1857-1861, 1986; Measurement of human Interleukin 11-Bennett, F., Giannotti, J., Clark, S. C. and Turner, K. J. In Current Protocols in Immunology. J. E. Coligan eds. Vol 1 pp. 6.15.1 John Wiley and Sons, Toronto. 1991; Measurement of mouse and human Interleukin 9-Ciarletta, A., Giannotti, J., Clark, S. C. and Turner, K. J. In Current Protocols in Immunology. J. E. Coligan eds. Vol 1 pp. 6.13.1, John Wiley and Sons, Toronto. 1991.  
       [0162] Assays for T-cell clone responses to antigens (which will identify, among others, proteins that affect APC-T cell interactions as well as direct T-cell effects by measuring proliferation and cytokine production) include, without limitation, those described in: Current Protocols in Immunology, Ed by J. E. Coligan, A. M. Kruisbeek, D. H. Margulies, E. M. Shevach, W Strober, Pub. Greene Publishing Associates and Wiley-Interscience (Chapter 3, In Vitro assays for Mouse Lymphocyte Function; Chapter 6, Cytokines and their cellular receptors; Chapter 7, Immunologic studies in Humans); Weinberger et al., Proc. Natl. Acad. Sci. USA 77:6091-6095, 1980; Weinberger et al., Eur. J. Immun. 11:405-411, 1981; Takai et al., J. Immunol. 137:3494-3500, 1986; Takai et al., J. Immunol. 140:508-512, 1988.  
       Stem Cell Growth Factor Activity  
       [0163] A polypeptide of the present invention may exhibit stem cell growth factor activity and be involved in the proliferation, differentiation and survival of pluripotent and totipotent stem cells including primordial germ cells, embryonic stem cells, hematopoietic stem cells and/or germ line stem cells. Administration of the polypeptide of the invention to stem cells in vivo or ex vivo is expected to maintain and expand cell populations in a totipotential or pluripotential state which would be useful for re-engineering damaged or diseased tissues, transplantation, manufacture of bio-pharmaceuticals and the development of bio-sensors. The ability to produce large quantities of human cells has important working applications for the production of human proteins which currently must be obtained from non-human sources or donors, implantation of cells to treat diseases such as Parkinson&#39;s, Alzheimer&#39;s and other neurodegenerative diseases; tissues for grafting such as bone marrow, skin, cartilage, tendons, bone, muscle (including cardiac muscle), blood vessels, cornea, neural cells, gastrointestinal cells and others; and organs for transplantation such as kidney, liver, pancreas (including islet cells), heart and lung.  
       [0164] It is contemplated that multiple different exogenous growth factors and/or cytokines may be administered in combination with the polypeptide of the invention to achieve the desired effect, including any of the growth factors listed herein, other stem cell maintenance factors, and specifically including stem cell factor (SCF), leukemia inhibitory factor (LIF), Flt-3 ligand (Flt-3L), any of the interleukins, recombinant soluble IL-6 receptor fused to IL-6, macrophage inflammatory protein 1-alpha (MIP-1-alpha), G-CSF, GM-CSF, thrombopoietin (TPO), platelet factor 4 (PF-4), platelet-derived growth factor (PDGF), neural growth factors and basic fibroblast growth factor (bFGF).  
       [0165] Since totipotent stem cells can give rise to virtually any mature cell type, expansion of these cells in culture will facilitate the production of large quantities of mature cells. Techniques for culturing stem cells are known in the art and administration of polypeptides of the invention, optionally with other growth factors and/or cytokines, is expected to enhance the survival and proliferation of the stem cell populations. This can be accomplished by direct administration of the polypeptide of the invention to the culture medium. Alternatively, stroma cells transfected with a polynucleotide that encodes for the polypeptide of the invention can be used as a feeder layer for the stem cell populations in culture or in vivo. Stromal support cells for feeder layers may include embryonic bone marrow fibroblasts, bone marrow stromal cells, fetal liver cells, or cultured embryonic fibroblasts (see U.S. Pat. No. 5,690,926).  
       [0166] Stem cells themselves can be transfected with a polynucleotide of the invention to induce autocrine expression of the polypeptide of the invention. This will allow for generation of undifferentiated totipotential/pluripotential stem cell lines that are useful as is or that can then be differentiated into the desired mature cell types. These stable cell lines can also serve as a source of undifferentiated totipotential/pluripotential mRNA to create cDNA libraries and templates for polymerase chain reaction experiments. These studies would allow for the isolation and identification of differentially expressed genes in stem cell populations that regulate stem cell proliferation and/or maintenance.  
       [0167] Expansion and maintenance of totipotent stem cell populations will be useful in the treatment of many pathological conditions. For example, polypeptides of the present invention may be used to manipulate stem cells in culture to give rise to neuroepithelial cells that can be used to augment or replace cells damaged by illness, autoimmune disease, accidental damage or genetic disorders. The polypeptide of the invention may be useful for inducing the proliferation of neural cells and for the regeneration of nerve and brain tissue, i.e. for the treatment of central and peripheral nervous system diseases and neuropathies, as well as mechanical and traumatic disorders which involve degeneration, death or trauma to neural cells or nerve tissue. In addition, the expanded stem cell populations can also be genetically altered for gene therapy purposes and to decrease host rejection of replacement tissues after grafting or implantation.  
       [0168] Expression of the polypeptide of the invention and its effect on stem cells can also be manipulated to achieve controlled differentiation of the stem cells into more differentiated cell types. A broadly applicable method of obtaining pure populations of a specific differentiated cell type from undifferentiated stem cell populations involves the use of a cell-type specific promoter driving a selectable marker. The selectable marker allows only cells of the desired type to survive. For example, stem cells can be induced to differentiate into cardiomyocytes (Wobus et al., Differentiation, 48: 173-182, (1991); Klug et al., J. Clin. Invest., 98(1): 216-224, (1998)) or skeletal muscle cells (Browder, L. W. In:  Principles of Tissue Engineering eds . Lanza et al., Academic Press (1997)). Alternatively, directed differentiation of stem cells can be accomplished by culturing the stem cells in the presence of a differentiation factor such as retinoic acid and an antagonist of the polypeptide of the invention which would inhibit the effects of endogenous stem cell factor activity and allow differentiation to proceed.  
       [0169] In vitro cultures of stem cells can be used to determine if the polypeptide of the invention exhibits stem cell growth factor activity. Stem cells are isolated from any one of various cell sources (including hematopoietic stem cells and embryonic stem cells) and cultured on a feeder layer, as described by Thompson et al. Proc. Natl. Acad. Sci, U.S.A., 92: 7844-7848 (1995), in the presence of the polypeptide of the invention alone or in combination with other growth factors or cytokines. The ability of the polypeptide of the invention to induce stem cells proliferation is determined by colony formation on semi-solid support e.g. as described by Bernstein et al., Blood, 77: 2316-2321 (1991).  
       Hematopoiesis Regulating Activity  
       [0170] A polypeptide of the present invention may be involved in regulation of hematopoiesis and, consequently, in the treatment of myeloid or lymphoid cell disorders. Even marginal biological activity in support of colony forming cells or of factor-dependent cell lines indicates involvement in regulating hematopoiesis, e.g. in supporting the growth and proliferation of erythroid progenitor cells alone or in combination with other cytokines, thereby indicating utility, for example, in treating various anemias or for use in conjunction with irradiation/chemotherapy to stimulate the production of erythroid precursors and/or erythroid cells; in supporting the growth and proliferation of myeloid cells such as granulocytes and monocytes/macrophages (i.e., traditional CSF activity) useful, for example, in conjunction with chemotherapy to prevent or treat consequent myelo-suppression; in supporting the growth and proliferation of megakaryocytes and consequently of platelets thereby allowing prevention or treatment of various platelet disorders such as thrombocytopenia, and generally for use in place of or complimentary to platelet transfusions; and/or in supporting the growth and proliferation of hematopoietic stem cells which are capable of maturing to any and all of the above-mentioned hematopoietic cells and therefore find therapeutic utility in various stem cell disorders (such-as those usually treated with transplantation, including, without limitation, aplastic anemia and paroxysmal nocturnal hemoglobinuria), as well as in repopulating the stem cell compartment post irradiation/chemotherapy, either iil-vivo or ex-vivo (i.e., in conjunction with bone marrow transplantation or with peripheral progenitor cell transplantation (homologous or heterologous)) as normal cells or genetically manipulated for gene therapy.  
       [0171] Therapeutic compositions of the invention can be used in the following:  
       [0172] Suitable assays for proliferation and differentiation of various hematopoietic lines are cited above.  
       [0173] Assays for embryonic stem cell differentiation (which will identify, among others, proteins that influence embryonic differentiation hematopoiesis) include, without limitation, those described in: Johansson et al. Cellular Biology 15:141-151, 1995; Keller et al., Molecular and Cellular Biology 13:473-486, 1993; McClanahan et al., Blood 81:2903-2915, 1993.  
       [0174] Assays for stem cell survival and differentiation (which will identify, among others, proteins that regulate Jympho-hematopoiesis) include, without limitation, those described in: Methylcellulose colony forming assays, Freshney, M. G. In Culture of Hematopoietic Cells. R. I. Freshney, et al. eds. Vol pp. 265-268, Wiley-Liss, Inc., New York, N.Y. 1994; Hirayama et al., Proc. Natl. Acad. Sci. USA 89:5907-5911, 1992; Primitive hematopoietic colony forming cells with high proliferative potential, McNiece, I. K. and Briddell, R. A. In Culture of Hematopoietic Cells. R. I. Freshney, et al. eds. Vol pp. 23-39, Wiley-Liss, Inc., New York, N.Y. 1994; Neben et al., Experimental Hematology 22:353-359, 1994; Cobblestone area forming cell assay, Ploemacher, R. E. In Culture of Hematopoietic Cells. R. I. Freshney, et al. eds. Vol pp. 1-21, Wiley-Liss, Inc., New York, N.Y. 1994; Long term bone marrow cultures in the presence of stromal cells, Spooncer, E., Dexter, M. and Allen, T. In Culture of Hematopoietic Cells. R. I. Freshney, et al. eds. Vol pp. 163-179, Wiley-Liss, Inc., New York, N.Y. 1994; Long term culture initiating cell assay, Sutherland, H. J. In Culture of Hematopoietic Cells. R. I. Freshney, et al. eds. Vol pp. 139-162, Wiley-Liss, Inc., New York, N.Y. 1994.  
       Tissue Growth Activity  
       [0175] A polypeptide of the present invention also may be involved in bone, cartilage, tendon, ligament and/or nerve tissue growth or regeneration, as well as in wound healing and tissue repair and replacement, and in healing of bums, incisions and ulcers.  
       [0176] A polypeptide of the present invention which induces cartilage and/or bone growth in circumstances where bone is not normally formed, has application in the healing of bone fractures and cartilage damage or defects in humans and other animals. Compositions of a polypeptide, antibody, binding partner, or other modulator of the invention may have prophylactic use in closed as well as open fracture reduction and also in the improved fixation of artificial joints. De novo bone formation induced by an osteogenic agent contributes to the repair of congenital, trauma induced, or oncologic resection induced craniofacial defects, and also is useful in cosmetic plastic surgery.  
       [0177] A polypeptide of this invention may also be involved in attracting bone-forming cells, stimulating growth of bone-forming cells, or inducing differentiation of progenitors of bone-forming cells. Treatment of osteoporosis, osteoarthritis, bone degenerative disorders, or periodontal disease, such as through stimulation of bone and/or cartilage repair or by blocking inflammation or processes of tissue destruction (collagenase activity, osteoclast activity, etc.) mediated by inflammatory processes may also be possible using the composition of the invention.  
       [0178] Another category of tissue regeneration activity that may involve the polypeptide of the present invention is tendon/ligament formation. Induction of tendon/ligament-like tissue or other tissue formation in circumstances where such tissue is not normally formed, has application in the healing of tendon or ligament tears, deformities and other tendon or ligament defects in humans and other animals. Such a preparation employing a tendon/ligament-like tissue inducing protein may have prophylactic use in preventing damage to tendon or ligament tissue, as well as use in the improved fixation of tendon or ligament to bone or other tissues, and in repairing defects to tendon or ligament tissue. De novo tendon/ligament-like tissue formation induced by a composition of the present invention contributes to the repair of congenital, trauma induced, or other tendon or ligament defects of other origin, and is also useful in cosmetic plastic surgery for attachment or repair of tendons or ligaments. The compositions of the present invention may provide environment to attract tendon- or ligament-forming cells, stimulate growth of tendon- or ligament-forming cells, induce differentiation of progenitors of tendon- or ligament-forming cells, or induce growth of tendon/ligament cells or progenitors ex vivo for return in vivo to effect tissue repair. The compositions of the invention may also be useful in the treatment of tendinitis, carpal tunnel syndrome and other tendon or ligarnent defects. The compositions may also include an appropriate matrix and/or sequestering agent as a carrier as is well known in the art.  
       [0179] The compositions of the present invention may also be useful for proliferation of neural cells and for regeneration of nerve and brain tissue, i.e. for the treatment of central and peripheral nervous system diseases and neuropathies, as well as mechanical and traumatic disorders, which involve degeneration, death or trauma to neural cells or nerve tissue. More specifically, a composition may be used in the treatment of diseases of the peripheral nervous system, such as peripheral nerve injuries, peripheral neuropathy and localized neuropathies, and central nervous system diseases, such as Alzheimer&#39;s, Parkinson&#39;s disease, Huntington&#39;s disease, amyotrophic lateral sclerosis, and Shy-Drager syndrome. Further conditions which may be treated in accordance with the present invention include mechanical and traumatic disorders, such as spinal cord disorders, head trauma and cerebrovascular diseases such as stroke. Peripheral neuropathies resulting from chemotherapy or other medical therapies may also be treatable using a composition of the invention.  
       [0180] Compositions of the invention may also be useful to promote better or faster closure of non-healing wounds, including without limitation pressure ulcers, ulcers associated with vascular insufficiency, surgical and traumatic wounds, and the like.  
       [0181] Compositions of the present invention may also be involved in the generation or regeneration of other tissues, such as organs (including, for example, pancreas, liver, intestine, kidney, skin, endothelium), muscle (smooth, skeletal or cardiac) and vascular (including vascular endothelium) tissue, or for promoting the growth of cells comprising such tissues. Part of the desired effects may be by inhibition or modulation of fibrotic scarring may allow normal tissue to regenerate. A polypeptide of the present invention may also exhibit angiogenic activity.  
       [0182] A composition of the present invention may also be useful for gut protection or regeneration and treatment of lung or liver fibrosis, reperfusion injury in various tissues, and conditions resulting from systemic cytokine damage.  
       [0183] A composition of the present invention may also be useful for promoting or inhibiting differentiation of tissues described above from precursor tissues or cells; or for inhibiting the growth of tissues described above.  
       [0184] Therapeutic compositions of the invention can be used in the following:  
       [0185] Assays for tissue generation activity include, without limitation, those described in: International Patent Publication No. WO95/16035 (bone, cartilage, tendon); International Patent Publication No. WO95/05846 (nerve, neuronal); International Patent Publication No. WO91/07491 (skin, endothelium).  
       [0186] Assays for wound healing activity include, without limitation, those described in: Winter, Epidermal Wound Healing, pps. 71-112 (Maibach, H. I. and Rovee, D. T., eds.), Year Book Medical Publishers, Inc., Chicago, as modified by Eaglstein and Mertz, J. Invest. Dermatol 71:382-84 (1978).  
       Immune Stimulating or Suppressing Activity  
       [0187] A polypeptide of the present invention may also exhibit immune stimulating or immune suppressing activity, including without limitation the activities for which assays are described herein. A polynucleotide of the invention can encode a polypeptide exhibiting such activities. A protein may be useful in the treatment of various immune deficiencies and disorders (including severe combined immunodeficiency (SCID)), e.g., in regulating (up or down) growth and proliferation of T and/or B lymphocytes, as well as effecting the cytolytic activity of NK cells and other cell populations. These immune deficiencies may be genetic or be caused by viral (e.g., HIV) as well as bacterial or fungal infections, or may result from autoimmune disorders. More specifically, infectious diseases causes by viral, bacterial, fungal or other infection may be treatable using a protein of the present invention, including infections by HIV, hepatitis viruses, herpes viruses, mycobacteria, Leishmania spp., malaria spp. and various fungal infections such as candidiasis. Of course, in this regard, proteins of the present invention may also be useful where a boost to the immune system generally may be desirable, i.e., in the treatment of cancer.  
       [0188] Autoimmune disorders which may be treated using a protein of the present invention include, for example, connective tissue disease, multiple sclerosis, systemic lupus erythematosus, rheumatoid arthritis, autoimmune pulmonary inflammation, Guillain-Barre syndrome, autoimmune thyroiditis, insulin dependent diabetes mellitis, myasthenia gravis, graft-versus-host disease and autoimmune inflammatory eye disease. Such a protein (or antagonists thereof, including antibodies) of the present invention may also to be useful in the treatment of allergic reactions and conditions (e.g., anaphylaxis, serum sickness, drug reactions, food allergies, insect venom allergies, mastocytosis, allergic rhinitis, hypersensitivity pneumonitis, urticaria, angioedema, eczema, atopic dermatitis, allergic contact dermatitis, erythema multiforme, Stevens-Johnson syndrome, allergic conjunctivitis, atopic keratoconjunctivitis, venereal keratoconjunctivitis, giant papillary conjunctivitis and contact allergies), such as asthma (particularly allergic asthma) or other respiratory problems. Other conditions, in which immune suppression is desired (including, for example, organ transplantation), may also be treatable using a protein (or antagonists thereof) of the present invention. The therapeutic effects of the polypeptides or antagonists thereof on allergic reactions can be evaluated by in vivo animals models such as the cumulative contact enhancement test (Lastbom et al., Toxicology 125: 59-66, 1998), skin prick test (Hoffmann et al., Allergy 54: 446-54, 1999), guinea pig skin sensitization test (Vohr et al., Arch. Toxocol. 73: 501-9), and murine local lymph node assay (Kimber et al., J. Toxicol. Environ. Health 53: 563-79).  
       [0189] Using the proteins of the invention it may also be possible to modulate immune responses, in a number of ways. Down regulation may be in the form of inhibiting or blocking an immune response already in progress or may involve preventing the induction of an immune response. The functions of activated T cells may be inhibited by suppressing T cell responses or by inducing specific tolerance in T cells, or both. Immunosuppression of T cell responses is generally an active, non-antigen-specific, process which requires continuous exposure of the T cells to the suppressive agent. Tolerance, which involves inducing non-responsiveness or anergy in T cells, is distinguishable from immunosuppression in that it is generally antigen-specific and persists after exposure to the tolerizing agent has ceased. Operationally, tolerance can be demonstrated by the lack of a T cell response upon reexposure to specific antigen in the absence of the tolerizing agent.  
       [0190] Down regulating or preventing one or more antigen functions (including without limitation B lymphocyte antigen functions (such as, for example, B7)), e.g., preventing high level lymphokine synthesis by activated T cells, will be useful in situations of tissue, skin and organ transplantation and in graft-versus-host disease (GVHD). For example, blockage of T cell function should result in reduced tissue destruction in tissue transplantation. Typically, in tissue transplants, rejection of the transplant is initiated through its recognition as foreign by T cells, followed by an immune reaction that destroys the transplant. The administration of a therapeutic composition of the invention may prevent cytokine synthesis by immune cells, such as T cells, and thus acts as an immunosuppressant. Moreover, a lack of costimulation may also be sufficient to anergize the T cells, thereby inducing tolerance in a subject. Induction of long-term tolerance by B lymphocyte antigen-blocking reagents may avoid the necessity of repeated administration of these blocking reagents. To achieve sufficient immunosuppression or tolerance in a subject, it may also be necessary to block the function of a combination of B lymphocyte antigens.  
       [0191] The efficacy of particular therapeutic compositions in preventing organ transplant rejection or GVHD can be assessed using animal models that are predictive of efficacy in humans. Examples of appropriate systems which can be used include allogeneic cardiac grafts in rats and xenogeneic pancreatic islet cell grafts in mice, both of which have been used to examine the immunosuppressive effects of CTLA4Ig fusion proteins in vivo as described in Lenschow et al., Science 257:789-792 (1992) and Turka et al., Proc. Natl. Acad. Sci USA, 89:11102-11105 (1992). In addition, murine models of GVHD (see Paul ed., Fundamental Immunology, Raven Press, New York, 1989, pp. 846-847) can be used to determine the effect of therapeutic compositions of the invention on the development of that disease.  
       [0192] Blocking antigen function may also be therapeutically useful for treating autoimmune diseases. Many autoimmune disorders are the result of inappropriate activation of T cells that are reactive against self-tissue and which promote the production of cytokines and autoantibodies involved in the pathology of the diseases. Preventing the activation of autoreactive T cells may reduce or eliminate disease symptoms. Administration of reagents which block stimulation of T cells can be used to inhibit T cell activation and prevent production of autoantibodies or T cell-delived cytokines which may be involved in the disease process. Additionally, blocking reagents may induce antigen-specific tolerance of autoreactive T cells which could lead to long-term relief from the disease. The efficacy of blocking reagents in preventing or alleviating autoimmune disorders can be determined using a number of well-characterized animal models of human autoimmune diseases. Examples include murine experimental autoimmune encephalitis, systemic lupus erythmatosis in MRL/lpr/lpr mice or NZB hybrid mice, murine autoimmune collagen arthritis, diabetes mellitus in NOD mice and BB rats, and murine experimental myasthenia gravis (see Paul ed., Fundamental Immunology, Raven Press, New York, 1989, pp. 840-856). Upregulation of an antigen function (e.g., a B lymphocyte antigen function), as a means of up regulating immune responses, may also be useful in therapy. Upregulation of immune responses may be in the form of enhancing an existing immune response or eliciting an initial immune response. For example, enhancing an immune response may. be useful in cases of viral infection, including systemic viral diseases such as influenza, the common cold, and encephalitis.  
       [0193] Alternatively, anti-viral immune responses may be enhanced in an infected patient by removing T cells from the patient, costimulating the T cells in vitro with viral antigen-pulsed APCs either expressing a peptide of the present invention or together with a stimulatory form of a soluble peptide of the present invention and reintroducing the in vitro activated T cells into the patient. Another method of enhancing anti-viral immune responses would be to isolate infected cells from a patient, transfect them with a nucleic acid encoding a protein of the present invention as described herein such that the cells express all or a portion of the protein on their surface, and reintroduce the transfected cells into the patient. The infected cells would now be capable of delivering a costimulatory signal to, and thereby activate, T cells in vivo.  
       [0194] A polypeptide of the present invention may provide the necessary stimulation signal to T cells to induce a T cell mediated immune response against the transfected tumor cells. In addition, tumor cells which lack MHC class I or MHC class II molecules, or which fail to reexpress sufficient mounts of MHC class I or MHC class It molecules, can be transfected with nucleic acid encoding all or a portion of (e.g., a cytoplasmic-domain truncated portion) of an MHC class I alpha chain protein and Γ 2  microglobulin protein or an MHC class II alpha chain protein and an MHC class II beta chain protein to thereby express MHC class I or MHC class II proteins on the cell surface. Expression of the appropriate class I or class II MHC in conjunction with a peptide having the activity of a B lymphocyte antigen (e.g., B7-1, B7-2, B7-3) induces a T cell mediated immune response against the transfected tumor cell. Optionally, a gene encoding an antisense construct which blocks expression of an MHC class II associated protein, such as the invariant chain, can also be cotransfected with a DNA encoding a peptide having the activity of a B lymphocyte antigen to promote presentation of tumor associated antigens and induce tumor specific immunity. Thus, the induction of a T cell mediated immune response in a human subject may be sufficient to overcome tumor-specific tolerance in the subject.  
       [0195] The activity of a protein of the invention may, among other means, be measured by the following methods:  
       [0196] Suitable assays for thymocyte or splenocyte cytotoxicity include, without limitation, those described in: Current Protocols in Immunology, Ed by J. E. Coligan, A. M. Kruisbeek, D. H. Margulies, E. M. Shevach, W. Strober, Pub. Greene Publishing Associates and Wiley-Interscience (Chapter 3, In Vitro assays for Mouse Lymphocyte Function 3.1-3.19; Chapter 7, Immunologic studies in Humans); Herrmann et al., Proc. Natl. Acad. Sci. USA 78:2488-2492, 1981; Herrmann et al., J. Immunol. 128:1968-1974, 1982; Handa et al., J. Immunol. 135:1564-1572, 1985; Takai et al., I. Immunol. 137:3494-3500, 1986; Takai et al., J. Immunol. 140:508-512, 1988; Bowman et al., J. Virology 61:1992-1998; Bertagnolli et al., Cellular Immunology 133:327-341, 1991; Brown et al., J. Immunol. 153:3079-3092, 1994.  
       [0197] Assays for T-cell-dependent immunoglobulin responses and isotype switching (which will identify, among others, proteins that modulate T-cell dependent antibody responses and that affect Th1/Th2 profiles) include, without limitation, those described in: Maliszewski, J. Immunol. 144:3028-3033, 1990; and Assays for B cell function: In vitro antibody production, Mond, J. J. and Brunswick, M. In Current Protocols in Immunology. J. E. e.a. Coligan eds. Vol 1 pp. 3.8.1-3.8.16, John Wiley and Sons, Toronto. 1994.  
       [0198] Mixed lymphocyte reaction (MLR) assays (which will identify, among others, proteins that generate predominantly Th1 and CTL responses) include, without limitation, those described in: Current Protocols in Immunology, Ed by J. E. Coligan, A. M. Kruisbeek, D. H. Margulies, E. M. Shevach, W. Strober, Pub. Greene Publishing Associates and Wiley-Interscience (Chapter 3, In Vitro assays for Mouse Lymphocyte Function 3.1-3.19; Chapter 7, Immunologic studies in Humans); Takai et al., J. Immunol. 137:3494-3500, 1986; Takai et al., J. Immunol. 140:508-512, 1988; Bertagnolli et al., J. Immunol. 149:3778-3783, 1992.  
       [0199] Dendritic cell-dependent assays (which will identify, among others, proteins expressed by dendritic cells that activate naive T-cells) include, without limitation, those described in: Guery et al., J. Immunol. 134:536-544, 1995; Inaba et al., Journal of Experimental Medicine 173:549-559, 1991; Macatonia et al., Journal of Immunology 154:5071-5079, 1995; Porgador et al., Journal of Experimental Medicine 182:255-260, 1995; Nair et al., Journal of Virology 67:4062-4069, 1993; Huang et al., Science 264:961-965, 1994; Macatonia et al., Journal of Experimental Medicine 169:1255-1264, 1989; Bhardwaj et al., Journal of Clinical Investigation 94:797-807, 1994; and Inaba et al., Journal of Experimental Medicine 172:631-640, 1990.  
       [0200] Assays for lymphocyte survival/apoptosis (which will identify, among others, proteins that prevent apoptosis after superantigen induction and proteins that regulate lymphocyte homeostasis) include, without limitation, those described in: Darzynkiewicz et al., Cytometry 13:795-808, 1992; Gorczyca et al., Leukemia 7:659-670, 1993; Gorczyca et al., Cancer Research 53:1945-1951, 1993; Itoh et al., Cell 66:233-243, 1991; Zacharchuk, Journal of Immunology 145:4037-4045, 1990; Zamai et al., Cytometry 14:891-897, 1993; Gorczyca et al., International Journal of Oncology 1:639-648, 1992.  
       [0201] Assays for proteins that influence early steps of T-cell commitment and development include, without limitation, those described in: Antica et al., Blood 84:111-117, 1994; Fine et al., Cellular Immunology 155:111-122, 1994; Galy et al., Blood 85:2770-2778, 1995; Toki et al., Proc. Nat. Acad Sci. USA 88:7548-7551, 1991.  
       Activin/Inhibin Activity  
       [0202] A polypeptide of the present invention may also exhibit activin- or inhibin-related activities. A polynucleotide of the invention may encode a polypeptide exhibiting such characteristics. Inhibins are characterized by their ability to inhibit the release of follicle stimulating hormone (FSH), while activins and are characterized by their ability to stimulate the release of follicle stimulating hormone (FSH). Thus, a polypeptide of the present invention, alone or in heterodimers with a member of the inhibin family, may be useful as a contraceptive based on the ability of inhibins to decrease fertility in female mammals and decrease spermatogenesis in male mammals. Administration of sufficient amounts of other inhibins can induce infertility in these mammals. Alternatively, the polypeptide of the invention, as a homodimer or as a heterodimer with other protein subunits of the inhibin group, may be useful as a fertility inducing therapeutic, based upon the ability of activin molecules in stimulating FSH release from cells of the anterior pituitary. See, for example, U.S. Pat. No. 4,798,885. A polypeptide of the invention may also be useful for advancement of the onset of fertility in sexually immature mammals, so as to increase the lifetime reproductive performance of domestic animals such as, but not limited to, cows, sheep and pigs.  
       [0203] The activity of a polypeptide of the invention may, among other means, be measured by the following methods.  
       [0204] Assays for activin/inhibin activity include, without limitation, those described in: Vale et al., Endocrinology 91:562-572, 1972; Ling et al., Nature 321:779-782, 1986; Vale et al., Nature 321:776-779, 1986; Mason et al., Nature 318:659-663, 1985; Forage et al., Proc. Natl. Acad. Sci. USA 83:3091-3095, 1986.  
       Chemotactic/Chemokinetic Activity  
       [0205] A polypeptide of the present invention may be involved in chemotactic or chemokinetic activity for mammalian cells, including, for example, monocytes, fibroblasts, neutrophils, T-cells, mast cells, eosinophils, epithelial and/or endothelial cells. A polynucleotide of the invention can encode a polypeptide exhibiting such attributes. Chemotactic and chemokinetic receptor activation can be used to mobilize or attract a desired cell population to a desired site of action. Chemotactic or chemokinetic compositions (e.g. proteins, antibodies, binding partners, or modulators of the invention) provide particular advantages in treatment of wounds and other trauma to tissues, as well as in treatment of localized infections. For example, attraction of lymphocytes, monocytes or neutrophils to tumors or sites of infection may result in improved immune responses against the tumor or infecting agent.  
       [0206] A protein or peptide has chemotactic activity for a particular cell population if it can stimulate, directly or indirectly, the directed orientation or movement of such cell population. Preferably, the protein or peptide has the ability to directly stimulate directed movement of cells. Whether a particular protein has chemotactic activity for a population of cells can be readily determined by employing such protein or peptide in any known assay for cell chemotaxis.  
       [0207] Therapeutic compositions of the invention can be used in the following:  
       [0208] Assays for chemotactic activity (which will identify proteins that induce or prevent chemotaxis) consist of assays that measure the ability of a protein to induce the migration of cells across a membrane as well as the ability of a protein to induce the adhesion of one cell population to another cell population. Suitable assays for movement and adhesion include, without limitation, those described in: Current Protocols in Immunology, Ed by J. E. Coligan, A. M. Kruisbeek, D. H. Marguiles, E. M. Shevach, W. Strober, Pub. Greene Publishing Associates and Wiley-Interscience (Chapter 6.12, Measurement of alpha and beta Chemokines 6.12.1-6.12.28; Taub et al. J. Clin. Invest. 95:1370-1376, 1995; Lind et al. APMIS 103:140-146, 1995; Muller et al Eur. J. Immunol. 25:1744-1748; Gruber et al. J. of Immunol. 152:5860-5867, 1994; Johnston et al. J. of Immunol. 153:1762-1768, 1994.  
       Hemostatic and Thrombolytic Activity  
       [0209] A polypeptide of the invention may also be involved in hemostatis or thrombolysis or thrombosis. A polynucleotide of the invention can encode a polypeptide exhibiting such attributes. Compositions may be useful in treatment of various coagulation disorders (including hereditary disorders, such as hemophilias) or to enhance coagulation and other hemostatic events in treating wounds resulting from trauma, surgery or other causes. A composition of the invention may also be useful for dissolving or inhibiting formation of thromboses and for treatment and prevention of conditions resulting therefrom (such as, for example, infarction of cardiac and central nervous system vessels (e.g., stroke).  
       [0210] Therapeutic compositions of the invention can be used in the following:  
       [0211] Assay for hemostatic and thrombolytic activity include, without limitation, those described in: Linet et al., J. Clin. Pharmacol. 26:131-140, 1986; Burdick et al., Thrombosis Res. 45:413-419, 1987; Humphrey et al., Fibrinolysis 5:71-79 (1991); Schaub, Prostaglandins 35:467-474, 1988.  
       Cancer Diagnosis and Therapy  
       [0212] Polypeptides of the invention may be involved in cancer cell generation, proliferation or metastasis. Detection of the presence or amount of polynucleotides or polypeptides of the invention may be useful for the diagnosis and/or prognosis of one or more types of cancer. For example, the presence or increased expression of a polynucleotide/polypeptide of the invention may indicate a hereditary risk of cancer, a precancerous condition, or an ongoing malignancy. Conversely, a defect in the gene or absence of the polypeptide may be associated with a cancer condition. Identification of single nucleotide polymorphisms associated with cancer or a predisposition to cancer may also be useful for diagnosis or prognosis.  
       [0213] Cancer treatments promote tumor regression by inhibiting tumor cell proliferation, inhibiting angiogenesis (growth of new blood vessels that is necessary to support tumor growth) and/or prohibiting metastasis by reducing tumor cell motility or invasiveness. Therapeutic compositions of the invention may be effective in adult and pediatric oncology including in solid phase tumors/malignancies, locally advanced tumors, human soft tissue sarcomas, metastatic cancer, including lymphatic metastases, blood cell malignancies including multiple myeloma, acute and chronic leukemias, and lymphomas, head and neck cancers including mouth cancer, larynx cancer and thyroid cancer, lung cancers including small cell carcinoma and non-small cell cancers, breast cancers including small cell carcinoma and ductal carcinoma, gastrointestinal cancers including esophageal cancer, stomach cancer, colon cancer, colorectal cancer and polyps associated with colorectal neoplasia, pancreatic cancers, liver cancer, urologic cancers including bladder cancer and prostate cancer, malignancies of the female genital tract including ovarian carcinoma, uterine (including endometrial) cancers, and solid tumor in the ovarian follicle, kidney cancers including renal cell carcinoma, brain cancers including intrinsic brain tumors, neuroblastoma, astrocytic brain tumors, gliomas, metastatic tumor cell invasion in the central nervous system, bone cancers including osteomas, skin cancers including malignant melanoma, tumor progression of human skin keratinocytes, squamous cell carcinoma, basal cell carcinoma, hemangiopericytoma and Karposi&#39;s sarcoma.  
       [0214] Polypeptides, polynucleotides, or modulators of polypeptides of the invention (including inhibitors and stimulators of the biological activity of the polypeptide of the invention) may be administered to treat cancer. Therapeutic compositions can be administered in therapeutically effective dosages alone or in combination with adjuvant cancer therapy such as surgery, chemotherapy, radiotherapy, thermotherapy, and laser therapy, and may provide a beneficial effect, e.g. reducing tumor size, slowing rate of tumor growth, inhibiting metastasis, or otherwise improving overall clinical condition, without necessarily eradicating the cancer.  
       [0215] The composition can also be administered in therapeutically effective amounts as a portion of an anti-cancer cocktail. An anti-cancer cocktail is a mixture of the polypeptide or modulator of the invention with one or more anti-cancer drugs in addition to a pharmaceutically acceptable carrier for delivery. The use of anti-cancer cocktails as a cancer treatment is routine. Anti-cancer drugs that are well known in the art and can be used as a treatment in combination with the polypeptide or modulator of the invention include: Actinomycin D, Aminoglutethimide, Asparaginase, Bleomycin, Busulfan, Carboplatin, Carmustine, Chlorambucil, Cisplatin (cis-DDP), Cyclophosphamide, Cytarabine HCl (Cytosine arabinoside), Dacarbazine, Dactinomycin, Daunorubicin HCl, Doxorubicin HCl, Estramustine phosphate sodium, Etoposide (V16-213), Floxuridine, 5-Fluorouracil (5-Fu), Flutamide, Hydroxyurea (hydroxycarbamide), Ifosfamide, Interferon Alpha-2a, Interferon Alpha-2b, Leuprolide acetate (LHRH-releasing factor analog), Lomustine, Mechlorethamine HCl (nitrogen mustard), Melphalan, Mercaptopurine, Mesna, Methotrexate (MTX), Mitomycin, Mitoxantrone HCl, Octreotide, Plicamycin, Procarbazine HCl, Streptozocin, Tamoxifen citrate, Thioguanine, Thiotepa, Vinblastine sulfate, Vinciistine sulfate, Amsacrine, Azacitidine, Hexamethylmelamine, Interleukin-2, Mitoguazone, Pentostatin, Semustine, Teniposide, and Vindesine sulfate.  
       [0216] In addition, therapeutic compositions of the invention may be used for prophylactic treatment of cancer. There are hereditary conditions and/or environmental situations (e.g. exposure to carcinogens) known in the art that predispose an individual to developing cancers. Under these circumstances, it may be beneficial to treat these individuals with therapeutically effective doses of the polypeptide of the invention to reduce the risk of developing cancers.  
       [0217] In vitro models can be used to determine the effective doses of the polypeptide of the invention as a potential cancer treatment. These in vitro models include proliferation assays of cultured tumor cells, growth of cultured tumor cells in soft agar (see Freshney, (1987) Culture of Animal Cells: A Manual of Basic Technique, Wily-Liss, New York, N.Y. Ch 18 and Ch 21), tumor systems in nude mice as described in Giovanella et al., J. Natl. Can. Inst., 52: 921-30 (1974), mobility and invasive potential of tumor cells in Boyden Chamber assays as described in Pilkington et al., Anticancer Res., 17: 4107-9 (1997), and angiogenesis assays such as induction of vascularization of the chick chorioallantoic membrane or induction of vascular endothelial cell migration as described in Ribatta et al., Intl. J. Dev. Biol., 40: 1189-97 (1999) and Li et al., Clin. Exp. Metastasis, 17:423-9 (1999), respectively. Suitable tumor cells lines are available, e.g. from American Type Tissue Culture Collection catalogs.  
       Receptor/Ligand Activity  
       [0218] A polypeptide of the present invention may also demonstrate activity as receptor, receptor ligand or inhibitor or agonist of receptor/ligand interactions. A polynucleotide of the invention can encode a polypeptide exhibiting such characteristics. Examples of such receptors and ligands include, without limitation, cytokine receptors and their ligands, receptor kinases and their ligands, receptor phosphatases and their ligands, receptors involved in cell-cell interactions and their ligands (including without limitation, cellular adhesion molecules (such as selectins, integrins and their ligands) and receptor/ligand pairs involved in antigen presentation, antigen recognition and development of cellular and humoral immune responses. Receptors and ligands are also useful for screening of potential peptide or small molecule inhibitors of the relevant receptor/ligand interaction. A protein of the present invention (including, without limitation, fragments of receptors and ligands) may themselves be useful as inhibitors of receptor/ligand interactions.  
       [0219] The activity of a polypeptide of the invention may, among other means, be measured by the following methods:  
       [0220] Suitable assays for receptor-ligand activity include without limitation those described in: Current Protocols in Lrnmunology, Ed by J. E. Coligan, A. M. Kruisbeek, D. H. Margulies, E. M. Shevach, W. Strober, Pub. Greene Publishing Associates and Wiley-Interscience (Chapter 7.28, Measurement of Cellular Adhesion under static conditions 7.28.1-7.28.22), Takai et al., Proc. Natl. Acad. Sci. USA 84:6864-6868, 1987; Bierer et al., J. Exp. Med. 168:1145-1156, 1988; Rosenstein et al., J. Exp. Med. 169:149-160 1989; Stoltenborg et al., J. Immunol. Methods 175:59-68, 1994; Stitt et al., Cell 80:661-670, 1995.  
       [0221] By way of example, the polypeptides of the invention may be used as a receptor for a ligand(s) thereby transmitting the biological activity of that ligand(s). Ligands may be identified through binding assays, affinity chromatography, dihybrid screening assays, BIAcore assays, gel overlay assays, or other methods known in the art.  
       [0222] Studies characterizing drugs or proteins as agonist or antagonist or partial agonists or a partial antagonist require the use of other proteins as competing ligands. The polypeptides of the present invention or ligand(s) thereof may be labeled by being coupled to radioisotopes, calorimetric molecules or a toxin molecules by conventional methods. (“Guide to Protein Purification” Murray P. Deutscher (ed) Methods in Enzymology Vol. 182 (1990) Academic Press, Inc. San Diego). Examples of radioisotopes include, but are not limited to, tritium and carbon-14 . Examples of colorimetric molecules include, but are not limited to, fluorescent molecules such as fluorescamine, or rhodamine or other calorimetric molecules. Examples of toxins include, but are not limited, to ricin.  
       Drug Screening  
       [0223] This invention is particularly useful for screening chemical compounds by using the novel polypeptides or binding fragments thereof in any of a variety of drug screening techniques. The polypeptides or fragments employed in such a test may either be free in solution, affixed to a solid support, borne on a cell surface or located intracellularly. One method of drug screening utilizes eukaryotic or prokaryotic host cells which are stably transformed with recombinant nucleic acids expressing the polypeptide or a fragment thereof. Drugs are screened against such transformed cells in competitive binding assays. Such cells, either in viable or fixed form, can be used for standard binding assays. One may measure, for example, the formation of complexes between polypeptides of the invention or fragments and the agent being tested or examine the diminution in complex formation between the novel polypeptides and an appropriate cell line, which are well known in the art.  
       [0224] Sources for test compounds that may be screened for ability to bind to or modulate (i.e., increase or decrease) the activity of polypeptides of the invention include (1) inorganic and organic chemical libraries, (2) natural product libraries, and (3) combinatorial libraries comprised of either random or mimetic peptides, oligonucleotides or organic molecules.  
       [0225] Chemical libraries may be readily synthesized or purchased from a number of commercial sources, and may include structural analogs of known compounds or compounds that are identified as “hits” or “leads” via natural product screening.  
       [0226] The sources of natural product libraries are microorganisms (including bacteria and fungi), animals, plants or other vegetation, or marine organisms, and libraries of mixtures for screening may be created by: (1) fermentation and extraction of broths from soil, plant or marine microorganisms or (2) extraction of the organisms themselves. Natural product libraries include Polypeptides, non-ribosomal peptides, and (non-naturally occurring) variants thereof. For a review, see  Science  282:63-68 (1998).  
       [0227] Combinatorial libraries are composed of large numbers of peptides, oligonucleotides or organic compounds and can be readily prepared by traditional automated synthesis methods, PCR, cloning or proprietary synthetic methods. Of particular interest are peptide and oligonucleotide combinatorial libraries. Still other libraries of interest include peptide, protein, peptidomimetic, multiparallel synthetic collection, recombinatorial, and polypeptide libraries. For a review of combinatorial chemistry and libraries created therefrom, see Myers,  Curr. Opin. Biotechnol . 8:701-707 (1997). For reviews and examples of peptidomimetic libraries, see Al-Obeidi et al.,  Mol. Biotechnol , 9(3):205-23 (1998); Hruby et al.,  Curr Opin Chem Biol , 1(1):114-19 (1997); Dorner et al.,  Bioorg Med Chem , 4(5):709-15 (1996) (alkylated dipeptides).  
       [0228] Identification of modulators through use of the various libraries described herein permits modification of the candidate “hit” (or “lead”) to optimize the capacity of the “hit” to bind a polypeptide of the invention. The molecules identified in the binding assay are then tested for antagonist or agonist activity in in vivo tissue culture or animal models that are well known in the art. In brief, the molecules are titrated into a plurality of cell cultures or animals and then tested for either cell/animal death or prolonged survival of the animal/cells.  
       [0229] The binding molecules thus identified may be complexed with toxins, e.g., ricin or cholera, or with other compounds that are toxic to cells such as radioisotopes. The toxin-binding molecule complex is then targeted to a tumor or other cell by the specificity of the binding molecule for a polypeptide of the invention. Alternatively, the binding molecules may be complexed with imaging agents for targeting and imaging purposes.  
       Assay for Receptor Activity  
       [0230] The invention also provides methods to detect specific binding of a polypeptide e.g. a ligand or a receptor. The art provides numerous assays particularly useful for identifying previously unknown binding partners for receptor polypeptides of the invention. For example, expression cloning using mammalian or bacterial cells, or dihybrid screening assays can be used to identify polynucleotides encoding binding partners. As another example, affinity chromatography with the appropriate immobilized polypeptide of the invention can be used to isolate polypeptides that recognize and bind polypeptides of the invention. There are a number of different libraries used for the identification of compounds, and in particular small molecules, that modulate (i.e., increase or decrease) biological activity of a polypeptide of the invention. Ligands for receptor polypeptides of the invention can also be identified by adding exogenous ligands, or cocktails of ligands to two cells populations that are genetically identical except for the expression of the receptor of the invention: one cell population expresses the receptor of the invention whereas the other does not. The responses of the two cell populations to the addition of ligands(s) are then compared. Alternatively, an expression library can be co-expressed with the polypeptide of the invention in cells and assayed for an autocrine response to identify potential ligand(s). As still another example, BIAcore assays, gel overlay assays, or other methods known in the art can be used to identify binding partner polypeptides, including, (1) organic and inorganic chemical libraries, (2) natural product libraries, and (3) combinatorial libraries comprised of random peptides, oligonucleotides or organic molecules.  
       [0231] The role of downstream intracellular signaling molecules in the signaling cascade of the polypeptide of the invention can be determined. For example, a chimeric protein in which the cytoplasmic domain of the polypeptide of the invention is fused to the extracellular portion of a protein, whose ligand has been identified, is produced in a host cell. The cell is then incubated with the ligand specific for the extracellular portion of the chimeric protein, thereby activating the chimeric receptor. Known downstream proteins involved in intracellular signaling can then be assayed for expected modifications i.e. phosphorylation. Other methods known to those in the art can also be used to identify signaling molecules involved in receptor activity.  
       Anti-Inflammatory Activity  
       [0232] Compositions of the present invention may also exhibit anti-inflammatory activity. The anti-inflammatory activity may be achieved by providing a stimulus to cells involved in the inflammatory response, by inhibiting or promoting cell-cell interactions (such as, for example, cell adhesion), by inhibiting or promoting chemotaxis of cells involved in the inflammatory process, inhibiting or promoting cell extravasation, or by stimulating or suppressing production of other factors which more directly inhibit or promote an inflammatory response. Compositions with such activities can be used to treat inflammatory conditions including chronic or acute conditions), including without limitation intimation associated with infection (such as septic shock, sepsis or systemic inflammatory response syndrome (SIRS)), ischemia-reperfusion injury, endotoxin lethality, arthritis, complement-mediated hyperacute rejection, nephritis, cytokine or chemokine-induced lung injury, inflammatory bowel disease, Crohn&#39;s disease or resulting from over production of cytokines such as TNF or IL-1. Compositions of the invention may also be useful to treat anaphylaxis and hypersensitivity to an antigenic substance or material. Compositions of this invention may be utilized to prevent or treat conditions such as, but not limited to, sepsis, acute pancreatitis, endotoxin shock, cytokine induced shock, rheumatoid arthritis, chronic inflammatory arthritis, pancreatic cell damage from diabetes mellitus type 1, graft versus host disease, inflammatory bowel disease, inflamation associated with pulmonary disease, other autoimmune disease or inflammatory disease, an antiproliferative agent such as for acute or chronic mylegenous leukemia or in the prevention of premature labor secondary to intrauterine infections.  
       Leukemias  
       [0233] Leukemias and related disorders may be treated or prevented by administration of a therapeutic that promotes or inhibits function of the polynucleotides and/or polypeptides of the invention. Such leukemias and related disorders include but are not limited to acute leukemia, acute lymphocytic leukemia, acute myelocytic leukemia, myeloblastic, promyelocytic, myelomonocytic, monocytic, erythroleukemia, chronic leukemia, chronic myelocytic (granulocytic) leukemia and chronic lymphocytic leukemia (for a review of such disorders, see Fishman et al., 1985, Medicine, 2d Ed., J. B. Lippincott Co., Philadelphia).  
       Nervous System Disorders  
       [0234] Nervous system disorders, involving cell types which can be tested for efficacy of intervention with compounds that modulate the activity of the polynucleotides and/or polypeptides of the invention, and which can be treated upon thus observing an indication of therapeutic utility, include but are not limited to nervous system injuries, and diseases or disorders which result in either a disconnection of axons, a diminution or degeneration of neurons, or demyelination. Nervous system lesions which may be treated in a patient (including human and non-human mammalian patients) according to the invention include but are not limited to the following lesions of either the central (including spinal cord, brain) or peripheral nervous systems:  
       [0235] (i) traumatic lesions, including lesions caused by physical injury or associated with surgery, for example, lesions which sever a portion of the nervous system, or compression injuries;  
       [0236] (ii) ischemic lesions, in which a lack of oxygen in a portion of the nervous system results in neuronal injury or death, including cerebral infarction or ischemia, or spinal cord infarction or ischemia;  
       [0237] (iii) infectious lesions, in which a portion of the nervous system is destroyed or injured as a result of infection, for example, by an abscess or associated with infection by human immunodeficiency virus, herpes zoster, or herpes simplex virus or with Lyme disease, tuberculosis, syphilis;  
       [0238] (iv) degenerative lesions, in which a portion of the nervous system is destroyed or injured as a result of a degenerative process including but not limited to degeneration associated with Parkinson&#39;s disease, Alzheimer&#39;s disease, Huntington&#39;s chorea, or amyotrophic lateral sclerosis;  
       [0239] (v) lesions associated with nutritional diseases or disorders, in which a portion of the nervous system is destroyed or injured by a nutritional disorder or disorder of metabolism including but not limited to, vitamin B12 deficiency, folic acid deficiency, Wernicke disease, tobacco-alcohol amblyopia, Marchiafava-Bignami disease (primary degeneration of the corpus callosum), and alcoholic cerebellar degeneration;  
       [0240] (vi) neurological lesions associated with systemic diseases including but not limited to diabetes (diabetic neuropathy, Bell&#39;s palsy), systemic lupus erythematosus, carcinoma, or sarcoidosis;  
       [0241] (vii) lesions caused by toxic substances including alcohol, lead, or particular neurotoxins; and  
       [0242] (viii) demyelinated lesions in which a portion of the nervous system is destroyed or injured by a demyelinating disease including but not limited to multiple sclerosis, human immunodeficiency virus-associated myelopathy, transverse myelopathy or various etiologies, progressive multifocal leukoencephalopathy, and central pontine myelinolysis.  
       [0243] Therapeutics which are useful according to the invention for treatment of a nervous system disorder may be selected by testing for biological activity in promoting the survival or differentiation of neurons. For example, and not by way of limitation, therapeutics which elicit any of the following effects may be useful according to the invention:  
       [0244] (i) increased survival time of neurons in culture;  
       [0245] (ii) increased sprouting of neurons in culture or in vivo;  
       [0246] (iii) increased production of a neuron-associated molecule in culture or in vivo, e.g., choline acetyltransferase or acetylcholinesterase with respect to motor neurons; or  
       [0247] (iv) decreased symptoms of neuron dysfunction in vivo.  
       [0248] Such effects may be measured by any method known in the art. In preferred, non-limiting embodiments, increased survival of neurons may be measured by the method set forth in Arakawa et al. (1990, J. Neurosci. 10:3507-3515); increased sprouting of neurons may be detected by methods set forth in Pestronk et al. (1980, Exp. Neurol. 70:65-82) or Brown et al. (1981, Ann. Rev. Neurosci. 4:17-42); increased production of neuron-associated molecules may be measured by bioassay, enzymatic assay, antibody binding, Northern blot assay, etc., depending on the molecule to be measured; and motor neuron dysfunction may be measured by assessing the physical manifestation of motor neuron disorder, e.g., weakness, motor neuron conduction velocity, or functional disability.  
       [0249] In specific embodiments, motor neuron disorders that may be treated according to the invention include but are not limited to disorders such as infarction, infection, exposure to toxin, trauma, surgical damage, degenerative disease or malignancy that may affect motor neurons as well as other components of the nervous system, as well as disorders that selectively affect neurons such as amyotrophic lateral sclerosis, and including but not limited to progressive spinal muscular atrophy, progressive bulbar palsy, primary lateral sclerosis, infantile and juvenile muscular atrophy, progressive bulbar paralysis of childhood (Fazio-Londe syndrome), poliomyelitis and the post polio syndrome, and Hereditary Motorsensory Neuropathy (Charcot-Marie-Tooth Disease).  
       Other Activities  
       [0250] A polypeptide of the invention may also exhibit one or more of the following additional activities or effects: inhibiting the growth, infection or function of, or killing, infectious agents, including, without limitation, bacteria, viruses, fungi and other parasites; effecting (suppressing or enhancing) bodily characteristics, including, without limitation, height, weight, hair color, eye color, skin, fat to lean ratio or other tissue pigmentation, or organ or body part size or shape (such as, for example, breast augmentation or diminution, change in bone form or shape); effecting biorhythms or circadian cycles or rhythms; effecting the fertility of male or female subjects; effecting the metabolism, catabolism, anabolism, processing, utilization, storage or elimination of dietary fat, lipid, protein, carbohydrate, vitamins, minerals, co-factors or other nutritional factors or component(s); effecting behavioral characteristics, including, without limitation, appetite, libido, stress, cognition (including cognitive disorders), depression (including depressive disorders) and violent behaviors; providing analgesic effects or other pain reducing effects; promoting differentiation and growth of embryonic stem cells in lineages other than hematopoietic lineages; hormonal or endocrine activity; in the case of enzymes, correcting deficiencies of the enzyme and treating deficiency-related diseases; treatment of hyperproliferative disorders (such as, for example, psoriasis); immunoglobulin-like activity (such as, for example, the ability to bind antigens or complement); and the ability to act as an antigen in a vaccine composition to raise an immune response against such protein or another material or entity which is cross-reactive with such protein.  
       Identification of Polymorphisms  
       [0251] The demonstration of polymorphisms makes possible the identification of such polymorphisms in human subjects and the pharmacogenetic use of this information for diagnosis and treatment. Such polymorphisms may be associated with, e.g., differential predisposition or susceptibility to various disease states (such as disorders involving inflammation or immune response) or a differential response to drug administration, and this genetic information can be used to tailor preventive or therapeutic treatment appropriately. For example, the existence of a polymorphism associated with a predisposition to inflammation or autoimmune disease makes possible the diagnosis of this condition in humans by identifying the presence of the polymorphism.  
       [0252] Polymorphisms can be identified in a variety of ways known in the art which all generally involve obtaining a sample from a patient, analyzing DNA from the sample, optionally involving isolation or amplification of the DNA, and identifying the presence of the polymorphism in the DNA. For example, PCR may be used to amplify an appropriate fragment of genomic DNA which may then be sequenced. Alternatively, the DNA may be subjected to allele-specific oligonucleotide hybridization (in which appropriate oligonucleotides are hybridized to the DNA under conditions permitting detection of a single base mismatch) or to a single nucleotide extension assay (in which an oligonucleotide that hybridizes immediately adjacent to the position of the polymorphism is extended with one or more labeled nucleotides). In addition, traditional restriction fragment length polymorphism analysis (using restriction enzymes that provide differential digestion of the genomic DNA depending on the presence or absence of the polymorphism) may be performed. Arrays with nucleotide sequences of the present invention can be used to detect polymorphisms. The array can comprise modified nucleotide sequences of the present invention in order to detect the nucleotide sequences of the present invention. In the alternative, any one of the nucleotide sequences of the present invention can be placed on the array to detect changes from those sequences.  
       [0253] Alternatively a polymorphism resulting in a change in the amino acid sequence could also be detected by detecting a corresponding change in amino acid sequence of the protein, e.g., by an antibody specific to the variant sequence.  
       Arthritis and Inflammation  
       [0254] The immunosuppressive effects of the compositions of the invention against rheumatoid arthritis is determined in an experimental animal model system. The experimental model system is adjuvant induced arthritis in rats, and the protocol is described by J. Holoshitz, et at., 1983, Science, 219:56, or by B. Waksman et al., 1963, Int. Arch. Allergy Appl. Immunol., 23:129. Induction of the disease can be caused by a single injection, generally intradermally, of a suspension of killed Mycobacterium tuberculosis in complete Freund&#39;s adjuvant (CFA). The route of injection can vary, but rats may be injected at the base of the tail with an adjuvant mixture. The polypeptide is administered in phosphate buffered solution (PBS) at a dose of about 1-5 mg/kg. The control consists of administering PBS only.  
       [0255] The procedure for testing the effects of the test compound would consist of intradermally injecting killed Mycobacterium tuberculosis in CFA followed by immediately administering the test compound and subsequent treatment every other day until day 24. At 14, 15, 18, 20, 22, and 24 days after injection of Mycobacterium CFA, an overall arthritis score may be obtained as described by J. Holoskitz above. An analysis of the data would reveal that the test compound would have a dramatic affect on the swelling of the joints as measured by a decrease of the arthritis score.  
       Therapeutic Methods  
       [0256] The compositions (including polypeptide fragments, analogs, variants and antibodies or other binding partners or modulators including antisense polynucleotides) of the invention have numerous applications in a variety of therapeutic methods. Examples of therapeutic applications include, but are not limited to, those exemplified herein.  
       Example  
       [0257] One embodiment of the invention is the administration of an effective amount of the polypeptides or other composition of the invention to individuals affected by a disease or disorder that can be modulated by regulating the peptides of the invention. While the mode of administration is not particularly important, parenteral administration is preferred. An exemplary mode of administration is to deliver an intravenous bolus. The dosage of the polypeptides or other composition of the invention will normally be determined by the prescribing physician. It is to be expected that the dosage will vary according to the age, weight, condition and response of the individual patient. Typically, the amount of polypeptide administered per dose will be in the range of about 0.01 μg/kg to 100 mg/kg of body weight, with the preferred dose being about 0.1 μg/kg to 10 mg/kg of patient body weight. For parenteral administration, polypeptides of the invention will be formulated in an injectable form combined with a pharmaceutically acceptable parenteral vehicle. Such vehicles are well known in the art and examples include water, saline, Ringer&#39;s solution, dextrose solution, and solutions consisting of small amounts of the human serum albumin. The vehicle may contain minor amounts of additives that maintain the isotonicity and stability of the polypeptide or other active ingredient. The preparation of such solutions is within the skill of the art.  
       Pharmaceutical Formulations and Routes of Administration  
       [0258] A protein or other composition of the present invention (from whatever source derived, including without limitation from recombinant and non-recombinant sources and including antibodies and other binding partners of the polypeptides of the invention) may be administered to a patient in need, by itself, or in pharmaceutical compositions where it is mixed with suitable carriers or excipient(s) at doses to treat or ameliorate a variety of disorders. Such a composition may optionally contain,(in addition to protein or other active ingredient and a carrier) diluents, fillers, salts, buffers, stabilizers, solubilizers, and other materials well known in the art. The term “pharmaceutically acceptable” means a non-toxic material that does not interfere with the effectiveness of the biological activity of the active ingredient(s). The characteristics of the carrier will depend on the route of administration. The pharmaceutical composition of the invention may also contain cytokines, lymphokines, or other hematopoietic factors such as M-CSF, GM-CSF, TNF, IL-1, IL-2, IL-3, IL-4, IL-5, IL-6, IL-7, IL-8, IL-9, IL-10, IL-11, IL-12, IL-13, IL-14, IL-15, IFN, TNFO, TNFI, TNF2, G-CSF, Meg-CSF, thrombopoietin, stem cell factor, and erythropoietin. In further compositions, proteins of the invention may be combined with other agents beneficial to the treatment of the disease or disorder in question. These agents include various growth factors such as epidermal growth factor (EGF), platelet-derived growth factor (PDGF), transforming growth factors (TGF-α and TGF- 62  ), insulin-like growth factor (IGF), as well as cytokines described herein.  
       [0259] The pharmaceutical composition may further contain other agents which either enhance the activity of the protein or other active ingredient or complement its activity or use in treatment. Such additional factors and/or agents may be included in the pharmaceutical composition to produce a synergistic effect with protein or other active ingredient of the invention, or to minimize side effects. Conversely, protein or other active ingredient of the present invention may be included in formulations of the particular clotting factor, cytokine, lymphokine, other hematopoietic factor, thrombolytic or anti-thrombotic factor, or anti-inflammatory agent to minimize side effects of the clotting factor, cytokine, lymphokine, other hematopoietic factor, thrombolytic or anti-thrombotic factor, or anti-inflammatory agent (such as IL-1Ra, IL-1 Hy1, IL-1 Hy2, anti-TNF, corticosteroids, immunosuppressive agents). A protein of the present invention may be active in multimers (e.g., heterodimers or homodimers) or complexes with itself or other proteins. As a result, pharmaceutical compositions of the invention may comprise a protein of the invention in such multimeric or complexed form.  
       [0260] As an alternative to being included in a pharmaceutical composition of the invention including a first protein, a second protein or a therapeutic agent may be concurrently administered with the first protein (e.g., at the same time, or at differing times provided that therapeutic concentrations of the combination of agents is achieved at the treatment site). Techniques for formulation and administration of the compounds of the instant application may be found in “Remington&#39;s Pharmaceutical Sciences,” Mack Publishing Co., Easton, Pa., latest edition. A therapeutically effective dose further refers to that amount of the compound sufficient to result in amelioration of symptoms, e.g., treatment, healing, prevention or amelioration of the relevant medical condition, or an increase in rate of treatment, healing, prevention or amelioration of such conditions. When applied to an individual active ingredient, administered alone, a therapeutically effective dose refers to that ingredient alone. When applied to a combination, a therapeutically effective dose refers to combined amounts of the active ingredients that result in the therapeutic effect, whether administered in combination, serially or simultaneously.  
       [0261] In practicing the method of treatment or use of the present invention, a therapeutically effective amount of protein or other active ingredient of the present invention is administered to a mammal having a condition to be treated. Protein or other active ingredient of the present invention may be administered in accordance with the method of the invention either alone or in combination with other therapies such as treatments employing cytokines, lymphokines or other hematopoietic factors. When co-administered with one or more cytokines, lymphokines or other hematopoietic factors, protein or other active ingredient of the present invention may be administered either simultaneously with the cytokine(s), lymphokine(s), other hematopoietic factor(s), thrombolytic or anti-thrombotic factors, or sequentially. If administered sequentially, the attending physician will decide on the appropriate sequence of administering protein or other active ingredient of the present invention in combination with cytokine(s), lymphokine(s), other hematopoietic factor(s), thrombolytic or anti-thrombotic factors.  
       Routes of Administration  
       [0262] Suitable routes of administration may, for example, include oral, rectal, transmucosal, or intestinal administration; parenteral delivery, including intramuscular, subcutaneous, intramedullary injections, as well as intrathecal, direct intraventricular, intravenous, intraperitoneal, intranasal, or intraocular injections. Administration of protein or other active ingredient of the present invention used in the pharmaceutical composition or to practice the method of the present invention can be carried out in a variety of conventional ways, such as oral ingestion, inhalation, topical application or cutaneous, subcutaneous, intraperitoneal, parenteral or intravenous injection. Intravenous administration to the patient is preferred.  
       [0263] Alternately, one may administer the compound in a local rather than systemic manner, for example, via injection of the compound directly into a arthritic joints or in fibrotic tissue, often in a depot or sustained release formulation. In order to prevent the scarring process frequently occurring as complication of glaucoma surgery, the compounds may be administered topically, for example, as eye drops. Furthermore, one may administer the drug in a targeted drug delivery system, for example, in a liposome coated with a specific antibody, targeting, for example, arthritic or fibrotic tissue. The liposomes will be targeted to and taken up selectively by the afflicted tissue.  
       [0264] The polypeptides of the invention are administered by any route that delivers an effective dosage to the desired site of action. The determination of a suitable route of administration and an effective dosage for a particular indication is within the level of skill in the art. Preferably for wound treatment, one administers the therapeutic compound directly to the site. Suitable dosage ranges for the polypeptides of the invention can be extrapolated from these dosages or from similar studies in appropriate animal models. Dosages can then be adjusted as necessary by the clinician to provide maximal therapeutic benefit.  
       Compositions/Formulations  
       [0265] Pharmaceutical compositions for use in accordance with the present invention thus may be formulated in a conventional manner using one or more physiologically acceptable carriers comprising excipients and auxiliaries which facilitate processing of the active compounds into preparations which can be used pharmaceutically. These pharmaceutical compositions may be manufactured in a manner that is itself known, e.g., by means of conventional mixing, dissolving, granulating, dragee-making, levigating, emulsifying, encapsulating, entrapping or lyophilizing processes. Proper formulation is dependent upon the route of administration chosen. When a therapeutically effective amount of protein or other active ingredient of the present invention is administered orally, protein or other active ingredient of the present invention will be in the form of a tablet, capsule, powder, solution or elixir. When administered in tablet form, the pharmaceutical composition of the invention may additionally contain a solid carrier such as a gelatin or an adjuvant. The tablet, capsule, and powder contain from about 5 to 95% protein or other active ingredient of the present invention, and preferably from about 25 to 90% protein or other active ingredient of the present invention. When administered in liquid form, a liquid carrier such as water, petroleum, oils of animal or plant origin such as peanut oil, mineral oil, soybean oil, or sesame oil, or synthetic oils may be added. The liquid form of the pharmaceutical composition may further contain physiological saline solution, dextrose or other saccharide solution, or glycols such as ethylene glycol, propylene glycol or polyethylene glycol. When administered in liquid form, the pharmaceutical composition contains from about 0.5 to 90% by weight of protein or other active ingredient of the present invention, and preferably from about 1 to 50% protein or other active ingredient of the present invention.  
       [0266] When a therapeutically effective amount of protein or other active ingredient of the present invention is administered by intravenous, cutaneous or subcutaneous injection, protein or other active ingredient of the present invention will be in the form of a pyrogen-free, parenterally acceptable aqueous solution. The preparation of such parenterally acceptable protein or other active ingredient solutions, having due regard to pH, isotonicity, stability, and the like, is within the skill in the art. A preferred pharmaceutical composition for intravenous, cutaneous, or subcutaneous injection should contain, in addition to protein or other active ingredient of the present invention, an isotonic vehicle such as Sodium Chloride Injection, Ringer&#39;s Injection, Dextrose Injection, Dextrose and Sodium Chloride Injection, Lactated Ringer&#39;s Injection, or other vehicle as known in the art. The pharmaceutical composition of the present invention may also contain stabilizers, preservatives, buffers, antioxidants, or other additives known to those of skill in the art. For injection, the agents of the invention may be formulated in aqueous solutions, preferably in physiologically compatible buffers such as Hanks&#39;s solution, Ringer&#39;s solution, or physiological saline buffer. For transmucosal administration, penetrants appropriate to the barrier to be permeated are used in the formulation. Such penetrants are generally known in the art.  
       [0267] For oral administration, the compounds can be formulated readily by combining the active compounds with pharmaceutically acceptable carriers well known in the art. Such carriers enable the compounds of the invention to be formulated as tablets, pills, dragees, capsules, liquids, gels, syrups, slurries, suspensions and the like, for oral ingestion by a patient to be treated. Pharmaceutical preparations for oral use can be obtained from a solid excipient, optionally grinding a resulting mixture, and processing the mixture of granules, after adding suitable auxiliaries, if desired, to obtain tablets or dragee cores. Suitable excipients are, in particular, fillers such as sugars, including lactose, sucrose, mannitol, or sorbitol; cellulose preparations such as, for example, maize starch, wheat starch, rice starch, potato starch, gelatin, gum tragacanth, methyl cellulose, hydroxypropylmethyl-cellulose, sodium carboxymethylcellulose, and/or polyvinylpyrrolidone (PVP). If desired, disintegrating agents may be added, such as the cross-linked polyvinyl pyrrolidone, agar, or alginic acid or a salt thereof such as sodium alginate. Dragee cores are provided with suitable coatings. For this purpose, concentrated sugar solutions may be used, which may optionally contain gum arabic, talc, polyvinyl pyrrolidone, carbopol gel, polyethylene glycol, and/or titanium dioxide, lacquer solutions, and suitable organic solvents or solvent mixtures. Dyestuffs or pigments may be added to the tablets or dragee coatings for identification or to characterize different combinations of active compound doses.  
       [0268] Pharmaceutical preparations which can be used orally include push-fit capsules made of gelatin, as well as soft, sealed capsules made of gelatin and a plasticizer, such as glycerol or sorbitol. The push-fit capsules can contain the active ingredients in admixture with filler such as lactose, binders such as starches, and/or lubricants such as talc or magnesium stearate and, optionally, stabilizers. In soft capsules, the active compounds may be dissolved or suspended in suitable liquids, such as fatty oils, liquid paraffin, or liquid polyethylene glycols. In addition, stabilizers may be added. All formulations for oral administration should be in dosages suitable for such administration. For buccal administration, the compositions may take the form of tablets or lozenges formulated in conventional manner.  
       [0269] For administration by inhalation, the compounds for use according to the present invention are conveniently delivered in the form of an aerosol spray presentation from pressurized packs or a nebuliser, with the use of a suitable propellant, e.g., dichlorodifluoromethane, trichlorofluoromethane, dichlorotetrafluoroethane, carbon dioxide or other suitable gas. In the case of a pressurized aerosol the dosage unit may be determined by providing a valve to deliver a metered amount. Capsules and cartridges of, e.g., gelatin for use in an inhaler or insufflator may be formulated containing a powder mix of the compound and a suitable powder base such as lactose or starch. The compounds may be formulated for parenteral administration by injection, e.g., by bolus injection or continuous infusion. Formulations for injection may be presented in unit dosage form, e.g., in ampules or in multi-dose containers, with an added preservative. The compositions may take such forms as suspensions, solutions or emulsions in oily or aqueous vehicles, and may contain formulatory agents such as suspending, stabilizing and/or dispersing agents.  
       [0270] Pharmaceutical formulations for parenteral administration include aqueous solutions of the active compounds in water-soluble form. Additionally, suspensions of the active compounds may be prepared as appropriate oily injection suspensions. Suitable lipophilic solvents or vehicles include fatty oils such as sesame oil, or synthetic fatty acid esters, such as ethyl oleate or triglycerides, or liposomes. Aqueous injection suspensions may contain substances which increase the viscosity of the suspension, such as sodium carboxymethyl cellulose, sorbitol, or dextran. Optionally, the suspension may also contain suitable stabilizers or agents which increase the solubility of the compounds to allow for the preparation of highly concentrated solutions. Alternatively, the active ingredient may be in powder form for constitution with a suitable vehicle, e.g., sterile pyrogen-free water, before use.  
       [0271] The compounds may also be formulated in rectal compositions such as suppositories or retention enemas, e.g., containing conventional suppository bases such as cocoa butter or other glycerides. In addition to the formulations described previously, the compounds may also be formulated as a depot preparation. Such long acting formulations may be administered by implantation (for example subcutaneously or intramuscularly) or by intramuscular injection. Thus, for example, the compounds may be formulated with suitable polymeric or hydrophobic materials (for example as an emulsion in an acceptable oil) or ion exchange resins, or as sparingly soluble derivatives, for example, as a sparingly soluble salt.  
       [0272] A pharmaceutical carrier for the hydrophobic compounds of the invention is a co-solvent system comprising benzyl alcohol, a nonpolar surfactant, a water-miscible organic polymer, and an aqueous phase. The co-solvent system may be the VPD co-solvent system. VPD is a solution of 3% w/v benzyl alcohol, 8% w/v of the nonpolar surfactant polysorbate 80, and 65% w/v polyethylene glycol 300, made up to volume in absolute ethanol. The VPD co-solvent system (VPD:5W) consists of VPD diluted 1:1 with a 5% dextrose in water solution. This co-solvent system dissolves hydrophobic compounds well, and itself produces low toxicity upon systemic administration. Naturally, the proportions of a co-solvent system may be varied considerably without destroying its solubility and toxicity characteristics. Furthermore, the identity of the co-solvent components may be varied: for example, other low-toxicity nonpolar surfactants may be used instead of polysorbate 80; the fraction size of polyethylene glycol may be varied; other biocompatible polymers may replace polyethylene glycol, e.g. polyvinyl pyrrolidone; and other sugars or polysaccharides may substitute for dextrose. Alternatively, other delivery systems for hydrophobic pharmaceutical compounds may be employed. Liposomes and emulsions are well known examples of delivery vehicles or carriers for hydrophobic drugs. Certain organic solvents such as dimethylsulfoxide also may be employed, although usually at the cost of greater toxicity. Additionally, the compounds may be delivered using a sustained-release system, such as semipermeable matrices of solid hydrophobic polymers containing the therapeutic agent. Various types of sustained-release materials have been established and are well known by those skilled in the art. Sustained-release capsules may, depending on their chemical nature, release the compounds for a few weeks up to over 100 days. Depending on the chemical nature and the biological stability of the therapeutic reagent, additional strategies for protein or other active ingredient stabilization may be employed.  
       [0273] The pharmaceutical compositions also may comprise suitable solid or gel phase carriers or excipients. Examples of such carriers or excipients include but are not limited to calcium carbonate, calcium phosphate, various sugars, starches, cellulose derivatives, gelatin, and polymers such as polyethylene glycols. Many of the active ingredients of the invention may be provided as salts with pharmaceutically compatible counter ions. Such pharmaceutically acceptable base addition salts are those salts which retain the biological effectiveness and properties of the free acids and which are obtained by reaction with inorganic or organic bases such as sodium hydroxide, magnesium hydroxide, ammonia, trialkylamine, dialkylamine, monoalkylamine, dibasic amino acids, sodium acetate, potassium benzoate, triethanol amine and the like.  
       [0274] The pharmaceutical composition of the invention may be in the form of a complex of the protein(s) or other active ingredient(s) of present invention along with protein or peptide antigens. The protein and/or peptide antigen will deliver a stimulatory signal to both B and T lymphocytes. B lymphocytes will respond to antigen through their surface immunoglobulin receptor. T lymphocytes will respond to antigen through the T cell receptor (TCR) following presentation of the antigen by MHC proteins. MHC and structurally related proteins including those encoded by class I and class II MHC genes on host cells will serve to present the peptide antigen(s) to T lymphocytes. The antigen components could also be supplied as purified MHC-peptide complexes alone or with co-stimulatory molecules that can directly signal T cells. Alternatively antibodies able to bind surface immunoglobulin and other molecules on B cells as well as antibodies able to bind the TCR and other molecules on T cells can be combined with the pharmaceutical composition of the invention.  
       [0275] The pharmaceutical composition of the invention may be in the form of a liposome in which protein of the present invention is combined, in addition to other pharmaceutically acceptable carriers, with amphipathic agents such as lipids which exist in aggregated form as micelles, insoluble monolayers, liquid crystals, or lamellar layers in aqueous solution. Suitable lipids for liposomal formulation include, without limitation, mono glycerides, diglycerides, sulfatides, lysolecithins, phospholipids, saponin, bile acids, and the like. Preparation of such liposomal formulations is within the level of skill in the art, as disclosed, for example, in U.S. Pat. Nos. 4,235,871; 4,501,728; 4,837,028; and 4,737,323, all of which are incorporated herein by reference.  
       [0276] The amount of protein or other active ingredient of the present invention in the pharmaceutical composition of the present invention will depend upon the nature and severity of the condition being treated, and on the nature of prior treatments which the patient has undergone. Ultimately, the attending physician will decide the amount of protein or other active ingredient of the present invention with which to treat each individual patient. Initially, the attending physician will administer low doses of protein or other active ingredient of the present invention and observe the patient&#39;s response. Larger doses of protein or other active ingredient of the present invention may be administered until the optimal therapeutic effect is obtained for the patient, and at that point the dosage is not increased further. It is contemplated that the various pharmaceutical compositions used to practice the method of the present invention should contain about 0.01 μg to about 100 mg (preferably about 0.1 μg to about 10 mg, more preferably about 0.1 μg to about 1 mg) of protein or other active ingredient of the present invention per kg body weight. For compositions of the present invention which are useful for bone, cartilage, tendon or ligament regeneration, the therapeutic method includes administering the composition topically, systematically, or locally as an implant or device. When administered, the therapeutic composition for use in this invention is, of course, in a pyrogen-free, physiologically acceptable form. Further, the composition may desirably be encapsulated or injected in a viscous form for delivery to the site of bone, cartilage or tissue damage. Topical administration may be suitable for wound healing and tissue repair. Therapeutically useful agents other than a protein or other active ingredient of the invention which may also optionally be included in the composition as described above, may alternatively or additionally, be administered simultaneously or sequentially with the composition in the methods of the invention. Preferably for bone and/or cartilage formation, the composition would include a matrix capable of delivering the protein-containing or other active ingredient-containing composition to the site of bone and/or cartilage damage, providing a structure for the developing bone and cartilage and optimally capable of being resorbed into the body. Such matrices may be formed of materials presently in use for other implanted medical applications.  
       [0277] The choice of matrix material is based on biocompatibility, biodegradability, mechanical properties, cosmetic appearance and interface properties. The particular application of the compositions will define the appropriate formulation. Potential matrices for the compositions may be biodegradable and chemically defined calcium sulfate, tricalcium phosphate, hydroxyapatite, polylactic acid, polyglycolic acid and polyanhydrides. Other potential materials are biodegradable and biologically well-defined, such as bone or dermal collagen. Further matrices are comprised of pure proteins or extracellular matrix components. Other potential matrices are nonbiodegradable and chemically defined, such as sintered hydroxyapatite, bioglass, aluminates, or other ceramics. Matrices may be comprised of combinations of any of the above-mentioned types of material, such as polylactic acid and hydroxyapatite or collagen and tricalcium phosphate. The bioceramics may be altered in composition, such as in calcium-aluminate-phosphate and processing to alter pore size, particle size, particle shape, and biodegradability. Presently preferred is a 50:50 (mole weight) copolymer of lactic acid and glycolic acid in the form of porous particles having diameters ranging from 150 to 800 microns. In some applications, it will be useful to utilize a sequestering agent, such as carboxymethyl cellulose or autologous blood clot, to prevent the protein compositions from disassociating from the matrix.  
       [0278] A preferred family of sequestering agents is cellulosic materials such as alkylcelluloses (including hydroxyalkylcelluloses), including methylcellulose, ethylcellulose, hydroxyethylcellulose, hydroxypropylcellulose, hydroxypropyl-methylcellulose, and carboxymethylcellulose, the most preferred being cationic salts of carboxymethylcellulose (CMC). Other preferred sequestering agents include hyaluronic acid, sodium alginate, poly(ethylene glycol), polyoxyethylene oxide, carboxyvinyl polymer and poly(vinyl alcohol). The amount of sequestering agent useful herein is 0.5-20 wt %, preferably 1-10 wt % based on total formulation weight, which represents the amount necessary to prevent desorption of the protein from the polymer matrix and to provide appropriate handling of the composition, yet not so much that the progenitor cells are prevented from infiltrating the matrix, thereby providing the protein the opportunity to assist the osteogenic activity of the progenitor cells. In further compositions, proteins or other active ingredients of the invention may be combined with other agents beneficial to the treatment of the bone and/or cartilage defect, wound, or tissue in question. These agents include various growth factors such as epidermal growth factor (EGF), platelet derived growth factor (PDGF), transforming growth factors (TGF-α and TGF-β), and insulin-like growth factor (IGF).  
       [0279] The therapeutic compositions are also presently valuable for veterinary applications. Particularly domestic animals and thoroughbred horses, in addition to humans, are desired patients for such treatment with proteins or other active ingredients of the present invention. The dosage regimen of a protein-containing pharmaceutical composition to be used in tissue regeneration will be determined by the attending physician considering various factors which modify the action of the proteins, e.g., amount of tissue weight desired to be formed, the site of damage, the condition of the damaged tissue, the size of a wound, type of damaged tissue (e.g., bone), the patient&#39;s age, sex, and diet, the severity of any infection, time of administration and other clinical factors. The dosage may vary with the type of matrix used in the reconstitution and with inclusion of other proteins in the pharmaceutical composition. For example, the addition of other known growth factors, such as IGF I (insulin like growth factor I), to the final composition, may also effect the dosage. Progress can be monitored by periodic assessment of tissue/bone growth and/or repair, for example, X-rays, histomorphometric determinations and tetracycline labeling.  
       [0280] Polynucleotides of the present invention can also be used for gene therapy. Such polynucleotides can be introduced either in vivo or ex vivo into cells for expression in a mammalian subject. Polynucleotides of the invention may also be administered by other known methods for introduction of nucleic acid into a cell or organism (including, without limitation, in the form of viral vectors or naked DNA). Cells may also be cultured ex vivo in the presence of proteins of the present invention in order to proliferate or to produce a desired effect on or activity in such cells. Treated cells can then be introduced in vivo for therapeutic purposes.  
       Effective Dosage  
       [0281] Pharmaceutical compositions suitable for use in the present invention include compositions wherein the active ingredients are contained in an effective amount to achieve its intended purpose. More specifically, a therapeutically effective amount means an amount effective to prevent development of or to alleviate the existing symptoms of the subject being treated. Determination of the effective amount is well within the capability of those skilled in the art, especially in light of the detailed disclosure provided herein. For any compound used in the method of the invention, the therapeutically effective dose can be estimated initially from appropriate in vitro assays. For example, a dose can be formulated in animal models to achieve a circulating concentration range that can be used to more accurately determine useful doses in humans. For example, a dose can be formulated in animal models to achieve a circulating concentration range that includes the IC 50  as determined in cell culture (i.e., the concentration of the test compound which achieves a half-maximal inhibition of the protein&#39;s biological activity). Such information can be used to more accurately determine useful doses in humans.  
       [0282] A therapeutically effective dose refers to that amount of the compound that results in amelioration of symptoms or a prolongation of survival in a patient. Toxicity and therapeutic efficacy of such compounds can be determined by standard pharmaceutical procedures in cell cultures or experimental animals, e.g., for determining the LD 50  (the dose lethal to 50% of the population) and the ED 50  (the dose therapeutically effective in 50% of the population). The dose ratio between toxic and therapeutic effects is the therapeutic index and it can be expressed as the ratio between LD 50  and ED 50 . Compounds which exhibit high therapeutic indices are preferred. The data obtained from these cell culture assays and animal studies can be used in formulating a range of dosage for use in human. The dosage of such compounds lies preferably within a range of circulating concentrations that include the ED 50  with little or no toxicity. The dosage may vary within this range depending upon the dosage form employed and the route of administration utilized. The exact formulation, route of administration and dosage can be chosen by the individual physician in view of the patient&#39;s condition. See, e.g., Fingl et al., 1975, in “The Pharmnacological Basis of Therapeutics”, Ch. 1 p.1. Dosage amount and interval may be adjusted individually to provide plasma levels of the active moiety which are sufficient to maintain the desired effects, or minimal effective concentration (AEC). The MEC will vary for each compound but can be estimated from in vitro data. Dosages necessary to achieve the MEC will depend on individual characteristics and route of administration. However, BPLC assays.or bioassays can be used to determine plasma concentrations.  
       [0283] Dosage intervals can also be determined using MEC value. Compounds should be administered using a regimen which maintains plasma levels above the MEC for 1O-90% of the time, preferably between 30-90% and most preferably between 50-90%. In cases of local administration or selective uptake, the effective local concentration of the drug may not be related to plasma concentration.  
       [0284] An exemplary dosage regimen for polypeptides or other compositions of the invention will be in the range of about 0.01 μg/kg to 100 mg/kg of body weight daily, with the preferred dose being about 0.1 μg/kg to 25 mg/kg of patient body weight daily, varying in adults and children. Dosing may be once daily, or equivalent doses may be delivered at longer or shorter intervals.  
       [0285] The amount of composition administered will, of course, be dependent on the subject being treated, on the subject&#39;s age and weight, the severity of the affliction, the manner of administration and the judgment of the prescribing physician.  
       Packaging  
       [0286] The compositions may, if desired, be presented in a pack or dispenser device which may contain one or more unit dosage forms containing the active ingredient. The pack may, for example, comprise metal or plastic foil, such as a blister pack. The pack or dispenser device may be accompanied by instructions for administration. Compositions comprising a compound of the invention formulated in a compatible pharmaceutical carrier may also be prepared, placed in an appropriate container, and labeled for treatment of an indicated condition.  
       Antibodies  
       [0287] Also included in the invention are antibodies to proteins, or fragments of proteins of the invention. The term “antibody” as used herein refers to immunoglobulin molecules and immunologically active portions of immunoglobulin (Ig) molecules, i.e., molecules that contain an antigen-binding site that specifically binds (immunoreacts with) an antigen. Such antibodies include, but are not limited to, polyclonal, monoclonal, chimeric, single chain, F ab , F ab , and F (ab′)2  fragments, and an F ab  expression library. In general, an antibody molecule obtained from humans relates to any of the classes IgG, IgM, IgA, IgE and IgD, which differ from one another by the nature of the heavy chain present in the molecule. Certain classes have subclasses as well, such as IgG 1 , IgG 2 , and others. Furthermore, in humans, the light chain may be a kappa chain or a lambda chain. Reference herein to antibodies includes a reference to all such classes, subclasses and types of human antibody species.  
       [0288] An isolated related protein of the invention may be intended to serve as an antigen, or a portion or fragment thereof, and additionally can be used as an immunogen to generate antibodies that immunospecifically bind the antigen, using standard techniques for polyclonal and monoclonal antibody preparation. The full-length protein can be used or, alternatively, the invention provides antigenic peptide fragments of the antigen for use as immunogens. An antigenic peptide fragment comprises at least 6 amino acid residues of the amino acid sequence of the full length protein, such as an amino acid sequence shown in SEQ ID NO: 338-674, or 837-998, or Tables 3, 5, 6, 8, or 9, and encompasses an epitope thereof such that an antibody raised against the peptide forms a specific immune complex with the full length protein or with any fragment that contains the epitope. Preferably, the antigenic peptide comprises at least 10 amino acid residues, or at least 15 amino acid residues, or at least 20 amino acid residues, or at least 30 amino acid residues. Preferred epitopes encompassed by the antigenic peptide are regions of the protein that are located on its surface; commonly these are hydrophilic regions.  
       [0289] In certain embodiments of the invention, at least one epitope encompassed by the antigenic peptide is a surface region of the protein, e.g., a hydrophilic region. A hydrophobicity analysis of the human related protein sequence will indicate which regions of a related protein are particularly hydrophilic and, therefore, are likely to encode surface residues useful for targeting antibody production. As a means for targeting antibody production, hydropathy plots showing regions of hydrophilicity and hydrophobicity may be generated by any method well known in the art, including, for example, the Kyte Doolittle or the Hopp Woods methods, either with or without Fourier transformation. See, e.g., Hopp and Woods, 1981, Proc. Nat. Acad. Sci. USA 78: 3824-3828; Kyte and Doolittle 1982, J. Mol. Biol. 157: 105-142, each of which is incorporated herein by reference in its entirety. Antibodies that are specific for one or more domains within an antigenic protein, or derivatives, fragments, analogs or homologs thereof, are also provided herein.  
       [0290] A protein of the invention, or a derivative, fragment, analog, homolog or ortholog thereof, may be utilized as an immunogen in the generation of antibodies that immunospecifically bind these protein components.  
       [0291] The term “specific for” indicates that the variable regions of the antibodies of the invention recognize and bind polypeptides of the invention exclusively (i.e., able to distinguish the polypeptide of the invention from other similar polypeptides despite sequence identity, homology, or similarity found in the family of polypeptides), but may also interact with other proteins (for example,  S. aureus  protein A or other antibodies in ELISA techniques) through interactions with sequences outside the variable region of the antibodies, and in particular, in the constant region of the molecule. Screening assays to determine binding specificity of an antibody of the invention are well known and routinely practiced in the art. For a comprehensive discussion of such assays, see Harlow et al. (Eds), Antibodies A Laboratory Manual; Cold Spring Harbor Laboratory; Cold Spring Harbor, N.Y. (1988), Chapter 6. Antibodies that recognize and bind fragments of the polypeptides of the invention are also contemplated, provided that the antibodies are first and foremost specific for, as defined above, full-length polypeptides of the invention. As with antibodies that are specific for full length polypeptides of the invention, antibodies of the invention that recognize fragments are those which can distinguish polypeptides from the same family of polypeptides despite inherent sequence identity, homology, or similarity found in the family of proteins.  
       [0292] Antibodies of the invention are useful for, for example, therapeutic purposes (by modulating activity of a polypeptide of the invention), diagnostic purposes to detect or quantitate a polypeptide of the invention, as well as purification of a polypeptide of the invention. Kits comprising an antibody of the invention for any of the purposes described herein are also comprehended. In general, a kit of the invention also includes a control antigen for which the antibody is immunospecific. The invention further provides a hybridoma that produces an antibody according to the invention. Antibodies of the invention are useful for detection and/or purification of the polypeptides of the invention.  
       [0293] Monoclonal antibodies binding to the protein of the invention may be useful diagnostic agents for the immunodetection of the protein. Neutralizing monoclonal antibodies binding to the protein may also be useful therapeutics for both conditions associated with the protein and also in the treatment of some forms of cancer where abnormal expression of the protein is involved. In the case of cancerous cells or leukemic cells, neutralizing monoclonal antibodies against the protein may be useful in detecting and preventing the metastatic spread of the cancerous cells, which may be mediated by the protein.  
       [0294] The labeled antibodies of the present invention can be used for in vitro, in vivo, and in situ assays to identify cells or tissues in which a fragment of the polypeptide of interest is expressed. The antibodies may also be used directly in therapies or other diagnostics. The present invention further provides the above-described antibodies immobilized on a solid support. Examples of such solid supports include plastics such as polycarbonate, complex carbohydrates such as agarose and Sepharose®, acrylic resins and such as polyacrylamide and latex beads. Techniques for coupling antibodies to such solid supports are well known in the art (Weir, D. M. et al., “Handbook of Experimental Immunology” 4th Ed., Blackwell Scientific Publications, Oxford, England, Chapter 10 (1986); Jacoby, W. D. et al., Meth. Enzym. 34 Academic Press, N.Y. (1974)). The immobilized antibodies of the present invention can be used for in vitro, in vivo, and in situ assays as well as for immuno-affinity purification of the proteins of the present invention.  
       [0295] Various procedures known within the art may be used for the production of polyclonal or monoclonal antibodies directed against a protein of the invention, or against derivatives, fragments, analogs homologs or orthologs thereof (see, for example, Antibodies: A Laboratory Manual, Harlow E, and Lane D, 1988, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., incorporated herein by reference). Some of these antibodies are discussed below.  
       Polyclonal Antibodies  
       [0296] For the production of polyclonal antibodies, various suitable host animals (e.g., rabbit, goat, mouse or other mammal) may be immunized by one or more injections with the native protein, a synthetic valiant thereof, or a derivative of the foregoing. An appropriate immunogenic preparation can contain, for example, the naturally occurring immunogenic protein, a chemically synthesized polypeptide representing the immunogenic protein, or a recombinantly expressed immunogenic protein. Furthermore, the protein may be conjugated to a second protein known to be immunogenic in the mammal being immunized. Examples of such immunogenic proteins include but are not limited to keyhole limpet hemocyanin, serum albumin, bovine thyroglobulin, and soybean trypsin inhibitor. The preparation can further include an adjuvant. Various adjuvants used to increase the immunological response include, but are not limited to, Freund&#39;s (complete and incomplete), mineral gels (e.g., aluminum hydroxide), surface-active substances (e.g., lysolecithin, pluronic polyols, polyanions, peptides, oil emulsions, dinitrophenol, etc.), adjuvants usable in humans such as Bacille Calmette-Guerin and Corynebacterium parvum, or similar immunostimulatory agents. Additional examples of adjuvants that can be employed include MPL-TDM adjuvant (monophosphoryl Lipid A, synthetic trehalose dicorynomycolate).  
       [0297] The polyclonal antibody molecules directed against the immunogenic protein can be isolated from the mammal (e.g., from the blood) and further purified by well known techniques, such as affinity chromatography using protein A or protein G, which provide primarily the IgG fraction of immune serum. Subsequently, or alternatively, the specific antigen which is the target of the immunoglobulin sought, or an epitope thereof, may be immobilized on a column to purify the immune specific antibody by immunoaffinity chromatography. Purification of immunoglobulins is discussed, for example, by D. Wilkinson (The Scientist, published by The Scientist, Inc., Philadelphia Pa., Vol. 14, No. 8 (Apr. 17, 2000), pp. 25-28).  
       Monoclonal Antibodies  
       [0298] The term “monoclonal antibody” (MAb) or “monoclonal antibody composition”, as used herein, refers to a population of antibody molecules that contain only one molecular species of antibody molecule consisting of a unique light chain gene product and a unique heavy chain gene product. In particular, the complementarity determining regions (CDRs) of the monoclonal antibody are identical in all the molecules of the population. MAbs thus contain an antigen-binding site capable of immunoreacting with a particular epitope of the antigen characterized by a unique binding affinity for it.  
       [0299] Monoclonal antibodies can be prepared using hybridoma methods, such as those described by Kohler and Milstein, Nature, 256, 495 (1975). In a hybridoma method, a mouse, hamster, or other appropriate host animal, is typically immunized with an immunizing agent to elicit lymphocytes that produce or are capable of producing antibodies that will specifically bind to the immunizing agent. Alternatively, the lymphocytes can be immunized in vitro.  
       [0300] The immunizing agent will typically include the protein antigen, a fragment thereof or a fusion protein thereof. Generally, either peripheral blood lymphocytes are used if cells of human origin are desired, or spleen cells or lymph node cells are used if non-human mammalian sources are desired. The lymphocytes are then fused with an immortalized cell line using a suitable fusing agent, such as polyethylene glycol, to form a hybridoma cell (Goding, Monoclonal Antibodies: Principles and Practice, Academic Press, (1986) pp. 59-103). Immortalized cell lines are usually transformed mammalian cells, particularly myeloma cells of rodent, bovine and human origin. Usually, rat or mouse myeloma cell lines are employed. The hybridoma cells can be cultured in a suitable culture medium that preferably contains one or more substances that inhibit the growth or survival of the unfused, immortalized cells. For example, if the parental cells lack the enzyme hypoxanthine guanine phosphoribosyl transferase (HGPRT or HPRT), the culture medium for the hybridomas typically will include hypoxanthine, aminopterin, and thymidine (“HAT medium”), which substances prevent the growth of HGPRT-deficient cells.  
       [0301] Preferred immortalized cell lines are those that fuse efficiently, support stable high level expression of antibody by the selected antibody-producing cells, and are sensitive to a medium such as HAT medium. More preferred immortalized cell lines are murine myeloma lines, which can be obtained, for instance, from the Salk Institute Cell Distribution Center, San Diego, Calif. and the American Type Culture Collection, Manassas, Va. Human myeloma and mouse-human heteromyeloma cell lines also have been described for the production of human monoclonal antibodies (Kozbor, J. Immunol., 133:3001 (1984); Brodeur et al., Monoclonal Antibody Production Techniques and Applications, Marcel Dekker, Inc., New York, (1987) pp. 51-63).  
       [0302] The culture medium in which the hybridoma cells are cultured can then be assayed for the presence of monoclonal antibodies directed against the antigen. Preferably, the binding specificity of monoclonal antibodies produced by the hybridoma cells is determined by immunoprecipitation or by an in vitro binding assay, such as radioimmunoassay (RIA) or enzyme-linked immunoabsorbent assay (ELISA). Such techniques and assays are known in the art. The binding affinity of the monoclonal antibody can, for example, be determined by the Scatchard analysis of Munson and Pollard, Anal. Biochem., 107, 220 (1980). Preferably, antibodies having a high degree of specificity and a high binding affinity for the target antigen are isolated.  
       [0303] After the desired hybridoma cells are identified, the clones can be subcloned by limiting dilution procedures and grown by standard methods. Suitable culture media for this purpose include, for example, Dulbecco&#39;s Modified Eagle&#39;s Medium and RPMI-1640 medium. Alternatively, the hybridoma cells can be grown in vivo as ascites in a mammal.  
       [0304] The monoclonal antibodies secreted by the subclones can be isolated or purified from the culture medium or ascites fluid by conventional immunoglobulin purification procedures such as, for example, protein A-Sepharose, hydroxylapatite chromatography, gel electrophoresis, dialysis, or affinity chromatography.  
       [0305] The monoclonal antibodies can also be made by recombinant DNA methods, such as those described in U.S. Pat. No. 4,816,567. DNA encoding the monoclonal antibodies of the invention can be readily isolated and sequenced using conventional procedures (e.g., by using oligonucleotide probes that are capable of binding specifically to genes encoding the heavy and light chains of murine antibodies). The hybridoma cells of the invention serve as a preferred source of such DNA. Once isolated, the DNA can be placed into expression vectors, which are then transfected into host cells such as simian COS cells, Chinese hamster ovary (CHO) cells, or myeloma cells that do not otherwise produce immunoglobulin protein, to obtain the synthesis of monoclonal antibodies in the recombinant host cells. The DNA also can be modified, for example, by substituting the coding sequence for human heavy and light chain constant domains in place of the homologous murine sequences (U.S. Pat. No. 4,816,567; Morrison, Nature 368, 812-13 (1994)) or by covalently joining to the immunoglobulin coding sequence all or part of the coding sequence for a non-immunoglobulin polypeptide. Such a non-immunoglobulin polypeptide can be substituted for the constant domains of an antibody of the invention, or can be substituted for the variable domains of one antigen-combining site of an antibody of the invention to create a chimeric bivalent antibody.  
       Humanized Antibodies  
       [0306] The antibodies directed against the protein antigens of the invention can further comprise humanized antibodies or human antibodies. These antibodies are suitable for administration to humans without engendering an immune response by the human against the administered immunoglobulin. Humanized forms of antibodies are chimeric immunoglobulins, immunoglobulin chains or fragments thereof (such as Fv, Fab, Fab′, F(ab′) 2  or other antigen-binding subsequences of antibodies) that are principally comprised of the sequence of a human immunoglobulin, and contain minimal sequence derived from a non-human immunoglobulin. Humanization can be performed following the method of Winter and co-workers (Jones et al., Nature, 321, 522-525 (1986); Riechmann et al., Nature, 332, 323-327 (1988); Verhoeyen et al., Science, 239, 1534-1536 (1988)), by substituting rodent CDRs or CDR sequences for the corresponding sequences of a human antibody. (See also U.S. Pat. No. 5,225,539). In some instances, Fv framework residues of the human immunoglobulin are replaced by corresponding non-human residues. Humanized antibodies can also comprise residues that are found neither in the recipient antibody nor in the imported CDR or framework sequences. In general, the humanized antibody will comprise substantially all of at least one, and typically two, variable domains, in which all or substantially all of the CDR regions correspond to those of a non-human immunoglobulin and all or substantially all of the framework regions are those of a human immunoglobulin consensus sequence. The humanized antibody optimally also will comprise at least a portion of an immunoglobulin constant region (Fc), typically that of a human immunoglobulin (Jones et al., 1986; Riechmann et al., 1988; and Presta, Curr. Op. Struct. Biol., 2, 593-596 (1992)).  
       Human Antibodies  
       [0307] Fully human antibodies relate to antibody molecules in which essentially the entire sequences of both the light chain and the heavy chain, including the CDRs, arise from human genes. Such antibodies are termed “human antibodies”, or “fully human antibodies” herein. Human monoclonal antibodies can be prepared by the trioma technique; the human B-cell hybridoma technique (see Kozbor, et al., 1983 Immunol Today 4: 72) and the EBV hybridoma technique to produce human monoclonal antibodies (see Cole, et al., 1985 In: Monoclonal Antibodies and Cancer Therapy, Alan R. Liss, Inc., pp. 77-96). Human monoclonal antibodies may be utilized in the practice of the present invention and may be produced by using human hybridomas (see Cote, et al., 1983. Proc Natl Acad Sci USA 80, 2026-2030) or by transforming human B-cells with Epstein Barr Virus in vitro (see Cole, et al., 1985 In: Monoclonal Antibodies and Cancer Therapy, Alan R. Liss, Inc., pp. 77-96).  
       [0308] In addition, human antibodies can also be produced using additional techniques, including phage display libraries (Hoogenboom and Winter, J. Mol. Biol., 227, 381 (1991); Marks et al., J. Mol. Biol., 222:581 (1991)). Similarly, human antibodies can be made by introducing human immunoglobulin loci into transgenic animals, e.g., mice in which the endogenous immunoglobulin genes have been partially or completely inactivated. Upon challenge, human antibody production is observed, which closely resembles that seen in humans in all respects, including gene rearrangement, assembly, and antibody repertoire. This approach is described, for example, in U.S. Pat. Nos. 5,545,807; 5,545,806; 5,569,825; 5,625,126; 5,633,425; 5,661,016, and in Marks et al. (Bio/Technology 10, 779-783 (1992)); Lonberg et al. (Nature 368, 856-859 (1994)); Morrison (Nature 368, 812-13 (1994)); Fishwild et al, (Nature Biotechnology 14, 845-51 (1996)); Neuberger (Nature Biotechnology 14, 826 (1996)); and Lonberg and Huszar (Intern. Rev. Immunol. 13, 65-93 (1995)).  
       [0309] Human antibodies may additionally be produced using transgenic nonhuman animals that are modified so as to produce fully human antibodies rather than the animal&#39;s endogenous antibodies in response to challenge by an antigen. (See PCT publication WO94/02602). The endogenous genes encoding the heavy and light immunoglobulin chains in the nonhuman host have been incapacitated, and active loci encoding human heavy and light chain immunoglobulins are inserted into the host&#39;s genome. The human genes are incorporated, for example, using yeast artificial chromosomes containing the requisite human DNA segments. An animal which provides all the desired modifications is then obtained as progeny by crossbreeding intermediate transgenic animals containing fewer than the full complement of the modifications. The preferred embodiment of such a nonhuman animal is a mouse, and is termed the Xenomouse™ as disclosed in PCT publications WO 96/33735 and WO 96/34096. This animal produces B cells that secrete fully human immunoglobulins. The antibodies can be obtained directly from the animal after immunization with an immunogen of interest, as, for example, a preparation of a polyclonal antibody, or alternatively from immortalized B cells derived from the animal, such as hybridomas producing monoclonal antibodies. Additionally, the genes encoding the immunoglobulins with human variable regions can be recovered and expressed to obtain the antibodies directly, or can be further modified to obtain analogs of antibodies such as, for example, single chain Fv molecules.  
       [0310] An example of a method of producing a nonhuman host, exemplified as a mouse, lacking expression of an endogenous immunoglobulin heavy chain is disclosed in U.S. Pat. No. 5,939,598. It can be obtained by a method including deleting the J segment genes from at least one endogenous heavy chain locus in an embryonic stem cell to prevent rearrangement of the locus and to prevent formation of a transcript of a rearranged immunoglobulin heavy chain locus, the deletion being effected by a targeting vector containing a gene encoding a selectable marker; and producing from the embryonic stem cell a transgenic mouse whose somatic and germ cells contain the gene encoding the selectable marker.  
       [0311] A method for producing an antibody of interest, such as a human antibody, is disclosed in U.S. Pat. No. 5,916,771. It includes introducing an expression vector that contains a nucleotide sequence encoding a heavy chain into one mammalian host cell in culture, introducing an expression vector containing a nucleotide sequence encoding a light chain into another mammalian host cell, and fusing the two cells to form a hybrid cell. The hybrid cell expresses an antibody containing the heavy chain and the light chain.  
       [0312] In a further improvement on this procedure, a method for identifying a clinically relevant epitope on an immunogen, and a correlative method for selecting an antibody that binds immunospecifically to the relevant epitope with high affinity, are disclosed in PCT publication WO 99/53049.  
       Fab Fragments and Single Chain Antibodies  
       [0313] According to the invention, techniques can be adapted for the production of single-chain antibodies specific to an antigenic protein of the invention (see e.g., U.S. Pat. No. 4,946,778). In addition, methods can be adapted for the construction of F ab  expression libraries (see e.g., Huse, et al., 1989 Science 246, 1275-1281) to allow rapid and effective identification of monoclonal F ab  fragments with the desired specificity for a protein or derivatives, fragments, analogs or homologs thereof. Antibody fragments that contain the idiotypes to a protein antigen may be produced by techniques known in the art including, but not limited to: (i) an F (ab′)2  fragment produced by pepsin digestion of an antibody molecule; (ii) an F ab  fragment generated by reducing the disulfide bridges of an F (ab′)2  fragment; (iii) an F ab  fragment generated by the treatment of the antibody molecule with papain and a reducing agent and (iv) F v  fragments.  
       Bispecific Antibodies  
       [0314] Bispecific antibodies are monoclonal, preferably human or humanized, antibodies that have binding specificities for at least two different antigens. In the present case, one of the binding specificities is for an antigenic protein of the invention. The second binding target is any other antigen, and advantageously is a cell-surface protein or receptor or receptor subunit.  
       [0315] Methods for making bispecific antibodies are known in the art. Traditionally, the recombinant production of bispecific antibodies is based on the co-expression of two immunoglobulin heavy-chain/light-chain pairs, where the two heavy chains have different specificities (Milstein and Cuello, Nature, 305, 537-539 (1983)). Because of the random assortment of immunoglobulin heavy and light chains, these hybridomas (quadromas) produce a potential mixture of ten different antibody molecules, of which only one has the correct bispecific structure. The purification of the correct molecule is usually accomplished by affinity chromatography steps. Similar procedures are disclosed in WO 93/08829, published May 13, 1993, and in Traunecker et al., 1991  EMBO J ., 10, 3655-3659.  
       [0316] Antibody variable domains with the desired binding specificities (antibody-antigen combining sites) can be fused to immunoglobulin constant domain sequences. The fusion preferably is with an immunoglobulin heavy-chain constant domain, comprising at least part of the hinge, CH2, and CH3 regions. It is preferred to have the first heavy-chain constant region (CH1) containing the site necessary for light-chain binding present in at least one of the fusions. DNAs encoding the immunoglobulin heavy-chain fusions and, if desired, the immunoglobulin light chain, are inserted into separate expression vectors, and are co-transfected into a suitable host organism. For further details of generating bispecific antibodies see, for example, Suresh et al., Methods in Enzymology, 121, 210 (1986).  
       [0317] According to another approach described in WO 96/27011, the interface between a pair of antibody molecules can be engineered to maximize the percentage of heterodimers that are recovered from recombinant cell culture. The preferred interface comprises at least a part of the CH3 region of an antibody constant domain. In this method, one or more small amino acid side chains from the interface of the first antibody molecule are replaced with larger side chains (e.g. tyrosine or tryptophan). Compensatory “cavities” of identical or similar size to the large side chain(s) are created on the interface of the second antibody molecule by replacing large amino acid side chains with smaller ones (e.g. alanine or threonine). This provides a mechanism for increasing the yield of the heterodimer over other unwanted end-products such as homodimers.  
       [0318] Bispecific antibodies can be prepared as full-length antibodies or antibody fragments (e.g. F(ab′) 2  bispecific antibodies). Techniques for generating bispecific antibodies from antibody fragments have been described in the literature. For example, bispecific antibodies can be prepared using chemical linkage. Brennan et al., Science 229, 81 (1985) describe a procedure wherein intact antibodies are proteolytically cleaved to generate F(ab′) 2  fragments. These fragments are reduced in the presence of the dithiol complexing agent sodium arsenite to stabilize vicinal dithiols and prevent intermolecular disulfide formation. The Fab′ fragments generated are then converted to thionitrobenzoate (TNB) derivatives. One of the Fab′-TNB derivatives is then reconverted to the Fab′-thiol by reduction with mercaptoethylamine and is mixed with an equimolar amount of the other Fab′-TNB derivative to form the bispecific antibody. The bispecific antibodies produced can be used as agents for the selective immobilization of enzymes.  
       [0319] Additionally, Fab′ fragments can be directly recovered from  E. coli  and chemically coupled to form bispecific antibodies. Shalaby et al., J. Exp. Med. 175, 217-225 (1992) describe the production of a fully humanized bispecific antibody F(ab′) 2  molecule. Each Fab′ fragment was separately secreted from  E. coli  and subjected to directed chemical coupling in vitro to form the bispecific antibody. The bispecific antibody thus formed was able to bind to cells overexpressing the ErbB2 receptor and normal human T cells, as well as trigger the lytic activity of human cytotoxic lymphocytes against human breast tumor targets.  
       [0320] Various techniques for making and isolating bispecific antibody fragments directly from recombinant cell culture have also been described. For example, bispecific antibodies have been produced using leucine zippers. Kostelny et al., J. Immunol. 148(5), 1547-1553 (1992). The leucine zipper peptides from the Fos and Jun proteins were linked to the Fab′ portions of two different antibodies by gene fusion. The antibody homodimers were reduced at the hinge region to form monomers and then re-oxidized to form the antibody heterodimers. This method can also be utilized for the production of antibody homodimers. The “diabody” technology described by Hollinger et al., Proc. Natl. Acad. Sci. USA 90, 6444-6448 (1993) has provided an alternative mechanism for making bispecific antibody fragments. The fragments comprise a heavy-chain variable domain (V H ) connected to a light-chain variable domain (V L ) by a linker which is too short to allow pairing between the two domains on the same chain. Accordingly, the V H  and V L  domains of one fragment are forced to pair with the complementary V L  and V H  domains of another fragment, thereby forming two antigen-binding sites. Another strategy for making bispecific antibody fragments by the use of single-chain Fv (sFv) dimers has also been reported. See, Gruber et al., J. Immunol. 152, 5368 (1994).  
       [0321] Antibodies with more than two valencies are contemplated. For example, trispecific antibodies can be prepared. Tutt et al., J. Immunol. 147, 60 (1991).  
       [0322] Exemplary bispecific antibodies can bind to two different epitopes, at least one of which originates in the protein antigen of the invention. Alternatively, an anti-antigenic arm of an immunoglobulin molecule can be combined with an arm which binds to a triggering molecule on a leukocyte such as a T-cell receptor molecule (e.g. CD2, CD3, CD28, or B7), or Fc receptors for IgG (FcγR), such as FcγRI (CD64), FcγRII (CD32) and FcγRIII (CD 16) so as to focus cellular defense mechanisms to the cell expressing the particular antigen. Bispecific antibodies can also be used to direct cytotoxic agents to cells which express a particular antigen. These antibodies possess an antigen-binding arm and an arm which binds a cytotoxic agent or a radionuclide chelator, such as EOTUBE, DPTA, DOTA, or TETA. Another bispecific antibody of interest binds the protein antigen described herein and further binds tissue factor (TF).  
       Heteroconjugate Antibodies  
       [0323] Heteroconjugate antibodies are also within the scope of the present invention. Heteroconjugate antibodies are composed of two covalently joined antibodies. Such antibodies have, for example, been proposed to target immune system cells to unwanted cells (U.S. Pat. No. 4,676,980), and for treatment of HIV infection (WO 91/00360; WO 92/200373; EP 03089). It is contemplated that the antibodies can be prepared in vitro using known methods in synthetic protein chemistry, including those involving crosslinking agents. For example, immunotoxins can be constructed using a disulfide exchange reaction or by forming a thioether bond. Examples of suitable reagents for this purpose include iminothiolate and methyl-4-mercaptobutyrimidate and those disclosed, for example, in U.S. Pat. No. 4,676,980.  
       Effector Function Engineering  
       [0324] It can be desirable to modify the antibody of the invention with respect to effector function, so as to enhance, e.g., the effectiveness of the antibody in treating cancer. For example, cysteine residue(s) can be introduced into the Fc region, thereby allowing interchain disulfide bond formation in this region. The homodimeric antibody thus generated can have improved internalization capability and/or increased complement-mediated cell killing and antibody-dependent cellular cytotoxicity (ADCC). See Caron et al., J. Exp Med., 176, 1191-1195 (1992) and Shopes, J. Immunol., 148, 2918-2922 (1992). Homodimeric antibodies with enhanced anti-tumor activity can also be prepared using heterobifunctional cross-linkers as described in Wolff et al. Cancer Research, 53, 2560-2565 (1993). Alternatively, an antibody can be engineered that has dual Fc regions and can thereby have enhanced complement lysis and ADCC capabilities. See Stevenson et al., Anti-Cancer Drug Design, 3, 219-230 (1989).  
       Immunoconjugates  
       [0325] The invention also pertains to immunoconjugates comprising an antibody conjugated to a cytotoxic agent such as a chemotherapeutic agent, toxin (e.g., an enzymatically active toxin of bacterial, fungal, plant, or animal origin, or fragments thereof), or a radioactive isotope (i.e., a radioconjugate).  
       [0326] Chemotherapeutic agents useful in the generation of such immunoconjugates have been described above. Enzymatically active toxins and fragments thereof that can be used include diphtheria A chain, nonbinding active fragments of diphtheria toxin, exotoxin A chain (from Pseudomonas aeruginosa), ricin A chain, abrin A chain, modeccin A chain, alpha-sarcin, Aleurites fordii proteins, dianthin proteins, Phytolaca americana proteins (PAPI, PAPII, and PAP-S), momordica charantia inhibitor, curcin, crotin, sapaonaria officinalis inhibitor, gelonin, mitogellin, restrictocin, phenomycin, enomycin, and the tricothecenes. A variety of radionuclides are available for the production of radioconjugated antibodies. Examples include  212 Bi,  131 I,  131 In,  90 Y, and  186 Re.  
       [0327] Conjugates of the antibody and cytotoxic agent are made using a variety of bifunctional protein-coupling agents such as N-succinimidyl-3-(2-pyridyldithiol) propionate (SPDP), imninothiolane (IT), bifunctional derivatives of imidoesters (such as dimethyl adipimidate HCL), active esters (such as disuccinimidyl suberate), aldehydes (such as glutareldehyde), bis-azido compounds (such as bis (p-azidobenzoyl) hexanediamine), bis-diazonium derivatives (such as bis-(p-diazoniumbenzoyl)-ethylenediamine), diisocyanates (such as tolyene 2,6-dilsocyanate), and bis-active fluorine compounds (such as 1,5-difluoro-2,4-dinitrobenzene). For example, a ricin immunotoxin can be prepared as described in Vitetta et al., Science, 238: 1098 (1987). Carbon-14-labeled 1-isothiocyanatobenzyl-3-methyldiethylene triaminepentaacetic acid (MX-DTPA) is an exemplary chelating agent for conjugation of radionucleotide to the antibody. See WO94/11026.  
       [0328] In another embodiment, the antibody can be conjugated to a “receptor” (such streptavidin) for utilization in tumor pretargeting wherein the antibody-receptor conjugate is administered to the patient, followed by removal of unbound conjugate from the circulation using a clearing agent and then administration of a “ligand” (e.g., avidin) that is in turn conjugated to a cytotoxic agent.  
       Computer Readable Sequences  
       [0329] In one application of this embodiment, a nucleotide sequence of the present invention can be recorded on computer readable media. As used herein, “computer readable media” refers to any medium which can be read and accessed directly by a computer. Such media include, but are not limited to: magnetic storage media, such as floppy discs, hard disc storage medium, and magnetic tape; optical storage media such as CD-ROM; electrical storage media such as RAM and ROM; and hybrids of these categories such as magnetic/optical storage media. A skilled artisan can readily appreciate how any of the presently known computer readable mediums can be used to create a manufacture comprising computer readable medium having recorded thereon a nucleotide sequence of the present invention. As used herein, “recorded” refers to a process for storing information on computer readable medium. A skilled artisan can readily adopt any of the presently known methods for recording information on computer readable medium to generate manufactures comprising the nucleotide sequence information of the present invention.  
       [0330] A variety of data storage structures are available to a skilled artisan for creating a computer readable medium having recorded thereon a nucleotide sequence of the present invention. The choice of the data storage structure will generally be based on the means chosen to access the stored information. In addition, a variety of data processor programs and formats can be used to store the nucleotide sequence information of the present invention on computer readable medium. The sequence information can be represented in a word processing text file, formatted in commercially-available software such as WordPerfect and Microsoft Word, or represented in the form of an ASCII file, stored in a database application, such as DB2, Sybase, Oracle, or the like. A skilled artisan can readily adapt any number of data processor structuring formats (e.g. text file or database) in order to obtain computer readable medium having recorded thereon the nucleotide sequence information of the present invention.  
       [0331] By providing any of the nucleotide sequences SEQ ID NO: 1-337, or 675-836 or a representative fragment thereof; or a nucleotide sequence at least 95% identical to any of the nucleotide sequences of SEQ ID NO: 1-337, or 675-836 in computer readable form, a skilled artisan can routinely access the sequence information for a variety of purposes. Computer software is publicly available which allows a skilled artisan to access sequence information provided in a computer readable medium. The examples which follow demonstrate how software which implements the BLAST (Altschul et al., J. Mol. Biol. 215:403-410 (1990)) and BLAZE (Brutlag et al., Comp. Chem. 17:203-207 (1993)) search algorithms on a Sybase system is used to identify open reading frames (ORFs) within a nucleic acid sequence. Such ORFs may be protein-encoding fragments and may be useful in producing commercially important proteins such as enzymes used in fermentation reactions and in the production of commercially useful metabolites.  
       [0332] As used herein, “a computer-based system” refers to the hardware means, software means, and data storage means used to analyze the nucleotide sequence information of the present invention. The minimum hardware means of the computer-based systems of the present invention comprises a central processing unit (CPU), input means, output means, and data storage means. A skilled artisan can readily appreciate that any one of the currently available computer-based systems are suitable for use in the present invention. As stated above, the computer-based systems of the present invention comprise a data storage means having stored therein a nucleotide sequence of the present invention and the necessary hardware means and software means for supporting and implementing a search means. As used herein, “data storage means” refers to memory which can store nucleotide sequence information of the present invention, or a memory access means which can access manufactures having recorded thereon the nucleotide sequence information of the present invention.  
       [0333] As used herein, “search means” refers to one or more programs which are implemented on the computer-based system to compare a target sequence or target structural motif with the sequence information stored within the data storage means. Search means are used to identify fragments or regions of a known sequence which match a particular target sequence or target motif. A variety of known algorithms are disclosed publicly and a variety of commercially available software for conducting search means are and can be used in the computer-based systems of the present invention. Examples of such software includes, but is not limited to, Smith-Waterman, MacPattern (EMBL), BLASTN and BLASTA (NPOLYPEPTIDEIA). A skilled artisan can readily recognize that any one of the available algorithms or implementing software packages for conducting homology searches can be adapted for use in the present computer-based systems. As used herein, a “target sequence” can be any nucleic acid or amino acid sequence of six or more nucleotides or two or more amino acids. A skilled artisan can readily recognize that the longer a target sequence is, the less likely a target sequence will be present as a random occurrence in the database. The most preferred sequence length of a target sequence is from about 10 to 300 amino acids, more preferably from about 30 to 100 nucleotide residues. However, it is well recognized that searches for commercially important fragments, such as sequence fragments involved in gene expression and protein processing, may be of shorter length.  
       [0334] As used herein, “a target structural motif,” or “target motif,” refers to any rationally selected sequence or combination of sequences in which the sequence(s) are chosen based on a three-dimensional configuration which is formed upon the folding of the target motif. There are a variety of target motifs known in the art. Protein target motifs include, but are not limited to, enzyme active sites and signal sequences. Nucleic acid target motifs include, but are not limited to, promoter sequences, hairpin structures and inducible expression elements (protein binding sequences).  
       Triple Helix Formation  
       [0335] In addition, the fragments of the present invention, as broadly described, can be used to control gene expression through triple helix formation or antisense DNA or RNA, both of which methods are based on the binding of a polynucleotide sequence to DNA or RNA. Polynucleotides suitable for use in these methods are preferably 20 to 40 bases in length and are designed to be complementary to a region of the gene involved in transcription (triple helix-see Lee et al., Nucl. Acids Res. 6, 3073 (1979); Cooney et al., Science 15241, 456 (1988); and Dervan et al., Science 251, 1360 (1991)) or to the mRNA itself (antisense-Olmno, J. Neurochem. 56:560 (1991); Oligodeoxynucleotides as Antisense Inhibitors of Gene Expression, CRC Press, Boca Raton, Fla. (1988)). Triple helix-formation optimally results in a shut-off of RNA transcription from DNA, while antisense RNA hybridization blocks translation of an mRNA molecule into polypeptide. Both techniques have been demonstrated to be effective in model systems. Information contained in the sequences of the present invention is necessary for the design of an antisense or triple helix oligonucleotide.  
       Diagnostic Assays and Kits  
       [0336] The present invention further provides methods to identify the presence or expression of one of the ORFs of the present invention, or homolog thereof, in a test sample, using a nucleic acid probe or antibodies of the present invention, optionally conjugated or otherwise associated with a suitable label.  
       [0337] In general, methods for detecting a polynucleotide of the invention can comprise contacting a sample with a compound that binds to and forms a complex with the polynucleotide for a period sufficient to form the complex, and detecting the complex, so that if a complex is detected, a polynucleotide of the invention is detected in the sample. Such methods can also comprise contacting a sample under stringent hybridization conditions with nucleic acid primers that anneal to a polynucleotide of the invention under such conditions, and amplifying annealed polynucleotides, so that if a polynucleotide is amplified, a polynucleotide of the invention is detected in the sample.  
       [0338] In general, methods for detecting a polypeptide of the invention can comprise contacting a sample with a compound that binds to and forms a complex with the polypeptide for a period sufficient to form the complex, and detecting the complex, so that if a complex is detected, a polypeptide of the invention is detected in the sample.  
       [0339] In detail, such methods comprise incubating a test sample with one or more of the antibodies or one or more of the nucleic acid probes of the present invention and assaying for binding of the nucleic acid probes or antibodies to components within the test sample.  
       [0340] Conditions for incubating a nucleic acid probe or antibody with a test sample vary. Incubation conditions depend on the format employed in the assay, the detection methods employed, and the type and nature of the nucleic acid probe or antibody used in the assay. One skilled in the art will recognize that any one of the commonly available hybridization, amplification or immunological assay formats can readily be adapted to employ the nucleic acid probes or antibodies of the present invention. Examples of such assays can be found in Chard, T., An Introduction to Radioimmunoassay and Related Techniques, Elsevier Science Publishers, Amsterdam, The Netherlands (1986); Bullock, G. R. et al., Techniques in Immunocytochemistry, Academic Press, Orlando, Fla. Vol. 1 (1982), Vol. 2 (1983), Vol. 3 (1985); Tijssen, P., Practice and Theory of immunoassays: Laboratory Techniques in Biochemistry and Molecular Biology, Elsevier Science Publishers, Amsterdam, The Netherlands (1985). The test samples of the present invention include cells, protein or membrane extracts of cells, or biological fluids such as sputum, blood, seilm, plasma, or urine. The test sample used in the above-described method will vary based on the assay format, nature of the detection method and the tissues, cells or extracts used as the sample to be assayed. Methods for preparing protein extracts or membrane extracts of cells are well known in the art and can be readily be adapted in order to obtain a sample which is compatible with the system utilized.  
       [0341] In another embodiment of the present invention, kits are provided which contain the necessary reagents to carry out the assays of the present invention. Specifically, the invention provides a compartment kit to receive, in close confinement, one or more containers which comprises: (a) a first container comprising one of the probes or antibodies of the present invention; and (b) one or more other containers comprising one or more of the following: wash reagents, reagents capable of detecting presence of a bound probe or antibody.  
       [0342] In detail, a compartment kit includes any kit in which reagents are contained in separate containers. Such containers include small glass containers, plastic containers or strips of plastic or paper. Such containers allows one to efficiently transfer reagents from one compartment to another compartment such that the samples and reagents are not cross-contaminated, and the agents or solutions of each container can be added in a quantitative fashion from one compartment to another. Such containers will include a container which will accept the test sample, a container which contains the antibodies used in the assay, containers which contain wash reagents (such as phosphate buffered saline, Tris-buffers, etc.), and containers which contain the reagents used to detect the bound antibody or probe. Types of detection reagents include labeled nucleic acid probes, labeled secondary antibodies, or in the alternative, if the primary antibody is labeled, the enzymatic, or antibody binding reagents which are capable of reacting with the labeled antibody. One skilled in the art will readily recognize that the disclosed probes and antibodies of the present invention can be readily incorporated into one of the established kit formats which are well known in the art.  
       Medical Imaging  
       [0343] The novel polypeptides and binding partners of the invention are useful in medical imaging of sites expressing the molecules of the invention (e.g., where the polypeptide of the invention is involved in the immune response, for imaging sites of inflammation or infection). See, e.g., Kunkel et al., U.S. Pat. No. 5,413,778. Such methods involve chemical attachment of a labeling or imaging agent, administration of the labeled polypeptide to a subject in a pharmaceutically acceptable carrier, and imaging the labeled polypeptide in vivo at the target site.  
       Screening Assays  
       [0344] Using the isolated proteins and polynucleotides of the invention, the present invention further provides methods of obtaining and identifying agents which bind to a polypeptide encoded by an ORF corresponding to any of the nucleotide sequences set forth in SEQ ID NO: 1-337, or 675-836, or bind to a specific domain of the polypeptide encoded by the nucleic acid. In detail, said method comprises the steps of:  
       [0345] (a) contacting an agent with an isolated protein encoded by an ORF of the present invention, or nucleic acid of the invention; and  
       [0346] (b) determining whether the agent binds to said protein or said nucleic acid.  
       [0347] In general, therefore, such methods for identifying compounds that bind to a polynucleotide of the invention can comprise contacting a compound with a polynucleotide of the invention for a time sufficient to form a polynucleotide/compound complex, and detecting the complex, so that if a polynucleotide/compound complex is detected, a compound that binds to a polynucleotide of the invention is identified.  
       [0348] Likewise, in general, therefore, such methods for identifying compounds that bind to a polypeptide of the invention can comprise contacting a compound with a polypeptide of the invention for a time sufficient to form a polypeptide/compound complex, and detecting the complex, so that if a polypeptide/compound complex is detected, a compound that binds to a polynucleotide of the invention is identified.  
       [0349] Methods for identifying compounds that bind to a polypeptide of the invention can also comprise contacting a compound with a polypeptide of the invention in a cell for a time sufficient to form a polypeptide/compound complex, wherein the complex drives expression of a receptor gene sequence in the cell, and detecting the complex by detecting reporter gene sequence expression, so that if a polypeptide/compound complex is detected, a compound that binds a polypeptide of the invention is identified.  
       [0350] Compounds identified via such methods can include compounds which modulate the activity of a polypeptide of the invention (that is, increase or decrease its activity, relative to activity observed in the absence of the compound). Alternatively, compounds identified via such methods can include compounds which modulate the expression of a polynucleotide of the invention (that is, increase or decrease expression relative to expression levels observed in the absence of the compound). Compounds, such as compounds identified via the methods of the invention, can be tested using standard assays well known to those of skill in the art for their ability to modulate activity/expression.  
       [0351] The agents screened in the above assay can be, but are not limited to, peptides, carbohydrates, vitamin derivatives, or other pharmaceutical agents. The agents can be selected and screened at random or rationally selected or designed using protein modeling techniques.  
       [0352] For random screening, agents such as peptides, carbohydrates, pharmaceutical agents and the like are selected at random and are assayed for their ability to bind to the protein encoded by the ORF of the present invention. Alternatively, agents may be rationally selected or designed. As used herein, an agent is said to be “rationally selected or designed” when the agent is chosen based on the configuration of the particular protein. For example, one skilled in the art can readily adapt currently available procedures to generate peptides, pharmaceutical agents and the like, capable of binding to a specific peptide sequence, in order to generate rationally designed antipeptide peptides, for example see Hurby et al., Application of Synthetic Peptides: Antisense Peptides,“In Synthetic Peptides, A User&#39;s Guide, W. H. Freeman, N.Y. (1992), pp. 289-307, and Kaspczak et al., Biochemistry 28:9230-8 (1989), or pharmaceutical agents, or the like.  
       [0353] In addition to the foregoing, one class of agents of the present invention, as broadly described, can be used to control gene expression through binding to one of the ORFs or EMFs of the present invention. As described above, such agents can be randomly screened or rationally designed/selected. Targeting the ORF or EMF allows a skilled artisan to design sequence specific or element specific agents, modulating the expression of either a single ORF or multiple ORFs which rely on the same EMF for expression control. One class of DNA binding agents are agents which contain base residues which hybridize or form a triple helix formation by binding to DNA or RNA. Such agents can be based on the classic phosphodiester, ribonucleic acid backbone, or can be a variety of sulfhydryl or polymeric derivatives which have base attachment capacity.  
       [0354] Agents suitable for use in these methods preferably contain 20 to 40 bases and are designed to be complementary to a region of the gene involved in transcription (triple helix—see Lee et al., Nucl. Acids Res. 6, 3073 (1979); Cooney et al., Science 241, 456 (1988); and Dervan et al., Science 251, 1360 (1991)) or to the mRNA itself (antisense-Okano, J. Neurochem. 56, 560 (1991); Oligodeoxynucleotides as Antisense Inhibitors of Gene Expression, CRC Press, Boca Raton, Fla. (1988)). Triple helix-formation optimally results in a shut-off of RNA transcription from DNA, while antisense RNA hybridization blocks translation of an mRNA molecule into polypeptide. Both techniques have been demonstrated to be effective in model systems. Information contained in the sequences of the present invention is necessary for the design of an antisense or triple helix oligonucleotide and other DNA binding agents.  
       [0355] Agents which bind to a protein encoded by one of the ORFs of the present invention can be used as a diagnostic agent. Agents which bind to a protein encoded by one of the ORFs of the present invention can be formulated using known techniques to generate a pharmaceutical composition.  
       Use of Nucleic Acids as Probes  
       [0356] Another aspect of the subject invention is to provide for polypeptide-specific nucleic acid hybridization probes capable of hybridizing with naturally occurring nucleotide sequences. The hybridization probes of the subject invention may be derived from any of the nucleotide sequences SEQ ID NO: 1-337, or 675-836. Because the corresponding gene is only expressed in a limited number of tissues, a hybridization probe derived from any of the nucleotide sequences SEQ ID NO: 1-337, or 675-836 can be used as an indicator of the presence of RNA of cell type of such a tissue in a sample.  
       [0357] Any suitable hybridization technique can be employed, such as, for example, in situ hybridization. PCR as described in U.S. Pat. Nos. 4,683,195 and 4,965,188 provides additional uses for oligonucleotides based upon the nucleotide sequences. Such probes used in PCR may be of recombinant origin, may be chemically synthesized, or a mixture of both. The probe will comprise a discrete nucleotide sequence for the detection of identical sequences or a degenerate pool of possible sequences for identification of closely related genomic sequences.  
       [0358] Other means for producing specific hybridization probes for nucleic acids include the cloning of nucleic acid sequences into vectors for the production of mRNA probes. Such vectors are known in the art and are commercially available and may be used to synthesize RNA probes in vitro by means of the addition of the appropriate RNA polymerase as T7 or SP6 RNA polymerase and the appropriate radioactively labeled nucleotides. The nucleotide sequences may be used to construct hybridization probes for mapping their respective genomic sequences. The nucleotide sequence provided herein may be mapped to a chromosome or specific regions of a chromosome using well-known genetic and/or chromosomal mapping techniques. These techniques include in situ hybridization, linkage analysis against known chromosomal markers, hybridization screening with libraries or flow-sorted chromosomal preparations specific to known chromosomes, and the like. The technique of fluorescent in situ hybridization of chromosome spreads has been described, among other places, in Verma et al (1988) Human Chromosomes: A Manual of Basic Techniques, Pergamon Press, New York N.Y.  
       [0359] Fluorescent in situ hybridization of chromosomal preparations and other physical chromosome mapping techniques may be correlated with additional genetic map data. Examples of genetic map data can be found in the 1994 Genome Issue of Science (265:1981f). Correlation between the location of a nucleic acid on a physical chromosomal map and a specific disease (or predisposition to a specific disease) may help delimit the region of DNA associated with that genetic disease. The nucleotide sequences of the subject invention may be used to detect differences in gene sequences between normal, carrier or affected individuals.  
       Preparation of Support Bound Oligonucleotides  
       [0360] Oligonucleotides, i.e., small nucleic acid segments, may be readily prepared by, for example, directly synthesizing the oligonucleotide by chemical means, as is commonly practiced using an automated oligonucleotide synthesizer.  
       [0361] Support bound oligonucleotides may be prepared by any of the methods known to those of skill in the art using any suitable support such as glass, polystyrene or Teflon. One strategy is to precisely spot oligonucleotides synthesized by standard synthesizers. Immobilization can be achieved using passive adsorption (Inouye &amp; Hondo, (1990) J. Clin. Microbiol. 28(6), 1469-72); using UV light (Nagata et al., 1985; Dahlen et al., 1987; Morrissey &amp; Collins, (1989) Mol. Cell Probes 3(2) 189-207) or by covalent binding of base modified DNA (Keller et al., 1988; 1989); all references being specifically incorporated herein.  
       [0362] Another strategy that may be employed is the use of the strong biotin-streptavidin interaction as a linker. For example, Broude et al. (1994) Proc. Natl. Acad. Sci. USA 91(8), 3072-6, describe the use of biotinylated probes, although these are duplex probes, that are immobilized on streptavidin-coated magnetic beads. Streptavidin-coated beads may be purchased from Dynal, Oslo. Of course, this same linking chemistry is applicable to coating any surface with streptavidin. Biotinylated probes may be purchased from various sources, such as, e.g., Operon Technologies (Alameda, Calif.).  
       [0363] Nunc Laboratories (Naperville, Ill.) is also selling suitable material that could be used. Nunc Laboratories have developed a method by which DNA can be covalently bound to the microwell surface termed Covalink NH. Covalink NH is a polystyrene surface grafted with secondary amino groups (&gt;NH) that serve as bridgeheads for further covalent coupling. CovaLink Modules may be purchased from Nunc Laboratories. DNA molecules may be bound to CovaLink exclusively at the 5′-end by a phosphoramidate bond, allowing immobilization of more than 1 pmol of DNA (Rasmussen et al., (1991) Anal. Biochem. 198(1) 138-42).  
       [0364] The use of CovaLink NH strips for covalent binding of DNA molecules at the 5′-end has been described (Rasmussen et al., (1991). In this technology, a phosphoramidate bond is employed (Chu et al., (1983) Nucleic Acids Res. 11(8) 6513-29). This is beneficial as immobilization using only a single covalent bond is preferred. The phosphoramidate bond joins the DNA to the CovaLink NH secondary amino groups that are positioned at the end of spacer arms covalently grafted onto the polystyrene surface through a 2 nm long spacer arm. To link an oligonucleotide to CovaLink NH via an phosphorarnidate bond, the oligonucleotide terminus must have a 5′-end phosphate group. It is, perhaps, even possible for biotin to be covalently bound to CovaLink and then streptavidin used to bind the probes.  
       [0365] More specifically, the linkage method includes dissolving DNA in water (7.5 ng/μl) and denaturing for 10 min. at 95° C. and cooling on ice for 10 min. Ice-cold 0.1 M 1-methylimidazole, pH 7.0 (1-MeIm 7 ), is then added to a final concentration of 10 mM 1-MeIm 7 . A ss DNA solution is then dispensed into CovaLink NH strips (75 μl/well) standing on ice.  
       [0366] Carbodiumide 0.2 M 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide (EDC), dissolved in 10 mM I-Me 1 m 7 , is made fresh and 25 μl added per well. The strips are incubated for 5 hours at 50° C. After incubation the strips are washed using, e.g., Nunc-Inuuno Wash; first the wells are washed 3 times, then they are soaked with washing solution for 5 min., and finally they are washed 3 times (where in the washing solution is 0.4 N NaOH, 0.25% SDS heated to 50° C.).  
       [0367] It is contemplated that a further suitable method for use with the present invention is that described in PCT Patent Application WO 90/03382 (Southern &amp; Maskos), incorporated herein by reference. This method of preparing an oligonucleotide bound to a support involves attaching a nucleoside 3′-reagent through the phosphate group by a covalent phosphodiester link to aliphatic hydroxyl groups carried by the support. The oligonucleotide is then synthesized on the supported nucleoside and protecting groups removed from the synthetic oligonucleotide chain under standard conditions that do not cleave the oligonucleotide from the support. Suitable reagents include nucleoside phosphoramidite and nucleoside hydrogen phosphorate.  
       [0368] An on-chip strategy for the preparation of DNA probe for the preparation of DNA probe arrays may be employed. For example, addressable laser-activated photodeprotection may be employed in the chemical synthesis of oligonucleotides directly on a glass surface, as described by Fodor et al. (1991) Science 251(4995), 767-73, incorporated herein by reference. Probes may also be immobilized on nylon supports as described by Van Ness et al. (1991) Nucleic Acids Res., 19(12) 3345-50; or linked to Teflon using the method of Duncan &amp; Cavalier (1988) Anal. Biochem. 169(1), 104-8; all references being specifically incorporated herein.  
       [0369] To link an oligonucleotide to a nylon support, as described by Van Ness et al. (1991), requires activation of the nylon surface via alkylation and selective activation of the 5′-amine of oligonucleotides with cyanuric chloride.  
       [0370] One particular way to prepare support bound oligonucleotides is to utilize the light-generated synthesis described by Pease et al., (1994) Proc. Natl. Acad. Sci., USA 91(11), 5022-6, incorporated herein by reference). These authors used current photolithographic techniques to generate arrays of immobilized oligonucleotide probes (DNA chips). These methods, in which light is used to direct the synthesis of oligonucleotide probes in high-density, miniaturized arrays, utilize photolabile 5′-protected N-acyl-deoxynucleoside phosphoramidites, surface linker chemistry and versatile combinatorial synthesis strategies. A matrix of 256 spatially defined oligonucleotide probes may be generated in this manner.  
       Preparation of Nucleic Acid Fragments  
       [0371] The nucleic acids may be obtained from any appropriate source, such as cDNAs, genomic DNA, chromosomal DNA, microdissected chromosome bands, cosmid or YAC inserts, and RNA, including mRNA without any amplification steps. For example, Sambrook et al. (1989) describes three protocols for the isolation of high molecular weight DNA from mammalian cells (p. 9.14-9.23).  
       [0372] DNA fragments may be prepared as clones in M13, plasmid or lambda vectors and/or prepared directly from genomic DNA or cDNA by PCR or other amplification methods. Samples may be prepared or dispensed in multiwell plates. About 100-1000 ng of DNA samples may be prepared in 2-500 ml of final volume.  
       [0373] The nucleic acids would then be fragmented by any of the methods known to those of skill in the art including, for example, using restriction enzymes as described at 9.24-9.28 of Sambrook et al. (1989), shearing by ultrasound and NaOH treatment.  
       [0374] Low pressure shearing is also appropriate, as described by Schriefer et al. (1990) Nucleic Acids Res. 18(24), 7455-6, incorporated herein by reference). In this method, DNA samples are passed through a small French pressure cell at a variety of low to intermediate pressures. A lever device allows controlled application of low to intermediate pressures to the cell. The results of these studies indicate that low-pressure shearing is a useful alternative to sonic and enzymatic DNA fragmentation methods.  
       [0375] One particularly suitable way for fragmenting DNA is contemplated to be that using the two base recognition endonuclease, CviJI, described by Fitzgerald et al. (1992) Nucleic Acids Res. 20(14) 3753-62. These authors described an approach for the rapid fragmentation and fractionation of DNA into particular sizes that they contemplated to be suitable for shotgun cloning and sequencing.  
       [0376] The restriction endonuclease CviJI normally cleaves the recognition sequence PuGCPy between the G and C to leave blunt ends. Atypical reaction conditions, which alter the specificity of this enzyme (CviJI**), yield a quasi-random distribution of DNA fragments form the small molecule pUC19 (2688 base pairs). Fitzgerald et al. (1992) quantitatively evaluated the randomness of this fragmentation strategy, using a CviJI** digest of pUC19 that was size fractionated by a rapid gel filtration method and directly ligated, without end repair, to a lac Z minus M13 cloning vector. Sequence analysis of 76 clones showed that CviJI** restricts pyGCPy and PuGCPu, in addition to PuGCPy sites, and that new sequence data is accumulated at a rate consistent with random fragmentation.  
       [0377] As reported in the literature, advantages of this approach compared to sonication and agarose gel fractionation include: smaller amounts of DNA are required (0.2-0.5 μg instead of 2-5 μg); and fewer steps are involved (no preligation, end repair, chemical extraction, or agarose gel electrophoresis and elution are needed).  
       [0378] Irrespective of the manner in which the nucleic acid fragments are obtained or prepared, it is important to denature the DNA to give single stranded pieces available for hybridization. This is achieved by incubating the DNA solution for 2-5 minutes at 80-90° C. The solution is then cooled quickly to 2° C. to prevent renaturation of the DNA fragments before they are contacted with the chip. Phosphate groups must also be removed from genomic DNA by methods known in the art.  
       Preparation of DNA Arrays  
       [0379] Arrays may be prepared by spotting DNA samples on a support such as a nylon membrane. Spotting may be performed by using arrays of metal pins (the positions of which correspond to an array of wells in a microtiter plate) to repeated by transfer of about 20 nl of a DNA solution to a nylon membrane. By offset printing, a density of dots higher than the density of the wells is achieved. One to 25 dots may be accommodated in 1 mm 2 , depending on the type of label used. By avoiding spotting in some preselected number of rows and columns, separate subsets (subarrays) may be formed. Samples in one subarray may be the same genomic segment of DNA (or the same gene) from different individuals, or may be different, overlapped genomic clones. Each of the subarrays may represent replica spotting of the same samples. In one example, a selected gene segment may be amplified from 64 patients. For each patient, the amplified gene segment may be in one 96-well plate (all 96 wells containing the same sample). A plate for each of the 64 patients is prepared. By using a 96-pin device, all samples may be spotted on one 8×12 cm membrane. Subarrays may contain 64 samples, one from each patient. Where the 96 subarrays are identical, the dot span may be 1 mm 2  and there may be a 1 mm space between subarrays.  
       [0380] Another approach is to use membranes or plates (available from NUNC, Naperville, Ill.) which may be partitioned by physical spacers e.g. a plastic grid molded over the membrane, the grid being similar to the sort of membrane applied to the bottom of multiwell plates, or hydrophobic strips. A fixed physical spacer is not preferred for imaging by exposure to flat phosphor-storage screens or x-ray films.  
       [0381] The present invention is illustrated in the following examples. Upon consideration of the present disclosure, one of skill in the art will appreciate that many other embodiments and variations may be made in the scope of the present invention. Accordingly, it is intended that the broader aspects of the present invention not be limited to the disclosure of the following examples. The present invention is not to be limited in scope by the exemplified embodiments which are intended as illustrations of single aspects of the invention, and compositions and methods which are functionally equivalent are within the scope of the invention. Indeed, numerous modifications and variations in the practice of the invention are expected to occur to those skilled in the art upon consideration of the present preferred embodiments. Consequently, the only limitations which should be placed upon the scope of the invention are those which appear in the appended claims.  
       [0382] All references cited within the body of the instant specification are hereby incorporated by reference in their entirety. 
     
    
    
     EXAMPLES  
     Example 1  
     [0383] Novel Nucleic Acid Sequences Obtained from Various Libraries  
     [0384] A plurality of novel nucleic acids were obtained from cDNA libraries prepared from various human tissues and in some cases isolated from a genomic library derived from human chromosome using standard PCR, SBH sequence signature analysis and Sanger sequencing techniques. The inserts of the library were amplified with PCR using primers specific for the vector sequences which flank the inserts. Clones from cDNA libraries were spotted on nylon membrane filters and screened with oligonucleotide probes (e.g., 7-mers) to obtain signature sequences. The clones were clustered into groups of similar or identical sequences. Representative clones were selected for sequencing.  
     [0385] In some cases, the 5′ sequence of the amplified inserts was then deduced using a typical Sanger sequencing protocol. PCR products were purified and subjected to fluorescent dye terminator cycle sequencing. Single pass gel sequencing was done using a 377 Applied Biosystems (ABI) sequencer to obtain the novel nucleic acid sequences.  
     Example 2  
     [0386] Assemblage of Novel Nucleic Acids  
     [0387] The contigs or nucleic acids of the present invention, designated as SEQ ID NO: 675-836 were assembled using an EST sequence as a seed. Then a recursive algorithm was used to extend the seed EST into an extended assemblage, by pulling additional sequences from different databases (i.e., Hyseq&#39;s database containing EST sequences, dbEST, gb pri, and UniGene, and exons from public domain genomic sequences predicated by GenScan) that belong to this assemblage. The algorithm terminated when there were no additional sequences from the above databases that would extend the assemblage. Further, inclusion of component sequences into the assemblage was based on a BLASTN hit to the extending assemblage with BLAST score greater than 300 and percent identity greater than 95%.  
     [0388] Table 8 sets forth the novel predicted polypeptides (including proteins) encoded by the novel polynucleotides (SEQ ID NO: 675-836) of the present invention, and their corresponding translation start and stop nucleotide locations to each of SEQ ID NO: 675-836. Table 8 also indicates the method by which the polypeptide was predicted. Method A refers to a polypeptide obtained by using a software program called FASTY (available from http://fasta.bioch.virginia,edu) which selects a polypeptide based on a comparison of the translated novel polynucleotide to known polynucleotides (W. R. Pearson, Methods in Enzymology, 183:63-98 (1990), herein incorporated by reference). Method B refers to a polypeptide obtained by using a software program called GenScan for human/vertebrate sequences (available from Stanford University, Office of Technology Licensing) that predicts the polypeptide based on a probabilistic model of gene structure/compositional properties (C. Burge and S. Karlin, J. Mol. Biol., 268:78-94 (1997), incorporated herein by reference). Method C refers to a polypeptide obtained by using a Hyseq proprietary software program that translates the novel polynucleotide and its complementary strand into six possible amino acid sequences (forward and reverse frames) and chooses the polypeptide with the longest open reading frame.  
     Example 3  
     [0389] Novel Nucleic Acids  
     [0390] The novel nucleic acids of the present invention SEQ ID NO: 1-337 were assembled from Hyseq&#39;s proprietary EST sequences as described in Example 1 and human genome sequences that are available from the public databases (http://www.ncbi.nlm.nih.gov/). Exons were predicted from human genome sequences using GenScan (http://genes.mit.edu/GENSCANinfo.html); HMMgene (http://www.cbs.dtu.dk/services/HMMgene/hmmgene1 1.html); and GenMark.hmm (http://genemark.biology.gatech.edu/GeneMark/whmm info.html). The Hyseq proprietary EST sequences and the predicted exons were assembled based on a BLASTN hit to the extending assemblage with BLAST score greater than 300 and percent identity greater than 95%. Then, the predicted genes were analyzed using Neural Network SignalP V1.1 program (from Center for Biological Sequence Analysis, The Technical University of Denmark) for presence of a signal peptide. These sequences were further analyzed for presence of transmembrane region(s) using the TMpred prograrn (http://www.ch.embnet.org/software/TMPRED form.html).  
     [0391] Table 1 shows the various tissue sources of SEQ ID NO: 1-337.  
     [0392] The homologs for polypeptides SEQ ID NO: 338-674, that correspond to nucleotide sequences SEQ ID NO: 1-337 were obtained by a BLASTP version 2.0 a1 19MP-WashU searches against Genpept release 124 and Geneseq (Derwent) release 200117 using BLAST algorithm. The results showing homologues for SEQ ID NO: 338-674 from Genpept 124 are shown in Table 2.  
     [0393] Using eMatrix software package (Stanford University, Stanford, Calif.) (Wu et al., J. Comp. Biol., Vol. 6, 219-235 (1999), http://motif.stanford.edu/ematrix-search/herein incorporated by reference), all the polypeptide sequences were examined to determine whether they had identifiable signature regions. Scoring matrices of the eMatrix software package are derived from the BLOCKS, PRINTS, PFAM, PRODOM, and DOMO databases. Table 3 shows the accession number of the homologous eMatlix signature found in the indicated polypeptide sequence, its description, and the results obtained which include accession number subtype; raw score; p-value; and the position of signature in amino acid sequence.  
     [0394] Using the Pfam software program (Sonnhammer et al., Nucleic Acids Res., Vol. 26(1) pp. 320-322 (1998) herein incorporated by reference) all the polypeptide sequences were examined for domains with homology to certain peptide domains. Table 4 shows the name of the Pfam model found, the description, the e-value and the Pfam score for the identified model within the sequence. Further description of the Pfam models can be found at http://pfam.wustl.edu/.  
     [0395] The GeneAtlas™ software package (Molecular Simulations Inc. (MSI), San Diego, Calif.) was used to predict the three-dimensional structure models for the polypeptides encoded by SEQ ID NO: 1-337 (i.e. SEQ ID NO: 338-674). Models were generated by (1) PST-BLAST which is a multiple alignment sequence profile-based searching developed by Altschul et al, (Nucl. Acids. Res. 25, 3389-3408 (1997)), (2) Hfigh Throughput Modeling (HTM) (Molecular Simulations Inc. (MSI) San Diego, Calif.,) which is an automated sequence and structure searching procedure (http://www.msi.com/), and (3) SeqFold™ which is a fold recognition method described by Fischer and Eisenberg (J. Mol. Biol. 209, 779-791 (1998)). This analysis was carried out, in part, by comparing the polypeptides of the invention with the known NMR (nuclear magnetic resonance) and x-ray crystal three-dimensional structures as templates. Table 5 shows: “PDB ID”, the Protein DataBase (PDB) identifier given to template structure; “Chain ID”, identifier of the subcomponent of the PDB template structure; “Compound Information”, information of the PDB template structure and/or its subcomponents; “PDB Function Annotation” gives function of the PDB template as annotated by the PDB files (http:/www.rcsb.org/PDB/); start and end amino acid position of the protein sequence aligned; PSI-BLAST score, the verify score, the SeqFold score, and the Potential(s) of Mean Force (PMF). The verify score is produced by GeneAtlas™ software (MSI), is based on Dr. Eisenberg&#39;s Profile-3D threading program developed in Dr. David Eisenberg&#39;s laboratory (U.S. Pat. No. 5,436,850 and Luthy, Bowie, and Eisenberg, Nature, 356:83-85 (1992)) and a publication by R. Sanchez and A. Sali, Proc. Natl. Acad. Sci. USA, 95:13597-12502. The verify score produced by GeneAtlas normalizes the verify score for proteins with different lengths so that a unified cutoff can be used to select good models as follows: 
     Verify score(normalized)=(raw score−½ high score)/(½ high score) 
     [0396] The PFM score, produced by GeneAtlas™ software (MSI), is a composite scoring function that depends in part on the compactness of the model, sequence identity in the alignment used to build the model, pairwise and surface mean force potentials (MFP) As given in table 5, a verify score between 0 to 1.0, with 1 being the best, represents a good model. Similarly, a PNF score between 0 to 1.0, with 1 being the best, represents a good model. A SeqFold™ score of more than 50 is considered significant. A good model may also be determined by one of skill in the art based all the information in Table 5 taken in totality.  
     [0397] Table 6 shows the position of the signal peptide in each of the polypeptides and the maximum score and mean score associated with that signal peptide using Neural Network SignalP V1.1 program (from Center for Biological Sequence Analysis, The Technical University of Denmark). The process for identifying prokaryotic and eukaryotic signal peptides and their cleavage sites are also disclosed by Henrik Nielson, Jacob Engelbrecht, Soren Brunak, and Gunnar von Heijne in the publication “ Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites” Protein Engineering, Vol. 10, no. 1, pp. 1-6 (1997), incorporated herein by reference. A maximum S score and a mean S score, as described in the Nielson et al reference, was obtained for the polypeptide sequences.  
     [0398] Table 7 correlates nucleotide sequences of the invention to a specific chromosomal location when assignable.  
     [0399] Table 9 shows the number of transmembrane regions, their location(s), and TMPred score obtained, for each of the SEQ ID NO: 338-674 that had a TMPred score of 800 or greater, using the TMpred program (http://www.ch.embnet.org/software/TMPRED form.html).  
     [0400] Table 10 is a correlation table of the novel polynucleotide sequences SEQ ID NO: 1-337, their corresponding polypeptide sequences SEQ ID NO: 338-674, their corresponding priority contig nucleotide sequences SEQ ID NO: 675-836, their corresponding priority contig polypeptide sequences SEQ ID NO: 837-998, and the U.S. serial number of the priority application (all of which are herein incorporated in their entirety), in which the contig sequence was filed.  
                           TABLE 1                           RNA/Tissue   Library           Tissue Origin   Source   Name   SEQ ID NO:                  adult brain   GIBCO   AB3001   17 21-22 34 82 263       adult brain   GIBCO   ABD003   23 29 34 62 82 107-108 120 157-158 191 197 206 233 263 327                   336       adult brain   Clontech   ABR001   29 55 71 95 125 258 286       adult brain   Clontech   ABR006   2 29 50 80 85 101 130 143 152 155 161 163 165-166 186 188-191                   197 215 244-254 266-267 276 280       adult brain   Clontech   ABR008   42 46 52 56-63 77-78 80-81 85-88 93 95 110 112-117 120 138                   150-152 156 158 166 174 186 194 197 211 215 220 241 245                   273 280 286 296-297 322-323 334 336       adult brain   Invitrogen   ABR014   82 286 322       adult brain   Invitrogen   ABR015   62 82       adult brain   Invitrogen   ABR016   62 304       adult brain   Invitrogen   ABT004   42-43 61 71-72 102 164 172 273 276 286       cultured   Stratagene   ADP001   9 43 45 79 136-138 263       preadipocytes       adrenal gland   Clontech   ADR002   39 52 54 64-65 71 121 125 164 170 258 298 309 320       adult heart   GIBCO   AHR001   9 12-13 34-35 45 71-72 82 85 99 110 113 120 127 150 158 163                   186 266 275 311 330       adult kidney   GIBCO   AKD001   9 11 14 26 31 34 46 52-54 66 72 82 150 158 164 174 195 233                   257 263 281 284 286       adult kidney   Invitrogen   AKT002   9 29 39-40 46 54 108 121 125 158 164 173-174 206 227 249                   257-258 284 300 311       adult lung   GIBCO   ALG001   31 108       lymph node   Clontech   ALN001   82 251 336       young liver   GIBCO   ALV001   79 94 263       adult liver   Invitrogen   ALV002   31 45 73 118 139-140 143 158 164 174 216 233 263 277 315       adult liver   Clontech   ALV003   3       adult ovary   Invitrogen   AOV001   24 26 29 32 34 39 44-46 50-51 54 82 85 102 108 121 125 132                   140 158 162 164 210 215 217 227 233-234 238 258 269 285-286                   297 306       adult placenta   Clontech   APL001   82 215 274       placenta   Invitrogen   APL002   79 286       adult spleen   GIBCO   ASP001   81-82 140 170 263 286       adult testis   GIBCO   ATS001   25 38 82 311       adult bladder   Invitrogen   BLD001   81 85 94       bone marrow   Clontech   BMD001   5 7-8 15 17 36 45-47 82 104 161 215       bone marrow   GF   BMD002   10 31 45-47 52 58 63 93 99 104 110 134-135 142-143 153 181-184                   191-192 221 228 311       adult colon   Invitrogen   CLN001   32 229 257 263-264       adult cervix   BioChain   CVX001   2 34 46 54 58 69 71 82 94 119-120 161 164 167 174 191 233                   266       endothelial cells   Stratagene   EDT001   39-40 45-46 75 77 82-83 108 121 143 164 194 199 216 285-286                   311       fetal brain   Clontech   FBR001   247 266       fetal brain   Clontech   FBR004   265-266       fetal brain   Clontech   FBR006   19 42 51 58 69 80 87 94-97 104 110 112 140 143 154-156 164                   174 186 191 196-197 199 220 230 245 267-274 282 286 297                   300 311 335       fetal brain   Invitrogen   FBT002   44 54 58 141 143 164 286       fetal heart   Invitrogen   FHR001   47 51 66 80 104 114 116 127 143 197 200-201 212-214 227 259                   263 280 286 318       fetal kidney   Clontech   FKD001   39 103 121       fetal kidney   Clontech   FKD002   59 81 88 110 162 186 202-203 221 223 247 273 280 284       fetal lung   Clontech   FLG001   20 102       fetal lung   Invitrogen   FLG003   98-99 126       fetal liver-   Columbia   FLS001   1-4 16 18 21 32 39-40 45-47 49 54 68-69 71 79 82 108 110 121       spleen   University       127-128 138 161 171 174-176 210 215-216 218 234 267 280                   286 328 330       fetal liver-   Columbia   FLS002   3 11 32 39-40 45 47 68 79 82 90 121 128-131 138 140 142-143       spleen   University       158 161 164 169 174-175 210 215-217 227 232 256 278 285-286                   305 307 314 319 328 330       fetal liver-   Columbia   FLS003   3 21 127-128 140 162 178-180 218-219 227       spleen   University       fetal liver   Invitrogen   FLV001   41 75 94 164 286 309       fetal liver   Clontech   FLV002   3 9 59 114       fetal liver   Clontech   FLV004   3 10 69 88 143 186 204 222-223 267 311 314 336       fetal muscle   Invitrogen   FMS001   75 164 263 286 311       fetal muscle   Invitrogen   FMS002   82 140 150 193-195 224-225 311       fetal skin   Invitrogen   FSK001   66 79 100 114 126 138 158-159 211 249 254 263 286 311 329       fetal skin   Invitrogen   FSK002   9 63 88 94 106 110 114 116 138 143 150 167-168 197 205-207                   226-232 259 267 311 329       umbilical cord   BioChain   FUC001   66 82 95 120 127 162 216 273 286 330       fetal brain   GIBCO   HFB001   6 19-20 26-27 32 34 45 62 82 138 141 157 163-164 216 238 263                   311       macrophage   Invitrogen   HMP001   281 325       infant brain   Columbia   IB2002   27 29 48 52 74 91 106-108 138 158 163 236 240 245 263 322           University       336       infant brain   Columbia   IB2003   29 37 46 71 74 79 118 141 237-241 251 266 269           University       infant brain   Columbia   IBM002   94 263           University       infant brain   Columbia   IBS001   29 37 46 164           University       lung, fibroblast   Stratagene   LFB001   82       lung tumor   Invitrogen   LGT002   9 18 28 30 32-33 45 59-60 72 75-77 79 82 92 118 120-124 140                   143 164 257 273 284-286 311 316       lymphocytes   ATCC   LPC001   21 27 46 89 93-94 116 132 143 160 169 228 233-235 286 333                   336       leukocyte   GIBCO   LUC001   9-10 27 30 32 41 46-47 54 58 79 82 89 94 109 143 160 186 233                   258 263 308 311       leukocyte   Clontech   LUC003   233 299       melanoma   Clontech   MEL004   54 105 282-283 286       from-cell-line-       ATCC-#CRL-       1424       mammary gland   Invitrogen   MMG001   16 29-31 34 45 54 66-68 78-79 82 85 118 174 211 217 256 263                   273 284 313 336       induced neuron-   Stratagene   NTD001   50 266 311       cells       retinoic acid-   Stratagene   NTR001   2 54 216 255 286       induced-       neuronal-cells       neuronal cells   Stratagene   NTU001   256 286       pituitary gland   Clontech   PIT004   50 58 261 286 311       placenta   Clontech   PLA003   116 186 206 208-209 228 232 244 329       prostate   Clontech   PRT001   59 72 90 217 221 233 262       rectum   Invitrogen   REC001   88 101 133 217 249 263       salivary gland   Clontech   SAL001   216       small intestine   Clontech   SIN001   27 37 40 66 69 72 82 108 143 152 162 177 184-186 191 206                   242-243 247 264       skeletal muscle   Clontech   SKM001   108 269       spinal cord   Clontech   SPC001   27 29 34 88 102 125 138 158 170 174 195 233 241 254 258-259       adult spleen   Clontech   SPLc01   66 81 110 140 161 228 236 260       stomach   Clontech   STO001   59 108       thalamus   Clontech   THA002   32 46 61 79 110       thymus   Clontech   THM001   68 89 102-103 233 331       thymus   Clontech   THMc02   29 39 69 71 79 81 89 93-94 104 110-111 121 186 211 235-236                   299 318 331       thyroid gland   Clontech   THR001   9 27 39 58 69-71 77 84 88 121 158 167 197 233 254 263 273                   311       trachea   Clontech   TRC001   10 63 69 81 227       uterus   Clontech   UTR001   125 233 266 286 311                  
 
     [0401]                                   TABLE 2                       SEQ ID   Accession               %       NO:   No.   Species   Description   Score   Identity                                                        338   gi201734     Mus musculus     t complex protein-10   76   44       338   gi53992     Mus musculus     Tcp-10   76   44       338   gi201727     Mus musculus     t complex protein-10   76   44       339   AAB88481     Homo sapiens     Human membrane or secretory protein clone   254   73                   PSEC0251.       339   gi57115     Rattus     ribosomal protein L31 (AA 1-125)   175   67                 norvegicus         339   gi14198321     Mus musculus     ribosomal protein L31   175   67       340   gi3093754     Neurospora     AR2   78   28                 crassa         340   gi3776090     Mus musculus     wolframin   76   29       340   gi3777585     Mus musculus     transmembrane protein   76   29       341   gi13507259     Homo sapiens     amnionless mRNA, complete cds.   1167   99       341   gi13649780     Mus musculus     amnionless precursor protein   840   71       341   AAY66714     Homo sapiens     Membrane-bound protein PRO1028.   1167   99       342   gi13183881     Homo sapiens     Fanconi anemia complementation group D2   657   90                   protein (FANCD2) mRNA, complete cds,                   alternatively spliced.       342   gi13324523     Homo sapiens     Fanconi anemia complementation group D2   657   90                   protein (FANCD2) gene, exons 43, 44, and                   complete cds, alternatively spliced.       342   gi10434106     Homo sapiens     cDNA FLJ12551 fis, clone NT2RM4000700.   175   100       343   gi4200216     Homo sapiens       H. sapiens  gene from PAC 1026E2, partial.   475   100       343   gi14141674     Rattus     BMP/retinoic acid-inducible neural-specific   151   54                 norvegicus     protein       343   gi3041877     Homo sapiens     IB3089A (IB3089A) mRNA, complete cds.   151   54       344   gi14193307   Candidatus   ATP synthase beta subunit   61   35                 Carsonella                   ruddii         344   gi2688677     Borrelia     oligopeptide ABC transporter, permease protein   65   28                 burgdorferi     (oppC-2)       344   gi14193323   Candidatus   ATP synthase beta subunit   59   31                 Carsonella                   ruddii         345   gi14250140     Homo sapiens     clone MGC: 14809, mRNA, complete cds.   173   100       345   gi561639     Homo sapiens     IgE receptor beta chain (HTm4) mRNA,   173   100                   complete cds.       345   AAW06503     Homo sapiens     HTm4 protein.   173   100       346   AAY27669     Homo sapiens     Human secreted protein encoded by gene No.   255   100                   103.       346   gi3719255     Mus musculus     Clq/MBL/SPA receptor ClqRp   50   35       346   gi5714405     Mus musculus     Clq/MBL/SP-A phagocytic receptor ClqRp   50   35       347   gi12580867     Picea abies     60S ribosomal protein L13E   83   33       347   gi3127821     Drosophila     Sex-Peptide   66   41                 subobscura         347   gi3549864     Drosophila     Sex-peptide   66   41                 subobscura         348   gi10176829     Arabidopsis     gene_id: MBB18.16˜   79   32                 thaliana         349   gi7380324     Neisseria     ClpB protein   91   32                 meningitidis                 Z2491       349   gi7226713     Neisseria     clpB protein   91   32                 meningitidis                 MC58       349   gi9658311     Vibrio     integrase-related protein   61   34                 cholerae         350   gi3986168     Lentinula     SHP1   55   31                 edodes         350   gi12805659     Mus musculus     Similar to syndecan 4   53   34       351   gi9789476     Mus musculus     claudin-19   98   41       351   gi3335182     Mus musculus     claudin-1   98   32       351   gi12805093     Mus musculus     claudin 1   98   32       352   AAB37990     Homo sapiens     Human secreted protein encoded by gene 7   303   98                   clone HWLHH15.       352   gi312188   Bovine   glycoprotein gD   85   29               herpesvirus 1       352   gi5668989   Bovine   glycoprotein D precursor   76   29               herpesvirus               type 1.1       353   gi7239364     Homo sapiens     acetylcholinesterase collagen-like tail subunit   136   29                   (COLQ) gene, exon 17; and complete cds,                   alternatively spliced.       353   gi3599478     Acanthamoeba     Myosin-IA   137   35                 castellanii         353   gi3858883     Acanthamoeba     myosin I heavy chain kinase   133   30                 castellanii         354   gi5901822     Drosophila     EG: 118B3.2   160   70                 melanogaster         354   AAB29877     Homo sapiens     Human secreted protein BLAST search protein   127   52                   SEQ ID NO: 135.       354   AAB29878     Homo sapiens     Human secreted protein BLAST search protein   121   41                   SEQ ID NO: 136.       355   AAB53400     Homo sapiens     Human colon cancer antigen protein sequence   220   91                   SEQ ID NO: 940.       355   gi1177469     Homo sapiens     gene for interleukin-10.   37   46       355   AAB62192     Homo sapiens     Human interleukin-10 (IL-10) protein.   37   46       356   gi2589210     Mus musculus     calcium-sensing receptor related protein 3   105   35       356   gi3130157     Takifugu     pheromone receptor   106   34                 rubripes         356   gi2589208     Mus musculus     calcium-sensing receptor related protein 2   99   33       357   gi3130189     Takifugu     pheromone receptor   212   63                 rubripes         357   gi2589208     Mus musculus     calcium-sensing receptor related protein 2   205   50       357   gi2589210     Mus musculus     calcium-sensing receptor related protein 3   203   48       358   AAB43892     Homo sapiens     Human cancer associated protein sequence SEQ   253   83                   ID NO: 1337.       358   gi6456100     Mus musculus     F-box protein FBL10   247   83       358   gi14250563     Homo sapiens     clone IMAGE: 3163445, mRNA, partial cds.   253   83       359   AAB13343     Homo sapiens     Human cortexin-like protein.   204   53       359   AAB38538     Homo sapiens     Human secreted protein sequence encoded by   57   39                   gene 17 SEQ ID NO: 75.       359   AAB34316     Homo sapiens     Human secreted protein sequence encoded by   54   34                   gene 18 SEQ ID NO: 77.       360   AAB24074     Homo sapiens     Human PRO1153 protein sequence SEQ ID   136   42                   NO: 49.       360   AAY66735     Homo sapiens     Membrane-bound protein PRO1153.   136   42       360   AAB65258     Homo sapiens     Human PRO1153 (UNQ583) protein sequence   136   42                   SEQ ID NO: 351.       361   AAB70534     Homo sapiens     Human PRO4 protein sequence SEQ ID NO: 8.   395   100       361   AAY13377     Homo sapiens     Amino acid sequence of protein PRO257.   395   100       361   AAB80245     Homo sapiens     Human PRO257 protein.   395   100       362   gi4731216     Boophilus     NADH dehydrogenase subunit 2   52   25                 microplus         362   gi6180101     Cafeteria     NADH dehydrogenase subunit 2   71   48                 roenbergensis         362   gi5869819     Globodera     NADH-ubiquinone oxidoreductase subunit 1   82   35                 pallida         363   AAB08944     Homo sapiens     Human secreted protein sequence encoded by   206   83                   gene 19 SEQ ID NO: 101.       363   AAB08909     Homo sapiens     Human secreted protein sequence encoded by   159   80                   gene 19 SEQ ID NO: 66.       363   gi14029247     Gnorimosphaeroma     cytochrome oxidase subunit I   66   53                 oregonense         364   gi13195147     Mus musculus     HCH   953   77       364   gi1339910     Homo sapiens     Human DOCK180 protein mRNA, complete   203   32                   cds.       364   AAW03515     Homo sapiens     Human DOCK180 protein.   203   32       365   gi10433539     Homo sapiens     cDNA FLJ12133 fis, clone MAMMA1000278.   224   35       365   AAW64461     Homo sapiens     Human secreted protein from clone B121.   218   35       365   gi4406644     Homo sapiens     clone 25130 mRNA sequence, complete cds.   223   41       366   gi1537002   Hepatitis C   envelope glycoprotein E2/NS1   61   32               virus       366   gi3153687   Hepatitis C   genome polyprotein   60   41               virus       366   AAB45374     Homo sapiens     Human secreted protein sequence encoded by   58   50                   gene 36 SEQ ID NO: 126.       367   gi2935614     Homo sapiens     PAC clone RP1-102K2 from 22q12.1-qter,   1306   100                   complete sequence.       367   gi386988     Homo sapiens     Human oncostatin M gene, exon 3.   1306   100       367   AAR33380     Homo sapiens     Cytokine hOSM.   1306   100       368   AAB87396     Homo sapiens     Human gene 8 encoded secreted protein   440   89                   HMAM121, SEQ ID NO: 137.       368   AAY95967     Homo sapiens     Human TANGO 240.   436   88       368   AAB88402     Homo sapiens     Human membrane or secretory protein clone   434   88                   PSEC0152.       369   AAB24476     Homo sapiens     Human secreted protein sequence encoded by   241   69                   gene 40 SEQ ID NO: 101.       369   gi452414     Mus musculus     mPit-1R   69   31       369   gi7769944     Leishmania     L354.10   87   25                 major         370   gi36853     Homo sapiens     Human mRNA for T-cell receptor alpha-chain   585   100                   HAVP02 (V(a)11.1-J(a)I).       370   gi2358022     Homo sapiens     T-cell receptor alpha delta locus from bases 1 to   585   100                   250529 (section 1 of 5) of the Complete                   Nucleotide Sequence.       370   gi404055     Macaca     T-cell receptor alpha chain   568   97                 mulatta         371   gi9963895     Homo sapiens     HT021 (HT021) mRNA, complete cds.   255   94       371   AAW54455     Homo sapiens     Mouse novel secreted protein isolated from   255   94                   clone BF290_li.       371   AAB59017     Homo sapiens     Breast and ovarian cancer associated antigen   255   94                   protein sequence SEQ ID 725.       372   gi2055228     Glycine max     SRC1   76   26       372   gi204144     Rattus     profilaggrin   97   25                 norvegicus         372   gi3820941   Hepatitis B   core antigen   71   24               virus       373   gi1234787     Xenopus     up-regulated by thyroid hormone in tadpoles;   1115   58                 laevis     expressed specifically in the tail and only at                   metamorphosis; membrane bound or                   extracellular protein; C-terminal basic region       373   gi10435980     Homo sapiens     cDNA FLJ13840 fis, clone THYRO1000783,   699   72                   moderately similar to Xenopus laevis tail-                   specific thyroid hormone up-regulated (gene 5)                   mRNA.       373   gi4868122     Mus musculus     hedgehog-interacting protein   405   33       374   gi1181494     Paramecium     a331L   61   46                 bursaria                 Chlorella virus 1       374   AAY91469     Homo sapiens     Human secreted protein sequence encoded by   57   40                   gene 19 SEQ ID NO: 142.       374   AAY91617     Homo sapiens     Human secreted protein sequence encoded by   57   40                   gene 19 SEQ ID NO: 290.       375   gi12007419     Mus musculus     B4 olfactory receptor   285   60       375   gi12007420     Mus musculus     B5 olfactory receptor   285   60       375   gi12007421     Mus musculus     B6 olfactory receptor   285   60       376   AAB20695     Homo sapiens     Polymeric immunoglobulin receptor binding   60   55                   domain peptide SEQ ID NO: 11.       376   gi1181346     Paramecium     a183L   56   28                 bursaria                 Chlorella virus 1       376   gi14030701     Arabidopsis     At2g28370/T1B3.11   72   27                 thaliana         378   gi1296632     Homo sapiens       H. sapiens  gene encoding G protein coupled   104   37                   receptor.       378   gi1124905     Homo sapiens       H. sapiens  P2Y4 gene.   104   37       378   AAW23606     Homo sapiens     Human P2Y4 receptor polypeptide.   104   37       379   gi4877582     Homo sapiens     lipoma HMGIC fusion partner (LHFP) mRNA,   110   25                   complete cds.       379   AAY87336     Homo sapiens     Human signal peptide containing protein HSPP-   110   25                   113 SEQ ID NO: 113.       380   AAY27721     Homo sapiens     Human secreted protein encoded by gene No.   1118   88                   29.       380   AAB87068     Homo sapiens     Human secreted protein TANGO 365, SEQ ID   621   99                   NO: 46.       380   AAB87146     Homo sapiens     Human secreted protein TANGO 365 A5V   617   98                   variant, SEQ ID NO: 161.       381   gi7208423     Caulobacter     CpaA   65   36                 crescentus         381   gi13424575     Caulobacter     pilus assembly protein CpaA   65   36                 crescentus         382   AAY28917     Homo sapiens     Human regulatory protein HRGP-3.   267   100       382   AAB53312     Homo sapiens     Human colon cancer antigen protein sequence   267   100                   SEQ ID NO: 852.       382   gi11526789     Homo sapiens     inorganic pyrophosphatase 2 (PPA2) mRNA,   258   98                   complete cds, nuclear gene for mitochondrial                   product.       383   gi13938575     Homo sapiens     Similar to RIKEN cDNA 2610511E22 gene,   655   89                   clone MGC: 4251, mRNA, complete cds.       383   AAY91458     Homo sapiens     Human secreted protein sequence encoded by   655   89                   gene 8 SEQ ID NO: 131.       383   AAY91598     Homo sapiens     Human secreted protein sequence encoded by   655   89                   gene 8 SEQ ID NO: 271.       384   gi2065210     Mus musculus     Pro-Pol-dUTPase polyprotein   1026   82       384   gi3860513     Mus famulus     reverse transcriptase   482   84       384   gi4379237     Mus musculus     reverse transcriptase   477   83       385   gi14190365     Arabidopsis     AT5g17300/MKP11_15   64   32                 thaliana         385   gi11275913   Protophormia   cytochrome oxidase subunit 1   55   44               atriceps       385   AAY29337     Homo sapiens     Human secreted protein clone gg894_13   63   28                   alternate reading frame protein.       386   AAY20840     Homo sapiens     Human neurofilament-H wild type protein   67   38                   fragment 1.       386   gi10584099   Halobacterium   Vng6036h   61   28               sp. NRC-1       386   gi7739781     Rattus     CCN family protein COP-1   80   26                 norvegicus         387   gi14042550     Homo sapiens     cDNA FLJ14779 fis, clone NT2RP4000398,   242   66                   moderately similar to ZINC FINGER PROTEIN                   140.       387   gi456269     Mus musculus     zinc finger protein 30   242   70               domesticus       387   gi5080758     Homo sapiens     chromosome 19, BAC 331191 (CIT-B-471f3),   244   69                   complete sequence.       388   AAB47106     Homo sapiens     Second splice variant of MAPP.   223   97       388   AAB47105     Homo sapiens     First splice variant of MAPP.   200   90       388   AAW25722     Homo sapiens     Human partial beta meltrin protein fragment 2.   184   66       389   AAB90649     Homo sapiens     Human secreted protein, SEQ ID NO: 192.   563   92       389   AAB90565     Homo sapiens     Human secreted protein, SEQ ID NO: 103.   472   100       389   AAB90651     Homo sapiens     Human secreted protein, SEQ ID NO: 194.   203   97       390   AAY87335     Homo sapiens     Human signal peptide containing protein HSPP-   623   99                   112 SEQ ID NO: 112.       390   gi2292988     Rattus     Inter-alpha-inhibitor H4 heavy chain   87   32                 norvegicus         390   AAY90288     Homo sapiens     Human peptidase, HPEP-5 protein sequence.   63   36       391   AAY92710     Homo sapiens     Human membrane-associated protein Zsig24.   230   100       391   AAY87250     Homo sapiens     Human signal peptide containing protein HSPP-   230   100                   27 SEQ ID NO: 27.       391   AAG00627     Homo sapiens     Human secreted protein, SEQ ID NO: 4708.   93   100       392   gi10441465     Homo sapiens     actin filament associated protein (AFAP)   274   90                   mRNA, complete cds.       392   gi13129531     Gallus gallus     actin filament-associated protein   204   71       392   gi13129529     Gallus gallus     neural actin filament protein   204   71       393   AAB64802     Homo sapiens     Human secreted protein sequence encoded by   58   41                   gene 30 SEQ ID NO: 88.       393   gi1711217     Caenorhabditis     F58A3.1b   77   30                 elegans         393   gi1711215     Caenorhabditis     F58A3.1a   77   30                 elegans         394   AAB12121     Homo sapiens     Hydrophobic domain protein from clone   153   68                   HP02962 isolated from KB cells.       394   AAY30812     Homo sapiens     Human secreted protein encoded from gene 2.   149   65       394   AAB88452     Homo sapiens     Human membrane or secretory protein clone   144   66                   PSEC0241.       395   gi13623237     Homo sapiens     clone MGC: 10671, mRNA, complete cds.   146   57       395   gi13310191   multiple   recombinant envelope protein   126   35               sclerosis               associated               retrovirus               element       395   gi4262296     Homo sapiens     endogenous retrovirus W envelope protein   117   35                   mRNA, partial cds.       396   gi10437485     Homo sapiens     cDNA: FLJ21394 fis, clone COL03536.   65   30       396   AAG02270     Homo sapiens     Human secreted protein, SEQ ID NO: 6351.   59   44       397   AAY20292     Homo sapiens     Human apolipoprotein E wild type protein   63   51                   fragment 2.       397   AAB32406     Homo sapiens     Human secreted protein sequence encoded by   62   36                   gene 5 SEQ ID NO: 92.       397   gi12667610   uncultured   dissimilatory sulfite reductase subunit A   72   39               sulfate-               reducing               bacterium               UMTRAdsr648-22       398   gi12053099     Homo sapiens     mRNA; cDNA DKFZp434A171 (from clone   172   65                   DKFZp434A171); complete cds.       398   gi3002799     Pseudomonas     2-aminomuconic acid semialdehyde   118   29                 pseudoalcaligenes     dehydrogenase       398   gi5821145     Homo sapiens     mRNA for RNA binding protein, partial cds,   120   22                   clone: R11.       399   gi14249823     Homo sapiens     cholecystokinin, clone MGC: 10571, mRNA,   356   100                   complete cds.       399   gi179996     Homo sapiens     Human cholecystokinin (CCK) gene, exon 3.   356   100       399   AAB24381     Homo sapiens     Human procholecystokinin amino acid sequence   356   100                   SEQ ID NO: 1.       400   gi1870554     Saguinus     T-cell receptor beta   79   32                 oedipus         400   gi1150925   Bovine   glycoprotein B   65   38               herpesvirus 1       400   gi159250     Holothuria     sperm specific protein phi-0   60   30                 tubulosa         401   gi4097231     Ureaplasma     multiple banded antigen   395   23                 urealyticum         401   gi560649     Neocallimastix     Xylanase B, XYLB {EC 3.2.1.8}   330   20                 patriciarum ,               Peptide, 860               aa       401   gi600118     Zea mays     extensin-like protein   331   35       402   AAB12140     Homo sapiens     Hydrophobic domain protein isolated from   172   51                   WERI-RB cells.       402   AAY25806     Homo sapiens     Human secreted protein fragment encoded from   130   46                   gene 23.       402   gi5901846     Drosophila     BcDNA.GH12144   124   39                 melanogaster         403   AAB66267     Homo sapiens     Human TANGO 272 SEQ ID NO: 14.   1329   97       403   gi2289904     Mus musculus     DRPLA   125   28       403   gi1549217     Mus musculus     DRPLA protein   124   28       404   gi4705     Saccharomyces     Ty protein   58   51                 cerevisiae         404   gi11139690     Ovis aries     muscle specific calpain 3   54   41       404   AAY41363     Homo sapiens     Human secreted protein encoded by gene 56   54   55                   clone HNGFE55.       405   gi13926111     Homo sapiens     2P domain potassium channel Talk-2   1430   100                   (KCNK17) mRNA, complete eds.       405   AAY90354     Homo sapiens     Human TWIK-3 protein.   1426   99       405   gi13507377     Homo sapiens     potassium channel TASK-4 mRNA, complete   1364   99                   cds.       406   gi514916     Bos taurus     tau protein   91   36       406   gi437055     Macaca     mucin   95   28                 mulatta         406   gi2754696     Gallus gallus     high molecular mass nuclear antigen   103   28       407   gi3127175     Homo sapiens     sulfonylurea receptor 2A (SUR2) gene,   713   98                   alternatively spliced product, exon 38a and                   complete cds.       407   gi3127176     Homo sapiens     sulfonylurea receptor 2B (SUR2) gene,   713   98                   alternatively spliced product, exon 38b and                   complete cds.       407   gi5814019     Oryctolagus     cardiac ventricle sulfonyl urea receptor   678   93                 cuniculus         408   AAB24035     Homo sapiens     Human PRO4397 protein sequence SEQ ID   1894   100                   NO: 42.       408   AAY93951     Homo sapiens     Amino acid sequence of a Brainiac-5   1241   100                   polypeptide.       408   AAY06462     Homo sapiens     Human Brainiac-3.   553   48       409   AAW88708     Homo sapiens     Secreted protein encoded by gene 175 clone   747   87                   HEMAM41.       409   gi159655     Ascaris suum     collagen   94   36       409   gi289662     Caenorhabditis     col-36 collagen   109   41                 elegans         410   gi975893     Homo sapiens     Human apolipoprotein apoC-IV (APOC4) gene,   693   100                   complete cds.       410   AAG03772     Homo sapiens     Human secreted protein, SEQ ID NO: 7853.   669   96       410   gi1185465     Oryctolagus     Apolipoprotein C-IV   379   55                 cuniculus         411   AAY57878     Homo sapiens     Human transmembrane protein HTMPN-2.   101   86       411   gi4406500     Carassius     gonadotropin releasing hormone receptor type A   72   31                 auratus         412   AAY59682     Homo sapiens     Secreted Protein 108-009-5-0-A2-FL.   488   100       412   AAY01635     Homo sapiens     Human PS214 derived polypeptide.   488   100       412   AAY64650     Homo sapiens     Human luman homology protein.   488   100       413   gi13442978     Mus musculus     D-glucuronyl C5-epimerase   1001   94       413   gi11935177     Mus musculus     heparin/heparan sulfate:glucuronic acid C5   1001   94                   epimerase       413   gi13654639     Bos taurus     D-glucuronyl C5 epimerase   972   92       414   AAG00122     Homo sapiens     Human secreted protein, SEQ ID NO: 4203.   102   100       414   gi4583535     Homo sapiens     integrin alpha 2 subunit (ITGA2) DNA, 5’ UTR   99   95                   and promoter region.       414   AAW70542     Homo sapiens     Integrin alpha-2 chain.   102   100       415   AAY01387     Homo sapiens     Secreted protein encoded by gene 5 clone   60   40                   HTLFE42.       415   gi3406819     Mus musculus     growth factor receptor   58   38       415   AAG02139     Homo sapiens     Human secreted protein, SEQ ID NO: 6220.   53   40       416   AAB12150     Homo sapiens     Hydrophobic domain protein isolated from HT-   683   100                   1080 cells.       416   gi13096862     Mus musculus     RIKEN cDNA 9430096L06 gene   634   90       416   AAB29651     Homo sapiens     Human membrane-associated protein HUMAP-8.   502   100       417   AAY41428     Homo sapiens     Fragment of human secreted protein encoded by   107   43                   gene 17.       417   AAY41324     Homo sapiens     Human secreted protein encoded by gene 17   108   40                   clone HNFIY77.       417   AAB67576     Homo sapiens     Amino acid sequence of a human hydrolytic   108   40                   enzyme HYENZ8.       418   gi7209315     Homo sapiens     mRNA for FLJ00007 protein, partial cds.   1024   79       418   AAY99428     Homo sapiens     Human PRO1431 (UNQ737) amino acid   430   93                   sequence SEQ ID NO: 315.       418   gi6599145     Homo sapiens     mRNA; cDNA DKFZp434L127 (from clone   320   33                   DKFZp434L127); partial cds.       419   gi297172     Rattus rattus     ribosomal protein S7   432   93       419   gi2811284     Mus musculus     ribosomal protein S7   432   93       419   gi12804027     Homo sapiens     ribosomal protein S7, clone MGC: 10268,   432   93                   mRNA, complete cds.       420   AAB68888     Homo sapiens     Human RECAP polypeptide, SEQ ID NO: 18.   277   64       420   AAB08944     Homo sapiens     Human secreted protein sequence encoded by   74   72                   gene 19 SEQ ID NO: 101.       420   AAY76198     Homo sapiens     Human secreted protein encoded by gene 75.   67   59       421   gi4096055     Homo sapiens     chromosome 19, cosmid R28379, complete   136   100                   sequence.       421   gi9950071     Pseudomonas     probable permease of ABC transporter   81   39                 aeruginosa         421   gi2113989     Mycobacterium     ccsA   79   34                 tuberculosis         422   gi10438804     Homo sapiens     cDNA: FLJ22419 fis, clone HRC08593.   262   92       422   gi10436785     Homo sapiens     cDNA FLJ14342 fis, clone THYRO1000569,   98   42                   highly similar to  Mus musculus  hematopoietic                   zinc finger protein mRNA.       422   gi6690339     Mus musculus     hematopoietic zinc finger protein   96   40       423   gi9963845     Homo sapiens     HT017 mRNA, complete cds.   558   38       423   AAW09405     Homo sapiens     Pineal gland specific gene-1 protein.   558   38       423   AAB69185     Homo sapiens     Human hISLR-iso protein SEQ ID NO: 7.   558   38       424   gi475542     Rattus     glutamate receptor delta-1 subunit   505   98                 norvegicus         424   gi220418     Mus musculus     glutamate receptor channel subunit delta-1   505   98       424   gi56286     Rattus     glutamate receptor subtype delta-1   482   98                 norvegicus         425   AAB61880     Homo sapiens     Human cytokine receptor Zcytor14.   163   28       425   AAB61881     Homo sapiens     Human variant Zcytor14 protein Zcytor14-1.   137   32       425   AAB87606     Homo sapiens     Human PRO20040.   143   28       426   gi13195147     Mus musculus     HCH   413   86       426   gi1339910     Homo sapiens     Human DOCK180 protein mRNA, complete   373   78                   cds.       426   AAW03515     Homo sapiens     Human DOCK180 protein.   366   76       427   gi12724402     Lactococcus     prophage pi3 protein 41   58   36                 lactis  subsp.               lactis       427   gi155287     Vibrio     disulfide isomerase   73   29                 cholerae         428   gi6822060     Arabidopsis     peptide transport-like protein   93   31                 thaliana         428   gi206311     Rattus     protein phosphatase-2Bc   58   30                 norvegicus         429   gi14042519     Homo sapiens     cDNA FLJ14763 fis, clone NT2RP3003621.   2026   99       429   gi13097630     Homo sapiens     clone MGC: 10791, mRNA, complete cds.   2026   99       429   gi13591620     Homo sapiens     kremen mRNA for kringle-containing   860   49                   transmembrane protein, complete cds.       430   gi13161409     Mus musculus     family 4 cytochrome P450   437   73       430   gi7331756     Caenorhabditis     contains similarity to Pfam family PF00067   139   37                 elegans     (Cytochrome P450), score = 356.1, E = 3.6e−103,                   N = 1       430   gi3876203     Caenorhabditis     contains similarity to Pfam domain: PF00067   135   37                 elegans     (Cytochrome P450), Score = 347.4, E-                   value = 5.1e−101, N = 1       431   AAB08862     Homo sapiens     Amino acid sequence of a human secretory   958   100                   protein.       431   gi12654587     Homo sapiens     clone MGC: 2463, mRNA, complete cds.   953   99       431   AAB12163     Homo sapiens     Hydrophobic domain protein from clone   953   99                   HP10671 isolated from Thymus cells.       432   gi4877582     Homo sapiens     lipoma HMGIC fusion partner (LHFP) mRNA,   195   30                   complete cds.       432   AAY87336     Homo sapiens     Human signal peptide containing protein HSPP-   195   30                   113 SEQ ID NO: 113.       432   gi7529641     Schizosacchar     calcium permease family membrane transporter   110   28                 omyces  pombe       433   gi3598974     Rattus     protein tyrosine phosphatase TD14   105   38                 norvegicus         433   gi6625751     Mink enteritis     capsid protein VP2   50   34               virus       433   gi5442034     Mus musculus     calmodulin-dependent protein kinase II beta M   66   37                   isoform       434   AAB33892     Homo sapiens     Human secreted protein BLAST search protein   43   60                   SEQ ID NO: 107.       434   AAB54248     Homo sapiens     Human pancreatic cancer antigen protein   62   42                   sequence SEQ ID NO: 700.       434   gi683548     Chironomus     gamma protein constant region   62   38                 pallidivittatus         435   gi41077     Escherichia     cal protein precursor (aa 1-51)   63   42                 coli         435   gi2995968     Leontopithecus     NADH dehydrogenase subunit 4   76   28                 rosalia         435   gi2995972     Leontopithecus     NADH dehydrogenase subunit 4   76   28                 chrysomelas         436   gi1196439     Homo sapiens     (clone H 4.4) latent transforming growth factor-   291   98                   beta binding protein (LTBP-1L) gene, partial                   cds.       436   gi207286     Rattus     TGF-beta masking protein large subunit   226   77                 norvegicus         436   gi3493176     Mus musculus     latent TGF beta binding protein   217   73       437   AAY57951     Homo sapiens     Human transmembrane protein HTMPN-75.   77   33       437   gi642017     Hordeum     phospholipid transfer protein precursor   72   30                 vulgare         437   gi11037708     Triticum     lipid transfer protein precursor   72   34                 aestivum         438   AAY20852     Homo sapiens     Human neurofilament-H mutant protein   108   38                   fragment 11.       438   gi1888411     Homo sapiens     mRNA encoding chimaeric transcript of   80   30                   collagen type 1 alpha 1 and platelet derived                   growth factor beta, 314 bp.       438   AAW18664     Homo sapiens     Fragmented human NF-H gene + 1 frameshift   100   38                   mutant product.       439   AAB08912     Homo sapiens     Human secreted protein sequence encoded by   251   100                   gene 22 SEQ ID NO: 69.       439   gi12248917     Homo sapiens     mRNA for spinesin, complete cds.   251   100       439   AAB11699     Homo sapiens     Human serine protease BSSP2 (hBSSP2), SEQ   251   100                   ID NO: 10.       440   gi13990776     Gallus gallus     immunoglobulin lambda chain   67   43       440   gi1086714     Caenorhabditis     coded for by  C. elegans  cDNA yk74c8.5;   55   45                 elegans     Similar to small type-II membrane antigen       440   gi1469906     Gallus gallus     beta-1,4-galactosyltransferase   56   46       441   AAY17526     Homo sapiens     Human secreted protein clone AM349 2 protein.   1131   100       441   AAY02361     Homo sapiens     Polypeptide identified by the signal sequence   1131   100                   trap method.       441   AAW52834     Homo sapiens     Secreted protein encoded by clone AM349_2.   664   100       442   gi5579130   Hepatitis E   non-structural polyprotein   71   37               virus       442   gi330005   Hepatitis E   poly-proline hinge   58   35               virus       442   gi7768740     Homo sapiens     genomic DNA, chromosome 21q, section   82   29                   89/105.       443   AAY86234     Homo sapiens     Human secreted protein HNTNC20, SEQ ID   476   60                   NO: 149.       443   AAB24074     Homo sapiens     Human PRO1153 protein sequence SEQ ID   111   46                   NO: 49.       443   AAY66735     Homo sapiens     Membrane-bound protein PRO1153.   111   46       444   gi12836893     Gallus gallus     IPR328-like protein   165   30       444   gi13357180     Homo sapiens     calcium channel gamma subunit 8 (CACNG8)   125   28                   mRNA, partial cds.       444   gi4558766     Homo sapiens     neuronal voltage gated calcium channel gamma-   158   30                   3 subunit mRNA, complete cds.       445   AAY79384     Homo sapiens     Human G protein coupled receptor SLGP 7   396   100                   transmembrane region.       445   gi11225483     Homo sapiens     ETL protein (ETL) mRNA, complete cds.   396   100       445   AAB61144     Homo sapiens     Human NOV14 protein.   396   100       446   gi13195147     Mus musculus     HCH   209   77       446   gi1339910     Homo sapiens     Human DOCK180 protein mRNA, complete   95   43                   cds.       446   AAW03515     Homo sapiens     Human DOCK180 protein.   95   43       447   gi10438431     Homo sapiens     cDNA: FLJ22155 fis, clone HRC00205.   518   34       447   gi10437336     Homo sapiens     cDNA: FLJ21267 fis, clone COL01717.   506   36       447   AAY07754     Homo sapiens     Human secreted protein fragment encoded from   291   37                   gene 11.       448   gi1552496     Homo sapiens     Human germline T-cell receptor beta chain   614   100                   Dopamine-beta-hydroxylase-like, TRY1, TRY2,                   TRY3, TCRBV27S1P, TCRBV22S1A2N1T,                   TCRBV9S1A1T, TCRBV7S1A1N2T,                   TCRBV5S1A1T, TCRBV13S3, TCRBV6S7P,                   TCRBV7S3A2T, TCRBV13S2A1T,                   TCRBV9S2A2PT, TCRBV7S2A1N4T,                   TCRBV13S9/13S2A1T, TCRBV6S5A1N1,                   TCRBV30S1P, TCRBV31S1, TCRBV13S5,                   TCRBV6S1A1N1, TCRBV32S1P,                   TCRBV5S5P, TCRBV1S1A1N1,                   TCRBV12S2A1T, TCRBV21S1, TCRBV8S4P,                   TCRBV12S3, TCRBV21S3A2N2T,                   TCRBV8S5P, TCRBV13S1 genes from bases 1                   to 267156 (section 1 of 3).       448   gi33560     Homo sapiens     Human mRNA for T-cell receptor V beta gene   609   100                   segment V-beta-9, clone IGRb20.       448   gi37634     Homo sapiens       H. sapiens  rearranged TCR Vbeta 9.1 mRNA for   609   100                   T cell receptor.       449   gi13960126     Homo sapiens     Similar to leucine-rich neuronal protein, clone   162   80                   MGC: 4126, mRNA, complete cds.       449   gi14043281     Homo sapiens     clone IMAGE: 3528313, mRNA, partial cds.   133   64       449   gi3135309     Homo sapiens     chromosome 7q22 sequence, complete   133   64                   sequence.       450   AAB61141     Homo sapiens     Human NOV11 protein.   370   86       450   gi4760778     Mus musculus     Ten-m2   369   100       450   gi5712201     Rattus     neurestin alpha   369   100                 norvegicus         451   AAW88628     Homo sapiens     Secreted protein encoded by gene 95 clone   78   30                   HPWAN23.       451   AAY57923     Homo sapiens     Human transmembrane protein HTMPN-47.   78   30       451   gi7109072     Plasmodium     PfEMP1 protein   78   37                 falciparum         452   gi1061424     Homo sapiens     Human PMS2 related (hPMSR3) gene, complete   194   48                   cds.       452   gi5738553     Homo sapiens     mRNA for zinc finger protein, clone cZNF41.5,   175   48                   partial.       452   gi5738547     Homo sapiens     mRNA for zinc finger protein, clone cZNF41.2,   174   71                   partial.       453   gi14161140     Streptococcus     M protein   75   35                 pyogenes         453   gi472917     Enterococcus     v-type Na-ATPase   64   37                 hirae         453   AAW00946     Homo sapiens     Human c-Fos protein.   63   40       454   gi6088092     Mesocricetus     cytochrome P450   92   47                 auratus         454   AAY91348     Homo sapiens     Human secreted protein sequence encoded by   130   40                   gene 3 SEQ ID NO: 69.       454   gi4249595     Mus musculus     CYP2C40   115   34       455   gi12053357     Homo sapiens     mRNA; cDNA DKFZp586G2122 (from clone   488   67                   DKFZp586G2122); complete cds.       455   AAY27649     Homo sapiens     Human secreted protein encoded by gene No.   62   35                   83.       455   gi9755390     Arabidopsis     F17F8.22   81   46                 thaliana         456   gi6273399     Homo sapiens     melanoma-associated antigen MG50 mRNA,   359   95                   partial cds.       456   AAW81030     Homo sapiens     Melanoma associated antigen MG50.   359   95       456   AAY70469     Homo sapiens     Human p53 target molecule, PRG2 protein.   359   95       457   AAB24074     Homo sapiens     Human PRO1153 protein sequence SEQ ID   1023   99                   NO: 49.       457   AAY66735     Homo sapiens     Membrane-bound protein PRO1153.   1023   99       457   AAB65258     Homo sapiens     Human PRO1153 (UNQ583) protein sequence   1023   99                   SEQ ID NO: 351.       458   gi1364247     Sus scrofa     Ca(2+)-transport ATPase (AA 989-1042); non-   57   38                   muscle isoform (1 is 3rd base in codon)       458   AAB65991     Homo sapiens     Human secreted protein BLAST search protein   73   34                   SEQ ID NO: 131.       458   AAB65992     Homo sapiens     Human secreted protein BLAST search protein   73   34                   SEQ ID NO: 132.       459   gi2150146     Mus musculus     sulfonylurea receptor 2A   634   73       459   gi8843832     Rattus     sulphonylurea receptor 2b   375   73                 norvegicus         459   gi3127175     Homo sapiens     sulfonylurea receptor 2A (SUR2) gene,   372   74                   alternatively spliced product, exon 38a and                   complete cds.       460   gi4467773     Helicobacter     cytotoxin associated protein A   60   34                 pylori         460   gi7248699     Helicobacter     cytotoxin associated protein CagA   60   34                 pylori         460   gi5851989     Helicobacter     cytotoxin associated protein A   59   31                 pylori         461   gi13278675     Homo sapiens     clone MGC: 11170, mRNA, complete cds.   77   41       461   gi6457690     Deinococcus     2-oxo acid dehydrogenase, E2 component   90   31                 radiodurans         461   gi179521     Homo sapiens     Human bullous pemphigoid (BP180) mRNA,   72   36                   partial cds.       462   AAB52176     Homo sapiens     Human secreted protein BLAST search protein   468   95                   SEQ ID NO: 132.       462   AAR27651     Homo sapiens     Human calcium channel 27980/13.   117   26       462   gi179764     Homo sapiens     Human neuronal DHP-sensitive, voltage-   117   26                   dependent, calcium channel alpha-1D subunit                   mRNA, complete cds.       463   gi13623421     Homo sapiens     Similar to RIKEN cDNA 5730589L02 gene,   495   98                   clone MGC: 13124, mRNA, complete cds.       463   gi12803383     Homo sapiens     clone MGC: 2099, mRNA, complete cds.   189   100       463   gi13111983     Homo sapiens     clone MGC: 4221, mRNA, complete cds.   189   100       464   AAW75100     Homo sapiens     Human secreted protein encoded by gene 44   121   83                   clone HE8CJ26.       464   gi11275978     Homo sapiens     NOTCH 2 (N2) mRNA, complete cds.   125   87       464   AAY06816     Homo sapiens     Human Notch2 (humN2) protein sequence.   125   87       465   gi2696709     Mus musculus     RST   258   43       465   gi2687858     Pseudopleuron     renal organic anion transporter   236   40                 ectes                 americanus       465   gi4586315     Homo sapiens     ORCTL3 mRNA for organic-cation transporter   232   37                   like 3, complete cds.       466   gi11463949     Homo sapiens     hUGTrel7 mRNA for UDP-glucuronic acid,   256   100                   complete cds.       466   AAB60119     Homo sapiens     Human transport protein TPPT-39.   175   63       466   AAB56473     Homo sapiens     Human prostate cancer antigen protein sequence   175   63                   SEQ ID NO: 1051.       467   AAB88377     Homo sapiens     Human membrane or secretory protein clone   370   94                   PSEC0113.       467   gi12656637     Mus musculus     equilibrative nucleoside transporter 3   109   25       467   gi3877156     Caenorhabditis     F44D12.9   92   32                 elegans         468   gi9828006     Leishmania     probable ctg26 alteRNAte open reading frame   60   40                 major         468   gi4096496     Homo sapiens     Human pre-B cell Ig heavy chain mRNA, third   55   47                   complementarity-determining region, clone                   PBT-55, partial cds.       468   gi3005708     Homo sapiens     clone 23619 phosphoprotein mRNA, partial cds.   66   33       469   gi1339910     Homo sapiens     Human DOCK180 protein mRNA, complete   121   54                   cds.       469   AAW03515     Homo sapiens     Human DOCK180 protein.   121   54       469   gi13195147     Mus musculus     HCH   107   61       470   gi11036344     Pichia     NADH dehydrogenase subunit 4L   69   38                 canadensis         470   gi10175432     Bacillus     D-alanine aminotransferase   87   35                 halodurans         470   gi10639223     Thermoplasma     ethanolamine permease related protein   88   27                 acidophilum         471   AAB90654     Homo sapiens     Human secreted protein, SEQ ID NO: 197.   58   29       471   AAY36085     Homo sapiens     Extended human secreted protein sequence,   56   34                   SEQ ID NO: 470.       471   gi3617829     Gallus gallus     gallinacin 1 prepropeptide   55   42       472   gi14189735     Homo sapiens     ATP-binding cassette transporter family A   251   43                   member 12 (ABCA12) mRNA, complete cds.       472   gi14209834     Mus musculus     ATP-binding cassette transporter sub-family A   199   39                   member 7       472   gi9211112     Homo sapiens     macrophage ABC transporter (ABCA7) mRNA,   196   40                   complete cds.       473   gi8919747   Cottontail   e8   65   36               rabbit               papillomavirus       473   gi8919568   Cottontail   E8   64   36               rabbit               papillomavirus       473   gi5679184     Xanthomonas     HrcU homolog   80   25                 campestris  pv.               glycines       474   AAY30817     Homo sapiens     Human secreted protein encoded from gene 7.   569   98       474   gi3411233     Mus musculus     IER5   107   37       474   AAG02396     Homo sapiens     Human secreted protein, SEQ ID NO: 6477.   85   61       475   AAY99353     Homo sapiens     Human PRO1415 (UNQ731) amino acid   1435   99                   sequence SEQ ID NO: 50.       475   AAB88426     Homo sapiens     Human membrane or secretory protein clone   1428   99                   PSEC0199.       475   gi11230635     Homo sapiens     CD30 gene for cytokine receptor CD30, exons   106   29                   1-8.       476   gi6636340     Rattus     myosin heavy chain Myr 8   157   61                 norvegicus         476   gi10863773     Rattus     myosin heavy chain Myr 8b   157   61                 norvegicus         476   AAB51865     Homo sapiens     Human secreted protein sequence encoded by   71   31                   gene 39 SEQ ID NO: 98.       477   gi213109     Discopyge     synaptic vesicle protein   75   36                 ommata         477   gi1679584     Cavia     membrane cofactor protein precursor   80   37                 porcellus         477   gi1655471     Cavia     membrane cofactor protein(GMP1-full)   80   37                 porcellus         478   gi14330016     Mus musculus     bM401L17.2.1 (cholinergic receptor, nicotinic,   164   50                   alpha polypeptide 4 (isoform 1))       478   gi9886085     Mus musculus     nicotinic acetlycholine receptor alpha 4 subunit   164   50       478   gi14330017     Mus musculus     bM401L17.2.2 (cholinergic receptor, nicotinic,   164   50                   alpha polypeptide 4 (isoform 2))       479   gi409995     Rattus sp.     mucin   137   47       479   gi4995986   Human   13.6% identical to DR8 gene of strain U1102 of   135   32               herpesvirus 6   HHV-6       479   gi2388546     Homo sapiens     Human Xq28 BAC RP11-159I8 (Roswell Park   118   37                   Cancer Institute Human BAC Library), Cosmid                   LL0XNC01-3C3 (LLNL X Chromsome                   Library), and BAC GS1-92B2 (Genome                   Systems Human BAC Library) complete                   sequence.       480   AAY58174     Homo sapiens     Human embryogenesis protein, EMPRO.   872   96       480   gi3879940     Caenorhabditis     Similarity to Mouse H(beta)58 protein   650   67                 elegans     (SW: HB58_MOUSE)       480   gi3342000     Homo sapiens     H beta 58 homolog   666   70       481   gi13359817     Escherichia     high-affinity choline transport   1021   100                 coli  O157:H7       481   gi1657512     Escherichia     high-affinity choline transport protein   1021   100                 coli         481   gi1786506     Escherichia     high-affinity choline transport   1021   100                 coli  K12       482   gi10584129   Halobacterium   Vng6071c   81   27               sp. NRC-1       482   gi10584473   Halobacterium   Vng6455c   81   27               sp. NRC-1       482   gi12723038     Lactococcus     UNKNOWN PROTEIN   58   28                 lactis  subsp.               lactis       483   gi13364609     Escherichia     fumarate reductase FrdD   515   96                 coli  O157:H7       483   gi145266     Escherichia     g13 protein   515   96                 coli         483   gi1790594     Escherichia     fumarate reductase, anaerobic, membrane   515   96                 coli  K12   anchor polypeptide       484   gi1160319     Escherichia     aldohexuronate transport system   928   96                 coli         484   gi13363448     Escherichia     transport protein of hexuronates   928   96                 coli  O157:H7       484   gi2367193     Escherichia     transport of hexuronates   928   96                 coli  K12       485   gi395270     Escherichia     FepE   402   100                 coli         485   gi1786802     Escherichia     ferric enterobactin (enterochelin) transport   402   100                 coli  K12       485   gi1778503     Escherichia     ferric enterobactin transport protein   402   100                 coli         486   gi145521     Escherichia     methyl-accepting chemotaxis protein II   411   73                 coli         486   gi1736539     Escherichia     Methyl-accepting chemotaxis protein II (MCP-   411   73                 coli     II) (Aspartate chemoreceptor protein).       486   gi1788195     Escherichia     methyl-accepting chemotaxis protein II,   411   73                 coli  K12   aspartate sensor receptor       487   gi14456429     Equus caballus     galanin receptor 1   69   28       487   gi3282259     Cucumaria     ND4L   69   30                 pseudocurata         487   gi3282257     Cucumaria     ND4L   68   30                 miniata         488   gi3702702   bacteriophage   Vpf77   65   30               Vf33       488   gi3702711   bacteriophage   Vpf77   65   30               Vf12       488   gi1742947   Alcaligenes sp.   urf-1 (merE)   64   31       489   gi263516     Azospirillum     NifB {N-terminal}   58   39                 brasilense ,               Sp7, Peptide               Partial, 70 aa       489   gi9622741     Conus catus     four-loop conotoxin precursor   57   33       489   gi149569   Lactobacillus   lactacin F   56   40               sp.       490   gi896286     Leishmania     NH2 terminus uncertain   123   19                 tarentolae         490   gi4155384     Helicobacter     IRON(III) DICITRATE TRANSPORT   120   27                 pylori  J99   SYSTEM PERMEASE PROTEIN       490   gi1542807     Asterina     NADH-dehydrogenase subunit 4L   98   27                 pectinifera         491   AAB88433     Homo sapiens     Human membrane or secretory protein clone   299   55                   PSEC0210.       491   gi6996444     Homo sapiens     CTL2 gene.   299   55       491   AAB24284     Homo sapiens     Human H38087 (clone GTB6) protein sequence   295   54                   SEQ ID NO: 7.       492   gi6807868     Homo sapiens     mRNA; cDNA DKFZp434G0625 (from clone   324   68                   DKFZp434G0625); partial cds.       492   AAY13373     Homo sapiens     Amino acid sequence of protein PRO235.   209   62       492   AAB33420     Homo sapiens     Human PRO235 protein UNQ209 SEQ ID   209   62                   NO: 31.       493   gi10434911     Homo sapiens     cDNA FLJ13068 fis, clone NT2RP3001739,   573   100                   weakly similar to HYPOTHETICAL 72.5 KD                   PROTEIN C2F7.10 IN CHROMOSOME I.       493   gi7022673     Homo sapiens     cDNA FLJ10562 fis, clone NT2RP2002701.   109   43       493   AAY87090     Homo sapiens     Human secreted protein sequence SEQ ID   109   43                   NO: 129.       494   AAB63630     Homo sapiens     Human gastric cancer associated antigen protein   165   55                   sequence SEQ ID NO: 992.       494   AAB63629     Homo sapiens     Human gastric cancer associated antigen protein   170   55                   sequence SEQ ID NO: 991.       494   AAR06471     Homo sapiens     Derived protein from clone ICA525 (ATCC   172   55                   40704).       495   gi13543949     Homo sapiens     Similar to RIKEN cDNA 2810432L12 gene,   2104   100                   clone MGC: 12992, mRNA, complete cds.       495   AAY87340     Homo sapiens     Human signal peptide containing protein HSPP-   2104   100                   117 SEQ ID NO: 117.       495   gi3876730     Caenorhabditis     F35C11.4   181   27                 elegans         496   gi5001993     Dissostichus     chimeric AFGP/trypsinogen-like serine protease   199   49                 mawsoni     precursor       496   gi295736     Dictyostelium     spore coat protein sp96   189   48                 discoideum         496   gi2114321     Equine     membrane glycoprotein   186   39                 herpesvirus  1       497   AAB66272     Homo sapiens     Human TANGO 378 SEQ ID NO: 29.   664   89       497   gi6006811     Mus musculus     serpentine receptor   261   40       497   AAB01247     Homo sapiens     Human HE6 receptor.   263   38       498   gi13623515     Homo sapiens     clone MGC: 12705, mRNA, complete cds.   94   87       498   gi1017781   bacteriophage   Rz1 protein precursor   44   41               lambda       498   gi6599136     Homo sapiens     mRNA; cDNA DKFZp434F216 (from clone   94   87                   DKFZp434F216); partial cds.       499   AAC84384 —       Homo sapiens     Human A236 polypeptide coding sequence.   693   100           aa1       499   gi10438797     Homo sapiens     cDNA: FLJ22415 fis, clone HRC08561.   692   100       499   AAY41692     Homo sapiens     Human PRO 363 protein sequence.   692   100       500   gi8515813     Rattus     RSD-6   84   25                 norvegicus         500   gi12657809   Simian   gag protein   83   25               immunodeficiency               virus       500   gi9454456   Human   pol protein   60   35               immunodeficiency               virus type 1       501   AAY71056     Homo sapiens     Human membrane transport protein, MTRP-1.   143   76       501   gi13096889     Mus musculus     Similar to ATPas, class II, type 9B   142   68       501   gi13905302     Mus musculus     Similar to ATPase, class II, type 9A   119   63       502   gi2384752     Paracentrotus     transcription factor; PaxA   56   47                 lividus         502   gi6601486     Ovis aries     pulmonary surfactant protein B   76   30       502   AAR41266     Homo sapiens     vWF fragment Arg441-Tyr508, deltaCys474-   56   47                   Pro488.       503   AAY99420     Homo sapiens     Human PRO1486 (UNQ755) amino acid   1082   100                   sequence SEQ ID NO: 287.       503   AAW88747     Homo sapiens     Secreted protein encoded by gene 45 clone   1069   99                   HCESF40.       503   gi6942096     Mus musculus     CBLN3   942   94       504   gi11558496     Sus scrofa     sodium iodide symporter   170   51       504   gi12642414     Mus musculus     sodium iodide symporter NIS   184   39       504   gi14290145     Mus musculus     sodium iodide symporter   184   39       505   AAY66645     Homo sapiens     Membrane-bound protein PRO1310.   554   100       505   AAB65168     Homo sapiens     Human PRO1310 protein sequence SEQ ID   554   100                   NO: 62.       505   gi2921092     Mus musculus     carboxypeptidase X2   281   58       507   gi58442   Human   8.0 K protein (AA 1-74)   56   44               adenovirus               type 41       507   gi388253     Trifolium     ribulose bisphosphate carboxylase   54   32                 repens         507   gi1345574     Sinapis alba     small subunit ribulose 1,5-bisphosphate   57   36                   carboxylase (AA 1-82)       508   gi3047402     Homo sapiens     monocarboxylate transporter 2 (hMCT2)   539   34                   mRNA, complete cds.       508   gi7688756     Mus musculus     monocarboxylate transporter 4   296   48       508   gi3834395     Homo sapiens     monocarboxylate transporter 2 (MCT2) mRNA,   528   33                   complete cds.       509   gi6136782     Mus musculus     synaptotagmin V   595   91       509   gi14210264     Rattus     synaptotagmin 5   592   91                 norvegicus         509   gi6136792     Mus musculus     synaptotagmin X   268   43       510   AAB53400     Homo sapiens     Human colon cancer antigen protein Sequence   493   100       510   gi6760350     Homo sapiens     cytomegalovirus partial fusion receptor mRNA,   348   98                   partial cds.       510   gi603380     Saccharomyces     Yer140wp   106   30                 cerevisiae         511   AAB12136     Homo sapiens     Hydrophobic domain protein from clone   1142   100                   HP10625 isolated from Liver cells.       511   AAB24036     Homo sapiens     Human PRO4407 protein sequence SEQ ID   1142   100                   NO: 47.       511   AAY57952     Homo sapiens     Human transmembrane protein HTMPN-76.   1142   100       512   gi2654984   Hepatitis GB   polyprotein   50   38               virus C       512   gi861305     Caenorhabditis     similar to  C. elegans  protein F59B2.2   75   32                 elegans         512   AAW75055     Homo sapiens     Fragment of human secreted protein encoded by   52   38                   gene 18.       513   gi2696709     Mus musculus     RST   95   47       513   gi1293672     Mus musculus     kidney-specific transport protein   93   40       513   gi7707622     Homo sapiens     hOAT4 mRNA for organic anion transporter 4,   93   37                   complete cds.       514   gi17829     Brassica napus     LEA76 peptide (AA 1-280)   137   27       514   gi11994339     Arabidopsis     embryonic abundant protein LEA-like   119   28                 thaliana         514   gi3873646     Caenorhabditis     AC3.3   123   27                 elegans         515   AAB74753     Homo sapiens     Human secreted protein sequence encoded by   38   54                   gene 21 SEQ ID NO: 62.       515   gi2369777     Drosophila     sex-peptide   39   53                 mauritiana         515   gi2369804     Drosophila     sex-peptide   39   53                 simulans         516   gi13959739   Caprine   envelope glycoprotein   87   33               arthritis-               encephalitis               virus       516   gi5732606   Hepatitis B   precore/core mutant protein   74   33               virus       516   gi4033542   Hepatitis B   truncated pre-core-protein   72   34               virus       517   gi1336041     Homo sapiens     Human olfactory receptor (OLF1) gene,   482   50                   complete cds.       517   gi1246530     Gallus gallus     olfactory receptor 2   474   50       517   gi1246534     Gallus gallus     olfactory receptor 4   474   50       518   AAY36243     Homo sapiens     Human secreted protein encoded by gene 20.   64   48       518   gi409995   Rattus sp.   mucin   65   57       518   gi11141770     Bos taurus     Toll-like receptor 4   80   29       519   gi8918871   Plasmid F   96 pct identical to gp: AB021078_30   288   98       519   gi4512467   Plasmid ColIb-   100 pct identical to 25 residues of 79 aa protein   256   93               P9   sp: YPF8_ECOLI       519   gi47517   Synechocystis   ATPase subunit epsilon   72   45               sp. PCC 6803       520   gi5139695     Cucumis     expressed in cucumber hypocotyls   85   28                 sativus         520   gi3406819     Mus musculus     growth factor receptor   63   47       520   AAG03497     Homo sapiens     Human secreted protein, SEQ ID NO: 7578.   61   51       521   AAB18985     Homo sapiens     Amino acid sequence of a human   251   35                   transmembrane protein.       521   gi6013381     Rattus     TM6P1   246   33                 norvegicus         521   AAE00330     Homo sapiens     Human membrane-bound protein-60 (Zsig60).   251   35       523   gi1046315     Plasmodium     merozoite surface protein-1   88   34                 vivax         523   gi2213834     Plasmodium     merozite surface protein 1   85   29                 vivax         523   gi537916     Lilium     meiotin-1   87   32                 longiflorum         524   AAY91618     Homo sapiens     Human secreted protein sequence encoded by   63   29                   gene 20 SEQ ID NO: 291.       524   AAG02988     Homo sapiens     Human secreted protein, SEQ ID NO: 7069.   58   29       525   gi220411     Mus musculus     N-methyl-D-aspartate receptor channel subunit   159   100                   epsilon 1       525   gi286234     Rattus     N-methyl-D-aspartate receptor subunit   159   100                 norvegicus         525   gi2155310     Rattus     N-methyl-D-aspartate receptor NMDAR2A   159   100                 norvegicus     subunit; NMDA receptor NMDAR2A subunit       526   AAB66267     Homo sapiens     Human TANGO 272 SEQ ID NO: 14.   697   50       526   AAY72712     Homo sapiens     HTLIH44 clone human attractin-like protein.   570   47       526   AAY72715     Homo sapiens     HFICU08 clone human attractin-like protein.   565   47       527   gi2384746     Mus musculus     testicular condensing enzyme   681   52       527   gi4633135     Mus musculus     condensing enzyme   681   52       527   gi12652723     Homo sapiens     clone MGC: 3295, mRNA, complete cds.   276   29       528   gi12224992     Homo sapiens     mRNA; cDNA DKFZp667O2416 (from clone   877   100                   DKFZp667O2416).       528   gi4929647     Homo sapiens     CGI-89 protein mRNA, complete cds.   603   61       528   gi12652585     Homo sapiens     CGI-89 protein, clone MGC: 845, mRNA,   602   60                   complete cds.       529   AAY36047     Homo sapiens     Extended human secreted protein sequence,   61   57                   SEQ ID NO. 432.       529   AAG01318     Homo sapiens     Human secreted protein, SEQ ID NO: 5399.   59   44       529   AAW74979     Homo sapiens     Human secreted protein encoded by gene 105   58   35                   clone HSVAF07.       530   gi12314108     Homo sapiens     Human DNA sequence from clone RP1-23013   634   100                   on chromosome 6q22.1-22.33 Contains part of a                   gene for a novel protein, STSs and GSSs,                   complete sequence.       530   gi10434835     Homo sapiens     cDNA FLJ13018 fis, clone NT2RP3000685.   435   68       530   gi1491712     Homo sapiens       H. sapiens  mRNA for novel protein.   95   56       532   gi861305     Caenorhabditis     similar to  C. elegans  protein F59B2.2   124   30                 elegans         532   gi10177114     Arabidopsis     amino acid transporter protein-like   91   34                 thaliana         532   gi2576363     Arabidopsis     amino acid transport protein   79   29                 thaliana         533   AAY28678     Homo sapiens     Human cw272_7 secreted protein.   324   38       533   gi13185723     Homo sapiens     n 1755 can be A, G, C, or T   248   30       533   AAB70537     Homo sapiens     Human PRO7 protein sequence SEQ ID NO: 14.   248   30       534   gi10186503     Homo sapiens     sialic acid-specific acetylesterase II mRNA,   932   100                   complete cds, alternatively spliced.       534   gi6808138     Homo sapiens     mRNA; cDNA DKFZp761A051 (from clone   923   100                   DKFZp761A051); partial cds.       534   gi10242345     Homo sapiens     sialic acid-specific 9-O-acetylesterase I mRNA,   753   100                   complete cds.       535   gi7328084     Homo sapiens     mRNA; cDNA DKFZp761L0812 (from clone   225   82                   DKFZp761L0812); partial cds.       535   gi7576817     Plasmodium     merozoite surface protein 2   94   38                 falciparum         535   gi3261822     Mycobacterium     PE_PGRS   103   36                 tuberculosis         536   gi3165565     Caenorhabditis     contains similarity to transmembrane domains   129   25                 elegans     found in HMG CoA reductases and drosophila                   patched protein (SW: P18502)       536   gi1825729     Caenorhabditis     similar to drosophila membrane protein   125   26                 elegans     PATCHED SP: P18502 (PID: g129645)       536   gi15120   enterobacteria   unidentified reading frame   67   31               phage P1       537   gi13452508     Mus musculus     claudin 14   438   40       537   gi12597447     Homo sapiens     claudin 14 (CLDN14) mRNA, complete cds.   438   39       537   gi7768724     Homo sapiens     genomic DNA. chromosome 21q, section   438   39                   70/105.       538   AAR12603     Homo sapiens     SIB 121 intestinal mucin.   148   53       538   AAW36946     Homo sapiens     Protein encoded by 5’ fragment of clone M8_2.   92   35       538   AAY91378     Homo sapiens     Human secreted protein sequence encoded by   86   45                   gene 33 SEQ ID NO: 99.       539   gi13561518     Homo sapiens     GalNAc-4-sulfotransferase 2 mRNA, complete   213   97                   cds, alternatively spliced.       539   gi12711481     Homo sapiens     N-acetylgalactosamine 4-O-sulfotransferase 2   187   97                   GalNAc4ST-2 mRNA, complete cds.        539   AAY86315     Homo sapiens     Human secreted protein HNTMX29, SEQ ID   63   27                   NO: 230.       540   gi3150438   Human   pol-env   264   51               endogenous               retrovirus K       540   gi3150441   Human   envelope protein   258   50               endogenous               retrovirus K       540   gi5802817     Homo sapiens     endogenous retrovirus HERV-K104 long   258   51                   terminal repeat, complete sequence; and Gag                   protein (gag) and envelope protein (env) genes,                   complete cds.       541   AAY91625     Homo sapiens     Human secreted protein sequence encoded by   547   97                   gene 22 SEQ ID NO: 298.       541   AAU00437     Homo sapiens     Human dendritic cell membrane protein FIRE.   547   97       541   AAW30638     Homo sapiens     Partial human 7-transmembrane receptor   374   66                   HAPO167 protein.       542   AAY96963     Homo sapiens     Wound healing tissue peptidoglycan recognition   1811   92                   protein-like protein.       542   AAY96962     Homo sapiens     Keratinocyte peptidoglycan recognition protein-   768   62                   like protein.       542   AAY76124     Homo sapiens     Human secreted protein encoded by gene 1.   768   62       543   AAB72286     Homo sapiens     Human ADAMTS-9 amino acid sequence.   1009   100       543   AAB72301     Homo sapiens     Human ADAMTS-9 alternative amino acid   1009   100                   sequence.       543   AAB90617     Homo sapiens     Human secreted protein, SEQ ID NO: 155.   358   39       544   gi4323581     Homo sapiens     senescence-associated epithelial membrane   150   100                   protein (SEMP1) mRNA, complete cds.       544   gi4559278     Homo sapiens     claudin-1 (CLDN1) mRNA, complete cds.   150   100       544   gi13383364     Homo sapiens     claudin-1 (CLDN1) gene, exon 4 and complete   150   100                   cds.       545   AAW93960     Homo sapiens     Human 53BP2: IP-2 protein fragment.   59   45       545   AAY19607     Homo sapiens     SEQ ID NO 325 from WO9922243.   57   64       545   AAY07942     Homo sapiens     Human secreted protein fragment encoded from   55   42                   gene 91.       546   gi4406172   Human   latent membrane protein-1   159   37               herpesvirus 4       546   gi475574   Human   latent membrane protein 1   153   39               herpesvirus 4               type 2       546   gi2736358     Caenorhabditis     Contains similarity to Pfam domain: PF00069   155   51                 elegans     (pkinase), Score = 214.7, E-value = 4.3e−61,                   N = 1       547   gi552087     Drosophila     crumbs protein   127   45                 melanogaster         547   AAY66747     Homo sapiens     Membrane-bound protein PRO1158.   67   46       547   AAB87559     Homo sapiens     Human PRO1158.   67   46       548   AAB39181     Homo sapiens     Human secreted protein sequence encoded by   57   41                   gene 3 SEQ ID NO: 61.       549   AAW71565     Homo sapiens     Hepatocyte nuclear factor 4 alpha polypeptide   44   36                   (exon 2 product).       549   gi2804240     Rattus     histidase   56   42                 norvegicus         549   gi149163   Plasmid pJHC-   streptomycin-spectinomycin resistance protein   65   71               MW1       550   gi10435833     Homo sapiens     cDNA FLJ13729 fis, clone PLACE3000121,   233   100                   weakly similar to VESICULAR TRAFFIC                   CONTROL PROTEIN SEC15.       550   gi6807998     Homo sapiens     mRNA; cDNA DKFZp761I2124 (from clone   195   80                   DKFZp761I2124); partial cds.       550   gi7023795     Homo sapiens     cDNA FLJ11251 fis, clone PLACE1008813.   195   80       551   gi5668598     Homo sapiens     Wiskott-Aldrich syndrome protein interacting   156   33                   protein (WASPIP) mRNA, partial cds.       551   gi1314755     Mus musculus     Wiskott-Aldrich Syndrome Protein   140   33       551   gi4096355     Mus musculus     Wiskott-Aldrich syndrome protein (WASP)   140   33       552   gi4886381   Human   E5 protein   54   36               papillomavirus               type 16       552   AAB28331     Homo sapiens     Human secreted protein BLAST search protein   54   36                   SEQ ID NO: 115.       552   gi4886413   Human   E5 protein   53   26               papillomavirus               type 16       553   gi12276062     Homo sapiens     group XII secreted phospholipase A2 mRNA,   354   100                   complete cds.       553   gi12276193     Homo sapiens     FKSG38 (FKSG38) mRNA, complete cds.   354   100       553   AAY88271     Homo sapiens     Human TANGO 180 protein.   354   100       554   gi4885010     Conus textile     O-superfamily conotoxin TxO5 precursor   73   26       554   gi6409400     Conus textile     conotoxin scaffold VI/VII precursor   71   25       554   AAW78192     Homo sapiens     Human secreted protein encoded by gene 67   67   39                   clone HTOFC34.       555   AAB38330     Homo sapiens     Human secreted protein encoded by gene 10   214   97                   clone HTEBV72.       555   gi2335059     Mus musculus     IgG receptor   76   52       555   gi969034     Mus musculus     Fc gamma receptor IIb1   76   52       556   gi13311009     Homo sapiens     NYD-SP16 mRNA, complete cds.   488   100       556   gi3287162   Human   vpu   69   26               immunodeficiency               virus type 1       556   gi1303982     Bacillus     YqkE   59   40                 subtilis         557   gi13938651     Mus musculus     Similar to conserved membrane protein at 44E   502   83       557   gi14194169     Arabidopsis     At1g05960/T21E18_20   124   30                 thaliana         557   gi265786   human,   betacellulin. [Homo   75   57               mRNA, 1271               nt       558   gi310100     Rattus     developmentally regulated protein   539   80                 norvegicus         558   AAW52812     Homo sapiens     Human induced tumor protein.   227   37       558   AAY07771     Homo sapiens     Human secreted protein fragment encoded from   221   40                   gene 28.       559   AAY71294     Homo sapiens     Human orphan G protein-coupled receptor   1711   100                   hRUP3.       559   AAB02828     Homo sapiens     Human G protein coupled receptor hRUP3   1711   100                   protein SEQ ID NO: 8.       559   gi1204095     Takifugu     dopamine receptor   237   28                 rubripes         560   gi3041879     Mus musculus     LNXp80   556   54       560   gi3041881     Mus musculus     LNXp70   556   54       560   gi13183073     Homo sapiens     multi-PDZ-domain-containing protein mRNA,   539   56                   complete cds.       561   AAB08872     Homo sapiens     Amino acid sequence of a human secretory   77   93                   protein.       561   gi5734537     Methanotherm     transmembrane protein 9.0 kDa   62   43                 obacter                 thermautotrophicus       561   gi13357178     Homo sapiens     calcium channel gamma subunit 7 (CACNG7)   78   38                   mRNA, complete cds.       562   gi5070458   tomato yellow   BV2 protein   60   33               leaf curl virus       562   gi9944667   Amsacta   AMV144   60   26               moorei               entomopoxvirus       562   gi293853     Mus musculus     betacellulin   48   25       563   gi10799398     Homo sapiens     chromosome 19, BAC BC349142 (CTC-   1513   100                   518B2), complete sequence.       563   gi6063386     Homo sapiens     kallikrein-like protein 4 KLK-L4 gene, complete   1513   100                   cds.       563   gi4884462     Homo sapiens     mRNA; cDNA DKFZp586J1923 (from clone   912   98                   DKFZp586J1923); partial cds.       564   AAB90602     Homo sapiens     Human secreted protein, SEQ ID NO: 140.   704   100       564   AAB90662     Homo sapiens     Human secreted protein, SEQ ID NO: 205.   704   100       564   AAB90571     Homo sapiens     Human secreted protein, SEQ ID NO: 109.   700   99       565   AAB53436     Homo sapiens     Human colon cancer antigen protein sequence   82   33                   SEQ ID NO: 976.       565   AAG02279     Homo sapiens     Human secreted protein, SEQ ID NO: 6360.   82   61       565   gi3879077     Caenorhabditis     R10E11.9   81   35                 elegans         566   gi581191     Escherichia     unidentified reading frame (AA 1-79)   64   36                 coli         566   gi929915   synthetic   insulin C chain   61   58               construct       566   AAP60248     Homo sapiens     Human proinsulin.   61   58       567   AAB08854     Homo sapiens     Amino acid sequence of a human secretory   787   100                   protein.       567   AAY87268     Homo sapiens     Human signal peptide containing protein HSPP-   787   100                   45 SEQ ID NO: 45.       567   AAY66723     Homo sapiens     Membrane-bound protein PRO1100.   787   100       568   gi14211714     Homo sapiens     naked cuticle-1 (NKD1) mRNA, complete cds.   193   92       568   AAB08216     Homo sapiens     A protein related to Drosophila naked cuticle   193   92                   polypeptide.       568   gi13487305     Mus musculus     Nkd   151   62       569   gi3452275     Pleuronectes     aminopeptidase N   215   28                 americanus         569   gi2766187     Gallus gallus     aminopeptidase Ey   178   32       569   gi3776238     Rattus     aminopeptidase N   151   29                 norvegicus         570   AAB58305     Homo sapiens     Lung cancer associated polypeptide sequence   273   100                   SEQ ID 643.       570   gi5830684   variola minor   A20L protein   57   24               virus       570   gi297302   Variola virus   A19L   57   24       571   AAB38019     Homo sapiens     Human secreted protein encoded by gene 27   583   99                   clone HPJBF63.       571   AAB38010     Homo sapiens     Human secreted protein encoded by gene 27   576   98                   clone HOUHD63.       571   gi167020     Hordeum     C-hordein storage protein   47   27                 vulgare         572   AAY91385     Homo sapiens     Human secreted protein sequence encoded by   969   100                   gene 40 SEQ ID NO: 106.       572   gi4126441     Homo sapiens     CD22 gene variant 6, partial cds.   68   34       572   gi201798     Mus musculus     T-cell receptor beta   95   29       573   gi9971734     Galleria     heavy-chain fibroin   121   34                 mellonella         573   gi3002791     Homo sapiens     macrophage receptor MARCO mRNA,   81   28                   complete cds.       573   gi5231092     Homo sapiens     macrophage receptor (MARCO) gene, exon 17   81   28                   and complete cds.       574   gi409995   Rattus sp.   mucin   173   64       574   gi4063042     Cryptosporidium     GP900; mucin-like glycoprotein   134   38                 parvum         574   gi5732924     Toxocara canis     excretory/secretory mucin MUC-4   112   29       575   gi1841555     Homo sapiens     HLA class III region containing NOTCH4 gene,   422   100                   partial sequence, homeobox PBX2 (HPBX)                   gene, receptor for advanced glycosylation end                   products (RAGE) gene, complete cds, and 6                   unidentified cds, complete sequence.       575   AAB25697     Homo sapiens     Human secreted protein sequence encoded by   122   40                   gene 33 SEQ ID NO: 86.       575   AAB25755     Homo sapiens     Human secreted protein sequence encoded by   122   40                   gene 33 SEQ ID NO: 144.       576   gi5732924     Toxocara canis     excretory/secretory mucin MUC-4   114   34       576   gi5732920     Toxocara canis     excretory/secretory mucin MUC-2   113   32       576   gi409995   Rattus sp.   mucin   95   29       577   gi12656447     Plasmodium     erythrocyte membrane protein 1   73   33                 falciparum         577   AAG04067     Homo sapiens     Human secreted protein, SEQ ID NO: 8148.   73   51       577   gi4200249     Homo sapiens       H. sapiens  gene from PAC 747L4.   76   32       578   gi12003279     Perilla     15 kD oleosin-like protein 1   77   36                 frutescens         578   gi409424     Homo sapiens     Human carboxyl ester lipase like protein   59   32                   (CELL) mRNA, complete cds.       578   gi609286     Xenopus     xsna   79   30                 laevis         579   gi1841555     Homo sapiens     HLA class III region containing NOTCH4 gene,   80   42                   partial sequence, homeobox PBX2 (HPBX)                   gene, receptor for advanced glycosylation end                   products (RAGE) gene, complete cds, and 6                   unidentified cds, complete sequence.       579   AAB18976     Homo sapiens     Amino acid sequence of a human   69   40                   transmembrane protein.       579   AAW73192     Homo sapiens     Human vesicle trafficking protein.   43   38       580   gi13241972     Mus musculus     SugarCrisp   841   56       580   gi13241970     Gallus gallus     SugarCrisp   840   59       580   gi2943716     Homo sapiens     mRNA for 25 kDa trypsin inhibitor, complete   840   63                   cds.       581   gi4584539     Arabidopsis     extensin-like protein   138   34                 thaliana         581   gi306316   Herpesvirus   EBNA-2   171   38               papio       581   gi1632787   Human   BYRF1, encodes EBNA-2 (Dambaugh et al,   142   35               herpesvirus 4   1984; Dillner et al, 1984)       582   gi13185723     Homo sapiens     n 1755 can be A, G, C, or T   373   100       582   AAB70537     Homo sapiens     Human PRO7 protein sequence SEQ ID NO: 14.   373   100       582   gi13185725     Homo sapiens     n 1755 can be A, G, C, or T.   373   100       583   gi202752     Rattus     adenylyl cyclase type II   261   59                 norvegicus         583   AAB02006     Homo sapiens     Adenylyl cyclase type II-C2 C2 alpha domain.   261   59       583   gi2204110     Bos taurus     adenylyl cyclase type VII   138   50       584   gi10433645     Homo sapiens     cDNA FLJ12221 fis, clone MAMMA1001091.   1086   69       584   gi10440418     Homo sapiens     mRNA for FLJ00044 protein, partial cds.   1086   69       584   AAB56941     Homo sapiens     Human prostate cancer antigen protein sequence   126   28                   SEQ ID NO: 1519.       585   AAY99402     Homo sapiens     Human PRO1382 (UNQ718) amino acid   492   98                   sequence SEQ ID NO: 220.       585   AAY32937     Homo sapiens     Human cerebellin-2 protein sequence.   300   70       585   gi5702371     Mus musculus     precerebellin-1   284   66       586   AAB44681     Homo sapiens     Human secreted protein sequence encoded by   361   63                   gene 41 SEQ ID NO: 146.       586   gi1293734     Saccharomyces     O3635p   279   34                 cerevisiae         586   gi13877141     Homo sapiens     FKSG89   162   33       587   AAY34120     Homo sapiens     Human potassium channel K+ Hnov4.   1597   99       587   gi206044     Rattus     potassium channel Kv3.2b   1582   98                 norvegicus         587   gi206914     Rattus     K+ channel protein   1582   98                 norvegicus         588   gi3790674     Caenorhabditis     contains similarity to a vac1/fab1-type domain   449   54                 elegans         589   AAB53626     Homo sapiens     Human colon cancer antigen protein sequence   55   47                   SEQ ID NO: 1166.       589   gi1049106     Homo sapiens     Human dystonin isoform 2 mRNA, partial cds.   63   100       589   gi470480     Homo sapiens     Human clone JL8 immunoglobulin kappa chain   58   34                   (IgK) mRNA, VKIII-JK3 region, partial cds.       590   AAY44985     Homo sapiens     Human epidermal protein-2.   82   37       590   gi11073     Drosophila     Mst84Da   75   37                 melanogaster         590   gi8571115     Homo sapiens     human endogenous retrovirus HRES-1 p8   75   40                   protein (p8) and p15 protein (p15) genes,                   complete cds.       591   gi13676322     Homo sapiens     chromosome 1 open reading frame 2, clone   230   31                   MGC: 1298, mRNA, complete cds.       591   gi13938585     Homo sapiens     clone MGC: 4509, mRNA, complete cds.   230   31       591   gi2564916     Homo sapiens     clk2 kinase (CLK2), propin1, cote1,   229   31                   glucocerebrosidase (GBA), and metaxin genes,                   complete cds; metaxin pseudogene and                   glucocerebrosidase pseudogene; and                   thrombospondin3 (THBS3) gene, partial cds.       592   gi56463     Rattus     gp210 (AA 1-1886)   363   79                 norvegicus         592   gi6650678     Mus musculus     nuclear pore membrane glycoprotein POM210   358   78       592   gi1703554     Caenorhabditis     strong similarity to rat integral membrane   143   32                 elegans     glycoprotein GP120 precursor (SP: P11654)       593   AAB73355     Homo sapiens     Human mesangial cell meg-1 protein.   317   52       593   gi4191594     Homo sapiens     protein serine/threonine phosphatase 4   292   52                   regulatory subunit 1 (PP4R1) mRNA, complete                   cds.       593   gi10120321     Salmo trutta     MHC class II alpha chain   58   30       594   gi11320944     Homo sapiens     peptide deformylase-like protein mRNA,   1300   100                   complete cds.       594   gi13195254     Homo sapiens     polypeptide deformylase-like protein (PDF)   1300   100                   mRNA, complete cds.       594   gi11320968     Lycopersicon     peptide deformylase-like protein   346   40                 esculentum         595   gi13279254     Homo sapiens     Similar to RIKEN cDNA 2610207I16 gene,   417   94                   clone MGC: 10940, mRNA, complete cds.       595   gi5869811     Glomus     Fox2 protein   187   30                 mosseae         595   gi432977     Homo sapiens     Human sterol carrier protein 2 mRNA, complete   174   32                   cds.       596   gi10803406     Homo sapiens     mRNA for cadherin-19 (CDH19 gene).   863   100       596   AAY41725     Homo sapiens     Human PRO941 protein sequence.   863   100       596   AAB44281     Homo sapiens     Human PRO941 (UNQ478) protein sequence   863   100                   SEQ ID NO: 264.       597   AAG02731     Homo sapiens     Human secreted protein, SEQ ID NO: 6812.   67   38       597   gi1841964     Toxocara canis     TcH SLdT.460   63   37       597   gi3986598     Ginglymostoma     antigen receptor   58   47                 cirratum         598   gi575501     Homo sapiens     thyrotropin beta-subunit (TSHB) gene, exon 3.   739   99       598   gi339998     Homo sapiens     Human thyrotropin beta (TSH-beta) subunit   739   99                   gene, exons 2 and 3.       598   gi340002     Homo sapiens     Human thyrotropin beta subunit gene, exons 2   739   99                   and 3.       599   AAB53436     Homo sapiens     Human colon cancer antigen protein sequence   368   97                   SEQ ID NO: 976.       599   AAB25691     Homo sapiens     Human secreted protein sequence encoded by   168   93                   gene 27 SEQ ID NO: 80.       599   AAY01428     Homo sapiens     Secreted protein encoded by gene 46 clone   81   42                   HAQBT52.       600   AAB54178     Homo sapiens     Human pancreatic cancer antigen protein   1025   99                   sequence SEQ ID NO: 630.       600   gi7321824     Drosophila     out at first   510   38                 melanogaster         600   gi2443448     Drosophila     out at first   508   39                 virilis         601   AAW75178     Homo sapiens     Human secreted protein encoded by gene 69   45   47                   clone HPEBD70.       601   gi6466876   Kashmir bee   RNA polymerase   72   43               virus       601   gi6646671   cloudy wing   RNA polymerase   72   43               virus       602   AAB88377     Homo sapiens     Human membrane or secretory protein clone   379   91                   PSEC0113.       602   gi190506     Homo sapiens     Human PRB1 locus salivary proline-rich protein   111   32                   mRNA, clone cP5, complete cds.       602   gi190475     Homo sapiens     Human salivary proline-rich protein 1 gene,   84   34                   segment 2.       603   gi1235645     Cladomyrma     cytochrome oxidase subunit II   57   50                 cryptata         603   gi4981606     Thermotoga     oligopeptide ABC transporter, permease protein   43   31                 maritima         603   gi6681644   Yaba monkey   similar to vaccinia A14.5L   55   45               tumor virus       604   gi7020918     Homo sapiens     cDNA FLJ20668 fis, clone KAIA585.   461   66       604   AAB54305     Homo sapiens     Human pancreatic cancer antigen protein   62   33                   sequence SEQ ID NO: 757.       604   AAY41352     Homo sapiens     Human secreted protein encoded by gene 45   58   21                   clone HTXFH55.       605   AAY54054     Homo sapiens     Angiostatin-binding domain of ABP-1,   137   39                   designated Big-3.       605   gi9887326     Homo sapiens     angiomotin mRNA, complete cds.   155   37       605   AAY54052     Homo sapiens     An angiogenesis-associated protein which binds   155   37                   plasminogen.       606   gi11072097     Homo sapiens     MLL/GAS7 fusion protein (MLL/GAS7)   83   25                   mRNA, partial cds.       606   gi7331837     Caenorhabditis     contains similarity to human X-linked deafness   60   25                 elegans     dystonia protein (GB: U66035)       606   AAG02452     Homo sapiens     Human secreted protein, SEQ ID NO: 6533.   59   44       607   gi854065   Human   U88   305   47               herpesvirus 6       607   gi9757150     Leishmania     extremely cysteine/valine rich protein   284   50                 major         607   gi10434098     Homo sapiens     cDNA FLJ12547 fis, clone NT2RM4000634.   219   38       608   AAY48278     Homo sapiens     Human prostate cancer-associated protein 64.   98   89       608   AAB58446     Homo sapiens     Lung cancer associated polypeptide sequence   98   89                   SEQ ID 784.       608   AAG00214     Homo sapiens     Human secreted protein, SEQ ID NO: 4295.   98   89       610   AAB61421     Homo sapiens     Human TANGO 300 protein.   1583   99       610   AAB23618     Homo sapiens     Human secreted protein SEQ ID NO: 36.   1581   99       610   AAB87592     Homo sapiens     Human PRO1925.   1354   98       611   gi6841194     Homo sapiens     HSPC272   421   66       611   gi12248392     Mus musculus     transcriptional inhibitory factor   90   28       611   gi2853265     Rattus     jun dimerization protein 2   90   28                 norvegicus         612   gi9964124     Helicobacter     HP0519-like protein   54   45                 pylori         612   gi6970424   Human   start codon is not identified   59   29               papillomavirus               type 69       613   gi14330385     Homo sapiens     mRNA for sodium/calcium exchanger, SCL8A3,   178   92                   alternative splice form B (SCL8A3 gene).       613   gi14330383     Homo sapiens     mRNA for sodium/calcium exchanger SCL8A3,   193   60                   alternative splice form A (SCL8A3 gene).       613   gi1552526     Rattus     sodium-calcium exchanger form 3   178   92                 norvegicus         614   gi58028   synthetic   suef protein   148   32               construct       614   gi2447210     Paramecium     a312aR   67   35                 bursaria                 Chlorella virus 1       615   gi8100892   Human   protease   76   30               immunodeficiency               virus type 1       615   gi14281259   Human   HIV Protease   71   28               immunodeficiency               virus       615   gi10504617   Human   protease   71   31               immunodeficiency               virus type 1       616   gi4128041     Homo sapiens     claudin-9 (CLDN9) gene.   146   37       616   AAB64401     Homo sapiens     Amino acid sequence of human intracellular   146   37                   signalling molecule INTRA33.       616   gi4325296     Mus musculus     claudin-9   143   36       617   AAY05376     Homo sapiens     Human HCMV inducible gene protein, SEQ ID   974   90                   NO: 20.       617   AAB60496     Homo sapiens     Human cell cycle and proliferation protein   974   90                   CCYPR-44, SEQ ID NO: 44.       617   gi13879501     Mus musculus     RIKEN cDNA 4933419D20 gene   348   41       618   AAY25451     Homo sapiens     Human secreted protein 2 derived from extended   123   53                   cDNA.       618   AAY35882     Homo sapiens     Extended human secreted protein sequence,   123   53                   SEQ ID NO: 19.       618   AAY66636     Homo sapiens     Membrane-bound protein PRO180.   126   47       619   gi14042279     Homo sapiens     cDNA FLJ14627 fis, clone NT2RP2000289.   208   82       619   AAW78193     Homo sapiens     Human secreted protein encoded by gene 68   103   46                   clone H2CBJ08.       620   gi10579884   Halobacterium   Vng0244h   68   32               sp. NRC-1       621   AAY19740     Homo sapiens     SEQ ID NO: 458 from WO9922243.   60   36       621   gi5911915     Homo sapiens     mRNA; cDNA DKFZp586M0622 (from clone   68   31                   DKFZp586M0622); partial cds.       621   gi4574260     Haemophilus     outer membrane protein 26   70   29                 influenzae         622   gi13543049     Mus musculus     Similar to RIKEN cDNA 0610030G03 gene   1147   87       622   gi5263332     Arabidopsis     F8K7.23   123   24                 thaliana         622   gi6552728     Arabidopsis     T26F17.1   123   24                 thaliana         623   gi14290586     Homo sapiens     Similar to RIKEN cDNA 2810403L02 gene,   1809   100                   clone IMAGE: 3868486, mRNA, partial cds.       623   gi11493522     Homo sapiens     PRO1512   1512   100       623   AAB58871     Homo sapiens     Breast and ovarian cancer associated antigen   1412   92                   protein sequence SEQ ID 579.       624   gi2114213     Homo sapiens     immunoglobulin lambda gene locus DNA,   788   100                   clone: 123E1 upstream contig.       624   gi2114308     Homo sapiens     immunoglobulin lambda gene locus DNA,   788   100                   clone: 123E1.       624   gi693811   human,   Vpre-B = VPre-B protein   788   100               chromosome               22, Genomic,               1100 nt].               [ Homo sapiens         625   gi14250299     Homo sapiens     Similar to RIKEN cDNA C030006K11 gene,   686   87                   clone MGC: 18180, mRNA, complete cds.       625   gi7230571     Mus musculus     lim homeodomain-containing transcription   87   26                   factor       625   gi587461     Mesocricetus     1mx1.1   83   25                 auratus         626   AAB24074     Homo sapiens     Human PRO1153 protein sequence SEQ ID   130   34                   NO: 49.       626   AAY66735     Homo sapiens     Membrane-bound protein PRO1153.   130   34       626   AAB65258     Homo sapiens     Human PRO1153 (UNQ583) protein sequence   130   34                   SEQ ID NO: 351.       627   gi405956     Escherichia     yeeE   1138   93                 coli         627   gi405954     Escherichia     exonuclease I   1014   86                 coli         627   gi1736685     Escherichia     Exodeoxyribonuclease I (EC 3.1.11.1)   1014   86                 coli     (Exonuclease I) (DNA                   deoxyribophosphodiesterase) (DRPase).       628   gi295196     Salmonella     level of amino acid identity between  E. coli  and   699   86                 typhimurium       S. typhimurium  strongly suggests authentic gene       628   gi405956     Escherichia     yeeE   96   36                 coli         628   AAG01568     Homo sapiens     Human secreted protein, SEQ ID NO: 5649.   65   25       629   AAW67894     Homo sapiens     Human secreted protein encoded by gene 2   60   28                   clone HBMCF37.       629   AAY87145     Homo sapiens     Human secreted protein sequence SEQ ID   60   28                   NO: 184.       629   AAY87182     Homo sapiens     Human secreted protein sequence SEQ ID   60   28                   NO: 221.       630   gi216539     Escherichia     BasS   825   98                 coli         630   gi1790551     Escherichia     sensor protein for basR   825   98                 coli  K12       630   gi536956     Escherichia     basS   825   98                 coli         631   gi1786804     Escherichia     ferric enterobactin transport protein   1021   100                 coli  K12       631   gi1778505     Escherichia     ferric enterobactin transport protein   1021   100                 coli         631   gi13360086     Escherichia     ferric enterobactin transport protein   1020   99                 coli  O157: H7       632   gi349227     Escherichia     transmembrane protein   1114   100                 coli         632   gi466681     Escherichia     dppC   1114   100                 coli         632   gi13363896     Escherichia     dipeptide transport system permease protein 2   1114   100                 coli  O157: H7       633   gi4063042     Cryptosporidium     GP900; mucin-like glycoprotein   359   57                 parvum         633   gi2827460     Cercopithecus     hepatitis A virus cellular receptor 1 short form   324   56                 aethiops         633   gi2827462     Cercopithecus     hepatitis A virus cellular receptor 1 long form   324   56                 aethiops         634   gi13959789     Homo sapiens     lung alpha/beta hydrolase protein 1 mRNA,   203   88                   complete cds.       634   gi13784946     Mus musculus     alpha/beta hydrolase-1   175   77       634   gi7545019     Neurospora     apocytochrome b   47   41                 crassa         635   AAB87774     Homo sapiens     Human T2R44 amino acid sequence SEQ ID   364   91                   NO: 70.       635   AAB87780     Homo sapiens     Human T2R50 amino acid sequence SEQ ID   363   89                   NO: 76.       635   AAB87745     Homo sapiens     Human T2R15 amino acid sequence SEQ ID   343   85                   NO: 28.       636   gi2275592     Homo sapiens     T cell receptor beta locus, TCRBV8S5P to   534   100                   TCRBV21S2A2 region.       636   gi2275570     Homo sapiens     T cell receptor beta locus, TCRBV6S4A1 to   534   100                   TCRBV8S1 region.       636   gi2218039     Homo sapiens     Human germline T-cell receptor beta chain   534   100                   TCRBV13S1, TCRBV6S8A2T,                   TCRBV5S6A3N2T, TCRBV13S6A2T,                   TCRBV6S9P, TCRBV5S3A2T, TCRBV13S8P,                   TCRBV6S3A1N1T, TCRBV5S2,                   TCRBV6S6A2T, TCRBV5S7P, TCRBV13S4,                   TCRBV6S2A1N1T, TCRBV5S4A2T,                   TCRBV6S4A1, TCRBV23S1A2T,                   TCRBV12S1A1N2, TCRBV21S2A2,                   TCRBV8S1, TCRBV8S2A1T, TCRBV8S3,                   TCRBV16S1A1N1, TCRBV24S1A3T,                   TCRBV25S1A2PT, TCRBV26S1P,                   TCRBV18S1, TCRBV17S1A1T, TCRBV2S1,                   TCRBV10S1P genes from bases 257519 to                   472940 (section 2 of 3).       637   AAB49502     Homo sapiens     Clone HYASC03.   310   98       637   gi7020468     Homo sapiens     cDNA FLJ20396 fis, clone KAT00561.   145   39       637   AAB18980     Homo sapiens     Amino acid sequence of a human   145   39                   transmembrane protein.       638   AAY38432     Homo sapiens     Human secreted protein encoded by gene No. 3.   81   46       638   AAY73420     Homo sapiens     Human secreted protein clone ye22_1 protein   75   33                   sequence SEQ ID NO: 62.       638   AAY20298     Homo sapiens     Human apolipoprotein E mutant protein   77   30                   fragment 11.       639   gi9948048     Pseudomonas     probable transporter (membrane subunit)   557   63                 aeruginosa         639   gi7227389     Neisseria     sodium/dicarboxylate symporter family protein   492   58                 meningitidis                 MC58       639   gi9657417     Vibrio     sodium/dicarboxylate symporter   474   55                 cholerae         640   gi13111711     Homo sapiens     solute carrier family 2 (facilitated glucose   1273   60                   transporter), member 5, clone MGC: 1619,                   mRNA, complete cds.       640   gi12804761     Homo sapiens     solute carrier family 2 (facilitated glucose   1273   60                   transporter), member 5, clone MGC: 3654,                   mRNA, complete cds.       640   gi183298     Homo sapiens     Human glucose transport-like 5 (GLUT5)   1273   60                   mRNA, complete cds.       641   gi14336709     Homo sapiens     16p13.3 sequence section 3 of 8.   358   57       641   gi9621664     Homo sapiens     RHBDL gene for rhomboid-related protein.   358   57       641   gi3287191     Homo sapiens     mRNA for rhomboid-related protein, complete   358   57                   CDS.       642   AAY45023     Homo sapiens     Human sensory transduction G-protein coupled   968   100                   receptor-B3.       642   gi13785657     Mus musculus     candidate taste receptor T1R1   786   77       642   gi13785659     Mus musculus     candidate taste receptor T1R2   303   36       643   gi871498     Oryza sativa     DNA binding protein   86   35       643   gi7160630     Bordetella     pertactin (P.68)   86   39                 bronchiseptica         643   gi9049498     Bordetella     pertactin   86   39                 bronchiseptica         644   gi5911988     Homo sapiens     mRNA; cDNA DKFZp434H2235 (from clone   164   73                   DKFZp434H2235); partial cds.       644   gi5262574     Homo sapiens     mRNA; cDNA DKFZp434G173 (from clone   164   73                   DKFZp434G173); complete cds.       644   AAW89030     Homo sapiens     Polypeptide fragment encoded by gene 165.   147   64       645   gi10437864     Homo sapiens     cDNA: FLJ21709 fis, clone COL10077.   429   74       645   AAY91433     Homo sapiens     Human secreted protein sequence encoded by   412   76                   gene 33 SEQ ID NO: 154.       645   gi14042074     Homo sapiens     cDNA FLJ14508 fis, clone NT2RM1000421,   411   80                   weakly similar to RIBONUCLEASE                   INHIBITOR.       646   gi9280561     Mus musculus     elafin-like protein I   66   30       646   AAY99453     Homo sapiens     Human PRO1784 (UNQ846) amino acid   77   31                   sequence SEQ ID NO: 390.       646   gi10176740     Arabidopsis     RING zinc finger protein-like   76   33                 thaliana         647   AAY19485     Homo sapiens     Amino acid sequence of a human secreted   53   52                   protein.       648   gi6900006     Ceratitis     chorion protein s18   95   31                 capitata         648   gi1491621   Bovine   UL36   104   35               herpesvirus 1       648   gi2653311   Bovine   very large virion protein (tegument)   104   35               herpesvirus               type 1.1       649   gi4877582     Homo sapiens     lipoma HMGIC fusion partner (LHFP) mRNA,   72   34                   complete cds.       649   AAY87336     Homo sapiens     Human signal peptide containing protein HSPP-   72   34                   113 SEQ ID NO: 113.       649   gi9658445     Vibrio     AzIC family protein   49   38                 cholerae         650   gi6899191     Ureaplasma     amino acid antiporter   67   33                 urealyticum         650   gi5708228     Rhodopseudo     LH2alpha7   62   35                 monas                 acidophila       650   gi7211354     Saimiri     olfactory receptor   77   34                 boliviensis         651   AAB19403     Homo sapiens     Amino acid sequence of a human secreted   712   89                   protein.       651   gi387048     Cricetus     DHFR-coamplified protein   230   47                 cricetus         651   gi3261597     Mycobacterium     lprA   77   29                 tuberculosis         652   gi12718841     Mus musculus     Skullin   310   38       652   gi4191356     Mus musculus     claudin-6   308   38       652   gi13543081     Mus musculus     claudin-6   308   38       653   gi801882     Vibrio     FkuB   83   31                 alginolyticus         653   gi2795895     Homo sapiens     clone 23819 white protein homolog mRNA,   71   30                   partial cds.       653   gi5777942     Equus caballus     IL-1ra   52   25       654   gi9872     Plasmodium     ATPase I   116   41                 falciparum         654   gi7688148     Homo sapiens     Novel human gene mapping to chomosome I.   119   42       654   gi3451312     Schizosacchar     membrane atpase   116   41                 omyces  pombe       655   gi6682873     Homo sapiens     rec mRNA, complete cds.   200   90       655   gi7230612     Rattus     small rec   197   87                 norvegicus         655   gi4959442     Drosophila     DNZDHHC/NEW1 zinc finger protein 11   93   41                 melanogaster         656   gi2204110     Bos taurus     adenylyl cyclase type VII   233   69       656   gi602412     Mus musculus     adenylyl cyclase type VII   209   66       656   AAB02011     Homo sapiens     Type VII adenylyl cyclase.   209   66       657   gi3297936     Rattus     rhomboid-related protein   267   71                 norvegicus         657   gi9621664     Homo sapiens     RHBDL gene for rhomboid-related protein.   266   71       657   gi14336709     Homo sapiens     16p13.3 sequence section 3 of 8.   266   71       658   gi10437529     Homo sapiens     cDNA: FLJ21432 fis, clone COL04219.   145   25       658   AAY76136     Homo sapiens     Human secreted protein encoded by gene 13.   113   28       658   gi4929559     Homo sapiens     CGI-45 protein mRNA. complete cds.   113   28       659   gi2429362     Santalum     proline rich protein   137   34                 album         659   gi5139695     Cucumis     expressed in cucumber hypocotyls   127   28                 sativus         659   gi7671460     Arabidopsis     AtAGP4   111   37                 thaliana         660   gi3165565     Caenorhabditis     contains similarity to transmembrane domains   94   23                 elegans     found in HMG CoA reductases and drosophila                   patched protein (SW: P18502)       660   gi160281     Plasmodium     erythrocyte binding protein   64   35                 falciparum         660   AAY28686     Homo sapiens     Human yb39_1 secreted protein.   57   43       662   AAY71948     Homo sapiens     Human ion channel protein (ICP).   1195   99       662   AAY71949     Homo sapiens     Human alternative ion channel protein (ICP).   1195   99       662   AAR27654     Homo sapiens     Human calcium channel 27980/16.   149   27       663   gi478889     Rana     transcription factor RcC/EPB-1   82   33                 catesbeiana         663   gi4098456     Sus scrofa     follicle-stimulating hormone beta subunit   60   38       663   AAR56767     Homo sapiens     Human FSH beta subunit fragment with   58   33                   residues −18 to 35.       664   gi5578778     Homo sapiens     mRNA for G18.2 protein (G18.2 gene, located   73   41                   in the class III region of the major                   histocompatibility complex).       664   gi213591     Pseudopleuronectes     HPLC6   65   43                 americanus         664   gi11345434     Thermus     competence factor ComEA   79   43                 thermophilus         665   gi13111831     Homo sapiens     clone IMAGE: 3451448, mRNA, partial cds.   606   60       665   AAW78128     Homo sapiens     Human secreted protein encoded by gene 3   606   60                   clone HOSBI96.       665   AAB18993     Homo sapiens     Amino acid sequence of a human   606   60                   transmembrane protein.       666   gi14249886     Homo sapiens     clone MGC: 15763, mRNA, complete cds.   196   77       666   gi217554     Bos taurus     endothelin receptor   50   32       666   gi3299894     Equus caballus     endothelin-B receptor   50   32       667   AAW52812     Homo sapiens     Human induced tumor protein.   123   38       667   gi8895091     Homo sapiens     Diff33 protein homolog mRNA, complete cds.   123   38       667   AAY95015     Homo sapiens     Human secreted protein vc61_1, SEQ ID   123   38                   NO: 70.       668   gi32093     Homo sapiens       H. sapiens  HGMIP07J gene for olfactory   849   54                   receptor.       668   AAF61132 —       Homo sapiens     Human OLFXY cDNA.   802   49           aa1       668   AAB46999     Homo sapiens     Human OLFXY protein.   799   49       669   gi9081843     Prunus dulcis     self-incompatibility associated ribonuclease   79   44       669   gi6539444     Prunus avium     S6-RNase   79   44       669   gi6539438     Prunus avium     S1-RNase   78   44       670   AAB66272     Homo sapiens     Human TANGO 378 SEQ ID NO: 29.   581   100       670   AAB61166     Homo sapiens     Human BBSR seven transmembrane receptor   168   39                   protein.       670   gi6006811     Mus musculus     serpentine receptor   168   41       671   AAY66750     Homo sapiens     Membrane-bound protein PRO1287.   785   98       671   AAB87561     Homo sapiens     Human PRO1287.   785   98       671   ANB65273     Homo sapiens     Human PRO1287 (UNQ656) protein sequence   785   98                   SEQ ID NO: 381.       672   AAY99421     Homo sapiens     Human PRO1433 (UNQ738) amino acid   915   48                   sequence SEQ ID NO: 292.       672   gi13537297     Homo sapiens     GS1999full mRNA, complete cds.   879   51       672   AAY94889     Homo sapiens     Human protein clone HP02485.   723   43       673   gi10435844     Homo sapiens     cDNA FLJ13737 fis, clone PLACE3000157.   93   28       673   gi205752     Rattus     Nopp140   95   27                 norvegicus         673   AAY53800     Homo sapiens     Amino acids 145-197 of the mature human   63   40                   chromogranin A (CgA) protein.       674   gi7717312     Homo sapiens     chromosome 21 segment HS21C049.   422   97       674   AAB18666     Homo sapiens     A human regulator of intracellular   115   92                   phosphorylation.       674   gi11342496   Bacteriophage   holin   77   27               phi-Ea1h                    
     [0402]                           TABLE 3                       SEQ ID                   NO:   Accession No.   Description   Results*                  339   BL01144   Ribosomal protein L31e proteins.   BL01144 25.07 6.684e−17 83-135       342   PF01325   Iron dependant repressor.   PF01325B 20.91 5.680e−09 34-56       354   BL00019   Actinin-rype actin-binding domain   BL00019D 15.33 3.948e−14 41-71               proteins.       357   BL00979   G-protein coupled receptors family   BL00979M 14.39 6.532e−11 30-81               3 proteins.       367   BL00590   LIF/OSM family proteins.   BL00590B 17.36 3.045e−19 183-201       375   PR00245   OLFACTORY RECEPTOR   PR00245A 18.03 1.419e−18 57-79               SIGNATURE       376   PR00927   ADENTNE NUCLEOTIDE   PR00927A 7.98 9.667e−09 14-27               TRANSLOCATOR 1               SIGNATURE       378   PR00237   RHODOPSIN-LIKE GPCR   PR00237B 13.50 2.250e−09 58-80               SUPERFAMILY SIGNATURE   PR00237G 19.63 9.372e−09 143-170       379   PR00698     C. ELEGANS  SRG FAMILY   PR00698E 14.43 8.714e−09 97-123               INTEGRAL MEMBRANE               PROTEIN SIGNATURE       384   PF00075   RNase H.   PF00075A 14.44 4.429e−09 231-248       387   PD01066   PROTEIN ZINC FINGER ZINC-   PD01066 19.43 9.727e−36 58-97               FINGER METAL-BINDING NU.       388   PR00907   THROMBOMODULIN   PR00907E 11.70 2.969e−10 49-72               SIGNATURE       399   PD01115   PRECURSOR AMPHIBIAN SKIN   PD01115A 12.27 9.750e−12 1-24               SIGNAL.       403   BL00970   Nuclear transition protein 2   BL00970B 10.09 8.966e−10 83-109               proteins.       405   PF01007   Inward rectifier potassium channel.   PF01007B 17.48 1.000e−08 95-139       419   BL00948   Ribosomal protein S7e proteins.   BL00948A 14.13 5.034e−20 68-91       423   PR00019   LEUCINE-RICH REPEAT   PR00019B 11.36 4.150e−10 70-84               SIGNATURE   PR00019B 11.36 9.100e−10 94-108                   PR00019A 11.19 8.000e−09 73-87       425   BL00476   Fatty acid desaturases family 1   BL00476B 18.34 4.938e−09 252-296               proteins.       429   BL01253   Type I fibronectin domain proteins.   BL01253C 15.89 6.654e−18 78-117       434   PR00049   WILM&#39;S TUMOUR PROTEIN   PR00049D 0.00 6.034e−09 7-22               SIGNATURE       436   PR00591   SOMATOSTATIN RECEPTOR   PR00591B 7.56 4.750e−09 117-132               TYPE 5 SIGNATURE       438   PR00709   AVIDIN SIGNATURE   PR00709A 4.60 1.170e−09 16-35       439   BL01253   Type I fibronectin domain proteins.   BL01253F 14.35 5.050e−14 78-117       445   BL00649   G-protein coupled receptors family   BL00649C 17.82 6.339e−12 4-30               2 proteins.       452   PD01066   PROTEIN ZINC FINGER ZINC-   PD01066 19.43 6.362e−29 129-168               FINGER METAL-BINDING NU.       454   PR00463   E-CLASS P450 GROUP I   PR00463B 17.50 3.3 14e−13 135-157               SIGNATURE   PR00463A 11.40 8.568e−10 111-131       459   BL00211   ABC transporters family proteins.   BL00211B 13.37 2.286e−13 222-254                   BL00211A 12.23 9.550e−09 160-172       474   PR00049   WILM&#39;S TUMOUR PROTEIN   PR00049D 0.00 8.780e−09 78-93               SIGNATURE       479   PF00624   Flocculin repeat proteins.   PF00624J 6.21 7.070e−09 40-95                   PF00624F 11.04 9.056e−09 68-104       481   BL01303   BCCT family of transporters   BL01303A 14.33 5.629e−31 89-122               proteins.   BL01303B 10.14 2.250e−18 142-161       482   PR00075   FATTY ACID DESATURASE   PR00075A 16.97 9.565e−09 9-30               FAMILY 1 SIGNATURE       486   BL00538   Bacterial chemotaxis sensory   BL00538C 10.61 1.000e−40 152-191               transducers proteins.   BL00538A 23.61 3.647e−39 96-144       488   BL00077   Heme-copper oxidase catalytic   BL00077C 18.98 9.697e−09 9-60               subunit, copper B binding regio.       494   PR00550   HYPERGLYCEMIC HORMONE   PR00550C 11.31 9.426e−10 29-40               SIGNATURE       496   DM01283   A-BINDING PROTEIN   DM01283A 14.91 9.600e−10 35-71               CHLOROPHYLL.       497   BL00649   G-protein coupled receptors family   BL00649B 20.68 5.061e−11 23-69               2 proteins.   BL00649C 17.82 4.955e−10 82-108       499   BL00312   Glycophorin A proteins.   BL00312B 9.22 9.911e−09 2-31       501   PR00957   GENE 66 (IR5) PROTEIN   PR00957A 7.65 3.473e−09 158-176               SIGNATURE       502   BL00479   Phorbol esters/diacylglycerol   BL00479A 19.86 1.220e−10 59-82               binding domain proteins.       503   PR00007   COMPLEMENT C1Q DOMAIN   PR00007B 14.16 7.698e−13 116-136               SIGNATURE   PR00007D 9.64 9.654e−11 193-204                   PR00007A 19.33 2.552e−10 89-116                   PR00007C 15.60 3.656e−10 163-185       505   PR00925   NONHISTONE   PR00925B 3.73 5.982e−10 78-91               CHROMOSOMAL PROTEIN               HMG17 FAMILY SIGNATURE       517   BL00237   G-protein coupled receptors   BL00237A 27.68 7.000e−14 67-107               proteins.       526   PR00011   TYPE III EGF-LIKE SIGNATURE   PR00011B 13.08 5.576e−13 76-95                   PR00011D 14.03 6.943e−13 76-95                   PR00011B 13.08 9.542e−13 33-52                   PR00011D 14.03 3.211e−12 33-52                   PR00011A 14.06 6.516e−12 33-52                   PR00011A 14.06 8.548e−12 76-95                   PR00011D 14.03 3.213e−11 162-181                   PR00011B 13.08 2.174e−10 162-181                   PR00011D 14.03 2.523e−10 119-138                   PR00011B 13.08 2.356e−09 119-138                   PR00011B 13.08 5.685e−09 205-224                   PR00011A 14.06 6.425e−09 119-138                   PR00011A 14.06 6.671e−09 162-181                   PR00011D 14.03 9.870e−09 205-224       531   PR00251   BACTERIAL OPSIN   PR00251G 16.33 4.000e−09 176-195               SIGNATURE       541   BL00649   G-protein coupled receptors family   BL00649C 17.82 6.073e−13 21-47               2 proteins.       546   BL00242   Integrins alpha chain proteins.   BL00242E 9.03 8.154e−09 82-111       551   DM00215   PROLINE-RICH PROTEIN 3.   DM00215 19.43 8.071e−10 122-155       555   PR00806   VINCULIN SIGNATURE   PR00806C 11.07 8.839e−09 13-31       559   BL00237   G-protein coupled receptors   BL00237A 27.68 9.129e−15 71-111               proteins.   BL00237C 13.19 1.346e−13 218-245                   BL00237D 11.23 9.308e−11 271-288       563   BL00495   Apple domain proteins.   BL00495N 11.04 8.239e−14 204-239                   BL00495O 13.75 9.000e−14 236-265       580   PR00838   VENOM ALLERGEN 5   PR00838G 16.07 9.760e−12 165-185               SIGNATURE   PR00838D 8.73 1.563e−10 87-106       581   PR00049   WILM&#39;S TUMOUR PROTEIN   PR00049D 0.00 7.344e−13 205-220               SIGNATURE   PR00049D 0.00 9.262e−13 206-221                   PR00049D 0.00 4.000e−12 207-222                   PR00049D 0.00 4.000e−12 208-223                   PR00049D 0.00 7.655e−11 202-217                   PR00049D 0.00 7.958e−11 204-219                   PR00049D 0.00 8.336e−11 203-218                   PR00049D 0.00 1.214e−10 209-224                   PR00049D 0.00 1.214e−10 210-225                   PR00049D 0.00 3.746e−09 211-226       585   BL01113   C1q domain proteins.   BL01113A 17.99 3.106e−10 22-49       586   PR00828   FORMIN SIGNATURE   PR00828H 8.87 4.081e−09 390-412       587   PR00169   POTASSIUM CHANNEL   PR00169H 8.09 5.696e−30 225-252               SIGNATURE   PR00169E 9.10 8.773e−28 127-154                   PR00169G 9.39 6.684e−27 196-219                   PR00169C 16.31 8.714e−25 59-83                   PR00169F 7.19 6.192e−24 156-180                   PR00169D 12.86 2.385e−20 85-106       590   PR00451   CHITIN-BINDING DOMAIN   PR00451A 6.49 1.871e−09 88-97               SIGNATURE       594   PF01327   Polypeptide deformylase.   PF01327D 18.82 2.440e−20 197-229                   PF01327A 18.58 2.187e−09 92-127       595   PD02796   PROTEIN STEROL CARRIER   PD02796B 20.92 6.507e−23 157-204               LIPID-TRAN.       596   BL00232   Cadherins extracellular repeat   BL00232A 27.72 7.218e−12 38-71               proteins domain proteins.       598   BL00261   Glycoprotein hormones beta chain   BL00261B 25.64 1.000e−40 72-116               proteins.   BL00261A 23.97 3.500e−34 22-56       599   PR00796   VIRAL SPIKE GLYCOPROTEIN   PR00796I 8.96 7.638e−11 32-58               PRECURSOR SIGNATURE       602   PR00209   ALPHA/BETA GLIADIN   PR00209B 4.88 8.594e−09 129-148               FAMILY SIGNATURE       605   PR00833   POLLEN ALLERGEN POA PI   PR00833H 2.30 6.625e−10 61-76               SIGNATURE       622   PR00779   INOSITOL 1,4,5-   PR00779H 8.81 6.909e−09 18-40               TRISPHOSPHATE-BINDING               PROTEIN RECEPTOR               SIGNATURE       624   DM00031   IMMUNOGLOBULIN V   DM00031B 15.41 4.508e−15 84-118               REGION.       628   PD01736   PROTEIN TRANSMEMBRANE   PD01736B 8.42 9.250e−09 118-130               INTERGENIC REGION RECQ-               PLD.       630   PF00512   Signal carboxyl-terminal domain   PF00512 13.94 3.571e−14 150-169               proteins.       631   PF01032   FecCD transport family.   PF01032B 9.12 7.300e−15 132-147       632   BL00713   Sodium: dicarboxylate symporter   BL00713D 20.98 6.063e−09 24-62               family proteins.       633   DM00784   APILLOMA VIRUS E4 PROTEIN.   DM00784B 17.87 7.492e−09 67-92       639   BL00713   Sodium: dicarboxylate symporter   BL00713C 19.76 1.964e−09 100-139               family proteins.       640   BL00216   Sugar transport proteins.   BL00216B 27.64 8.000e−25 108-158       642   BL00979   G-protein coupled receptors family   BL00979M 14.39 5.114e−12 126-177               3 proteins.       643   BL00402   Binding-protein-dependent   BL00402A 5.93 7.000e−09 55-69               transport systems inner membrane               co.       645   PR00237   RHODOPSIN-LIKE GPCR   PR00237F 13.57 8.342e−09 24-49               SUPERFAMILY SIGNATURE       662   PR00170   SODIUM CHANNEL   PR00170G 7.74 3.374e−09 37-66               SIGNATURE       668   BL00237   G-protein coupled receptors   BL00237A 27.68 5.974e−12 83-123               proteins.                    
     [0403]                               TABLE 4                       SEQ ID NO:   Pfam Model   Description   E-value   Pfam Score                                                    339   Ribosomal_L31e   Ribosomal protein L31e   0.00061   16.6       357   7tm_3   7 transmembrane receptor (metabotropic   0.0073   −95.1               glutamate family)       367   LIF_OSM   LIF/OSM family     8e−145   494.5       370   ig   Immunoglobulin domain   1.5e−05   23.0       375   7tm_1   7 transmembrane receptor (rhodopsin   3.8e−06   21.7               family)       378   7tm_1   7 transmembrane receptor (rhodopsin   0.064   8.3               family)       380   DUF6   Integral membrane protein DUF6   1.4e−05   32.0       384   rvt   Reverse transcriptase (RNA-dependent     3e−15   61.0               DNA Polymerase)       387   KRAB   KRAB box     2e−42   154.4       399   Gastrin   Gastrin/cholecystokinin family   7.5e−22   83.9       401   Cornifin       0.0031   5.4       405   ion_trans   Ion transport protein   0.0034   24.0       408   Galactosyl_T   Galactosyltransferase   2.9e−28   107.3       419   Ribosomal_S7e   Ribosomal protein S7e   6.9e−17   69.5       423   LRR   Leucine Rich Repeat   1.8e−15   64.8       429   kringle   Kringle domain   1.2e−17   72.1       430   p450   Cytochrome P450   0.034   10.6       439   trypsin   Trypsin   1.9e−06   23.0       444   PMP22_Claudin   PMP-22/EMP/MP20/Claudin family   0.002   −5.3       448   ig   Immunoglobulin domain   1.7e−08   32.5       452   KRAB   KRAB box   6.4e−22   86.3       454   p450   Cytochrome P450   8.3e−13   48.0       459   ABC_tran   ABC transporter   0.0016   −23.4       478   neur_chan   Neurotransmitter-gated ion-channel   4.8e−15   54.0       481   BCCT   BCCT family transporter   8.5e−22   85.8       483   Fumarate_red_D       3.4e−64   226.7       486   HAMP       1.1e−11   52.2       497   7tm_2   7 transmembrane receptor (Secretin   0.0039   −87.5               family)       503   C1q   C1q domain   2.2e−45   164.2       508   MCT   Monocarboxylate transporter   4.4e−59   209.7       517   7tm_1   7 transmembrane receptor (rhodopsin   5.4e−22   72.0               family)       526   EGF   EGF-like domain   0.00021   28.1       527   DUF6   Integral membrane protein DUF6   0.043   13.8       528   zf-DHHC   DHHC zinc finger domain   1.2e−32   121.9       533   CUB   CUB domain   6.9e−32   119.4       537   PMP22_Claudin   PMP-22/EMP/MP20/Claudin family   7.6e−31   115.9       541   7tm_2   7 transmembrane receptor (Secretin   3.7e−05   −46.4               family)       543   tsp_1   Thrombospondin type 1 domain   0.028   12.1       559   7tm_1   7 transmembrane receptor (rhodopsin   9.3e−40   128.4               family)       560   PDZ   PDZ domain (Also known as DHR or   2.1e−42   154.3               GLGF).       563   trypsin   Trypsin   9.8e−99   313.5       569   Peptidase_M1   Peptidase family M1   3.7e−11   32.8       572   ig   Immunoglobulin domain   1.2e−06   26.5       580   SCP   SCP-like extracellular protein   2.9e−21   80.4       585   C1q   C1q domain   5.4e−08   35.2       587   ion_trans   Ion transport protein   3.9e−31   116.9       594   Pep_deformylase   Polypeptide deformylase   2.1e−20   81.2       595   SCP2   SCP-2 sterol transfer family   5.2e−23   89.9       596   cadherin   Cadherin domain   2.9e−08   40.9       598   Cys_knot   Cystine-knot domain   3.3e−52   186.9       624   ig   Immunoglobulin domain   2.6e−09   35.1       630   HAMP       1.1e−08   42.3       631   FecCD_family   FecCD transport family   7.4e−44   159.1       632   BPD_transp   Binding-protein-dependent transport     6e−05   29.9               systems inner membrane component       636   ig   Immunoglobulin domain   8.8e−13   46.2       639   SDF   Sodium: dicarboxylate symporter family   3.4e−58   206.8       640   sugar_tr   Sugar (and other) transporter     2e−99   343.7       642   7tm_3   7 transmembrane receptor (metabotropic   2.1e−06   −21.8               glutamate family)       652   PMP22_Claudin   PMP-22/EMP/MP20/Claudin family   4.1e−08   40.4       655   zf-DHHC   DHHC zinc finger domain   0.0085   −6.4       657   Rhomboid   Rhomboid family   0.072   −20.3       668   7tm_1   7 transmembrane receptor (rhodopsin   7.1e−30   97.1               family)                    
     [0404]                                                       TABLE 5                       SEQ                                               ID   PDB   Chain   Start   End   PSI-   Verify   PMF   SeqFold       NO:   ID   ID   AA   AA   BLAST   Score   Score   Score   Coumpound   PDB annotation                                                                            354   1bhd   A   42   87   8.5e−18   0.00   0.04       UTROPHIN; CHAIN: A, B;   STRUCTURAL PROTEIN CALPONIN                                               HOMOLOGY, ACTIN BINDING,                                               STRUCTURAL PROTEIN       354   1bkr   A   41   89   1.7e−20   −0.24   0.28       SPECTRIN BETA CHAIN;   ACTIN-BINDING CALPONIN                                           CHAIN: A;   HOMOLOGY (CH) DOMAIN;                                               FILAMENTOUS ACTIN-BINDING                                               DOMAIN, CYTOSKELETON       354   1dxx   A   26   76     1e−09   −0.48   0.41       DYSTROPHIN; CHAIN: A,   STRUCTURAL PROTEIN                                           B, C, D;   DYSTROPHIN, MUSCULAR                                               DYSTROPHY, CALPONIN                                               HOMOLOGY DOMAIN, 2 ACTIN-                                               BINDING, UTROPHIN       354   1dxx   A   42   89   1.5e−16   −0.35   0.11       DYSTROPHIN; CHAIN: A,   STRUCTURAL PROTEIN                                           B, C, D;   DYSTROPHIN, MUSCULAR                                               DYSTROPHY, CALPONIN                                               HOMOLOGY DOMAIN, 2 ACTIN-                                               BINDING, UTROPHIN       354   1qag   A   42   87   8.5e−18   −0.59   0.09       UTROPHIN ACTIN   STRUCTURAL PROTEIN CALPONIN                                           BINDING REGION; CHAIN:   HOMOLOGY DOMAIN, DOMAIN                                           A, B;   SWAPPING, ACTIN BINDING, 2                                               UTROPHIN, DYSTROPHIN,                                               STRUCTURAL PROTEIN       358   1fqv   A   28   67   0.005   −0.85   0.43       SKP2; CHAIN: A, C, E, G, I,   LIGASE CYCLIN A/CDK2-                                           K, M, O; SKP1; CHAIN: B,   ASSOCIATED PROTEIN P45; CYCLIN                                           D, F, H, J, L, N, P;   A/CDK2-ASSOCIATED PROTEIN P19;                                               SKP1, SKP2, F-BOX, LRR, LEUCINE-                                               RICH REPEAT, SCF, UBIQUITIN, 2                                               E3, UBIQUITIN PROTEIN LIGASE       361   1sfp       38   78   0.0015   −0.73   0.71       ASFP; CHAIN: NULL;   SPERMADHESIN ACIDIC SEMINAL                                               PROTEIN; SPERMADHESIN, BOVINE                                               SEMINAL PLASMA PROTEIN,                                               ACIDIC 2 SEMINAL FLUID PROTEIN,                                               ASFP, CUB DOMAIN, X-RAY                                               CRYSTAL 3 STRUCTURE, GROWTH                                               FACTOR       361   1spp   B   24   78   0.0015   −0.08   0.10       MAJOR SEMINAL PLASMA   COMPLEX (SEMINAL PLASMA                                           GLYCOPROTEIN PSP-I;   PROTEIN/SPP) SEMINAL PLASMA                                           CHAIN: A; MAJOR   PROTEINS, SPERMADHESINS, CUB                                           SEMINAL PLASMA   DOMAIN 2 ARCHITECTURE,                                           GLYCOPROTEIN PSP-II;   COMPLEX (SEMINAL PLASMA                                           CHAIN: B   PROTEIN/SPP)       367   1evs   A   29   212   1.8e−78   1.02   1.00       ONCOSTATIN M; CHAIN:   CYTOKINE 4-HELIX BUNDLE, GP130                                           A;   BINDING CYTOKINE       367   1evs   A   29   212   5.1e−76   1.13   1.00       ONCOSTATIN M; CHAIN:   CYTOKINE 4-HELIX BUNDLE, GP130                                           A;   BINDING CYTOKINE       370   1ac6   A   27   119   1.3e−15           56.47   T-CELL RECEPTOR   RECEPTOR RECEPTOR, V ALPHA                                           ALPHA; CHAIN: A, B;   DOMAIN, SITE-DIRECTED                                               MUTAGENESIS, 2 THREE-                                               DIMENSIONAL STRUCTURE,                                               GLYCOPROTEIN, SIGNAL       370   1ao7   D   26   119   7.5e−21           51.88   HLA-A 0201; CHAIN: A;   COMPLEX (MHC/VIRAL                                           BETA-2 MICROGLOBULIN;   PEPTIDE/RECEPTOR) HLA-A2                                           CHAIN: B; TAX PEPTIDE;   HEAVY CHAIN; CLASS I MHC, T-                                           CHAIN: C; T CELL   CELL RECEPTOR, VIRAL PEPTIDE, 2                                           RECEPTOR ALPHA;   COMPLEX (MHC/VIRAL                                           CHAIN: D; T CELL   PEPTIDE/RECEPTOR                                           RECEPTOR BETA; CHAIN:                                           E;       370   1aqk   L   28   117   5.1e−48   0.35   0.89       FAB B7-15A2; CHAIN: L, H;   IMMUNOGLOBULIN HUMAN FAB,                                               ANTI-TETANUS TOXOID, HIGH                                               AFFINITY, CRYSTAL 2 PACKING                                               MOTIF, PROGRAMMING                                               PROPENSITY TO CRYSTALLIZE, 3                                               IMMUNOGLOBULIN       370   1b6d   A   25   114   1.2e−44   0.16   0.60       IMMUNOGLOBULIN;   IMMUNOGLOBULIN                                           CHAIN: A, B;   IMMUNOGLOBULIN, KAPPA LIGHT-                                               CHAIN DIMER HEADER       370   1bjl   L   25   114   5.1e−46   0.37   0.63       FAB FRAGMENT; CHAIN:   COMPLEX (ANTIBODY/ANTIGEN)                                           L, H, J, K; VASCULAR   FAB-12; VEGF; COMPLEX                                           ENDOTHELIAL GROWTH   (ANTIBODY/ANTIGEN),                                           FACTOR; CHAIN: V, W;   ANGIOGENIC FACTOR       370   1bjm   A   27   116   5.1e−45   0.13   0.83       LOC-LAMBDA 1 TYPE   IMMUNOGLOBULIN BENCE-JONES                                           LIGHT-CHAIN DIMER;   PROTEIN; 1BJM 8 BENCE JONES,                                           1BJM 6 CHAIN: A, B; 1BJM 7   ANTIBODY, MULTIPLE                                               QUATERNARY STRUCTURES 1BJM                                               13       370   1bww   A   23   114   1.7e−45   0.27   0.31       IG KAPPA CHAIN V-I   IMMUNE SYSTEM REIV,                                           REGION REI; CHAIN: A, B;   STABILIZED IMMUNOGLOBULIN                                               FRAGMENT, BENCE-JONES 2                                               PROTEIN, IMMUNE SYSTEM       370   1dee   A   25   114   3.4e−47   0.25   0.48       IGM RF 2A2; CHAIN: A, C,   IMMUNE SYSTEM FAB-IBP                                           E; IGM RF 2A2; CHAIN: B,   COMPLEX CRYSTAL STRUCTURE                                           D, F; IMMUNOGLOBULIN   2.7A RESOLUTION BINDING 2                                           G BINDING PROTEIN A;   OUTSIDE THE ANTIGEN                                           CHAIN: G, H;   COMBINING SITE SUPERANTIGEN                                               FAD VH3 3 SPECIFICITY       370   1dfb   L   25   119   8.5e−47   0.50   0.64       IMMUNOGLOBULIN 3D6                                           FAB 1DFB 3       370   1fgv   L   25   114   1.4e−45   0.21   0.53       IMMUNOGLOBULIN FV                                           FRAGMENT OF A                                           HUMANIZED VERSION OF                                           THE ANTI-CD18 1FGV 3                                           ANTIBODY ’H52’ (HUH52-                                           AA FV) 1FGV 4       370   2fb4   L   26   117   1.2e−44   0.35   0.82       IMMUNOGLOBULIN                                           IMMUNOGLOBULIN FAB                                           2FB4 4       370   2fgw   L   25   114   1.7e−45   0.32   0.77       IMMUNOGLOBULIN FAB                                           FRAGMENT OF A                                           HUMANIZED VERSION OF                                           THE ANTI-CD18 2FGW 3                                           ANTIBODY ’H52’ (HUH52-                                           OZ FAB) 2FGW 4       373   1cru   A   169   400   1.5e−46   0.13   0.28       SOLUBLE QUINOPROTEIN   OXIDOREDUCTASE BETA-                                           GLUCOSE   PROPELLER, SUPERBARREL,                                           DEHYDROGENASE;   COMPLEX WITH THE COFACTOR                                           CHAIN: A, B;   PQQ 2 AND THE INHIBITOR                                               METHYLHYDRAZINE,                                               OXIDOREDUCTASE       373   1cru   A   186   404   7.5e−49   0.01   0.27       SOLUBLE QUINOPROTEIN   OXIDOREDUCTASE BETA-                                           GLUCOSE   PROPELLER, SUPERBARREL,                                           DEHYDROGENASE;   COMPLEX WITH THE COFACTOR                                           CHAIN: A, B;   PQQ 2 AND THE INHIBITOR                                               METHYLHYDRAZINE,                                               OXIDOREDUCTASE       384   1c0t   A   174   431   1.7e−65   −0.24   0.25       HIV-1 REVERSE   TRANSFERASE HIV-1 REVERSE                                           TRANSCRIPTASE (A-   TRANSCRIPTASE, AIDS, NON-                                           CHAIN); CHAIN: A; HIV-1   NUCLEOSIDE INHIBITOR, 2 DRUG                                           REVERSE   DESIGN                                           TRANSCRIPTASE (B-                                           CHAIN); CHAIN: B;       384   1c0t   B   176   431     1e−62   −0.31   0.23       HIV-1 REVERSE   TRANSFERASE HIV-1 REVERSE                                           TRANSCRIPTASE (A-   TRANSCRIPTASE, AIDS, NON-                                           CHAIN); CHAIN: A; HIV-1   NUCLEOSIDE INHIBITOR, 2 DRUG                                           REVERSE   DESIGN                                           TRANSCRIPTASE (B-                                           CHAIN); CHAIN: B;       384   1c1c   B   175   431     1e−74   −0.12   0.39       HIV-1 REVERSE   TRANSFERASE HIV-1 REVERSE                                           TRANSCRIPTASE (A-   TRANSCRIPTASE, AIDS, NON-                                           CHAIN); CHAIN: A; HIV-1   NUCLEOSIDE INHIBITOR, 2 DRUG                                           REVERSE   DESIGN                                           TRANSCRIPTASE (B-                                           CHAIN); CHAIN: B;       384   1c9r   A   171   431     1e−70   −0.08   0.94       HIV-1 REVERSE   TRANSFERASE/IMMUNE                                           TRANSCRIPTASE (CHAIN   SYSTEM/DNA HIV-1 RT; HIV-1 RT;                                           A); CHAIN: A; HIV-1   HIV, REVERSE TRANSCRIPTASE,                                           REVERSE   MET184ILE, 3TC, PROTEIN-DNA 2                                           TRANSCRIPTASE (CHAIN   COMPLEX, DRUG RESISTANCE,                                           B); CHAIN: B; ANTIBODY   M184I, TRANSFERASE/IMMUNE 3                                           (LIGHT CHAIN); CHAIN: L;   SYSTEM/DNA                                           ANTIBODY (HEAVY                                           CHAIN); CHAIN: H; DNA                                           (5’-CHAIN: T; DNA (5’-                                           CHAIN: P;       384   1c9r   B   171   431   1.7e−79   −0.14   0.59       HIV-1 REVERSE   TRANSFERASE/IMMUNE                                           TRANSCRIPTASE (CHAIN   SYSTEM/DNA HIV-1 RT; HIV-1 RT;                                           A); CHAIN: A; HIV-1   HIV, REVERSE TRANSCRIPTASE,                                           REVERSE   MET184ILE, 3TC, PROTEIN-DNA 2                                           TRANSCRIPTASE (CHAIN   COMPLEX, DRUG RESISTANCE,                                           B); CHAIN: B; ANTIBODY   M184I, TRANSFERASE/IMMUNE 3                                           (LIGHT CHAIN); CHAIN: L;   SYSTEM/DNA                                           ANTIBODY (HEAVY                                           CHAIN); CHAIN: H; DNA                                           (5’-CHAIN: T; DNA (5’-                                           CHAIN: P;       384   1mml       154   396   5.1e−50           116.10   MMLV REVERSE   REVERSE TRANSCRIPTASE                                           TRANSCRIPTASE; 1MML 4                                           CHAIN: NULL; 1MML 5       384   1rth   A   171   431   3.4e−86   −0.12   0.74       HIV-1 REVERSE   NUCLEOTIDYLTRANSFERASE HIV-                                           TRANSCRIPTASE; 1RTH 4   1 RT; 1RTH 6 HIV-1 REVERSE                                           CHAIN: A, B; 1RTH 5   TRANSCRIPTASE 1RTH 15       384   1rth   B   173   431     1e−75   −0.09   0.23       HIV-1 REVERSE   NUCLEOTIDYLTRANSFERASE HIV-                                           TRANSCRIPTASE; 1RTH 4   1 RT; 1RTH 6 HIV-1 REVERSE                                           CHAIN: A, B; 1RTH 5   TRANSCRIPTASE 1RTH 15       384   1vrt   A   174   431   1.7e−85   −0.26   0.40       HIV-1 REVERSE   NUCLEOTIDYLTRANSFERASE HIV-                                           TRANSCRIPTASE; 1VRT 4   1 RT; 1VRT 6 HIV-1 REVERSE                                           CHAIN: A, B; 1VRT 5   TRANSCRIPTASE 1VRT 15       384   1vrt   B   175   431   1.7e−75   −0.20   0.11       HIV-1 REVERSE   NUCLEOTIDYLTRANSFERASE HIV-                                           TRANSCRIPTASE; 1VRT 4   1 RT; 1VRT 6 HIV-1 REVERSE                                           CHAIN: A, B; 1VRT 5   TRANSCRIPTASE 1VRT 15       384   3hvt   B   172   431   3.4e−74   −0.14   0.00       NUCLEOTIDYLTRANSFER                                           ASE REVERSE                                           TRANSCRIPTASE                                           (E.C.2.7.7.49) 3HVT 3       388   1aut   L   47   75   0.00068   −0.18   0.42       ACTIVATED PROTEIN C;   COMPLEX (BLOOD                                           CHAIN: C, L; D-PHE-PRO-   COAGULATION/INHIBITOR)                                           MAI; CHAIN: P;   AUTOPROTHROMBIN IIA;                                               HYDROLASE, SERINE                                               PROTEINASE), PLASMA CALCIUM                                               BINDING, 2 GLYCOPROTEIN,                                               COMPLEX (BLOOD                                               COAGULATION/INHIBITOR)       388   1diy   A   46   77   0.00068   0.69   0.25       PROSTAGLANDIN H2   OXIDOREDUCTASE ARACHIDONIC                                           SYNTHASE-1; CHAIN: A;   ACID, MEMBRANE PROTEIN,                                               PEROXIDASE, DIOXYGENASE       388   1fsb       46   75   0.0034   1.08   0.34       P-SELECTIN; CHAIN:   CELL ADHESION PROTEIN EGF-                                           NULL;   LIKE DOMAIN, CELL ADHESION                                               PROTEIN, TRANSMEMBRANE, 2                                               GLYCOPROTEIN       395   1mgl   A   260   376   3.4e−28   −0.94   0.06       HTLV-1 GP21   LEUKEMIA VIRUS TYPE 1 HUMAN T                                           ECTODOMAIN/MALTOSE-   CELL LEUKEMIA VIRUS TYPE 1,                                           BINDING PROTEIN CHAIN:   HTLV-1, ENVELOPE 2 PROTEIN,                                           A;   MEMBRANE FUSION, MALTOSE-                                               BINDING PROTEIN CHIMERA       395   2ebo   A   304   376   5.1e−22   −0.56   0.21       EBOLA VIRUS ENVELOPE   ENVELOPE GLYCOPROTEIN                                           GLYCOPROTEIN; CHAIN:   ENVELOPE GLYCOPROTEIN,                                           A, B, C;   FILOVIRUS, EBOLA VIRUS, GP2,                                               COAT 2 PROTEIN       423   1a9n   A   27   164   2.5e−18   0.22   0.69       U2 RNA HAIRPIN IV;   COMPLEX (NUCLEAR                                           CHAIN: Q, R; U2 A′; CHAIN:   PROTEIN/RNA) COMPLEX                                           A, C; U2 B″; CHAIN: B, D;   (NUCLEAR PROTEIN/RNA), RNA,                                               SNRNP, RIBONUCLEOPROTEIN       423   1a9n   A   54   188     5e−24   0.30   0.48       U2 RNA HAIRPIN IV;   COMPLEX (NUCLEAR                                           CHAIN: Q, R; U2 A′; CHAIN:   PROTEIN/RNA) COMPLEX                                           A, C; U2 B″; CHAIN: B, D;   (NUCLEAR PROTEIN/RNA), RNA,                                               SNRNP, RIBONUCLEOPROTEIN       423   1a9n   C   27   164   7.5e−18   0.38   0.96       U2 RNA HAIRPIN IV;   COMPLEX (NUCLEAR                                           CHAIN: Q, R; U2 A′; CHAIN:   PROTEIN/RNA) COMPLEX                                           A, C; U2 B″; CHAIN: B, D;   (NUCLEAR PROTEIN/RNA), RNA,                                               SNRNP, RIBONUCLEOPROTEIN       423   1a9n   C   54   188   1.5e−23   0.46   0.53       U2 RNA HAIRPIN IV;   COMPLEX (NUCLEAR                                           CHAIN: Q, R; U2 A′; CHAIN:   PROTEIN/RNA) COMPLEX                                           A, C; U2 B″; CHAIN: B, D;   (NUCLEAR PROTEIN/RNA), RNA,                                               SNRNP, RIBONUCLEOPROTEIN       423   1d0b   A   70   237   1.7e−21   −0.00   0.41       INTERNALIN B; CHAIN: A;   CELL ADHESION LEUCINE RICH                                               REPEAT, CALCIUM BINDING, CELL                                               ADHESION       423   1dce   A   98   218   1.2e−09   −0.43   0.30       RAB   TRANSFERASE CRYSTAL                                           GERANYLGERANYLTRAN   STRUCTURE, RAB                                           SFERASE ALPHA   GERANYLGERANYLTRANSFERASE,                                           SUBUNIT; CHAIN: A, C;   2.0 A 2 RESOLUTION, N-                                           RAB   FORMYLMETHIONINE, ALPHA                                           GERANYLGERANYLTRAN   SUBUNIT, BETA SUBUNIT                                           SFERASE BETA SUBUNIT;                                           CHAIN: B, D;       423   1ds9   A   55   178   2.5e−17   −0.29   0.06       OUTER ARM DYNEIN;   CONTRACTILE PROTEIN LEUCINE-                                           CHAIN: A;   RICH REPEAT, BETA-BETA-ALPHA                                               CYLINDER, DYNEIN, 2                                               CHLAMYDOMONAS, FLAGELLA       423   2bnh       34   183     1e−21   0.28   −0.03       RIBONUCLEASE   ACETYLATION RNASE INHIBITOR,                                           INHIBITOR; CHAIN: NULL;   RIBONUCLEASE/ANGIOGENIN                                               INHIBITOR ACETYLATION,                                               LEUCINE-RICH REPEATS       429   1a0h   A   30   150   2.5e−29   0.37   0.65       MEIZOTHROMBIN; CHAIN:   COMPLEX (SERINE                                           A, B, D, E; D-PHE-PRO-   PROTEASE/INHIBITOR) DESF1;                                           ARG; CHAIN: C, F;   PPACK; SERINE PROTEASE,                                               COAGULATION, THROMBIN,                                               PROTHROMBIN, 2                                               MEIZOTHROMBIN, COMPLEX                                               (SERINE PROTEASE/INHIBITOR)       429   1a0h   A   30   169   6.8e−10   0.28   0.76       MEIZOTHROMBIN; CHAIN:   COMPLEX (SERINE                                           A, B, D, E; D-PHE-PRO-   PROTEASE/INHIBITOR) DESF1;                                           ARG; CHAIN: C, F;   PPACK; SERINE PROTEASE,                                               COAGULATION, THROMBIN,                                               PROTHROMBIN, 2                                               MEIZOTHROMBIN, COMPLEX                                               (SERINE PROTEASE/INHIBITOR)       429   1a0h   A   30   201   2.5e−29           82.71   MEIZOTHROMBIN; CHAIN:   COMPLEX (SERINE                                           A, B, D, E; D-PHE-PRO-   PROTEASE/INHIBITOR) DESF1;                                           ARG; CHAIN: C, F;   PPACK; SERINE PROTEASE,                                               COAGULATION, THROMBIN,                                               PROTHROMBIN, 2                                               MEIZOTHROMBIN, COMPLEX                                               (SERINE PROTEASE/INHIBITOR)       429   1b2i   A   32   120   7.5e−26           72.58   PLASMINOGEN; CHAIN: A;   HYDROLASE SERINE PROTEASE,                                               FIBRINOLYSIS, LYSINE-BINDING                                               DOMAIN, 2 PLASMINOGEN,                                               KRINGLE 2, HYDROLASE       429   1b2i   A   34   119   7.5e−26   0.90   0.81       PLASMINOGEN; CHAIN: A;   HYDROLASE SERINE PROTEASE,                                               FIBRINOLYSIS, LYSINE-BINDING                                               DOMAIN, 2 PLASMINOGEN,                                               KRINGLE 2, HYDROLASE       429   1cea   A   35   119   1e−24           68.58   PLASMINOGEN; 1CEA 7   SERINE PROTEASE K1PG; 1CEA 10                                           CHAIN: A, B; 1CEA 8       429   1kdu       35   120   2.5e−28           71.09   PLASMINOGEN                                           ACTIVATION                                           PLASMINOGEN                                           ACTIVATOR (UROKINASE-                                           TYPE, KRINGLE DOMAIN)                                           1KDU 3 (U-PA K) (NMR,                                           MINIMIZED AVERAGE                                           STRUCTURE) 1KDU 4       429   1kdu       36   119   2.5e−28   0.91   0.96       PLASMINOGEN                                           ACTIVATION                                           PLASMINOGEN                                           ACTIVATOR (UROKINASE-                                           TYPE, KRINGLE DOMAIN)                                           1KDU 3 (U-PA K) (NMR,                                           MINIMIZED AVERAGE                                           STRUCTURE) 1KDU 4       429   1krn       35   119     5e−22           76.76   PLASMINOGEN; CHAIN:   SERINE PROTEASE KRINGLE,                                           NULL;   BLOOD, PLASMINOGEN, SERINE                                               PROTEASE       429   1pml   A   34   119   1.3e−28   0.89   1.00       HYDROLASE(SERINE                                           PROTEASE) TISSUE                                           PLASMINOGEN                                           ACTIVATOR KRINGLE 2                                           (E.C.3.4.21.68) 1PML 3       429   1pml   A   34   121   1.3e−28           86.47   HYDROLASE(SERINE                                           PROTEASE) TISSUE                                           PLASMINOGEN                                           ACTIVATOR KRINGLE 2                                           (E.C.3.4.21.68) 1PML 3       429   1pml   C   34   119     1e−28   0.94   0.96       HYDROLASE(SERINE                                           PROTEASE) TISSUE                                           PLASMINOGEN                                           ACTIVATOR KRINGLE 2                                           (E.C.3.4.21.68) 1PML 3       429   1pml   C   34   120     1e−28           86.67   HYDROLASE(SERINE                                           PROTEASE) TISSUE                                           PLASMINOGEN                                           ACTIVATOR KRINGLE 2                                           (E.C.3.4.21.68) 1PML 3       429   1sfp       218   329   2.5e−17   1.13   0.99       ASFP; CHAIN: NULL;   SPERMADHESIN ACIDIC SEMINAL                                               PROTEIN; SPERMADHESIN, BOVINE                                               SEMINAL PLASMA PROTEIN,                                               ACIDIC 2 SEMINAL FLUID PROTEIN,                                               ASFP, CUB DOMAIN, X-RAY                                               CRYSTAL 3 STRUCTURE, GROWTH                                               FACTOR       429   1sfp       238   327   3.4e−07   0.62   0.09       ASFP; CHAIN: NULL;   SPERMADHESIN ACIDIC SEMINAL                                               PROTEIN; SPERMADHESIN, BOVINE                                               SEMINAL PLASMA PROTEIN,                                               ACIDIC 2 SEMINAL FLUID PROTEIN,                                               ASFP, CUB DOMAIN, X-RAY                                               CRYSTAL 3 STRUCTURE, GROWTH                                               FACTOR       429   1spp   A   218   323   2.5e−16   0.67   0.11       MAJOR SEMINAL PLASMA   COMPLEX (SEMINAL PLASMA                                           GLYCOPROTEIN PSP-I;   PROTEIN/SPP) SEMINAL PLASMA                                           CHAIN: A; MAJOR   PROTEINS, SPERMADHESINS, CUB                                           SEMINAL PLASMA   DOMAIN 2 ARCHITECTURE,                                           GLYCOPROTEIN PSP-II;   COMPLEX (SEMINAL PLASMA                                           CHAIN: B   PROTEIN/SPP)       429   1spp   B   218   323   2.5e−15   0.62   −0.07       MAJOR SEMINAL PLASMA   COMPLEX (SEMINAL PLASMA                                           GLYCOPROTEIN PSP-I;   PROTEIN/SPP) SEMINAL PLASMA                                           CHAIN: A; MAJOR   PROTEINS, SPERMADHESINS, CUB                                           SEMINAL PLASMA   DOMAIN 2 ARCHITECTURE,                                           GLYCOPROTEIN PSP-II;   COMPLEX (SEMINAL PLASMA                                           CHAIN: B   PROTEIN/SPP)       429   1spp   B   245   328   6.8e−06   0.38   0.09       MAJOR SEMINAL PLASMA   COMPLEX (SEMINAL PLASMA                                           GLYCOPROTEIN PSP-I;   PROTEIN/SPP) SEMINAL PLASMA                                           CHAIN: A; MAJOR   PROTEINS, SPERMADHESINS, CUB                                           SEMINAL PLASMA   DOMAIN 2 ARCHITECTURE,                                           GLYCOPROTEIN PSP-II;   COMPLEX (SEMINAL PLASMA                                           CHAIN: B   PROTEIN/SPP)       429   1urk       1   123   2.2e−23           69.71   PLASMINOGEN                                           ACTIVATION                                           PLASMINOGEN                                           ACTIVATOR (UROKINASE-                                           TYPE) (AMINO TERMINAL                                           FRAGMENT) (NMR, 15                                           STRUCTURES)       429   2hpp   P   36   119     5e−25           66.47   HYDROLASE(SERINE                                           PROTEINASE) ALPHA-                                           THROMBIN (E.C.3.4.21.5)                                           COMPLEX WITH 2HPP 3 D-                                           PHE-PRO-ARG-                                           CHLOROMETHYLKETONE                                           (PPACK)                                           CHLOROMETHYLKETONE                                           2HPP 4 REPLACED BY A                                           METHYLENE GROUP AND                                           BOVINE PROTHROMBIN                                           2HPP 5 FRAGMENT 2 2HPP 6       429   2hpp   P   36   119     5e−25   0.71   0.39       HYDROLASE(SERINE                                           PROTEINASE) ALPHA-                                           THROMBIN (E.C.3.4.21.5)                                           COMPLEX WITH 2HPP 3 D-                                           PHE-PRO-ARG-                                           CHLOROMETHYLKETONE                                           (PPACK)                                           CHLOROMETHYLKETONE                                           2HPP 4 REPLACED BY A                                           METHYLENE GROUP AND                                           BOVINE PROTHROMBIN                                           2HPP 5 FRAGMENT 2 2HPP 6       429   2hpq   P   36   119   1.2e−24           60.25   HYDROLASE(SERINE                                           PROTEINASE) ALPHA-                                           THROMBIN (E.C.3.4.21.5)                                           COMPLEX WITH 2HPQ 3 D-                                           PHE-PRO-ARG-                                           CHLOROMETHYLKETONE                                           (PPACK)                                           CHLOROMETHYLKETONE                                           2HPQ 4 REPLACED BY A                                           METHYLENE GROUP AND                                           HUMAN PROTHROMBIN                                           2HPQ 5 FRAGMENT 2                                           2HPQ 6       429   2pf1       20   119   2.3e−25   0.85   0.71       HYDROLASE(SERINE                                           PROTEINASE)                                           PROTHROMBIN                                           FRAGMENT 1                                           (RESIDUES 1-156)                                           2PF1 3       429   2pf1       5   131   2.3e−25           58.78   HYDROLASE(SERINE                                           PROTEINASE)                                           PROTHROMBIN                                           FRAGMENT 1                                           (RESIDUES 1-156)                                           2PF1 3       429   2pf2       35   119   2.5e−25   0.82   0.77       HYDROLASE(SERINE                                           PROTEASE)                                           PROTHROMBIN                                           FRAGMENT 1                                           (RESIDUES 1-156)                                           COMPLEX WITH                                           2PF2 3 CALCIUM 2PF2 4       429   3kiv       35   119     5e−27           76.56   APOLIPOPROTEIN; CHAIN:   KRINGLE KRINGLE, LYSINE                                           NULL;   BINDING SITE,                                               APOLIPOPROTEIN(A)       429   3kiv       35   119     5e−27   0.76   0.87       APOLIPOPROTEIN; CHAIN:   KRINGLE KRINGLE, LYSINE                                           NULL;   BINDING SITE,                                               APOLIPOPROTEIN(A)       429   5hpg   A   35   122     1e−26           77.19   PLASMINOGEN; CHAIN: A,   SERINE PROTEASE SERINE                                           B;   PROTEASE, KRINGLE 5, HUMAN                                               PLASMINOGEN, FIBRINOLYSIS       429   5hpg   A   35   122     1e−26   0.65   0.70       PLASMINOGEN; CHAIN: A,   SERINE PROTEASE SERINE                                           B;   PROTEASE, KRINGLE 5, HUMAN                                               PLASMINOGEN, FIBRINOLYSIS       429   9wga   A   21   168   1.7e−13   0.15   −0.12       LECTIN (AGGLUTININ)                                           WHEAT GERM                                           AGGLUTININ (ISOLECTIN                                           2) 9WGA 3       429   9wga   A   51   234   3.4e−10   0.16   −0.19       LECTIN (AGGLUTININ)                                           WHEAT GERM                                           AGGLUTININ (ISOLECTIN                                           2) 9WGA 3       448   1a14   L   20   126   3.4e−25           55.31   NEURAMINIDASE; CHAIN:   COMPLEX (ANTIBODY/ANTIGEN)                                           N; SINGLE CHAIN   COMPLEX (ANTIBODY/ANTIGEN),                                           ANTIBODY; CHAIN: H, L;   SINGLE-CHAIN ANTIBODY, 2                                               GLYCOSYLATED PROTEIN       448   1a2y   A   20   126   5.1e−27           54.70   MONOCLONAL   COMPLEX                                           ANTIBODY D1.3; CHAIN:   (IMMUNOGLOBULIN/HYDROLASE)                                           A, B; LYSOZYME; CHAIN:   COMPLEX                                           C;   (IMMUNOGLOBULIN/HYDROLASE),                                               IMMUNOGLOBULIN V 2 REGION,                                               SIGNAL, HYDROLASE,                                               GLYCOSIDASE, BACTERIOLYTIC 3                                               ENZYME, EGG WHITE       448   1a7q   L   20   136   1.5e−25           52.86   MONOCLONAL   IMMUNOGLOBULIN                                           ANTIBODY D1.3; CHAIN:   IMMUNOGLOBULIN, VARIANT                                           L, H;       448   1ao7   E   22   142   3.4e−46   −0.08   0.06       HLA-A 0201; CHAIN: A;   COMPLEX (MHC/VIRAL                                           BETA-2 MICROGLOBULIN;   PEPTIDE/RECEPTOR) HLA-A2                                           CHAIN: B; TAX PEPTIDE;   HEAVY CHAIN; CLASS I MHC, T-                                           CHAIN: C; T CELL   CELL RECEPTOR, VIRAL PEPTIDE, 2                                           RECEPTOR ALPHA;   COMPLEX (MHC/VIRAL                                           CHAIN: D; T CELL   PEPTIDE/RECEPTOR                                           RECEPTOR BETA; CHAIN:                                           E;       448   1ap2   A   20   128   5.1e−30           51.96   MONOCLONAL   IMMUNOGLOBULIN VARIABLE                                           ANTIBODY C219; CHAIN:   DOMAIN; SINGLE CHAIN FV,                                           A, B, C, D;   MONOCLONAL ANTIBODY, C219, P-                                               GLYCOPROTEIN, 2                                               IMMUNOGLOBULIN       448   1ar1   D   20   136   3.4e−26           52.90   CYTOCHROME C   COMPLEX                                           OXIDASE; CHAIN: A, B;   (OXIDOREDUCTASE/ANTIBODY)                                           ANTIBODY FV   CYTOCHROME AA3, COMPLEX IV,                                           FRAGMENT; CHAIN: C, D;   FERROCYTOCHROME C, COMPLEX                                               (OXIDOREDUCTASE/ANTIBODY),                                               ELECTRON TRANSPORT, 2                                               TRANSMEMBRANE, CYTOCHROME                                               OXIDASE, ANTIBODY COMPLEX       448   1b0w   A   20   127   5.1e−27           55.43   BENCE-JONES KAPPA 1   IMMUNE SYSTEM BENCE-JONES;                                           PROTEIN BRE; CHAIN: A,   IMMUNOGLOBULIN, AMYLOID,                                           B, C;   IMMUNE SYSTEM       448   1bd2   E   22   160   1.7e−48   −0.10   0.07       HLA-A 0201; CHAIN: A;   COMPLEX (MHC/VIRAL                                           BETA-2 MICROGLOBULIN;   PEPTIDE/RECEPTOR) HLA A2                                           CHAIN: B; TAX PEPTIDE;   HEAVY CHAIN; COMPLEX                                           CHAIN: C; T CELL   (MHC/VIRAL PEPTIDE/RECEPTOR)                                           RECEPTOR ALPHA;                                           CHAIN: D; T CELL                                           RECEPTOR BETA; CHAIN:                                           E;       448   1bec       23   143   1.7e−46   0.27   0.30       14.3.D T CELL ANTIGEN   RECEPTOR T CELL RECEPTOR 1BEC                                           RECEPTOR; 1BEC 6   14                                           CHAIN: NULL; 1BEC 6       448   1bfv   L   20   127   1.7e−25           51.18   FV4155; CHAIN: L, H;   IMMUNOGLOBULIN                                               IMMUNOGLOBULIN, FV                                               FRAGMENT, STEROID HORMONE, 2                                               FINE SPECIFICITY       448   1bvk   A   20   127   1.2e−29           57.64   HULYS11; CHAIN: A, B, D,   COMPLEX (HUMANIZED                                           E; LYSOZYME; CHAIN: C,   ANTIBODY/HYDROLASE)                                           F;   MURAMIDASE; HUMANIZED                                               ANTIBODY, ANTIBODY COMPLEX,                                               FV, ANTI-LYSOZYME, 2 COMPLEX                                               (HUMANIZED                                               ANTIBODY/HYDROLASE)       448   1bwm   A   23   138   3.4e−45   0.06   0.12       ALPHA-BETA T CELL   IMMUNE SYSTEM                                           RECEPTOR (TCR) (D10);   IMMUNOGLOBULIN,                                           CHAIN: A;   IMMUNORECEPTOR, IMMUNE                                               SYSTEM       448   1bww   A   18   126     1e−28           52.26   IG KAPPA CHAIN V-I   IMMUNE SYSTEM REIV,                                           REGION RE1; CHAIN: A, B;   STABILIZED IMMUNOGLOBULIN                                               FRAGMENT, BENCE-JONES 2                                               PROTEIN, IMMUNE SYSTEM       448   1d9k   B   23   138   3.4e−45   0.12   0.34       T-CELL RECEPTOR D10   IMMUNE SYSTEM MHC I-AK; MHC                                           (ALPHA CHAIN); CHAIN:   I-AK; T-CELL RECEPTOR, MHC                                           A, E; T-CELL RECEPTOR   CLASS II, D10, I-AK                                           D10 (BETA CHAIN);                                           CHAIN: B, F; MHC I-AK A                                           CHAIN (ALPHA CHAIN);                                           CHAIN: C, G; MHC I-AK B                                           CHAIN (BETA CHAIN);                                           CHAIN: D, H;                                           CONALBUMIN PEPTIDE;                                           CHAIN: P, Q;       448   1d1f   L   20   127   8.5e−26           54.31   ANTI-DANSYL   IMMUNOGLOBULIN ANTI-DANSYL                                           IMMUNOGLOBULIN   FV FRAGMENT FV FRAGMENT,                                           IGG2A(S); CHAIN: L, H;   IMMUNOGLOBULIN       448   1dsf   L   20   129   5.1e−23           53.77   ANTICANCER ANTIBODY   IMMUNOGLOBULIN B1DSFV;                                           B1; CHAIN: L, H;   MONOCLONAL ANTIBODY,                                               ANTITUMOR, IMMUNOGLOBULIN       448   1f11   A   20   159   6.8e−34   −0.00   0.07       F124 IMMUNOGLOBULIN   IMMUNE SYSTEM                                           (KAPPA LIGHT CHAIN);   IMMUNOGLOBULIN, ANTIBODY,                                           CHAIN: A, C; F124   FAB, HEPATITIS B, PRES2                                           IMMUNOGLOBULIN (IGG1                                           HEAVY CHAIN); CHAIN: B,                                           D;       448   1fgv   L   20   136   1.7e−31           55.11   IMMUNOGLOBULIN FV                                           FRAGMENT OF A                                           HUMANIZED VERSION OF                                           THE ANTI-CD18 1FGV 3                                           ANTIBODY ’H52’ (HUH52-                                           AAFV) 1FGV4       448   1fvc   A   20   128   6.8e−31           54.26   IMMUNOGLOBULIN FV                                           FRAGMENT OF                                           HUMANIZED ANTIBODY                                           4D5, VERSION 8 1FVC 3       448   1fyt   E   22   160   6.8e−44   0.05   0.10       HLA CLASS II   IMMUNE SYSTEM HLA-DR1, DRA;                                           HISTOCOMPATIBILITY   HLA-DR1, DRB1 0101; TCR HA1.7                                           ANTIGEN, DR CHAIN: A;   ALPHA CHAIN; TCR HA1.7 BETA                                           HLA CLASS II   CHAIN; PROTEIN-PROTEIN                                           HISTOCOMPATIBILITY   COMPLEX, IMMUNOGLOBULIN                                           ANTIGEN, DR-1 CHAIN: B;   FOLD                                           HEMAGGLUTININ HA1                                           PEPTIDE CHAIN; CHAIN:                                           C; T-CELL RECEPTOR                                           ALPHA CHAIN; CHAIN: D;                                           T-CELL RECEPTOR BETA                                           CHAIN; CHAIN: E;       448   1igm   L   20   134   5.1e−30           57.34   IMMUNOGLOBULIN                                           IMMUNOGLOBULIN M                                           (IG-M) FV FRAGMENT                                           1IGM 3       448   1ivl   A   20   126     1e−24           60.97   IMMUNOGLOBULIN                                           IMMUNOGLOBULIN VL                                           DOMAIN (VARIABLE                                           DOMAIN OF KAPPA LIGHT                                           1IVL 3 CHAIN) OF                                           DESIGNED ANTIBODY                                           M29B 1IVL 4       448   1jhl   L   20   127   3.4e−28           57.95   COMPLEX(ANTIBODY-                                           ANTIGEN) FV FRAGMENT                                           (IGG1, KAPPA) (LIGHT                                           AND HEAVY VARIABLE                                           DOMAINS 1JHL 3 NON-                                           COVALENTLY                                           ASSOCIATED) OF                                           MONOCLONAL ANTI-HEN                                           EGG 1JHL 4 LYSOZYME                                           ANTIBODY D11.15                                           COMPLEX WITH                                           PHEASANT EGG 1JHL 5                                           LYSOZYME 1JHL 6       448   1kb5   B   21   136   1.7e−33           50.75   KB5-C20 T-CELL ANTIGEN   COMPLEX                                           RECEPTOR; CHAIN: A, B;   (IMMUNOGLOBULIN/RECEPTOR)                                           ANTIBODY DESTIRE-1;   TCR VAPLHA VBETA DOMAIN; T-                                           CHAIN: L, H;   CELL RECEPTOR, STRAND SWITCH,                                               FAB, ANTICLONOTYPIC, 2                                               (IMMUNOGLOBULIN/RECEPTOR)       448   1maj       20   127   6.8e−24           50.59   IMMUNOGLOBULIN                                           MURINE ANTIBODY 26-10                                           VL DOMAIN (NMR, 15                                           ENERGY MINIMIZED                                           1MAJ 3 STRUCTURES)                                           1MAJ 4       448   1nfd   B   20   143     1e−45   0.08   0.27       N15 ALPHA-BETA T-CELL   COMPLEX                                           RECEPTOR; CHAIN: A, B,   (IMMUNORECEPTOR/                                               IMMUNOGLOBULIN)                                           C, D; H57 FAB; CHAIN: E, F,   COMPLEX                                           G, H   (IMMUNORECEPTOR/                                               IMMUNOGLOBULIN)       448   1nmb   L   20   128   8.5e−27           58.89   N9 NEURAMINIDASE;   COMPLEX                                           1NMB 4 CHAIN: N; 1NMB 5   (HYDROLASE/IMMUNOGLOBULIN)                                           FAB NC10; 1NMB 9 CHAIN:                                           L, H; 1NMB 10       448   1rvf   L   20   130   5.1e−26           54.02   HUMAN RHINOVIRUS 14   COMPLEX (COAT                                           COAT PROTEIN; CHAIN: 1,   PROTEIN/IMMUNOGLOBULIN)                                           2,3,4; FAB 17-IA; CHAIN:   POLYPROTEIN, COAT PROTEIN,                                           L, H   CORE PROTEIN, RNA-DIRECTED                                               RNA 2 POLYMERASE, HYDROLASE,                                               THIOL PROTEASE,                                               MYRISTYLATION, 3 COMPLEX                                               (COAT                                               PROTEIN/IMMUNOGLOBULIN)       448   1sbs   L   20   159   1.2e−33   0.10   0.33       MONOCLONAL   MONOCLONAL ANTIBODY                                           ANTIBODY 3A2; CHAIN: H,   MONOCLONAL ANTIBODY, FAB-                                           L;   FRAGMENT, REPRODUCTION       448   1tcr   B   20   143     1e−45   0.06   0.17       ALPHA, BETA T-CELL   RECEPTOR TCR; T-CELL,                                           RECEPTOR CHAIN: A, B;   RECEPTOR, TRANSMEMBRANE,                                               GLYCOPROTEIN, SIGNAL       448   1wtl   A   20   127   6.8e−28           54.08   IMMUNOGLOBULIN WAT,                                           A VARIABLE DOMAIN                                           FROM IMMUNOGLOBULIN                                           LIGHT-CHAIN 1WTL 3                                           (BENCE-JONES PROTEIN)                                           1WTL 4       448   2rhe       21   130   1.7e−24           52.52   IMMUNOGLOBULIN                                           BENCE-*JONES PROTEIN                                           (LAMBDA, VARIABLE                                           DOMAIN) 2RHE 4       449   1fo1   A   1   53   0.00012   −0.34   0.12       NUCLEAR RNA EXPORT   RNA BINDING PROTEIN TAP                                           FACTOR 1; CHAIN: A, B;   (NFX1); RIBONUCLEOPROTEIN                                               (RNP, RBD OR RRM) AND LEUCINE-                                               RICH-REPEAT 2 (LRR)       454   1dt6   A   60   248   8.5e−52   −0.41   0.05       CYTOCHROME P450 2C5;   OXIDOREDUCTASE                                           CHAIN: A;   PROGESTERONE 21-                                               HYDROXYLASE, CYPIIC5 P450 1,                                               MEMBRANE PROTEIN,                                               PROGESTERONE 21-                                               HYDROXYLASE, BENZO(A) 2                                               PYRENE HYDROXYLASE,                                               ESTRADIOL 2-HYDROXYLASE,                                               P450, CYP2C5       459   1b0u   A   129   254   5.1e−24   0.37   0.36       HISTIDINE PERMEASE;   TRANSPORT PROTEIN ABC                                           CHAIN: A;   TRANSPORTER, HISP; ABC                                               TRANSPORTER, HISTIDINE                                               PERMEASE, TRANSPORT PROTEIN       459   1f2u   A   141   175   0.0025   −0.78   0.09       RAD50 ABC-ATPASE;   REPLICATION DNA DOUBLE-                                           CHAIN: A, C; RAD50 ABC-   STRAND BREAK REPAIR, ABC-                                           ATPASE; CHAIN: B, D;   ATPASE       459   1f2u   A   160   213   0.0048   −0.91   0.12       RAD50 ABC-ATPASE;   REPLICATION DNA DOUBLE-                                           CHAIN: A, C; RAD50 ABC-   STRAND BREAK REPAIR, ABC-                                           ATPASE; CHAIN: B, D;   ATPASE       459   1g29   1   142   253   3.4e−21   −0.28   0.34       MALTOSE TRANSPORT   SUGAR BINDING PROTEIN MALK;                                           PROTEIN MALK; CHAIN: 1,   ATPASE, ACTIVE TRANSPORT,                                           2;   MALTOSE UPTAKE AND                                               REGULATION       459   1gky       158   184   0.0027   −0.82   0.28       TRANSFERASE                                           GUANYLATE KINASE                                           (E.C.2.7.4.8) COMPLEX                                           WITH 1GKY 3 GUANOSINE                                           MONOPHOSPHATE 1GKY 4       461   1e3y   A   103   159   0.0025   0.21   0.52       FADD PROTEIN; CHAIN: A;   APOPTOSIS FAS-ASSOCIATING                                               DEATH DOMAIN-CONTAINING                                               PROTEIN; DEATH DOMAIN,                                               ADAPTER MOLECULE, FAS                                               RECEPTOR DEATH INDUCING 2                                               SIGNALLING COMPLEX       461   1fad   A   103   150   0.00075   0.14   1.00       FADD PROTEIN; CHAIN: A;   APOPTOSIS APOPTOSIS, FADD,                                               DEATH DOMAIN       461   1lrv       19   202   0.0018   0.32   0.03       LEUCINE-RICH REPEAT   LEUCINE-RICH REPEATS LRV;                                           VARIANT; CHAIN: NULL;   LEUCINE-RICH REPEATS,                                               REPETITIVE STRUCTURE, IRON                                               SULFUR 2 PROTEINS, NITROGEN                                               FIXATION       483   1fum   D   2   100   1.7e−44   −0.68   1.00       FUMARATE REDUCTASE   OXIDOREDUCTASE COMPLEX II;                                           FLAVOPROTEIN SUBUNIT;   COMPLEX II; COMPLEX II;                                           CHAIN: A, M; FUMARATE   COMPLEX II; FUMARATE                                           REDUCTASE IRON-   REDUCTASE, COMPLEX II,                                           SULFUR PROTEIN; CHAIN:   SUCCINATE DEHYDROGENASE, 2                                           B, N; FUMARATE   RESPIRATION, OXIDOREDUCTASE                                           REDUCTASE 15 KD                                           HYDROPHOBIC PROTEIN;                                           CHAIN: C, O; FUMARATE                                           REDUCTASE 13 KD                                           HYDROPHOBIC PROTEIN;                                           CHAIN: D, P;       483   1fum   D   2   117   1.7e−44           168.49   FUMARATE REDUCTASE   OXIDOREDUCTASE COMPLEX II;                                           FLAVOPROTEIN SUBUNIT;   COMPLEX II; COMPLEX II;                                           CHAIN: A, M; FUMARATE   COMPLEX II; FUMARATE                                           REDUCTASE IRON-   REDUCTASE, COMPLEX II,                                           SULFUR PROTEIN; CHAIN:   SUCCINATE DEHYDROGENASE, 2                                           B, N; FUMARATE   RESPIRATION, OXIDOREDUCTASE                                           REDUCTASE 15 KD                                           HYDROPHOBIC PROTEIN;                                           CHAIN: C, O; FUMARATE                                           REDUCTASE 13 KD                                           HYDROPHOBIC PROTEIN;                                           CHAIN: D, P;       486   1qu7   A   154   214   2.5e−09   −0.49   0.90       METHYL-ACCEPTING   SIGNALING PROTEIN SERINE,                                           CHEMOTAXIS PROTEIN I;   CHEMOTAXIS, FOUR HELICAL-                                           CHAIN: A, B;   BUNDLE       486   2asr       38   71     5e−10   −0.81   0.51       CHEMOTAXIS                                           ASPARTATE RECEPTOR                                           (LIGAND BINDING                                           DOMAIN) 2ASR 3       486   2lig   A   26   71   2.5e−14   −0.79   0.47       ASPARTATE RECEPTOR;   CHEMOTAXIS                                           2LIG 4 CHAIN: A, B; 2LIG 5       490   1c17   M   130   265   0.001           73.12   ATP SYNTHASE SUBUNIT   MEMBRANE PROTEIN MEMBRANE                                           C; CHAIN: A, B, C, D, E, F,   PROTEIN, HELIX, COMPLEX                                           G, H, I, J, K, L; ATP                                           SYNTHASE SUBUNIT A;                                           CHAIN: M;       496   1d0s   A   2   91   1.3e−09   0.26   −0.20       NICOTINATE   TRANSFERASE DINUCLEOTIDE-                                           MONONUCLEOTIDE: 5, 6-   BINDING MOTIF,                                           CHAIN: A;   PHOSPHORIBOSYL TRANSFERASE       496   1eut       24   125     1e−09   0.40   −0.20       SIALIDASE; CHAIN: NULL;   HYDROLASE NEURAMINIDASE;                                               HYDROLASE, GLYCOSIDASE       496   2pro   A   10   136     1e−18   0.12   −0.20       ALPHA-LYTIC PROTEASE;   PRO REGION PRO REGION,                                           CHAIN: A, B, C;   FOLDASE, PROTEIN FOLDING,                                               SERINE PROTEASE       503   1c28   A   71   204   1.7e−34   0.72   0.89       30 KD ADIPOCYTE   SERUM PROTEIN ACRP30 C1Q TNF                                           COMPLEMENT-RELATED   TRIMER ALL-BETA, SERUM                                           PROTEIN CHAIN: A, B, C;   PROTEIN       503   1c28   A   73   203   6.8e−33   0.52   0.98       30 KD ADIPOCYTE   SERUM PROTEIN ACRP30 C1Q TNF                                           COMPLEMENT-RELATED   TRIMER ALL-BETA, SERUM                                           PROTEIN CHAIN: A, B, C;   PROTEIN       503   1c28   A   77   204   1.7e−34           64.45   30 KD ADIPOCYTE   SERUM PROTEIN ACRP30 C1Q TNF                                           COMPLEMENT-RELATED   TRIMER ALL-BETA, SERUM                                           PROTEIN CHAIN: A, B, C;   PROTEIN       503   1c28   B   73   203     1e−30   0.76   0.83       30 KD ADIPOCYTE   SERUM PROTEIN ACRP30 C1Q TNF                                           COMPLEMENT-RELATED   TRIMER ALL-BETA, SERUM                                           PROTEIN CHAIN: A, B, C;   PROTEIN       503   1c28   B   81   196     1e−30           53.80   30 KD ADIPOCYTE   SERUM PROTEIN ACRP30 C1Q TNF                                           COMPLEMENT-RELATED   TRIMER ALL-BETA, SERUM                                           PROTEIN CHAIN: A, B, C;   PROTEIN       503   1c28   C   73   203   8.5e−28   0.56   0.37       30 KD ADIPOCYTE   SERUM PROTEIN ACRP30 C1Q TNF                                           COMPLEMENT-RELATED   TRIMER ALL-BETA, SERUM                                           PROTEIN CHAIN: A, B, C;   PROTEIN       514   4hb1       290   328   0.00051   0.28   0.53       DHP1; CHAIN: NULL;   DESIGNED HELICAL BUNDLE                                               DESIGNED HELICAL BUNDLE       526   1aut   L   97   202   2.5e−13           51.11   ACTIVATED PROTEIN C;   COMPLEX (BLOOD                                           CHAIN: C, L; D-PHE-PRO-   COAGULATION/INHIBITOR)                                           MAI; CHAIN: P;   AUTOPROTHROMBIN IIA;                                               HYDROLASE, SERINE                                               PROTEINASE), PLASMA CALCIUM                                               BINDING, 2 GLYCOPROTEIN,                                               COMPLEX (BLOOD                                               COAGULATION/INHIBITOR)       526   1dan   L   114   245     5e−16           53.38   BLOOD COAGULATION   BLOOD COAGULATION, SERINE                                           FACTOR VIIA; CHAIN: L,   PROTEASE, COMPLEX, CO-FACTOR,                                           H; SOLUBLE TISSUE   2 RECEPTOR ENZYME, INHIBITOR,                                           FACTOR; CHAIN: T, U; D-   GLA, EGF, 3 COMPLEX (SERINE                                           PHE-PHE-ARG-   PROTEASE/COFACTOR/LIGAND)                                           CHLOROMETHYLKETONE                                           (DFFRCMK) WITH CHAIN:                                           C;       526   1dan   L   151   232   8.5e−12   0.07   0.30       BLOOD COAGULATION   BLOOD COAGULATION, SERINE                                           FACTOR VIIA; CHAIN: L,   PROTEASE, COMPLEX, CO-FACTOR,                                           H; SOLUBLE TISSUE   2 RECEPTOR ENZYME, INHIBITOR,                                           FACTOR; CHAIN: T, U; D-   GLA, EGF, 3 COMPLEX (SERINE                                           PHE-PHE-ARG-   PROTEASE/COFACTOR/LIGAND)                                           CHLOROMETHYLKETONE                                           (DFFRCMK) WITH CHAIN:                                           C;       526   1dan   L   32   154   2.5e−15   0.23   −0.13       BLOOD COAGULATION   BLOOD COAGULATION, SERINE                                           FACTOR VIIA; CHAIN: L,   PROTEASE, COMPLEX, CO-FACTOR,                                           H; SOLUBLE TISSUE   2 RECEPTOR ENZYME, INHIBITOR,                                           FACTOR; CHAIN: T, U; D-   GLA, EGF, 3 COMPLEX (SERINE                                           PHE-PHE-ARG-   PROTEASE/COFACTOR/LIGAND)                                           CHLOROMETHYLKETONE                                           (DFFRCMK) WITH CHAIN:                                           C;       526   1dan   L   82   197     5e−16   0.45   −0.12       BLOOD COAGULATION   BLOOD COAGULATION, SERINE                                           FACTOR VIIA; CHAIN: L,   PROTEASE, COMPLEX, CO-FACTOR,                                           H; SOLUBLE TISSUE   2 RECEPTOR ENZYME, INHIBITOR,                                           FACTOR; CHAIN: T, U; D-   GLA, EGF, 3 COMPLEX (SERINE                                           PHE-PHE-ARG-   PROTEASE/COFACTOR/LIGAND)                                           CHLOROMETHYLKETONE                                           (DFFRCMK) WITH CHAIN:                                           C;       526   1dva   L   151   232   8.5e−12   −0.02   0.63       DES-GLA FACTOR VIIA   HYDROLASE/HYDROLASE                                           (HEAVY CHAIN); CHAIN:   INHIBITOR PROTEIN-PEPTIDE                                           H, I; DES-GLA FACTOR   COMPLEX                                           VIIA (LIGHT CHAIN);                                           CHAIN: L, M; (DPN)-PHE-                                           ARG; CHAIN: C, D;                                           PEPTIDE E-76; CHAIN: X,                                           Y;       526   1dx5   I   107   225   2.5e−15   0.30   0.04       THROMBIN LIGHT CHAIN;   SERINE PROTEINASE                                           CHAIN: A, B, C, D;   COAGULATION FACTOR II;                                           THROMBIN HEAVY   COAGULATION FACTOR II;                                           CHAIN; CHAIN: M, N, O, P;   FETOMODULIN, TM, CD141                                           THROMBOMODULIN;   ANTIGEN; EGR-CMK SERINE                                           CHAIN: I, J, K, L;   PROTEINASE, EGF-LIKE DOMAINS,                                           THROMBIN INHIBITOR L-   ANTICOAGULANT COMPLEX, 2                                           GLU-L-GLY-L-ARM;   ANTIFIBRINOLYTIC COMPLEX                                           CHAIN: E, F, G, H;       526   1dx5   I   149   259   6.8e−14   −0.00   −0.18       THROMBIN LIGHT CHAIN;   SERINE PROTEINASE                                           CHAIN: A, B, C, D;   COAGULATION FACTOR II;                                           THROMBIN HEAVY   COAGULATION FACTOR II;                                           CHAIN; CHAIN: M, N, O, P;   FETOMODULIN, TM, CD141                                           THROMBOMODULIN;   ANTIGEN; EGR-CMK SERINE                                           CHAIN: I, J, K, L;   PROTEINASE, EGF-LIKE DOMAINS,                                           THROMBIN INHIBITOR L-   ANTICOAGULANT COMPLEX, 2                                           GLU-L-GLY-L-ARM;   ANTIFIBRINOLYTIC COMPLEX                                           CHAIN: E, F, G, H;       526   1dx5   I   70   193     2e−16   0.42   −0.12       THROMBIN LIGHT CHAIN;   SERINE PROTEINASE                                           CHAIN: A, B, C, D;   COAGULATION FACTOR II;                                           THROMBIN HEAVY   COAGULATION FACTOR II;                                           CHAIN; CHAIN: M, N, O, P;   FETOMODULIN, TM, CD141                                           THROMBOMODULIN;   ANTIGEN; EGR-CMK SERINE                                           CHAIN: I, J, K, L;   PROTEINASE, EGF-LIKE DOMAINS,                                           THROMBIN INHIBITOR L-   ANTICOAGULANT COMPLEX, 2                                           GLU-L-GLY-L-ARM;   ANTIFIBRINOLYTIC COMPLEX                                           CHAIN: E, F, G, H;       526   1ext   A   33   173     5e−15   0.13   −0.15       TUMOR NECROSIS   SIGNALLING PROTEIN BINDING                                           FACTOR RECEPTOR;   PROTEIN, CYTOKINE, SIGNALLING                                           CHAIN: A, B;   PROTEIN       526   1ext   A   53   203   1.8e−15           65.24   TUMOR NECROSIS   SIGNALLING PROTEIN BINDING                                           FACTOR RECEPTOR;   PROTEIN, CYTOKINE, SIGNALLING                                           CHAIN: A, B;   PROTEIN       526   1ext   A   54   197   1.8e−15   0.30   −0.06       TUMOR NECROSIS   SIGNALLING PROTEIN BINDING                                           FACTOR RECEPTOR;   PROTEIN, CYTOKINE, SIGNALLING                                           CHAIN: A, B;   PROTEIN       526   1fak   L   151   232   8.5e−12   −0.08   0.78       BLOOD COAGULATION   BLOOD CLOTTING                                           FACTOR VIIA; CHAIN: L;   COMPLEX (SERINE                                           BLOOD COAGULATION   PROTEASE/COFACTOR/LIGAND),                                           FACTOR VIIA; CHAIN: H;   BLOOD COAGULATION, 2 SERINE                                           SOLUBLE TISSUE   PROTEASE, COMPLEX, CO-FACTOR,                                           FACTOR; CHAIN: T; 5L15;   RECEPTOR ENZYME, 3 INHIBITOR,                                           CHAIN: I;   GLA, EGF, COMPLEX (SERINE 4                                               PROTEASE/COFACTOR/LIGAND),                                               BLOOD CLOTTING       526   1igr   A   8   214     1e−21   0.15   −0.12       INSULIN-LIKE GROWTH   HORMONE RECEPTOR HORMONE                                           FACTOR RECEPTOR 1;   RECEPTOR, INSULIN RECEPTOR                                           CHAIN: A;   FAMILY       526   1klo       111   237   3.4e−17   0.52   0.88       LAMININ; CHAIN: NULL;   GLYCOPROTEIN GLYCOPROTEIN       526   1klo       154   268   8.5e−16   0.34   0.10       LAMININ; CHAIN: NULL;   GLYCOPROTEIN GLYCOPROTEIN       526   1klo       31   198   2.5e−29   0.39   0.01       LAMININ; CHAIN: NULL;   GLYCOPROTEIN GLYCOPROTEIN       526   1klo       33   199   2.5e−29           91.67   LAMININ; CHAIN: NULL;   GLYCOPROTEIN GLYCOPROTEIN       526   1klo       68   197   1.2e−18   0.51   0.90       LAMININ; CHAIN: NULL;   GLYCOPROTEIN GLYCOPROTEIN       526   1klo       68   218   2.5e−26   0.24   −0.14       LAMININ; CHAIN: NULL;   GLYCOPROTEIN GLYCOPROTEIN       526   1ncf   A   39   180     5e−17   0.23   −0.07       TUMOR NECROSIS   SIGNALLING PROTEIN TYPE I                                           FACTOR RECEPTOR; 1NCF   RECEPTOR, STNFR1; 1NCF 8                                           4 CHAIN: A, B; 1NCF 5   BINDING PROTEIN, CYTOKINE                                               1NCF 19       526   1ncf   A   51   180     5e−17           54.09   TUMOR NECROSIS   SIGNALLING PROTEIN TYPE I                                           FACTOR RECEPTOR; 1NCF   RECEPTOR, STNFR1; 1NCF 8                                           4 CHAIN: A, B; 1NCF 5   BINDING PROTEIN, CYTOKINE                                               1NCF 19       526   1ncf   A   96   218   2.5e−16   0.33   −0.14       TUMOR NECROSIS   SIGNALLING PROTEIN TYPE I                                           FACTOR RECEPTOR; 1NCF   RECEPTOR, STNFR1; 1NCF 8                                           4 CHAIN: A, B; 1NCF 5   BINDING PROTEIN, CYTOKINE                                               1NCF 19       526   1pfx   L   64   214   1.8e−26   0.20   −0.18       FACTOR IXA; CHAIN: C,   COMPLEX (BLOOD                                           L,; D-PHE-PRO-ARG;   COAGULATION/INHIBITOR)                                           CHAIN: I;   CHRISTMAS FACTOR; COMPLEX,                                               INHIBITOR, HEMOPHILIA/EGF,                                               BLOOD COAGULATION, 2 PLASMA,                                               SERINE PROTEASE, CALCIUM-                                               BINDING, HYDROLASE, 3                                               GLYCOPROTEIN       526   1pfx   L   72   208     5e−28           62.61   FACTOR IXA; CHAIN: C,   COMPLEX (BLOOD                                           L,; D-PHE-PRO-ARG;   COAGULATION/INHIBITOR)                                           CHAIN: I;   CHRISTMAS FACTOR; COMPLEX,                                               INHIBITOR, HEMOPHILIA/EGF,                                               BLOOD COAGULATION, 2 PLASMA,                                               SERINE PROTEASE, CALCIUM-                                               BINDING, HYDROLASE, 3                                               GLYCOPROTEIN       526   1pp2   R   64   184     1e−17   0.13   −0.18       HYDROLASE CALCIUM-                                           FREE PHOSPHOLIPASE                                           A = 2 = (E.C.3.1.1.4)                                           1PP2 4       526   1qfk   L   107   206   7.5e−17   0.34   −0.02       COAGULATION FACTOR   SERINE PROTEASE FVIIA; FVIIA;                                           VIIA (LIGHT CHAIN);   BLOOD COAGULATION, SERINE                                           CHAIN: L; COAGULATION   PROTEASE                                           FACTOR VIIA (HEAVY                                           CHAIN); CHAIN: H;                                           TRIPEPTIDYL INHIBITOR;                                           CHAIN: C;       526   1qfk   L   151   232   8.5e−12   0.04   0.83       COAGULATION FACTOR   SERINE PROTEASE FVIIA; FVIIA;                                           VIIA (LIGHT CHAIN);   BLOOD COAGULATION, SERINE                                           CHAIN: L; COAGULATION   PROTEASE                                           FACTOR VIIA (HEAVY                                           CHAIN); CHAIN: H;                                           TRIPEPTIDYL INHIBITOR;                                           CHAIN: C;       526   1qub   A   11   297   2.5e−33           60.56   HUMAN BETA2-   MEMBRANE ADHESION SHORT                                           GLYCOPROTEIN I; CHAIN:   CONSENSUS REPEAT, SUSHI,                                           A;   COMPLEMENT CONTROL PROTEIN,                                               2 N-GLYCOSYLATION, MULTI-                                               DOMAIN, MEMBRANE ADHESION       526   1skz       106   216   2.5e−20           66.23   ANTISTASIN; CHAIN:   SERINE PROTEASE INHIBITOR                                           NULL;   FACTOR XA INHIBITOR;                                               ANTISTASIN, CRYSTAL                                               STRUCTURE, FACTOR XA                                               INHIBITOR, 2 SERINE PROTEASE                                               INHIBITOR, THROMBOSIS       526   1skz       64   216   2.5e−20   0.18   0.21       ANTISTASIN; CHAIN:   SERINE PROTEASE INHIBITOR                                           NULL;   FACTOR XA INHIBITOR;                                               ANTISTASIN, CRYSTAL                                               STRUCTURE, FACTOR XA                                               INHIBITOR, 2 SERINE PROTEASE                                               INHIBITOR, THROMBOSIS       526   1tpg       37   143   2.2e−18   0.38   0.11       T-PLASMINOGEN   PLASMINOGEN ACTIVATION                                           ACTIVATOR F1-G; 1TPG 7                                           CHAIN: NULL; 1TPG 8       526   1tpg       81   184     5e−18   0.49   −0.08       T-PLASMINOGEN   PLASMINOGEN ACTIVATION                                           ACTIVATOR F1-G; 1TPG 7                                           CHAIN: NULL; 1TPG 8       526   1vap   A   70   184   1.8e−15   −0.14   0.00       PHOSPHOLIPASE A2;   LIPID DEGRADATION                                           CHAIN: A, B;   PHOSPHOLIPASE A2, LIPID                                               DEGRADATION, HYDROLASE       526   1xka   L   70   154     5e−15   0.14   0.18       BLOOD COAGULATION   BLOOD COAGULATION FACTOR                                           FACTOR XA; CHAIN: L, C;   STUART FACTOR; BLOOD                                               COAGULATION FACTOR, SERINE                                               PROTEINASE, EPIDERMAL 2                                               GROWTH FACTOR LIKE DOMAIN       526   2not   A   34   137     5e−15   0.11   −0.13       PHOSPHOLIPASE A2;   HYDROLASE HYDROLASE, LIPID                                           CHAIN: A, B;   DEGRADATION, CALCIUM,                                               PRESYNAPTIC 2 NEUROTOXIN,                                               VENOM       526   9wga   A   20   181   1.7e−16   0.20   0.05       LECTIN (AGGLUTININ)                                           WHEAT GERM                                           AGGLUTININ (ISOLECTIN                                           2) 9WGA 3       526   9wga   A   31   180   2.5e−27   0.32   −0.17       LECTIN (AGGLUTININ)                                           WHEAT GERM                                           AGGLUTININ (ISOLECTIN                                           2) 9WGA 3       526   9wga   A   53   219     5e−30           79.05   LECTIN (AGGLUTININ)                                           WHEAT GERM                                           AGGLUTININ (ISOLECTIN                                           2) 9WGA 3       526   9wga   A   55   229   3.4e−15   0.39   0.10       LECTIN (AGGLUTININ)                                           WHEAT GERM                                           AGGLUTININ (ISOLECTIN                                           2) 9WGA 3       526   9wga   A   64   218     5e−30   0.79   −0.05       LECTIN (AGGLUTININ)                                           WHEAT GERM                                           AGGLUTININ (ISOLECTIN                                           2) 9WGA 3       533   1ckl   A   12   132   8.5e−11   −0.11   0.05       CD46; CHAIN: A, B, C, D, E,   GLYCOPROTEIN MEMBRANE                                           F;   COFACTOR PROTEIN (MCP); VIRUS                                               RECEPTOR, COMPLEMENT                                               COFACTOR, SHORT CONSENSUS                                               REPEAT, 2 SCR, MEASLES VIRUS,                                               GLYCOPROTEIN       533   1ckl   A   67   131     5e−11   0.36   0.03       CD46; CHAIN: A, B, C, D, E,   GLYCOPROTEIN MEMBRANE                                           F;   COFACTOR PROTEIN (MCP); VIRUS                                               RECEPTOR, COMPLEMENT                                               COFACTOR, SHORT CONSENSUS                                               REPEAT, 2 SCR, MEASLES VIRUS,                                               GLYCOPROTEIN       533   1e5g   A   72   192   3.4e−14   0.10   0.24       COMPLEMENT CONTROL   COMPLEMENT INHIBITOR VCP,                                           PROTEIN; CHAIN: A;   SP35; COMPLEMENT, NMR,                                               MODULES, PROTEIN STRUCTURE,                                               VACCINIA VIRUS       533   1e5g   A   73   155   1.3e−15   0.11   0.24       COMPLEMENT CONTROL   COMPLEMENT INHIBITOR VCP,                                           PROTEIN; CHAIN: A;   SP35; COMPLEMENT, NMR,                                               MODULES, PROTEIN STRUCTURE,                                               VACCINIA VIRUS       533   1hcc       73   132     5e−10   0.35   0.57       GLYCOPROTEIN 16TH                                           COMPLEMENT CONTROL                                           PROTEIN (/CCP$) OF                                           FACTOR H 1HCC 3       533   1hfh       70   192   1.3e−10           51.85   GLYCOPROTEIN FACTOR                                           H, 15TH AND 16TH C-                                           MODULE PAIR (NMR,                                           MINIMIZED 1HFHA 1                                           AVERAGED STRUCTURE)                                           1HFH 4 1HFHA 5       533   1hfh       71   155   1.3e−10   0.36   0.22       GLYCOPROTEIN FACTOR                                           H, 15TH AND 16TH C-                                           MODULE PAIR (NMR,                                           MINIMIZED 1HFHA 1                                           AVERAGED STRUCTURE)                                           1HFH 4 1HFHA 5       533   1qub   A   21   297   3.4e−27           56.46   HUMAN BETA2-   MEMBRANE ADHESION SHORT                                           GLYCOPROTEIN I; CHAIN:   CONSENSUS REPEAT, SUSHI,                                           A;   COMPLEMENT CONTROL PROTEIN,                                               2 N-GLYCOSYLATION, MULTI-                                               DOMAIN, MEMBRANE ADHESION       533   1sfp       129   245   2.3e−27           51.76   ASFP; CHAIN: NULL;   SPERMADHESIN ACIDIC SEMINAL                                               PROTEIN; SPERMADHESIN, BOVINE                                               SEMINAL PLASMA PROTEIN,                                               ACIDIC 2 SEMINAL FLUID PROTEIN,                                               ASFP, CUB DOMAIN, X-RAY                                               CRYSTAL 3 STRUCTURE, GROWTH                                               FACTOR       533   1sfp       135   242   2.3e−27   0.38   0.81       ASFP; CHAIN: NULL;   SPERMADHESIN ACIDIC SEMINAL                                               PROTEIN; SPERMADHESIN, BOVINE                                               SEMINAL PLASMA PROTEIN,                                               ACIDIC 2 SEMINAL FLUID PROTEIN,                                               ASFP, CUB DOMAIN, X-RAY                                               CRYSTAL 3 STRUCTURE, GROWTH                                               FACTOR       533   1sfp       155   244   1.7e−07   0.01   0.16       ASFP; CHAIN: NULL;   SPERMADHESIN ACIDIC SEMINAL                                               PROTEIN; SPERMADHESIN, BOVINE                                               SEMINAL PLASMA PROTEIN,                                               ACIDIC 2 SEMINAL FLUID PROTEIN,                                               ASFP, CUB DOMAIN, X-RAY                                               CRYSTAL 3 STRUCTURE, GROWTH                                               FACTOR       533   1spp   A   135   242     5e−28   0.38   0.71       MAJOR SEMINAL PLASMA   COMPLEX (SEMINAL PLASMA                                           GLYCOPROTEIN PSP-I;   PROTEIN/SPP) SEMINAL PLASMA                                           CHAIN: A; MAJOR   PROTEINS, SPERMADHESINS, CUB                                           SEMINAL PLASMA   DOMAIN 2 ARCHITECTURE,                                           GLYCOPROTEIN PSP-II;   COMPLEX (SEMINAL PLASMA                                           CHAIN: B   PROTEIN/SPP)       533   1spp   B   129   242     5e−29   0.36   0.62       MAJOR SEMINAL PLASMA   COMPLEX (SEMINAL PLASMA                                           GLYCOPROTEIN PSP-I;   PROTEIN/SPP) SEMINAL PLASMA                                           CHAIN: A; MAJOR   PROTEINS, SPERMADHESINS, CUB                                           SEMINAL PLASMA   DOMAIN 2 ARCHITECTURE,                                           GLYCOPROTEIN PSP-II;   COMPLEX (SEMINAL PLASMA                                           CHAIN: B   PROTEIN/SPP)       533   1vvc       10   127   3.4e−15   0.24   −0.14       VACCINIA VIRUS   COMPLEMENT INHIBITOR SP35,                                           COMPLEMENT CONTROL   VCP, VACCINIA VIRUS SP35;                                           PROTEIN; CHAIN: NULL;   COMPLEMENT INHIBITOR,                                               COMPLEMENT MODULE, SCR,                                               SUSHI DOMAIN, 2 MODULE PAIR       533   1vvc       72   194   1.7e−12   0.09   0.25       VACCINIA VIRUS   COMPLEMENT INHIBITOR SP35,                                           COMPLEMENT CONTROL   VCP, VACCINIA VIRUS SP35;                                           PROTEIN; CHAIN: NULL;   COMPLEMENT INHIBITOR,                                               COMPLEMENT MODULE, SCR,                                               SUSHI DOMAIN, 2 MODULE PAIR       533   1vvc       72   196   1.7e−12           50.78   VACCINIA VIRUS   COMPLEMENT INHIBITOR SP35,                                           COMPLEMENT CONTROL   VCP, VACCINIA VIRUS SP35;                                           PROTEIN; CHAIN: NULL;   COMPLEMENT INHIBITOR,                                               COMPLEMENT MODULE, SCR,                                               SUSHI DOMAIN, 2 MODULE PAIR       542   1lba       230   375     5e−39   0.08   0.05       HYDROLASE(ACTING ON                                           LINEAR AMIDES)                                           LYSOZYME (E.C.3.5.1.28)                                           MUTANT WITH ALA 6                                           REPLACED BY LYS 1LBA 3                                           AND RESIDUES 2-5                                           DELETED (DEL(2-5), A6K)                                           1LBA 4       542   1lba       258   359   1.7e−23   0.03   0.33       HYDROLASE(ACTING ON                                           LINEAR AMIDES)                                           LYSOZYME (E.C.3.5.1.28)                                           MUTANT WITH ALA 6                                           REPLACED BY LYS 1LBA 3                                           AND RESIDUES 2-5                                           DELETED (DEL(2-5), A6K)                                           1LBA 4       542   1lba       72   232   2.5e−23           54.86   HYDROLASE(ACTING ON                                           LINEAR AMIDES)                                           LYSOZYME (E.C.3.5.1.28)                                           MUTANT WITH ALA 6                                           REPLACED BY LYS 1LBA 3                                           AND RESIDUES 2-5                                           DELETED (DEL(2-5), A6K)                                           1LBA 4       542   1lba       74   214   2.5e−23   0.26   0.55       HYDROLASE(ACTING ON                                           LINEAR AMIDES)                                           LYSOZYME (E.C.3.5.1.28)                                           MUTANT WITH ALA 6                                           REPLACED BY LYS 1LBA 3                                           AND RESIDUES 2-5                                           DELETED (DEL(2-5), A6K)                                           1LBA 4       542   1lba       81   175   3.4e−23   0.66   0.88       HYDROLASE(ACTING ON                                           LINEAR AMIDES)                                           LYSOZYME (E.C.3.5.1.28)                                           MUTANT WITH ALA 6                                           REPLACED BY LYS 1LBA 3                                           AND RESIDUES 2-5                                           DELETED (DEL(2-5), A6K)                                           1LBA 4       543   1c2a   A   35   148   0.0027   −0.45   0.03       BOWMAN-BIRK TRYPSIN   HYDROLASE INHIBITOR ALL-BETA                                           INHIBITOR; CHAIN: A   STRUCTURE, HYDROLASE                                               INHIBITOR       546   1c17   M   110   248   1.2e−07           79.86   ATP SYNTHASE SUBUNIT   MEMBRANE PROTEIN MEMBRANE                                           C; CHAIN: A, B, C, D, E, F,   PROTEIN, HELIX, COMPLEX                                           G, H, I, J, K, L; ATP                                           SYNTHASE SUBUNIT A;                                           CHAIN: M;       560   1b8q   A   223   353   1.2e−13           50.34   NEURONAL NITRIC OXIDE   OXIDOREDUCTASE PDZ DOMAIN,                                           SYNTHASE; CHAIN: A;   NNOS, NITRIC OXIDE SYNTHASE                                           HEPTAPEPTIDE; CHAIN: B;       560   1b8q   A   224   302   1.2e−13   0.05   0.88       NEURONAL NITRIC OXIDE   OXIDOREDUCTASE PDZ DOMAIN,                                           SYNTHASE; CHAIN: A;   NNOS, NITRIC OXIDE SYNTHASE                                           HEPTAPEPTIDE; CHAIN: B;       560   1b8q   A   313   429   1.8e−17   0.38   0.11       NEURONAL NITRIC OXIDE   OXIDOREDUCTASE PDZ DOMAIN,                                           SYNTHASE; CHAIN: A;   NNOS, NITRIC OXIDE SYNTHASE                                           HEPTAPEPTIDE; CHAIN: B;       560   1be9   A   116   229   1.7e−14   −0.22   0.70       PSD-95; CHAIN: A; CRIPT;   PEPTIDE RECOGNITION PEPTIDE                                           CHAIN: B;   RECOGNITION, PROTEIN                                               LOCALIZATION       560   1be9   A   221   337   1.3e−09           51.39   PSD-95; CHAIN: A; CRIPT;   PEPTIDE RECOGNITION PEPTIDE                                           CHAIN: B;   RECOGNITION, PROTEIN                                               LOCALIZATION       560   1be9   A   230   338   1.3e−09   0.71   1.00       PSD-95; CHAIN: A; CRIPT;   PEPTIDE RECOGNITION PEPTIDE                                           CHAIN: B;   RECOGNITION, PROTEIN                                               LOCALIZATION       560   1be9   A   315   380     1e−10   0.07   0.18       PSD-95; CHAIN: A; CRIPT;   PEPTIDE RECOGNITION PEPTIDE                                           CHAIN: B;   RECOGNITION, PROTEIN                                               LOCALIZATION       560   1be9   A   349   413     1e−10   −0.39   0.28       PSD-95; CHAIN: A; CRIPT;   PEPTIDE RECOGNITION PEPTIDE                                           CHAIN: B;   RECOGNITION, PROTEIN                                               LOCALIZATION       560   1i16       231   330     2e−10   −0.19   0.01       INTERLEUKIN 16; CHAIN:   CYTOKINE LCF; CYTOKINE,                                           NULL;   LYMPHOCYTE                                               CHEMOATTRACTANT FACTOR, PDZ                                               DOMAIN       560   1i16       282   413   2.5e−16           52.15   INTERLEUKIN 16; CHAIN:   CYTOKINE LCF; CYTOKINE,                                           NULL;   LYMPHOCYTE                                               CHEMOATTRACTANT FACTOR, PDZ                                               DOMAIN       560   1i16       315   388   2.5e−16   0.93   1.00       INTERLEUKIN 16; CHAIN:   CYTOKINE LCF; CYTOKINE,                                           NULL;   LYMPHOCYTE                                               CHEMOATTRACTANT FACTOR, PDZ                                               DOMAIN       560   1kwa   A   234   321   1.5e−11   0.44   1.00       HCASK/LIN-2 PROTEIN;   KINASE HCASK, GLGF REPEAT,                                           CHAIN: A, B;   DHR; PDZ DOMAIN,                                               NEUREXIN,                                               SYNDECAN, RECEPTOR                                               CLUSTERING, KINASE       560   1kwa   A   313   388   2.3e−16   0.21   1.00       HCASK/LIN-2 PROTEIN;   KINASE HCASK, GLGF REPEAT,                                           CHAIN: A, B;   DHR; PDZ DOMAIN, NEUREXIN,                                               SYNDECAN, RECEPTOR                                               CLUSTERING, KINASE       560   1pdr       122   218   1.2e−13   −0.25   0.27       HUMAN DISCS LARGE   SIGNAL TRANSDUCTION HDLG,                                           PROTEIN; CHAIN: NULL;   DHR3 DOMAIN; SIGNAL                                               TRANSDUCTION, SH3 DOMAIN,                                               REPEAT       560   1pdr       228   295   2.5e−12   0.23   0.99       HUMAN DISCS LARGE   SIGNAL TRANSDUCTION HDLG,                                           PROTEIN; CHAIN: NULL;   DHR3 DOMAIN; SIGNAL                                               TRANSDUCTION, SH3 DOMAIN,                                               REPEAT       560   1pdr       311   380     2e−12   0.41   0.82       HUMAN DISCS LARGE   SIGNAL TRANSDUCTION HDLG,                                           PROTEIN; CHAIN: NULL;   DHR3 DOMAIN; SIGNAL                                               TRANSDUCTION, SH3 DOMAIN,                                               REPEAT       560   1qau   A   117   224   7.5e−15   0.12   −0.01       NEURONAL NITRIC OXIDE   OXIDOREDUCTASE BETA-FINGER                                           SYNTHASE (RESIDUES                                           1-130);                                           CHAIN: A;       560   1qau   A   231   346   2.3e−13   0.45   0.83       NEURONAL NITRIC OXIDE   OXIDOREDUCTASE BETA-FINGER                                           SYNTHASE (RESIDUES                                           1-130);                                           CHAIN: A;       560   1qau   A   313   388     5e−16   0.88   1.00       NEURONAL NITRIC OXIDE   OXIDOREDUCTASE BETA-FINGER                                           SYNTHASE (RESIDUES                                           1-130);                                           CHAIN: A;       560   1qav   A   114   212   1.5e−15   0.01   1.00       ALPHA-1 SYNTROPHIN   MEMBRANE                                           (RESIDUES 77-171);   PROTEIN/OXIDOREDUCTASE BETA-                                           CHAIN: A; NEURONAL   FINGER, HETERODIMER                                           NITRIC OXIDE SYNTHASE                                           (RESIDUES 1-130); CHAIN:                                           B;       560   1qav   A   229   309   7.5e−12   0.68   1.00       ALPHA-1 SYNTROPHIN   MEMBRANE                                           (RESIDUES 77-171);   PROTEIN/OXIDOREDUCTASE BETA-                                           CHAIN: A; NEURONAL   FINGER, HETERODIMER                                           NITRIC OXIDE SYNTHASE                                           (RESIDUES 1-130); CHAIN:                                           B;       560   1qav   A   311   388     2e−16   0.66   1.00       ALPHA-1 SYNTROPHIN   MEMBRANE                                           (RESIDUES 77-171);   PROTEIN/OXIDOREDUCTASE BETA-                                           CHAIN: A; NEURONAL   FINGER, HETERODIMER                                           NITRIC OXIDE SYNTHASE                                           (RESIDUES 1-130); CHAIN:                                           B;       560   1qlc   A   116   213     5e−15   0.81   0.89       POSTSYNAPTIC DENSITY   PEPTIDE RECOGNITION PSD-95;                                           PROTEIN 95; CHAIN: A;   PDZ DOMAIN, NEURONAL NITRIC                                               OXIDE SYNTHASE, NMDA                                               RECEPTOR 2 BINDING       560   1qlc   A   120   213   5.1e−15   0.36   0.22       POSTSYNAPTIC DENSITY   PEPTIDE RECOGNITION PSD-95;                                           PROTEIN 95; CHAIN: A;   PDZ DOMAIN, NEURONAL NITRIC                                               OXIDE SYNTHASE, NMDA                                               RECEPTOR 2 BINDING       560   1qlc   A   229   309   1.5e−09   0.68   1.00       POSTSYNAPTIC DENSITY   PEPTIDE RECOGNITION PSD-95;                                           PROTEIN 95; CHAIN: A;   PDZ DOMAIN, NEURONAL NITRIC                                               OXIDE SYNTHASE, NMDA                                               RECEPTOR 2 BINDING       560   1qlc   A   311   388   1.5e−14   0.75   1.00       POSTSYNAPTIC DENSITY   PEPTIDE RECOGNITION PSD-95;                                           PROTEIN 95; CHAIN: A;   PDZ DOMAIN, NEURONAL NITRIC                                               OXIDE SYNTHASE, NMDA                                               RECEPTOR 2 BINDING       560   3pdz   A   113   212     5e−15   0.36   0.96       TYROSINE PHOSPHATASE   HYDROLASE PDZ DOMAIN, HUMAN                                           (PTP-BAS, TYPE 1); CHAIN:   PHOSPHATASE, HPTP1E, PTP-BAS,                                           A;   SPECIFICITY 2 OF BINDING       560   3pdz   A   227   324   7.5e−12   0.47   0.99       TYROSINE PHOSPHATASE   HYDROLASE PDZ DOMAIN, HUMAN                                           (PTP-BAS, TYPE 1); CHAIN:   PHOSPHATASE, HPTP1E, PTP-BAS,                                           A;   SPECIFICITY 2 OF BINDING       560   3pdz   A   311   388   2.5e−15   1.23   1.00       TYROSINE PHOSPHATASE   HYDROLASE PDZ DOMAIN, HUMAN                                           (PTP-BAS, TYPE 1); CHAIN:   PHOSPHATASE, HPTP1E, PTP-BAS,                                           A;   SPECIFICITY 2 OF BINDING       563   1a0j   A   36   265   0           235.32   TRYPSIN; CHAIN: A, B, C,   SERINE PROTEASE SERINE                                           D;   PROTEINASE, TRYPSIN,                                               HYDROLASE       563   1a0j   A   36   265   0   1.07   1.00       TRYPSIN; CHAIN: A, B, C,   SERINE PROTEASE SERINE                                           D;   PROTEINASE, TRYPSIN,                                               HYDROLASE       563   1a01   A   36   264   5.1e−82           167.61   BETA-TRYPTASE; CHAIN:   SERINE PROTEINASE TRYPSIN-                                           A, B, C, D;   LIKE SERINE PROTEINASE,                                               TETRAMER, HEPARIN, ALLERGY, 2                                               ASTHMA       563   1a5i   A   23   263   2.5e−83           173.85   PLASMINOGEN   COMPLEX (SERINE                                           ACTIVATOR; CHAIN: A;   PROTEASE/INHIBITOR)                                           GLU-GLY-ARG   (DELTAFEK)DSPAALPHA1;                                           CHLOROMETHYL   EGRCMK; SERINE PROTEASE,                                           KETONE; CHAIN: I;   FIBRINOLYTIC ENZYMES,                                               PLASMINOGEN 2 ACTIVATORS       563   1ao5   A   36   266   2.5e−96           226.34   GLANDULAR   SERINE PROTEASE PRORENIN                                           KALLIKREIN-13; CHAIN:   CONVERTING ENZYME (PRECE),                                           A, B;   EPIDERMAL GLANDULAR                                               KALLIKREIN, SERINE PROTEASE,                                               PROTEIN MATURATION       563   1ao5   A   38   264   2.5e−96   1.16   1.00       GLANDULAR   SERINE PROTEASE PRORENIN                                           KALLIKREIN-13; CHAIN:   CONVERTING ENZYME (PRECE),                                           A, B;   EPIDERMAL GLANDULAR                                               KALLIKREIN, SERINE PROTEASE,                                               PROTEIN MATURATION       563   1aut   C   36   263   2.2e−88           172.05   ACTIVATED PROTEIN C;   COMPLEX (BLOOD                                           CHAIN: C, L; D-PHE-PRO-   COAGULATION/INHIBITOR)                                           MAI; CHAIN: P;   AUTOPROTHROMBIN IIA;                                               HYDROLASE, SERINE                                               PROTEINASE), PLASMA CALCIUM                                               BINDING, 2 GLYCOPROTEIN,                                               COMPLEX (BLOOD                                               COAGULATION/INHIBITOR)       563   1bio       36   263     5e−89           198.56   COMPLEMENT FACTOR D;   SERINE PROTEASE SERINE                                           CHAIN: NULL;   PROTEASE, HYDROLASE,                                               COMPLEMENT, FACTOR D,                                               CATALYTIC 2 TRIAD, SELF-                                               REGULATION       563   1bqy   A   36   271     1e−92           205.81   PLASMINOGEN   BLOOD CLOTTING TSV-PA;                                           ACTIVATOR; CHAIN: A, B;   FIBRINOLYSIS, PLASMINOGEN                                           GLU-GLY-ARG-   ACTIVATOR, SERINE PROTEINASE,                                           CHLOROMETHYLKETONE   2 SNAKE VENOM, COMPLEX                                           INHIBITOR; CHAIN: E, F;   (HYDROLASE/INHIBITOR), BLOOD                                               CLOTTING       563   1cgh   A   36   264   3.4e−74           175.67   CATHEPSIN G; CHAIN: A;   COMPLEX (SERINE                                           PHOSPHONATE   PROTEASE/INHIBITOR)                                           INHIBITOR SUC-VAL-PRO-   INFLAMMATION, INHIBITOR,                                           PHEP-(OPH)2; CHAIN: S;   SPECIFICITY, SERINE PROTEASE, 2                                               COMPLEX (SERINE                                               PROTEASE/INHIBITOR)       563   1dpo       36   265     1e−97           226.55   TRYPSIN; CHAIN: NULL;   SERINE PROTEASE HYDROLASE,                                               SERINE PROTEASE, DIGESTION,                                               PANCREAS, ZYMOGEN, 2 SIGNAL,                                               MULTIGENE FAMILY       563   1fxy   A   36   266   1.7e−91           218.47   COAGULATION FACTOR   COMPLEX (PROTEASE/INHIBITOR)                                           XA-TRYPSIN CHIMERA;   TRYPSIN, COAGULATION FACTOR                                           CHAIN: A; D-PHE-PRO-   XA, CHIMERA, PROTEASE, PPACK, 2                                           ARG-   CHLOROMETHYLKETONE,                                           CHLOROMETHYLKETONE   COMPLEX (PROTEASE/                                               INHIBITOR)                                           (PPACK) WITH CHAIN: I;       563   1mct   A   36   265   0           234.27   COMPLEX(PROTEINASE/                                               INHIBITOR)                                           TRYPSIN                                           (E.C.3.4.21.4) COMPLEXED                                           WITH INHIBITOR FROM                                           BITTER 1MCT 3 GOURD                                           1MCT 4       563   1mct   A   36   265   0   1.20   1.00       COMPLEX(PROTEINASE/                                           INHIBITOR)                                           TRYPSIN                                           (E.C.3.4.21.4) COMPLEXED                                           WITH INHIBITOR FROM                                           BITTER 1MCT 3 GOURD                                           1MCT 4       563   1npm   A   36   263     5e−94           253.14   NEUROPSIN; CHAIN: A, B;   SERINE PROTEINASE SERINE                                               PROTEINASE, GLYCOPROTEIN       563   1pfx   C   36   263     5e−91           177.42   FACTOR IXA; CHAIN: C,   COMPLEX (BLOOD                                           L,; D-PHE-PRO-ARG;   COAGULATION/INHIBITOR)                                           CHAIN: I;   CHRISTMAS FACTOR; COMPLEX,                                               INHIBITOR, HEMOPHILIA/EGF,                                               BLOOD COAGULATION, 2 PLASMA,                                               SERINE PROTEASE, CALCIUM-                                               BINDING, HYDROLASE, 3                                               GLYCOPROTEIN       563   1qrz   A   21   265   1.7e−88           176.03   PLASMINOGEN; CHAIN: A,   HYDROLASE                                           B, C, D;   MICROPLASMINOGEN, SERINE                                               PROTEASE, ZYMOGEN,                                               CHYMOTRYPSIN 2 FAMILY,                                               HYDROLASE       563   1rfn   A   36   263   1.3e−90           177.83   COAGULATION FACTOR   COAGULATION FACTOR SERINE                                           IX; CHAIN: A;   PROTEINASE, BLOOD                                           COAGULATION FACTOR   COAGULATION, COAGULATION                                           IX; CHAIN: B;   FACTOR       563   1rtf   B   36   264     1e−84           177.39   TWO CHAIN TISSUE   SERINE PROTEASE (TC)-T-PA;                                           PLASMINOGEN   SERINE PROTEASE, FIBRINOLYTIC                                           ACTIVATOR; CHAIN: A, B;   ENZYMES       563   1sgf   A   45   266   7.5e−83           179.65   NERVE GROWTH FACTOR;   GROWTH FACTOR 7S NGF;                                           CHAIN: A, B, G, X, Y, Z;   GROWTH FACTOR (BETA-NGF),                                               HYDROLASE - SERINE PROTEINASE                                               2 (GAMMA-NGF), INACTIVE SERINE                                               PROTEINASE (ALPHA-NGF)       563   1sgf   G   36   265   8.5e−99   1.03   1.00       NERVE GROWTH FACTOR;   GROWTH FACTOR 7S NGF;                                           CHAIN: A, B, G, X, Y, Z;   GROWTH FACTOR (BETA-NGF),                                               HYDROLASE - SERINE PROTEINASE                                               2 (GAMMA-NGF), INACTIVE SERINE                                               PROTEINASE (ALPHA-NGF)       563   1sgf   G   36   266   8.5e−99           248.29   NERVE GROWTH FACTOR;   GROWTH FACTOR 7S NGF;                                           CHAIN: A, B, G, X, Y, Z;   GROWTH FACTOR (BETA-NGF),                                               HYDROLASE - SERINE PROTEINASE                                               2 (GAMMA-NGF), INACTIVE SERINE                                               PROTEINASE (ALPHA-NGF)       563   1slw   B   36   265     1e−99           223.23   ECOTIN; CHAIN: A;   COMPLEX (SERINE                                           ANIONIC TRYPSIN;   PROTEASE/INHIBITOR) TRYPSIN                                           CHAIN: B;   INHIBITOR; SERINE PROTEASE,                                               INHIBITOR, COMPLEX, METAL                                               BINDING SITES, 2 PROTEIN                                               ENGINEERING, PROTEASE-                                               SUBSTRATE INTERACTIONS, 3                                               METALLOPROTEINS       563   1slw   B   36   265     1e−99   1.25   1.00       ECOTIN; CHAIN: A;   COMPLEX (SERINE                                           ANIONIC TRYPSIN;   PROTEASE/INHIBITOR) TRYPSIN                                           CHAIN: B;   INHIBITOR; SERINE PROTEASE,                                               INHIBITOR, COMPLEX, METAL                                               BINDING SITES, 2 PROTEIN                                               ENGINEERING, PROTEASE-                                               SUBSTRATE INTERACTIONS, 3                                               METALLOPROTEINS       563   1ton       36   266     5e−97           232.87   HYDROLASE(SERINE                                           PROTEINASE) TONIN (E.C.                                           NUMBER NOT ASSIGNED)                                           1TON 4       563   1ton       38   264     5e−97   1.16   1.00       HYDROLASE(SERINE                                           PROTEINASE) TONIN (E.C.                                           NUMBER NOT ASSIGNED)                                           1TON 4       563   1trn   A   36   266   0           229.81   HYDROLASE (SERINE                                           PROTEINASE) TRYPSIN                                           (E.C.3.4.21.4) COMPLEXED                                           WITH THE INHIBITOR                                           1TRN 3 DIISOPROPYL-                                           FLUOROPHOSPHOFLUORI                                           DATE (DFP) 1TRN 4                                           HUMAN TRYPSIN, DFP                                           INHIBITED 1TRN 6       563   1trn   A   36   266   0   1.00   1.00       HYDROLASE (SERINE                                           PROTEINASE) TRYPSIN                                           (E.C.3.4.21.4) COMPLEXED                                           WITH THE INHIBITOR                                           1TRN 3 DIISOPROPYL-                                           FLUOROPHOSPHOFLUORI                                           DATE (DFP) 1TRN 4                                           HUMAN TRYPSIN, DFP                                           INHIBITED 1TRN 6       563   2tbs       36   265     1e−99           222.15   HYDROLASE (SERINE                                           PROTEINASE) TRYPSIN                                           (E.C.3.4.21.4) COMPLEXED                                           WITH BENZAMIDINE                                           INHIBITOR 2TBS 3       563   2tbs       36   265     1e−99   1.04   1.00       HYDROLASE (SERINE                                           PROTEINASE) TRYPSIN                                           (E.C.3.4.21.4) COMPLEXED                                           WITH BENZAMIDINE                                           INHIBITOR 2TBS 3       563   5ptp       36   265   0           230.52   BETA TRYPSIN; CHAIN:   SERINE PROTEASE HYDROLASE,                                           NULL;   SERINE PROTEASE, DIGESTION,                                               PANCREAS, 2 ZYMOGEN, SIGNAL       563   5ptp       36   265   0   1.26   1.00       BETA TRYPSIN; CHAIN:   SERINE PROTEASE HYDROLASE,                                           NULL;   SERINE PROTEASE, DIGESTION,                                               PANCREAS, 2 ZYMOGEN, SIGNAL       572   1epf   A   18   124     5e−07   0.22   0.33       NEURAL CELL ADHESION   CELL ADHESION NCAM; NCAM,                                           MOLECULE; CHAIN: A, B,   IMMUNOGLOBULIN FOLD,                                           C, D;   GLYCOPROTEIIN       572   1f5w   A   15   107     1e−06   0.02   0.36       COXSACKIE VIRUS AND   VIRUS/VIRAL PROTEIN RECEPTOR                                           ADENOVIRUS RECEPTOR;   IMMUNOGLOBULIN V DOMAIN                                           CHAIN: A, B;   FOLD, SYMMETRIC DIMER       572   1fhg   A   22   109   2.5e−07   0.09   0.06       TELOKIN; CHAIN: A   CONTRACTILE PROTEIN                                               IMMUNOGLOBULIN FOLD, BETA                                               BARREL       572   1tnm       22   107   2.5e−06   0.11   0.11       MUSCLE PROTEIN TITIN                                           MODULE M5                                           (CONNECTIN) 1TNM 3                                           (NMR, MINIMIZED                                           AVERAGE STRUCTURE)                                           1TNM 4 1TNM 58       572   2ncm       20   109     2e−06   0.12   0.30       NEURAL CELL ADHESION   CELL ADHESION NCAM DOMAIN 1;                                           MOLECULE; CHAIN:   CELL ADHESION, GLYCOPROTEIN,                                           NULL;   HEPARIN-BINDING, GPI-ANCHOR, 2                                               NEURAL ADHESION MOLECULE,                                               IMMUNOGLOBULIN FOLD, SIGNAL       572   3ncm   A   22   109     5e−07   −0.09   0.12       NEURAL CELL ADHESION   CELL ADHESION PROTEIN NCAM                                           MOLECULE, LARGE   MODULE 2; CELL ADHESION,                                           ISOFORM; CHAIN: A;   GLYCOPROTEIN, HEPARIN-                                               BINDING, GPI-ANCHOR, 2 NEURAL                                               ADHESION MOLECULE,                                               IMMUNOGLOBULIN FOLD,                                               HOMOPHILIC 3 BINDING, CELL                                               ADHESION PROTEIN       580   1cfe       60   219   5.1e−42   0.22   1.00       PATHOGENESIS-RELATED   PATHOGENESIS-RELATED PROTEIN                                           PROTEIN P14A; CHAIN:   PATHOGENESIS-RELATED LEAF                                           NULL;   PROTEIN 6, ETHYLENE                                               PATHOGENESIS-RELATED                                               PROTEIN, PR-1 PROTEINS, 2 PLANT                                               DEFENSE       580   1cfe       61   219   5.1e−42           75.76   PATHOGENESIS-RELATED   PATHOGENESIS-RELATED PROTEIN                                           PROTEIN P14A; CHAIN:   PATHOGENESIS-RELATED LEAF                                           NULL;   PROTEIN 6, ETHYLENE                                               PATHOGENESIS-RELATED                                               PROTEIN, PR-1 PROTEINS, 2 PLANT                                               DEFENSE       580   1qnx   A   58   220   1.7e−42   0.33   1.00       VES V 5; CHAIN: A;   ALLERGEN ANTIGEN 5; ANTIGEN 5,                                               ALLERGEN, VESPID VENOM       594   1def       63   229   3.4e−46           62.32   PEPTIDE DEFORMYLASE;   HYDROLASE HYDROLASE, ZINC                                           CHAIN: NULL;   METALLOPROTEASE       595   1c44   A   92   211   8.5e−37   0.82   0.99       STEROL CARRIER   LIPID BINDING PROTEIN NON                                           PROTEIN 2; CHAIN: A;   SPECIFIC LIPID BINDING PROTEIN;                                               STEROL CARRIER PROTEIN, NON                                               SPECIFIC LIPID TRANSFER                                               PROTEIN, 2 FATTY ACID BINDING,                                               FATTY ACYL COA BINDING       596   1edh   A   46   166   3.4e−17   −0.18   0.25       E-CADHERIN; CHAIN: A,   CELL ADHESION PROTEIN                                           B;   EPITHELIAL CADHERIN DOMAINS 1                                               AND 2, ECAD12; CADHERIN, CELL                                               ADHESION PROTEIN, CALCIUM                                               BINDING PROTEIN       596   1edh   A   51   164   1.7e−23   0.24   0.98       E-CADHERIN; CHAIN: A,   CELL ADHESION PROTEIN                                           B;   EPITHELIAL CADHERIN DOMAINS 1                                               AND 2, ECAD12; CADHERIN, CELL                                               ADHESION PROTEIN, CALCIUM                                               BINDING PROTEIN       596   1ncg       45   138   7.5e−17   0.44   0.93       N-CADHERIN; 1NCG 3   CELL ADHESION PROTEIN                                               CADHERIN 1NCG 13       596   1nci   B   45   140     5e−16   −0.22   0.63       N-CADHERIN; 1NCI 3   CELL ADHESION PROTEIN                                               CADHERIN 1NCI 13       596   1ncj   A   45   164     5e−20   0.22   0.86       N-CADHERIN; CHAIN: A;   CELL ADHESION PROTEIN CELL                                               ADHESION PROTEIN       596   1ncj   A   45   165   3.4e−19   −0.11   0.36       N-CADHERIN; CHAIN: A;   CELL ADHESION PROTEIN CELL                                               ADHESION PROTEIN       596   1suh       44   144     5e−24           55.29   EPITHELIAL CADHERIN;   CELL ADHESION UVOMORULIN;                                           CHAIN: NULL;   CADHERIN, CALCIUM BINDING,                                               CELL ADHESION       596   1suh       45   144   3.4e−09   0.31   0.59       EPITHELIAL CADHERIN;   CELL ADHESION UVOMORULIN;                                           CHAIN: NULL;   CADHERIN, CALCIUM BINDING,                                               CELL ADHESION       596   1suh       45   144     5e−24   0.66   0.98       EPITHELIAL CADHERIN;   CELL ADHESION UVOMORULIN;                                           CHAIN: NULL;   CADHERIN, CALCIUM BINDING,                                               CELL ADHESION       598   1hcn   B   15   126     1e−45           94.05   HORMONE HUMAN                                           CHORIONIC                                           GONADOTROPIN 1HCN 3       598   1hcn   B   16   125     1e−45   0.10   1.00       HORMONE HUMAN                                           CHORIONIC                                           GONADOTROPIN 1HCN 3       598   1hcn   B   17   126   1.7e−43   −0.14   1.00       HORMONE HUMAN                                           CHORIONIC                                           GONADOTROPIN 1HCN 3       624   1a14   H   20   139   5.1e−14           61.90   NEURAMINIDASE; CHAIN:   COMPLEX (ANTIBODY/                                               ANTIGEN)                                           N; SINGLE CHAIN   COMPLEX (ANTIBODY/ANTIGEN),                                           ANTIBODY; CHAIN: H, L;   SINGLE-CHAIN ANTIBODY, 2                                               GLYCOSYLATED PROTEIN       624   1a2y   A   19   134   3.4e−28           57.90   MONOCLONAL   COMPLEX                                           ANTIBODY D1.3; CHAIN:   (IMMUNOGLOBULIN/HYDROLASE)                                           A, B; LYSOZYME; CHAIN:   COMPLEX                                           C;   (IMMUNOGLOBULIN/HYDROLASE),                                               IMMUNOGLOBULIN V 2 REGION,                                               SIGNAL, HYDROLASE,                                               GLYCOSIDASE, BACTERIOLYTIC 3                                               ENZYME, EGG WHITE       624   1a7q   L   19   132   3.4e−26           56.95   MONOCLONAL   IMMUNOGLOBULIN                                           ANTIBODY D1.3; CHAIN:   IMMUNOGLOBULIN, VARIANT                                           L, H;       624   1adq   L   21   141   6.8e−46   0.39   0.95       IGG4 REA; CHAIN: A; RF-   COMPLEX                                           AN IGM/LAMBDA; CHAIN:   (IMMUNOGLOBULIN/                                               AUTOANTIGEN)                                           H, L;   COMPLEX                                               (IMMUNOGLOBULIN/                                               AUTOANTIGEN),                                               RHEUMATOID FACTOR 2 AUTO-                                               ANTIBODY COMPLEX       624   1ao7   D   20   142   2.3e−19           59.00   HLA-A 0201; CHAIN: A;   COMPLEX (MHC/VIRAL                                           BETA-2 MICROGLOBULIN;   PEPTIDE/RECEPTOR) HLA-A2                                           CHAIN: B; TAX PEPTIDE;   HEAVY CHAIN; CLASS I MHC, T-                                           CHAIN: C; T CELL   CELL RECEPTOR, VIRAL PEPTIDE, 2                                           RECEPTOR ALPHA;   COMPLEX (MHC/VIRAL                                           CHAIN: D; T CELL   PEPTIDE/RECEPTOR                                           RECEPTOR BETA; CHAIN:                                           E;       624   1ap2   A   19   133   3.4e−31           57.34   MONOCLONAL   IMMUNOGLOBULIN VARIABLE                                           ANTIBODY C219; CHAIN:   DOMAIN; SINGLE CHAIN FV,                                           A, B, C, D;   MONOCLONAL ANTIBODY, C219, P-                                               GLYCOPROTEIN, 2                                               IMMUNOGLOBULIN       624   1aqk   L   22   141   3.4e−50   0.07   0.95       FAB B7-15A2; CHAIN: L, H;   IMMUNOGLOBULIN HUMAN FAB,                                               ANTI-TETANUS TOXOID, HIGH                                               AFFINITY, CRYSTAL 2 PACKING                                               MOTIF, PROGRAMMING                                               PROPENSITY TO CRYSTALLIZE, 3                                               IMMUNOGLOBULIN       624   1ar1   D   19   129     1e−24           57.17   CYTOCHROME C   COMPLEX                                           OXIDASE; CHAIN: A, B;   (OXIDOREDUCTASE/ANTIBODY)                                           ANTIBODY FV   CYTOCHROME AA3, COMPLEX IV,                                           FRAGMENT; CHAIN: C, D;   FERROCYTOCHROME C, COMPLEX                                               (OXIDOREDUCTASE/ANTIBODY),                                               ELECTRON TRANSPORT, 2                                               TRANSMEMBRANE, CYTOCHROME                                               OXIDASE, ANTIBODY COMPLEX       624   1bow   A   19   127   1.7e−29           58.09   BENCE-JONES KAPPA I   IMMUNE SYSTEM BENCE-JONES;                                           PROTEIN BRE; CHAIN: A,   IMMUNOGLOBULIN, AMYLOID,                                           B, C;   IMMUNE SYSTEM       624   1bfv   L   19   135   8.5e−28           57.62   FV4155; CHAIN: L, H;   IMMUNOGLOBULIN                                               IMMUNOGLOBULIN, FV                                               FRAGMENT, STEROID HORMONE, 2                                               FINE SPECIFICITY       624   1bjm   A   21   142   5.1e−45   0.33   0.90       LOC - LAMBDA 1 TYPE   IMMUNOGLOBULIN BENCE-JONES                                           LIGHT-CHAIN DIMER;   PROTEIN; 1BJM 8 BENCE JONES,                                           1BJM 6 CHAIN: A, B; 1BJM 7   ANTIBODY, MULTIPLE                                               QUATERNARY STRUCTURES 1BJM                                               13       624   1bvk   A   19   135   5.1e−32           61.61   HULYS11; CHAIN: A, B, D,   COMPLEX (HUMANIZED                                           E; LYSOZYME; CHAIN: C,   ANTIBODY/HYDROLASE)                                           F;   MURAMIDASE; HUMANIZED                                               ANTIBODY, ANTIBODY COMPLEX,                                               FV, ANTI-LYSOZYME, 2 COMPLEX                                               (HUMANIZED                                               ANTIBODY/HYDROLASE)       624   1bww   A   17   132   1.7e−31           61.59   IG KAPPA CHAIN V-I   IMMUNE SYSTEM REIV,                                           REGION REI; CHAIN: A, B;   STABILIZED IMMUNOGLOBULIN                                               FRAGMENT, BENCE-JONES 2                                               PROTEIN, IMMUNE SYSTEM       624   1cd0   A   22   122   1.2e−46   0.57   1.00       JTO, A VARIABLE   IMMUNE SYSTEM                                           DOMAIN FROM LAMBDA-   IMMUNOGLOBULIN, BENCE-JONES                                           6 TYPE CHAIN: A, B;   PROTEIN, LAMDA-6       624   1dlf   L   19   135   3.4e−27           57.84   ANTI-DANSYL   IMMUNOGLOBULIN ANTI-DANSYL                                           IMMUNOGLOBULIN   FV FRAGMENT FV FRAGMENT,                                           IGG2A(S); CHAIN: L, H;   IMMUNOGLOBULIN       624   1fgv   L   19   134   1.7e−33           67.61   IMMUNOGLOBULIN FV                                           FRAGMENT OF A                                           HUMANIZED VERSION OF                                           THE ANTI-CD18 1FGV 3                                           ANTIBODY ’H52’ (HUH52-                                           AA FV) 1FGV 4       624   1fvc   A   19   136   3.4e−31           64.02   IMMUNOGLOBULIN FV                                           FRAGMENT OF                                           HUMANIZED ANTIBODY                                           4D5, VERSION 8 1FVC 3       624   1igm   L   19   144     1e−30           62.66   IMMUNOGLOBULIN                                           IMMUNOGLOBULIN M                                           (IG-M) FV FRAGMENT                                           1IGM 3       624   1maj       19   135   1.2e−25           56.76   IMMUNOGLOBULIN                                           MURINE ANTIBODY 26-10                                           VL DOMAIN (NMR, 15                                           ENERGY MINIMIZED                                           1MAJ 3 STRUCTURES)                                           1MAJ 4       624   1mel   A   22   145   3.4e−12           58.28   VH SINGLE-DOMAIN   COMPLEX (ANTIBODY/                                               ANTIGEN)                                           ANTIBODY; CHAIN: A, B;   CAB-LYS3 COMPLEX; CAMEL                                           LYSOZYME; CHAIN: L, M;   SINGLE-DOMAIN                                               ANTI-LYSOZYME,                                               COMPLEX 2 (ANTIBODY/                                               ANTIGEN)       624   1rvf   L   20   138   1.2e−31           62.39   HUMAN RHINOVIRUS 14   COMPLEX (COAT                                           COAT PROTIEN; CHAIN: 1,   PROTEIN/IMMUNOGLOBULIN)                                           2,3,4; FAB 17-IA; CHAIN:   POLYPROTEIN, COAT PROTEIN,                                           L, H   CORE PROTEIN, RNA-DIRECTED                                               RNA 2 POLYMERASE, HYDROLASE,                                               THIOL PROTEASE,                                               MYRISTYLATION, 3 COMPLEX                                               (COAT                                               PROTEIN/IMMUNOGLOBULIN)       624   1wtl   A   19   127   1.5e−31           60.42   IMMUNOGLOBULIN WAT,                                           A VARIABLE DOMAIN                                           FROM IMMUNOGLOBULIN                                           LIGHT-CHAIN 1WTL 3                                           (BENCE-JONES PROTEIN)                                           1WTL4       624   2cd0   A   23   122   5.1e−47   0.67   1.00       BENCE-JONES PROTEIN   IMMUNE SYSTEM                                           WIL, A VARIABLE   IMMUNOGLOBULIN, BENCE-JONES                                           DOMAIN FROM CHAIN: A,   PROTEIN, LAMBDA-6                                           B;       624   2fb4   L   20   142   1.7e−46   0.21   0.86       IMMUNOGLOBULIN                                           IMMUNOGLOBULIN FAB                                           2FB4 4       624   2imn       19   127   6.8e−33           60.82   IMUNOGLOBULIN                                           IMMUNOGLOBULIN VL                                           DOMAIN (VARIABLE                                           DOMAIN OF KAPPA 2IMN                                           3 LIGHT CHAIN) OF                                           MCPC603 MUTANT IN                                           WHICH 2IMN 4                                           COMPLEMENTARITY-                                           DETERMINING REGION I                                           HAS BEEN REPLACED BY                                           2IMN 5 THAT FROM                                           MOPC167 2IMN 6       624   2mcg   1   21   142   1.7e−52   0.32   0.72       IMMUNOGLOBULIN                                           IMMUNOGLOBULIN                                           LAMBDA LIGHT CHAIN                                           DIMER (/MCG$) 2MCG 3                                           (TRIGONAL FORM) 2MCG 4       624   2rhe       20   140   1.2e−44           68.90   IMMUNOGLOBULIN                                           BENCE-*JONES PROTEIN                                           (LAMBDA, VARIABLE                                           DOMAIN) 2RHE 4       624   2rhe       21   121   1.2e−44   0.59   1.00       IMMUNOGLOBULIN                                           BENCE-*JONES PROTEIN                                           (LAMBDA, VARIABLE                                           DOMAIN) 2RHE 4       624   43c9   A   19   134   1.7e−31           57.86   IMMUNOGLOBULIN   IMMUNOGLOBULIN                                           (LIGHT CHAIN); CHAIN: A,   IMMUNOGLOBULIN                                           C, E, G;                                           IMMUNOGLOBULIN                                           (HEAVY CHAIN); CHAIN:                                           B, D, F, H;       624   43c9   B   18   140   5.1e−15           61.03   IMMUNOGLOBULIN   IMMUNOGLOBULIN                                           (LIGHT CHAIN); CHAIN: A,   IMMUNOGLOBULIN                                           C, E, G;                                           IMMUNOGLOBULIN                                           (HEAVY CHAIN); CHAIN:                                           B, D, F, H;       624   7fab   L   21   141   1.4e−43   0.29   0.21       IMMUNOGLOBULIN                                           IMMUNOGLOBULIN FAB’                                           NEW (LAMBDA LIGHT                                           CHAIN) 7FAB 3       624   8fab   A   23   141   3.4e−44   0.31   0.84       IMMUNOGLOBULIN FAB                                           FRAGMENT FROM                                           HUMAN                                           IMMUNOGLOBULIN IGG1                                           (LAMBDA, HIL) 8FAB 3       627   1fxx   A   224   454   6.8e−97   0.07   1.00       EXONUCLEASE I; CHAIN:   HYDROLASE                                           A;   EXODEOXYRIBONUCLEASE I;                                               ALPHA-BETA DOMAIN, SH3-LIKE                                               DOMAIN, DNAQ SUPERFAMILY       636   1ao7   E   74   194   3.4e−53   0.46   1.00       HLA-A 0201; CHAIN: A;   COMPLEX (MHC/VIRAL                                           BETA-2 MICROGLOBULIN;   PEPTIDE/RECEPTOR) HLA-A2                                           CHAIN: B; TAX PEPTIDE;   HEAVY CHAIN; CLASS I MHC, T-                                           CHAIN: C; T CELL   CELL RECEPTOR, VIRAL PEPTIDE, 2                                           RECEPTOR ALPHA;   COMPLEX (MHC/VIRAL                                           CHAIN: D; T CELL   PEPTIDE/RECEPTOR                                           RECEPTOR BETA; CHAIN:                                           E;       636   1ao7   E   74   217   3.4e−53           80.28   HLA-A 0201; CHAIN: A;   COMPLEX (MHC/VIRAL                                           BETA-2 MICROGLOBULIN;   PEPTIDE/RECEPTOR) HLA-A2                                           CHAIN: B; TAX PEPTIDE;   HEAVY CHAIN; CLASS 1 MHC, T-                                           CHAIN: C; T CELL   CELL RECEPTOR, VIRAL PEPTIDE, 2                                           RECEPTOR ALPHA;   COMPLEX (MHC/VIRAL                                           CHAIN: D; T CELL   PEPTIDE/RECEPTOR                                           RECEPTOR BETA; CHAIN:                                           E;       636   1bd2   E   74   194   1e−55   0.58   1.00       HLA-A 0201; CHAIN: A;   COMPLEX (MHC/VIRAL                                           BETA-2 MICROGLOBULIN;   PEPTIDE/RECEPTOR) HLA A2                                           CHAIN: B; TAX PEPTIDE;   HEAVY CHAIN; COMPLEX                                           CHAIN: C; T CELL   (MHC/VIRAL PEPTIDE/RECEPTOR)                                           RECEPTOR ALPHA;                                           CHAIN: D; T CELL                                           RECEPTOR BETA; CHAIN:                                           E;       636   1bd2   E   74   217   1e−55           62.05   HLA-A 0201; CHAIN: A;   COMPLEX (MHC/VIRAL                                           BETA-2 MICROGLOBULIN;   PEPTIDE/RECEPTOR) HLA A2                                           CHAIN: B; TAX PEPTIDE;   HEAVY CHAIN; COMPLEX                                           CHAIN: C; T CELL   (MHC/VIRAL PEPTIDE/RECEPTOR)                                           RECEPTOR ALPHA;                                           CHAIN: D; T CELL                                           RECEPTOR BETA; CHAIN:                                           E;       636   1bec       74   217   8.5e−57           72.58   14.3.D T CELL ANTIGEN   RECEPTOR T CELL RECEPTOR 1BEC                                           RECEPTOR; 1BEC 5   14                                           CHAIN: NULL; 1BEC 6       636   1bec       75   195   8.5e−57   0.51   1.00       14.3.D T CELL ANTIGEN   RECEPTOR T CELL RECEPTOR 1BEC                                           RECEPTOR; 1BEC 5   14                                           CHAIN: NULL; 1BEC 6       636   1bwm   A   74   217   1.7e−48           61.36   ALPHA-BETA T CELL   IMMUNE SYSTEM                                           RECEPTOR (TCR) (D10);   IMMUNOGLOBULIN,                                           CHAIN: A;   IMMUNORECEPTOR, IMMUNE                                               SYSTEM       636   1bwm   A   75   185   1.7e−48   0.55   1.00       ALPHA-BETA T CELL   IMMUNE SYSTEM                                           RECEPTOR (TCR) (D10);   IMMUNOGLOBULIN,                                           CHAIN: A;   IMMUNORECEPTOR, IMMUNE                                               SYSTEM       636   1d9k   B   75   185   1.7e−48   0.63   1.00       T-CELL RECEPTOR D10   IMMUNE SYSTEM MHC I-AK; MHC                                           (ALPHA CHAIN); CHAIN:   I-AK; T-CELL RECEPTOR, MHC                                           A, E; T-CELL RECEPTOR   CLASS II, D10, I-AK                                           D10 (BETA CHAIN);                                           CHAIN: B, F; MHC I-AK A                                           CHAIN (ALPHA CHAIN);                                           CHAIN: C, G; MHC I-AK B                                           CHAIN (BETA CHAIN);                                           CHAIN: D, H;                                           CONALBUMIN PEPTIDE;                                           CHAIN: P, Q;       636   Ifyt   E   74   194   3.4e−50   0.39   1.00       HLA CLASS II   IMMUNE SYSTEM HLA-DR1, DRA;                                           HISTOCOMPATIBILITY   HLA-DR1, DRB1 0101; TCR HA1.7                                           ANTIGEN, DR CHAIN: A;   ALPHA CHAIN; TCR HA1.7 BETA                                           HLA CLASS II   CHAIN; PROTEIN-PROTEIN                                           HISTOCOMPATIBILITY   COMPLEX, IMMUNOGLOBULIN                                           ANTIGEN, DR-1 CHAIN: B;   FOLD                                           HEMAGGLUTININ HA1                                           PEPTIDE CHAIN; CHAIN:                                           C; T-CELL RECEPTOR                                           ALPHA CHAIN; CHAIN: D;                                           T-CELL RECEPTOR BETA                                           CHAIN; CHAIN: E;       636   1nct       27   93   0.0015   −0.00   0.11       TITIN; CHAIN: NULL;   MUSCLE PROTEIN CONNECTIN,                                               NEXTM5; CELL ADHESION,                                               GLYCOPROTEIN,                                               TRANSMEMBRANE, REPEAT,                                               BRAIN, 2 IMMUNOGLOBULIN FOLD,                                               ALTERNATIVE SPLICING, SIGNAL, 3                                               MUSCLE PROTEIN       636   1tcr   B   72   195   8.5e−55   0.45   1.00       ALPHA, BETA T-CELL   RECEPTOR TCR; T-CELL,                                           RECEPTOR CHAIN: A, B;   RECEPTOR, TRANSMEMBRANE,                                               GLYCOPROTEIN, SIGNAL       636   1tcr   B   72   217   8.5e−55           74.81   ALPHA, BETA T-CELL   RECEPTOR TCR; T-CELL,                                           RECEPTOR CHAIN: A, B;   RECEPTOR, TRANSMEMBRANE,                                               GLYCOPROTEIN, SIGNAL       645   1a4y   A   52   166     5e−05   0.05   0.43       RIBONUCLEASE   COMPLEX (INHIBITOR/                                               NUCLEASE)                                           INHIBITOR; CHAIN: A, D;   COMPLEX (INHIBITOR/                                               NUCLEASE),                                           ANGIOGENIN; CHAIN: B, E;   COMPLEX (RI-ANG),                                               HYDROLASE 2                                               MOLECULAR RECOGNITION,                                               EPITOPE MAPPING, LEUCINE-RICH                                               3 REPEATS                    
     [0405]                           TABLE 6                           Position               SEQ ID NO:   of the Signal Peptide   Maximum Score   Mean Score                                                338   1-23   0.964   0.838       339   1-29   0.941   0.708       340   1-44   0.855   0.504       341   1-19   0.991   0.956       342   1-20   0.965   0.833       343   1-33   0.981   0.884       344   1-26   0.956   0.717       345   1-21   0.990   0.950       346   1-44   0.990   0.644       347   1-29   0.968   0.793       348   1-39   0.986   0.641       349   1-58   0.925   0.495       350   1-20   0.916   0.453       351   1-22   0.943   0.746       352   1-19   0.993   0.953       353   1-49   0.956   0.507       354   1-33   0.988   0.893       355   1-31   0.894   0.613       356   1-16   0.989   0.500       357   1-42   0.872   0.606       358   1-18   0.902   0.649       359   1-24   0.909   0.643       360   1-38   0.930   0.725       361   1-24   0.967   0.918       362   1-22   0.981   0.881       363   1-41   0.987   0.895       364   1-15   0.935   0.811       365   1-75   0.981   0.516       366   1-45   0.954   0.577       367   1-23   0.989   0.965       368   1-33   0.937   0.526       369   1-18   0.898   0.665       370   1-25   0.974   0.872       371   1-39   0.990   0.515       372   1-72   0.963   0.485       373   1-19   0.976   0.950       374   1-43   0.966   0.542       375   1-49   0.994   0.792       376   1-24   0.993   0.937       377   1-39   0.996   0.930       378   1-70   0.938   0.480       379   1-40   0.967   0.492       380   1-43   0.987   0.765       381   1-41   0.977   0.722       382   1-23   0.952   0.651       383   1-19   0.983   0.492       384   1-19   0.987   0.898       385   1-27   0.930   0.465       386   1-26   0.972   0.732       387   1-13   0.923   0.755       388   1-25   0.951   0.738       389   1-34   0.845   0.537       390   1-30   0.967   0.769       391   1-48   0.979   0.568       392   1-43   0.973   0.486       393   1-18   0.956   0.655       394   1-27   0.975   0.831       395   1-44   0.987   0.725       396   1-35   0.969   0.616       397   1-35   0.954   0.759       398   1-20   0.926   0.787       399   1-20   0.974   0.908       400   1-16   0.888   0.686       401   1-28   0.889   0.529       402   1-27   0.973   0.870       403   1-37   0.956   0.698       404   1-25   0.969   0.873       405   1-48   0.985   0.679       406   1-60   0.988   0.525       407   1-11   0.977   0.958       408   1-22   0.953   0.916       409   1-39   0.972   0.817       410   1-29   0.983   0.897       411   1-24   0.917   0.657       412   1-23   0.967   0.856       413   1-49   0.963   0.532       414   1-25   0.928   0.667       415   1-69   0.982   0.489       416   1-38   0.966   0.856       417   1-41   0.971   0.804       418   1-19   0.937   0.870       419   1-15   0.987   0.802       420   1-20   0.925   0.699       421   1-74   0.996   0.456       422   1-40   0.977   0.661       423   1-14   0.967   0.876       424   1-41   0.990   0.724       425   1-23   0.968   0.924       426   1-27   0.882   0.585       427   1-38   0.868   0.535       428   1-17   0.950   0.658       429   1-25   0.971   0.897       430   1-39   0.996   0.868       431   1-20   0.987   0.946       432   1-45   0.991   0.468       433   1-14   0.946   0.864       434   1-49   0.963   0.513       435   1-66   0.981   0.530       436   1-26   0.982   0.896       437   1-32   0.989   0.841       438   1-37   0.972   0.775       439   1-76   0.979   0.577       440   1-42   0.943   0.626       441   1-34   0.993   0.933       442   1-43   0.943   0.527       443   1-33   0.968   0.827       444   1-28   0.995   0.945       445   1-26   0.994   0.932       446   1-41   0.959   0.629       447   1-28   0.988   0.935       448   1-24   0.981   0.776       449   1-25   0.898   0.612       450   1-14   0.943   0.864       451   1-24   0.976   0.925       452   1-13   0.835   0.583       453   1-21   0.896   0.706       454   1-58   0.924   0.495       455   1-39   0.983   0.710       456   1-26   0.971   0.899       457   1-27   0.970   0.898       458   1-53   0.987   0.512       459   1-29   0.964   0.562       460   1-33   0.937   0.698       461   1-24   0.988   0.952       462   1-18   0.995   0.978       463   1-13   0.972   0.733       464   1-25   0.992   0.929       465   1-20   0.987   0.963       466   1-41   0.972   0.714       467   1-19   0.940   0.480       468   1-40   0.993   0.805       469   1-42   0.890   0.551       470   1-11   0.975   0.532       471   1-21   0.942   0.816       472   1-25   0.954   0.816       473   1-66   0.976   0.499       474   1-41   0.983   0.859       475   1-25   0.980   0.906       476   1-15   0.953   0.860       477   1-31   0.995   0.895       478   1-17   0.959   0.867       479   1-22   0.874   0.557       480   1-18   0.981   0.858       481   1-40   0.935   0.478       482   1-22   0.993   0.966       483   1-49   0.987   0.594       484   1-66   0.893   0.506       485   1-25   0.990   0.857       486   1-26   0.985   0.956       487   1-48   0.985   0.571       488   1-17   0.976   0.772       489   1-15   0.932   0.796       490   1-40   0.996   0.972       491   1-60   0.980   0.490       492   1-25   0.941   0.656       493   1-16   0.984   0.949       494   1-47   0.956   0.497       495   1-34   0.971   0.910       496   1-42   0.983   0.683       497   1-45   0.878   0.636       498   1-17   0.961   0.884       499   1-26   0.996   0.922       500   1-20   0.947   0.881       501   1-48   0.940   0.755       502   1-30   0.968   0.777       503   1-32   0.953   0.778       504   1-20   0.963   0.551       505   1-25   0.958   0.928       506   1-56   0.968   0.630       507   1-24   0.933   0.671       508   1-44   0.956   0.803       509   1-47   0.967   0.826       510   1-48   0.992   0.807       511   1-25   0.976   0.909       512   1-36   0.932   0.534       513   1-29   0.973   0.792       514   1-29   0.922   0.662       515   1-32   0.967   0.646       516   1-21   0.933   0.785       517   1-46   0.981   0.714       518   1-44   0.955   0.611       519   1-17   0.950   0.712       520   1-14   0.989   0.917       521   1-27   0.998   0.952       522   1-35   0.969   0.716       523   1-17   0.943   0.681       524   1-21   0.956   0.879       525   1-25   0.985   0.718       526   1-17   0.943   0.794       527   1-29   0.998   0.924       528   1-21   0.986   0.966       529   1-22   0.942   0.465       530   1-73   0.968   0.573       531   1-25   0.872   0.581       532   1-25   0.988   0.947       533   1-18   0.900   0.591       534   1-23   0.975   0.884       535   1-18   0.898   0.719       536   1-43   0.907   0.701       537   1-20   0.989   0.960       538   1-40   0.998   0.990       539   1-35   0.984   0.757       540   1-42   0.977   0.671       541   1-15   0.978   0.902       542   1-17   0.976   0.927       543   1-34   0.957   0.706       544   1-18   0.978   0.937       545   1-49   0.967   0.531       546   1-9   0.806   0.506       547   1-36   0.978   0.657       548   1-19   0.973   0.788       549   1-20   0.964   0.774       550   1-24   0.978   0.709       551   1-21   0.968   0.782       552   1-45   0.998   0.924       553   1-22   0.989   0.960       554   1-49   0.986   0.825       555   1-38   0.959   0.769       556   1-28   0.988   0.744       557   1-20   0.972   0.830       558   1-48   0.957   0.617       559   1-20   0.980   0.902       560   1-17   0.905   0.697       561   1-47   0.995   0.684       562   1-19   0.848   0.605       563   1-20   0.983   0.888       564   1-31   0.977   0.806       565   1-48   0.986   0.542       566   1-38   0.968   0.457       567   1-20   0.972   0.888       568   1-10   0.993   0.569       569   1-34   0.994   0.867       570   1-23   0.904   0.643       571   1-22   0.974   0.877       572   1-17   0.959   0.814       573   1-48   0.946   0.768       574   1-24   0.807   0.500       575   1-19   0.957   0.838       576   1-38   0.988   0.950       577   1-72   0.974   0.510       578   1-31   0.945   0.695       579   1-46   0.992   0.562       580   1-23   0.958   0.866       581   1-25   0.973   0.888       582   1-41   0.981   0.577       583   1-43   0.970   0.727       584   1-32   0.913   0.607       585   1-27   0.962   0.882       586   1-22   0.989   0.887       587   1-28   0.972   0.825       588   1-31   0.990   0.766       589   1-30   0.995   0.964       590   1-24   0.955   0.640       591   1-37   0.977   0.860       592   1-38   0.983   0.775       593   1-18   0.990   0.922       594   1-24   0.993   0.923       595   1-22   0.948   0.754       596   1-22   0.989   0.927       597   1-31   0.979   0.864       598   1-16   0.988   0.968       599   1-55   0.996   0.513       600   1-27   0.977   0.934       601   1-43   0.994   0.918       602   1-45   0.995   0.686       603   1-44   0.965   0.514       604   1-26   0.975   0.807       605   1-30   0.982   0.647       606   1-42   0.982   0.664       607   1-36   0.999   0.992       608   1-66   0.972   0.489       609   1-41   0.901   0.614       610   1-20   0.994   0.976       611   1-21   0.940   0.738       612   1-38   0.991   0.889       613   1-16   0.915   0.719       614   1-57   0.960   0.515       615   1-28   0.974   0.886       616   1-21   0.981   0.911       617   1-30   0.993   0.832       618   1-21   0.993   0.979       619   1-38   0.884   0.655       620   1-25   0.963   0.849       621   1-27   0.954   0.863       622   1-27   0.961   0.767       623   1-14   0.952   0.606       624   1-19   0.972   0.877       625   1-21   0.901   0.545       626   1-25   0.986   0.802       627   1-26   0.895   0.712       628   1-23   0.956   0.836       629   1-19   0.989   0.950       630   1-40   0.967   0.821       631   1-19   0.968   0.923       632   1-44   0.990   0.566       633   1-41   0.922   0.748       634   1-34   0.991   0.758       635   1-36   0.952   0.513       636   1-32   0.968   0.678       637   1-16   0.969   0.917       638   1-19   0.978   0.930       639   1-39   0.982   0.678       640   1-36   0.987   0.866       641   1-24   0.942   0.780       642   1-46   0.963   0.617       643   1-76   0.976   0.542       644   1-49   0.998   0.716       645   1-45   0.996   0.966       646   1-32   0.971   0.914       647   1-25   0.998   0.958       648   1-69   0.984   0.491       649   1-41   0.962   0.555       650   1-19   0.973   0.893       651   1-37   0.968   0.621       652   1-24   0.983   0.949       653   1-40   0.980   0.824       654   1-21   0.953   0.854       655   1-46   0.990   0.503       656   1-45   0.987   0.852       657   1-46   0.826   0.557       658   1-24   0.959   0.869       659   1-20   0.982   0.852       660   1-44   0.894   0.594       661   1-48   0.981   0.692       662   1-61   0.990   0.551       663   1-17   0.992   0.969       664   1-35   0.915   0.516       665   1-29   0.975   0.835       666   1-17   0.924   0.748       667   1-18   0.943   0.843       668   1-33   0.970   0.887       669   1-25   0.980   0.893       670   1-18   0.973   0.922       671   1-26   0.994   0.969       672   1-34   0.961   0.562       673   1-39   0.978   0.791       674   1-17   0.928   0.753                    
     [0406]                           TABLE 7                                   SEQ ID NO:   Chromosomal Location                                                    1   6           4   14           5   3p           6   1q24.1-25.3           12   13           17   17           19   19           20   19           22   5           23   22           27   5           28   6           36   14           39   11           40   17           44   18           45   4           48   6           49   22q13.1-13.33           51   20           53   6           54   11           55   4           60   3           62   3           64   1           68   6p21.1-21.2           70   12           71   16           72   5           73   19           74   17           78   18           81   5           85   3           87   10           89   5           90   8           92   16           93   4           95   6           99   2           100   6           105   3q           116   10           118   1           121   11           122   12q           126   19           129   1p31.2-32.3           133   17           137   22           140   17           150   15           151   22           153   1           154   1           158   9           160   16           170   15           172   11           174   7           175   2           176   11           177   4p16.3           180   14           184   19           185   7           188   16           189   5           193   6q22.1-22.33           197   11           199   6           207   3q           208   13           210   1           212   13           214   5           216   4           221   5           223   13           225   6p11.2-12.3           226   19           227   6q16-21           228   1q23-24           229   5           230   17           232   5           235   19           238   18           239   5           243   20           249   8           251   4p16.3           255   3           256   20           257   16           260   22q13.1-13.2            262   16           264   17           267   06           270   19           271   19           273   16           275   6           276   14           278   1           280   8           283   6           285   17           286   19           289   17           296   1           301   21           303   1           307   14           312   7           313   16           314   3           315   12q           316   5           317   3           319   13           321   15           325   5           327   9           328   4           329   3           330   15           333   16           336   11                        
     [0407]                               TABLE 8                                       Amino acid sequence (A = Alanine, C = Cysteine,                   Location of   D = Aspartic Acid, E = Glutamic Acid, F =                   first   Phenylalanine, G = Glycine, H = Histidine, I =                   nucleotide of   Isoleucine, K = Lysine, L = Leucine, M = Methionine,                   codon   N = Asparagine, P = Proline, Q = Glutamine, R =       SEQ ID       Nucleotide location   corresp. to   Arginine, S = Serine, T = Threonine, V = Valine, W =       NO: of       corresp. to first   last residue   Tryptophan, Y = Tyrosine, X = Unknown, * = Stop codon,       peptide       residue of peptide   of peptide   / = possible nucleotide deletion, = possible nucleotide       sequence   Method   sequence   sequence   insertion)                                                    837   A   583   989   PVETHCALVIGKSPTSRPFHSLVQGRAILGIMLAITVL                               GQFFINLNQFDPEVGDEEEQQQSHGEEDPKEQEPARE                               LPHES*QHRAHCQPHRPHGDHGSHTQDQGSFPLSLY                               LFSSGAPAFAQHVLSGTFCGLCSI               838   A   1   1143   MVVCNWYTLSFSLLFVSVTPDYVPPLGNFDVETLDIT                               PHTVTAISAKIRKKGKIERKQKTDGSKTSSSDTLSEEK                               NSECDPTPSHRGQLNKEFTGKEEKTSLLLHNSHAFFR                               ELDIEVFSILHCGLVTKFILDTEMHTECLAAENHGVV                               DGPGVKVQEYHIMSSCYQRLLQIFHGLFAWSGFSQP                               ENQNLLYSALHVLSSRLKQGEHSQPLEELLSIYLEHT                               ESILKAIEEIAGVGVPELINSPKDASSSTFPTLTRHTFV                               VFFRVMMAELEKTVKKIEPGTAADSQQIHEEKLLYW                               NMAVRDFSILINLIKVFDSHPVLHVCLKGEEIKSQNSQ                               ESTADESEDDMSSQASKSKATEDGEEDEVSAGEKEQ                               DSDESYDDSD               839   A   1   2337   TRFRGLRPAVAPWTALLALGLPGWVLAVSATAAAV                               VPEQHASVAGQHPLDWLLTDRGPFHRAQEYADFME                               RYRQGFTTRYRIYREFARWKVNNLALERKDFFSLPLP                               LAPEFIRNIRLLGRRPNLQQVTENLIKKYGTHFLLSAT                               LGGEESLTIFVDKQKLGRKTETTGGASHGGSGNSTA                               VSLETLHQLAASYFIDRESTLRRLHHIQIATGAIKVTE                               TRTGPLGCSNYDNLDSVSSVLVQSPENKVQLLGLQV                               LLPEYLRERFVAAALSYITCSSEGELVCKENDCWCKC                               SPTFPECNCPDADIQAMEDSLLQIQDSWATHNRQFEE                               SEEFQALLKRLPDDRFLNSTAISQFWAMDTSLQHRY                               QQLGAGLKVLFKKTHRILRRLFNLCKRCHRQPRFRLP                               KERSLSYWWNRIQSLLYCGESTFPGTFLEQSHSCTCP                               YDQSSCQGPIPCALGEGPACAHCAPDNSTRCGSCNPG                               YVLAQGLCRPEVAESLENFLGLETDLQDLELKYLLQ                               KQDSRIEVHSIFISNDMRLGSWFDPSWRKRMLLTLKS                               NKYKPGLVHVMLALSLQICLTKNSTLEPVMAIYVNP                               FGGSHSESWFMPVNEGSFPDWERTNVDAAAQCQNW                               TITLGNRWKTFFETVHVYLRSRIKSLDDSSNETIYYEP                               LEMTDPSKNLGYMKINTL\QVFGYSLPFDPD\AIRDLI                               LQLDYPYTQGSQDSALLQLIELRDRVNQLSPPGKVRL                               DLFSCLLRHRLKLANNEVGRIQSSLRAFNSKLPNPVE                               YETGKLCS               840   A   763   244   FLGPRIIGLRHEISVETQDHKSAVRGNNTHDNYENVE                               AGPPKAKGKTDKELYENTGQSNFEEHIYGNETSSDY                               YNFQKPRPSEVPQDEDIYILPDSY*L/CQNIDFCYWMI                               NIHCNFSTAKTRNQTKC*STVDWIKKMWYTYTIEYY                               AAVKK/DTKLTWEQKIKYHIFSLKSGS               841   A   263   467   LQSRPLGAWRGPPHGKQPHGPHCPVGPASPSCWSWP                               PWLRSSSSPPLCWLNACSAVLSAQTPATVHPP               842   B   1   5652   MGRGGLTRAGFARAWATRSWRPLAGERAQRRGRTP                               SPHPRAAGGRHCYLGPRFQSPWQRSRSVRDAAAESG                               DGGGAGMRMYDGAAGQNDGIQTRNRFIQCPRVRST                               WGYWEAQGFTFAMEESTGTPTCSPASGWASPPELW                               EEPIPSYTSGPRLSELLWRNMLGVVYANARLLGLYRF                               LQENVLTHTRSVLKSLIQQTPETSSFILCLSHRSAPPHT                               GQPQRQDPVPILLSALLSHLTTTHAVVQLMLTSDGLG                               CHLPPLPTTVAVVFTMAVSSVLASGSPGVCQTPSTSP                               SSYLQRAAVLQLLDNLPAPYHSAQGKSTVAVEIFSS                               WLPWQGCWVASLPQMYIILLKPERNAPDWPHDLGS                               RTRWAGVRGGLETTHRAAPLRKRGLRHRLGASPSG                               ALPRSVRVLVAISALVFDSLLSRSGGFVPLKFTAPGD                               MPNGPTRQPGKRLSRTIWRPPGRRRKSPPGYELQQTP                               RRAPVDAGKAAAMSAAEVRPLLRLWVRRSAGLGGS                               GEPAGRGGVRLGFAVFLGSAWSISPRDGSHQPVGLW                               GRAVRLEVLFYFSCIDLIMIGAFHSALCSWPISLLNSR                               PDPSPTQSPHHPPPNQPSQPSSLPLPCIPSALPFTLPQL                               VYYGTPPCGILAPNALPTPEPSLTGAVNTSSMSLSIRL                               SGKALLPIPAIEFGARLQISVPMPGPPQIAHGGAQILLT                               SHVDLIPFTSSQALFIFQKQPPSVQDSHQLSKPRDTEA                               QRLRFRQFQYQWRAGRTSRWASSGRCAPVAEARGA                               LQGADAGAVVLEQFLGALPSKMRTWCSHRAPEAAG                               RPPAWWGPHTDVPAGRGAAGMFGESLPPQKAWRIG                               GSGKNRPLYDPFLPHSSGISGLGRTQDWSFGEEEDGK                               SPRSRKNHRRACVPLLGRPQGCPIKDCVRLSPALPVF                               PHPDYAAASGVDRERPPGSPGTCSSTRTSGVGQRRR                               HDRKSIAKPEVISLLEQGEEPCQWSRHVLNALVQPC                               WITTSQTPDVSIDGVIDIFHLCATDISPLQTLTVRETFC                               QTCCQLIQRFVNAACATSFRQAKPAAIAIGYRKAYPP                               DRPDPSGPGIHYITTTTECAYRHSTPMILPRQLKPRSR                               FNHAVVPTSRWLGAEIAREQIRRISFDHNFSAGINGKS                               SRSSSPVVHRKPNRARYNIITVFANCELVKLTPISNILS                               PYDNRPDGRLNLFFSFSLSASASFSSSRFRPLQRKSVR                               RRHRFQTDSTWDRQQRLREDIRRRQQHPDNECTNQH                               IRAFFAISDTIKVSLIGVKKARPRRWRSSLNLAATADQ                               WRGYQMRDKRLSIFYRQFTVYHSTKGKVQRFSVSV                               RSRFYHRLWRGFWLRSGELACVCAAAGVTPSAQLH                               YLSPPGYGWCALIARLFRIVCNVGTLHRPAAWRSSSI                               DAFSSGVIELSDHHRLCRQAFMRLSVSRNRKGTSSKF                               ITGDNRQSYSSRTFPYRWCRHYAADHRLRVTESAVR                               ERFNFSSPLVLSCNKSLNFSPQYVASGQRILTAWSASS                               QANEHEIRIRVAESRCPICRVPIDNRSAWSSYILAGITG                               CTVISVHLAHTGASLLMLMAAFILVTRLQVLKDIIVK                               SKGLSGYDSLRAKCREYAATQVDGQRKTLSVWCVL                               GDWSHPYLPWTSKLKPTSSARWAKYRQRSPAQRRE                               ASSLRNAAYRRDHYTILGTVKGAELELLRLPIRLWAS                               TFRQSSAIRYPGCRYRCRSHRAWPRPDDYVIGQKYG                               LETANRLARTALICRALIRRWWRERLQSERHRRCAA                               AEKGALLHVEKMQHSYPCAGVTKRRSSSARRRSGR                               QHGSERSACAVTERDQGVQWIPDWGQARIESMLLT                               VLTGVSPVSAPGVTDVTVRAQRHGRAASASLELMEE                               VANALKSMASGVVGIL               843   A   2313   1475   DDGAAHVMHREVWMAVFSYLSHQDLCVCMRVCRT                               WNRWCCDKRLWTRIDLNHCKSITPLMLSGIIRRQPVS                               LDLSWTNISKKQLSWLINRLPGLRDLVLSGCSWIAVS                               ALCSSSCPLLRTLDVQWVEGLKDAQMRDLLSPPTDN                               RPGQMDNRSKLRNIVELRLAGLDITDASLRLIIRHMP                               LLSKLHLSYCNHVTDQSINLLTAVGTTTRDSLTEINLS                               DCNKVTDQCLSFFKRCGNICHIDLRYCKQVTKEGCE                               QFIAEMSVSVQFGQV\EEKLLQKLS               844   C   477   737   MDPKRIRKHRTMRMPKKINNRIPKTNVIFCSRDMLES                               ADTFPRGTRDEGMGCPPSMVQGSQSTGYPGFLFFHH                               QSAEVMVAALWRG               845   A   113   358   MELVRRLMPLTLLILSCLAELTMAEAEGNASCTVSL                               GGANMAETHKAMILQLNPSENCTWTIERPENKSIRIIF                               CYVQLGSE               846   A   16   381   SLTYLLTSAKKEIELMSEELRGLKSEKQLLSQEGNDL                               KLENGSLLSKLVELEAKIALLQGDQQKLWSVNETLN                               LEKEKFLEEKQDAEKYYEQEHLNKEALAVEREKLLK                               EINVVQEELLKIM               847   A   3   5530   LPHGRTRGPGPAMAPWRKADKERHGVAIYNFQGSG                               APQLSLQIGDVVRIQETCGDWYRGYLIKHKMLQGIFP                               KSFIHIKEVTVEKRRNTENIIPAEIPLAQEVTTTLWEW                               GSIWKQLYVASKKERFLQVQSMMYDLMEWRSQLLS                               GTLPKDELKELKQKVTSKIDYGNKILELDLIVRDEDG                               NILDPDNTSVISLFHAHEEATDKITERIKEEMSKDQPD                               YAMYSRISSSPTHSLYVFVRNFVCRIGEDAELFMSLY                               DPNKQTVISENYLVRWGSRGFPKEIEMLNNLKVVFT                               DLGNKDLNRDKIYLICQIVRVGKMDLKDTGAKKCTQ                               GLRRPFGVAVMDITDIIKGKAESDEEKQHFIPFHPVTA                               ENDFLHSLLGKVIASKGDSGGQGLWVTMKMLVGDII                               QIRKDYPHLVDRTTVVARKLGFPEIIMPGDVRNDIYIT                               LLQGDFDKYNKTTQRNVEVIMCVCAEDGKTLPNAIC                               VGAGDKPMNEYRSVVYYQVKQPRWMETVKVAVPI                               EDMQRIHLRFMFRHRSSLESKDKGEKNFAMSYVKL                               MKEDGTTLHDGFHDLVVLKGDSKKMEDASAYLTLP                               SYRHHVENKGATLSRSSSSVGGLSVSSRDVFSISTLV                               CSTKLTQNVGLLGLLKWRMKPQLLQENLEKLKIVDG                               EEVVKFLQDTLDALFNIMMEHSQSDEYDILVFDALIY                               IIGLIADRKFQHFNTVLEAYIQQHFSATLAYKKLMTV                               LKTYLDTSSRGEQCEPILRTLKALEYVFKFIVRSRTLF                               SQLYEGKEQMEFEESMRRLFESINNLMKSQYKTTILL                               QVAALKYIPSVLHDVEMVFDAKLLSQLLYEFYTCIPP                               VKLQKQKVQSMNEIVQSNLFKKQECRDILLPVITKEL                               KELLEQKDDMQHQVLERKYCVELLNSILEVLSYQDA                               AFTYHHIQEIMVQLLRTVNRTVITMGRDHILISHFVA                               CMTAILNQMGDQHYSFYIETFQTSSELVDFLMETFIM                               FKDLIGKNVYPGDWMAMSMVQNRVFLRAINKFAET                               MNQKFLEHTNFEFQLWNNYFHLAVAFITQDSLQLEQ                               FSHAKYNKILNKYGDMRRLIGFSIRDMWYKLGQNKI                               CFIPGMVGPILEMTLIPEAELRKATIPIFFDMMLCEYQ                               RSGDFKKFENEIILKLDHEVEGGRGDEQYMQLLESIL                               MECAAEHPTIAKSVENFVNLVKGLLEKLLDYRGVMT                               DESKDNRMSCTVNLLNFYKDNNREEMYIRYLYKLR                               DLHLDCDNYTEAAYTLLLHTWLLKWSDEQCASQVM                               QTGQQHPQTHRQLKETLYETIIGYFDKGKMWEEAIS                               LCKELAEQYEMEIFDYELLSQNLIQQAKFYESIMKILR                               PKPDYFAVGYYGQGFPSFLRNKVFIYRGKEYERRED                               FQMQLMTQFPNAEKMNTTSAPGDDVKNAPGQYIQC                               FTVQPVLDEHPRFNKPVPDQIINFYKSNYVQRFHYS                               RPVRRGTVDPENEFASMWIERTSFVTAYKLPGILRWF                               EVVHMSQTTISPLENAIETMSTANEKILMMINQYQSD                               ETLPINPLSMLLNGIVDPAVMGGFAKYEKAFFTEEYV                               RDHPEDQDKLTHLKDLIAWQIPFLGAGIKIHEKRVSD                               NLRPFHDRMEECFKNLKMKVEKEYGVREMPDFDDR                               RVGRPRSMLRSYRQMSIISLASMNSDCSTPSKPTSESF                               DLELASPKTPRVEQEEPISPGSTLPEVKLRRSKKRTKR                               SSVVFADEKAAAESDLKRLSRKHEFMSDTNLSEHAA                               IPLKASVLSQMSFASQSMPTIPALALSVAGIPGLDEAN                               TSPRLSQTFLQLSDGDKKTLTRKKVNQFFKTMLASK                               SAEEGKQIPDSLSTDL               848   A   3   453   RGIRSWRLFTGCCVNPRKIFPRGHSCRFFYVLGQITLS                               SLVAPVMWLSVALLNGTFYECAMSGTRSSGLLELIC                               KGKPKECWEELHKVSCGKTSMLPTVNEELKLSLQAQ                               SQILGWCLICSASFFSLLTTCYARCRSKVSYLQLSFW                               KTY               849   A   2   807   VEFHPQRARAGARAPSMGVLLTQRTLLSLVLALLFPS                               MASMAAIGSCSKEYRVLLGQLQKQTDLMQDTSRLL                               DPYIRIQGLDVPKLREHCRERPGAFPSEETLRGLGRR                               CFLQTLNATLGCVLHRLADLEQRLPKAQDLERSGLNI                               EDLEKLQMARPNILGLRNNIYCMAQLLDNSDTAEPT                               KAGRGASQPPTPTPASDAFQRKLEGCRFLHGYHRFM                               HSVGRVFSKWGESPNRSRRHSPHQALRKGVRRTRPS                               RKGKRLMTRGQLPR               850   A   1   2808   MGDFNTPLSTLDRSTRQKVNKDIQELNSALHQADLI                               DIYRTLHPKSTEYTFFSAPHHTYSKIDHIVGSKALLSK                               CKRTEIITNCLSDHSAIKLELRIKKLTQNRSTTWKLNK                               NDYWVHNEMKAEIKMFFETNKNKDTTYQNLWDTF                               KAVCRGKFIALNAHKRKQERSKIDTLTSQLKEPEKQE                               QTHSKASRRQEITKIRAELKEIETQKTLQKINESRSWF                               FERINKIDRPLARLIKKKREKNQIDPIKNDKGDITTDP                               TEIQTTIREYYKHLYTNKLENLEEMDKFLDTYTLPRL                               NQEEVESLNRPLTGSEIVAIINSLPTKKSPGPDGFTAEF                               YQRYKEELVPFLLKLFQSIEKEGILPNSFDEASIILIPKP                               GRDSTKKENFRPISLMNIDAKILNKILANRIQQHIKKLI                               HHDQVGFIPGMQVWFNIRKSINVIQHINRTKDKNHMI                               ISIDAEKAFDTIQQPFMLKTLNKLGIDGMYLKIIRAIY                               DKPTANITLNGQKLEAFPLKTGTRQGCPLSPFLFNIVL                               GYPSLLLPHTYTPDHVVGPGADIDPTQITFPGCICVKT                               PCLPGTCSCLRHGENYDDNSCLRDIGSGGKYAEPVFE                               CNVLCRCSDHCRNRVVQKGLQFHFQVFKTHKKGWG                               LRTLEFIPKGRFVCEYAGEVLGFSEVQRRIHLQTKSDS                               NYIIAIREHVYNGQVMETFVDPTYIGNIGRFLNHSCEP                               NLLMIPVRIDSMVPKLALFAAKDIVPEEELSYDYSGR                               YLNLTVSEDKERLDHGKLRKPCYCGAKSCTAFLPFD                               SSLYCPVEKSNISCGNEKEPSMCGSAPSVFPSCKRLTL                               EVDAFPPNGYGLYNIVGNAWEWTSDWWTVHHSVE                               ETLNPMVPIPAGVFTMGTDDPQIKQDGEAPARRVTID                               AFYMDAYEVSNTEFEKFVNSTGYLTEVPHTTPGDYG                               NYNSR               851   A   1   1528   APSPHNRQHKHRRKRRNQCDFRLNLGQRWNFTLPLL                               RSHEQSELNSFLWTIKRDPPSYFFGTIHVPYTRVWDFI                               PDNSKEAFLQSSIVYFELDLTDPYTISALTSCQMLPQG                               ENLQDVLPRDIYCRLKRHLEYVKLMMPLWMTPDQR                               GKGLYADYLFNAIAGNWERKRPVWVMLMVNSLTE                               VDIKSRGVPVLDLFLAQEAERLRKQTGAVEKVEEQC                               HPLNGLNFSQVIFALNQTLLQQESLRAGSLQIPYTTED                               LIKHYNCGDLSSVILSHDSSQVPNFINATLPPQERITA                               QEIDSYLRRELIYKRNERIGKRVKALLEEFPDKGFFFA                               FGAGHFMGNNTVLDVLRREGYEVEHAPAGRPIHKG                               KSKKTSTRPTLSTIFAPKVPTLEVPAPEAVSSGHSTLP                               PLVSRPGSADTPSEAEQRFRKKRRRSQRRPRLRQFSD                               LWVRLEESDIVPQLQVPVLDRHISTELRLPRRGHSHH                               SQMVASSACLSLWTPVFWVLVLAFQTETPLL               852   A   2   409   ALQSTLGAVWLGLLLNSLWKVAESKDQVFQPSTAA                               SSEGAVVEIFCNHSVSNAYNFFWYLHFPGCAPRLLV                               KGSKPSQQGRYNMTYERFSSSLLILQVREADAAVYY                               CAVEVPNTDKLIFGTGTRLQVFPNIQNPD               853   B   418   1620   METIAFTGPLARGCRPRLQPTCHIEQVLRCCWKAWK                               SICNCCFFLFFHSSSFSSSSTTGILFVILFVITVECLTLW                               RPGNPTYLRSCKGQVNRQEVQKESHLPPPERTEQNP                               YTPRRSQQASGKCQSSPQQTRHMGCSEVHARVLQA                               GAHTRVRSLFWTGTSALAGYPGVPDGERVESGSPGT                               VETREMHRYGVLQHPGEHAGSQRGKSSEASRRNGT                               DLALKEEAGLPVADAGPTRGSSKRKAEIKPLESWHS                               HGRSEPEENQGSGGAGCALTGATDLGCVPRLPYKGY                               SVWVPAPLSGLSDWLQLQLLPVTEQQGPVSFPKDFR                               QSPVLLAILLVSTLGKLGAGDSETTVQTSSPSQAQPT                               GCDPTETPPQQVIHSVLLASLGFLITCCFRREQSTLE               854   A   385   3   RNRSVVPEFVLLGLSAGPQTQTLLFVLFVVICLLTVM                               GNLLLLVVINADSCLHTPMYFFLGQLSFLDLCHSSVT                               APKLLENLLSEKKTISVEGCMA*VFFVFATGGTESSL                               LAVMAYDRYVAIRTRG               855   A   1674   1839   VVRVTCCPPARSTTERTNAYDEEDCVEMVASGGWN                               DVACHTTMYFMCEFDKKNM               856   A   1   318   GFGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTT                               MSGFSNTEEEQTLNQLLVEMDGASLDQLPSQGTMRK                               LRGKTPACSCLTEPTGSRRAMEGHSLCWGCLLH               857   A   2   462   EFQEAAKLYHTNYVRNSRAIGVLWAIFTICFAIVNVV                               CFIQPYWIGDGVDTPQAGYFGLFHYCIGNGFSRELTC                               RGSFTDFSTLPSGAFKAASFFIGLSMMLIIACIICFTLFF                               FCNTATVYKICAWMQLTSAACLVLGCMIFPDGWDS                               DEVN               858   A   997   758   MIQLFFVLYGILALAFLSGYYVTLAAQILAVLLPPVM                               LLIDGNVAYWHNTRRVEFWNQMKLLGESVGIFGTA                               VILATDG*               859   A   126   392   ARGSKHTGLIAQWAHEQSGHGGRAGGYAWAQQHG                               LPLTKADLP\AMATAECPICQQQRPTLSPRYGTIPW/W                               AWDAPGGRGCWRLQKAGE               860   A   405   3   LSLLLVPTASFCKSPTISQTLIKVNHSTGVRAVRNSLP                               FIIFCWEKVQGTSHSVGTRAKLPHHGNTLPTHSST*Q                               QAILPRPLPPRPISTPACKRWWALALGWFPTSVGVML                               DIKPAFPVELPSVCMSFFNPC               861   B   1   1575   MRSPCVNKIQGLEPNAKPVLSPATLQLLALMYPVPF                               KEMWSRKGNAYTADSGAENYQSLIAGSCDTRGLGY                               VGGVAFGMMTTGNNEWPRAQISVGTQDRDGSGNIG                               LQMHFRFMASGQISYAGPQGAGSFQQVPASDRNIKH                               SIKDDESSIAYNNIKSMRFRNFIFNDDEQERLGARRH                               NQHHLVAMVDTESPLCPLSPLEAGDLESPLSEEFLQE                               MGNIQEISQSIGEDSSGSFGFTEYQYLGSCPGSDGSVI                               TGSIQQTAAVEKEEYGAAATEGHVALLGPSSTIHNKI                               TNRTHDWGALALDGGPVPRCSGCRVQVVGWLCIPP                               RKAKCLTQREHYPFYKVINTGCQVPHLKKNLDHLLG                               MGSSRAWLPSTQIHRWRGAAGGPRTSRFLRATPERL                               QPLAAPGKASRPMWPRPRAPPETSGAHRGLGKILRD                               LTAQGRTHSSHKQLEMDGLAEKGNPSTNPAPGPTLQ                               QVCPCQSPRGAQPDPDRWPGGTQGFGQPLSWAQVS                               WRSQGRQGLPPLATYPGDA               862   A   3   690   SLSLPSSWDYRRAPPRPANFVFLVETGFTMLTTIVLIS                               *PHHPPASASQNAGIV/GVSHSPRPGIACLITRLDF/HQ                               GTQSRVPALGSS*PIPHARPRGHTLKALPYRLYTQTA                               RGFGQPRVRIPLLSLLGSLKPSELRGQVGHAFASAIFA                               SAISLCVFTLLVEGKLKPPGASVRRCLQSNRDLGFRA                               TFPTSHRGHGALGLNYISQRATGTPNLWLPFRFRVVL                               LQAACG               863   A   1073   480   XXPDALSTVAEXPGRPTRPPTRTAAPWPRPGCSSASA                               PPTPASAPWPASPSSSSGRWSTDSRGPRPWEGSQGC                               WHCGSW*RT*CTCKIIGGPGSRGCAASSSWASSSRPS                               PSLPSAPSSCWPSPGIRASQTPPATTSPASGASFPSSGP                               SCSASMPTATGLTLLTSASSAISDPGGSVYA*SGMVH                               QSGKEPSTVYTS               864   A   31   390   MVLPLPWLSRYHFLRLLLPSWSLAPQGSHGCCSQNP                               KASMEEQTNSRGNGKMTSPPRGPGTHRTAELARAEE                               LLEQQLELYQALLEGQEGAWEAQALVLKIHKLKEQ                               MRRHQESLGGGA*               865   A   841   1209   SPARGKSNRTDVMITAPKNKKMTENLAAPEALDSST                               HSSSTATQSRAKMNTPAPTPSTVPAIPRGGSGGPPPC                               APHDRVSSVLQCDTQAMDHKTESSHSVVEFLFKRTK                               TPSPFHPAVRENRN               866   A   5157   2939   AVRAEPGLEELSSGLRAHSPSATTVCEPEAQGSASGC                               RYAAHPHWGLGGAAAAGGSWEPQPPRPVCEPAGRG                               KPHPPAAPRSPLLPGSRRRPHAAQPGARARTSPPPAS                               ARNMAARPAATLAWSLLLLSSALLREGCRARFVAER                               DSEDDGEEPVVFPESPLQSPTVLVAVLARNAAHTLPH                               FLGCLERLDYPKSRMAIWAATDHNVDNTTEIFREWL                               KNVQRLYHYVEWRPMDEPESYPDEIGPKHWPTSRFA                               HVMKLRQAALRTAREKWSDYILFIDVDNFLTNPQTL                               NLLIAENKTIVAPMLESRGLYSNFWCGITPKGFYKRT                               PDY\VQIREWKRTGCFPVPMVHSTFLIDLRKEASDKL                               TFYPPHQDYTWTFDDIIVFAFSSRQAGIQMYLCNREH                               YGYLPIPLKPHQTLQEDIENLIHVQIEAMIDRPPMEPS                               QYVSVVPKYPDKMGFDEIFMINLKRRKGQGGDRWL                               RTLYEQEIEVKIVEAVDGKALNTSQLKALNIEMLPGY                               RDPYSSRPLTRGEIGCFLSHYSVWKEVIDRELEKTLVI                               EDDVRFEHQFKKKLMKLMDNIDQAQLDWELIYIGR                               KRMQVKEPEKAVPNVANLVEADYSYWTLGYVISLE                               GAQKLVGANPFGKMLPVDEFLPVMYNKHPVAEYKE                               YYESRDLKAFSAEPLLIYPTHYTGQPGYLSDTETSTI                               WDNETVATDWDRTHAWKSRKQSRIYSNAKNTEALP                               PPTSLDTVPSRDEL               867   A   1   2088   PTQSTRRIATVSIAAAVAPLTLFLYRGDGGLSSRRRA                               DAAAGALCGEVAVKPPINPFTEFMEKAVNDGSHSEE                               LFCHLKTISEKEDLPRCTSESHLSCLKQDILNEKTELE                               ATLKEAELVTHSVELLLPLPKDTIEKINFENANLSALN                               LKISEQKEILIKELDTFKSVKLALEHLLRKRDYKQTG                               DNLSSMLLENLTDNESENTNLKKKVFEKEAHIQELSC                               LFQSEKANTLKANRFSQSVKVVHERLQIQIHKREAEN                               DKLKEYVKSLETKIAKWNLQSRMNKNEAIVMKEAS                               RQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQE                               AKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQI                               INLLEDLKKMEDHGKNSCEEILRKVHSIEHENETLNL                               ENTKLKLRFPCRITESKNMNILIVLDMLCYISSEKTTL                               AALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQ                               KLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKMRG                               QMESHLKELERVCDSLTAAERRLHECQESLQCCKGK                               CADQEHTIRELQGQVDGNHNLLTKLSLEEENCLIQLK                               CENLQQKLEQMDAENKELEKKLANQEECLKHSNLK                               FKEKSAEYTALARQLEAALEEGRQKVAEEIEKMSSR                               ESALQIKILDLETELRKKNEEQNQLVCKMNSDPETP               868   A   749   1020   VLVRDPSQPAQPFSVSFSPQKHRDEKLYFLPKGVSGG                               SELRGRPQPYLPCPVSPTLCPWGHLSLAPPSVPPTACE                               SSSELWPSLSWTWAE               869   A   114   549   RPLVLPELGSAAGLLRLETPSQLRPNPKAMNSGVCLC                               VLMAVLAAGALTQPVPPADPAGSGLQRAEEAPRRQL                               RVSQRTDGESRAHLGALLARYIQQARKAPSGRMSTV                               KNLQNLDPSHRISDRDYMGWMDFGRRSAEEYEYPS               870   C   169   423   MDGDLQGPRIPRRSVLVVHETGLRTLIMDHTARGDT                               GNPLLLGSGGRGEWQPPQAPFIAQVPRNKLSSKKKG                               DTVEGKLPPTQP               871   A   54   410   MPTTPVAYNSLGAVIGIAVLGSLVVALVALFIGYRH                               WQKGKEHHHLAVAYSSGRLDGSEYVMPDVPPSYSH                               YYSNPSYHTLSQCSPNPPPPNKVPGPLFASLQKPERPG                               GAQGHDNHTT               872   A   1   542   LPGAGHRRVLDAGGPRGAGLQPQLPARQVGAVAEL                               HVSGPPGAGLA/GSGSGASGVGLGAAGWGSGPRGVR                               AEGEGAYSGPGQVFPVQGNVGNADAGTTGVGVPAG                               WWPPLPTRLQTLSVASPWLCP*AAASARSPPSGLSGE                               *TLFYTFSFLPPVVIAASPPAGLASEARPCFPRFHSYP               873   A   131   677   PSSLS/CDIFLRSPISTPSPSPLPRTPTSTPVHVKQGTAG                               SVINNPYVIMDKQPGQVIGATTPSTGSPTNKISTASQI                               SQGTGSPVPKIHGSSFVTSTVKVIIKQEPGEAPHVPAT                               GAASQSPLPQYVTVKGGHMIAVSPQKQVITPGEGIAQ                               SAKVQPSKVL/GQIG*CLPTLARADLLYSVC               874   A   1617   4994   MWFLFLCPNLWAMPVQIIMGVILLYNLLGSSALVGA                               AVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEI                               LKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALY                               TSLSIFMNAAIPIAAVLATFVTHAYASGNNLKPAEAF                               ASLSLFHILVTPLFLLSTVVRFAVKAIISVQKLNEFLLS                               DEIGDDSWRTGESSLPFESCKKHTGVQPKTINRKQPG                               RYHLDSYEQSTRRLRPAETEDIAIKVTNGYFSWGSGL                               ATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ                               TLEGKVHWSNVNESEPSFEATRSRNRYSVAYAAQKP                               WLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDL                               LPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIV                               FLDDPFSALDIHLSDHLMQEGILKFLQDDKRTLVLVT                               HKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVEL                               YEHWKTLMNRQDQELEKDMEADQTTLERKTLRRA                               MYSREAKAQMEDEDEEEEEEEDEDDNMSTVMRLRT                               KMPWKTCWRYLTSGGFFLLILMIFSKLLKHSVIVAID                               YWLATWTSEYSINNTGKADQTYYVAGFSILCGAGIF                               LCLVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFD                               TTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAI                               GMISYATPVFLVALLPLGVAFYFIQKYFRVASKDLQE                               LDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRML                               ELTDTNNIAYLFLSAANRWLEVRTDYLGACIVLTASI                               ASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLE                               VQMGAVKKVNSFLTMESENYEGTMDPSQVPEHWPQ                               EGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGIC                               GRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHT                               LRSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALE                               IAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCL                               ARAFVRKSSILIMDEATASIDMATENILQKVVMTAFA                               DRTVVTMAHRVSSIMDAGLVLVFSEGILVECDTVPN                               LFAHKNGPFSTLVMTNK*               875   A   3   1004   KYSGVHFNSQSIAPTIEQIDQSFGATHPGVYNSAEQLF                               HLNFRGLSFSFQLDSWTEAPKYEPNFAHGLASLQIPH                               GATVKRMYIYSGNSLQDTKAPMMPLSCFLGNVYAE                               SVDVLRDGTGPAGLRLRLLAAGCGPGLLADAKMRV                               FERSVYFGDSCQDVLSMLGSPHKVFYKSEDKMKIHS                               PSPHKQVPSKCNDYFFNYFTLGVDILFDANTHKVKK                               FVLHTNYPGHYNFNIYHRCEFKIPLAIKKENADGQTE                               TCTTYSKWDNIQELLGHPVEKPVVLHRSSSPNNTNPF                               GSTFCFGLQRMIFEVMQNNHIASVTLYGPPRPGSHLR                               TAELP               876   A   485   717   EPLLLLYLVSKIRTSGSNPLRSTFLSRSRSISKNGDPGA                               ASAACSRTARGPLSSGSNSRRRTEAKRWLRQQQHCE                               AF               877   A   2   1828   NYKTLIIICALFTLVTVLLWNKCSSDKAIQFPRRSSSG                               FRVDGFEKRAAASESNNYMNHVAKQQSEEAFPQEQ                               QKAPPVVGGFNSNVGSKVLGLKYEEIDCLINDEHTIK                               GRREGNEVFLPFTWVEKYFDVYGKVVQYDGYDRFE                               FSHSYSKVYAQRAPYHPDGVFMSFEGYNVEVRDRV                               KCISGVEGVPLSTQWGPQGYFYPIQIAQYGLSHYSKN                               LTEKPPHIEVYETAEDRDKNKPNDWTVPKGCFMAN                               VADKSRFTNVKQFIAPETSEGVSLQLGNTKDFIISFDL                               KFLTNGSVSVVLETTEKNQLFTIHYVSNAQLIAFKER                               DIYYGIGPRTSWSTVTRDLVTDLRKGVGLSNTKAVK                               PTKIMPKKVVRLIAKGKGFLDNITISTTAHMAAFFAA                               SDWLVRNQDEKGGWPIMVTRKLGEGFKSLEPGWYS                               AMAQGQAISTLVRAYLLTKDHIFLNSALRATAPYKF                               LSEQHGVKAVFMNKHDWYEEYPTTPSSFVLNGFMY                               SLIGLYDLKETAGEKLGKEARSLYERGMESLKAMLP                               LYDTGSGTIYDLRHFMLGIAPNLARWDYHTTHINQL                               QLLSTIDESPIFKEFVKRWKSYLKGSRAKHN               878   A   353   646   FYWNWVPFTNWQNPRLMGQK*HARWLHLRSLLPA                               M*ATLL*RENNR*LLLLTLTSIFKTFRIRRLSVSKP*VK                               AKKKTRLIIWSTSKFLSCMMLKFT               879   A   1648   1258   NSTFICYVASSASAFLTAPLLEFLLALYFLFADAMQL                               NDKWQGLCWPMMDFLRCVTAALIYFAISITAIAKYS                               DGASKAAGVFGFFATIVFATDFYLIFNDVAKFLKQG                               DSADETTAHKTEEENSDSDSD               880   A   92   422   ASAEPPAMPGIVVFRRRWSVGSDDLVLPAIFLFLLHT                               TWFVILSVVLFGLVYNPHEACSLNLVDHGRGYLGILL                               SCMIAEMAIIWLSMRGGILYTEPRDSMQYVLYVRLA               881   A   946   1424   YFRFLCVIFCSFLLRCLVSRVLLYPMLIAEIPRVQGRG                               GPSWPGLGGRLLKELSRLLTFLKVRKLSILSGWREVP                               LGQPSLTEPP/PPAPPHPGPGSWLASASAPHILSQPPAA                               GPAGQPPSPGSPVPGGCSLALPVTSVLCLEPPALKPA                               AASAPVVAVH               882   A   1   1917   MVIGRADGENKRKKTFIEHLLCPNPCDFQHKITVQAS                               PNLDKRRSLNSSSSSPPSSPTMMPRLRAIQLTSDESNK                               TWGRNTVFRQEEFEDVKRNFKKKGCTWGPNSIQMK                               DRTDCKERIRPLSDGNSPWSTILIKNQKTMPLASLFV                               DQPGSCEEPKLSPDGLEHRKPKQIKLPSQAYIDLPLG                               KDAQRENPAEAESWEEAASANAATVSIEMTPTNSLS                               RSPQRKKTESALYGCTVLLASVALGLDLRELHKAQA                               AEEPLPKEEKKKREGIFQRASKSRRSASPPTSLPSTCG                               EASSPPSLPLSSALGILSTPSFSTKCLLQMDSEDPLVDS                               APVTCDSEMLTPDFCPTAPGSGREPALMPRLDTDCSV                               SRNLPSSFLQQTCGNVPYCASSKHRPSHHRRTMSDG                               NPTPTGATIISATGASALPLCPSPAPHSHLPREVSPKK                               HSTVHIVPQRRPASLRSRSDLPQAYPQTAVSQLAQTA                               CVVGRPGPHPTQFLAAKERTKSHVPSLLDADVEGMK                               PQTFAVSVAALKGAASGVVSSSQRVRDLADLRSEAV                               DLHTPRDRTLPTHQVQGQGQQQEEQPQVEVAAVGE                               LALLRVVVPAPGLLQYIPLSITTPSKHRSPYDRTSRGL                               RYGYAKEQTLMSM               883   A   1   684   RTRGPPPQSRSGGRRRRIPLYLPTSCIKELVAGGVAVE                               SWPGRDAAQLLLCSCLLSPPPVMTETREPAETGGYA                               SLEEDDEDLSPGPEHSSDSEYTLSEPDSEEEEDEEEEE                               EETTDDPEYDPGYKVK*RLGGGRGGPSRRAPR\AAQP                               PAQPCQLCGRSPLGEAPPGTPRCTGTSCCMPGVRCR                               QSPHTGSLAEGVGWEEGAEEIGVVTVVMGDGVLPV                               CVVLEVDV               884   A   1   1047   MGITCWIALYAVEALPTCPFSCKCDSRSLEVDCSGLG                               LTTVPPDVPAATRTLLLLNNKLSALPSWAFANLSSLQ                               RLDLSNNFLDRLPRSIFGDLTNLTELQLRNNSIRTLDR                               DLLRHSPLLRHLDLSINGLAQLPPGLFDGLLALRSLSL                               RSNRLQNLDRLTFEPLANLQLLQVGDNPWECDCNLR                               EFKHWMEWFSYRGGRLDQLACTLPKELRGKDMRM                               VPMEMFNYCSQLEDENSSAGLDIPGPPCTKASPEPAK                               PKPGAEPEPEPSTACPQKQRHRPASVRRAMGTVIIAG                               VVCGVVCIMMVVAAAYGCIYASLMNAKYHRELKKR                               QPLMGDPEGEHEDQKQISSVA               885   A   87   554   MEALTLWLLPWICQCVSVRADSIIHIGAIFEENAAKD                               DRVFQLAVSDLSLNDDILQSEKITYSIKVIEANNPFQA                               VQEACDLMTQGILALVTSTGCASANALQSLTDAIMHI                               PHLFVQRNPGGSPRTACHLNPSPDGEAYTLASRPPVR                               LNDVMLRL               886   A   269   832   MGSSRLAALLLPLLLIVIDLSDSAGIGFRHLPHWNTR                               CPLASHTDDSFTGSSAYIPCRTWWALFSTKPWCVRV                               WHCSRCLCQHLLSGGSGLQRGLFHLLVQKSKKSSTF                               KFYRRHKMPAPAQRKLLPRRHLSEKSHHISIPSPDISH                               KGLRSKRTPPFGSRDMGKAFPKWDSPTPGGDRPSSFE                               LLP*               887   A   3   5530   LPHGRTRGPGPAMAPWRKADKERHGVAIYNFQGSG                               APQLSLQIGDVVRIQETCGDWYRGYLIKHKMLQGIFP                               KSFIHIKEVTVEKRRNTENIIPAEIPLAQEVTTTLWEW                               GSIWKQLYVASKKERFLQVQSMMYDLMEWRSQLLS                               GTLPKDELKELKQKVTSKIDYGNKILELDLIVRDEDG                               NILDPDNTSVISLFHAHEEATDKITERIKEEMSKDQPD                               YAMYSRISSSPTHSLYVFVRNFVCRIGEDAELFMSLY                               DPNKQTVISENYLVRWGSRGFPKEIEMLNNLKVVFT                               DLGNKDLNRDKIYLICQIVRVGKMDLKDTGAKKCTQ                               GLRRPFGVAVMDITDIIKGKAESDEEKQHFIPFHPVTA                               ENDFLHSLLGKVIASKGDSGGQGLWVTMKMLVGDII                               QIRKDYPHLVDRTTVVARKLGFPEIIMPGDVRNDIYIT                               LLQGDFDKYNKTTQRNVEVIMCVCAEDGKTLPNAIC                               VGAGDKPMNEYRSVVYYQVKQPRWMETVKVAVPI                               EDMQRIHLRFMFRHRSSLESKDKGEKNFAMSYVKL                               MKEDGTTLHDGFHDLVVLKGDSKKMEDASAYLTLP                               SYRHHVENKGATLSRSSSSVGGLSVSSRDVFSISTLV                               CSTKLTQNVGLLGLLKWRMKPQLLQENLEKLKIVDG                               EEVVKFLQDTLDALFNIMMEHSQSDEYDILVFDALIY                               IIGLIADRKFQHFNTVLEAYIQQHFSATLAYKKLMTV                               LKTYLDTSSRGEQCEPILRTLKALEYVFKFIVRSRTLF                               SQLYEGKEQMEFEESMRRLFESINNLMKSQYKTTILL                               QVAALKYIPSVLHDVEMVFDAKLLSQLLYEFYTCIPP                               VKLQKQKVQSMNEIVQSNLFKKQECRDILLPVITKEL                               KELLEQKDDMQHQVLERKYCVELLNSILEVLSYQDA                               AFTYHHIQEIMVQLLRTVNRTVITMGRDHILISHFVA                               CMTAILNQMGDQHYSFYIETFQTSSELVDFLMETFIM                               FKDLIGKNVYPGDWMAMSMVQNRVFLRAINKFAET                               MNQKFLEHTNFEFQLWNNYFHLAVAFITQDSLQLEQ                               FSHAKYNKILNKYGDMRRLIGFSIRDMWYKLGQNKI                               CFIPGMVGPILEMTLIPEAELRKATIPIFFDMMLCEYQ                               RSGDFKKFENEIILKLDHEVEGGRGDEQYMQLLESIL                               MECAAEHPTIAKSVENFVNLVKGLLEKLLDYRGVMT                               DESKDNRMSCTVNLLNFYKDNNREEMYIRYLYKLR                               DLHLDCDNYTEAAYTLLLHTWLLKWSDEQCASQVM                               QTGQQHPQTHRQLKETLYETLYETIIGYFDKGKMWEEAIS                               LCKELAEQYEMEIFDYELLSQNLIQQAKFYESIMKILR                               PKPDYFAVGYYGQGFPSFLRNKVFIYRGKEYERRED                               FQMQLMTQFPNAEKMNTTSAPGDDVKNAPGQYIQC                               FTVQPVLDEHPRFKNKPVPDQIINFYKSNYVQRFHYS                               RPVRRGTVDPENEFASMWIERTSFVTAYKLPGILRWF                               EVVHMSQTTISPLENAIETMSTANEKILMMINQYQSD                               ETLPINPLSMLLNGIVDPAVMGGFAKYEKAFFTEEYV                               RDHPEDQDKLTHLKDLIAWQIPFLGAGIKIHEKRVSD                               NLRPFHDRMEECFKNLKMKVEKEYGVREMPDFDDR                               RVGRPRSMLRSYRQMSIISLASMNSDCSTPSKPTSESF                               DLELASPKTPRVEQEEPISPGSTLPEVKLRRSKKRTKR                               SSVVFADEKAAAESDLKRLSRKHEFMSDTNLSEHAA                               IPLKASVLSQMSFASQSMPTIPALALSVAGIPGLDEAN                               TSPRLSQTFLQLSDGDKKTLTRKKVNQFFKTMLASK                               SAEEGKQIPDSLSTDL               888   A   586   959   NWECILHRVTGSSLLRPAPQAAGSWLIGGWERGCGP                               RCAPGGAP/APYLARPASSAARGPPVGRRGPPWGWA                               ASAAISARSSPPSAAGSGPDWRRPGKGHSPRPTAAAS                               ATRAPARAPPSPRLAAA               889   A   399   2002   LSLTHSHLCPHTPTHAHTQTTSAAGGPGQTPMG/PLI                               GGPRIKVRG*HPGGLGGGKPQWPHGLSHRTPKGPSM                               ALGPRGSGKR/GVRPGPV*GGLSPA*A*SPFSTETKPA                               TCRDGCGGPGGRALGPVCSVGGE*RPPGRPPVGGEL                               CPK*LGSSWC**WHKGRGEQLGRPGWVPMLVLSVH                               RSWCGMAGA*GQGGASVGTADEGGSHSQREGLLRP                               PRSRPGLPAEWGQESAGQRALGLSWAGGSQRPPKEP                               SGEGRKLAAEGGVGAGAAGPR/GLPG*ERCCSGFPSG                               PGEQGPIAGCHVLGATQP\RGPPSTVGAPPAHSHQGD                               GARPQEPTTDGEGRELGGLHPNLNPHLRGPRSDTQG/                               PAAPRAGPGSGAPWPPPVQVLGAAGPAPVHSVLIAG                               SLHVVSSQTATSFSPLTPSQ\GW*AQSG*FPS*SDSEGL                               LSPQGCASR*QGRAAQVGENSTLARPLS\ELKAARFG                               GDREETGWPLP*GVHRQGMRGQHFRMSPGVQDQPG                               QHGETLSLRIGFFAIFWDGSVGSCGPATWSS               890   A   3   655   IQCGGIPLLPLPSPLSMA/HCVQFQAGPPV\HWRVHAG                               LVSHSAVRPHQGALVERIIPHPLYSAQNHDYDVALLR                               LQTALNFSDTVGAVCLPAKEQHFPKGSRCWVSGWG                               HTHPSHTYSSDMLQDTVVPLLSTQLCNSSCVYSGAL                               TPRMLCAGYLDGRADACQGDSGGPLVCPDGDTWRL                               VGVVSWGRGCAEPNHPGVYAKVAEFLDWIHDTAQD                               SLL               891   A   336   1043   MPRRGLILHTRTHWLLLGLALLCSLVLFMYLLECAP                               QTDGNASLPGVVGENYGKEYYQALLQEQEEHYQTR                               ATSLKRQIAQLKQELQEMSEKMRSLQERRNVGANGI                               GYQSNKEQAPSDLLEFLHSQIDKAEVSIGAKLPSEYG                               VIPFESFTLMKVFQLEMGLTRHPEEKPVRKDKRDELV                               EVIEAGLEVINNPDEDDEQEDEEGPLGEKLIFNENDF                               VEGYYRTERDKGTQYELF               892   A   319   492   MQGVRVSFGWAMGLAWGSCALEAFSGTLLLSAAW                               TLSLSPPICGHLSPQQVGGRGGD*               893   A   3   1441   KLSVNHRRTHLTKLMHTVEQATLRISQSFQKTTEFDT                               NSTDIALKVFFFDSYNMKHIHPHMNMDGDYINIFPKR                               KAAYDSNGNVAVAFLYYKSIGPLLSSSDNFLLKPQN                               YDNSEEEERVISSVISVSMSSNPPTLYELEKITFTLSHR                               KVTDRYRSLCAFWNYSPDTMNGSWSSEGCELTYSN                               ETHTSCRCNHLTHFAILMSSGPSIGIKDYNILTRITQLG                               IIISLICLAICIFTFWFFSEIQSTRTTIHKNLCCSLFLAEL                               VFLVGINTNTNKLFCSIIAGLLHYFFLAAFAWMCIEGI                               HLYLIVVGVIYNKGFLHKNFYIFGYLSPAVVVGFSAA                               LGYRYYGTTKVCWLSTENNFIWSFIGPACLIILVNLL                               AFGVIIYKVFRHTAGLKPEVSCFENIRSWARGALALL                               FLLGTTWIFGVLHVVHASVVTAYLFTVSNAFQGMFIF                               LFLCVLSRKIQEEYYRLFKNVPCCFGCLR               894   A   303   368   LSSSSSSSSSSSSSSSSSSSSSSSSSHYHHHHHHHHHHH                               HHHHVDWIP               895   A   260   1   SSSQMQVKTQDEEMSGQKTRKPRSAPGTTERS*LAA                               PTPGLPAPDSAEARKAPAPPPGPAAPPQPAGPAPRSLT                               HLGGP*KSTPSR               896   A   1   482   MGCRLLCCVVFCLLQAGPLDTAVSQTPKYLVTQMG                               NDKSIKCEQNLGHDTMYWYKQDSKKFLKIMFSYNN                               KELIINETVPNRFSPKSPDKAHLNLHINSLELGDSAVY                               FCASSQDTALQSHCIPVHKPPGSARKLQGSVCTCTQG                               SSLHSLMASDGVPVC               897   A   2   760   YGYTPPPRLLPRNTFSRKAFKLKKPSKYCSWKCAAL                               SAIAAALLLAILLAYFIAMHLLGLNWQLQPADGHTF                               NNGIRTGLPGNDDVATMPSGGKVPWSLKNSSIDSGE                               AEVGRWVTQEVPPGVFWRSQIHISQPQFLKFNISLGK                               DALFGVYIRRGLPPSHAQCPLTSHIGSTGPHLSHGAE                               MWRQCQGLAVSLHSTSNRALQKPLIRSFISFWRKPDL                               YRHVFQNLPFQRSSSCRERLCETKRTLVSSELD               898   A   77   273   PRTGMGCCLPGADPAEIRSSPSPSWSTAGSQGCWMT                               SFSPCSCAPCCSSGCACTTGFVSREKESV               899   A   1   4499   SRPWWLRASERPSAPSAMAKRSRGPGRRCLLALVLF                               CAWGTLAVVAQKPGAGCPSRCLCFRTTVRCMHLLL                               EAVPAVAPQTSILDLRFNRIREIQPGAFRRLRNLNTLL                               LNNNQIKRIPSGAFEDLENLKYLYLYKNEIQSIDRQAF                               KGLASLEQLYLHFNQIETLDPDSFQHLPKLERLFLHN                               NRITHLVPGTFNHLESMKRLRLDSNTLHCDCEILWLA                               DLLKTYAESGNAQAAAICEYPRRIQGRSVATITPEEL                               NCERPRITSEPQDADVTSGNTVYFTCRAEGNPKPEII                               WLRNNNELSMKTDSRLNLLDDGTLMIQNTQETDQGI                               YQCMAKNVAGEVKTQEVTLRYFGSPARPTFVIQPQN                               TEVLVGESVTLECSATGHPPPRISWTRGDRTPLPVDP                               RVNITPSGGLYIQNVVQGDSGEYACSATNNIDSVHAT                               AFHVQALPQFTVTPQDRVVIEGQTVDFQCEAKGNPP                               PVIAWTKGGSQLSVDRRHLVLSSGTLRISGVALHDQ                               GQYECQAVNIIGSQKVVAHLTVQPRVTPVFASIPSDT                               TVEVGANVQLPCSSQGEPEPAITWNKDGVQVTESGK                               FHISPEGFLTINDVGPADAGRYECVARNTIGSASVSM                               VLSVNVPDVSRNGDPFVATSIVEAIATVDRAINSTRT                               HLFDSRPRSPNDLLALFRYTPRDPYTVEQARAGEIFER                               TLQLIQEHVQHGLMVDLNGTSYHYNDLVSPQYLNLI                               ANLSGCTAHRRVNNCSDMCFHQKYRTHDGTCNNLQ                               HPMWGASLTAFERLLKSVYENGFNTPRGINPHRLYN                               GHALPMPRLVSTTLIGTETVTPDEQFTHMLMQWGQF                               LDHDLDSTVVALSQARFSDGQHCSNVCSNDPPCFSV                               MIPPNDSRARSGARCMFFVRSSPVCGSGMTSLLMNS                               VYPREQINQLTSYIDASNVYGSTEHEARSIRDLASHR                               GLLRQGIVQRSGKPLLPFATGPPTECMRDENESPIPCF                               LAGDHRANEQLGLTSMHTLWFREHNRIATELLKLNP                               HWDGDTIYYETRKIVGAEIQHITYQHWLPKILGEVG                               MRTLGEYHGYDPGINAGIFNAFAT\AAFRFGHTLVNP                               LLLPGLDENFQPIAQDHLPLHKAFFSPFRIVNEGGIDP                               LLRGLFGVAGKMRVPSQLLNTELTERLFSMAHTVAL                               DLAAINIQRGRDHGIPPYHDYRVYCNLSAAHTFEDLK                               NEIKNPEIREKLKRLYGSTLNIDLFPALVVEDLVPGSR                               LGPTLMCLLSTQFKRLRDGDRLWYENPGVFPAQLT                               QIKQTSLARILCDNADNITRVQSDVFRVAEFPHGYGS                               CDEIPRVDLRVWQDCCEDCRTRGQFNAFSYHFRGRR                               SLEFSYQEDKPTKKTRPRKIPSVGRQGEHLSNSTSA\F                               STRSDASG\TNDFQRVCSWEMQKTITDLRTQIKKLES                               R\LSTTECVDAGGESHANNTKWKKDACTICECKDGQ                               VTCFVEACPPATCAVPVNIPGACCPVCLQKRAEEKP               900   A   1674   1839   VVRVTCCPPARSTTERTNAYDEEDCVEMVASGGWN                               DVACHTTMYFMCEFDKKNM               901   A   397   2   DPPTSAMSESPSPSLGVGSPLVPS/PPPPLGLPTVRSLL                               PPTIR/VAFGTPPPSPARSPSTSPSPHSPRSLVPARDGG                               ADSGERLGPGALGLGAGSGGGRARYGPSRSRPSDRA                               ADPGGVRPFPVAPGIPPHCTR               902   A   1   411   LLVFQVHQCLHCKLL*/PSYVPLGYTEAFLATQNIGR                               VSLWAKHGHPDPFPLARADFRAQESPSPNDPSWLL*                               YEER*WSQATTKG*NRCC*RCD*LQAPSRRPEAVHTN                               DPR*REVREEHMVLQVLTR               903   A   1   193   LLPRPGSGLDFLLSPVLPS/HSASWACPLPRPSPMPSS                               CC*R*RKEMASGFSKGPTLGCCPTCPP               904   A   119   571   MNRRASQMLLMFLLAICLLAIIFVPQEMQMLREVLA                               TLGLGASALANTLAFAHGNEVIPTIIRARAMGINATF                               ANIAGALAPLMMILSVYSPPLPWIIYGVFPFISGFAFLL                               LPETRNKPLFDTIQDEKNERKDPREPKQEDPRVEVTQ                               F*               905   A   1   840   MGSVGSQCLEEPSVAGTPDPGIVMSVTFDSHQLEEA                               AEAAQGQGLGQGRPSPHGYQVGCVTPGEALWHRGA                               MGGHGGLEVVPVTLEEPVPNDRYHAIYFAMLLSGV                               GFLLPYNSFITDVDYLHHKYPGTSIVFDMSLTYILVAL                               AAVLLNNVLVERLTLHTRITASYLLALGPLLFISICDV                               WLQLFSRDQAYAINLAAVGTVAFGCTVQNQNEQVL                               VGGPGKEAGDKAKEQQQSRERPIPSPTVQFLYYTRL                               DPFLYEQKNQTICSFGGENVLSIMHLA               906   A   257   1559   GTKFCFAIYLSSTGSNTSLTSLIMLGRYFKAAPCKKN                               TKGKFIQSIPDNQLVRQKLNCMTKIVESTLFRQSECR                               EVLLPLLTDQLSGQLDDNSNKPDHEASSQLLSNILEV                               LDRKDVGATAVHIQLIMERLL\RRINRTVIGMNRQSP                               HIGSFVACMIALLQQMDDSHYSHYISTFKTRQDIIDFL                               METFIMFKDLIGKNVYAKDWMVMNMTQNRVFLRAI                               NRFAEVLTRFFMDQASFELQLWNNYFHLAVAFLTHE                               SLQLETFSQAKRNKIVKKYGDMRKEIGFRIRDMWYN                               LGPHRIKFIPSMVGPILEVTLTPEVELRKATIPIFFDMM                               QCEFNFSGNGNFHMFENELITKLDQEVEGGRGDEQY                               KVLLEKLLLEHCRKHKYLSSSGEVFALLVSSLLENLL                               DYRTIIMQDESKENRMSCTVNVLNFYKKKK               907   A   14   616   TNPTPTAVLTATPATPVSSLTSMQTTRSEETPASAARP                               SARSSSRGTSTYIPSTSSTASSPPPCCMSCGRMWVDS                               WPPPLATATPQPLSASSGRPFLLARFWACCSSWWGW                               LSSSSTRFK*AGTGAAPGRPWSSTTASTLSAWDSPPW                               SA*AAPSSTVLTAGPWTTIRTPRALWTWPC*WVPPLV                               STPSLTTPSXXVXAGT               908   A   3   211   SSFSIPTLVITEQFATAYQGTRARSDNTHYWLIISCSIA                               YVALVTLLIWVPVKVILHKKRYIYRKIKGW               909   A   310   546   MSVVMLSYLLSAFFSQANTAALCTSLVYMISFLPYIV                               LLVLHNQLSFVNQTFLCLLSTTAFGQGVFFITFLEGQE                               TGIH               910   A   74   541   MHNNYTALLGVWIYGFFVLMLLVLDLLYYSAMNYD                               ICKVYLARWGIQGRWMKQDPRRWGNPARAPRPGQR                               APQPQPPPGPLPQAPQAVHTLRGDAHSPPLMTFQSSS                               AWEGASQQQEIPENEETEKGDDQISSFLGVTSNTKEA                               SVIGIQKTVDVL               911   A   1157   918   RSGVPDQPGQHGEAPSLLKIQNLAGRSGGPL*SQLLR                               RENRLNLGGGLP*AKIAPRLHPCTPAWVTDRDSVSK                               KKILFP               912   A   1199   795   MSWWRNNFWIILAVAIIVVSVGLGLILYCVCKWQLR                               RGKKWEIAKPLKHKQVDEEKMYENVLNESPVQLPPL                               PPRNWPSLEDSSPQEAPSQPPATYSLVNKVKNKKTVS                               IPSYIEPEDDYDDVEIPANTEKASF*               913   A   1   955   PQRAPLQDFGSSKVVNPKGSSPGA*SKPPMGRGPHK                               KGWRGPLGGGFPLKSPPLPQRKFSPK*KKQPWAPKR                               PPWCQGLFGGGGKRGLFWVFFLSPQKKKKGKGVLP                               QASGHPRQEGPPAGASQPLRSHS*PRKEQPQLGPAPR                               ATPCSCPHIWQLGPLMQCGSGFLHLKSASLSLL*DQC                               LLPASMAPG*PHSPRVSLRPGSSGRGAAGADGRAGA                               GQSSADGVLNT/QGDVGGARGLGMPRIWHGGLCVPP                               TPGTKAPASGPRSQAPGGGGDQQQFRGRCGQCGPES                               PPHSRHCPRGHSGISGALGMPGSLVPREAY               914   A   414   244   MTVMVTVTVTVMVMVMVMVMVTVMVTVTVMVT                               VMVTAEMTVMVGVMMMMMMVANIC*               915   A   2   4571   AAASRCPGIMVALRGLGSGLQPWCPLDLRLEWVDT                               VWELDFTETEPLDPSTEAEIIETGLAAFTKLYESLLPFA                               TGEHGSMESIWTFFIENNVSHSTLVALFYHFVQIVHK                               KNVSVQYREYGLHAAGLYFLLLEVPGSVANQVFHP                               VMFDKCIQTLKKSWPQESNLNRKKEQPKSSQANP                               GRHRKRGKPPRREDIEMDEIIEEQEDENICFSARDLSQ                               IRNAIFHLLKNFLRLLPKFSLKEKPQCVQNCIEVFVSL                               TNFEPVLHECHVTQARALNQAKYIPELAYYGLYLLC                               SPIHGEGDKVISCVFHQMLSVILMLEVGEGSHRAPLA                               VTSQVINCRNQAVQFISALVDELKESIFPVVRILLQHI                               CAKVVDKSEYRTFAAQSLVQLLSKLPCGEYAMFIAW                               LYKYSRSSKIPHRVFTLDVVLALLELPEREVDNTLSL                               EHQKFLKHKFLVQEIMFDRCLDKAPTVRSKALSSFA                               HCLELTVTSASESILELLINSPTFSVIESHPGTLLRNSSA                               FSYQRQTSNRSEPSGEINIDSSGETVGSGERCVMAML                               RRRIRDEKTNVRKSALQVLVSILKHCDVSGMKEDLW                               ILQDQCRDPAVSVRKQALQSLTELLMAQPRCVQIQK                               AWLRGVVPVVMDCESTVQEKALEFLDQLLLQNIRH                               HSHFHSGDDSQVLAWALLTLLTTESQELSRYLNKAF                               HIWSKKEKFSPTFINNVISHTGTEHSAPAWMLLSKIA                               GSSPRLDYSRIIQSWEKISSQQNPNSNTLGHILCVIGHI                               AKHLPKSTRDKVTDAVKCKLNGISVGL*EVISSAVDA                               LQRLCRASAETPAEEQELLTQVCGDVLSTCEHRLSNI                               VLKENGTGNMDEDLLVKYIFTLGDIAQLCPARVEKRI                               FLLIQSVLASSADADHSPSSQGSSEAPASQPPPQVRGS                               VMPSVIRAHAIITLGKLCLQHEDLAKKSIPALVRELEV                               CEDVAVRNNVIIVMCDLCIRYTIMVDKYIPNISMCLK                               DSDPFIRKQTLILLTNLLQEEFVKWKGSLFFRFVSTLI                               DSHPDIASFGEFCLAHLLLKRNPVMFFQHFIECIFHFN                               NYEKHEKYNKFPQSEREKRLFSLKGKSNKERRMKIY                               KFLLEHFTDEQRFNITSKICLSILACFADGILPLDLDAS                               ELLSDTFEVLSSKEIKLLAMRSKPDKDLLMEEDDMA                               LANVVMQEAQKKLISQVQKRNFIENIIPIIISLKTVLEK                               NKIPALRELMHYLREVMQDYRDELKDFFAVDKQLA                               SELEYDMKKYQEQLVQEQELAKHADVAGTAGGAE                               VAPVAQVALCLETVPVPAGQENPAMSPAVSQPCTPR                               ASAGHVAVSSPTPETGPLQRLLPKARPMSLSTIAILNS                               VKKAVESKSRHRSRSLGVLPFTLNSGSPEKTCSQVSS                               YSLEQESNGEIEHVTKRAISTPEKSISDVTFGAGVSYI                               GTPRTPSSAKEKIEGRSQGNDILCLSLPDKPPPQPQQW                               NVRSPARNKDTPACSRRSLRKTPLKNSQLKQRLPTSV                               QAGRSP               916   A   315   569   QSRSCSRHQSKPDRRTDARLHTLHGSFLHTRRGSVN                               TAREGHQMADEIDAMALYRAWQQLDNGSCAQIRRV                               SEYGEHNNSHADD               917   A   544   983   SVQNPRVNWIHAALQRTGRGRRRHEQHGEDHFVNG                               AAGVHQAANGLVNPPRHQVFGAHQAKGDGENHRQ                               RGAPDGDLQRDGHFGEVILPLAEIGREEVGGERRHV                               AAVFDQ/S*AGPFPRPATRRPTRRVQRPSSEARTSCA                               WVGRW               918   A   1   361   MINPNPERSDDLVFWGLFRAGGMWSAIIAPVMILLV                               GILLPLGLFPGDALSYERVLAFAQSFIGRVFLFLMIVL                               PLWCGLHRMHHAMHDLKIHVPAGKWV\FYGLAAIL                               TVVTLIGVVTI               919   A   1   971   MWALFMIRNVKKQRPVNLDLQTIRFPITAIASILHRV                               SGVITFVAVGILLWLLEYRLSYLKGSSKLRDYGQLLT                               LEIPAALLPIHTGIVNQNINCTETLTASSDNLLRRAFC                               GDTHLHEVHLNTLFFNHFLCFAVIFDETRNKDICATS                               GQHAHFVDKKRKRELLSHMIGKGNWQQVLVFTRTK                               HGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADF                               KSGDIRVLVATDIAA/RGLDIEELPHVVNYELPNVPED                               YVHRIGRTGRAAATGEALSLVRSFFDWCDDCAAAG                               GMGNRNAQLADGIYHLRCIELYLGDGMADFL               920   B   1   5305   MDWLAKYWWILVIVFLVGVLLNVIKDLKRVDHKKF                               LANKPELPPHRDFNDKWDDDDDWPKKDQPKKPGNL                               SFTSFQSHHHRQAYRHLEYRQYARVHLRLQQCRTGP                               ATSDSGIEVNQNIAVARAGDIVSARFGIPWNATIRIGI                               CIRCPSGKSSHMRGATINITLIGKQQEKEANGLDPEVL                               AEINREREAFLAAQQGSTSTELFTTIEGNYADAVRLL                               TTAHSVPFDGKATLFVAERTLQEGMSPERAWSPWIA                               ELDIYRQDCAHVDIISPGTFEKIGPIIRATLNRLYPMSS                               LNIKQGSDAHFPDYPLASPSNNEIDLLNLISVLWRAK                               KTVMAVVFAFACAGLLISFILPQKWTSAAVVTPPEPV                               QWQELEKSFTKLRVLDLDIKIDRTEAFNLFIKKFQSVS                               LLEEYLRSSPYVMDQLKEAKIDELDLHRAIVALSEK                               MKAVDDSASKKKDEPSLYTSWTLSFTAPTSEEAQTV                               LSGMFAQTAGKHYPAPITAVKTIEAAARFGREEALN                               LENKSFVPLAHTNEARALVGIFLNDQYVKGKAKKLT                               KDVETPKQAAACRYVMKDINDKSLTLGMTEAAKLL                               NKQLERGKIDGLKLAGVISTIHPTLDYAGFDRVDIVV                               EAVVENPKVKKAVLAETEQKVRQDTVLASNTSTIPIS                               ELANALERPENFCGMHFFNPVHRMPLVEIIRGEKSSD                               ETIAKVVAWASKMGKTPIVVNDCPGFFVNRVLFPYF                               AGFSQLLRDGADFRKIDKVMEKQFGWPMGPAYLLD                               VVGIDTAHHAQAVMAAGFPQRMQKDYRDAIDALFD                               ANRFGQKNGLGFWRYKEDSKGKPKKEEDAAVEDLL                               AEVSQPKRDFSEEEIIARMMIPMVNEVVRCLEEGIIAT                               PAEADMALVYGLGFPPFHGGAFRWLDTLGSAKYLD                               MAQQYQHLGPLYEVPEVGVAVGLHGASVQQQKSFC                               PSVSIYSQPIPGLQQLCAAPPPPGLVHRTAISEGVGMP                               LHVVNLPPKRFARKRLEPKWVRITWQFADMQDIGKT                               PLTACRCQQVFSNVTRRHQRPQHRHNATFAPDLPITI                               ELFDYHIPRIVSISSAFSPIIDVASALRRVFSRSGVITAC                               NNQSISCASRVSKTLSRFESVVGVNFATRLHISEDIRT                               PECIYCLLRVAISNNAVPADGARYREKSVLLGDRVAP                               SGGERCKRGNGGARKGGRARGGAPRDPKGAARAK                               ANAWPWTEPRECSLIAGEIAIECQRGIGHQDRFQRLIT                               TLRQVLECDASALLRYDSRQFIPLAIDGLAKDVLGRR                               FALEGHPRLEAIARAGDVVRFPADSELPDPYDGLIPG                               QESLKVHACVGLPLFAGQNLIGALTLDGMQPDQFDV                               FSDEELRLIAALAAGALSNALLIEQLESQNMLPGDAT                               PFEAVKQTQMIGLSPGMTQLKKEIEIVAASDLNVLIS                               GETGTGKELVAKAIHEASPRAAKLLRVLQYGDIQRV                               GDDRCLRVDVRVLAATNRDLRIEEVLAGDCRDRFVS                               SPERVSTFGAAAAAVEALRDHLNTLGGEHHDPVQLL                               NIYYETPDNWLRGHDMGLRIRGENGRYEMTMKVAG                               RVTGGLHQRPEYNVALSEPTLDLAQLPTEVWPNGEL                               PADLASRVQPLFSTDFYREKWLVAVDGSQIEIALDQG                               EVKAGEFAEPICELELELLSGDTRAVLKLANQLVSQT                               GLRQGSLSKAARGYHLAQGNPAREIKPTTILHVAAK                               ADVEQGLEAALELALAQWQYHEELWVRGNDAAKE                               Q               921   A   121   1819   KTMHEIADSSKKIADIISVIDGIAFQTNILALNAAVET                               ARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIE                               DSVSRVDTGSVLVESAGETMNNIVNAVTRVTDIMGE                               NCFASDEQSRGIDQIALAVSEMDRVTQQNTLYYGCG                               LVIPEHLENCWILDLGSGSGRDCYVLSQLVGEKGHV                               TGIDMTKGQRSLALRIIGVLALTSCGLAAINADDIW                               YFASGGVIGSLLSTTLQPLLHSSGGTIALLCVWAAGL                               TLFTGWSWVTIAEKLGGWILNILTFASNRTRRDDTW                               VDEDEYEDDEEYEDENHGKQHESRRARILRGALARR                               KRLAEKFINPMGRQTDAALFSGKRMDDDEEITYTAR                               GVAADPDDVLFSGNRATQPEYDEYDPLLNGSPRDIL                               KEQRLQTLKLVREMRADVSELVEMLLATPNMEQRT                               QGIGILDRQIARDLRFDHPYADYGNIPKTLFTFTGGD                               VFSRVMVRVKETFDSLAMLEFALDNMPDTPLLTEGF                               SYKPHAFALGFVEAPRGEYVHWSMLGDNQKLFRWR                               FPAITYPQLAGVALHAERQYRL               922   A   338   3   MAIPSVVISGLAVLLVAMALPSLSGSEAIKSMTIPGLV                               VPTVVRFMAVPGLIVPAVAKFTVLPDLTVPTEDKSLA                               VPSLISRAGNSVPVSSWDVFGVAKLIAKLGLLAAVA               923   A   1   60   FRQSHGP*SLHHHTQKNED*YIHEPYQSHGHP*SLH                               HHAQKNED*YIHEQYQSHGHP*SLHHHTQKNED               924   A   2   369   TLVYPAITFILLSICICYWIVTAVFLTTSGVPVYKVIAP                               GGHCIHENQTCDPEIFNTPEIAKACPGALCNFAFYGE                               KSLYHQYIPTFHVYNLFVFLWLINFVIALGQCALA\G                               AFATYYWA               925   A   3   400   VEGQEIDFLLDNGAAFSVLISCPRQLSSRSVTIRGILG                               QPVTRYFSHLLSCNWETFLQISSPLEDTTTAGPFFTPI                               QEEVARVVIIQFPTAIGVSCLEGGLTGEANRASESAL                               KIRAPLLLQRNAAPHQQRN               926   A   269   394   AAALRWLMSPRTLLCCFTSTLTQPWNRCGGKRKRK                               KSEVPE               927   A   434   1333   GASLCQWLNAHCLARHPPAPGWRSPSSLWTGSLAST                               TYCRLCPSSTGFFSNVAPSAEGHQLFLCNVERSVSHF                               DAKLLSKYVPVANRYEGTEDDYGDDPSTNSFEKEKQ                               DYVYCLESSLQTYNPDYVLMVEDDAVPEEQIFPVLE                               HLLRARFSEPHLRDALYLKLYHPERLQHYINPEPMRI                               LEWVGVGMLLGPLLTWIYMRFASRPGVSWPGMLFF                               SLYSMGLAELVGRHYFLELGRVSPSLYSVVPAPQCC                               TPAMLFPAPAARRTLTYLSQVYCHKGFGKDMALYSL                               VEGPRERGPM               928   A   1   306   CGCGSCGGCGGRCGGGCGGGCSGGCGGGCGGGCG                               GGCGSCTTCRCYRVGCCSSCCPCCRGCCGGCCSTPVI                               CCCRRTCGSCGCGYGKGCCQQKCCCQKQCCC               929   A   334   413   T*NGSAAGL*SARPRWRCCSPRGRCT*EVPATLQGPG                               LGRVAAGGKRGWRPQA*YRPSSQPQSEGPPEASSPSP                               LPHKPSHGPGLNKAMADTVSFAPSTSPISLFFYECLPS               930   A   1   419   EKEGEDERLPPKSRIDYNHPGRVLLQNLTMSYSGLY                               QCTAGNEAGKESCVVRVTVQYVQSIGMVAGAVTGI                               VAGALLIFLLVWLLIRRKDKERYEEEERPNEIREDAE                               APKARFVKPSSSSSGSRSSRSGSSSTSLHSK               931   A   1   375   IETTQPSEDTNANSQDNSMQPETSSQQQLLSPTLSDR                               GGSRQDAADAGKPQRKFGQWRLPSAPKPISHSVSSV                               NLRFGGRTTMKSVVCKMNPMTDAASCGSEVKKWW                               TRQLTVESDESGDDLLDI               932   A   254   652   GRSLSFKTFLIWVLISIYQGGILMYGALVLFESEFVHV                               VAISFTALILTELLMVALTVRTWHWLMVVAEPLSLG                               CYVSSLAFLNEYFDVAFITTVTFLWKVSAITVVSCLP                               LYVLKYLRRKLSPPSYCKLAS               933   A   9   422   ESRERSGNRRGAEDRGTCGLQSPSAMLGAKPHWLPG                               PLHSPGLPLVLVLLALGAGWAQEGSEPVLLEGECLV                               VCEPGRAAAGGPGGAALGEAPPGRVAFAAVRSHHH                               EPAGETGNGTSGAIYFDQVLVNEGGGFDRAS               934   C   346   471   MRFCMLFTLLPLRVFLGTIQAPHFALLWLKGQTFAS                               ACPGV               935   A   27   483   RDAEDAIYGRNGYDYGQCRLRVEFPRTYGGRGGWP                               RGGRNGPPTRRSDFRVLVS/GWQ/DLKDHMREAGDV                               CYADVQKDGVGMVEYLRKEDMEYALRKLDDTKFR                               SHEGETSYIRVYPERSTSYGYSRSRSGSRGRDSPYQSR                               GSPHYFSPFRPY               936   B   1   654   MTSESPEVKSCEPTTNHRETIRVDEQRKKSSRPTTTDF                               SQHKFLPGDNATWNCESIKSLFVDKLPSFGYVFITSV                               NTDKYILDEPGGPNAIKRVIVRGKQEGDKSHRNPSGC                               VALRGFGQGYLLNNVELFDITTPGYSHSGSINGWLFV                               DSILFPGDSSTTPADNGQCMTQHRLTHTSTSSEKDVG                               ASLCGFLSPPLVLGKVTALSIVNERSISRNT               937   A   6323   7130   PGCIRCKCVAVDGDPCMKSNNALIVILGTVTLDAVGI                               GLVMPVLPGLLRDIVHSDSIASHYGVLLALYALMQF                               LCAPVLGALSDRFGRRPVLLASLLGATIDYAIMATTP                               VLWIYPLVNSPFCWPRASRYQQGHQDLFILRSDLPSQ                               VFIRDKLMERRNRRTGRTEKARIWEVTDRTVRTWIG                               EAVAAAAADGVTFSVPVTPHTFRHSYAMHMLYAGI                               PLKVLQSLMGHKSISSTEVYTKVFALDVAARHRVQF                               AMPESDAVAMLKQLS               938   B   1   806   MPQRALLCQLTYACISAQLICPFAMEQQLVACCHPM                               SGECACKPGWSGLYCNETCSPGFYGEACQQICSCQN                               GADCDSVTGKCTCAPGFKGIDCSTPCPLGTYGINCSS                               RCGCKNDAVCSPVDGSCTCKAGWHGVDCSIRCPSGT                               WGFGCNLTCQCLNGGACNTLDGTCTCAPGWRGEKC                               ELPCQDGTYGLNCAERCDCSHADGCHPTTGHCRCLP                               GWSVFTGNGVPINNIHIIVWDCFHVKVQTVVTFCLIT                               LEAKTVTQDMTVSASX               939   A   3   627   GRLMLAGHGGVFALTLLLILTTTGLFFVFDCPYLARK                               LTLAIPIIAAILFFFVMSCLLQTSFTDPGILPRATVCEA                               AALEKQIDNTGSSTYRPPPRTREVLINGQMVKLKYCF                               TCKMFRPPRTSHCSVCDNCVERFDHHCP\WVGNCVG                               RRNYRFFYTFILSLSFLTAFIFACVVTHLTLRELWVRA                               VGSGRGQPASSRVSKLQQSLSL               940   A   2   464   FVGVVVGVAEVRNWRCCCLGSTCWCRSLVLVCVLA                               ALCFASLALVRRYLHHLLLWVESLDSLLGVLLFVVG                               FIAVSFPCGWGYIVLNVAAGYLYGFVLGMGLMMVG                               VLIGTFIAHVVCKRLLTAWVAARIQSSEKLSAVIRVK                               EGGSGLKWWRL               941   A   1   421   FRSFVTEQNWDSLEVFDGADNTVTMLGSFSGTTVPA                               LLNSTSNQLYLHFYSDISVSAAGFHLEYKTVGLSSCP                               EPAVPSNGVKTGERYLVNDVVSFQCEPGYALQGHA                               HISCMPGTVRRWNYPPPLCIAQCGGTVEEMEG               942   A   120   530   MVAPGLVLGLVLPLILWADRSAGIGFRFASYINNDM                               VLQKEPAGAVIWGFGTPGATVTVTLRQGQETIMKKV                               TSVKAHSDTWMVVLDPMKPGGPFEVMAQQTLEKIN                               FTLRVHDVLFGDVWLCSGQSNMQMTVLQIF               943   A   205   377   NIVENIVFCWPGVCFLQTCTVCINPETSDE/WPGAVA                               HACNPSTLGGQDGQITRSGDRE               944   A   2   408   EDGEYFLMIRGKLLKIFCAGMHSDHPKEYVTLVHGD                               SENFSEVYGHRLHNPTECPYNGSRRDDCQCRKDYTA                               AGFSSFQKIRIDLTSMQIITTDLQFARTSEGHPVPFATA                               GDCYSAAKCPQVCPWGLPPCQGFT               945   A   1   4218   MALKNINYLLIFYLSFSLLIYIKNSFCNKNNTRCLSNS                               CQNNSTCKDFSKDNDCSCSDTANNLDKDCDNMKDP                               CFSNPCQGSATCVNTPGERSFLCKCPPGYSGTICETTI                               GSCGKNSCQHGGICHQDPIYPVCICPAGYAGRFCEID                               HDECASSPCQNGAVCQDGIDGYSCFCVPGYQGRHCD                               LEVDECASDPCKNEATCLNEIGRYTCICPHNYSGVNC                               ELEIDECWSQPCLNGATCQDALGAYFCDCAPGFLGD                               HCELNTDECASQPCLHGGLCVDGENRYSCNCTGSGF                               TGTHCETLMPLCWSKPCHNNATCEDSVDNYTCHCW                               PGYTGAQCEIDLNECNSNPCQSNGECVELSSEKQYG                               RITGLPSSFSYHEASGYVCICQPGFTGIHCEEDVNECS                               SNPCQNGGTCENLPGNYTCHCPFDNLSRTFYGGRDC                               SDILLGCTHQQCLNNGTCIPHFQDGQHGFSCLCPSGY                               TGSLCEIATTLSFEGDGFLWVKSGSVTTKGSVCNIAL                               RFQTVQPMALLLFRSNRDVFVKLELLSGYIHLSIQVN                               NQSKVLLFISHNTSDGEWHFVEVIFAEAVTLTLIDDS                               CKEKCIAKAPTPLESDQSICAFQNSFLGGLPVGMTSN                               GVALLNFYNMPSTPSFVGCLQDIKIDWNHITLENISSG                               SSLNVKAGCVRKDWCESQPCQSRGRCINLWLSYQC                               DCHRPYEGPNCLREYVAGRFGQDDSTGYVIFTLDES                               YGDTISLSMFVRTLQPSGLLLALENSTYQYIRVWLER                               GRLAMLTPNSPKLVVKFVLNDGNVHLISLKIKPYKIE                               LYQSSQNLGFISASTWKIEKGDVIYIGGLPDKQETELN                               GGFFKGCIQDVRLNNQNLEFFPNPTNNASLNPVLVN                               VTQGCAGDNSCKSNPCHNGGVCHSRWDDFSCSCPA                               LTSGKACEEGQRCGFSPCPHGAHCQPVLQGFECIAN                               AVFNGQSGQILFRSNGNITRELTNITFGFRTRDANVIIL                               HAEKEPEFLNISIQDSRLFFQLQSGNSFYMLSLTSLQS                               VNDGTWHEVTLSMTDPLSQTSRWQMEVDNETPFVT                               STIATGSLNFLKDNTDIYVGDRAIDNIKGLQGCLSTIEI                               GGIYLSYFENVHGFINKPQEEQFLKISTNSVVTGCLQL                               NVCNSNPCLHGGNCEDIYSSYHCSCPLGWSGKHCEL                               NIDECFSNPCIHGNCSDRVAAYHCTCEPGYTGVNCE                               VDIDNCQSHQCANGATCISHTNGYSCLCFGNFTGKF                               CRQSRLPSTVCGNEKTNLTCYNGGNCTEFQTELKCM                               CRPGFTGEWCEKDIDECASDPCVNGGLCQDLLNKFQ                               CLCDVAFAGERCEVDLADDLISDIFTTIGSVTVALLLI                               LLLAIVASVVTSNKRATQGTYSPSRQEKEGSRVEMW                               NLMPPPAMERLI               946   A   2   2131   RVARGWGGCGACGGSGIVGQGKGEPSRRRGRAAGR                               PQSMERGKMAEAESLETAAEHERILREIESTDTACIGP                               TLRSVYDGEEHGRFMEKLETRIRNHDREIEKMCNFH                               YQGFVDSITELLKVRGEAQKLKNQVTDTNRKLQHEG                               KELVIAMEELKQCRLQQRNISATVDKLMLCLPVLEM                               YSKLRDQMKTKRHYPALKTLEHLEHTYLPQVSHYRF                               CKVMVDNIPKLREEIKDVSMSDLKDFLESIRKHSDKI                               GETAMKQAQQQRNLDNIVLQQPRIGSKRKSKKDAYI                               IFDTEIESTSPKSEQDSGILDVEDEEDDEEVPGAQDLV                               DFSPVYRCLHIYSVLGARETFENYYRKQRRKQARLV                               LQPPSNMHETLDGYRKYFNQIVGFFVVEDHILHTTQ                               GLVNRAYIDELWEMALSKTIAALRTHSSYCSDPNLV                               LDLKNLIVLFADTLQVYGFPVNQLFDMLLEIRDQYSE                               TLLKKWAGIFRNILDSDNYSPIPVTSEEMYKKVVGQF                               PFQDIELEKQPFPKKFPFSEFVPKVYNQIKEFIYACLKF                               SEDLHLSSTEVDDMIRKSTNLLLTRTLSNSLQNVIKR                               KNIGLTELVQIIINTTHLEKSCKYLEEFITNITNVLPET                               VHTTKLYGTTTFKDARHAAEEEIYTNLNQKIDQFLQL                               ADYDWMTGDLGNKASDYLVDLIAFLRSTFAVFTHLP                               VSGSCSYFVLYI               947   A   236   3   MLSVTAFILAETVLASQEVQGGVQVRVYLMNAVPD                               GLQGGSPVGGLGLLLAPDNSGHRRSSCRIPAARVYX                               XXXPRPP               948   A   1   2369   AGGARLRPARGRPPRLLPPRPGPCRPPPVPAPTVNER                               RAPPRAGWERRSDAGLSRGARPAEMYGVCGCYGAL                               RPRYKRLVDNIFPEDPEDGLVKTNMEKLTFYALSAPE                               KLDRIGAYLSERLIRDVGRHRYGYVCIAMEALDQLL                               MACHCQSINLFVESFLKMVAKLLESEKPNLQILGTNS                               FVKFANIEEDTPSYHRSYDFFVSRFSEMCHSSHDDLEI                               KTKIRMSGIKGLQGVVRKTVNDELQANIWDPQHMD                               KIVPSLLFNLQHVEEAESRSPSPLQAPEKEKESPAELA                               ERCLRELLGRAAFGNIKNAIKPVLIHLDNHSLWEPKV                               FAIRCFKIIMYSIQPQHSHLVIQQLLGHLDANSRSAAT                               VRAGIVEVLSEAAVIAATGSVGPTVLEMFN\TLLRQL                               RLSIDYALTGSYDGAVSLGTKIIKEHEERMFQEAVIK                               TVGSFASTLPTYQRSEVILFIMSKVPRPSLHQAVDTGR                               TGENRNRLTQIMLLKSLLQVSTGFQCNNMMSALPSN                               FLDRLLSTALMEDAEIRLFVLEILISFIDRHGNRHKFST                               ISTLSDISVLKLKVDKCSRQDTVFMKKHSQQLYRHIY                               LSCKEETNVQKHYEALYGLLALISIELANEEVVVDLI                               RLVLAVQDVAQVNEENLPVYNRCALYALGAAYLNL                               ISQLTTVPAFCQHIHEVIETRKKEAPYMLPEDVFVERP                               RLSQNLDGVVIELLFRQSKISEVLGGSGYNSDRLCLP                               YIPQLTDEDRLSKRRSIGETISLQVEVESRNSPEKEEVS                               VRATVLGQPHLL               949   A   906   1046   PDHHNWSQ*TTTGAQRQT*KRTVKEV*SAHNEAMCF                               GTCASDCLYR               950   A   489   855   RPVGRGGSRSDRGARAGRCAPDTLSALRCCWRSPAG                               APGTQDPDPAGPGAATEAPALHPAGGTGTSPPPPATA                               APTGGRGRPCADCCRRGARPGPAPTTAAAPAAATAA                               TNTSAARLSGPAP               951   A   310   393   PHTDISGTPEIMHYVHVHRVTTQPRNKP               952   A   3   428   SSRLVLLAGAAALASGSQGDREPVYRDCVLQCEEQN                               CSGGALNHFRSRQPIYMSLAGWTCRDDCKYECMWV                               TVGLYLQEGHKVPQFHGKWPFSRFLFFQEPASAVAS                               FLNGLASLVMLCRYRTFVPASSPMYHTCVAFAWVS               953   A   105   335   GRLFPKVLSYHSVGYLPLILFCHFLLANCILCCLMHFL                               *FFQSYRF*G*KFGFTQHHCHYIFHKQWPLLWKNFPE                               H               954   A   51   482   MVLGLLVQIWALQEASSLSVQQGPNLLQVRQGSQAT                               LVCQVDQATAWERLRVKWTKDGAILCQPYITNGSLS                               LGVCGPQGRLSWQAPSHLTLQLDPVSLNHSGAYVC                               WAAVEIPELEEAEGNITRLFVDPDDPTQNRNRIASPP               955   A   425   1333   ELFMIKPPRNIIILNQQKLEAFPLKTGTRQGCPLSPLLF                               NIVLEVLARAIRQEKEIKGIQLGKEEVKLSLFADDMIV                               YLENPIVSAQNLLKLISNFSKVSGYKINVQKSQAFLY                               TNNRQTESQIMSELPFTIASKRIKYLGIQLTRDVKDLF                               KENYKPLLKEIKEDTNKWKNIPCSWVGRINIVKMAIL                               PKVIYRFNAIPIKLPMTFFTELEKTTLKFIWNQKRARI                               AKSILSQKNKSGGITLPDFKLYYKATVTKTACSPHSIV                               LPATMMEQNRALRNNTTHHGRGSDPAGQAAAAAG                               ATCQ               956   A   226   444   MRPDDINPRTGLVVALVRVFLVFGFMFTVSGMKGET                               LGNIPLLAIGPAICLPGIAAIALARKTEGCTKWPEND               957   A   3   1371   SYFSSSTPTYPVGTTVEFSCDPGYTLEQGSIIIECVDPH                               DPQWNETEPACRAVCSGEITDSAGVVLSPNWPEPYG                               RGQDCIWGVHVEEDKRIMLDIRVLRIGPGDVLTFYD                               GDDLTARVLGQYSGPRSHFKLFTSMADVTIQFQSDP                               GTSVLGYQQGFVIHFFEVPRNDTCPELPEIPNGWKSP                               SQPELVHGTVVTYQCYPGYQVVGSSVLMCQWDLT                               WSEDLPSCQRVTSCHDPGDVEHSRRLISSPKFPVGAT                               VQYICDQGFVLMGSSILTCHDRQAGSPKWSDRAPKC                               LLEQLKPCHGLSAPENGARSPEKQLHPAGATIHFSCA                               PGYVLKGQASIKCVPGHPSHWSDPPPICRAASLDGFY                               NSRSLDVAKAPAASSTLDAAHIAAAIFLPLVAMVLLV                               GGVYFYFSRLQGKSSLQLPRPRPRP\YNRI\TIESAF\DN                               PTYETGETREYEVSI               958   A   1   2667   GAYHKHLMELALQQTYQDTCNCIKSRIKLEFEKRQQ                               ERLLLSLLPAHIAMEMKAEIIQRLQGPKAGQMENTN                               NFHNLYVKRHTNVSILYADIVGFTRLASDCSPGELVH                               MLNELFGKFDQIAKENECMRIKILGDCYYCVSGLPIS                               LPNHAKNCVKMGLDMCEAIKKVRDATGVDINMRV                               GVHSGNVLCGVIGLQKWQYDVWSHDVTLANHMEA                               GGVPGRVHISSVTLEHLNGAYKVEEGDGDIRDPYLK                               QHLVKTYFVINPKGERRSPQHLFRPRHTLDGAKMRA                               SVRMTRYLESWGAAKPFAHLHHRDSMTTENGKISTT                               DVPMGQHNFQNRTLRTKSQKKRFEEELNERMIQAID                               GINAQKQWLKSEDIQRISLLFYNKVLEKEYRATALPA                               FKYYVTCACLIFFCIFIVQILVLPKTSVLGISFGAAFLL                               LAFILFVCFAGQLLQCSKKASPLLMWLLKSSGIIANRP                               WPRISLTIITTAIILMMAVFNMFFLSDSEETIPPTANTT                               NTSFSASNNQVAILRAQNLFFLPYFIYSCILGLISCS\VF                               LRVNYELKMLIMMVALVGYNTILLHTHAHVLGDYS                               QVLFERPGIWKDLKTMGSVSLSIFFITLLVLGRQNEY                               YCRLDFLWKNKFKKEREEIETMENLNRVLLENVLPA                               HVAEHFLARSLKNEELYHQSYDCVCVMFASIPDFKE                               FYTESDVNKEGLECLRLLNEIIADF\DDLLSKPKFSGV                               EKIKTIGSTYMAATGLSAVPSQEHSQEPERQYMHIGT                               MV\EFAFAL\VGKLDAINKHSFNDFKLRVGINHGPVIA                               GVIGAQKPQYDIWGNTVNVASRMDSTGVLDKIQVTE                               ETSLVLQTLGYTCTCRGIINVKGKGDLKTYFVNTEMS                               RSLSQSNVAS               959   A   281   1092   AFCTVTLIFPHFQGAVIHKLGITLVSLLLFLTLTKTFPV                               TCLVDDWFVHKASFPARLCYLYVVMQASKPKYYFA                               WTLADAVNNAAGFGFSGVDKNGNFCWDLLSNLNIW                               KIETATSFKMYLENWNIQTATWLKCVCYQRVPWYP                               TVLTFILSALWHGVYPGYYFTFLTGILVTLAARAVRN                               NYRHYFLSSRALKAVYDAGTWAVTQLAVSYTVAPF                               VMLAVEPTISLYKSMYFYLHIISLLIILFLPMKPQAHT                               QRRPQTLNSINKRKTD               960   A   1   361   VCFYVSAMVPVKSPREYYVQQEVIVLFCETVERALD                               FGYLTQDMIDDYEPALMFSIPRLAIVWGLVVYADGP                               LNLDRKVEDMSELFRPFHTLLRKIRDLLQTLTEEELH                               TLERNLCISQD               961   A   710   1831   IRMKSKEIIARCIKPYHSMARTQPGTRNKENGPAGPT                               ALDNVASSDDTGRHRPQTTQLAPGFAHPLQLASFRR                               MVLFLSGEGRSRGGPELQFPASCRRGEGSPGVRESGS                               GGIAATSTPNYPPNQDSKEHDIRGAEHQKQEQPAKPP                               HTARSAYPPQKSSYPANAKATRHSPETAAAKEARAP                               AAAQPQRHQPNPSPAPHTRPATAATRQPERRVPSPTH                               RHPAATRLSPRRQSPSPRPHHDRRGFPRLAETLQHPM                               CPLPLVASAGHHRKHHRLLLLLAPQAPEREASDEI\VFS                               GRSRSRGCPTEFQESAMCFPNPGLPDSCGESQAVTILI                               LRKFQKVIWVIEVPLDYKKGSWEYFSRMETIIMPFEN                               IQSE               962   A   3   226   LDPNGEQVVWQASGWAARIIQHEMDHLQGCLFIDK                               MDSRTFTNVYWMKDGTQKVQNNILSHVAILQLCPD                               EENG               963   A   2   505   QGSRAKLSTPLGLSCTRSTAGPSRFARCSLGGCSHPS                               RHSPHLPPPPPVQFRAGPRGRQGSPSRGSPS\GAFPAG                               PGGAAAAAVGDDQQQQEQHGAHEGEENNEGNSVP                               CG/PGKTGGSSVSPGLPEPWPPAPLWTQPSWSAPCH\P                               *KPPIPPTRQVLGRTGCFLLPAP               964   A   1   709   DDPDYAQLGTRWHEGDADSISLELRKPDGTLVSFTA                               DFKKDVKVFRALILGELEKGQSQFQALCFVTQLQHN                               EIIPSEAMAKLRQKNPRAVRQAEEVRGLEHLHMDVA                               VNFSQGALLSPHLHNVCAEAVDAIYTRQEDVRFWLE                               QGVDSSVFEALPKASEQAELPRCRQVGDRGKPCVCH                               YGLSLAWYPCMLKYCHSRDRPTPYKCGIRSCQKSYS                               FDFYVPQRQLCLWDEDPYPG               965   A   1   1183   RLITVKLRR/GDTGRIPLSHIRLLPPDYKIQCAEPSPAL                               LVPSAKRRSRKTSKDTGEGKDGGTAGSEEPGAKARG                               RGRKPSAKAKGDRAATLEEGNPTDEVPSTPLALEPSS                               TPGSKKSPPEPVDKRAKAPKARPALPQPSPAPPAFTS                               CPAPEPFVELPAPATTLAPAPLITMPATRPKPKKARA                               AKESGAKGPRRPGEEAELLVKLDHEGVMSPKSKKA                               KEALLLWEDPGRGGLGPDRDLAQEPGPGLTFEDSGN                               PKSPDKAQAEQDGAEESESSSSSSSSSSGSETEGEEEG                               DKNGDGGCGAGGRGAPHQGHQAGWQGAASAHSPG                               KKTPAPQPQAPPPQPTQPLQPKTQAGAKSRPKKREG                               VHLPTTKELAKRQRLPSVENRPKIAAFLPA               966   A   1023   766   MLCSRLGTTASWRRLGIRAWAPLLLLFPWDWHFILS                               FSSRPWAGTLLAPHDVIMGSSTFPQSCQAEAGPRHA                               WPTGRFSRRLRRV*               967   A   651   836   TPGAPSGAQSNGWSSCEQSRPDVGEKGPLGRALCVP                               CPSSPTHPKAKDGFPPFTAVILTSF               968   A   1   1206   MALSSWPVVLRLNMADFVFSFLCLGIGTSIVLGILFY                               LLQAHRYLQEGMTYQLALSFYLTWASVFLFLMTGM                               GEDEESALQTLLDPRSSYLLVSLEILPTNPSPLSPCAVS                               EDESEMRGLSLLRRQSQATGRLEPTFKHDSTLLALQG                               ALGLYDGHTPPYAACLGFEFRKHLGNPAKDGGNVT                               VSLFYRNDSAHLPLPLSLPGCPAPCPLGRFYQLTAPA                               RPPAHGVSCHGPYEAVIPPGPGAIIPSTGPAVGMQRE                               RSEVGSGVPARTVYASEQHAYMWHSALIPDSGLRGK                               PTLSSRKPPQTSCGPEFANVLSLALCGALVVCKARA                               MDQARPRQLIGIDALRDPRASSRTRAGGLGMIRRQEE                               EPAARTVLARCDSSPSECPSHARAPYDTGPLFNAKG               969   A   250   1013   NQPGWHGGGPSAGRAAKKCPGEVGPGAPAAAAEPA                               RGDAGGEAGGCHPE/SPSTTSS*VIPST*ESSS*PSSPGF                               GSSHMPGSTLMPPWCTPRSGPRTHSQRREVTCAWCS                               CWEPGRTAASPAASQTSAGAS*PSPAAQATACPTNCS                               SSSGPE*GGAHRDHSNRARTISTSSAPT*WT*TAKLRP                               LDTPTLPGTSSWKTSCSVEWAASPTSTSSGGWRPFSA                               GRNSRKDASGSLMLKMKNHLKLFNISSIFRGE               970   A   1   6384   MVSPEPKTGHSIRNWLDELKDLPILHAYSNLPSSPAV                               DLAIHSSKEGRMDWTEGQVTGPVVRSAATSGAGSTT                               SGVVSGSLGSREINYILRVLGPAACRNPDIFTEVANCC                               IRIALPAPRGSGTGNGSSRIPRESAPEMATAESLVEEL                               SEDAAGGASPGVELPALGCSELPAAEVSPTASSKNLE                               TICEYAYCMAMLPETGLDPYPKRGFLDLTQERIWTDI                               PPSPGNIPTTHPLMVRHADHSSLTLGSGSSTTRLTQGI                               GRSQRTLRQLTANTGHTIHVHYPGNRQPNPPLILQRL                               LGPSAAADILQLSSSLPLQSRGRARLL\VGNDDVHIIA                               RSDDELLDDFFHDQ\STATSQAGTLSSIPTALTRWTEE                               CKVLDAESMHDCVSVVKVSIVNHLEFLRDEELEERR                               EKRRKQLAEEETKITDKGKEDKENRDQSAQCTASKS                               NDSTEQNLSDGTPMPDSYPTTPSSTDAATSESKETLG                               TLQSSQQQPTLPTPPALGEVPQELQSPAGEGGSSTQL                               LMPVEPEELGPTRPSGEAETTQMELSPAPTITSLSPER                               AEDSDALTAVSSQLEGSPMDTSSLASCTLEEAVGDTS                               AAGSSEQPRAGSSTPGDAPPAVAEVQGRSDGSGESA                               QPPEDSSPRASSESSSTRDSAVAISGADSRGILEEPLPS                               TSSEEEDPLAGISLPEGVDPSFLAALPDDIRREVLQNQ                               LGIRPPTRTAPSTNSSAPAVVGNPGVTEVSPEFLAALP                               PAIQEEVLAQQRAEQQRRELAQNASSDTPMDPVTFIQ                               TLPSDLRRSVLEDMEDSVLAVMPPDIAAEAQALRRE                               QEARQRQLMHERLFGHSSTSALSAILRSPAFTSRLSG                               NRGVQYTRLAVQRGGTFQMGGSSSHNRPSGSNVDT                               LLRLRGRLLLDHEALSCLLVLLFVDEPKLNTSRLHRV                               LRNLCYHAQTRHWVIRSLLSILQRSSESELCIETPKLT                               TSEEKGKKSSKSCGSSSHENRPLDLLHKMESKSSNQL                               SWLSVSMDAALGCRTNIFQIQRSGGRKHTEKHASGG                               STVHIHPQAAPVVCRHVLDTLIQLAKVFPSHFTQQRT                               KETNCESDRERGNKACSPCSSQSSSSGICTDFWDLLV                               KLDNMNVSRKGK\NSV\KSVPVSAGG\EGETSPYSL\E                               ASPLG\QLMNMLSHPVIRRSSLLTEKLLRLLSLISIALP                               ENKVSEAQANSGSGASSTTTATSTTSTTTTTAASTTP                               TPPYVHPPRVTSAPA\LVAATAISTIVVAASTTVTTPT                               TATTTVSISPTTKGSKSPAKVSDGGSSSTDFKM\VSSG                               LTENQLQLSVEVLTSHSCSEEGLEDAANVLLQLSRGD                               SGTRDTVLKLLLNGARHLGYTLCKQIGTLLAELREY                               NLEQQRRAQCETLSPDGLPEEQPQTTKLKGKMQSRF\                               DMAENVVIVASQKRPLGGRELQLPSMSMLTSKTSTQ                               KFFLRVLQVIIQLRDDTRRANKKAKQTGRLGSSGLGS                               ASSIQAAVRQLEG*RLDAIIQMVREGQRARRQQQAA                               TSESSQSEASVRREESPMDVDQSPSAQDTQSIASDG                               TPQGEKEKEERPPELPLLSEQLS\LDELWDMLGECLK                               ELEESHDQHAVLVLQAVEAFFLVHATERESKPPVR                               DTRESQLAHIKDEPPPLSPAPLTPATP\SSFDQFFSGEP                               S\SMHIS\SSLPPDTQKFLRFAETHRTVLNQILRQSTTH                               LADGPFAVLVDYIRVLDFDVKRKYFRQELERLDEGL                               RK\EDMAVHVRRDHVFEDSYRELHRKSPEEMKNRLY                               IVFEGEEGQDAG\GLLREWVYDSSFREMF\NPMYGLF\                               RTSPG*FESPNTINPS\SH\CNPNHLS\YFKFCSGRIV\AK                               AVYDN\RLL\ECYFTRSFYKHHLGASSVRYTDM\ESE\                               DYHF\YQGLGLSGWENDVSTL\GYDLTFQALRVPGV                               LGVCEV\R\DLKPNGGQPSWVTEE\NKKEVCTPWYCQ                               MRMTGAIRQQVAAFL\EGF\YEIIPK\RLISIF\TEHELEL                               LISGLPTIDIDDLNPNTEYHKYQSNSI\QI\QWFLEETLP                               FLSNQN*PVPKVPSQFVHGVPSKGNPWQGLCLPLEG                               HGMGISGSFQVPFGGGQVPQIALPSAHTCF\N\QLDLP                               AYESFEKLRHMLLLAI\QECSEGFGLA               971   A   3   1186   GGGGFSPRSKSQKPGRGRDGAVTPNRKNKGNYKKN                               PAKRCEASESSHGKVRSSSTCSVQLPQVKEALKTIHI                               KVIDDEAYEKNKYFIEMMGPRMVDMSFQKDVTDR                               KLTMEEEEAKRIAEMGKPVLGEHPKLEVIIEESYEFK                               TTVDKLIKKTNLALVVGTHSWRDQFMEAITVSAAGD                               EDEDESGEERLPSCFDYVMHFLTVFWKVLFACVPPT                               EYCHGWACFAVSILIIGMLTAIIGDLASHFGCTIGLKD                               SVTAVVFVAFGTSVPDTFASKAAALQDVYADASIGN                               VTGSNAVNVFLGIGLAWSVAAIYWALQGQEFHVSA                               GTLAFSVTLFTIFAFVCISVLLYRRRPHLGGELGGPRG                               CKLATTWLFVSLWLLYILFATLEAYCYIKGF               972   A   1   284   ERQDWESRLEAMECAFHLEKSVNQSLLELHQLAME                               KGDPQLCDFLESHFLNQQVKAIKKLGDYLSNLCKT*                               APEAGLAEYLFDKLTLGGSEEDT               973   A   2   2020   SQVRASLPEPRNSAAAMASNMDREMILADFQACTGI                               ENIDEAITLLEQNNWDLVAAINGVIPQENGILQSEYG                               GETIPGPAFNP\ASHPASAPYS/SPSSLPAFRPVMPTQG                               RL*ER\QPRMLDFRVEYRDRNVDVVLEDTCTVGEIKQ                               ILENELQIPVSKMLLKGWKTGDVEDSTVLKSLHLPK                               NNSLYVLTPDLPPPSSSSHAGALQESLNQNFMLIITHR                               EVQREYNLNFSGSSTIQEVKRNVYDLTSIPVRHQLWE                               GWPTSATDDSMCLAESGLSYPCHRLTVGRRSSPAQT                               REQSEEQITDVHMVSDSDGDDFEDATEFGVDDGEVF                               GMASSALRKSPMMPENAENEGDALLQFTAEFSSRYG                               DCHPVFFIGSLEAAFQEAFYVKARDRKLLAIYLHHDE                               SVLTNVFCSQMLCAESIVSYLSQNFITWAWDLTKDS                               NRARFLTMCNRHFGSVVAQTIRTQKTDQFPLFLIIMG                               KRSSNEVLNVIQGNTTVDELMMRLMAAMEIFTAQQ                               QEDIKDEDEREARENVKREQDEAYRLSLEADRAKRE                               AHEREMAEQFRLEQIRKEQEEEREAIRLSLEQALPPEP                               *EENAEPVSKLRIRTPSGEFLERGFLASNKLQIVFDFV                               ASK\GF\PWDEYKLLSTFP\RRDVTQLDPNKS\LL\EVK                               LFP\QETLFPWKPKE               974   A   1   1232   FPGRRFRLVVRLRGAEAASERQVYSVTMKLLLLHPA                               FQSCLLLTLLGLWRTTPEAHASSPGAPAISAASFL*DL                               IHRYGEGDSLTLQQLKALLNHLDVGVGRGNVSQHV                               QGHRNPTTCFSSGDLFTAHNF\SEQLRIGSSELHEFCP                               TILQQLDSRACTSENQENEENEQTEEGRPSAVEVWGF                               GFLSVSLINLASLLGVLVLPCTEKAFFSRVLTYFIALSI                               GTLLSNALFQLIPERSYKNKAQVDSLPTFLAQAGMLL                               WRVRIRRRVVDPIRESWMLPFTKIPLWGYGLLCVTVI                               SLCSLLGASVVPFMKKTFYKRLLLYFIALAIGTLYSN                               ALFQLIPENRRKWWQPVHNTFGGSTAWHTDKSIEQS                               IDTLFDEVKKESEKETPSLQIGDLGPQESLKTFNNTNS                               PHH               975   A   1   740   AFVPFLLVTWSSAAFIISYVVAVLSGHVNPFLPYISDT                               GTTPPESGIFGFMINFSAFLGAATMYTRYKIVQKQNQ                               TCYFSTPVFNLVSLVLGLVGCFGMGIVANEQELAVP                               VVHDGGALLAFVCGVVYTLLQSIISYKSCPQWNSLST                               CHIRMVISAVSCAAVIPMIVCASLISITKLEWNPREKD                               YVYHVVSAICEWTVAFGFIFYFLTFIQDFQSVTL\GYP                               QKSMVIFEERRIQSHSVNVAGHF               976   A   2   374   IRRESTHLQQALGTTPQDRLTCTGHSAQPPACSASPL                               PPGPP*SSAWPLPPSTRLARQKQAAATAQP*PLTTQTL                               GPWSSASTWTSAHKQPGAAAQEWTSTAGSRQLLAG                               ASGSSPSSCSVWTN               977   A   2   728   PSLIQCGGIPLTFRALRRALCRLPLPVHVRADPLRTW                               RWHNLLVSFAHSIVSGIWALLCVWQTPDMLVEIETA                               WSLSGYLLVCFSAGYFIHDTVDIVASGQTRASWEYL                               VHHVMAMGAFFSGIFWSSFVGGGVLTLLVEVSNIFL                               TIRMMMKISNAQDHLLYRVNKYVNLVMYFLFRLAP                               QA\YLTHFFLRYVNQRTLGTFLLGILLMLDVMIIIYFS                               RLLRSDFCPEHVPKKQHKDKFLTE               978   A   120   327   RGKLLEQGLDAWALLKPPASGQRPLRMQEDAGELQ                               NERVGWLVVRFLQRVCCCGPCALVLPRLPISAA               979   A   238   2526   ALTKVNEGSMETKDLIVIGGGINGAGIAADAAGRGL                               SVLMLEAQDLACATSSASSKLIHGGLRYLEHYEFRLV                               SEALAEREVLLKMAPHIAFPMRFRLPHRPHLRPAWM                               IRIGLFMYDHLGKRTSLPGSTGLRFGANSVLKPEIKR                               GFEYSDCWVDDARLVLANAQMVALEKCNSIVAFVV                               CHTSDEPCNCLPQVYGSDENASLTAYWYSGGVQGV                               CALLPGHHRVPGLLYAGSAAAVSGLLRQFGIRLDVQ                               VRLIPILAQFAGISVLLGVWAFSRPWHQPGKALALAK                               RKADVAFEFFHKLHVPFYCFHDVDVSHESASLKEYI                               NNFAQMVNVLAGKQEESGVKVLCGTVNCFTNPRYG                               AGYKTLLNTDLRQEREHLGRFMQMVVEHKHKIGFQ                               GTLLIEPNPQDPTKHQYDCDAATVYGFLKQFGLEKEI                               KLNIQAIHATLAGLSFHQGTKLEPLKKGWLNCGKGR                               SLRSFWLLRNVAKGVCVQRRLSWQFKHAWLIKFWA                               PIPAVIASGILSTYYFGITGTFWTVTGEFTRWGGQLLQ                               LFGVHAEEWGYFKIIHLEGSPLSRIDGMMILGMFGGC                               FAAALWANNVKLRMPRTRTRIMQAIIGGILAGFGARL                               AMGCSLAAFFTGIPGYRARNSNPGKEFCQVTAHCQT                               RVKAGDNAANDGLHNSDTAARHSQFDIVGPQLFGK                               PAANHREDHHPVDAVTPLFSMDADQLQELAAPTGK                               FTRDSPKGASNAKIVSIENTRRYDRRDGGPEFNQPGV                               FEMLP               980   B   1   3129   MASGRLNALAPEATPQGHNLQVDIVYGVDYQASVF                               VQGAAFATGIPPDLYAFHRYTWNSTPLYETQACQYQ                               MQFPVIPINACTLRITAAGFSKKFRSFPWAYTMVRAP                               VFTTVNRRNPLRSRSGGVCGCFRKLTRKLAAKSALT                               NCCVPSTKSMHTGSTTLPDFFAGMSDDFTPPIFAGYC                               RDDSHELRFRLYALLLISDAIALGIEQKPDLILLGGDY                               VLFDMSLNFSAFSDVLSPLAECAPTFACFGNHDRPGR                               IAAASIGPLNNTVRKKASTRSSDSIQGVKRPQWRSQV                               HDRGNKPDAHQQPEEKHATDNTLTVCVIFGGEPANS                               ANNQRAYYALTQYGGYYTGSFQPGFQIRERIFPRTVS                               RCDLRTGSECTRCLRNLRNFGDEKDIELQETECAVIR                               ALVQVSHWQSTLAAAGQVLTIIVRTITVAFQHAADK                               AADNGNLTAISWIHVSSLFLQAMRVAIPAVIVALSVG                               TSEVQNMLNAIPEVVTNGLNIAGGMIVVVGYAMVIN                               MMRAGYLMPFFYLGFVTAAFTNFNLVALGVIGTVM                               AVLYIQLSPKYNRVAVRLLRQLVSEMVDTTQTTTEK                               KLTQSDIRGVFLRSNLFQGSWNFERMQALGFCFSMV                               PAIRRLYPENNEARKQAIRRHLEFFNTQPFVAAPILGV                               TLALEEQRANGAEIDDGAINGIKVGLMGPLAGVGDPI                               FWGTVRPVFAALGAGIAMSGSLLSPLLFFILFNLVRL                               ATRYYGVRLVVLDLGLPDEDGLHFLARIRQKKYTLP                               VLILTARDTLTDKIAGLDVGADDYLVKPFALEELHA                               RIRALLRRHNNQGESELIVGNLTLNMGRRQVWMGG                               EELILTPKEYALLSRLMLKAGSPVHREILYNDIYNWD                               NEPSTNTLEVHIHNLRDKVGKARIRTVRGPGYMLLIS                               VFWLWHESTEQIQLFEQALRDNRNNDRHIMREIREA                               VASLIVPGVFMVSLTLFICYQAVRRITRPLAELQKELE                               ARTADNLTPIAIHSATLEIEAVVSALNDLVSRLTSTLD                               NERLFTADVAHELRTPLAG               981   A   1   939   MVPDRPAYPDVYDQLRFWQAGSLDIRNLHTLKVVLI                               PGADRRSNCAITESRAEQFEPRQRHRDGAGQSRGAH                               TVDWSAGDYRALCATAIVGPIAFIGLMMPHMARWL                               VGADHRWSLPVTLLATPALLLFADIIGRVIVPGELRV                               SVVSAFIGAPVLIFLVRRKTRGIWGLRSGAVTLETSQ                               VFAALMGDAPRSMTMVVTEWRLPRVLMALLIGAAL                               GVSGAIFQSLMRNPLGSPDVMGFNTGAWSGVLVAM                               VLFGQDLTAIALSAMVGGIVTSLLVWLLAWRNGIDT                               FRLIIIGIGVRAMLVAFNTWLLLKAS               982   B   1   1941   MKLTTHHLRTGAALLLAGILLAGCDQSSSDAKHIKV                               GVINGAEQDVAEVAKKVAKEKYGLDVELVGFSGSL                               LPNDATNHGELDANVFQHRTFLEQDNQAHGYKLVA                               VGNTFVFPMADYGTRGGAVPRVLDDPKVDVAIISTT                               YIQQTGLSPVHDSVFIEDKNSPYVNILVAREDNKNAE                               NVQTKCQGRTNDHQIKKRQNQTAVNDKVCSLSGIK                               RQQNQTANQHTPADDWTCRHIKCLQVIIMRVVDIML                               ALQVCCWRWCWWQFSARRLINYRCISATKARRFRV                               VDRISYSVKQGEVVGIVGESGSVNQTSSPAFPPAPAR                               RRGTHPETRRNRQCVPELSSNKPTVSTSRETIATFTPP                               KRSGIQPNMTRITTNAPPNAISPTTLHSDGRSPARPVT                               LRTVPLQAHASTGNTIVVIASHVQNDRGSPVSYIAW                               MPAGPLVILLFFTIYCASGIVAGARLFESTFGMSYETA                               LWAGAAATILYTFIGGFLAVSWTDTVQASLMIFALIL                               TPVIVIISVGGFGDSLEVIKQKSIENVDMLKGLNFVAII                               SLMGWGLGYFGQPHILARFMAADSHHSIVHARRISM                               TWMILCLAGAVAVGFFGIAYPNDHPALAGAVNQNA                               ERVFIELAQILFNPWIAGILLSQFWRR               983   A   3   964   TISTVRWNSRIGMVLGVAIQKRAV\PGLY\SFEEAYAR                               ADKEAPRPCHKGSWCSSNQLCRECQAFMAHTMPKL                               KAFSMSSAYNAYRAVYAVAHGLHQLLGCASGACSR                               GRVYPWQLLEQIHKVHFLLHKDTVAFNDNRDPLSSY                               NILAWDWNGPKWTFTVLGSSTWSPVQLNINETKIQW                               HGKDNQVPKSVCSSDCLEGHQRVVTGFHHCCFECVP                               CGAGTFLNK/QCYLGKDLPENYNEAKCVTFSLLFNFV                               SWIAFFTTASVYDGKYLPAANMMAGLSSLSSGFGGY                               FLPKCYVILCRPDLNSTEHFQASIQDYTRRCGST               984   A   163   431   PTRNMATSAVPSDNLPTYKLVVVGDGGVFIIALNILS                               FQTILAPGYYPYMCNIYLLHTAMDNHMPFLDV\LDK                               PGPVEGTTIRYQYLRPG               985   A   398   553   ETGACIHCHCYWTPCQGHQRHHHHHHHQYHHHHH                               HHQCHHHQYYHHHHHHFH               986   C   123   359   MRLKKHRWYKKILKSQDPIIFSVGWRRFQTILLYYIE                               DHNGRQXASKXIPHSTCIVEQPFWAWIFRIAATRSLS                               LXLG               987   A   2   410   IEIHSQCGGIPHRKLGMAGQKLGSSALLCYIRPDTAD                               PASSFSLTVANVGTCQAVLCRGGKPVPLSKVFSLEQD                               PEEAQRVKDQKAIITEVPEDLKEFQTTDIPVHHCNFP                               AVLGCLCSASVLGSYAGPAPRWRRT               988   A   482   23   VASHGLGLLGLLLCSFGSECFQFTRIRWVFKRRLGLL                               GRTLEASASATTLLPVSWVAHATIQDFWDDSIPDIIPR                               WEFGGALYLGWAAGIFLALGGLLLIFSACLGKEDVP                               FPLMAGPTVPLSCAPVEESDGSFHLMLRPRNLEFLVT                               AYGLD               989   A   3   455   SWTLWRCCQRVVGWVPVLFITFVVVWSYYAYVVEL                               CVY*CGNQGH*FEPELSYYPWK*R/QMFYLSNSEKER                               YEKEFSQERQQEILRRAARALPIYTTSASKTIRYCEKC                               QLIKLPDRAHHCSACDSCILKMDHHCPWVNNCVG\FS                               NYKFFLL               990   A   93   320   VTPTPPQYYTCSCVLGFIACSIFLQMSLKPKVMLLTV                               ALVACLVFNLSQCWQRDCCSQGLGNLTEPSGTNR*                               GPA               991   A   2   445   EIDRKWYYDSYTCCPPPWFMITVTLLEVAFFLYNWV                               SLGQFVLQVTHPRYLKNSLVYHPQLRAQVWRYLTYI                               FMHAGIEHLGLNVVLQLLVGVPLEMVHGATRIGLVY                               MAGVVAGSLAVSVADMTAPVVGSSGGVYALVSAH                               LANIVM               992   A   3   457   VQRSIEDDGAERPS/PPGRSGASLVSGFPF*PLADSLLF                               SSSVERGTDSGDGHPQRPSLGFPGTS/GFSAALGRKS                               AHGPGLQAP\TGAPGG*YLPMPPGPCRILAGS*GGRA                               ASLSYSPGFPLSLALFCHWAARGGLRSSLQQRERPRA                               QTGV               993   A   27   437   RVDDIHCTAA*GRATPGSGTSLPGTLSSSPRRRCSSPS                               CSAPASAATRSRRAWSTCWRPSTAWPRSSATSLTAS                               SRPTAPSTVSTRTCRPPGATAGSSSPPSRKPTCWTSITP                               T*S*SCMLLSPRSRFQGLVLITRL               994   A   2   406   FLVETEFCYVGQAGLELLTSRDPPASASKGAGMTGV                               SHQVQPQ**S*LWT*/PSSVEAGTSFGLSFLSSSWALS                               AQEGCLAVPS/SGSRGLLVGALLLWTKPSPQLSPVPA                               SQRLSSLSLMPPLPQPQHLTHTSIET               995   A   1   439   GTRKPVYKPLVFVLLAVLVLSVTTQINYLNKALDT                               FNTSLVTPIYYVFFTSMVVTCSAILFQEWYGMTAGDI                               IGTLSGFFTIIIGIFLLHAEKNTDITWSELTSTAKKEAVS                               LNVNENNYVLLENLECSAPGYNDDVTLFSRTDD               996   A   756   1016   KLRPFIFSNQSLWLHSYEGAELEKTFIKGSWATFWVK                               VASCWACVLLYLGLLLAPLCWPPTQKPQPLILRRRR                               HRIISPDNKYPPV               997   A   1497   717   HTPMA/FFL/SFLSTSET/VYTFVILPKMLINLLSVARTI                               SFNCCALQMFFFLGFAITNCLLLGVMGYDRYAAICH                               PLHYPTLMSWQVCGKLAAACAIGGFLASLTVVNLVF                               SLPFCSTNKVNHYFCDISAVILLACTNTDVNGFVIFIC                               GVLVLVVPFLFICVSYFCILRTILKIPSAEGRRKAPSTC                               ASHLSVVIVHYGCASFIYLRPTANYVSNKDRLVTVTY                               TIVTPLLNPMVYSLRNKDVQLAIRKVLGKKGSLKLY                               N               998   B   1   975   MSPPGREQGLLLNLLRPSGLDNAGKTTILKKFNGEDI                               DTISPTLGFNIKTLEHRGFKLNIWDVGGQKSLRSYWR                               NYFESTDGLIWVVDSADRQRMQDCQRELQSLLVEEV                               GSSYPLCTWRFFSYLRIEQMYNLVLYRDIQFPDFCFN                               SNTDWSKGLKTHARFGNTSLHVAHTDSTNTTNFVD                               VWRGRTKSLACLLQLSSLTCIYTAGKMRLQDRIATFF                               FPKGMMLTTAALMLFFLHLGIFIRDVHNFCITYHYDH                               MSFHYTVVLMFSQVISICWAAMGSLYAEMTENKYV                               CFSALTILMLNGAMFFNRLSLEFLAIEYREEHH                    
     [0408]                               TABLE 9                                       Number of   Position of               Transmembrane   Transmembrane               Regions   Region;           SEQ ID NO:   Predicted   TMPred Score                                                        338   1   184-201; 807           340   2   21-46; 1142                   54-70; 3147           341   1   297-319; 2854           343   1   14-34; 1660           346   1   20-47; 3001           347   1   9-31; 2958           348   1   28-44; 2183           349   1   41-59; 2412           350   2   34-53; 1125                   67-84; 2061           353   2   34-51; 1665                   133-151; 1190           354   1   20-39; 1830           355   1   75-92; 1800           356   1   48-63; 2723           357   3   28-43; 1680                   58-73; 1675                   90-105; 1928           359   1   53-68; 3633           360   1   142-159; 2140           362   1   69-87; 2593           363   1   17-35; 2291           365   3   16-37; 895                   52-69; 1796                   100-120; 1617           366   1   22-37; 2183           369   2   238-257; 908                   396-412; 1281           371   1   27-42; 2043           372   3   52-75; 2018                   325-346; 865                   375-392; 839           373   1   353-370; 2096           374   1   25-45; 2047           375   1   24-47; 2800           376   2   71-86; 1595                   102-121; 2779           377   10   25-41; 1489                   54-72; 2563                   87-103; 1436                   116-134; 2525                   149-165; 1474                   178-196; 2516                   211-227; 1420                   240-258; 2456                   273-289; 1392                   302-320; 2395           378   2   22-48; 2007                   141-164; 1410           379   2   21-41; 1941                   102-117; 3056           380   8   29-44; 1389                   61-74; 917                   88-103; 1267                   115-129; 890                   179-193; 898                   204-221; 1978                   220-238; 1076                   259-275; 1735           381   1   26-43; 1767           383   2   36-51; 2233                   100-113; 2408           384   2   40-56; 1175                   69-85; 1803           387   1   35-53; 2023           389   4   17-32; 2238                   39-60; 1679                   79-95; 2605                   114-129; 1098           391   1   23-42; 2878           392   2   36-58; 1952                   189-210; 874           395   4   25-48; 2108                   276-291; 1253                   334-351; 1063                   399-416; 1680           396   4   22-37; 2458                   45-60; 1250                   82-98; 1641                   159-176; 933           397   1   12-38; 1749           402   1   43-59; 2213           403   1   13-34; 2984           405   6   25-41; 1898                   103-119; 1328                   131-148; 2506                   180-203; 1533                   205-228; 1303                   245-260; 1634           406   1   30-49; 2416           407   1   32-50; 1597           408   1   284-299; 1055           409   1   124-141; 2071           411   1   92-108; 1857           413   1   28-44; 2543           415   2   43-58; 1396                   60-75; 2059           416   3   5-35; 1780                   59-73; 1361                   80-103; 1826           417   5   16-32; 1576                   72-87; 1083                   104-121; 1825                   145-160; 1294                   227-247; 1337           419   1   39-53; 1731           420   1   245-258; 1771           421   1   58-81; 2868           422   1   16-33; 1894           423   1   290-310; 2684           425   2   264-282; 1757                   383-403; 1000           427   2   18-33; 892                   108-126; 1867           428   1   37-56; 2054           429   1   369-387; 2530           430   2   14-34; 1939                   187-208; 1365           431   2   43-58; 1060                   155-170; 2602           432   4   24-45; 2509                   98-119; 2954                   129-147; 1343                   183-201; 2141           433   1   142-157; 1775           434   1   33-49; 2264           435   1   43-57; 1794           437   1   15-38; 1948           438   2   20-34; 1518                   82-98; 1908           439   1   64-80; 1560           440   1   24-40; 2347           441   1   14-32; 2720           442   1   23-44; 1807           443   2   15-31; 1300                   118-140; 3012           444   4   95-111; 2524                   104-139; 1338                   125-147; 2138                   174-209; 1036           445   2   6-38; 1711                   49-67; 1103           446   2   15-31; 3431                   69-86; 889           447   3   13-32; 2547                   95-110; 1692                   112-132; 1903           451   3   41-57; 1768                   82-97; 2647                   122-136; 968           452   1   250-265; 1867           453   3   46-62; 911                   68-84; 1367                   154-166; 1297           454   2   32-51; 2342                   114-130; 1188           455   1   23-39; 2309           457   2   85-114; 2984                   221-238; 959           458   2   35-50; 1595                   66-85; 2779           459   2   17-32; 1331                   57-71; 1728           460   3   14-31; 1963                   40-58; 1009                   66-86; 1248           461   1   226-242; 2202           462   2   46-61; 832                   73-90; 2191           463   1   34-56; 1058           464   1   154-172; 2074           465   3   34-49; 1210                   66-99; 1252                   97-113; 2355           466   1   18-33; 1975           467   4   158-174; 1945                   199-216; 1112                   225-242; 1673                   254-271; 946           468   1   15-33; 1775           469   1   181-199; 1868           470   5   38-54; 1712                   67-94; 2110                   114-128; 918                   240-256; 855                   277-292; 1359           471   2   50-74; 2625                   130-149; 1166           472   4   16-38; 1473                   43-59; 1371                   77-94; 1851                   199-214; 1092           473   1   46-62; 3051           474   1   17-34; 2743           475   1   95-118; 3033           476   1   213-230; 985           477   1   8-31; 3667           478   1   83-101; 2361           479   3   47-62; 1204                   51-79; 1625                   96-109; 1118           481   4   13-35; 1282                   58-73; 2648                   91-107; 1319                   148-165; 1783           482   4   41-56; 1354                   62-78; 1639                   88-103; 977                   134-150; 1946           483   2   25-46; 2369                   66-81; 1705           484   5   20-43; 823                   51-73; 1163                   87-106; 1827                   105-125; 1017                   153-186; 1554           486   1   74-89; 3414           487   1   31-57; 2521           488   3   27-46; 2157                   130-160; 1822                   236-250; 888           490   10   28-44; 2267                   50-76; 1625                   68-88; 2769                   93-113; 1629                   118-138; 2697                   153-168; 1629                   178-194; 2313                   203-238; 1733                   244-263; 2730                   269-284; 1367           491   1   40-67; 1986           494   3   23-40; 2163                   266-285; 985                   291-304; 1229           495   3   18-34; 2249                   256-272; 1362                   280-299; 1671           496   1   21-39; 2045           497   4   21-37; 2440                   57-74; 1286                   84-112; 1585                   122-143; 1004           498   2   48-63; 1829                   197-216; 1112           501   1   29-48; 1619           503   2   16-32; 1602                   191-205; 890           504   3   44-60; 2409                   103-123; 941                   165-185; 2002           506   3   19-35; 2153                   38-53; 1100                   78-97; 1064           507   2   57-72; 2060                   93-110; 939           508   8   23-47; 1290                   60-80; 1779                   87-106; 1447                   159-187; 2236                   202-216; 1085                   234-249; 981                   270-299; 1491                   324-338; 1352           509   1   21-39; 2481           510   2   27-52; 1562                   66-84; 864           511   2   15-31; 1529                   41-56; 2722           512   1   21-36; 2544           513   2   16-34; 1960                   40-55; 951           514   1   174-191; 1728           515   1   16-32; 827           516   1   45-66; 1964           517   3   17-40; 2165                   71-83; 1112                   116-143; 1198           518   1   23-39; 3165           519   1   42-59; 859           521   5   75-90; 1359                   107-122; 1520                   135-151; 1967                   175-191; 1416                   236-251; 2332           522   1   14-32; 2317           526   2   214-236; 1046                   282-294; 966           527   6   125-141; 2144                   157-173; 1116                   185-204; 1756                   223-238; 926                   243-259; 1271                   273-288; 1225           528   2   38-55; 1680                   151-168; 2550           529   2   30-51; 2155                   161-176; 905           530   6   36-50; 2210                   58-74; 1644                   126-141; 914                   152-173; 1406                   187-202; 2224                   221-236; 1055           531   5   49-70; 1075                   88-104; 1052                   123-140; 1710                   157-175; 2590                   191-204; 1390           532   2   25-45; 1365                   64-84; 1812           534   2   46-59; 1059                   186-206; 1046           535   1   97-112; 1026           536   1   26-41; 1887           537   3   82-102; 1765                   119-134; 1405                   167-183; 2521           538   4   15-45; 1726                   42-67; 2522                   207-229; 861                   274-291; 922           539   1   13-31; 2843           540   3   23-38; 1889                   50-66; 831                   121-137; 1096           541   3   19-35; 1356                   72-87; 1830                   105-120; 1373           543   2   22-48; 1148                   384-399; 2339           545   1   36-51; 2076           546   6   83-100; 2781                   111-133; 1847                   157-173; 2151                   175-191; 1172                   236-251; 3053                   307-322; 1307           547   1   14-34; 2733           548   1   31-50; 2047           549   1   118-137; 812           551   1   234-248; 948           552   1   7-41; 2396           554   1   18-33; 1771           555   1   15-39; 2946           557   1   36-51; 1750           558   3   30-58; 2255                   69-85; 1303                   102-116; 965           559   7   5-33; 2407                   48-62; 834                   82-101; 1768                   116-136; 1635                   165-185; 2884                   226-247; 1338                   263-282; 1779           561   1   26-47; 2958           562   1   43-58; 2185           563   1   51-66; 896           564   1   20-39; 1851           565   1   30-48; 2719           566   2   50-67; 1746                   105-120; 1144           567   1   108-123; 1623           568   1   34-48; 2268           569   2   14-38; 2868                   281-297; 941           571   1   217-239; 1272           572   1   146-168; 2684           573   2   90-107; 1944                   363-377; 1338           574   3   64-81; 2157                   84-100; 1243                   97-133; 1672           575   1   48-72; 2661           576   3   2-38; 971                   22-46; 1497                   84-99; 1261           577   2   34-61; 2058                   93-108; 1716           578   2   40-59; 1918                   234-249; 859           579   1   24-45; 2330           581   1   296-313; 812           582   1   21-44; 2763           583   1   21-36; 2617           584   1   26-51; 825           586   4   34-55; 2354                   150-169; 1592                   311-333; 1867                   353-375; 892           587   5   59-80; 1228                   88-107; 866                   157-176; 3161                   198-216; 1250                   223-238; 2194           588   1   195-210; 1193           589   1   19-35; 2865           590   1   69-98; 822           591   3   18-33; 2344                   94-115; 1093                   232-249; 1415           592   1   14-31; 2117           593   1   166-182; 2113           597   1   11-31; 871           599   1   31-53; 2985           601   1   20-44; 2459           602   1   20-37; 2284           603   1   22-42; 3116           604   1   46-62; 2496           606   1   19-33; 1834           607   2   41-71; 1782                   65-86; 3101           608   3   19-34; 1101                   46-62; 1928                   185-201; 1841           609   1   17-39; 1978           610   1   364-379; 1065           612   1   22-40; 1765           614   1   38-53; 1788           615   1   14-32; 2099           616   2   32-52; 1769                   77-102; 2317           617   4   153-175; 2138                   189-204; 1068                   261-283; 2271                   290-306; 1112           618   1   1-34; 1975           619   1   10-38; 1023           620   1   15-31; 1522           621   1   74-91; 2543           622   5   49-64; 1187                   82-96; 1485                   119-140; 1408                   129-153; 2110                   206-222; 2257           623   1   66-83; 2200           626   2   75-94; 924                   180-195; 1494           627   5   43-67; 2282                   70-91; 1282                   121-137; 2440                   169-183; 1439                   197-232; 1120           628   3   14-34; 1791                   83-97; 1381                   115-144; 1592           629   4   43-62; 1533                   195-216; 2160                   222-237; 1314                   257-270; 1867           630   2   13-31; 1516                   69-88; 2277           631   5   25-42; 1555                   74-89; 1237                   114-142; 2195                   154-169; 1023                   185-200; 2114           632   3   24-47; 1711                   61-79; 2020                   192-207; 2454           633   2   36-56; 1076                   90-110; 1216           634   1   16-33; 2206           635   2   17-36; 2654                   64-76; 932           636   1   19-34; 1366           637   1   28-46; 2247           638   2   23-43; 1069                   58-75; 1756           639   4   21-39; 1494                   81-97; 1518                   125-143; 1312                   148-169; 2440           640   10   7-32; 2014                   82-96; 1124                   107-123; 1475                   148-167; 1298                   170-193; 1565                   258-273; 1090                   296-316; 1839                   324-345; 1356                   354-369; 1159                   420-437; 1669           641   2   44-60; 963                   75-90; 3007           642   4   29-44; 1865                   76-93; 1315                   119-138; 1894                   155-176; 1330           643   1   42-69; 2215           644   2   36-55; 2620                   41-76; 845           645   1   3-35; 3176           646   1   56-73; 3062           648   3   45-61; 2010                   110-125; 1024                   175-193; 839           649   1   18-39; 2254           650   3   55-76; 2276                   89-112; 1167                   148-168; 2134           651   1   16-36; 2701           652   2   82-107; 1813                   168-186; 2844           653   1   17-35; 2449           654   1   36-53; 2305           655   1   29-45; 2349           656   1   26-43; 2340           657   2   50-68; 1787                   82-94; 808           658   2   41-55; 1214                   76-91; 2379           659   1   120-139; 1924           660   2   25-41; 2077                   208-223; 986           661   2   25-45; 1955                   167-181; 1187           662   3   47-62; 2783                   76-92; 1090                   115-130; 2791           664   1   58-85; 1106           665   4   33-48; 1166                   71-88; 2044                   108-123; 1229                   134-154; 2709           667   1   79-94; 1909           668   6   16-33; 2461                   94-113; 2485                   137-152; 1212                   190-212; 3236                   237-253; 971                   266-285; 1138           670   2   48-66; 1420                   56-86; 2350           671   1   14-32; 2650           672   2   23-42; 2154                   134-155; 1123           673   3   16-34; 1811                   55-70; 1301                   82-99; 1627           674   1   43-58; 890                        
     [0409]                               TABLE 10                       SEQ ID   SEQ ID   SEQ ID   SEQ ID   Identification of Priority       NO: of   NO: of   NO: of   NO:   Application that contig       full-length   full-length   contig   of contig   nucleotide sequence was       nucleotide   peptide   nucleotide   peptide   filed (Attorney Docket       sequence   sequence   sequence   sequence   No._SEQ ID NO.)*                                                    1   338                   2   339       3   340   675   837   787_7102       4   341       5   342   676   838   790_16366       6   343   677   839   784_3345       7   344       8   345       9   346       10   347   678   840   788_13033       11   348       12   349       13   350       14   351       15   352   679   841   790_28890       16   353       17   354       18   355       19   356       20   357   680   842   790_24599       21   358   681   843   784_3534       22   359   682   844   790_9494       23   360       24   361   683   845   785_3560       25   362   684   846   787_2054       26   363       27   364   685   847   784_4307       28   365   686   848   787_2905       29   366       30   367   687   849   784_8386       31   368   688   850   790_17736       32   369   689   851   784_5156       33   370   690   852   787_2104       34   371       35   372   691   853   790_935       36   373       37   374       38   375   692   854   787_3283       39   376   693   855   787_7951       40   377   694   856   784_2168       41   378       42   379   695   857   784_9629       43   380       44   381       45   382       46   383   696   858   785_14       47   384   697   859   790_7599       48   385   698   860   787_4843       49   386   699   861   790_2819       50   387   700   862   790_8044       51   388       52   389   701   863   784_337       53   390   702   864   785_706       54   391   703   865   787_9834       55   392       56   393       57   394   704   866   787_3554       58   395   705   867   790_8276       59   396       60   397   706   868   790_18037       61   398       62   399   707   869   784_7084       63   400       64   401       65   402   708   870   790_3034       66   403   709   871   785_1867       67   404       68   405   710   872   790_3651       69   406   711   873   790_22283       70   407   712   874   785_1538       71   408   713   875   784_5140       72   409   714   876   790_14249       73   410       74   411       75   412       76   413   715   877   787_5698       77   414   716   878   790_29400       78   415       79   416   717   879   784_4813       80   417   718   880   784_9771       81   418   719   881   790_10961       82   419   720   882   790_11763       83   420       84   421   721   883   790_9831       85   422       86   423   722   884   790_16986       87   424   723   885   785_3654       88   425   724   886   785_102       89   426   725   887   784_4307       90   427       91   428       92   429       93   430   726   888   787_6896       94   431   727   889   789_3174       95   432       96   433       97   434       98   435       99   436       100   437       101   438       102   439   728   890   784_3746       103   440       104   441   729   891   785_2855       105   442       106   443       107   444   730   892   785_1465       108   445   731   893   784_1644       109   446   732   894   789_5053       110   447   733   895   787_1411       111   448   734   896   787_5936       112   449       113   450   735   897   784_2486       114   451   736   898   790_28311       115   452       116   453       117   454       118   455       119   456   737   899   784_3665       120   457       121   458   738   900   787_7951       122   459       123   460       124   461   739   901   787_4539       125   462   740   902   790_26713       126   463   741   903   790_10585       127   464       128   465   742   904   785_1092       129   466       130   467   743   905   790_17470       131   468       132   469   744   906   784_844       133   470   745   907   787_9644       134   471   746   908   789_1867       135   472   747   909   785_612       136   473       137   474   748   910   785_852       138   475   749   911   787_7533       139   476       140   477   750   912   785_2515       141   478   751   913   784_715       142   479   752   914   785_631       143   480   753   915   784_3853       144   481   754   916   790_10815       145   482   755   917   790_25607       146   483   756   918   790_10374       147   484   757   919   790_10504       148   485   758   920   790_21640       149   486   759   921   790_18317       150   487       151   488   760   922   785_640       152   489       153   490   761   923   787_5233       154   491   762   924   788_2575       155   492   763   925   790_22555       156   493   764   926   790_18977       157   494       158   495   765   927   792_4675       159   496   766   928   784_2550       160   497   767   929   787_7445       161   498       162   499   768   930   787_5416       163   500   769   931   784_4167       164   501   770   932   784_4677       165   502       166   503   771   933   784_10126       167   504       168   505       169   506       170   507       171   508       172   509       173   510   772   934   790_19568       174   511       175   512   773   935   791_3005       176   513       177   514       178   515       179   516       180   517       181   518   774   936   790_1155       182   519   775   937   790_10740       183   520       184   521       185   522       186   523       187   524       188   525       189   526   776   938   790_8077       190   527       191   528   777   939   784_929       192   529       193   530       194   531   778   940   787_5943       195   532       196   533   779   941   787_2691       197   534   780   942   785_3660       198   535       199   536       200   537       201   538       202   539       203   540       204   541   781   943   788_2020       205   542       206   543   782   944   787_4919       207   544       208   545       209   546       210   547   783   945   784_4970       211   548       212   549       213   550   784   946   784_4845       214   551       215   552       216   553   785   947   785_1670       217   554       218   555       219   556       220   557   786   948   787_4525       221   558   787   949   792_4456       222   559       223   560       224   561       225   562       226   563       227   564   788   950   790_16768       228   565   789   951   788_11952       229   566       230   567   790   952   787_2489       231   568       232   569       233   570   791   953   792_3487       234   571       235   572   792   954   785_395       236   573       237   574       238   575       239   576       240   577   793   955   790_10170       241   578   794   956   785_1618       242   579       243   580       244   581       245   582   795   957   787_4486       246   583   796   958   787_4256       247   584       248   585       249   586   797   959   784_5437       250   587       251   588   798   960   787_2155       252   589   799   961   790_15300       253   590       254   591       255   592       256   593       257   594   800   962   790_11358       258   595       259   596       260   597       261   598       262   599   801   963   790_3760       263   600   802   964   784_4787       264   601       265   602   803   965   787_4483       266   603       267   604   804   966   785_598       268   605       269   606   805   967   791_2994       270   607       271   608   806   968   790_11947       272   609       273   610   807   969   787_6368       274   611   808   970   790_21374       275   612       276   613   809   971   790_26925       277   614   810   972   788_8317       278   615   811   973   784_5609       279   616       280   617   812   974   790_4252       281   618   813   975   784_3437       282   619       283   620       284   621   814   976   790_11072       285   622   815   977   784_1021       286   623   816   978   790_16269       287   624       288   625       289   626       290   627       291   628   817   979   790_16011       292   629       293   630   818   980   790_28920       294   631   819   981   790_17932       295   632   820   982   790_25383       296   633       297   634       298   635       299   636       300   637       301   638       302   639       303   640       304   641       305   642   821   983   784_3789       306   643   822   984   787_4340       307   644       308   645   823   985   790_17189       309   646       310   647       311   648   824   986   790_20324       312   649       313   650   825   987   784_2129       314   651       315   652   826   988   787_5627       316   653       317   654       318   655   827   989   787_614       319   656   828   990   784_1483       320   657   829   991   787_2548       321   658       322   659   830   992   789_3213       323   660   831   993   789_4901       324   661       325   662       326   663       327   664   832   994   788_1187       328   665   833   995   784_4265       329   666       330   667   834   996   784_4819       331   668   835   997   784_3677       332   669       333   670       334   671       335   672       336   673   836   998   790_21539       337   674                       # Docket No. 784CIP3A/PCT, PCT Ser. No. PCT/US00/35017 filed Dec. 22, 2000, both of which are incorporated herein by reference in their entirety, including Tables, and Sequence Listing.                        # Docket No. 787CIP3/PCT, PCT Ser. No. PCT/US01/03800 filed Feb. 5, 2001, both of which are incorporated herein by reference in their entirety, including Tables, and Sequence Listing.                # Docket No. 788CIP3/PCT, PCT Ser. No. PCT/US01/04927 filed Feb. 26, 2001, both of which are incorporated herein by reference in their entirety, including Tables, and Sequence Listing.                # Docket No. 789CIP3/PCT, PCT Ser. No. PCT/US01/04941 filed Mar. 5, 2001, both of which are incorporated herein by reference in their entirety, including Tables, and Sequence Listing.                # Docket No. 790CIP3/PCT, PCT Ser. No. PCT/US01/08631 filed Mar. 30, 2001, both of which are incorporated herein by reference in their entirety, including Tables, and Sequence Listing.                # Docket No. 791CIP3/PCT, PCT Ser. No. PCT/US01/8656 filed Apr. 18, 2001, both of which are incorporated herein by reference in their entirety, including Tables, and Sequence Listing.