Novel nucleic acids and secreted polypeptides

Abstract

The present invention provides novel nucleic acids, novel polypeptide sequences encoded by these nucleic acids and uses thereof.

Description

2. BACKGROUND OF THE INVENTION

[0002] 2.1 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] 2.2 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.

3. 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: 1-244, or 489-706 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: 1-244, or 489-706 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: 1-244, or 489-706. A polynucleotide comprising a nucleotide sequence having at least 90% identity to an identifying sequence of SEQ ID NO: 1-244, or 489-706 or a degenerate variant or fragment thereof. The identitying 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: 1-244, or 489-706. The sequence information can be a segment of any one of SEQ ID NO: 1-244, or 489-706 that uniquely identifies or represents the sequence information of SEQ ID NO: 1-244, or 489-706.

[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: 1-244, or 489-706 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: 1-244, or 489-706 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 Voltrath 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: 1-244, or 489-706; a polynucleotide comprising any of the full length protein coding sequences of SEQ ID NO: 1-244, or 489-706; and a polynucleotide comprising any of the nucleotide sequences of the mature protein coding sequences of SEQ ID NO: 1-244, or 489-706. 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: 1-244, or 489-706; (b) a nucleotide sequence encoding any one of the amino acid sequences set forth in SEQ ID NO: 1-244, or 489-706; (c) a polynucleotide which is an allelic variant of any polynucleotides recited above; (d) a polynucleotide which encodes a species homolog (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 the Sequence Listing.

[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: 1-244, or 489-706; 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 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.

[0017] The invention also provides host cells transformed or transfected with a polynucleotide of the invention.

[0018] 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.

[0019] 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.

[0020] 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 Volirath et al., Science 258:52-59 (1992), as expressed sequence tags for physical mapping of the human genome.

[0021] 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.

[0022] 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.

[0023] 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.

[0024] 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.

[0025] 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.

[0026] 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.

[0027] 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.

[0029] Compounds and other substances can affect such modulation either on the level of target gene/protein expression or target protein activity.

[0030] 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.

4. DETAILED DESCRIPTION OF THE INVENTION

[0031] 4.1 Definitions

[0032] 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.

[0033] 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.

[0034] 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.

[0035] The terms “complementary” or “complementarity” 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′. Complementarity 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.

[0036] 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 (GS Cs)” 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.

[0037] The term “expression modulating fragment,” EMF, means a series of nucleotides which modulates the expression of an operably linked ORF or another EMF.

[0038] 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.

[0039] 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.

[0040] 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: 1-244, or 489-706.

[0041] 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 & Sons, New York N.Y., both of which are incorporated herein by reference in their entirety.

[0042] The nucleic acid sequences of the present invention also include the sequence information from the nucleic acid sequences of SEQ ID NO: 1-244, or 489-706. The sequence information can be a segment of any one of SEQ ID NO: 1-244, or 489-706 that uniquely identifies or represents the sequence information of that sequence of SEQ ID NO: 1-244, or 489-706, or those segments identified in Tables 3, 5, 6, and 8. 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 420 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.

[0043] 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 (1425) 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.

[0044] 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.

[0045] 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.

[0046] 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.

[0047] 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.

[0048] 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.

[0049] 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.

[0050] 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.

[0051] 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.

[0052] 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.

[0053] 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.

[0054] 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, tryptophan, 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.

[0055] 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.

[0056] 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).

[0057] 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.

[0058] 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.

[0059] 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.

[0060] 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.

[0061] The term “recombinant expression system” means host cells which have stably integrated a recombinant transcriptional unit into chromosomal DNA or carry 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.

[0062] 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)

[0063] 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.

[0064] 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 NaHPO4, 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.

[0065] 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).

[0066] 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 15 known in the art, e.g. by varying hybridization conditions.

[0067] The term “totipotent” refers to the capability of a cell to differentiate into all of the cell types of an adult organism.

[0068] 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.

[0069] 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.

[0070] Each of the above terms is meant to encompass all that is described for each, unless the context dictates otherwise.

[0071] 4.2 Nucleic Acids of the Invention

[0072] Nucleotide sequences of the invention are set forth in the Sequence Listing.

[0073] The isolated polynucleotides of the invention include a polynucleotide comprising the nucleotide sequences of SEQ ID NO: 1-244, or 489-706; a polynucleotide encoding any one of the peptide sequences of SEQ ID NO: 1-244, or 489-706; and a polynucleotide comprising the nucleotide sequence encoding the mature protein coding sequence of the polynucleotides of any one of SEQ ID NO: 1-244, or 489-706. 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: 1-244, or 489-706; (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 homolog 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: 1-244, or 489-706 (for example, as set forth in Tables 3, 5, 6, or 8). 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.

[0074] 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.

[0075] 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: 1-244, or 489-706 can be obtained by screening appropriate cDNA or genomic DNA libraries under suitable hybridization conditions using any of the polynucleotides of SEQ ID NO: 1-244, or 489-706 or a portion thereof as a probe.

[0076] Alternatively, the polynucleotides of SEQ ID NO: 1-244, or 489-706 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.

[0077] 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, gbpi, and UniGene. The EST sequences can provide identifying sequence information, representative fragment or segment information, or novel segment information for the full-length gene.

[0078] 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.

[0079] 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: 1-244, or 489-706, 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.

[0080] 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: 1-244, or 489-706, a representative fragment thereof, or a nucleotide sequence at least 90% identical, preferably 95% identical, to SEQ ID NO: 1-244, or 489-706 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.

[0081] The nearest neighbor or homology results for the nucleic acids of the present invention, including SEQ ID NO: 1-244, or 489-706 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.

[0082] 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.

[0083] 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.

[0084] 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.

[0085] 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.

[0086] 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.

[0087] 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.

[0088] 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.

[0089] In accordance with the invention, polynucleotide sequences comprising the mature protein coding sequences corresponding to any one of SEQ ID NO: 1-244, or 489-706, 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.

[0090] 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.

[0091] The present invention further provides recombinant constructs comprising a nucleic acid having any of the nucleotide sequences of SEQ ID NO: 1-244, or 489-706 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: 1-244, or 489-706 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).

[0092] 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.

[0093] 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 lac, 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 glycolytic 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.

[0094] 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.

[0095] 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 intramuscular 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.

[0096] 4.3 Antisense

[0097] 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: 1-244, or 489-706, 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: 1-244, or 489-706 or antisense nucleic acids complementary to a nucleic acid sequence of SEQ ID NO: 1-244, or 489-706 are additionally provided.

[0098] 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).

[0099] Given the coding strand sequences encoding a nucleic acid disclosed herein (e.g., SEQ ID NO: 1-244, or 489-706, 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.

[0100] 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-N-6-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).

[0101] 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 systemic 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.

[0102] 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 Left 215: 327-330).

[0103] 4.4 Ribozymes and PNA Moieties

[0104] 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: 1-244, or 489-706). 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.

[0105] 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.

[0106] 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'Keefe et al. (1996) PNAS 93: 14670-675.

[0107] 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 imodulation 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'Keefe (1996), above).

[0108] 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-thyrnidine 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.

[0109] 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. WO88/09810) or the blood-brain barrier (see, e.g., PCT Publication No. WO89/10134). 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 hybridization-triggered cleavage agent, etc.

[0110] 4.5 Hosts

[0111] 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.

[0112] 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.

[0113] 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.

[0114] 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.

[0115] 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, 3 T3 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, 1HL-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.

[0116] 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 Saccharomyces cerevisiae, Schizosaccharomyces pombe, Kluyveromyces 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.

[0117] 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'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.

[0118] 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.

[0119] 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.

[0120] 4.6 Polypeptides of the Invention

[0121] 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: 245-488, or 707-924 or an amino acid sequence encoded by any one of the nucleotide sequences SEQ ID NO: 1-244, or 489-706 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: 1-244, or 489-706 or (b) polynucleotides encoding any one of the amino acid sequences set forth as SEQ ID NO: 245-488, or 707-924 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: 245-488, or 707-924 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: 245-488, or 707-924.

[0122] 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, and 8. 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.

[0123] 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.

[0124] Protein compositions of the present invention may further comprise an acceptable carrier, such as a hydrophilic, e.g., pharmaceutically acceptable, carrier. 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.

[0125] 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.

[0126] 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.

[0127] 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 fill length or mature form of the protein.

[0128] 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, BPLC, 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.

[0129] 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.

[0130] 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: 245-488, or 707-924.

[0131] 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.

[0132] 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.

[0133] 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.

[0134] 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.

[0135] 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.

[0136] 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.).

[0137] Finally, one or more reverse-phase high performance liquid chromatography (RP-HPLC) steps employing hydrophobic RP-BPLC 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.”

[0138] 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.

[0139] 4.6.1 Determining Polypeptide and Polynucleotide Identity and Similarity

[0140] 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 at, 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), 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.expasy.ch/sprot). Predictions are based upon the maximum likelihood estimation.

[0141] 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).

[0142] 4.7 Chimeric and Fusion Proteins

[0143] The invention also provides chimeric or fission 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.

[0144] 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.

[0145] 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.

[0146] 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.

[0147] 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 & 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.

[0148] 4.8 Gene Therapy

[0149] 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.

[0150] 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.

[0151] 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.

[0152] 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.

[0153] 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'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.

[0154] 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.

[0155] 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,

[0156] 4.9 Transgenic Animals

[0157] 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 nonhuman 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. 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.

[0158] 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.

[0159] 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.

[0160] 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.

[0161] 4.10 Uses and Biological Activity

[0162] 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.

[0163] The polypeptides of the present invention may likewise be involved in cellular activation or in one of the other physiological pathways described herein.

[0164] 4.10.1 Research Uses and Utilities

[0165] 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.

[0166] 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.

[0167] Any or all of these research utilities are capable of being developed into reagent grade or kit format for commercialization as research products.

[0168] 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. Kimmeleds., 1987.

[0169] 4.10.2 Nutritional Uses

[0170] 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.

[0171] 4.10.3 Cytokine and Cell Proliferation/Differentiation Activity

[0172] 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, DAI, 123, T1165, HT2, CTLL2, TF-1, Mo7e, CMK, HUVEC, and Caco. Therapeutic compositions of the invention can be used in the following:

[0173] 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.

[0174] 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 edsi 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.

[0175] 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.

[0176] 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.

[0177] 4.10.4 Stem Cell Growth Factor Activity

[0178] 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's, Alzheimer'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.

[0179] 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 L-6 receptor fused to IL-6, macrophage inflammatory protein I-alpha-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).

[0180] 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).

[0181] 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.

[0182] 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.

[0183] 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): 21-6-224, (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.

[0184] 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).

[0185] 4.10.5 Hematopoiesis Regulating Activity

[0186] 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 in-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.

[0187] Therapeutic compositions of the invention can be used in the following:

[0188] Suitable assays for proliferation and differentiation of various hematopoietic lines are cited above.

[0189] 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.

[0190] Assays for stem cell survival and differentiation (which will identify, among others, proteins that regulate lympho-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 Celts. 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.

[0191] 4.10.6 Tissue Growth Activity

[0192] 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 burns, incisions and ulcers.

[0193] 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.

[0194] 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.

[0195] 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 ligament defects. The compositions may also include an appropriate matrix and/or sequestering agent as a carrier as is well known in the art.

[0196] 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's, Parkinson's disease, Huntington'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.

[0197] 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.

[0198] 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.

[0199] 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.

[0200] 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.

[0201] Therapeutic compositions of the invention can be used in the following:

[0202] 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).

[0203] 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).

[0204] 4.10.7 Immune Stimulating or Suppressing Activity

[0205] 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.

[0206] 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).

[0207] 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.

[0208] 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.

[0209] 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 CTLA41 g 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.

[0210] 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-derived 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).

[0211] 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.

[0212] 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.

[0213] 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 II 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 P2 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.

[0214] The activity of a protein of the invention may, among other means, be measured by the following methods:

[0215] 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., 1. 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.

[0216] 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.

[0217] 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.

[0218] 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.

[0219] 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;

[0220] 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.

[0221] 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.

[0222] 4.10.8 Activin/Inhibin Activity

[0223] 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.

[0224] The activity of a polypeptide of the invention may, among other means, be measured by the following methods.

[0225] 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.

[0226] 4.10.9 Chemotactic/Chemokinetic Activity

[0227] 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.

[0228] 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.

[0229] Therapeutic compositions of the invention can be used in the following:

[0230] 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.

[0231] 4.10.10 Hemostatic and Thrombolytic Activity

[0232] 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).

[0233] Therapeutic compositions of the invention can be used in the following:

[0234] 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.

[0235] 4.10.11 Cancer Diagnosis and Therapy

[0236] 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.

[0237] 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's sarcoma.

[0238] 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.

[0239] 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,

[0240] Doxorubicin HCl, Estramustine phosphate sodium, Etoposide (VI 6-213), Floxuridine, 5-Fluorouracil (5-Fu), Flutamide, Hydroxyurea (hydroxycarbamide), Ifosfamide, Interferon Alpha-2a, Interferon Alpha-2b, Leuprolide acetate (LBRH-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, Vincristine sulfate, Amsacrine, Azacitidine, Hexamethylmelamine, Interleukin-2, Mitoguazone, Pentostatin, Semustine, Teniposide, and Vindesine sulfate.

[0241] 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.

[0242] 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.

[0243] 4.10.12 Receptor/Ligand Activity

[0244] 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.

[0245] The activity of a polypeptide of the invention may, among other means, be measured by the following methods:

[0246] Suitable assays for receptor-ligand activity 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 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.

[0247] 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.

[0248] 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, colorimetric 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 calorimetric molecules include, but are not limited to, fluorescent molecules such as fluorescamine, or rhodamine or other colorimetric molecules. Examples of toxins include, but are not limited, to ricin.

[0249] 4.10.13 Drug Screening

[0250] 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.

[0251] 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.

[0252] 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.

[0253] 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.

[0254] 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 polyketides, non-ribosomal peptides, and (non-naturally occurring) variants thereof For a review, see Science 282:63-68 (1998).

[0255] 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); Dormer et al., Bioorg Med Chem, 4(5):709-15 (1996) (alkylated dipeptides).

[0256] 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.

[0257] 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.

[0258] 4.10.14 Assay for Receptor Activity

[0259] 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.

[0260] 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.

[0261] 4.10.15 Anti-Inflammatory Activity

[0262] 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'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.

[0263] 4.10.16 Leukemias

[0264] 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).

[0265] 4.10.17 Nervous System Disorders

[0266] 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 demyelinatiorl 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:

[0267] (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;

[0268] (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;

[0269] (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;

[0270] (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's disease, Alzheimer's disease, Huntington's chorea, or amyotrophic lateral sclerosis;

[0271] (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 B 12 deficiency, folic acid deficiency, Wernicke disease, tobacco-alcohol amblyopia, Marchiafava-Bignami disease (primary degeneration of the corpus callosum), and alcoholic cerebellar degeneration,

[0272] (vi) neurological lesions associated with systemic diseases including but not limited to diabetes (diabetic neuropathy, Bell's palsy), systemic lupus erythematosus, carcinoma, or sarcoidosis;

[0273] (vii) lesions caused by toxic substances including alcohol, lead, or particular neurotoxins; and

[0274] (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.

[0275] 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:

[0276] (i) increased survival time of neurons in culture;

[0277] (ii) increased sprouting of neurons in culture or in vivo;

[0278] (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

[0279] (iv) decreased symptoms of neuron dysfunction in vivo.

[0280] 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.

[0281] 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).

[0282] 4.10.18 Other Activities

[0283] 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.

[0284] 4.10.19 Identification of Polymorphisms

[0285] 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 autoimnune disease makes possible the diagnosis of this condition in humans by identifying the presence of the polymorphism.

[0286] 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.

[0287] 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.

[0288] 4.10.20 Arthritis And Inflammation

[0289] 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 al., 1983, Science, 219:56, or by B. Waksman et al., 1963,

[0290] 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'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.

[0291] 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.

[0292] 4.11 Therapeutic Methods

[0293] 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.

[0294] 4.11.1 Example

[0295] 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.

[0296] While the mode of administration is not particularly important, parenteral administration is preferred. An exemplary mode of administration is to deliver an intravenous bolus.

[0297] 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'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.

[0298] 4.12 Pharmaceutical Formulations and Routes of Administration

[0299] 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-C SF, GM-C SF, TNF, IL-1, IL-2, IL-3, IL-4, IL-5, IL-6, IL-7, EL-8, IL-9, IL-10, IL-11, IL-12, IL-13, IL-14, IL-IS, IFN, TNF0, TNF1, 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-A and TGF-(3), insulin-like growth factor (IGF), as well as cytokines described herein.

[0300] 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 Hy 1, 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.

[0301] 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'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.

[0302] 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.

[0303] 4.12.1 Routes of Administration

[0304] 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.

[0305] 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.

[0306] 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.

[0307] 4.12.2 Compositions/Formulations

[0308] 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.

[0309] 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's Injection, Dextrose Injection, Dextrose and Sodium Chloride Injection, Lactated Ringer'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's solution, Ringer'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.

[0310] 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.

[0311] 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.

[0312] 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.

[0313] 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.

[0314] 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.

[0315] 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.

[0316] 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.

[0317] 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.

[0318] 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, monoglycerides, 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.

[0319] 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'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.

[0320] 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.

[0321] 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-o and TGF-β), and insulin-like growth factor (IGF).

[0322] 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'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.

[0323] 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.

[0324] 4.12.3 Effective Dosage

[0325] 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 IC50 as determined in cell culture (i.e., the concentration of the test compound which achieves a half-maximal inhibition of the protein's biological activity). Such information can be used to more accurately determine useful doses in humans.

[0326] 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 LD50 (the dose lethal to 50% of the population) and the ED50 (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 LD50 and ED50. 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 ED50 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's condition. See, e.g., Fingl et al., 1975, in “The Pharmacological 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 (MEC). 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.

[0327] 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.

[0328] 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.

[0329] The amount of composition administered will, of course, be dependent on the subject being treated, on the subject's age and weight, the severity of the affliction, the manner of administration and the judgment of the prescribing physician.

[0330] 4.12.4 Packaging

[0331] 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.

[0332] 4.13 Antibodies

[0333] 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, Fab, Fab′, and F(ab′)2 fragments, and an Fab 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 IgG1, IgG2, 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.

[0334] 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: 1-244, or 489-706, 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.

[0335] 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.

[0336] 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.

[0337] 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.

[0338] 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.

[0339] 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.

[0340] 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.

[0341] 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.

[0342] 4.13.1 Polyclonal Antibodies

[0343] 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 variant 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'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).

[0344] 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).

[0345] 4.13.2 Monoclonal Antibodies

[0346] 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.

[0347] 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.

[0348] 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 KPRT), the culture medium for the hybridomas typically will include hypoxanthine, aminopterin, and thymidine (“HAT medium”), which substances prevent the growth of HGPRT-deficient cells.

[0349] 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.

[0350] Immunol., 133:3001 (1984); Brodeur et al., Monoclonal Antibody Production Techniques and Applications, Marcel Dekker, Inc., New York, (1987) pp. 51-63).

[0351] 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.

[0352] 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's Modified Eagle's Medium and RPMI-1640 medium. Alternatively, the hybridoma cells can be grown in vivo as ascites in a mammal.

[0353] 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.

[0354] 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.

[0355] 4.13.3 Humanized Antibodies

[0356] 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)).

[0357] 4.13.4 Human Antibodies

[0358] 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).

[0359] 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)).

[0360] Human antibodies may additionally be produced using transgenic nonhuman animals that are modified so as to produce fully human antibodies rather than the animal'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'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 farther modified to obtain analogs of antibodies such as, for example, single chain Fv molecules.

[0361] 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.

[0362] 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.

[0363] 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.

[0364] 4.13.5 Far Fragments and Single Chain Antibodies

[0365] 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 Fab expression libraries (see e.g., Huse, et al., 1989 Science 246, 1275-1281) to allow rapid and effective identification of monoclonal Fab 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 Fab fragment generated by reducing the disulfide bridges of an F(ab′)2 fragment; (iii) an Fab fragment generated by the treatment of the antibody molecule with papain and a reducing agent and (iv) Fv fragments.

[0366] 4.13.6 Bispecific Antibodies

[0367] 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.

[0368] 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 (Mistein 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.

[0369] 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 (CHI) 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).

[0370] 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.

[0371] 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.

[0372] 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.

[0373] 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 (VH) connected to a light-chain variable domain (VL) by a linker which is too short to allow pairing between the two domains on the same chain. Accordingly, the VH and VL domains of one fragment are forced to pair with the complementary VL and VH 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).

[0374] Antibodies with more than two valencies are contemplated. For example, trispecific antibodies can be prepared. Tutt et al., J. Immunol. 147, 60 (1991).

[0375] 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).

[0376] 4.13.7 Heteroconjugate Antibodies

[0377] 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.

[0378] 4.13.8 Effector Function Engineering

[0379] 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).

[0380] 4.13.9 Immunoconjugates

[0381] 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).

[0382] 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 212Bi, 131I, 131In, 90Y, and 186Re.

[0383] 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), iminothiolane (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-diisocyanate), 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.

[0384] 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.

[0385] 4.14 Computer Readable Sequences

[0386] 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.

[0387] 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.

[0388] By providing any of the nucleotide sequences SEQ ID NO: 1-244, or 489-706 or a representative fragment thereof; or a nucleotide sequence at least 95% identical to any of the nucleotide sequences of SEQ ID NO: 1-244, or 489-706 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.

[0389] 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.

[0390] 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.

[0391] 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).

[0392] 4.15 Triple Helix Formation

[0393] If 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.

[0394] 4.16 Diagnostic Assays and Kits

[0395] 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.

[0396] 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.

[0397] 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.

[0398] 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.

[0399] 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:

[0400] 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, serum, 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.

[0401] 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.

[0402] 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.

[0403] 4.17 Medical Imaging

[0404] 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.

[0405] 4.18 Screening Assays

[0406] 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: 1-244, or 489-706, or bind to a specific domain of the polypeptide encoded by the nucleic acid. In detail, said method comprises the steps of:

[0407] (a) contacting an agent with an isolated protein encoded by an ORF of the present invention, or nucleic acid of the invention; and

[0408] (b) determining whether the agent binds to said protein or said nucleic acid.

[0409] 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.

[0410] 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.

[0411] 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.

[0412] 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.

[0413] 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.

[0414] 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's Guide, W. H. Freeman, NY (1992), pp. 289-307, and Kaspczak et al., Biochemistry 28:9230-8 (1989), or pharmaceutical agents, or the like.

[0415] 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.

[0416] 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.

[0417] 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.

[0418] 4.19 Use of Nucleic Acids as Probes

[0419] 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: 1-244, or 489-706. 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: 1-244, or 489-706 can be used as an indicator of the presence of RNA of cell type of such a tissue in a sample.

[0420] 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.

[0421] 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.

[0422] 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.

[0423] 4.20 Preparation of Support Bound Oligonucleotides

[0424] 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.

[0425] 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 & Hondo, (1990) J. Clin. Microbiol. 28(6), 1469-72); using UV light (Nagata et al., 1985; Dahlen et al., 1987; Morrissey & 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.

[0426] 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 lining 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.).

[0427] 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 (>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).

[0428] 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 phosphoramidate 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.

[0429] 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-MeIm7), is then added to a final concentration of 10 mM 1-MeIm7. A ss DNA solution is then dispensed into CovaLink NH strips (75 μl/well) standing on ice.

[0430] Carbodiimide 0.2 M 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide (EDC), dissolved in 10 mM 1-MeIm7, 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-Immuno 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, 10.25% SDS heated to 50° C.).

[0431] 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 & 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.

[0432] 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 inmmobilized 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 & Cavalier (1988) Anal. Biochem. 169(1), 104-8; all references being specifically incorporated herein.

[0433] 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.

[0434] One particular way to prepare support bound oligonucleotides is to utilize the light-generated synthesis described by Pease et al., (1994) Proc. Nat'l. 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,

[0435] 4.21 Preparation of Nucleic Acid Fragments

[0436] 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).

[0437] 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.

[0438] 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.

[0439] 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.

[0440] 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.

[0441] 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.

[0442] 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).

[0443] 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.

[0444] 4.22 Preparation Of DNA Arrays

[0445] 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 mm2, 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 mm2 and there may be a 1 mm space between subarrays.

[0446] 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.

[0447] 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.

[0448] All references cited within the body of the instant specification are hereby incorporated by reference in their entirety.

5.0 EXAMPLES

5.1 Example 1

[0449] Novel Nucleic Acid Sequences Obtained From Various Libraries

[0450] 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.

[0451] 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.

5.2 Example 2

[0452] Assemblage of Novel Nucleic Acids

[0453] The contigs or nucleic acids of the present invention, designated as SEQ ID NO: 489-706 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'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%.

[0454] Table 8 sets forth the novel predicted polypeptides (including proteins) encoded by the novel polynucleotides (SEQ ID NO: 489-706) of the present invention, and their corresponding translation start and stop nucleotide locations to each of SEQ ID NO: 489-706. 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.

5.3 Example 3

[0455] Novel Nucleic Acids

[0456] The novel nucleic acids of the present invention were assembled from sequences that were obtained from a cDNA library by methods described in Example 1 above, and in some cases sequences obtained from one or more public databases. The nucleic acids 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 (Flyseq's database containing EST sequences, dbEST, gb pri, and UniGene) that belong to this assemblage. The algorithm terminated when there was no additional sequences from the above databases that would extend the assemblage. 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%. Using PURAP (Univ. of Washington) or CAP4 (Paracel), a full-length gene cDNA sequence and its corresponding protein sequence were generated from the assemblage. Any frame shifts and incorrect stop codons were corrected by hand editing. During editing, the sequences were checked using FASTY and/or BLAST against Genebank (i.e., dbEST, gb pri, UniGene, and Genpept) and the Geneseq (Derwent). Other computer programs which may have been used in the editing process were phredPhrap and Consed (University of Washington) and ed-ready, ed-ext and cg-zip-2 (Hyseq, Inc.). The full-length nucleotide and amino acid sequences, including splice variants resulting from these procedures are shown in the Sequence Listing as SEQ ID NO: 1-488.

[0457] SEQ ID NO: 1-132 were classified as secreted according to their predicted cellular localization using the Pfam software program (Sonnhammer et al., Nucleic Acids Res., Vol. 26(1) pp. 320-322 (1998), and http://pfam.wstl.edu/, herein incorporated by reference).

[0458] SEQ ID NO: 133-197 were determined to contain signal peptide sequences and their cleavage sites 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.

[0459] SEQ ID NO: 198-244 were determined to be secreted polypeptides using a proprietary algorithm, SeqLoc™ (Hyseq Inc.). SeqLoc™ classifies the proteins into three sets of locales: intracellular, membrane, or secreted. This prediction is calculated using maximum likelihood estimation of three characteristics of each polypeptide, 1) percentage of cysteine residues, 2) Kyte-Doolittle scores for the first 20 amino acids of each protein (J. Mol Biol, 157, pp. 105-31 (1982), incorporated herein by reference), and 3) Kyte-Doolittle scores to calculate the longest hydrophobic stretch (LHS) of the said protein (J. Mol Biol, 157, pp. 105-31 (1982), incorporated herein by reference). The LHS is calculated by finding the stretch of 20 amino acid residues in the protein that have the highest sum of Kyte-Doolittle hydrophobicity values.

[0460] Table 1 shows the various tissue sources of SEQ ID NO: 1-244.

[0461] The homologs for polypeptides SEQ ID NO: 245-488, that correspond to nucleotide sequences SEQ ID NO: 1-244 were obtained by a BLASTP version 2.0al 19 MP-WashU searches against Genpept release 124 and the Geneseq release 200112 (Derwent) using BLAST algorithm. The results showing homologues for SEQ ID NO: 245-488 from Genpept 124 and Geneseq are shown in Table 2.

[0462] 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 eMatrix 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.

[0463] 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/.

[0464] 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 1-244 (i.e. SEQ ID NO: 245-488). Models were generated by (1) PSI-BLAST which is a multiple alignment sequence profile-based searching developed by Altschul et al, (Nucl. Acids. Res. 25, 3389-3408 (1997)), (2) High 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 NM (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's Profile-3D threading program developed in Dr. David Eisenberg'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:

[0465] Verify score (normalized)=(raw score−½ high score)/(½ high score)

[0466] 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 (WP). As given in table 5, a verify score between 0 to 1.0, with 1 being the best, represents a good model. Similarly, a PMF 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.

[0467] 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.

[0468] Table 7 correlates SEQ ID NO: 1-244 to a specific chromosomal location.

[0469] Table 9 is a correlation table of the novel polynucleotide sequences SEQ ID NO: 1-244, their corresponding polypeptide sequences SEQ ID NO: 245-488, their corresponding priority contig nucleotide sequences SEQ ID NO: 489-706, their corresponding priority contig polypeptide sequences SEQ ID NO: 707-924, and the US serial number of the priority application in which the contig sequence was filed.

TABLE 1
	RNA	Library
Tissue Origin	Source	Name	SEQ ID NO:
adult brain	GIBCO	AB3001	1 5 7 13 34 90 99 127 151 207 224 239
adult brain	GIBCO	ABD003	1 8 11 13 43 55 62 64 75 81 84-85 102 127 129-131 133 144 146-147
			151-152 186 189 197 200-201 207-208 210 225 241
adult brain	Clontech	ABR001	13 22 64 66 102 112 182 186 206 211 238
adult brain	Clontech	ABR006	1-5 18 22 24 36-39 47 52 55-56 60-61 93-94 98 106 112 125 128 133
			143 145 147 151 157 162 165 179 182 184 189-191 235 238-239
adult brain	Clontech	ABR008	1-2 4 7-8 11 13-14 22 24 27 35-40 42 48-49 56-57 59 61 64 67 70 73
			78-82 92 95 98-99 102 104-105 108 112 115 119 121 123 126-130
			133 140-143 147 150 153 157 159 162 165 171 176 180-182 189-190
			195-197 212 222 225-227 231 236-237 241
adult brain	BioChain	ABR013	183
adult brain	Invitrogen	ABR014	140 176 189
adult brain	Invitrogen	ABR015	133 136 208 241
adult brain	Invitrogen	ABR016	8 13 186
adult brain	Invitrogen	ABT004	11 42 48 60 85 129 133 141-142 147 149
cultured	Stratagene	ADP001	10 25 42-43 48 75 81 91 122 130 140 144 163 178 186 205 241
preadipocytes
adrenal gland	Clontech	ADR002	4 7 9 13 24-26 31 33 42-43 56 60 71 84-85 94 98 100-101 118 127
			133-134 141-144 163 182 189 199 201 207 212
adult heart	GIBCO	AHR001	1 4 6-8 13 21 23-24 42-43 45 53-54 60-61 67 70 72 81 90-91 98-99
			102 115 120 130 133 137-140 143-144 146 166-169 178-179 183
			186 189 197 204 207 213 224-225
adult kidney	GIBCO	AKD001	4 6 8 12-13 20 23-26 34 39-43 53-54 62 64 66 73 79 81 90 98 102
			108 123 127 130 133 135 144-148 163 171-172 179 186 189 197 200
			204 206-207 210 213 224-225 227 233 241-242
adult kidney	Invitrogen	AKT002	6 12-13 24 39 42-43 51 60 66 86 93 102 125 132 143 146-148 156
			178 184 186 189 197 200 202 210 219 225 233
adult lung	GIBCO	ALG001	25-26 41 48 60 74 81 146 178 189 197
lymph node	Clontech	ALN001	8 13 18 25 35-38
young liver	GIBCO	ALV001	1 24 27 48 73 85 136 173-175 178-179 189 196-197 201
adult liver	Invitrogen	ALV002	4-5 12-13 32 39 42 48 51 56 73 81 98 102 120 133 136 140 143-144
			163 165 173-175 178-179 182 189 193 225 231 241
adult liver	Clontech	ALV003	36-38 51 73 135-136 165 173-175 224
adult ovary	Invitrogen	AOV001	4 7 9 12-14 20-21 23-26 31 34 39-40 42-43 48 52 60 62 64 73 75 78-79
			81 94 96 98 112 118-119 122-123 127 130 133 135 140 144 146-147
			149 153 163 172 178 182 186 193 195 202 206-207 209 213 222
			224 231 233 236 239-240 242
adult placenta	Clontech	APL001	43 73 178
placenta	Invitrogen	APL002	41 75 224
adult spleen	GIBCO	ASP001	4 8 13 23-24 27 41 48 64 75 81 102 104 124 141-144 146 189 201
			224
adult testis	GIBCO	ATS001	10 13 34 43 46 60 81 102 123 143-144 155 183 189 200 206 224
Genomic	Research	BAC002	80
DNA-from-	Genetics
BAC-393I6	(CITB
	BAC
	library)
Genomic	Genomic	BAC003	80
DNA-from-	DNA from
BAC-393I6	Genetic
	Research
adult bladder	Invitrogen	BLD001	8 12-13 25 71 122-123 129 134 140 144 178 181 184 241-242
bone marrow	Clontech	BMD001	1-2 7 12 14 17-19 23 26 46-47 63-64 81 91 102 106 118 122 124 133
			144 146 186 189 198-203 205 207 224-225 236
bone marrow	Clontech	BMD002	1-2 11-12 14 19 28-29 36-38 40-41 43 48-49 59-61 71 73 76 90 93
			95 97-98 104 115 118 120 122 125 130 134 143 162-163 171 186
			189 197 202 206-207 212 225 240-241 243
bone marrow	Clontech	BMD007	11
adult colon	Invitrogen	CLN001	13 71 75 93 122 129 134 141-142 224 241
mixture of	various	CTL016	71 122 207
16 tissues-	vendors
mRNAs*
mixture of	various	CTL021	189
16 tissues-	vendors
mRNAs*
adult cervix	BioChain	CVX001	1 7 12 14 21 24 26-27 35 43 51 60 62 64 71 84 95 98-99 122-123
			127 129-130 140-142 144 146 176 178 186 195 197 200-201 206
			211-213 220 222 240
endothelial	Stratagene	EDT001	1 4 7-8 10-11 13 19-20 23 25 30-31 48 62 64 66 75 78 81 90-91 93
cells			95 98 118 133 137-139 144-146 150 156 178 186 197 200 206-207
			209 213 215 224 230 241
fetal brain	Clontech	FBR001	35 53-54 129 182
fetal brain	Clontech	FBR004	36-38 70 94 126 171 187 231 238
fetal brain	Clontech	FBR006	1-2 5 7 13 15 24 32 35-39 42 56-57 62 67 73 79 83 90 92 98 112 114
			117 119 123 127 129 135 140-143 150 155 157-158 162 171-172
			176 180-182 190 192 212 218 220 222 228 230-231 236-237 241-243
fetal brain	Invitrogen	FBT002	9 34 36-38 81 102 127 147 197 207
fetal heart	Invitrogen	FHR001	4 7-8 10 13-14 21 23 27 34 36-38 43 48 60-61 73 78-79 98-101 104
			120 122 126-127 129 133 143-144 155 160 163 185-186 197 202
			217-218 225 231
fetal kidney	Clontech	FKD001	6 23 66 81 146
fetal kidney	Clontech	FKD002	19 26 42 60 78-79 92 102 127-130 140 143 182 186 189 202 212 220
fetal kidney	Invitrogen	FKD007	122 189
fetal lung	Clontech	FLG001	6 8 32 35 62 122 129 197 211 215
fetal lung	Invitrogen	FLG003	10 39-40 69 83 98 102 126 135 178 183 189 199 202 224 242
fetal liver-	Columbia	FLS001	1-13 17 20-21 23 25 30 39 41-43 48 61 63-64 75-76 79 85 90 95 98-99
spleen	University		102 108 115 120 127 130 133-144 146-147 154 173-175 178-179
			182 185 187 189 196-197 201-203 205 210 212 218 224-226 241
fetal liver-	Columbia	FLS002	1 4-5 8 11 13 17-18 20-25 32 39 41-42 48 51 56 63-64 79 90-91 95
spleen	University		98 102 118 130 136 143-144 146 171 173-175 178-179 182 185-187
			193 197 203 214 218 225-226 230 238 243
fetal liver-	Columbia	FLS003	1 3 9 13 21 43 50 61 66 90 95 98 115 122 130 136 173-175 187-188
spleen	University		196 202-203 218 225 241
fetal liver	Invitrogen	FLV001	23 31 42 70 75 122 133 140 172-175 178-179 205
fetal liver	Clontech	FLV002	2 11 42 133 173-175 180 224 226
fetal liver	Clontech	FLV004	2 11 35-38 40 48 98 118 127 133 136 148 162 173-175 179 182 186
			189 196-197 202 225
fetal muscle	Invitrogen	FMS001	4 8 10 21 27 33 49 102 122 130 133 164 166-169 192 244
fetal muscle	Invitrogen	FMS002	7-8 10 13 23 26 33 42 49 61-62 76 86 98 118 122 124 129-130 140-142
			164 166-169 192 204 207 244
fetal skin	Invitrogen	FSK001	1 4 9-10 12-13 27 36-38 48 50 61-62 64 71 73-75 80-81 87-91 94 99
			107 122 130 132-134 140-142 156 163 166-170 172 178-179 181
			184 189 196-197 202 212 214 221 227 231 238 241
fetal skin	Invitrogen	FSK002	10 14 22-23 25 39 48 88-91 98 100-101 104 106 108 115 117-118
			120 122 124 130 133 160 176 180 182 186 197 207 225 232 242
umbilical cord	BioChain	FUC001	6 12 18 32 36-38 40 61 70-71 75 84 94-95 98-99 118 122 127 140
			144 156 163 180 184 189 205 210 215 241
fetal brain	GIBCO	HFB001	1 4 11-13 15 24 26 30 32 42-44 46 48 64 81 90 94 112 125 130 133
			135 140 143 151 155 162 189 197 200-201 206-208 210 227 241
macrophage	Invitrogen	HMP001	1 12 25 140 144 181 194 197
infant brain	Columbia	IB2002	4 9-10 15 22-23 33 43 48-49 55 63 67 73 75 81 85 90 99 102 120
	University		122 124 135-136 141-142 145-148 151 155 157-158 162 171 182
			189 197 200 206-207 224-225 233 238-239
infant brain	Columbia	IB2003	7 10 12 22 47 49 53-54 61 75 84-85 90 94-95 102 122 133 135 141-142
	University		147 176 189 204 207 231 239 241
infant brain	Columbia	IBM002	12 157-158 224
	University
infant brain	Columbia	IBS001	6 10 33 108 135 233
	University
lung,	Stratagene	LFB001	1 4 8 12-13 30 66 81 117 133 140 144 211 215 238
fibroblast
lung tumor	Invitrogen	LGT002	1 3-4 12 15 39 42-43 48 50-51 62-63 66 69 75 81 83-84 95 102 116
			123 125 137-139 144 146 178-179 181 185 189 195-197 204 209-212
			216 218 222 224-225 227 231 238 240-242
lymphocytes	ATCC	LPC001	4 14 21 25-27 35 46 48 53-54 66 68-69 75 81 88-89 102 104 110 118
			122 129-130 133 145 171 176-177 189 195-196 201 207 212 225-226
leukocyte	GIBCO	LUC001	1-2 4 7-8 12-14 17 21-22 25-29 36-38 43 50 61 63-64 71 75 81 88-90
			94 98 102 104 118 120 127 130 134 140 146-147 170 186 189 195
			197 200-201 205-207 224-225 233 240
leukocyte	Clontech	LUC003	14 27 81 146 197 201 204 242
melanoma	Clontech	MEL004	4 52 81 130 133 143 146 186 194 196 200 212 218
from cell line
ATCC #CRL
1424
mammary	Invitrogen	MMG001	4 6 9 12-13 25 27 31 33-34 36-39 42 48 51 53-56 60-62 70 72 75 81
gland			85 88-89 94-95 102 119 122 127 129 131-133 140 144 146 156 163
			172 176 178-179 181 185 189 192 205-206 210 218 224 231 236 238
			240-243
induced	Stratagene	NTD001	1 22 30 32 42 84 117 125 144 206 222
neuron-cells
retinoic acid-	Stratagene	NTR001	1 3 34 104 124 129 140 225 241
induced-
neuronal-cells
neuronal cells	Stratagene	NTU001	3-4 15 60 63 75 120 122 133 140 171 181 196 206 210
pituitary gland	Clontech	PIT004	13 20 33 43 66 74 90 123 130 217
placenta	Clontech	PLA003	4-5 7 25 36-39 56 93 100-101 103-104 120 122 134 186-187 189 231
prostate	Clontech	PRT001	20 26 34 62 72 81 143 166-169 178-179 197 202 218 241
rectum	Invitrogen	REC001	3 25 33 51 74 88-89 122 129 133 155 189 197 224 241 243
salivary gland	Clontech	SAL001	1 18 34 69 71 120 179 204 214 235-236
salivary gland	Clontech	SALs03	179
small intestine	Clontech	SIN001	1 4 7-8 10 12 20-22 26 32 36-38 43 48 51 61 68 71 75 86 91-92 96-99
			118 122 124-125 130 133-134 140 143-144 148 160 185 189 196
			201 210 212 224 229 234 241
skeletal	Clontech	SKM001	7 42 49 73 75 102 130 143 223
muscle
spinal cord	Clontech	SPC001	2 8 13 24 26 35 43 63-64 127-128 130 135 156 178 185 189 196 206
			210
adult spleen	Clontech	SPLc01	7-8 14 36-38 53-54 59 71 92 104 108 125 129 133 140-142 162 237
stomach	Clontech	STO001	32 99 143 161 172 189
thalamus	Clontech	THA002	7 10-11 60 79 98 127 131 136 143 153 183 186 190 206-207 212 227
thymus	Clontech	THM001	1 14 26 30 46 50 74 79 98 115 118 130 154 196-197 217 222 224
			233
thymus	Clontech	THMc02	1-2 4 10 13 24-25 30 32 36-39 48 61 64-65 73-74 76-77 79 82 88-89
			100-101 105-106 115 118 120 122 127 130 133 140 146 171 183 185
			199 202 206 224-225 231 237 242
thyroid gland	Clontech	THR001	1 4-5 7-8 20-21 24 26 31 43 49 53-54 64 66 70 73 75 81 90 92 98
			110 120 124 130 133 140 143-144 162-163 172 189 197 199 201
			206-208 212-213 219-220 224 236 238 241-242
trachea	Clontech	TRC001	4-5 40 48 62 111 144 146 179 200 226
uterus	Clontech	UTR001	10 12-13 21 71 130 134 140 144 208 210 213 218
*The 16 tissue-mRNAs and their vendor source, are as follows: 1) Normal adult brain mRNA (Invitrogen),
# 2) normal adult kidney mRNA (Invitrogen), 3) normal adult liver mRNA (Invitrogen), 4) normal fetal brain
# mRNA (Invitrogen), 5) normal fetal kidney mRNA (Invitrogen), 6) normal fetal liver mRNA (Invitrogen),
# 7) normal fetal skin mRNA (Invitrogen), 8) human adrenal gland mRNA (Clontech), 9) human bone marrow
# mRNA (Clontech), 10) human leukemia lymphablastic mRNA (Clontech), 11) human thymus mRNA (Clontech),
# 12) human lymph node mRNA (Clontech), 13) human spinal cord mRNA (Clontech), 14) human thyroid mRNA (Clontech),
# 15) human esophagus mRNA (BioChain), 16) human conceptional umbilical cord mRNA (BioChain).

[0470]

TABLE 2
SEQ
ID	Accession
NO:	Number	Species	Description	Score	% identity
245	W78199	Homo sapiens	Human secreted protein encoded by gene 74 clone	2952	99
			HGBAC11.
245	gi11139753	Homo sapiens	bA48B24.1 (A novel protein containing a formin	2809	99
			binding protein (FBP28) domain)
245	W85610	Homo sapiens	Secreted protein clone eh80_1.	1678	98
246	gi1213539	Caenorhabditis	coded for by C. elegans cDNA CEMSG95FB;	208	34
		elegans	coded for by C. elegans cDNA CEMSG95RB;
			coded for by C. elegans cDNA CEMSG95RC;
			coded for by C. elegans cDNA yk9h1.3; coded for
			by C. elegans cDNA yk9h1.5; coded for by C.
			elegans cDNA yk42a10.5; coded for by C. elegans
			cDNA yk91f4.5; coded for by C. elegans cDNA
			yk127h3.5; coded for by C. elegans cDNA
			yk91f4.3; Similar to ubiquitin conjugating
			enzyme; recoverin subfamily of EF-hand calcium
			binding protein
246	gi8650530	Naegleria	calcineurin B	160	30
		fowleri
246	Y69996	Homo sapiens	Human receptor-associated protein from Incyte	154	30
			clone 2132846.
247	gi7332056	Caenorhabditis	contains similarity to Pfam family PF00078	228	22
		elegans	(Reverse transcriptase (RNA-dependent)),
			score = 79.6, E = 6.3e−20, E = 1
247	gi1572721	Homo sapiens	megakaryocyte stimulating factor; MSF	230	21
247	B29773	Homo sapiens	Human megakaryocyte stimulating factor (MSF),	230	21
			SEQ ID NO: 1.
248	gi11967711	Homo sapiens	Tsg24 protein	10136	99
248	gi642252	Mus musculus	tsg24	9437	92
248	gi10178133	Arabidopsis	meiotic check point regulator-like protein	1243	35
		thaliana
249	gi156297	Caenorhabditis	putative	656	39
		elegans
249	gi2624972	Mus musculus	proline-rich protein 48	672	49
249	gi6523547	Volvox carteri	hydroxyproline-rich glycoprotein DZ-HRGP	589	39
		f. nagariensis
250	gi10334640	Homo sapiens	bA425A6.1 (frizzled (Drosophila) homolog 8)	3785	100
250	gi1151260	Mus musculus	transmembrane receptor	3539	95
250	gi4164471	Danio rerio	frizzled 8a protein	1139	82
251	gi10176983	Arabidopsis	GTP-binding membrane protein LepA homolog	1836	58
		thaliana
251	gi3004655	Drosophila	waclaw	1558	51
		melanogaster
251	gi2984041	Aquifex	G-protein LepA	1656	52
		aeolicus
252	gi2460318	Homo sapiens	RNA-binding protein regulatory subunit	505	92
252	gi5731801	Homo sapiens	bk215D11.1 (RNA-binding protein regulatory	505	92
			subunit)
252	gi1780755	Homo sapiens	DJ-1 protein	505	92
253	gi3883070	Yersinia pestis	putative endonuclease	190	34
253	gi4154837	Helicobacter	putative ENDONUCLEASE	174	28
		pylori J99
253	gi2313422	Helicobacter	membrane bound endonuclease (nuc)	172	30
		pylori 26695
254	gi1407657	Mus musculus	endophilin II	1377	94
254	gi1869810	Homo sapiens	SH3-containing Grb-2-like 1	1445	100
254	gi6120106	Homo sapiens	SH3-containing protein EEN	1445	100
255	gi437365	Homo sapiens	AD amyloid	579	86
255	gi11118352	Homo sapiens	SNCA isoform NACP140	579	86
255	R70127	Homo sapiens	Precursor of novel amyloid component (NACP).	579	86
256	gi6433901	Homo sapiens	Graf protein	1681	55
256	W97809	Homo sapiens	Human GTPase regulator GRAF.	1681	55
256	gi5081652	Homo sapiens	oligophrenin-1 like protein	1461	53
257	gi2460318	Homo sapiens	RNA-binding protein regulatory subunit	632	100
257	gi5731801	Homo sapiens	bK215D11.1 (RNA-binding protein regulatory	632	100
			subunit)
257	gi1780755	Homo sapiens	DJ-1 protein	624	99
258	gi5020264	Mus musculus	Cdc42 GTPase-activating protein	927	49
258	gi2477513	Homo sapiens	F25965_3	678	50
258	gi7271811	Drosophila	GTPase activating protein	580	53
		melanogaster
259	gi12005724	Homo sapiens	mixed lineage kinase MLK1	5618	100
259	gi971420	Homo sapiens	mixed lineage kinase 2	1941	61
259	gi758593	Homo sapiens	serine/threonine kinase with SH3 domain, leucine	1939	61
			zipper domain and proline rich domain
260	gi551608	Homo sapiens	receptor protein-tyrosine kinase	4490	100
260	R85092	Homo sapiens	EPH-like receptor protein tyrosine kinase HEK11.	4490	100
260	gi755568	Rattus	Ehk-3, full length form	4449	98
		norvegicus
261	gi181176	Homo sapiens	connective tissue activating peptide III	618	96
261	gi344294	synthetic	novel factor having neutrophil-stimulating activity	618	96
		construct
261	R13519	Homo sapiens	Leukocyte derived growth factor.	618	96
262	gi9651963	Xenopus laevis	putative N-terminal acetyltransferase	603	80
262	gi6730746	Arabidopsis	putative N-terminal acetyltransferase; 84330-89402	514	67
		thaliana
262	gi7326500	Caenorhabditis	contains similarity toTR: O74985	454	54
		elegans
263	G01995	Homo sapiens	Human secreted protein, SEQ ID NO: 6076.	523	100
263	gi1825586	Caenorhabditis	contains similarity to C2 domains	228	36
		elegans
263	gi6687541	Erysiphe pisi	transmembrane protein	188	36
264	gi1944389	Mus musculus	Sh3y11	1238	86
264	Y44988	Homo sapiens	Human epidermal protein-5.	1333	94
264	gi500710	Saccharomyces	Ysc84p	562	52
		cerevisiae
265	gi2645229	Plectonema	kinesin light chain	411	43
		boryanum
265	gi1208772	Gallus gallus	kinesin light chain	373	31
265	gi161532	Strongylocentrotus	kinesin light chain isoform 4	379	41
		purpuratus
266	gi4966262	Caenorhabditis	Contains similarity to Pfam domain: PF00646 (F-	1872	56
		elegans	box), Score = 28.7, E-value = 4.3e−05, N = 1
266	gi6164741	Homo sapiens	F-box protein Fbx11	661	99
266	Y83079	Homo sapiens	F-box protein FBP-11.	661	99
267	gi10441465	Homo sapiens	actin filament associated protein	1403	45
267	gi487416	Gallus gallus	actin filament protein	1138	50
267	gi487418	Gallus gallus	actin filament-associated protein	1285	46
268	gi11323315	Homo sapiens	dJ998C11.1 (continues in Em: AL445192 as	374	30
			bA269H4.1)
268	gi4185567	Mus musculus	cAMP-dependent Rap1 guanine-nucleotide	181	35
			exchange factor
268	gi11611477	Mus musculus	cAMP-GEFII	181	35
269	gi6580315	Caenorhabditis	Y51H4A.13	144	29
		elegans
269	W50192	Homo sapiens	Amino acid sequence of salivary protein CON-1.	91	32
269	gi32384	Homo sapiens	Hox2I protein (AA 1-301)	126	29
270	gi2815888	Homo sapiens	MEK kinase 1	6983	99
270	gi4583380	Mus musculus	MAP kinase kinase kinase 1	6192	89
270	gi1354137	Rattus	MAP kinase kinase kinase 1	6153	89
		norvegicus
271	gi6649931	Homo sapiens	interleukin-1 receptor-associated kinase	2317	95
271	W14306	Homo sapiens	Interleukin-1 receptor-associated protein kinase.	2311	94
271	gi12409196	Mus musculus	pelle-like protein kinase	1767	74
272	gi5051670	Homo sapiens	apoptotic protease activating factor-1 long isoform	3274	100
			APAF-1L
272	gi5869888	Homo sapiens	apoptotic protease activating factor 1	3274	100
272	gi3694813	Mus musculus	apoptotic protease activating factor 1	2819	84
273	gi5051670	Homo sapiens	apoptotic protease activating factor-1 long isoform	3274	100
			APAF-1L
273	gi5869888	Homo sapiens	apoptotic protease activating factor 1	3274	100
273	gi3694813	Mus musculus	apoptotic protease activating factor 1	2819	84
274	gi1374695	Homo sapiens	human protein homologous to DROER protein	244	100
274	gi6841073	Xenopus laevis	enhancer of rudimentary homologue ERH	244	100
274	gi1620874	Mus musculus	Mer	244	100
275	gi1657835	Mus musculus	Rho-guanine nucleotide exchange factor	2545	80
275	gi5199316	Homo sapiens	non-ocogenic Rho GTPase-specific GTP exchange	710	36
			factor
275	gi4469558	Homo sapiens	breast cancer nuclear receptor-binding auxiliary	663	35
			protein
276	gi8388704	Leishmania	probable CG14353 protein	532	49
		major
276	G03317	Homo sapiens	Human secreted protein, SEQ ID NO: 7398.	285	98
276	gi1907211	Saccharomyces	YCR072c, len: 515	87	28
		cerevisiae
277	gi5823454	Homo sapiens	GTPase-activating protein 6 isoform 4	728	38
277	gi7243304	Homo sapiens	rho-type GTPase-activating protein isoform 3	723	38
277	gi5724778	Mus musculus	rho-type GTPase-activating protein rhoGAPX-1	724	36
278	gi1666073	Homo sapiens	RRP22 protein	509	52
278	gi861254	Caenorhabditis	similar to RAS-related proteins	216	36
		elegans
278	gi3947880	Schizosaccharomyces	putative ras-related GTP-binding protein	212	30
		pombe
279	B29791	Homo sapiens	Human steroidogenic acute regulatory protein	336	34
			homologue StAR-B.
279	gi11992399	Mus musculus	StAR-related protein 1-4E	327	36
279	gi11992401	Mus musculus	StAR-related protein p3-15E/p3-16E	317	38
280	gi3986768	Mus musculus	G9A	1074	47
280	gi287865	Homo sapiens	G9a	1087	47
280	gi4529889	Homo sapiens	G9A	1087	47
281	gi287865	Homo sapiens	G9a	584	47
281	gi4529889	Homo sapiens	G9A	584	47
281	gi12803701	Homo sapiens	ankyrin repeat-containing protein	584	47
282	gi3986768	Mus musculus	G9A	1022	47
282	gi287865	Homo sapiens	G9a	1035	47
282	gi4529889	Homo sapiens	G9A	1035	47
283	gi6563258	Homo sapiens	insulin receptor tyrosine kinase substrate	1598	99
283	gi4454524	Homo sapiens	similar to insulin receptor substrate BAP2; similar	1526	100
			to PID: g4126477
283	gi12803353	Homo sapiens	Similar to BAI1-associated protein 2	400	31
284	W88399	Homo sapiens	Human testis secreted protein dx290_1.	2605	99
284	gi5281051	Arabidopsis	stress-induced protein sti1-like protein	159	28
		thaliana
284	gi872116	Glycine max	sti (stress inducible protein)	156	26
285	gi6492338	Mus musculus	adaptor protein; DOKL	1795	77
285	gi7363368	Mus musculus	inhibitory adapter molecule DOK3	1795	77
285	gi3043919	Homo sapiens	docking protein	509	39
286	gi36619	Homo sapiens	serine/threonine protein kinase	2452	97
286	gi12654445	Homo sapiens	PCTAIRE protein kinase 1	2452	97
286	gi53611	Mus musculus	PCTAIRE-1 protein kinase	2408	94
287	gi12484136	Rattus	SMHS2	1905	84
		norvegicus
287	gi3297882	Homo sapiens	atopy related autoantigen CALC	335	28
287	gi2827631	Arabidopsis	putative protein	318	30
		thaliana
288	gi1326341	Caenorhabditis	weak similarity to regions of guanine-nucleotide	262	35
		elegans	releasing factors
288	Y99660	Homo sapiens	Human GTPase associated protein-11.	205	81
288	gi1293099	Dictyostelium	aimless RasGEF	200	26
		discoideum
289	gi10801596	Mus musculus	Doc2gamma	1104	76
289	gi1575774	Rattus	Doc2A	582	47
		norvegicus
289	gi285646	Bos taurus	‘rabphilin-3A’	576	51
290	Y99660	Homo sapiens	Human GTPase associated protein-11.	1043	100
290	gi1326341	Caenorhabditis	weak similarity to regions of guanine-nucleotide	658	42
		elegans	releasing factors
290	gi2981229	Drosophila	putative guanine nucleotide releasing factor	575	61
		affinis
291	gi1123123	Caenorhabditis	coded for by C. elegans cDNA yk99b4.3; similar	876	43
		elegans	to human transforming protein (PIR: S22157)
291	gi4099012	Dictyostelium	drainin	487	45
		discoideum
291	gi1039341	Schizosaccharomyces	putative GTPase-activator protein of Rab-like	374	30
		pombe	small GTPases
292	gi550060	Homo sapiens	GTP-binding protein	562	100
292	gi55457	Mus musculus	Ypt1 protein (AA 1-205)	562	100
292	gi763158	Mus musculus	GTP-binding protein	562	100
293	gi10279705	Homo sapiens	bA243J16.3 (similar to MYLK (myosin, light	3106	100
			polypeptide kinase))
293	gi165506	Oryctolagus	myosin light chain kinase (EC 2.7.1.-)	2669	86
		cuniculus
293	gi205497	Rattus	skeletal muscle light chain kinase (E.C. 2.7.1.37)	2454	79
		norvegicus
294	gi3599940	Mus musculus	faciogenital dysplasia protein 2	2548	82
294	gi3342246	Rattus	actin-filament binding protein Frabin	1558	49
		norvegicus
294	gi722343	Mus musculus	Fgd1	1491	49
295	gi3851202	Homo sapiens	ZO-3	4819	98
295	gi3033501	Canis familiaris	ZO-3	3858	83
295	gi6690528	Mus musculus	tight junction-associtated protein ZO-3	3629	79
296	gi10440353	Homo sapiens	FLJ00011 protein	135	31
296	gi915208	Sus scrofa	gastric mucin	145	20
296	gi3108057	Mus musculus	channel interacting PDZ domain protein	137	27
297	Y83085	Homo sapiens	F-box protein FBP-17.	2277	81
297	gi10764488	Homo sapiens	dactylin	2217	100
297	B07748	Homo sapiens	A human cancer-associated protein-2 (CAP-2).	2155	100
298	gi10764488	Homo sapiens	dactylin	1597	100
298	B07748	Homo sapiens	A human cancer-associated protein-2 (CAP-2).	1597	100
298	gi7594782	Mus musculus	mouse ortholog of the zebrafish hagoromo gene	1530	94
299	Y97293	Homo sapiens	Lipid associated protein (LIPAP) 3335404CD1.	2283	78
299	gi5670328	Homo sapiens	copine III	1335	50
299	B24231	Homo sapiens	Human vesicle associated protein 10 SEQ ID	1332	49
			NO: 10.
300	gi10178646	Hydra vulgaris	dishevelled	199	46
300	gi458868	Drosophila	dishevelled	193	41
		melanogaster
300	gi516485	Drosophila	dsh	193	41
		melanogaster
301	gi3560124	Homo sapiens	LGMD2B protein	126	34
301	gi6572442	Mus musculus	dysferlin	125	34
301	gi3600028	Homo sapiens	dysferlin	126	34
302	gi51144	Mus musculus	h2-calponin	1030	76
302	gi1526432	Homo sapiens	neutral calponin	1029	75
302	gi1962	Sus scrofa	h2-calponin	1029	76
303	gi2909372	Homo sapiens	small glutamine-rich tetratricopeptide (SGT)	860	58
303	gi4539082	Homo sapiens	small glutamine-rich tetratricopeptide repeat	860	58
			containing protein
303	gi4235146	Homo sapiens	small glutamine-rich tetratricopeptide (SGT)	860	58
304	gi11320938	Homo sapiens	SM-20	2314	100
304	B10873	Homo sapiens	Human tumor-associated antigen 9D7 protein.	797	63
304	gi469478	Rattus	SM-20	786	62
		norvegicus
305	gi11527997	Homo sapiens	NOTCH2 protein	1483	99
305	gi11275978	Homo sapiens	NOTCH 2	1471	98
305	Y06816	Homo sapiens	Human Notch2 (humN2) protein sequence.	1471	98
306	G02355	Homo sapiens	Human secreted protein, SEQ ID NO: 6436.	597	96
306	gi3320122	Rattus	espin	160	36
		norvegicus
306	gi9754902	Mus musculus	espin	158	38
307	G04075	Homo sapiens	Human secreted protein, SEQ ID NO: 8156.	567	99
307	gi5732618	Homo sapiens	myosin-IXa	142	46
307	Y05781	Homo sapiens	Human myosin IXa.	142	46
308	Z92427_aa1	Homo sapiens	26-JUN-1997 cDNA encoding human WD-40	1886	99
			protein, WDPro1.
308	W84085	Homo sapiens	Human membrane fusion protein WDPro1.	1885	99
308	Y77488	Homo sapiens	Human WD-40 protein, WDPro1.	1885	99
309	gi1245357	Homo sapiens	procollagen C-proteinase	3836	99
309	W13670	Homo sapiens	C-proteinase encoded by clone pCP-2.	3836	99
309	gi179500	Homo sapiens	bone morphogenetic protein 1	3836	99
310	gi2429474	Caenorhabditis	Contains similarity to Pfam domain: PF00169	448	32
		elegans	(PH), Score = 36.2, E-value = 4.4e−10, N = 1
310	gi6650370	Dictyostelium	rac serine/threonine kinase homolog	114	29
		discoideum
310	gi9759096	Arabidopsis	AtPH1-like protein	100	31
		thaliana
311	gi5139689	Homo sapiens	MOK protein kinase	1848	94
311	gi5139691	Mus musculus	MOK protein kinase	1491	81
311	gi1127036	Rattus	serine/threonine protein kinase	475	40
		norvegicus
312	gi202806	Rattus	vasopressin receptor	1578	67
		norvegicus
312	gi11096303	Homo sapiens	NALP1	614	36
312	gi12656105	Homo sapiens	NAC-alpha splice variant	614	36
314	Y69156	Homo sapiens	Peptide HH2040-BF04 comprising domains V,	392	100
			VIA and VIB of protein kinase.
314	Y84322	Homo sapiens	A human cardiovascular system associated protein	125	36
			kinase-3.
314	G02730	Homo sapiens	Human secreted protein, SEQ ID NO: 6811.	116	80
315	gi3327808	Homo sapiens	latent transforming growth factor-beta binding	5211	97
			protein 4S
315	gi2190402	Homo sapiens	latent TGF-beta binding protein-4	4983	93
315	gi3327814	Homo sapiens	latent transforming growth factor-beta binding	3871	99
			protein 4
316	gi6624055	Homo sapiens	similar to ankyrin motif; note: this is probably the	683	100
			ankryin motif gene; h
316	gi1655418	Homo sapiens	ankyrin motif	554	98
316	B28628	Homo sapiens	Human B11Ag1 antigen splice isoform B11C-15.	452	44
317	gi3157494	Homo sapiens	myosin phosphatase targeting/regulatory subunit	536	33
317	gi12642660	Homo sapiens	myosin phosphatase target subunit 2	536	33
317	W71632	Homo sapiens	Human myosin L-chain binding subunit affinity	536	33
			protein.
318	gi1176422	Mus musculus	rhophilin	1817	75
318	B43571	Homo sapiens	Human cancer associated protein sequence SEQ	1278	99
			ID NO: 1016.
318	gi4868350	Drosophila	rhophilin	881	38
		melanogaster
319	gi12654513	Homo sapiens	Similar to block of proliferation 1	3618	100
319	gi1679772	Mus musculus	Bop1	3300	83
319	gi4586061	Arabidopsis	putative WD-40 repeat protein	1435	41
		thaliana
320	gi6907097	Oryza sativa	Similar to Arabidopsis thaliana DNA chromosome	216	37
			4, ESSA I contig fragment No. 6; calcium channel
			protein alpha-1 chain isoform A —rat. (Z97341)
320	gi5123545	Arabidopsis	arginine methyltransferase (pam1)	190	29
		thaliana
320	gi498761	Saccharomyces	YBR0320	186	37
		cerevisiae
321	gi2459833	Rattus	Maxp1	1696	86
		norvegicus
321	gi2997698	Mus musculus	putative ras effector Nore1	1606	82
321	Y94451	Human	965	98
		inflammation
		associated
		protein
322	B45187	Homo sapiens	Human secreted protein sequence encoded by	874	100
			gene 15 SEQ ID NO: 128.
322	B45186	Gene 15 human	441	47
		secreted protein
		homologous
		amino acid
		sequence
322	gi4808585	Homo sapiens	KH type splicing regulatory protein; KSRP	83	42
323	gi10764778	Homo sapiens	phosphoinositol 3-phosphate-binding protein-2	5835	100
323	B32403	Homo sapiens	Human secreted protein sequence encoded by	2040	99
			gene 33 SEQ ID NO: 89.
323	W44864	Homo sapiens	Human TPC2 telomere length and telomerase	649	49
			regulatory protein.
324	gi9651791	Mus musculus	interleukin-1 delta	309	45
324	gi6165413	Mus musculus	IL-1L1 protein	307	47
324	gi7769118	Mus musculus	interleukin-1 homolog 3	307	47
325	gi2447128	Paramecium	contains 10 ankyrin-like repeats; similar to human	278	40
		bursaria	ankyrin, corresponds to Swiss-Prot Accession
		Chlorella virus 1	Number P16157
325	gi3893155	Homo sapiens	ankyrin repeat protein	231	32
325	gi3618345	Homo sapiens	26S proteasome subunit p28	231	32
326	gi3860079	Drosophila	bicoid-interacting protein 4	427	41
		melanogaster
326	gi1072163	Caenorhabditis	similar to protein kinases	389	44
		elegans
326	gi871986	Avena sativa	putative pp70 ribosomal protein S6 kinase	410	40
327	gi11559550	Homo sapiens	dynein axonemal intermediate chain	3183	99
327	gi11493148	Homo sapiens	intermediate dynein chain	3179	99
327	gi927639	Anthocidaris	dynein intermediate chain 3	2152	68
		crassispina
328	gi2565396	Mus musculus	schwannoma-associated protein	359	38
328	W57899	Homo sapiens	Protein of clone CI480_9.	353	43
328	B08441	Homo sapiens	Amino acid sequence of secreted protein clone	353	43
			CI480_9.
329	gi1772658	Rattus	Srg1	2076	95
		norvegicus
329	gi11559313	Halocynthia	synaptotagmin	443	33
		roretzi
329	gi643654	Rattus	synaptotagmin VI	442	36
		norvegicus
330	G03274	Homo sapiens	Human secreted protein, SEQ ID NO: 7355.	424	100
330	gi4099880	Homo sapiens	myosin heavy chain 12	120	29
330	gi3776579	Arabidopsis	Strong similarity to F22O13.22	119	22
		thaliana
331	gi9837385	Takifugu	retinitis pigmentosa GTPase regulator-like protein	278	20
		rubripes
331	gi9837379	Homo sapiens	retinitis pigmentosa GTPase regulator	256	22
331	gi1747	Oryctolagus	trichohyalin	161	41
		cuniculus
332	gi404634	Mus musculus	serine/threonine kinase	407	44
332	gi2738898	Mus musculus	protein kinase	405	43
332	gi992651	Saccharomyces	Gin4p	341	38
		cerevisiae
333	gi2738898	Mus musculus	protein kinase	444	41
333	gi404634	Mus musculus	serine/threonine kinase	442	43
333	gi2632254	Sorghum	serine/threonine kinase	350	33
		bicolor
334	gi6066585	Mus musculus	GCN2 eIF2alpha kinase	6539	91
334	gi10764163	Mus musculus	GCN2beta	6529	90
334	gi10764165	Mus musculus	GCN2gamma	6529	90
335	gi1504010	Homo sapiens	Similar to Mouse TFIIi-associated transactivator	7797	100
			factor p17(GB_RO: MMU11548): Containing
			protein kinase motif
335	gi1932805	Mus musculus	MEK kinase 4b	7233	89
335	gi2352277	Homo sapiens	MAP kinase kinase kinase	6155	96
336	gi1931654	Arabidopsis	BRCA1-associated RING domain protein isolog;	226	41
		thaliana	106935-111081
336	gi4225948	Caenorhabditis	centaurin gamma 1A	243	37
		elegans
336	gi6465806	Arabidopsis	GCN4-complementing protein (GCP1)	226	41
		thaliana
337	gi6088096	Homo sapiens	protein kinase PKNbeta	3912	98
337	gi11493219	Homo sapiens	dJ905H16.1 (protein kinase C-like 2)	1186	60
337	gi914100	Homo sapiens	protein kinase PRK2	1186	60
338	gi6448792	Rattus	activator of G-protein signaling 3	1521	91
		norvegicus
338	gi1408182	Homo sapiens	LGN protein	570	42
338	gi1065449	Caenorhabditis	similar to the postsynaptic membrane 43K protein	191	31
		elegans	from Xenopus (PIR: A60088)
339	gi1177682	Simian T-cell	Rex protein	97	30
		lymphotropic
		virus
339	gi1850850	murine	serine threonine rich glycoprotein	120	26
		herpesvirus 68
339	gi2317953	murid	glycoprotein 150	120	26
		herpesvirus 4
340	gi12005908	Homo sapiens	AD037	507	37
340	Y73381	Homo sapiens	HTRM clone 1877278 protein sequence.	503	37
340	B38475	Homo sapiens	Fragment of human secreted protein encoded by	408	43
			gene 33 clone HACBZ59.
341	gi1789285	Escherichia	putative nucleotide-binding protein	652	47
		coli K12
341	gi12517450	Escherichia	putative nucleotide-binding protein	647	47
		coli O157: H7
341	gi3647204	Escherichia	chromosome arginine transport ATPase	599	47
		coli
342	gi9998950	Homo sapiens	ankyrin repeat-containing protein	3872	100
342	gi12044278	Homo sapiens	krev interaction trapped 1	3864	99
342	gi12044280	Mus musculus	krev interaction trapped 1	3637	93
343	gi12003994	Homo sapiens	membrane-associated guanylate kinase-related	4713	99
			MAGI-3
343	gi12003992	Mus musculus	membrane-associated guanylate kinase-related	4459	94
			MAGI-3
343	gi7650497	Rattus	scaffolding protein SLIPR	4322	92
		norvegicus
344	gi8052233	Homo sapiens	putative ankyrin-repeat containing protein	726	62
344	gi12060822	Homo sapiens	serologically defined breast cancer antigen NY-	305	32
			BR-16
344	gi11321435	Rattus	ankyrin repeat-rich membrane-spanning protein	281	31
		norvegicus
345	gi8052233	Homo sapiens	putative ankyrin-repeat containing protein	1475	67
345	gi12060822	Homo sapiens	serologically defined breast cancer antigen NY-	402	31
			BR-16
345	gi11415014	Rattus	KIDINS220	385	30
		norvegicus
346	gi3930525	Mus musculus	sex-determination protein homolog Fem1a	2585	78
346	gi9187608	Homo sapiens	similar to (NP_034322.1|) sex-determination	1134	69
			protein homolog Fem1a
346	gi3930527	Mus musculus	sex-determination protein homolog Fem1b	510	29
347	gi12274842	Homo sapiens	bA157P1.1.1 (laminin alpha 5)	20092	100
347	gi2599232	Mus musculus	laminin alpha 5 chain	15824	79
347	gi2281044	Homo sapiens	laminin alpha 5 chain	4948	99
348	gi9622151	Homo sapiens	TNF intracellular domain-interacting protein	332	40
348	Y96727	Homo sapiens	Casein kinase II interacting protein 1 (CKIP-1).	332	40
348	gi9622149	Mus musculus	TNF intracellular domain-interacting protein	327	31
349	gi8101585	Mus musculus	testis specific serine kinase-3	1241	90
349	gi2738898	Mus musculus	protein kinase	671	47
349	gi404634	Mus musculus	serine/threonine kinase	661	46
350	G01248	Homo sapiens	Human secreted protein, SEQ ID NO: 5329.	288	100
350	Y83073	Homo sapiens	F-box motif of FBP protein.	65	43
350	gi3293318	Caenorhabditis	leucine-rich repeat protein SOC-2	88	25
		elegans
351	gi9837385	Takifugu	retinitis pigmentosa GTPase regulator-like protein	278	20
		rubripes
351	gi9837379	Homo sapiens	retinitis pigmentosa GTPase regulator	256	22
351	gi1747	Oryctolagus	trichohyalin	161	41
		cuniculus
352	gi1504038	Homo sapiens	similar to human ankyrin 1(S08275)	521	44
352	gi3320122	Rattus	espin	256	33
		norvegicus
352	gi12018147	Chlamydomonas	vegetative cell wall protein gp1	314	29
		reinhardtii
353	gi9502080	Mus musculus	tubby super-family protein	295	35
353	gi9858154	Homo sapiens	tubby super-family protein	295	35
353	gi7176	Dictyostelium	coding region (AA 1-437)	143	26
		discoideum
354	gi404634	Mus musculus	serine/threonine kinase	541	44
354	gi2738898	Mus musculus	protein kinase	525	42
354	gi8101585	Mus musculus	testis specific serine kinase-3	501	41
355	gi35833	Homo sapiens	inducible membrane protein	242	29
355	gi258295	Homo sapiens	C33 antigen = type III integral membrane protein	242	29
355	gi806806	Homo sapiens	cell surface glycoprotein	242	29
356	gi4689229	Rattus	b-tomosyn isoform	2651	68
		norvegicus
356	gi3790389	Rattus	m-tomosyn	2651	68
		norvegicus
356	gi4689231	Rattus	s-tomosyn isoform	2651	68
		norvegicus
357	gi6996558	Mus musculus	myosin X	873	43
357	gi1755049	Bos taurus	myosin X	875	43
357	gi7188794	Homo sapiens	myosin X	862	43
358	gi484296	Rattus	Synaptotagmin III	2965	95
		norvegicus
358	gi1840399	Mus musculus	synaptotagmin 3	2958	95
358	gi1321655	Mus musculus	synaptotagumin III	2947	94
359	gi5757703	Mus musculus	syntrophin-associated serine-threonine protein	3106	49
			kinase
359	gi406058	Mus musculus	protein kinase	2964	65
359	gi6729348	Arabidopsis	IRE homolog 1	764	39
		thaliana
360	gi1666071	Homo sapiens	GAR22 protein	783	57
360	gi12804707	Homo sapiens	GAS2-related on chromosome 22	783	57
360	gi1707491	Homo sapiens	GAR22 protein	774	58
361	gi6066585	Mus musculus	GCN2 eIF2alpha kinase	7782	90
361	gi10764163	Mus musculus	GCN2beta	7772	90
361	gi10764165	Mus musculus	GCN2gamma	7379	90
362	gi286103	Mus musculus	nedd-1 protein	2689	84
362	gi10177570	Arabidopsis	contains similarity to regulatory protein	394	26
		thaliana	Nedd1˜gene_id: K18J17.16
362	gi6979998	Drosophila	putative microtubule severing protein katanin p80	212	27
		melanogaster	subunit
363	gi5410330	Homo sapiens	spindlin	1099	84
363	gi11559844	Homo sapiens	spindlin 1	1091	84
363	gi12061053	Homo sapiens	Spin	1091	84
364	gi2330663	Schizosaccharomyces	coronin-like protein	500	33
		pombe
364	gi7630165	Schizosaccharomyces	WD repeat protein; possible nuclear pore complex	196	26
		pombe	associated
364	gi886024	Thermomonospora	PkwA	197	26
		curvata
365	gi607134	Mus musculus	developmental kinase 1	937	66
365	gi2462302	Gallus gallus	Eph-like receptor tyrosine kinase	927	57
365	gi755568	Rattus	Ehk-3, full length form	937	65
		norvegicus
366	gi49809	Mus musculus	alpha-2 collagen	4206	91
366	gi62877	Gallus gallus	type VI collagen alpha-2 subunit preprotein	3267	74
366	gi62882	Gallus gallus	type VI collagen subunit alpha2	3267	74
367	gi1498250	Dictyostelium	myosin light chain kinase	557	40
		discoideum
367	gi9837341	Homo sapiens	CamKI-like protein kinase	526	39
367	gi406113	Rattus	protein kinase I	522	36
		norvegicus
368	gi12382787	Homo sapiens	OSBP-related protein 6; ORP6	4915	99
368	gi10880973	Homo sapiens	oxysterol binding protein-related protein 3	2720	59
368	gi12382789	Homo sapiens	OSBP-related protein 7; ORP7	1575	58
369	gi4539084	Homo sapiens	GRIP1 protein	4364	100
369	gi1890856	Rattus	AMPA receptor interacting protein GRIP	4220	94
		norvegicus
369	gi4587895	Rattus	glutamate receptor interacting protein 2	1956	59
		norvegicus
370	gi8052233	Homo sapiens	putative ankyrin-repeat containing protein	1755	64
370	gi12060822	Homo sapiens	serologically defined breast cancer antigen NY-	402	31
			BR-16
370	gi11415014	Rattus	KIDINS220	385	30
		norvegicus
371	gi4929729	Homo sapiens	CGI-130 protein	527	92
371	gi12804521	Homo sapiens	Similar to CGI-130 protein	350	100
371	gi1788628	Escherichia	putative alpha helix protein	124	30
		coli K12
372	gi3608372	Rattus	brain specific cortactin-binding protein CBP90	2650	82
		norvegicus
372	gi8980338	Takifugu	FRANK2 protein	1872	33
		rubripes
372	gi2914719	Homo sapiens	match to Z43555 (NID: g572788)	1365	100
373	gi12382789	Homo sapiens	OSBP-related protein 7; ORP7	4473	100
373	gi12382787	Homo sapiens	OSBP-related protein 6; ORP6	1582	58
373	gi10880973	Homo sapiens	oxysterol binding protein-related protein 3	1626	56
374	gi11493840	Homo sapiens	zinc finger protein 106	9818	99
374	gi3372657	Mus musculus	zinc finger protein 106	6212	69
374	gi2772588	Mus musculus	potential grb2 and fyn-binding protein; serine- and	1793	61
			threonine-rich protein
375	gi1200456	Mus musculus	MUS p66 Shc	409	51
375	gi558999	Mus musculus	Shcp52	409	51
375	gi36454	Homo sapiens	SHC transforming protein	407	53
376	gi11546046	Homo sapiens	dJ1100H13.4 (putative RhoGAP domain	562	94
			containing protein)
376	gi3184264	Homo sapiens	F02569_2	127	42
376	gi984749	Mus musculus	RIP1	143	33
377	gi3337443	Homo sapiens	NADH-ubiquinone oxidoreductase NDUFS2	1263	100
			subunit
377	gi12652835	Homo sapiens	NADH dehydrogenase (ubiquinone) Fe-S protein	1263	100
			2 (49 kD) (NADH-coenzyrne Q reductase)
377	Y14555	Homo sapiens	Human NADH dehydrogenase subunit 1 protein.	1263	100
378	gi550013	Homo sapiens	ribosomal protein L5	554	93
378	gi11640568	Homo sapiens	MSTP030	554	93
378	gi57125	Rattus	ribosomal protein L5 (AA 1-297)	548	92
		norvegicus
379	gi2853081	Arabidopsis	ATP binding protein-like	781	59
		thaliana
379	gi9655501	Vibrio cholerae	mrp protein	699	53
379	gi12516326	Escherichia	putative ATPase	690	51
		coli O157:H7
380	gi2706447	Sorex araneus	transthyretin	306	85
380	gi1420	Ovis aries	transthyretin	296	85
380	gi2696504	Bos taurus	transthyretin	287	86
381	gi255248	Saccharomyces	QRI5	77	40
		cerevisiae ,
		Peptide, 111 aa
381	gi544504	Saccharomyces	Qri5p	77	40
		cerevisiae
381	gi33442	Homo sapiens	Ly91 Ig mu heavy chain precursor	64	32
382	gi255248	Saccharomyces	QRI5	77	40
		cerevisiae,
		Peptide, 111 aa
382	gi544504	Saccharomyces	Qri5p	77	40
		cerevisiae
382	gi4579731	Clostridium	NTNH	61	30
		botulinum D
		phage
383	gi12249115	Coprinus	Clp1	71	30
		cinereus
383	Y21090	Homo sapiens	Human p53 cellular tumor antigen mutant protein	62	38
			fragment 27.
383	gi3127111	Hydra vulgaris	protein-tyrosine kinase HTK48	61	33
384	gi12803105	Homo sapiens	nucleobindin 1	1028	75
384	gi1144316	Homo sapiens	nucleobindin	1006	73
384	R49667	Homo sapiens	Human nucleobindin.	999	73
385	B44867	Homo sapiens	Human secreted protein encoded by gene 38.	130	96
385	gi3093373	Mus musculus	SPR2I protein	83	44
385	gi3093367	Mus musculus	SPR2F protein	79	41
386	B44867	Homo sapiens	Human secreted protein encoded by gene 38.	130	96
386	gi643447	Malus x	S3-RNase precursor	77	24
		domestica
386	gi9955513	Arabidopsis	putative protein	76	29
		thaliana
387	gi10934059	Homo sapiens	non-biotin containing subunit of 3-	2923	100
			methylcrotonyl-CoA carboxylase
387	gi12382294	Homo sapiens	3-methylcrotonyl-CoA carboxylase beta subunit	2923	100
387	gi9948017	Pseudomonas	probable acyl-CoA carboxyltransferase beta chain	1854	65
		aeruginosa
388	Y48524	Homo sapiens	Human breast tumor-associated protein 69.	257	100
388	gi4490721	Arabidopsis	squalene epoxidase-like protein	45	58
		thaliana
388	gi535358	Neisseria	Opa15063G	62	42
		gonorrhoeae
389	gi155798	Aplysia sp.	R15-1 neuroactive peptide precursor	46	53
389	gi7959741	Homo sapiens	PRO1051	57	32
389	gi155800	Aplysia sp.	R15-2 neuroactive peptide precursor	46	53
390	gi35071	Homo sapiens	precursor polypeptide (AA-29 to 315)	1749	100
390	gi200071	Mus musculus	methylenetetrahydrofolate dehydrogenase-	1652	92
			methenyltetrahydrofolate cyclohydrolase
390	gi200081	Mus musculus	NAD-dependent methylenetetrahydrofolate	1652	92
			dehydrogenase-methenyltetrahydrofolate
			cyclohydrolase
391	gi3287265	Rattus	E-STOP protein	188	33
		norvegicus
391	gi1370291	Rattus	STOP protein	188	33
		norvegicus
391	gi3171934	Mus musculus	neuronal-STOP protein	186	34
392	gi9957242	Canis familiaris	progesterone receptor	103	32
392	gi2058326	Homo sapiens	subunit of RNA polymerase II transcription factor	95	33
			TFIID
392	gi2290390	Strongyloides	IgG and IgE immunoreactive antigen recognized	83	37
		stercoralis	by sera from patients with strongyloidiasis
393	gi11386113	Homo sapiens	FKSG25	2664	100
393	gi10934047	Mus musculus	Scot-t1	2048	75
393	gi10934052	Mus musculus	Scot-t2	2038	75
394	Y27573	Homo sapiens	Human secreted protein encoded by gene No. 7.	331	46
394	Y31830	Homo sapiens	Human adult brain secreted protein nh899_8.	329	51
394	Y79328	Homo sapiens	Human ligand receptor Lynx2.	106	34
395	gi529225	Caenorhabditis	similar to ZK1236.3	75	23
		elegans
396	W58386	Homo sapiens	Human secreted protein BR595_4.	492	95
396	gi8250239	Homo sapiens	protein phosphatase 4 regulatory subunit 2	302	95
396	gi8468621	Plasmodium	mature parasite-infected erythrocyte surface	127	32
		falciparum	antigen
397	gi11094293	Homo sapiens	brain link protein-1	1869	100
397	B12304	Homo sapiens	Human secreted protein encoded by gene 4 clone	1856	99
			HFXHC41.
397	gi11094297	Rattus	brain link protein-1	1708	91
		norvegicus
398	gi58059	synthetic	BBI(AA 1-72)	57	40
		construct
398	B25671	Homo sapiens	Human secreted protein sequence encoded by	75	30
			gene 7 SEQ ID NO: 60.
398	gi508623	Glycine max	Bowman-Birk protease inhibitor	55	52
399	gi3041877	Homo sapiens	IB3089A	2152	52
399	W70899	Homo sapiens	Protein encoded by tumor suppressor gene	2152	52
			IB3089A.
399	Y44704	Homo sapiens	Human tumor suppressor protein IB3089A.	2152	52
400	G03576	Homo sapiens	Human secreted protein, SEQ ID NO: 7657.	153	53
400	gi8650491	porcine	198R	64	35
		adenovirus 3
400	gi643439	Pneumocystis	major surface glycoprotein	85	48
		carinii
401	gi7248902	Gallus gallus	NOELIN-2	1618	64
401	gi442368	Rattus	neuronal olfactomedin-related ER localized	1614	64
		norvegicus	protein
401	gi3218528	Mus musculus	pancortin-3	1610	64
402	gi442370	Rattus	neuronal olfactomedin-related ER localized	1744	66
		norvegicus	protein
402	gi7211681	Gallus gallus	neuronal olfactomedin-related ER localized	1743	65
			protein
402	gi3218524	Mus musculus	pancortin-1	1740	66
403	V28845_aa1	Homo sapiens	13-SEP-1996 Human coxsackievirus and	372	34
			adenovirus receptor encoding DNA.
403	gi1881447	Homo sapiens	coxsackie and adenovirus receptor protein	368	34
403	gi1946351	Homo sapiens	cell surface protein HCAR	368	34
404	B12127	Homo sapiens	Hydrophobic domain protein isolated from HT-	2437	97
			1080 cells.
404	gi7573504	Drosophila	TEP2 protein	510	30
		melanogaster
404	gi7573506	Drosophila	TEP3 protein	445	27
		melanogaster
405	gi5901808	Drosophila	BcDNA.GH03694	839	48
		melanogaster
405	gi9502156	Arabidopsis	contains similarity to Drosophila melanogaster	308	30
		thaliana	BcDNA.GH03694 (GB: AAD55412)
405	gi6850839	Arabidopsis	putative protein	248	28
		thaliana
406	gi310102	Rattus	elongation factor G	1218	89
		norvegicus
406	gi4895248	Arabidopsis	putative mitochondrial translation elongation	776	66
		thaliana	factor G
406	gi12321017	Arabidopsis	mitochondrial elongation factor, putative	774	65
		thaliana
407	Y76143	Homo sapiens	Human secreted protein encoded by gene 20.	1380	98
407	B44778	Homo sapiens	Human secreted protein sequence encoded by	62	27
			gene 17 SEQ IDNO: 77.
407	gi3093324	Myxine	ATPase 8	39	60
		glutinosa
408	gi10716074	Mus musculus	M83 protein	315	33
408	Y52590	Homo sapiens	Human prostate growth-associated membrane	285	30
			protein PGAMP-2.
408	gi10716072	Homo sapiens	M83 protein	290	31
409	gi10303605	Homo sapiens	CYP4F11	2804	99
409	gi4519535	Homo sapiens	Leukotriene B4 omega-hydroxylase	2459	86
409	gi1857022	Homo sapiens	leukotriene B4 omega-hydroxylase	2454	86
410	Y54321	Homo sapiens	A polypeptide designated ACRP30R1L which is a	489	43
			homologue of ACRP30.
410	B30232	Homo sapiens	Human adipocyte complement related protein	489	43
			homologue zacrp2.
410	gi687606	Lepomis	saccular collagen	488	44
		macrochirus
411	gi687606	Lepomis	saccular collagen	418	44
		macrochirus
411	gi30054	Homo sapiens	alpha1 (III) collagen	424	48
411	gi164896	Oryctolagus	alpha-1 (VIII) collagen precursor	383	49
		cuniculus
412	gi177179	Homo sapiens	alpha-2 type VIII collagen	606	45
412	gi264	Bos taurus	type X collagen	593	42
412	gi4225951	Homo sapiens	collagen X	586	42
413	gi687606	Lepomis	saccular collagen	411	44
		macrochirus
413	gi164896	Oryctolagus	alpha-1 (VIII) collagen precursor	387	50
		cuniculus
413	gi50481	Mus musculus	alpha 1 (X) collagen chain	362	46
414	gi506431	Homo sapiens	lysosomal acid lipase	1150	53
414	gi434306	Homo sapiens	sterol esterase	1148	53
414	gi460143	Homo sapiens	lysosomal acid lipase/cholesteryl ester hydrolase	1148	53
415	B08899	Homo sapiens	Human secreted protein sequence encoded by	2602	99
			gene 9 SEQ ID NO: 56.
415	gi7331693	Caenorhabditis	contains similarity to TR: Q22863	301	27
		elegans
415	gi7320695	Caenorhabditis	Y116F11B.7	307	28
		elegans
416	W81030	Homo sapiens	Melanoma associated antigen MG50.	204	32
416	gi1504040	Homo sapiens	similar to D. melanogaster peroxidasin(U11052)	203	32
416	gi6273399	Homo sapiens	melanoma-associated antigen MG50	203	32
417	gi178284	Homo sapiens	alpha-2-HS-glycoprotein	1161	91
417	gi7106502	Homo sapiens	alpha2-HS glycoprotein	1161	91
417	W61492	Homo sapiens	Human fetuin glycoprotein type 2.	1161	91
418	gi178284	Homo sapiens	alpha-2-HS-glycoprotein	1806	100
418	gi7106502	Homo sapiens	alpha2-HS glycoprotein	1806	100
418	W61492	Homo sapiens	Human fetuin glycoprotein type 2.	1806	100
419	gi178284	Homo sapiens	alpha-2-HS-glycoprotein	1602	98
419	gi7106502	Homo sapiens	alpha2-HS glycoprotein	1602	98
419	W61492	Homo sapiens	Human fetuin glycoprotein type 2.	1602	98
420	gi5123855	Mus musculus	very-long-chain Acyl-CoA dehydrogenase	1362	48
420	gi2765125	Mus musculus	very-long-chain acyl-CoA dehydrogenase	1362	48
420	gi559722	Rattus	very-long-chain Acyl-CoA dehydrogenase	1354	47
		norvegicus
421	gi11125672	Homo sapiens	dJ591C20.1 (novel protein similar to mouse	2511	100
			NG26)
421	gi4337103	Homo sapiens	BAT5	1147	63
421	Y91669	Homo sapiens	Human secreted protein sequence encoded by	1147	63
			gene 73 SEQ ID NO: 342.
422	gi10732648	Homo sapiens	angiopoietin-like protein PP1158	1021	96
422	Y54496	Homo sapiens	Human muscle angiopoietin-like growth factor	1021	96
			protein sequence.
422	Y86289	Homo sapiens	Human secreted protein HDRMI82, SEQ ID	1021	96
			NO: 204.
423	gi467671	Homo sapiens	ZN-alpha-2-glycoprotein	754	91
423	gi38026	Homo sapiens	Zn-alpha2-glycoprotein	754	91
423	gi340442	Homo sapiens	Zn-alpha-2-glycoprotein	754	91
424	gi9864185	Drosophila	Crossveinless 2	930	36
		melanogaster
424	gi7768636	Xenopus laevis	Kielin	672	29
424	gi3649748	Mus musculus	IgG Fc binding protein	367	30
425	B00073	Homo sapiens	Human lysyl oxidase related protein (Lor)-2.	2286	99
425	A47799_aa1	Homo sapiens	27-JAN-1999 Human lysyl oxidase related protein	2286	99
			(Lor)-2 cDNA (CDS).
425	B12307	Homo sapiens	Human secreted protein encoded by gene 7 clone	2279	99
			HAMFE82.
426	B18927	Homo sapiens	A novel polypeptide designated PRO6030.	1549	100
426	Y73431	Homo sapiens	Human secreted protein clone yb186_1 protein	1169	100
			sequence SEQ ID NO: 84.
426	gi3169566	Drosophila	faint sausage	126	29
		melanogaster
427	gi189772	Homo sapiens	prostaglandin D2 synthase	561	95
427	Y71471	Homo sapiens	Human prostaglandin D2 synthase (PD2	561	95
			synthase).
427	gi6178152	Macaca fuscata	prostaglandin D synthase	520	89
428	B24476	Homo sapiens	Human secreted protein sequence encoded by	1302	77
			gene 40 SEQ ID NO: 101.
428	gi5816699	Canis familiaris	D4 dopamine receptor	97	38
428	gi11559408	Canis familiaris	dopamine receptor D4	97	37
429	B15563	Homo sapiens	Fragment of apoptosis related protein encoded by	46	37
			gene 4 clone HEGAL46.
429	gi5458572	Pyrococcus	LSU ribosomal protein L34E	65	40
		abyssi
429	W87504	Homo sapiens	Human N-methyl-D-aspartate receptor subunit	70	31
			encoded by clone NMDA24.
430	Y36120	Homo sapiens	Extended human secreted protein sequence, SEQ	78	46
			ID NO: 505.
430	Y27854	Homo sapiens	Human secreted protein encoded by gene No. 101.	65	39
430	W88627	Homo sapiens	Secreted protein encoded by gene 94 clone	63	38
			HPMBQ32.
431	gi4826463	Homo sapiens	dJ287G14.1 (exon of a yet unidentified gene, or	620	99
			part of a psendogene?; similar to parts of BMP and
			Tolloid proteins)
431	G00601	Homo sapiens	Human secreted protein, SEQ ID NO: 4682.	426	97
431	gi619861	Homo sapiens	bone morphogenetic protein	202	35
432	gi11225238	Homo sapiens	cytochrome P450 subfamily IIIA polypeptide 43	2624	99
432	gi12642642	Homo sapiens	cytochrome P450 CYP3A43	2624	99
432	gi11225240	Homo sapiens	cytochrome P450 subfamily IIIA polypeptide 43	2615	99
433	Q89844_aa1	Homo sapiens	12-OCT-1993 Human death associated protein	1838	90
			DAP-7, also called cathepsin D.
433	V60292_aa1	Homo sapiens	03-MAR-1997 DNA sequence encoding death	1838	90
			associated protein (DAP)-7 (cathepsin D).
433	X87255_aa1	Homo sapiens	20-NOV-1998 cDNA clone encoding human	1838	90
			PRO292 (cathepsin D)
434	G01648	Homo sapiens	Human secreted protein, SEQ ID NO: 5729.	281	100
434	Y13398	Homo sapiens	Amino acid sequence of protein PRO346.	272	31
434	gi50369	Mus musculus	precursor protein (AA-34 to 244)	184	30
435	gi3168604	Homo sapiens	proline and glutamic acid rich nuclear protein	5107	98
			isoform
435	W31186	Homo sapiens	Human p160 polypeptide 160.2.	4723	98
435	W31185	Homo sapiens	Human p160 polypeptide 160.1.	2948	99
436	Y99357	Homo sapiens	Human PRO1190 (UNQ604) amino acid sequence	650	99
			SEQ ID NO: 58.
436	Y27574	Homo sapiens	Human secreted protein encoded by gene No. 8.	602	98
436	W52289	Homo sapiens	Homo sapiens cdo tumor suppressor protein.	184	43
437	gi10799172	Homo sapiens	uterine-derived 14 kDa protein	742	100
437	Y38388	Homo sapiens	Human secreted protein encoded by gene No. 3.	72	29
437	gi6957462	Homo sapiens	dJ159A19.3 (novel protein)	81	35
438	Y02692	Homo sapiens	Human secreted protein encoded by gene 43 clone	461	87
			HTADX17.
438	gi10197717	Homo sapiens	cell-surface molecule Ly-9	86	38
438	G00272	Homo sapiens	Human secreted protein, SEQ ID NO: 4353.	86	38
439	W59874	Homo sapiens	Amino acid sequence of the cDNA clone CAT-1	454	96
			(HTXET53).
439	Y08326	Homo sapiens	Human granulysin P522 active fragment.	454	96
439	gi35065	Homo sapiens	NKG5 product	222	93
440	gi6572165	Homo sapiens	dJ1119A7.5 (novel protein (isoform 2))	546	99
440	gi6572166	Homo sapiens	dJ1119A7.5 (novel protein (isoform 1))	283	100
440	gi10178387	Streptomyces	putative monooxygenase	110	27
		coelicolor
441	B23602	Homo sapiens	Human secreted protein SEQ ID NO: 4.	1754	98
441	Y52389	Homo sapiens	Human transmembrane protein HP02219.	887	100
441	gi1065948	Caenorhabditis	similar to thymidine diphosphoglucose 4,6-	1281	67
		elegans	dehydratase
442	Y27621	Homo sapiens	Human secreted protein encoded by gene No. 55.	441	46
442	gi3983152	Mus musculus	schlafen3	133	31
442	gi3983162	Mus musculus	schlafen4	119	29
443	gi4235144	Homo sapiens	BC39498_1	1452	65
443	gi9802037	Homo sapiens	zinc finger protein SBZF3	1396	61
443	gi1017722	Homo sapiens	repressor transcriptional factor	1366	62
444	gi11493481	Homo sapiens	PRO2474	433	100
444	gi1171608	Plasmodium	rps7	67	38
		falciparum
444	gi10038818	Buchnera sp.	glycyl-tRNA synthetase beta chain	65	38
		APS
445	gi6841740	Homo sapiens	T-cell receptor beta chain	55	62
445	gi222640	Strawberry	24 K protein	60	55
		mild yellow
		edge-associated
		virus
445	gi847913	Mus musculus	T cell receptor Vb14/Jb1.6 beta chain	54	62
446	gi12751092	Homo sapiens	PNAS-123	346	100
446	gi408899	Mus musculus	serum amyloid A protein	46	58
446	gi1644360	Mus musculus	serum amyloid A 5	46	58
447	gi8886935	Arabidopsis	F2D10.27	97	24
		thaliana
447	gi1129158	Saccharomyces	J1575L	81	22
		cerevisiae
447	gi1022328	Myxococcus	Four tandem repeats of a DNA-binding domain	89	34
		xanthus	known as the AT-hook are found at the carboxy
			terminus of CarD. This protein has been purified
			and found to bind in vitro to a promoter region
448	Y07896	Homo sapiens	Human secreted protein fragment encoded from	66	31
			gene 45.
448	Y94967	Homo sapiens	Human secreted protein clone au36_42 protein	64	28
			sequence SEQ ID NO: 140.
448	gi9280539	Hepatitis B	surface antigen	41	63
		virus
449	Y19743	Homo sapiens	SEQ ID NO 461 from WO9922243.	972	99
449	Y19541	Homo sapiens	Amino acid sequence of a human secreted protein.	265	100
449	Y19745	Homo sapiens	SEQ ID NO 463 from WO9922243.	145	100
450	gi186774	Homo sapiens	zinc finger protein	1557	51
450	gi10440398	Homo sapiens	FLJ00032 protein	1739	58
450	gi2739353	Homo sapiens	ZNF91L	1497	50
451	gi8920230	Homo sapiens	Spir-1 protein	66	32
451	gi9968169	Human	gp120	55	30
		immunodeficiency
		virus type 1
452	G02783	Homo sapiens	Human secreted protein, SEQ ID NO: 6864.	344	100
452	gi167684	Dictyostelium	cAMP receptor	56	35
		discoideum
452	gi265734	Dictyostelium,	cAMP receptor subtype 3	62	27
		Peptide, 490 aa
453	gi11493502	Homo sapiens	PRO3102	545	100
453	gi6822268	Mus musculus	CIP7	81	36
453	W61601	Homo sapiens	Human metallothionein HMBP-I.	73	27
454	G02139	Homo sapiens	Human secreted protein, SEQ ID NO: 6220.	287	98
454	gi6448725	Streptomyces	putative oxidoreductase	67	38
		coelicolor
		A3(2)
454	gi1486421	Rhizobium sp.	OppC homologue	66	34
455	G01003	Homo sapiens	Human secreted protein, SEQ ID NO: 5084.	112	40
455	gi12407427	Mus musculus	tripartite motif protein TRIM13	108	36
455	gi8217434	Homo sapiens	bA67K19.2 (zinc-finger protein HT2A (72 kD	129	32
			TAT-interacting protein))
456	gi12584159	Homo sapiens	zinc finger protein 268	891	54
456	gi4567178	Homo sapiens	R31665_2	900	45
456	gi498152	Homo sapiens	ha0946 protein is Kruppel-related.	900	52
457	G00579	Homo sapiens	Human secreted protein, SEQ ID NO: 4660.	254	94
457	gi5295832	Homo sapiens	dJ21O18.2 (protein similar to collagen)	48	37
457	gi6526769	Homo sapiens	HRIHFB2003	48	37
458	gi213862	Oncorhynchus	alpha-tubulin	407	91
		mykiss
458	gi202212	Mus musculus	alpha-tubulin isotype M-alpha-6	407	91
458	gi2843123	Homo sapiens	alpha tubulin	407	91
459	gi532688	Homo sapiens	thrombospondin-p50	292	97
459	W40287	Homo sapiens	Human TSP1 protein.	134	50
459	Y06182	Homo sapiens	Thrombospondin I fragment.	134	50
460	gi9885325	Homo sapiens	XAGE-1	796	100
460	Y83169	Homo sapiens	PAGE3 polypeptide.	65	51
460	Y83167	Homo sapiens	PAGE1 polypeptide.	62	52
461	gi12044051	Homo sapiens	ELOVL4	1712	99
461	gi12044041	Mus musculus	Elovl4	1595	92
461	gi8101521	Mus musculus	SSC2	682	45
462	gi159725	Octopus	alpha tubulin	274	77
		dofleini
462	gi10242166	Notothenia	alpha tubulin	269	74
		coriiceps
462	gi2098753	Gecarcinus	alpha-2-tubulin	271	75
		lateralis
463	gi12314165	Homo sapiens	bA526D8.4 (novel KRAB box containing C2H2	4537	100
			type zinc finger protein)
463	gi5679576	Homo sapiens	zinc finger 41	2357	61
463	gi340444	Homo sapiens	zinc finger protein 41	2082	69
464	gi10696977	Homo sapiens	bA6J24.2 (A putative novel protein)	388	88
464	gi11127941	Lotus	chalcone reductase	52	31
		corniculatus
465	gi12655452	Homo sapiens	keratin associated protein 4.7	506	43
465	gi12655456	Homo sapiens	keratin associated protein 4.9	486	44
465	gi12655460	Homo sapiens	keratin associated protein 4.12	486	42
466	gi6467206	Homo sapiens	gonadotropin inducible transcription repressor-4	1172	56
466	gi487785	Homo sapiens	zinc finger protein ZNF136	1149	57
466	gi3953593	Mus musculus	Zinc finger protein s11-6	1031	51
467	gi12314284	Homo sapiens	dJ353C17.1 (novel protein)	628	99
467	gi8651	Drosophila	structural sperm protein	42	75
		melanogaster
467	W71565	Homo sapiens	Hepatocyte nuclear factor 4 alpha polypeptide	57	43
			(exon 2 product).
468	gi11493560	Homo sapiens	PRO2730	711	100
468	W74873	Homo sapiens	Human secreted protein encoded by gene 145	531	100
			clone HFXHL79.
468	B34691	Homo sapiens	Human secreted protein encoded by DNA clone	490	100
			vp16 1.
469	gi189498	Homo sapiens	pyrroline-5-carboxylate reductase	496	83
469	G03518	Homo sapiens	Human secreted protein, SEQ ID NO: 7599.	302	76
469	gi4960118	Homo sapiens	pyrroline-5-carboxylate reductase isoform	229	52
470	gi2689443	Homo sapiens	R28830_2	3075	100
470	gi9968290	Homo sapiens	zinc finger protein 304	1624	51
470	gi1020145	Homo sapiens	DNA binding protein	1412	53
471	gi1167849	Homo sapiens	NAD (H)-specific isocitrate dehydrogenase	1984	97
			gamma subunit precursor
471	gi1673432	Homo sapiens	NAD(H)-specific isocitrate dehydrogenase	1984	97
			gamma-subunit precursor
471	gi4096803	Homo sapiens	NAD+-specific isocitrate dehydrogenase gamma	1984	97
			subunit precursor
472	gi7459861	Homo sapiens	Zinc finger protein ZNF45	845	35
472	gi1160977	Homo sapiens	zinc finger protein	842	35
472	gi6984172	Homo sapiens	zinc finger protein ZNF226	819	36
473	gi11074	Drosophila	Mst84Db	66	37
		melanogaster
473	B44778	Homo sapiens	Human secreted protein sequence encoded by	62	32
			gene 17 SEQ ID NO: 77.
473	gi6642750	Homo sapiens	PRO0806	59	44
474	gi9802037	Homo sapiens	zinc finger protein SBZF3	2576	99
474	gi4235144	Homo sapiens	BC39498_1	1456	61
474	gi1017722	Homo sapiens	repressor transcriptional factor	1380	57
475	B21040	Homo sapiens	Human nucleic acid-binding protein, NuABP-44.	2479	99
475	gi5757625	Homo sapiens	C2H2 zinc finger protein	1270	47
475	gi3294544	Homo sapiens	C2H2-type zinc finger protein	1270	47
476	gi12655452	Homo sapiens	keratin associated protein 4.7	537	41
476	gi12655460	Homo sapiens	keratin associated protein 4.12	522	43
476	gi12655464	Homo sapiens	keratin associated protein 4.15	485	42
477	Y86431	Homo sapiens	Human gene 35-encoded protein fragment, SEQ	230	94
			ID NO: 346.
477	Y86430	Homo sapiens	Human gene 35-encoded protein fragment, SEQ	154	91
			ID NO: 345.
477	gi4007683	Streptomyces	putative transcriptional regulator	85	30
		coelicolor
		A3(2)
478	Y14426	Homo sapiens	Human secreted protein encoded by gene 16 clone	222	100
			HSAVP17.
478	Y14481	Homo sapiens	Fragment of human secreted protein encoded by	79	100
			gene 16.
478	B27647	Homo sapiens	Human secreted protein BLAST search protein	56	40
			SEQ ID NO: 148.
479	gi12407395	Homo sapiens	tripartite motif protein TRIM7	1169	100
479	gi12407397	Mus musculus	tripartite motif protein TRIM7	916	84
479	gi563127	Homo sapiens	acid finger protein	280	34
480	gi6467206	Homo sapiens	gonadotropin inducible transcription repressor-4	1363	54
480	Y58627	Homo sapiens	Protein regulating gene expression PRGE-20.	1382	48
480	B52154	Homo sapiens	Human secreted protein BLAST search protein	1300	53
			SEQ ID NO: 110.
481	gi1504006	Homo sapiens	similarto human ZFY protein.	720	43
481	gi7638237	Homo sapiens	mesenchymal stem cell protein DSC43	212	27
481	B03946	Homo sapiens	Human mesenchymal stem cell polypeptide.	212	27
482	G03930	Homo sapiens	Human secreted protein, SEQ ID NO: 8011.	97	50
482	gi3116064	Squalus	s-sgk1	93	44
		acanthias
482	gi3116066	Squalus	s-sgk2	92	27
		acanthias
483	B12318	Homo sapiens	Human secreted protein encoded by gene 18 clone	494	96
			HE2FL70.
483	gi2827286	Homo sapiens	novel antagonist of FGF signaling	73	36
483	W48795	Homo sapiens	Homo sapiens sprouty 3 protein.	73	36
484	R23732	Homo sapiens	Gene 519 cDNA derived peptide.	327	69
484	gi35065	Homo sapiens	NKG5 product	325	67
484	W59874	Homo sapiens	Amino acid sequence of the cDNA clone CAT-1	325	67
			(HTXET53).
485	gi607028	Homo sapiens	putative	201	31
485	gi529680	Rattus	rARL1	200	31
		norvegicus
485	gi506475	Rattus	ARF-like protein 1	200	31
		norvegicus
486	gi388319	Homo sapiens	CACCC box-binding protein	324	49
486	gi1724124	Mus musculus	transcription factor BFCOL1	324	49
486	gi2760486	Mus musculus	G-rich box-binding protein	324	49
487	gi514215	Chlamydomonas	dynein beta heavy chain	200	23
		reinhardtii
487	gi2772561	Homo sapiens	similar to ciliary dynein beta heavy chain; 78%	183	24
			Similarity to P23098 (PID: g118965)
487	gi6007859	Chlamydomonas	dynein heavy chain alpha	188	27
		reinhardtii
488	Y58627	Homo sapiens	Protein regulating gene expression PRGE-20.	1004	44
488	gi3135968	Homo sapiens	b34I8. 1 (Kruppel related Zinc Finger protein 184)	823	42
488	gi1769491	Homo sapiens	kruppel-related zinc finger protein	807	41

[0471]

TABLE 3
SEQ	Accession
ID NO:	Number	Description	Results*
245	BL01159	WW/rsp5/WWP domain proteins.	BL01159 13.85 3.755e−10 101-116
246	PR00450	RECOVERIN FAMILY SIGNATURE	PR00450C 12.22 1.818e−12 236-258
247	PR00659	CHROMOGRANIN SIGNATURE	PR00659B 13.09 9.746e−09 539-555
248	BL00115	Eukaryotic RNA polymerase II	BL00115Z 3.12 4.176e−09 312-361
		heptapeptide repeat proteins.
249	BL00904	Protein prenyltransferases alpha subunit	BL00904A 8.30 1.574e−09 628-678
		repeat proteins proteins.
250	PR00489	FRIZZLED PROTEIN SIGNATURE	PR00489C 9.29 2.250e−28 398-423
			PR00489E 9.95 4.808e−25 486-509
			PR00489G 8.99 6.478e−25 585-606
			PR00489B 13.69 4.273e−24 308-331
			PR00489A 11.81 7.353e−24 280-303
			PR00489D 15.68 2.703e−22 441-465
			PR00489F 14.55 1.675e−21 529-551
251	PR00315	GTP-BINDING ELONGATION	PR00315A 11.81 8.000e−14 70-84
		FACTOR SIGNATURE	PR00315C 13.85 3.250e−12 137-148
253	PF00614	Phospholipase D. Active site proteins	PF00614B 14.45 3.294e−09 200-220
		motifs.
254	BL50002	Src homology 3 (SH3) domain proteins	BL50002A 14.19 4.750e−12 332-351
		profile.
256	BL50002	Src homology 3 (SH3) domain proteins	BL50002B 15.18 5.200e−10 693-707
		profile.
258	PD00930	PROTEIN GTPASE DOMAIN	PD00930B 33.72 2.098e−20 137-178
		ACTIVATION.
259	BL00107	Protein kinases ATP-binding region	BL00107B 13.31 1.000e−14 329-345
		proteins.
260	BL00790	Receptor tyrosine kinase class V proteins.	BL00790B 21.59 1.000e−40 62-114
			BL00790C 16.65 1.000e−40 166-220
			BL00790E 29.58 1.000e−40 276-324
			BL00790G 22.06 1.000e−40 379-423
			BL00790J 14.21 1.000e−40 603-643
			BL00790K 9.30 1.000e−40 655-709
			BL00790O 7.68 1.000e−40 795-828
			BL00790R 16.20 1.000e−40 891-935
			BL00790N 13.25 7.618e−33 761-788
			BL00790I 20.01 4.094e−28 504-535
			BL00790D 12.41 2.125e−27 246-271
			BL00790H 13.42 2.957e−27 458-484
			BL00790M 8.74 3.483e−27 739-761
			BL00790L 11.16 2.350e−25 719-739
			BL00790F 15.90 6.143e−25 342-369
			BL00790A 19.74 2.688e−18 32-54
			BL00790P 12.33 1.261e−16 828-853
261	BL00471	Small cytokines (intercrine/chemokine)	BL00471 23.92 1.000e−40 72-120
		C-x-C subfamily signat.
262	PD00126	PROTEIN REPEAT DOMAIN TPR	PD00126A 22.53 3.483e−09 87-108
		NUCLEA.
263	PR00360	C2 DOMAIN SIGNATURE	PR00360A 14.59 8.839e−10 57-70
			PR00360B 13.61 3.455e−09 82-96
264	PR00499	NEUTROPHIL CYTOSOL FACTOR 2	PR00499D 10.18 1.875e−12 269-290
		SIGNATURE
265	BL01160	Kinesin light chain repeat proteins.	BL01160F 9.68 8.161e−21 399-440
			BL01160F 9.68 6.243e−17 291-332
			BL01160E 8.74 6.938e−17 484-523
			BL01160E 8.74 5.140e−16 442-481
			BL01160E 8.74 7.300e−16 400-439
			BL01160E 8.74 3.972e−14 250-289
			BL01160E 8.74 5.075e−14 526-565
			BL01160F 9.68 2.017e−13 483-524
			BL01160F 9.68 4.913e−13 249-290
			BL01160F 9.68 6.009e−13 525-566
			BL01160E 8.74 7.300e−13 292-331
			BL01160C 2.94 1.354e−12 366-413
			BL01160G 13.67 2.948e−12 398-425
			BL01160F 9.68 6.067e−12 441-482
			BL01160F 9.68 6.748e−12 357-398
			BL01160G 13.67 1.089e−11 248-275
			BL01160G 13.67 4.653e−11 524-551
			BL01160C 2.94 7.614e−11 258-305
			BL01160E 8.74 9.773e−11 358-397
			BL01160G 13.67 4.600e−10 440-467
			BL01160C 2.94 4.971e−10 450-497
			BL01160I 12.96 7.165e−10 525-573
			BL01160I 12.96 9.575e−10 441-489
			BL01160C 2.94 1.503e−09 492-539
			BL01160G 13.67 4.436e−09 356-383
			BL01160G 13.67 5.909e−09 482-509
			BL01160I 12.96 8.241e−09 399-447
			BL01160I 12.96 9.797e−09 483-531
266	PF00646	F-box domain proteins.	PF00646A 14.37 3.893e−10 75-89
269	PF00642	Zinc finger C-x8-C-x5-C-x3-H type (and	PF00642 11.59 4.673e−10 312-323
		similar).
270	PR00109	TYROSINE KINASE CATALYTIC	PR00109B 12.27 5.059e−12 1198-1217
		DOMAIN SIGNATURE
271	BL00107	Protein kinases ATP-binding region	BL00107A 18.39 8.650e−17 356-387
		proteins.
272	BL00678	Trp-Asp (WD) repeat proteins proteins.	BL00678 9.67 8.615e−11 1038-1049
			BL00678 9.67 9.400e−10 1338-1349
			BL00678 9.67 1.474e−09 952-963
			BL00678 9.67 3.842e−09 1177-1188
			BL00678 9.67 6.684e−09 1380-1391
273	BL00678	Trp-Asp (WD) repeat proteins proteins.	BL00678 9.67 8.615e−11 711-722
			BL00678 9.67 9.400e−10 1011-1022
			BL00678 9.67 1.474e−09 625-636
			BL00678 9.67 3.842e−09 850-861
			BL00678 9.67 6.684e−09 1053-1064
274	BL01290	Enhancer of rudimentary proteins.	BL01290B 17.01 4.231e−39 39-79
			BL01290A 11.13 6.226e−19 21-50
276	BL00678	Trp-Asp (WD) repeat proteins proteins.	BL00678 9.67 3.769e−11 134-145
278	PR00449	TRANSFORMING PROTEIN P21 RAS	PR00449A 13.20 9.206e−14 5-27
		SIGNATURE	PR00449D 10.79 6.276e−10 119-133
280	PF00791	Domain present in ZO-1 and Unc5-like	PF00791B 28.49 9.053e−12 821-876
		netrin receptors.
281	PF00791	Domain present in ZO-1 and Unc5-like	PF00791B 28.49 9.053e−12 773-828
		netrin receptors.
282	PF00791	Domain present in ZO-1 and Unc5-like	PF00791B 28.49 9.053e−12 796-851
		netrin receptors.
286	BL00107	Protein kinases ATP-binding region	BL00107A 18.39 1.000e−23 262-293
		proteins.	BL00107B 13.31 1.692e−12 328-344
287	PR00450	RECOVERIN FAMILY SIGNATURE	PR00450C 12.22 6.280e−10 370-392
290	BL00720	Guanine-nucleotide dissociation	BL00720B 16.57 9.419e−17 156-180
		stimulators CDC25 family sign.
291	PF00566	Probable rabGAP domain proteins.	PF00566A 12.64 7.333e−10 547-557
292	PR00449	TRANSFORMING PROTEIN P21 RAS	PR00449A 13.20 5.846e−21 12-34
		SIGNATURE	PR00449E 13.50 6.684e−17 118-141
			PR00449D 10.79 3.368e−13 83-97
			PR00449B 14.34 5.500e−13 35-52
293	PR00109	TYROSINE KINASE CATALYTIC	PR00109B 12.27 2.068e−10 396-415
		DOMAIN SIGNATURE
294	DM01970	0 kw ZK632.12 YDR313C	DM01970B 8.60 3.898e−15 477-490
		ENDOSOMAL III.
295	PF00791	Domain present in ZO-1 and Unc5-like	PF00791C 20.98 1.222e−14 423-462
		netrin receptors.	PF00791D 20.37 7.476e−14 466-509
			PF00791A 27.85 9.308e−13 74-129
297	BL00678	Trp-Asp (WD) repeat proteins proteins.	BL00678 9.67 1.947e−09 398-409
298	BL00678	Trp-Asp (WD) repeat proteins proteins.	BL00678 9.67 1.947e−09 366-377
299	PR00308	TYPE I ANTIFREEZE PROTEIN	PR00308B 4.28 2.075e−10 39-51
		SIGNATURE	PR00308C 3.83 9.182e−09 39-49
300	BL00434	HSF-type DNA-binding domain proteins.	BL00434C 23.85 6.556e−09 128-168
302	PR00048	C2H2-TYPE ZINC FINGER	PR00048A 10.52 1.000e−12 337-351
		SIGNATURE
303	PD00126	PROTEIN REPEAT DOMAIN TPR	PD00126A 22.53 3.423e−10 92-113
		NUCLEA.	PD00126A 22.53 8.448e−09 160-181
304	PR00049	WILM'S TUMOR PROTEIN	PR00049D 0.00 3.898e−09 75-90
		SIGNATURE
305	BL01187	Calcium-binding EGF-like domain	BL01187B 12.04 7.300e−14 198-214
		proteins pattern proteins.
307	BL00479	Phorbol esters/diacylglycerol binding	BL00479A 19.86 5.091e−12 841-864
		domain proteins.	BL00479B 12.57 1.837e−11 865-881
308	BL00678	Trp-Asp (WD) repeat proteins proteins.	BL00678 9.67 9.308e−11 109-120
309	BL01187	Calcium-binding EGF-like domain	BL01187B 12.04 6.250e−17 563-579
		proteins pattern proteins.
311	PR00109	TYROSINE KINASE CATALYTIC	PR00109B 12.27 7.706e−12 88-107
		DOMAIN SIGNATURE
312	PR00918	CALICIVIRUS NON-STRUCTURAL	PR00918A 13.76 4.923e−11 192-213
		POLYPROTEIN FAMILY SIGNATURE
314	PR00109	TYROSINE KINASE CATALYTIC	PR00109B 12.27 5.255e−11 410-429
		DOMAIN SIGNATURE
315	DM00215	PROLINE-RICH PROTEIN 3.	DM00215 19.43 7.107e−10 1229-1262
316	PF00791	Domain present in ZO-1 and Unc5-like	PF00791C 20.98 1.614e−12 217-256
		netrin receptors.	PF00791B 28.49 4.320e−10 203-258
317	PR00806	VINCULIN SIGNATURE	PR00806B 4.28 2.440e−09 393-407
318	PR00834	HTRA/DEGQ PROTEASE FAMILY	PR00834F 10.91 6.700e−10 547-560
		SIGNATURE
319	PR00320	G-PROTEIN BETA WD-40 REPEAT	PR00320A 16.74 1.000e−11 428-443
		SIGNATURE	PR00320C 13.01 4.522e−11 428-443
			PR00320B 12.19 9.710e−11 428-443
321	BL00479	Phorbol esters/diacylglycerol binding	BL00479B 12.57 1.931e−13 145-161
		domain proteins.
323	BL01159	WW/rsp5/WWP domain proteins.	BL01159 13.85 6.510e−10 27-42
324	PR00264	INTERLEUKIN-1 SIGNATURE	PR00264B 20.98 8.453e−11 77-104
			PR00264C 17.77 1.851e−10 117-146
325	PF00791	Domain present in ZO-1 and Unc5-like	PF00791B 28.49 4.727e−11 97-152
		netrin receptors.
326	PR00109	TYROSINE KINASE CATALYTIC	PR00109B 12.27 5.582e−11 219-238
		DOMAIN SIGNATURE
327	PR00320	G-PROTEIN BETA WD-40 REPEAT	PR00320C 13.01 3.160e−10 280-295
		SIGNATURE	PR00320A 16.74 5.765e−10 280-295
329	PF00168	C2 domain proteins.	PF00168C 27.49 8.941e−13 362-388
331	BL00303	S-100/ICaBP type calcium binding	BL00303A 21.77 7.375e−16 137-174
		protein.	BL00303B 26.15 8.676e−09 183-220
332	PR00109	TYROSINE KINASE CATALYTIC	PR00109B 12.27 8.116e−14 62-81
		DOMAIN SIGNATURE
333	PR00109	TYROSINE KINASE CATALYTIC	PR00109B 12.27 8.116e−14 62-81
		DOMAIN SIGNATURE
334	BL00107	Protein kinases ATP-binding region	BL00107A 18.39 6.625e−21 567-598
		proteins.	BL00107A 18.39 1.783e−14 144-175
335	BL00107	Protein kinases ATP-binding region	BL00107A 18.39 8.412e−20 1403-1434
		proteins.	BL00107B 13.31 9.308e−12
			1475-1491
336	PR00405	HIV REV INTERACTING PROTEIN	PR00405A 17.71 4.396e−13 184-204
		SIGNATURE	PR00405B 11.83 9.842e−11 203-221
337	BL00107	Protein Kinases ATP-binding region	BL00107A 18.39 3.813e−21 549-580
		proteins.	BL00107B 13.31 1.692e−12 614-630
338	PR00377	INOSITOL	PR00377C 11.91 3.388e−10 593-608
		PHOSPHATASE/FRUCTOSE-1,6-
		BISPHOSPHATASE FAMILY
		SIGNATURE
341	PR00449	TRANSFORMING PROTEIN P21 RAS	PR00449A 13.20 1.466e−09 144-166
		SIGNATURE
342	PF00023	Ank repeat proteins.	PF00023A 16.03 8.875e−10 359-375
343	PD00289	PROTEIN SH3 DOMAIN REPEAT	PD00289 9.97 3.160e−10 837-851
		PRESYNA.
344	PD00078	REPEAT PROTEIN ANK NUCLEAR	PD00078B 13.14 9.550e−10 400-413
		ANKYR.
345	PD00078	REPEAT PROTEIN ANK NUCLEAR	PD00078B 13.14 9.550e−10 400-413
		ANKYR.	PD00078B 13.14 2.174e−09 466-479
346	PD00078	REPEAT PROTEIN ANK NUCLEAR	PD00078B 13.14 5.950e−10 714-727
		ANKYR.
347	BL00790	Receptor tyrosine kinase class V proteins.	BL00790E 29.58 7.964e−11 526-574
349	BL00107	Protein kinases ATP-binding region	BL00107B 13.31 5.154e−12 190-206
		proteins.	BL00107A 18.39 8.759e−11 124-155
351	BL00303	S-100/ICaBP type calcium binding	BL00303A 21.77 7.375e−16 3-40
		protein.	BL00303B 26.15 8.676e−09 49-86
352	BL00790	Receptor tyrosine kinase class V proteins.	BL00790R 16.20 6.400e−12 579-623
			BL00790R 16.20 1.536e−11 509-553
353	PR00750	BETA-AMYLASE (GLYCOSYL	PR00750F 13.15 9.620e−09 201-218
		HYDROLASE FAMILY 14)
		SIGNATURE
354	PR00109	TYROSINE KINASE CATALYTIC	PR00109B 12.27 8.116e−14 138-157
		DOMAIN SIGNATURE
355	PR00259	TRANSMEMBRANE FOUR FAMILY	PR00259A 9.27 9.100e−12 12-36
		SIGNATURE	PR00259C 16.40 7.164e−10 80-109
356	PR00319	BETA G-PROTEIN (TRANSDUCIN)	PR00319B 11.47 4.714e−09 126-141
		SIGNATURE
358	PF00168	C2 domain proteins.	PF00168C 27.49 1.643e−15 475-501
359	PR00109	TYROSINE KINASE CATALYTIC	PR00109B 12.27 6.362e−13 492-511
		DOMAIN SIGNATURE
360	PR00563	BETA-3 ADRENERGIC RECEPTOR	PR00563E 7.48 3.084e−09 180-199
		SIGNATURE
361	BL00107	Protein kinases ATP-binding region	BL00107A 18.39 2.200e−22 838-869
		proteins.	BL00107A 18.39 1.783e−14 415-446
362	PR00320	G-PROTEIN BETA WD-40 REPEAT	PR00320C 13.01 7.652e−11 58-73
		SIGNATURE	PR00320B 12.19 2.543e−10 58-73
			PR00320A 16.74 5.765e−10 58-73
			PR00320B 12.19 6.400e−09 144-159
			PR00320A 16.74 8.683e−09 144-159
364	PR00319	BETA G-PROTEIN (TRANSDUCIN)	PR00319A 15.27 3.803e−09 187-204
		SIGNATURE
365	BL00107	Protein kinases ATP-binding region	BL00107B 13.31 2.636e−13 663-679
		proteins.	BL00107A 18.39 9.280e−13 597-628
366	PR00453	VON WILLEBRAND FACTOR TYPE	PR00453A 12.79 6.684e−17 614-632
		A DOMAIN SIGNATURE	PR00453B 14.65 4.545e−12 659-674
			PR00453C 12.26 9.000e−09 726-735
367	PR00109	TYROSINE KINASE CATALYTIC	PR00109B 12.27 6.651e−14 187-206
		DOMAIN SIGNATURE
368	BL01013	Oxysterol-binding protein family	BL01013D 26.81 6.081e−18 850-894
		proteins.	BL01013A 25.14 1.148e−17 580-616
			BL01013C 9.97 4.231e−13 668-678
			BL01013B 11.33 3.017e−11 646-657
369	PF00595	PDZ domain proteins (Also known as	PF00595 13.40 1.600e−09 502-513
		DHR or GLGF).
370	PD00078	REPEAT PROTEIN ANK NUCLEAR	PD00078B 13.14 9.550e−10 978-991
		ANKYR.	PD00078B 13.14 2.174e−09 1044-1057
371	PD00301	PROTEIN REPEAT MUSCLE	PD00301B 5.49 4.115e−09 95-106
		CALCIUM-BI.
372	PF00791	Domain present in ZO-1 and Unc5-like	PF00791B 28.49 8.261e−14 748-803
		netrin receptors.	PF00791B 28.49 1.364e−11 814-869
			PF00791C 20.98 4.913e−11 795-834
			PF00791C 20.98 3.029e−09 762-801
			PF00791B 28.49 3.477e−09 715-770
373	BL01013	Oxysterol-binding protein family	BL01013A 25.14 1.500e−20 488-524
		proteins.	BL01013D 26.81 6.516e−18 758-802
			BL01013C 9.97 1.000e−13 576-586
			BL01013B 11.33 3.017e−11 554-565
375	PR00401	SH2 DOMAIN SIGNATURE	PR00401B 12.94 8.200e−11 143-154
			PR00401A 14.00 3.025e−09 126-141
376	PD00930	PROTEIN GTPASE DOMAIN	PD00930A 25.62 6.523e−13 113-139
		ACTIVATION.
377	BL00535	Respiratory chain NADH dehydrogenase	BL00535A 22.06 1.000e−40 86-141
		49 Kd subunit proteins.	BL00535C 22.70 5.345e−40 190-236
			BL00535D 27.70 1.818e−39 245-293
			BL00535E 14.99 4.150e−33 298-330
			BL00535F 19.62 5.500e−33 371-408
			BL00535B 22.59 6.000e−28 156-190
378	PR00058	RIBOSOMAL PROTEIN L5	PR00058F 8.67 6.400e−28 60-81
		SIGNATURE
379	BL01215	Mrp family proteins.	BL01215C 18.97 5.154e−35 154-196
			BL01215D 30.07 6.308e−31 210-260
			BL01215A 9.75 6.400e−25 66-93
			BL01215B 9.34 6.860e−12 101-114
380	PR00189	TRANSTHYRETIN SIGNATURE	PR00189C 10.36 1.692e−39 72-102
			PR00189D 5.14 1.000e−28 102-125
			PR00189A 10.47 1.310e−26 31-52
387	PD01307	LIGASE CARBOXYLASE ACETYL-	PD01307B 24.35 7.750e−25 383-427
		COENZY.
390	BL00766	Tetrahydrofolate	BL00766B 24.49 1.000e−40 108-156
		dehydrogenase/cyclohydrolase proteins.	BL00766E 13.78 1.000e−40 288-325
			BL00766C 25.86 5.500e−39 174-222
			BL00766D 17.05 4.536e−26 249-279
			BL00766A 21.48 6.063e−24 68-98
393	BL01273	CoA transferases proteins.	BL01273C 12.54 1.000e−40 130-170
			BL01273D 19.11 9.750e−37 206-250
			BL01273B 14.85 9.830e−20 81-115
			BL01273A 12.56 2.286e−16 62-75
394	BL00272	Snake toxins proteins.	BL00272C 8.27 8.953e−09 117-129
397	BL01241	Link domain proteins.	BL01241 35.81 1.237e−37 165-218
			BL01241 35.81 5.974e−15 261-314
399	BL00279	Membrane attack complex components/	BL00279C 31.64 6.063e−09 108-162
		perforin proteins.
404	BL00477	Alpha-2-macroglobulin family thiolester	BL00477A 13.50 9.690e−18 131-160
		region proteins.	BL00477C 15.70 9.538e−14 246-263
			BL00477B 9.05 9.250e−13 219-232
406	BL01176	Initiation factor 2 proteins.	BL01176B 8.74 6.380e−13 116-154
407	DM01554	1 THYROLIBERIN PRECURSOR.	DM01554A 6.07 6.118e−09 1-11
409	BL00086	Cytochrome P450 cysteine heme-iron	BL00086 20.87 2.588e−23 458-490
		ligand proteins.
410	PR00007	COMPLEMENT C1Q DOMAIN	PR00007C 15.60 2.000e−16 240-262
		SIGNATURE	PR00007B 14.16 1.771e−15 196-216
			PR00007A 19.33 4.064e−13 169-196
			PR00007D 9.64 4.349e−09 275-286
411	PR00007	COMPLEMENT C1Q DOMAIN	PR00007C 15.60 3.631e−09 258-280
		SIGNATURE
412	PR00007	COMPLEMENT C1Q DOMAIN	PR00007C 15.60 2.000e−16 285-307
		SIGNATURE	PR00007B 14.16 1.771e−15 241-261
			PR00007A 19.33 9.143e−15 214-241
			PR00007D 9.64 4.349e−09 320-331
413	PR00007	COMPLEMENT C1Q DOMAIN	PR00007C 15.60 2.000e−16 258-280
		SIGNATURE	PR00007D 9.64 4.349e−09 293-304
415	PD01066	PROTEIN ZINC FINGER ZINC-	PD01066 19.43 3.739e−19 280-319
		FINGER METAL-BINDING NU.
416	PR00019	LEUCINE-RICH REPEAT	PR00019A 11.19 4.667e−09 185-199
		SIGNATURE	PR00019A 11.19 6.667e−09 111-125
			PR00019B 11.36 1.000e−08 182-196
417	BL01254	Fetuin family proteins.	BL01254B 14.36 1.000e−40 78-124
			BL01254D 16.81 1.000e−40 158-205
			BL01254A 14.53 1.000e−39 32-69
			BL01254E 13.25 3.250e−28 292-321
			BL01254C 13.84 7.648e−18 107-158
			BL01254F 10.02 2.440e−13 340-350
418	BL01254	Fetuin family proteins.	BL01254B 14.36 1.000e−40 78-124
			BL01254C 13.84 1.000e−40 125-176
			BL01254D 16.81 1.000e−40 176-223
			BL01254A 14.53 1.000e−39 32-69
			BL01254E 13.25 1.659e−24 310-339
			BL01254F 10.02 2.440e−13 340-350
419	BL01254	Fetuin family proteins.	BL01254B 14.36 1.000e−40 60-106
			BL01254C 13.84 1.000e−40 107-158
			BL01254D 16.81 1.000e−40 158-205
			BL01254E 13.25 3.250e−28 292-321
			BL01254F 10.02 2.440e−13 340-350
			BL01254A 14.53 5.133e−11 32-69
420	BL00072	Acyl-CoA dehydrogenases proteins.	BL00072C 25.30 8.425e−27 253-294
			BL00072E 24.12 3.600e−24 396-439
			BL00072D 30.08 5.105e−20 307-358
			BL00072B 9.48 1.600e−16 205-218
			BL00072A 12.45 6.786e−11 104-115
422	BL00514	Fibrinogen beta and gamma chains C-	BL00514C 17.41 4.414e−23 175-212
		terminal domain proteins.	BL00514G 15.98 1.000e−14 302-332
			BL00514H 14.95 7.545e−13 337-362
			BL00514D 15.35 3.118e−11 216-229
423	BL00290	Immunoglobulins and major	BL00290B 13.17 1.500e−12 230-248
		histocompatibility complex proteins.	BL00290A 20.89 1.900e−12 174-197
424	PF00094	von Willebrand factor type D domain	PF00094B 10.43 6.400e−17 491-509
		proteins.
425	BL00420	Speract receptor repeat proteins domain	BL00420B 22.67 5.500e−29 311-366
		proteins.	BL00420B 22.67 5.442e−24 49-104
			BL00420C 11.90 7.840e−13 134-145
			BL00420B 22.67 3.972e−12 180-235
			BL00420C 11.90 8.017e−11 396-407
426	PD02327	GLYCOPROTEIN ANTIGEN	PD02327B 19.84 3.864e−09 51-73
		PRECURSOR IMMUNOGLO.
427	PR00179	LIPOCALIN SIGNATURE	PR00179A 13.78 5.680e−10 37-50
432	BL00086	Cytochrome P450 cysteine heme-iron	BL00086 20.87 9.500e−22 432-464
		ligand proteins.
433	PR00792	PEPSIN (A1) ASPARTIC PROTEASE	PR00792A 11.54 4.273e−24 113-134
		FAMILY SIGNATURE	PR00792D 12.74 5.000e−17 411-427
			PR00792C 9.10 1.000e−11 320-332
			PR00792B 12.78 4.682e−11 271-285
435	PR00211	GLUTELIN SIGNATURE	PR00211B 0.86 5.413e−10 682-703
			PR00211B 0.86 3.167e−09 688-709
439	PR00343	SELECTIN SUPERFAMILY	PR00343A 13.78 9.578e−09 72-92
		COMPLEMENT-BINDING REPEAT
		SIGNATURE
440	BL00982	Bacterial-type phytoene dehydrogenase	BL00982A 18.41 8.644e−13 34-66
		proteins.
441	DM00934	kw DIHYDROFLAVONOL YOL151W	DM00934A 20.07 5.784e−09 98-146
		YDR541C YGL157W.
443	PD01066	PROTEIN ZINC FINGER ZINC-	PD01066 19.43 3.182e−36 10-49
		FINGER METAL-BINDING NU.
450	PD01066	PROTEIN ZINC FINGER ZINC-	PD01066 19.43 1.667e−40 10-49
		FINGER METAL-BINDING NU.
456	PD01066	PROTEIN ZINC FINGER ZINC-	PD01066 19.43 3.531e−37 45-84
		FINGER METAL-BINDING NU.
458	BL00227	Tubulin subunits alpha, beta, and gamma	BL00227A 24.55 4.536e−31 10-44
		proteins.
459	BL01208	VWFC domain proteins.	BL01208B 15.83 5.235e−14 3-18
461	BL01188	GNS1/SUR4 family proteins.	BL01188C 22.65 5.333e−10 169-220
			BL01188D 8.62 1.247e−09 254-271
462	BL00227	Tubulin subunits alpha, beta, and gamma	BL00227A 24.55 5.135e−26 17-51
		proteins.
463	PD00066	PROTEIN ZINC-FINGER METAL-	PD00066 13.92 4.600e−14 674-687
		BINDI.	PD00066 13.92 5.200e−14 702-715
			PD00066 13.92 5.800e−14 394-407
			PD00066 13.92 5.800e−14 562-575
			PD00066 13.92 6.400e−14 478-491
			PD00066 13.92 6.400e−14 618-631
			PD00066 13.92 1.500e−13 366-379
			PD00066 13.92 5.000e−13 590-603
			PD00066 13.92 7.000e−13 730-743
			PD00066 13.92 1.000e−12 450-463
			PD00066 13.92 2.286e−12 534-547
			PD00066 13.92 5.286e−12 758-771
			PD00066 13.92 8.962e−10 422-435
465	PD02283	PROTEIN SPORULATION REPEAT	PD02283C 17.54 4.713e−09 98-126
		PRECU.
466	PD01066	PROTEIN ZINC FINGER ZINC-	PD01066 19.43 3.750e−35 6-45
		FINGER METAL-BINDING NU.
469	BL00521	Delta 1-pyrroline-5-carboxylate reductase	BL00521A 10.16 3.919e−11 3-19
		proteins.	BL00521B 10.93 6.400e−11 62-74
470	PD01066	PROTEIN ZINC FINGER ZINC-	PD01066 19.43 6.200e−30 105-144
		FINGER METAL-BINDING NU.
471	BL00470	Isocitrate and isopropylmalate	BL00470D 21.75 8.500e−13 269-300
		dehydrogenases proteins.	BL00470C 15.43 4.375e−11 162-177
			BL00470A 16.25 6.077e−11 57-78
472	PD01066	PROTEIN ZINC FINGER ZINC-	PD01066 19.43 1.305e−23 10-49
		FINGER METAL-BINDING NU.
474	PD01066	PROTEIN ZINC FINGER ZINC-	PD01066 19.43 1.844e−37 6-45
		FINGER METAL-BINDING NU.
475	PD01066	PROTEIN ZINC FINGER ZINC-	PD01066 19.43 4.000e−30 16-55
		FINGER METAL-BINDING NU.
476	BL01208	VWFC domain proteins.	BL01208B 15.83 4.162e−09 199-214
479	BL00518	Zinc finger, C3HC4 type (RING finger),	BL00518 12.23 5.800e−11 44-53
		proteins.
480	PD01066	PROTEIN ZINC FINGER ZINC-	PD01066 19.43 4.255e−29 6-45
		FINGER METAL-BINDING NU.
481	BL00028	Zinc finger, C2H2 type, domain proteins.	BL00028 16.07 4.300e−10 583-600
485	BL01019	ADP-ribosylation factors family proteins.	BL01019B 19.49 5.970e−17 80-135
486	PD00066	PROTEIN ZINC-FINGER METAL-	PD00066 13.92 2.200e−14 147-160
		BINDI.	PD00066 13.92 6.087e−11 119-132
488	PD01066	PROTEIN ZINC FINGER ZINC-	PD01066 19.43 7.600e−30 6-45
		FINGER METAL-BINDING NU.
*Results include in order: accession number subtype; raw score; p-value; position of signature in amino acid sequence

[0472]

TABLE 4
SEQ ID				Pfam
NO:	Pfam Model	Description	e-value	Score
245	WW	WW domain	4.9e−08	40.1
246	efhand	EF hand	0.0023	24.6
248	PC_rep	Proteasome/cyclosome repeat	0.00016	28.5
249	PH	PH domain	2.8e−15	59.6
250	Frizzled	Frizzled/Smoothened family membrane region	7.6e−226	758.6
251	GTP_EFTU	Elongation factor Tu family	9.5e−103	354.8
252	ThiJ	ThiJ/PfpI family	2.1e−54	194.2
253	PLDc	Phospholipase D. Active site motif	0.0098	22.5
254	SH3	SH3 domain	6.8e−20	79.5
255	Synuclein	Synuclein	1.8e−77	270.8
256	RhoGAP	RhoGAP domain	3.3e−39	143.7
257	ThiJ	ThiJ/PfpI family	6.1e−45	162.7
258	RhoGAP	RhoGAP domain	5.3e−47	169.6
259	pkinase	Eukaryotic protein kinase domain	3.2e−94	326.5
260	EPH_lbd	Ephrin receptor ligand binding domain	1.1e−140	480.7
261	IL8	Small cytokines (intecrine/chemokine), interleukin-8 like	3.7e−36	124.9
262	TPR	TPR Domain	9.4e−07	35.9
263	C2	C2 domain	4e−18	73.7
264	SH3	SH3 domain	2.9e−22	87.4
265	TPR	TPR Domain	1.1e−38	141.9
266	F-box	F-box domain.	0.004	23.8
267	PH	PH domain	2.5e−22	84.4
268	DEP	Domain found in Dishevelled, Egl-10, and Pleckstrin	7e−22	86.1
270	pkinase	Eukaryotic protein kinase domain	5.9e−81	282.4
271	pkinase	Eukaryotic protein kinase domain	2.1e−30	113.6
272	NB-ARC	NB-ARC domain	8e−112	384.9
273	NB-ARC	NB-ARC domain	8e−112	384.9
274	ER	Enhancer of rudimentary	2.3e−59	210.6
275	PH	PH domain	4.5e−10	40.9
276	WD40	WD domain, G-beta repeat	6.3e−06	33.1
277	RhoGAP	RhoGAP domain	3e−24	94.0
278	ras	Ras family	1.2e−12	7.0
279	START	START domain	0.00075	24.2
280	ank	Ank repeat	4.7e−19	76.7
281	ank	Ank repeat	4.7e−19	76.7
282	ank	Ank repeat	4.7e−19	76.7
283	SH3	SH3 domain	0.00011	26.4
284	TPR	TPR Domain	3.7e−11	50.5
285	IRS	PTB domain (IRS-1 type)	6.1e−19	76.4
286	pkinase	Eukaryotic protein kinase domain	1.6e−94	327.5
287	efhand	EF hand	2.9e−06	34.2
288	RasGEF	RasGEF domain	0.00021	−30.8
289	C2	C2 domain	0.002	23.4
290	RasGEF	RasGEF domain	6.2e−30	112.9
291	TBC	TBC domain	1.1e−42	155.2
292	ras	Ras family	1.2e−65	231.5
293	pkinase	Eukaryotic protein kinase domain	1.5e−71	251.1
294	RhoGEF	RhoGEF domain	6.5e−63	222.4
295	PDZ	PDZ domain (Also known as DHR or GLGF).	3.4e−50	180.2
296	PDZ	PDZ domain (Also known as DHR or GLGF).	0.034	15.5
297	WD40	WD domain, G-beta repeat	7.8e−10	46.1
298	WD40	WD domain, G-beta repeat	7.8e−10	46.1
299	C2	C2 domain	1.2e−11	52.1
300	DIX	DIX domain	3.9e−22	87.0
301	PH	PH domain	0.025	13.4
302	calponin	Calponin family	7.2e−17	59.4
303	TPR	TPR Domain	1.7e−29	111.4
304	zf-MYND	MYND finger	8.3e−11	49.3
305	EGF	EGF-like domain	4.8e−35	129.8
306	ank	Ank repeat	0.00097	25.9
307	PDZ	PDZ domain (Also known as DHR or GLGF).	7.7e−10	46.1
308	WD40	WD domain, G-beta repeat	5.9e−22	86.4
309	CUB	CUB domain	9.8e−186	630.4
310	PH	PH domain	6.8e−17	65.1
311	pkinase	Eukaryotic protein kinase domain	4.1e−61	216.5
312	PAAD_DAPIN		8.5e−09	42.7
313	cyclin	Cyclin	9.9e−18	65.7
314	pkinase	Eukaryotic protein kinase domain	4.1e−09	36.8
315	EGF	EGF-like domain	9.1e−81	281.7
316	ank	Ank repeat	2.4e−42	154.1
317	ank	Ank repeat	3.6e−39	143.5
318	HR1	Hr1 repeat motif	5.5e−17	69.9
319	WD40	WD domain, G-beta repeat	1.7e−25	98.1
320	TPR	TPR Domain	0.011	22.4
321	RA	Ras association (Ra1GDS/AF-6) domain	2.7e−26	100.8
322	PX	PX domain	1.5e−19	78.4
323	PH	PH domain	1.9e−21	81.3
324	IL1	Interleukin 10	2.5e−22	83.4
325	ank	Ank repeat	2.6e−38	140.7
326	pkinase	Eukaryotic protein kinase domain	1.1e−53	191.7
327	WD40	WD domain, G-beta repeat	4.7e−08	40.2
328	PLDc	Phospholipase D. Active site motif	1.3e−05	32.1
329	C2	C2 domain	9e−21	82.4
330	IQ	IQ calmodulin-binding motif	1.1e−12	55.5
331	S_100	S-100/ICaBP type calcium binding domain	5.6e−08	39.9
332	pkinase	Eukaryotic protein kinase domain	2.2e−48	174.2
333	pkinase	Eukaryotic protein kinase domain	6.9e−56	199.1
334	pkinase	Eukaryotic protein kinase domain	4.1e−79	276.3
335	pkinase	Eukaryotic protein kinase domain	6.8e−81	282.2
336	ArfGap	Putative GTP-ase activating protein for Arf	1.3e−30	115.2
337	pkinase	Eukaryotic protein kinase domain	2.4e−72	253.8
338	GoLoco	LGN motif, putative GEF specific for G-alpha GTPase	8.8e−45	162.2
339	PH	PH domain	2.3e−13	52.6
340	RA	Ras association (Ra1GDS/AF-6) domain	2.4e−09	44.5
342	Band_41	FERM domain (Band 4.1 family)	0.0023	13.0
343	PDZ	PDZ domain (Also known as DHR or GLGF).	5.7e−65	229.3
344	ank	Ank repeat	4.9e−42	153.1
345	ank	Ank repeat	3.3e−68	240.0
346	ank	Ank repeat	2.3e−44	160.8
347	laminin_EGF	Laminin EGF-like (Domains III and V)	1.2e−215	729.8
348	PH	PH domain	2.2e−12	49.1
349	pkinase	Eukaryotic protein kinase domain	1.9e−80	280.7
350	F-box	F-box domain.	0.0022	24.7
351	S_100	S-100/ICaBP type calcium binding domain	5.6e−08	39.9
352	ank	Ank repeat	3.2e−45	163.7
353	WD40	WD domain, G-beta repeat	0.00031	27.5
354	pkinase	Eukaryotic protein kinase domain	8.8e−67	235.3
355	transmembrane 4	Transmembrane 4 family	1.4e−28	94.4
356	WD40	WDdomain, G-beta repeat	4.2e−15	63.6
357	MyTH4	Domain in Myosin and Kinesin Tails	7.8e−15	62.7
358	C2	C2 domain	5.4e−87	302.4
359	pkinase	Eukaryotic protein kinase domain	1.5e−73	257.8
360	GAS2	Growth-Arrest-Specific Protein 2 Domain	6.4e−44	159.3
361	pkinase	Eukaryotic protein kinase domain	7.8e−81	282.0
362	WD40	WD domain, G-beta repeat	3.9e−15	63.7
363	Spin-Ssty		1.1e−163	557.2
364	WD40	WD domain, G-beta repeat	7.2e−16	66.2
365	EPH_1bd	Ephrin receptor ligand binding domain	1.7e−119	410.4
366	Collagen	Collagen triple helix repeat (20 copies)	2.2e−62	220.7
367	pkinase	Eukaryotic protein kinase domain	4e−84	292.9
368	Oxysterol_BP	Oxysterol-binding protein	8.6e−77	268.5
369	PDZ	PDZ domain (Also known as DHR or GLGF).	4e−68	239.8
370	ank	Ank repeat	2.8e−52	187.1
371	HD	HD domain	0.00025	27.8
372	ank	Ank repeat	6.2e−36	132.8
373	Oxysterol_BP	Oxysterol-binding protein	1.6e−65	231.1
374	WD40	WD domain, G-beta repeat	4.2e−32	120.1
375	SH2	Src homology domain 2	8.9e−27	80.8
376	RhoGAP	RhoGAP domain	0.0097	−18.5
377	complex1_49 Kd	Respiratory-chain NADH dehydrogenase, 49 Kd subunit	3e−220	612.0
379	fer4_NifH	4Fe-4S iron sulfur cluster binding proteins, NifH/frxC	0.0013	16.1
		family
380	Transthyretin	Transthyretin precursor (formerly prealbumin)	6.4e−83	277.2
387	Carboxyl_trans	Carboxyl transferase domain	4e−209	708.1
390	THF_DHG_CYH	Tetrahydrofolate dehydrogenase/cyclohydrolase	6.4e−177	601.1
393	CoA_trans	Coenzyme A transferase	6.1e−192	651.0
395	Agglutinin	Lectin (probable mannose binding)	0.0015	11.4
397	Xlink	Extracellular link domain	7.1e−121	280.3
401	OLF	Olfactomedin-like domain	1.4e−120	414.0
402	OLF	Olfactomedin-like domain	1.4e−120	414.0
403	ig	Immunoglobulin domain	6e−13	46.8
404	A2M_N	Alpha-2-macroglobulin family N-terminal region	2.7e−42	145.3
406	GTP_EFTU	Elongation factor Tu family	2.1e−69	236.6
409	p450	Cytochrome P450	3.2e−141	482.6
410	C1q	C1q domain	3.1e−38	140.5
411	Collagen	Collagen triple helix repeat (20 copies)	3.9e−24	93.6
412	C1q	C1q domain	8.8e−42	152.2
413	Collagen	Collagen triple helix repeat (20 copies)	3.4e−23	90.5
414	abhydrolase	alpha/beta hydrolase fold	1.2e−12	55.5
415	KRAB	KRAB box	7.6e−14	59.4
416	LRR	Leucine Rich Repeat	1e−14	62.3
417	cystatin	Cystatin domain	2.1e−52	183.9
418	cystatin	Cystatin domain	4.2e−55	193.2
419	cystatin	Cystatin domain	1.5e−41	146.8
421	abhydrolase	alpha/beta hydrolase fold	0.0026	10.4
422	fibrinogen_C	Fibrinogen beta and gamma chains, C-terminal globular	5.4e−49	171.7
		domain
423	MHC_I	Class I Histocompatibility antigen, domains alpha 1 and 2	1.3e−57	204.8
424	vwd	von Willebrand factor type D domain	1.6e−37	134.9
425	SRCR	Scavenger receptor cysteine-rich domain	5.2e−69	242.7
427	lipocalin	Lipocalin/cytosolic fatty-acid binding protein family	2.6e−11	43.1
431	CUB	CUB domain	1.9e−32	121.2
432	p450	Cytochrome P450	8.3e−155	527.7
433	asp	Eukaryotic aspartyl protease	5.5e−183	621.3
434	ig	Immunoglobulin domain	6.4e−09	33.8
436	ig	Immunoglobulin domain	3.9e−07	28.0
440	pyr_redox	Pyridine nucleotide-disulphide oxidoreductase	0.00077	15.7
441	Epimerase	NAD dependent epimerase/dehydratase family	2.2e−43	157.6
443	zf-C2H2	Zinc finger, C2H2 type	2.3e−47	170.8
450	zf-C2H2	Zinc finger, C2H2 type	5.2e−113	388.8
455	zf-C3HC4	Zinc finger, C3HC4 type (RING finger)	0.025	11.8
456	zf-C2H2	Zinc finger, C2H2 type	9.6e−77	268.4
458	tubulin	Tubulin/FtsZ family	7.9e−40	145.7
461	GNS1_SUR4	GNS1/SUR4 family	1.1e−08	−37.4
462	tubulin	Tubulin/FtsZ family	7.2e−20	79.4
463	zf-C2H2	Zinc finger, C2H2 type	1.4e−127	437.2
465	Keratin_B2	Keratin, high sulfur B2 protein	1.2e−05	8.8
466	zf-C2H2	Zinc finger, C2H2 type	1.1e−51	185.1
469	P5CR	Delta 1-pyrroline-5-carboxylate reductase	5.5e−05	−62.2
470	zf-C2H2	Zinc finger, C2H2 type	1.8e−100	347.2
471	isodh	Isocitrate and isopropylmalate dehydrogenases	1.6e−85	288.4
472	zf-C2H2	Zinc finger, C2H2 type	6.5e−29	109.5
474	zf-C2H2	Zinc finger, C2H2 type	5e−51	183.0
475	zf-C2H2	Zinc finger, C2H2 type	1.4e−91	317.7
476	Keratin_B2	Keratin, high sulfur B2 protein	6.3e−07	28.6
479	zf-B_box	B-box zinc finger.	6.7e−15	62.9
480	zf-C2H2	Zinc finger, C2H2 type	2.3e−73	257.2
481	zf-C2H2	Zinc finger, C2H2 type	2.5e−24	94.2
485	arf	ADP-ribosylation factor family	7.8e−09	−4.2
486	zf-C2H2	Zinc finger, C2H2 type	4.9e−11	50.1
488	zf-C2H2	Zinc finger, C2H2 type	5.3e−56	199.5

[0473]

TABLE 5
SEQ ID								SeqFold
NO:	PDB ID	Chain ID	Start AA	End AA	PSI BLAST	Verify score	PMF score	score	Compound	PDB Annotation
246	1aui	B	183	331	5.20E−16	−0.06	0.25		“SERINE/THREONINE	“HYDROLASE CALCINEURIN;
									PHOSPHATASE 2B; CHAIN:	HYDROLASE, PHOSPHATASE,
									A, B;”	IMMUNOSUPPRESSION”
246	1aui	B	21	146	0.00039	0.27	0.46		“SERINE/THREONINE	“HYDROLASE CALCINEURIN;
									PHOSPHATASE 2B; CHAIN:	HYDROLASE, PHOSPHATASE,
									A, B;”	IMMUNOSUPPRESSION”
246	1aui	B	183	351	5.20E−16			60.79	“SERINE/THREONINE	“HYDROLASE CALCINEURIN;
									PHOSPHATASE 2B; CHAIN:	HYDROLASE, PHOSPHATASE,
									A, B;”	IMMUNOSUPPRESSION”
246	1bjf	A	183	331	2.60E−16	0.14	0.87		“NEUROCALCIN DELTA;	“CALCIUM-BINDING CALCIUM-BINDING,
									CHAIN: A, B;”	MYRISTOYLATION, NEURONAL SPECIFIC
										GUANYLATE 2 CYCLASE ACTIVATOR”
246	1bjf	A	21	146	6.50E−05	0.19	0.7		“NEUROCALCIN DELTA;	“CALCIUM-BINDING CALCIUM-BINDING,
									CHAIN: A, B;”	MYRISTOYLATION, NEURONAL SPECIFIC
										GUANYLATE 2 CYCLASE ACTIVATOR”
246	1bjf	A	174	350	2.60E−16			73.38	“NEUROCALCIN DELTA;	“CALCIUM-BINDING CALCIUM-BINDING,
									CHAIN: A, B;”	MYRISTOYLATION, NEURONAL SPECIFIC
										GUANYLATE 2 CYCLASE ACTIVATOR”
246	1cll		21	146	0.0039	−0.11	0.49			CALCIUM-BINDING PROTEIN
										CALMODULIN (VERTEBRATE) 1CLL 3
246	1cmf		93	146	0.0078	0.55	1		CALMODULIN	CALCIUM-BINDING PROTEIN
									(VERTEBRATE); 1CMF 6	CALMODULIN APO TR2C-DOMAIN; 1CMF 9
									CHAIN: NULL; 1CMF 7
246	1dgv	A	11	129	0.0039	−0.28	0.16		APO CIB; CHAIN: A	“BLOOD CLOTTING HELICAL, EF-HAND,
										BLOOD CLOTTING”
246	1eg3	A	80	150	0.00078	0.64	0.9		DYSTROPHIN; CHAIN: A;	“STRUCTURAL PROTEIN EF-HAND LIKE
										DOMAIN, WW DOMAIN”
246	1exr	A	21	148	0.0013	0.21	0.58		CALMODULIN; CHAIN: A;	“METAL TRANSPORT CALMODULIN,
										HIGH RESOLUTION, DISORDER”
246	1fpw	A	174	331	2.60E−21	−0.03	0.89		CALCIUM-BINDING	“METAL BINDING PROTEIN YEAST
									PROTEIN NCS-1; CHAIN: A;	FREQUENIN EF-HAND, CALCIUM”
246	1fpw	A	1	120	1.30E−06	0.07	0.09		CALCIUM-BINDING	“METAL BINDING PROTEIN YEAST
									PROTEIN NCS-1; CHAIN: A;	FREQUENIN EF-HAND, CALCIUM”
246	1iku		178	331	1.00E−21	0.15	0.84		RECOVERIN; CHAIN: NULL;	“CALCIUM-BINDING PROTEIN CALCIUM-
										MYRISTOYL SWITCH, CALCUIM-
										BINDING PROTEIN”
246	1iku		4	129	9.10E−06	0.08	0.93		RECOVERIN; CHAIN: NULL;	“CALCIUM-BINDING PROTEIN CALCIUM-
										MYRISTOYL SWITCH, CALCUIM-
										BINDING PROTEIN”
246	1iku		174	351	1.00E−21			72.88	RECOVERIN; CHAIN: NULL;	“CALCIUM-BINDING PROTEIN CALCIUM-
										MYRISTOYL SWITCH, CALCUIM-
										BINDING PROTEIN”
246	1jba	A	211	331	2.60E−17	−0.15	0.25		GUANYLATE CYCLASE	“LYASE GCAP-2; EF-HAND, CALCIUM-
									ACTIVATING PROTEIN 2;	BINDING PROTEIN, GUANYLYL CYCLASE
									CHAIN: A;	2 REGULATION”
246	1rec		178	331	5.20E−19	0.03	0.42			CALCIUM-BINDING PROTEIN
										RECOVERIN (CALCIUM SENSOR IN
										VISION) 1REC 3
246	1rec		10	139	0.0001	−0.26	0.12			CALCIUM-BINDING PROTEIN
										RECOVERIN (CALCIUM SENSOR IN
										VISION) 1REC 3
246	1rec		178	351	5.20E−19			50.07		CALCIUM-BINDING PROTEIN
										RECOVERIN (CALCIUM SENSOR IN
										VISION) 1REC 3
246	1top		90	148	0.0078	0.59	0.29			CONTRACTILE SYSTEM PROTEIN
										TROPONIN C 1TOP 3
246	1trc	A	93	146	0.0052	−0.01	0.76			CALCIUM BINDING PROTEIN
										CALMODULIN (/TR = 2 = C$ FRAGMENT
										COMPRISING RESIDUES 78-148 1TRC 3
										OF THE INTACT MOLECULE) 1TRC 4
246	1vrk	A	190	331	1.00E−10	−0.33	0.19		CALMODULIN; CHAIN: A;	“CALMODULIN, CALCIUM BINDING,
									RS20; CHAIN: B;	HELIX-LOOP-HELIX, SIGNALLING, 2
										COMPLEX(CALCIUM-BINDING
										PROTEIN/PEPTIDE)”
246	1vrk	A	72	148	0.0026	−0.07	0.4		CALMODULIN; CHAIN: A;	“CALMODULIN, CALCIUM BINDING,
									RS20; CHAIN: B;	HELIX-LOOP-HELIX, SIGNALLING, 2
										COMPLEX(CALCIUM-BINDING
										PROTEIN/PEPTIDE)”
246	1wdc	B	191	324	1.00E−10	−0.4	0.22		“SCALLOP MYOSIN; CHAIN:	“MUSCLE PROTEIN MYOSIN, CALCIUM
									A, B, C;”	BINDING PROTEIN, MUSCLE PROTEIN”
246	1wdc	B	72	146	0.0039	−0.23	0.04		“SCALLOP MYOSIN; CHAIN:	“MUSCLE PROTEIN MYOSIN, CALCIUM
									A, B, C;”	BINDING PROTEIN, MUSCLE PROTEIN”
246	5pal		55	146	0.0065	0.05	0.59			CALCIUM-BINDING PROTEIN
										PARVALBUMIN (ALPHA LINEAGE) 5PAL 3
251	1aip	A	92	442	0			85.64	“ELONGATION FACTOR TU;	“COMPLEX OF TWO ELONGATION
									CHAIN: A, B, E, F;	FACTORS EF-TU; EF-TS; ELONGATION
									ELONGATION FACTOR TS;	FACTOR, NUCLEOTIDE EXCHANGE, GTP-
									CHAIN: C, D, G, H;”	BINDING, 2 COMPLEX OF TWO
										ELONGATION FACTORS”
251	1d2e	A	69	451	0			117.42	“ELONGATION FACTOR TU	“RNA BINDING PROTEIN G-PROTEIN,
									(EF-TU); CHAIN: A, B, C, D”	BETA-BARREL”
251	1dar		4	553	2.60E−87			114.99	ELONGATION FACTOR G;	“TRANSLATIONAL GTPASE EF-G
									CHAIN: NULL;	RIBOSOMAL TRANSLOCASE,
										TRANSLATIONAL GTPASE”
251	1efc	A	65	442	0			108.03	“ELONGATION FACTOR;	“RNA BINDING PROTEIN EFTU;
									CHAIN: A, B;”	TRANSPORT AND PROTECTION PROTEIN,
										RNA BINDING PROTEIN”
251	1efu	A	69	437	0			83.78	“ELONGATION FACTOR TU;	“COMPLEX (TWO ELONGATION
									CHAIN: A, C; ELONGATION	FACTORS) ELONGATION FACTOR FOR
									FACTOR TS; CHAIN: B, D;”	TRANSFER, HEAT UNSTABLE,
										ELONGATION FACTOR FOR TRANSFER,
										HEAT STABLE, ELONGATION FACTOR,
										COMPLEX (TWO ELONGATION
										FACTORS)”
251	2efg	A	2	552	1.30E−84			116.45	ELONGATION FACTOR G;	“PROTEIN BINDING EF-G; EF-G
									CHAIN: A; ELONGATION	ELONGATION FACTOR, TRANSLOCASE,
									FACTOR G DOMAIN 3;	RIBOSOME, ELONGATION, 2
									CHAIN: B;	TRANSLATION, PROTEIN SYNT FACTOR,
										GTPASE, GTP BINDING, 3 GUANOSINE
										NUCLEOTIDE BINDING,, PROTEIN
										BINDING”
253	1byr	A	111	257	1.20E−28			82.42	ENDONUCLEASE; CHAIN:	“ENDONUCLEASE ENDONUCLEASE,
									A;	PHOSPHODIESTERASE,”
254	1avl	A	113	313	0.0017			58.59	“APOLIPOPROTEIN A-I;	“LIPID TRANSPORT APO A-I;
									CHAIN: A, B, C, D;”	LIPOPROTEIN, LIPID TRANSPORT,
										CHOLESTEROL METABOLISM, 2
										ATHEROSCLEROSIS, HDL, LCAT-
										ACTIVATION”
256	1rgp		289	484	3.90E−44			74.05	RHOGAP; CHAIN: NULL;	“G-PROTEIN CDC42 GTPASE-ACTIVATING
										PROTEIN; G-PROTEIN, GAP, SIGNAL-
										TRANSDUCTION”
256	1tx4	A	292	495	2.60E−46			78.72	P50-RHOGAP; CHAIN: A;	“COMPLEX (GTPASE ACTIVATN/PROTO-
									TRANSFORMING PROTEIN	ONCOGENE) GTPASE-ACTIVATING
									RHOA; CHAIN: B;	PROTEIN RHOGAP; COMPLEX (GTPASE
										ACTIVATION/PROTO-ONCOGENE),
										GTPASE, 2 TRANSITION STATE, GAP”
258	1pbw	A	21	210	3.90E−45	0.26	0.99		“PHOSPHATIDYLINOSITOL	“PHOSPHOTRANSFERASE RHOGAP
									3-KINASE; CHAIN: A, B;”	DOMAIN; PHOSPHOTRANSFERASE,
										TPASE ACTIVATING PROTEIN, GAP,
										CDC42, 2 PHOSPHOINOSITIDE 3-KINASE,
										SH3 DOMAIN, SH2 DOMAIN, 3 SIGNAL
										TRANSDUCTION”
258	1pbw	B	21	215	6.50E−45	0.44	0.99		“PHOSPHATIDYLINOSITOL	“PHOSPHOTRANSFERASE RHOGAP
									3-KINASE; CHAIN: A, B;”	DOMAIN; PHOSPHOTRANSFERASE,
										TPASE ACTIVATING PROTEIN, GAP,
										CDC42, 2 PHOSPHOINOSITIDE 3-KINASE,
										SH3 DOMAIN, SH2 DOMAIN, 3-SIGNAL
										TRANSDUCTION”
258	1pbw	B	34	214	5.10E−22	0.37	0.99		“PHOSPHATIDYLINOSITOL	“PHOSPHOTRANSFERASE RHOGAP
									3-KINASE; CHAIN: A, B;”	DOMAIN; PHOSPHOTRANSFERASE,
										TPASE ACTIVATING PROTEIN, GAP,
										CDC42, 2 PHOSPHOINOSITIDE 3-KINASE,
										SH3 DOMAIN, SH2 DOMAIN, 3 SIGNAL
										TRANSDUCTION”
258	1pbw	A	34	190	3.40E−21	0.4	0.8		“PHOSPHATIDYLINOSITOL	“PHOSPHOTRANSFERASE RHOGAP
									3-KINASE; CHAIN: A, B;”	DOMAIN; PHOSPHOTRANSFERASE,
										TPASE ACTIVATING PROTEIN, GAP,
										CDC42, 2 PHOSPHOINOSITIDE 3-KINASE,
										SH3 DOMAIN, SH2 DOMAIN, 3 SIGNAL
										TRANSDUCTION”
258	1pbw	A	20	201	3.90E−45			81.22	“PHOSPHATIDYLINOSITOL	“PHOSPHOTRANSFERASE RHOGAP
									3-KINASE; CHAIN: A, B;”	DOMAIN; PHOSPHOTRANSFERASE,
										TPASE ACTIVATING PROTEIN, GAP,
										CDC42, 2 PHOSPHOINOSITIDE 3-KINASE,
										SH3 DOMAIN, SH2 DOMAIN, 3 SIGNAL
										TRANSDUCTION”
258	1pbw	B	20	217	6.50E−45			79.67	“PHOSPHATIDYLINOSITOL	“PHOSPHOTRANSFERASE RHOGAP
									3-KINASE; CHAIN: A, B;”	DOMAIN; PHOSPHOTRANSFERASE,
										TPASE ACTIVATING PROTEIN, GAP,
										CDC42, 2 PHOSPHOINOSITIDE 3-KINASE,
										SH3 DOMAIN, SH2 DOMAIN, 3 SIGNAL
										TRANSDUCTION”
258	1rgp		12	215	2.60E−51	0.42	1		RHOGAP; CHAIN: NULL;	“G-PROTEIN CDC42 GTPASE-ACTIVATING
										PROTEIN; G-PROTEIN, GAP, SIGNAL-
										TRANSDUCTION”
258	1rgp		9	182	6.80E−35	0.39	1		RHOGAP; CHAIN: NULL;	“G-PROTEIN CDC42 GTPASE-ACTIVATING
										PROTEIN; G-PROTEIN, GAP, SIGNAL-
										TRANSDUCTION”
258	1rgp		9	195	2.60E−51			102.59	RHOGAP; CHAIN: NULL;	“G-PROTEIN CDC42 GTPASE-ACTIVATING
										PROTEIN; G-PROTEIN, GAP, SIGNAL-
										TRANSDUCTION”
258	1tx4	A	14	215	9.10E−55	0.67	1	40	P50-RHOGAP; CHAIN: A;	“COMPLEX(GTPASE ACTIVATN/PROTO-
									TRANSFORMING PROTEIN	ONCOGENE) GTPASE-ACTIVATING
									RHOA; CHAIN: B;	PROTEIN RHOGAP; COMPLEX (GTPASE
										ACTIVATION/PROTO-ONCOGENE),
										GTPASE, 2 TRANSITION STATE, GAP”
258	1tx4	A	12	182	1.70E−33	0.46	1		P50-RHOGAP; CHAIN: A;	“COMPLEX(GTPASE ACTIVATN/PROTO-
									TRANSFORMING PROTEIN	ONCOGENE) GTPASE-ACTIVATING
									RHOA; CHAIN: B;	PROTEIN RHOGAP; COMPLEX(GTPASE
										ACTIVATION/PROTO-ONCOGENE),
										GTPASE, 2 TRANSITION STATE, GAP”
258	1tx4	A	12	215	9.10E−55			107.19	P50-RHOGAP; CHAIN: A;	“COMPLEX(GTPASE ACTIVATN/PROTO-
									TRANSFORMING PROTEIN	ONCOGENE) GTPASE-ACTIVATING
									RHOA; CHAIN: B;	PROTEIN RHOGAP; COMPLEX (GTPASE
										ACTIVATION/PROTO-ONCOGENE),
										GTPASE, 2 TRANSITION STATE, GAP”
259	1apm	E	109	466	6.50E−42			103.32		“TRANSFERASE(PHOSPHOTRANSFERASE
										) $C-/AMP$-DEPENDENT PROTEIN
										KINASE (E.C.2.7.1.37) ($C/APK$) 1APM 3
										(CATALYTIC SUBUNIT) ““ALPHA””
										ISOENZYME MUTANT WITH SER 139
										1APM 4 REPLACED BY ALA (/S139A$)
										COMPLEX WITH THE PEPTIDE 1APM 5
										INHIBITOR PKI(5-24) AND THE
										DETERGENT MEGA-8 1APM 6”
259	1aze	A	59	111	1.30E−15	0.14	0.76		GRB2; CHAIN: A; SOS;	“COMPLEX (ADAPTOR PROTEIN/PEPTIDE)
									CHAIN: B;	ASH, GROWTH FACTOR RECEPTOR-
										BOUND PROTEIN 2; COMPLEX (ADAPTOR
										PROTEIN/PEPTIDE), SH3 DOMAIN, 2
										GUANINE-NUCLEOTIDE RELEASING
										FACTOR”
259	1b6c	B	137	409	3.90E−67	0.4	0.89		“FK506-BINDING PROTEIN;	“COMPLEX (ISOMERASE/PROTEIN
									CHAIN: A, C, E, G; TGF-B	KINASE) FKBP12; SERINE/THREONINE-
									SUPERFAMILY RECEPTOR	PROTEIN KINASE RECEPTOR R4;
									TYPE I; CHAIN: B, D, F, H;”	COMPLEX (ISOMERASE/PROTEIN
										KINASE), RECEPTOR 2
										SERINE/THREONINE KINASE”
259	1bb9		58	113	9.10E−18	−0.17	0.89		AMPHIPHYSIN 2; CHAIN:	“TRANSFERASE TRANSFERASE, SH3
									NULL;	DOMAIN”
259	1bbz	A	59	113	1.30E−15	0.34	0.8		“ABL TYROSINE KINASE;	“COMPLEX (TRANSFERASE/PEPTIDE)
									CHAIN: A, C, E, G; PEPTIDE	COMPLEX (TRANSFERASE/PEPTIDE),
									P41; CHAIN: B, D, F, H;”	SIGNAL TRANSDUCTION, 2 SH3 DOMAIN”
259	1blx	A	138	436	1.30E−36			105.3	CYCLIN-DEPENDENT	“COMPLEX (INHIBITOR
									KINASE 6; CHAIN: A;	PROTEIN/KINASE) INHIBITOR PROTEIN,
									P19INK4D; CHAIN: B;	CYCLIN-DEPENDENT KINASE, CELL
										CYCLE 2 CONTROL, ALPHA/BETA,
										COMPLEX (INHIBITOR
										PROTEIN/KINASE)”
259	1byg	A	138	409	6.50E−77	0.6	1		C-TERMINAL SRC KINASE;	“TRANSFERASE CSK; PROTEIN KINASE,
									CHAIN: A;	C-TERMINAL SRC KINASE,
										PHOSPHORYLATION, 2 STAUROSPORINE,
										TRANSFERASE”
259	1byg	A	150	406	6.80E−49	0.27	1		C-TERMINAL SRC KINASE;	“TRANSFERASE CSK; PROTEIN KINASE,
									CHAIN: A;	C-TERMINAL SRC KINASE,
										PHOSPHORYLATION, 2 STAUROSPORINE,
										TRANSFERASE”
259	1byg	A	137	411	6.50E−77			126.82	C-TERMINAL SRC KINASE;	“TRANSFERASE CSK; PROTEIN KINASE,
									CHAIN: A;	C-TERMINAL SRC KINASE,
										PHOSPHORYLATION, 2 STAUROSPORINE,
										TRANSFERASE”
259	1cki	A	146	403	5.20E−48	0.22	0.78		“CASEIN KINASE I DELTA;	PHOSPHOTRANSFERASE PROTEIN
									1CKI 6 CHAIN: A, B; 1CKI 7”	KINASE 1CKI 18
259	1cmk	E	90	466	1.20E−41			107.48		PHOSPHOTRANSFERASE CAMP-
										DEPENDENT PROTEIN KINASE
										CATALYTIC SUBUNIT 1CMK 3
										(E.C.2.7.1.37) 1CMK 4
259	1f3m	C	145	400	3.90E−52	0.28	1		“SERINE/THREONINE-	“TRANSFERASE KINASE DOMAIN,
									PROTEIN KINASE PAK-	AUTOINHIBITORY FRAGMENT,
									ALPHA; CHAIN: A, B;	HOMODIMER”
									SERINE/THREONINE-
									PROTEIN KINASE PAK-
									ALPHA; CHAIN: C, D;”
259	1fgk	B	138	406	3.90E−77	0.56	1		“FGF RECEPTOR 1; CHAIN:	“PHOSPHOTRANSFERASE FGFR1K,
									A, B;”	FIBROBLAST GROWTH FACTOR
										RECEPTOR 1; TRANSFERASE, TYROSINE-
										PROTEIN KINASE, ATP-BINDING, 2
										PHOSPHORYLATION, RECEPTOR,
										PHOSPHOTRANSFERASE”
259	1fgk	A	138	406	1.00E−76	0.68	1		“FGF RECEPTOR 1; CHAIN:	“PHOSPHOTRANSFERASE FGFR1K,
									A, B;”	FIBROBLAST GROWTH FACTOR
										RECEPTOR 1; TRANSFERASE, TYROSINE-
										PROTEIN KINASE, ATP-BINDING, 2
										PHOSPHORYLATION, RECEPTOR,
										PHOSPHOTRANSFERASE”
259	1fgk	B	137	410	1.20E−45	0.71	1		“FGF RECEPTOR 1; CHAIN:	“PHOSPHOTRANSFERASE FGFR1K,
									A, B;”	FIBROBLAST GROWTH FACTOR
										RECEPTOR 1; TRANSFERASE, TYROSINE-
										PROTEIN KINASE, ATP-BINDING, 2
										PHOSPHORYLATION, RECEPTOR,
										PHOSPHOTRANSFERASE”
259	1fgk	A	166	410	1.70E−44	0.42	1		“FGF RECEPTOR 1; CHAIN:	“PHOSPHOTRANSFERASE FGFR1K,
									A, B;”	FIBROBLAST GROWTH FACTOR
										RECEPTOR 1; TRANSFERASE, TYROSINE-
										PROTEIN KINASE, ATP-BINDING, 2
										PHOSPHORYLATION, RECEPTOR,
										PHOSPHOTRANSFERASE”
259	1fgk	B	127	410	3.90E−77			154.88	“FGF RECEPTOR 1; CHAIN:	“PHOSPHOTRANSFERASE FGFR1K,
									A, B;”	FIBROBLAST GROWTH FACTOR
										RECEPTOR 1; TRANSFERASE, TYROSINE-
										PROTEIN KINASE, ATP-BINDING, 2
										PHOSPHORYLATION, RECEPTOR,
										PHOSPHOTRANSFERASE”
259	1fgk	A	135	410	1.00E−76			149.68	“FGF RECEPTOR 1; CHAIN:	“PHOSPHOTRANSFERASE FGFR1K,
									A, B;”	FIBROBLAST GROWTH FACTOR
										RECEPTOR 1; TRANSFERASE, TYROSINE-
										PROTEIN KINASE, ATP-BINTDING, 2
										PHOSPHORYLATION, RECEPTOR,
										PHOSPHOTRANSFERASE”
259	1fmk		51	417	6.80E−81	0.53	1		TYROSINE-PROTEIN	“PHOSPHOTRANSFERASE C-SRC, P60-
									KINASE SRC; CHAIN: NULL;	SRC; SRC, TYROSINE KINASE,
										PHOSPHORYLATION, SH2, SH3, 2
										PHOSPHOTYROSINE, PROTO-ONCOGENE,
										PHOSPHOTRANSFERASE”
259	1fmk		1	419	6.80E−81			125.36	TYROSINE-PROTEIN	“PHOSPHOTRANSFERASE C-SRC, P60-
									KINASE SRC; CHAIN: NULL;	SRC; SRC, TYROSINE KINASE,
										PHOSPHORYLATION, SH2, SH3, 2
										PHOSPHOTYROSINE, PROTO-ONCOGENE,
										PHOSPHOTRANSFERASE”
259	1fpu	A	127	406	1.20E−73	0.75	1		“PROTO-ONCOGENE	“TRANSFERASE P150, C-ABL; KINASE,
									TYROSINE-PROTEIN	KINASE INHIBITOR, STI-571, ACTIVATION
									KINASE ABL; CHAIN: A, B;”	LOOP”
259	1fpu	A	134	408	140E−65	0.69	1		“PROTO-ONCOGENE	“TRANSFERASE P150, C-ABL; KINASE,
									TYROSINE-PROTEIN	KINASE INHIBITOR, STI-571, ACTIVATION
									KINASE ABL; CHAIN: A, B;”	LOOP”
259	1fyn	A	55	113	9.10E−15	0.38	0.9		PHOSPHOTRANSFERASE	“TRANSFERASE PROTO-ONCOGENE
									FYN; CHAIN: A; 3BP-2;	TYROSINE KINASE; PROTO-ONCOGENE,
									CHAIN: B;	TRANSFERASE, TYROSINE-PROTEIN
										KINASE, 2 PHOSPHORYLATION, ATP-
										BINDING, MYRISTYLATION, SH3
										DOMAIN, 3 COMPLEX
										(PHOSPHOTRANSFERASE/PEPTIDE)”
259	1gbq	A	59	113	9.10E−16	0.21	0.96		GRB2; CHAIN: A; SOS-1;	“COMPLEX (SIGNAL
									CHAIN: B;	TRANSDUCTION/PEPTIDE) COMPLEX
										(SIGNAL TRANSDUCTION/PEPTIDE), SH3
										DOMAIN”
259	1gfc		55	113	7.80E−17	0.31	0.99			“ADAPTOR PROTEIN CONTAINING SH2
										AND SH3 GROWTH FACTOR RECEPTOR-
										BOUND PROTEIN 2 (GRB2) 1GFC3 (C-
										TERMINAL SH3 DOMAIN) (NMR,
										MINIMIZED MEAN STRUCTURE) 1GFC 4”
259	1gri	A	56	113	1.00E−14	0.45	0.99		“GROWTH FACTOR BOUND	“SIGNAL TRANSDUCTION ADAPTOR SH2,
									PROTEIN 2; 1GRI 5 CHAIN:	SH3 1GRI 14”
									A, B; 1GRI6”
259	1hsq		49	113	2.60E−16	0.32	0.77			“PHOSPHORIC DIESTER HYDROLASE
										PHOSPHOLIPASE C-GAMMA (SH3
										DOMAIN) (E.C.3.1.4.11) 1HSQ 3 (NMR,
										MINIMIZED MEAN STRUCTURE) 1HSQ 4”
259	1ir3	A	138	425	3.90E−79	0.48	1		INSULIN RECEPTOR;	“COMPLEX (TRANSFERASE/SUBSTRATE)
									CHAIN: A; PEPTIDE	TYROSINE KINASE, SIGNAL
									SUBSTRATE; CHAIN: B;	TRANSDUCTION,
										PHOSPHOTRANSFERASE, 2 COMPLEX
										(KINASE/PEPTIDE SUBSTRATE/ATP
										ANALOG), ENZYME, 3 COMPLEX
										(TRANSFERASE/SUBSTRATE)”
259	1ir3	A	131	425	3.40E−50	0.51	1		INSULIN RECEPTOR;	“COMPLEX (TRANSFERASE/SUBSTRATE)
									CHAIN: A; PEPTIDE	TYROSINE KINASE, SIGNAL
									SUBSTRATE; CHAIN: B;	TRANSDUCTION,
										PHOSPHOTRANSFERASE, 2 COMPLEX
										(KINASE/PEPTIDE SUBSTRATE/ATP
										ANALOG), ENZYME, 3 COMPLEX
										(TRANSFERASE/SUBSTRATE)”
259	1ir3	A	128	425	3.90E−79			134.78	INSULIN RECEPTOR;	“COMPLEX (TRANSFERASE/SUBSTRATE)
									CHAIN: A; PEPTIDE	TYROSINE KINASE, SIGNAL
									SUBSTRATE; CHAIN: B;	TRANSDUCTION,
										PHOSPHOTRANSFERASE, 2 COMPLEX
										(KINASE/PEPTIDE SUBSTRATE/ATP
										ANALOG), ENZYME, 3 COMPLEX
										(TRANSFERASE/SUBSTRATE)”
259	1koa		128	553	2.60E−45			118.08	TWITCHIN; CHAIN: NULL;	“KINASE KINASE, TWITCHIN,
										INTRASTERIC REGULATION”
259	1kob	A	107	470	1.00E−40			105.15	“TWITCHIN; CHAIN: A, B;”	“KINASE KINASE, TWITCHIN,
										INTRASTERIC REGULATION”
259	1qcf	A	127	409	1.30E−80	0.54	1		HAEMATOPOETIC CELL	“TYROSINE KINASE TYROSINE KINASE-
									KINASE (HCK); CHAIN: A;	INHIBITOR COMPLEX, DOWN-
										REGULATED KINASE, 2 ORDERED
										ACTIVATION LOOP”
259	1qcf	A	52	413	6.80E−70	0.39	1		HAEMATOPOETIC CELL	“TYROSINE KINASE TYROSINE KINASE-
									KINASE (HCK); CHAIN: A;	INHIBITOR COMPLEX, DOWN-
										REGULATED KINASE, 2 ORDERED
										ACTIVATION LOOP”
259	1qcf	A	1	415	6.80E−70			138.77	HAEMATOPOETIC CELL	“TYROSINE KINASE TYROSINE KINASE-
									KINASE (HCK); CHAIN: A;	INHIBITOR COMPLEX, DOWN-
										REGULATED KINASE, 2 ORDERED
										ACTIVATION LOOP”
259	1qly	A	54	113	1.30E−15	0.32	0.62		TYROSINE-PROTEIN	“TYROSINE-PROTEIN KINASE BRUTONS
									KINASE BTK; CHAIN: A;	TYROSINE KINASE, B CELL PROGENITOR
										KINASE, TRANSFERASE, TYROSINE-
										PROTEIN KINASE, PHOSPHORYLATION, 2
										SH3 DOMAIN”
259	1qpc	A	138	409	3.90E−80	0.68	1		LCK KINASE; CHAIN: A;	TRANSFERASE ALPHA BETA FOLD
259	1qpc	A	135	411	1.20E−64	0.63	1		LCK KINASE; CHAIN: A;	TRANSFERASE ALPHA BETA FOLD
259	1sem	A	55	113	5.20E−17	0.54	1		“SEM-5; ISEM 3 CHAIN: A,	“SIGNAL TRANSDUCTION PROTEIN SRC-
									B; ISEM 5 10-RESIDUE	HOMOLOGY 3 (SH3) DOMAIN, PEPTIDE-
									PROLINE-RICH PEPTIDE	BINDING PROTEIN, 1SEM 18 2 GUANINE
									FROM MSOS 1SEM 8 CHAIN:	NUCLEOTIDE EXCHANGE FACTOR 1SEM
									C, D 1SEM 10”	19”
259	1tki	A	146	400	7.80E−45	0.34	0.77		“TITIN; CHAIN: A, B;”	“SERINE KINASE SERINE KINASE, TITIN,
										MUSCLE, AUTOINHIBITION”
259	1vr2	A	138	409	1.30E−71	0.58	1		VASCULAR ENDOTHELIAL	TRANSFERASE KDR; TYROSINE KINASE
									GROWTH FACTOR
									RECEPTOR CHAIN: A;
261	1mgs	A	55	127	1.70E−21	0.41	1			“CHEMOKINE(GROWTH FACTOR)
										HUMAN MELANOMA GROWTH
										STIMULATING ACTIVITY
										(MGSA/GRO_ALPHA) 1MGS 3 (NMR, 25
										STRUCTURES) 1MGS 4”
261	1mgs	A	55	127	1.70E−21			78.78		“CHEMOKINE(GROWTH FACTOR)
										HUMAN MELANOMA GROWTH
										STIMULATING ACTIVITY
										(MGSA/GRO_ALPHA) 1MGS 3 (NMR, 25
										STRUCTURES) 1MGS 4”
261	1mi2	A	55	127	5.10E−20	0.38	1		“MACROPHAGE	“CYTOKINE MIP-2, CHEMOKINE, NMR,
									INFLAMMATORY PROTEIN-	CYTOKINE”
									2; CHAIN: A, B;”
261	1mi2	A	55	126	5.10E−20			70.46	“MACROPHAGE	“CYTOKINE MIP-2, CHEMOKINE, NMR,
									INFLAMMATORY PROTEIN-	CYTOKINE”
									2; CHAIN: A, B;”
261	1qnk	A	59	127	1.00E−19	0.62	1		“GROB[5-73]; CHAIN: A, B;”	“CHEMOKINE CHEMOKINE 15-O, HUMAN
										CHEMOKINE GROB[5-73], CXC
										CHEMOKINE”
261	1rod	A	60	127	2.60E−27	0.29	1		“CHIMERIC PROTEIN OF	“CHEMOKINE CHI1, CIL-8M, NAP-1/M12;
									INTERLEUKIN 8 AND	CYTOKINE, CHEMOTAXIS,
									HUMAN CHAIN: A, B;”	INFLAMMATORY RESPONSE,
										CHEMOKINE”
261	1rod	A	57	127	2.60E−27			66.9	“CHIMERIC PROTEIN OF	“CHEMOKINE CHI1, CIL-8M, NAP-1/M12;
									INTERLEUKIN 8 AND	CYTOKINE, CHEMOTAXIS,
									HUMAN CHAIN: A, B;”	INFLAMMATORY RESPONSE,
										CHEMOKINE”
261	1tvx	B	54	121	1.20E−22	0.66	1		“NEUTROPHIL ACTIVATING	CYTOKINE NAP-2; CYTOKINE
									PEPTIDE 2 VARIANT;
									CHAIN: A, B, C, D;”
261	1tvx	A	61	121	2.60E−21	0.56	1		“NEUTROPHIL ACTIVATING	CYTOKINE NAP-2; CYTOKINE
									PEPTIDE 2 VARIANT;
									CHAIN: A, B, C, D;”
261	1tvx	B	55	119	3.40E−19	0.27	1		“NEUTROPHIL ACTIVATING	CYTOKINE NAP-2; CYTOKINE
									PEPTIDE 2 VARIANT;
									CHAIN: A, B, C, D;”
261	1tvx	A	61	119	1.70E−18	0.79	1		“NEUTROPHIL ACTIVATING	CYTOKINE NAP-2; CYTOKINE
									PEPTIDE 2 VARIANT;
									CHAIN: A, B, C, D;”
261	1tvx	B	54	124	1.20E−22			106.99	“NEUTROPHIL ACTIVATING	CYTOKINE NAP-2; CYTOKINE
									PEPTIDE 2 VARIANT;
									CHAIN: A, B, C, D;”
261	1tvx	A	61	124	2.60E−21			95.42	“NEUTROPHIL ACTIVATING	CYTOKINE NAP-2; CYTOKINE
									PEPTIDE 2 VARIANT;
									CHAIN: A, B, C, D;”
262	1a17		44	188	6.80E−28	0.11	0.42		SERINE/THREONINE	“HYDROLASE TETRATRICOPEPTIDE, TRP;
									PROTEIN PHOSPHATASE 5;	HYDROLASE, PHOSPHATASE, PROTEIN-
									CHAIN: NULL;	PROTEIN INTERACTIONS, TPR, 2 SUPER-
										HELIX, X-RAY STRUCTURE”
262	1a17		8	134	1.50E−18	0.58	0.71		SERINE/THREONINE	“HYDROLASE TETRATRICOPEPTIDE, TRP;
									PROTEIN PHOSPHATASE 5;	HYDROLASE, PHOSPHATASE, PROTEIN-
									CHAIN: NULL;	PROTEIN INTERACTIONS, TPR, 2 SUPER-
										HELIX, X-RAY STRUCTURE”
262	1a17		2	100	1.00E−08	0.34	0.6		SERINE/THREONINE	“HYDROLASE TETRATRICOPEPTIDE, TRP;
									PROTEIN PHOSPHATASE 5;	HYDROLASE, PHOSPHATASE, PROTEIN-
									CHAIN: NULL;	PROTEIN INTERACTIONS, TPR, 2 SUPER-
										HELIX, X-RAY STRUCTURE”
262	1d8d	A	14	113	6.50E−09	−0.07	0		FARNESYLTRANSFERASE	“TRANSFERASE FTASE; FTASE; FTASE,
									(ALPHA SUBUNIT); CHAIN:	PFT, PFTASE, FARNESYLTRANSFERASE,
									A;	FARNESYL 2 TRANSFERASE, CAAX, RAS,
									FARNESYLTRANSFERASE	CANCER”
									(BETA SUBUNIT); CHAIN: B;
									K-RAS4B PEPTIDE
									SUBSTRATE; CHAIN: P;
262	1d8d	A	55	188	1.40E−08	−0.09	0.03		FARNESYLTRANSFERASE	“TRANSFERASE FTASE; FTASE; FTASE,
									(ALPHA SUBUNIT); CHAIN:	PFT, PFTASE, FARNESYLTRANSFERASE,
									A;	FARNESYL 2 TRANSFERASE, CAAX, RAS,
									FARNESYLTRANSFERASE	CANCER”
									(BETA SUBUNIT); CHAIN: B;
									K-RAS4B PEPTIDE
									SUBSTRATE; CHAIN: P;
262	1e53	B	45	192	1.20E−18	0.04	1		RAS-RELATED C3	“SIGNALLING COMPLEX RAC1; P67PHOX;
									BOTULINUM TOXIN	SIGNALLING COMPLEX, GTPASE, NADPH
									SUBSTRATE 1; CHAIN: A;	OXIDASE, PROTEIN-PROTEIN 2
									NEUTROPHIL CYTOSOL	COMPLEX, TPR MOTIF”
									FACTOR 2 (NCF-2) CHAIN:
									B;
262	1e53	B	6	116	5.10E−10	−0.03	0.16		RAS-RELATED C3	“SIGNALLING COMPLEX RAC1; P67PHOX;
									BOTULINUM TOXIN	SIGNALLING COMPLEX, GTPASE, NADPH
									SUBSTRATE 1; CHAIN: A;	OXIDASE, PROTEIN-PROTEIN 2
									NEUTROPHIL CYTOSOL	COMPLEX, TPR MOTIF”
									FACTOR 2 (NCF-2) CHAIN:
									B;
262	1e53	B	13	113	1.20E−07	0.31	1		RAS-RELATED C3	“SIGNALLING COMPLEX RAC1; P67PHOX;
									BOTULINUM TOXIN	SIGNALLING COMPLEX, GTPASE, NADPH
									SUBSTRATE 1; CHAIN: A;	OXIDASE, PROTEIN-PROTEIN 2
									NEUTROPHIL CYTOSOL	COMPLEX, TPR MOTIF”
									FACTOR 2 (NCF-2) CHAIN:
									B;
262	1elr	A	50	141	1.70E−19	0.04	0.12		TPR2A-DOMAIN OF HOP;	“CHAPERONE HOP, TPR-DOMAIN,
									CHAIN: A; HSP90-PEPTIDE	PEPTIDE-COMPLEX, HELICAL REPEAT,
									MEEVD; CHAIN: B;	HSP90, 2 PROTEIN BINDING”
262	1elr	A	14	107	5.10E−15	0.27	0.89		TPR2A-DOMAIN OF HOP;	“CHAPERONE HOP, TPR-DOMAIN,
									CHAIN: A; HSP90-PEPTIDE	PEPTIDE-COMPLEX, HELICAL REPEAT,
									MEEVD; CHAIN: B;	HSP90, 2 PROTEIN BINDING”
262	1elr	A	86	175	1.00E−14	0.28	0.53		TPR2A-DOMAIN OF HOP;	“CHAPERONE HOP, TPR-DOMAIN,
									CHAIN: A; HSP90-PEPTIDE	PEPTIDE-COMPLEX, HELICAL REPEAT,
									MEEVD; CHAIN: B;	HSP90, 2 PROTEIN BINDING”
262	1elr	A	2	73	1.20E−13	0.12	0.37		TPR2A-DOMAIN OF HOP;	“CHAPERONE HOP, TPR-DOMAIN,
									CHAIN: A; HSP90-PEPTIDE	PEPTIDE-COMPLEX, HELICAL REPEAT,
									MEEVD; CHAIN: B;	HSP90, 2 PROTEIN BINDING”
262	1elr	A	9	123	3.90E−07	0.3	0.7		TPR2A-DOMAIN OF HOP;	“CHAPERONE HOP, TPR-DOMAIN,
									CHAIN: A; HSP90-PEPTIDE	PEPTIDE-COMPLEX, HELICAL REPEAT,
									MEEVD; CHAIN: B;	HSP90, 2 PROTEIN BINDING”
262	1elw	A	44	160	3.40E−24	0.12	0.39		“TPR1-DOMAIN OF HOP;	“CHAPERONE HOP, TPR-DOMAIN,
									CHAIN: A, B; HSC70-	PEPTIDE-COMPLEX, HELICAL REPEAT,
									PEPTIDE; CHAIN: C, D;”	HSC70, 2 HSP70, PROTEIN BINDING”
262	1elw	A	87	194	5.10E−18	0.26	0.69		“TPR1-DOMAIN OF HOP;	“CHAPERONE HOP, TPR-DOMAIN,
									CHAIN: A, B; HSC70-	PEPTIDE-COMPLEX, HELICAL REPEAT,
									PEPTIDE; CHAIN: C, D;”	HSC70, 2 HSP70, PROTEIN BINDING”
262	1elw	A	8	115	1.70E−12	0.31	0.6		“TPR1-DOMAIN OF HOP;	“CHAPERONE HOP, TPR-DOMAIN,
									CHAIN: A, B; HSC70-	PEPTIDE-COMPLEX, HELICAL REPEAT,
									PEPTIDE; CHAIN: C, D;”	HSC70, 2 HSP70, PROTEIN BINDING”
262	1elw	A	2	86	3.40E−09	0.21	0.34		“TPR1-DOMAIN OF HOP;	“CHAPERONE HOP, TPR-DOMAIN,
									CHAIN: A, B; HSC70-	PEPTIDE-COMPLEX, HELICAL REPEAT,
									PEPTIDE; CHAIN: C, D;”	HSC70, 2 HSP70, PROTEIN BINDING”
262	1fch	A	2	184	6.80E−28	0.19	0.94		“PEROXISOMAL	“SIGNALING PROTEIN PEROXISMORE
									TARGETING SIGNAL 1	RECEPTOR 1, PTS1-BP, PEROXIN-5, PTS1
									RECEPTOR; CHAIN: A, B;	PROTEIN-PEPTIDE COMPLEX,
									PTS1-CONTAINING	TETRATRICOPEPTIDE REPEAT, TPR, 2
									PEPTIDE; CHAIN: C, D;”	HELICAL REPEAT”
262	1qqe	A	21	131	7.80E−05	0.15	0.62		VESICULAR TRANSPORT	“PROTEIN TRANSPORT HELIX-TURN-
									PROTEIN SEC17; CHAIN: A;	HELIX TPR-LIKE REPEAT, PROTEIN
										TRANSPORT”
263	1a25	A	23	148	5.10E−28	0.51	0.92		“PROTEIN KINASE C	“CALCIUM-BINDING PROTEIN CALB;
									(BETA); CHAIN: A, B;”	CALCIUM++/PHOSPHOLIPID BINDING
										PROTEIN, 2 CALCIUM-BINDING PROTEIN”
263	1byn	A	23	143	1.00E−30	0.26	0.99		SYNAPTOTAGMIN I; CHAIN:	“ENDOCYTOSIS/EXOCYTOSIS
									A;	SYNAPTOTAGMIN, C2-DOMAIN,
										EXOCYTOSIS, NEUROTRANSMITTER 2
										RELEASE, ENDOCYTOSIS/EXOCYTOSIS”
263	1cjy	A	41	144	3.90E−21	0.02	0.24		“CYTOSOLIC	“HYDROLASE CPLA2; PHOSPHOLIPASE,
									PHOSPHOLIPASE A2;	LIPID-BINDING, HYDROLASE”
									CHAIN: A, B;”
263	1djx	B	4	159	3.40E−27	0.19	−0.05		“PHOSPHOINOSITIDE-	“LIPID DEGRADATION PLC-D1;
									SPECIFIC PHOSPHOLIPASE	PHOSPHORIC DIESTER HYDROLASE,
									C, CHAIN: A, B;”	HYDROLASE, LIPID DEGRADATION, 2
										TRANSDUCER, CALCIUM-BINDING,
										PHOSPHOLIPASE C, 3
										PHOSPHOINOSITIDE-SPECIFIC”
263	1djx	A	4	159	3.40E−27	0.16	−0.11		“PHOSPHOINOSITIDE-	“LIPID DEGRADATION PLC-D1;
									SPECIFIC PHOSPHOLIPASE	PHOSPHORIC DIESTER HYDROLASE,
									C, CHAIN: A, B;”	HYDROLASE, LIPID DEGRADATION, 2
										TRANSDUCER, CALCIUM-BINDING,
										PHOSPHOLIPASE C, 3
										PHOSPHOINOSITIDE-SPECIFIC”
263	1dqv	A	25	170	1.50E−35	0.05	0.63		SYNAPTOTAGMIN III;	“ENDOCYTOSIS/EXOCYTOSIS BETA
									CHAIN: A;	SANDWICH, CALCIUM ION, C2 DOMAIN”
263	1dsy	A	23	154	6.80E−30	0.57	0.96		“PROTEIN KINASE C,	“TRANSFERASE CALCIUM++,
									ALPHA TYPE; CHAIN: A;”	PHOSPHOLIPID BINDING PROTEIN,
										CALCIUM-BINDING 2 PROTEIN,
										PHOSPHATIDYLSERINE, PROTEIN
										KINASE C”
263	1rlw		40	141	2.60E−22	0.21	0.49		PHOSPHOLIPASE A2;	“HYDROLASE CALB DOMAIN;
									CHAIN: NULL;	HYDROLASE, C2 DOMAIN, CALB
										DOMAIN”
263	1rsy		23	143	1.00E−30	0.24	0.82			CALCIUM/PHOSPHOLIPID BINDING
										PROTEIN SYNAPTOTAGMIN I (FIRST C2
										DOMAIN) (CALB) 1RSY 3
263	3rpb	A	25	151	1.70E−24	0.16	0.17		RABPHILIN 3-A; CHAIN: A;	“ENDOCYTOSIS/EXOCYTOSIS C2-
										DOMAINS, C2B-DOMAIN, RABPHILIN,
										ENDOCYTOSIS/EXOCYTOSIS”
264	1awj		236	321	1.30E−17	0.01	0.03		JTK; CHAIN: NULL;	“TRANSFERASE IL-2-INDUCIBLE T-CELL
										KINASE; TRANSFERASE, REGULATORY
										INTRAMOLECULAR COMPLEX, KINASE”
264	1aww		258	321	1.30E−16	0.31	0.81		BRUTON'S TYROSINE	“TRANSFERASE ATK, AMGX1, BPK;
									KINASE; CHAIN: NULL;	TYROSINE KINASE, X-LINKED
										AGAMMAGLOBULINEMIA, XLA, BTK,
										SH3 2 DOMAIN, TRANSFERASE”
264	1aze	A	267	322	7.80E−19	0.83	0.96		GRB2; CHAIN: A; SOS;	“COMPLEX (ADAPTOR PROTEIN/PEPTIDE)
									CHAIN: B;	ASH, GROWTH FACTOR RECEPTOR-
										BOUND PROTEIN 2; COMPLEX (ADAPTOR
										PROTEIN/PEPTIDE), SH3 DOMAIN, 2
										GUANINE-NUCLEOTIDE RELEASING
										FACTOR”
264	1csk	A	267	322	1.30E−15	0.05	1			PHOSPHOTRANSFERASE C-SRC KINASE
										(SH3 DOMAIN) (E.C.2.7.1.112) 1CSK 3
264	1gbq	A	267	322	1.00E−17	0.74	1		GRB2; CHAIN: A; SOS-1;	“COMPLEX (SIGNAL
									CHAIN: B;	TRANSDUCTION/PEPTIDE) COMPLEX
										(SIGNAL TRANSDUCTION/PEPTIDE), SH3
										DOMAIN”
264	1gbr	A	258	320	1.30E−17	0.86	0.75			“SIGNAL TRANSDUCTION PROTEIN
										GROWTH FACTOR RECEPTOR-BOUND
										PROTEIN 2 (GRB2, N-TERMINAL 1GBR 3
										SH3 DOMAIN) COMPLEXED WITH SOS-A
										PEPTIDE 1GBR 4 (NMR, 29 STRUCTURES)
										1GBR 5”
264	1gfc		269	321	3.90E−17	0.86	1			“ADAPTOR PROTEIN CONTAINING SH2
										AND SH3 GROWTH FACTOR RECEPTOR-
										BOUND PROTEIN 2 (GRB2) 1GFC 3 (C-
										TERMINAL SH3 DOMAIN) (NMR,
										MINIMIZED MEAN STRUCTURE) 1GFC 4”
264	1gfc		265	323	3.90E−17			51.2		“ADAPTOR PROTEIN CONTAINING SH2
										AND SH3 GROWTH FACTOR RECEPTOR-
										BOUND PROTEIN 2 (GRB2) 1GFC 3 (C-
										TERMINAL SH3 DOMAIN) (NMR,
										MINIMIZED MEAN STRUCTURE) 1GFC 4”
264	1gri	A	239	321	1.30E−15	0.12	0.89		“GROWTH FACTOR BOUND	“SIGNAL TRANSDUCTION ADAPTOR SH2,
									PROTEIN 2; 1GRI 5 CHAIN:	SH3 1GRI 14”
									A, B; 1GRI 6”
264	1nlo	C	271	320	2.60E−14	0.14	0.98		C-SRC; CHAIN: C; NL1 (MN7-	“COMPLEX (TRANSFERASE/PEPTIDE)
									MN2-MN1-PLPPLP); CHAIN:	SRC, SH3 DOMAIN, LIGANDS, NON-
									N;	PEPTIDE ELEMENTS, 2 COMPLEX
										(TRANSFERASE/PEPTIDE)”
264	1sem	A	269	321	1.30E−17	0.78	1		“SEM-5; 1SEM 3 CHAIN: A,	“SIGNAL TRANSDUCTION PROTEIN SRC-
									B; 1SEM 5 10-RESIDUE	HOMOLOGY 3 (SH3) DOMAIN, PEPTIDE-
									PROLINE-RICH PEPTIDE	BINDING PROTEIN, 1SEM 18 2 GUANINE
									FROM MSOS 1SEM 8 CHAIN:	NUCLEOTIDE EXCHANGE FACTOR 1SEM
									C, D 1SEM 10”	19”
264	1sem	A	265	323	1.30E−17			53.02	“SEM-5; 1SEM 3 CHAIN: A,	“SIGNAL TRANSDUCTION PROTEIN SRC-
									B; 1SEM 5 10-RESIDUE	HOMOLOGY 3 (SH3) DOMAIN, PEPTIDE-
									PROLINE-RICH PEPTIDE	BINDING PROTEIN, 1SEM 18 2 GUANINE
									FROM MSOS 1SEM 8 CHAIN:	NUCLEOTIDE EXCHANGE FACTOR 1SEM
									C, D 1SEM 10”	19”
265	1a17		415	573	6.50E−16	0.09	0.89		SERINE/THREONINE	“HYDROLASE TETRATRICOPEPTIDE, TRP;
									PROTEIN PHOSPHATASE 5;	HYDROLASE, PHOSPHATASE, PROTEIN-
									CHAIN: NULL;	PROTEIN INTERACTIONS, TPR, 2 SUPER-
										HELIX, X-RAY STRUCTURE”
265	1a17		307	488	3.90E−11	0.02	−0.09		SERINE/THREONINE	“HYDROLASE TETRATRICOPEPTIDE, TRP;
									PROTEIN PHOSPHATASE 5;	HYDROLASE, PHOSPHATASE, PROTEIN-
									CHAIN: NULL;	PROTEIN INTERACTIONS, TPR, 2 SUPER-
										HELIX, X-RAY STRUCTURE”
265	1a17		265	444	1.30E−10	0.1	0.05		SERINE/THREONINE	“HYDROLASE TETRATRICOPEPTIDE, TRP;
									PROTEIN PHOSPHATASE 5;	HYDROLASE, PHOSPHATASE, PROTEIN-
									CHAIN: NULL;	PROTEIN INTERACTIONS, TPR, 2 SUPER-
										HELIX, X-RAY STRUCTURE”
265	1a17		499	609	3.40E−07	0.27	0.12		SERINE/THREONINE	“HYDROLASE TETRATRICOPEPTIDE, TRP;
									PROTEIN PHOSPHATASE 5;	HYDROLASE, PHOSPHATASE, PROTEIN-
									CHAIN: NULL;	PROTEIN INTERACTIONS, TPR, 2 SUPER-
										HELIX, X-RAY STRUCTURE”
265	1a17		371	499	0.00068	0.14	0.77		SERINE/THREONINE	“HYDROLASE TETRATRICOPEPTIDE, TRP;
									PROTEIN PHOSPHATASE 5;	HYDROLASE, PHOSPHATASE, PROTEIN-
									CHAIN: NULL;	PROTEIN INTERACTIONS, TPR, 2 SUPER-
										HELIX, X-RAY STRUCTURE”
265	1b43	A	528	584	0.0026	−0.54	0.04		“FEN-1; CHAIN: A, B;”	“TRANSFERASE NUCLEASE, DNA
										REPAIR, DNA REPLICATION,
										TRANSFERASE”
265	1cii		56	610	1.20E−11			95.9	COLICIN IA; CHAIN: NULL;	“TRANSMEMBRANE PROTEIN COLICIN,
										BACTERIOCIN, ION CHANNEL
										FORMATION, TRANSMEMBRANE 2
										PROTEIN”
265	1d8d	A	340	533	5.20E−09	−0.18	0.18		FARNESYLTRANSFERASE	“TRANSFERASE FTASE; FTASE; FTASE,
									(ALPHA SUBUNIT); CHAIN:	PFT, PFTASE, FARNESYLTRANSFERASE,
									A;	FARNESYL 2 TRANSFERASE, CAAX, RAS,
									FARNESYLTRANSFERASE	CANCER”
									(BETA SUBUNIT); CHAIN: B;
									K-RAS4B PEPTIDE
									SUBSTRATE; CHAIN: P;
265	1e53	B	415	532	6.50E−11	0.17	1		RAS-RELATED C3	“SIGNALLING COMPLEX RAC1; P67PHOX;
									BOTULINUM TOXIN	SIGNALLING COMPLEX, GTPASE, NADPH
									SUBSTRATE 1; CHAIN: A;	OXIDASE, PROTEIN-PROTEIN 2
									NEUTROPHIL CYTOSOL	COMPLEX, TPR MOTIF”
									FACTOR 2 (NCF-2) CHAIN:
									B;
265	1e53	B	340	483	3.90E−05	0.38	0.31		RAS-RELATED C3	“SIGNALLING COMPLEX RAC1; P67PHOX;
									BOTULINUM TOXIN	SIGNALLING COMPLEX, GTPASE, NADPH
									SUBSTRATE 1; CHAIN: A;	OXIDASE, PROTEIN-PROTEIN 2
									NEUTROPHIL CYTOSOL	COMPLEX, TPR MOTIF”
									FACTOR 2 (NCF-2) CHAIN:
									B;
265	1e53	B	504	610	0.0012	0.1	0.04		RAS-RELATED C3	“SIGNALLING COMPLEX RAC1; P67PHOX;
									BOTULINUM TOXIN	SIGNALLING COMPLEX, GTPASE, NADPH
									SUBSTRATE 1; CHAIN: A;	OXIDASE, PROTEIN-PROTEIN 2
									NEUTROPHIL CYTOSOL	COMPLEX, TPR MOTIF”
									FACTOR 2 (NCF-2) CHAIN:
									B;
265	1e53	B	223	313	0.0052	0.01	0.45		RAS-RELATED C3	“SIGNALLING COMPLEX RAC1; P67PHOX;
									BOTULINUM TOXIN	SIGNALLING COMPLEX, GTPASE, NADPH
									SUBSTRATE 1; CHAIN: A;	OXIDASE, PROTEIN-PROTEIN 2
									NEUTROPHIL CYTOSOL	COMPLEX, TPR MOTIF”
									FACTOR 2 (NCF-2) CHAIN:
									B;
265	1elr	A	373	511	2.60E−15	0.16	1		TPR2A-DOMAIN OF HOP;	“CHAPERONE HOP, TPR-DOMAIN,
									CHAIN: A; HSP90-PEPTIDE	PEPTIDE-COMPLEX, HELICAL REPEAT,
									MEEVD; CHAIN: B;	HSP90, 2 PROTEIN BINDING”
265	1elr	A	457	577	2.60E−15	0.29	0.99		TPR2A-DOMAIN OF HOP;	“CHAPERONE HOP, TPR-DOMAIN,
									CHAIN: A; HSP90-PEPTIDE	PEPTIDE-COMPLEX, HELICAL REPEAT,
									MEEVD; CHAIN: B;	HSP90, 2 PROTEIN BINDING”
265	1elr	A	223	344	2.60E−12	0.08	0.98		TPR2A-DOMAIN OF HOP;	“CHAPERONE HOP, TPR-DOMAIN,
									CHAIN: A; HSP90-PEPTIDE	PEPTIDE-COMPLEX, HELICAL REPEAT,
									MEEVD; CHAIN: B;	HSP90, 2 PROTEIN BINDING”
265	1elr	A	307	446	5.20E−11	0.12	0.24		TPR2A-DOMAIIN OF HOP;	“CHAPERONE HOP, TPR-DOMAIN,
									CHAIN: A; HSP90-PEPTIDE	PEPTIDE-COMPLEX, HELICAL REPEAT,
									MEEVD; CHAIN: B;	HSP90, 2 PROTEIN BINDING”
265	1elr	A	268	404	1.70E−05	−0.28	0.12		TPR2A-DOMAIN OF HOP;	“CHAPERONE HOP, TPR-DOMAIN,
									CHAIN: A; HSP90-PEPTIDE	PEPTIDE-COMPLEX, HELICAL REPEAT,
									MEEVD; CHAIN: B;	HSP90, 2 PROTEIN BINDING”
265	1elw	A	371	511	5.20E−14	0.43	0.95		“TPR1-DOMAIN OF HOP;	“CHAPERONE HOP, TPR-DOMAIN,
									CHAIN: A, B; HSC70-	PEPTIDE-COMPLEX, HELICAL REPEAT,
									PEPTIDE; CHAIN: C, D; ”	HSC70, 2 HSP70, PROTEIN BINDING”
265	1elw	A	457	570	6.50E−13	0.13	0.93		“TPR1-DOMAIN OF HOP;	“CHAPERONE HOP, TPR-DOMAIN,
									CHAIN: A, B; HSC70-	PEPTIDE-COMPLEX, HELICAL REPEAT,
									PEPTIDE; CHAIN: C, D; ”	HSC70, 2 HSP70, PROTEIN BINDING”
265	1elw	A	201	319	2.60E−07	0	0.25		“TPR1-DOMAIN OF HOP;	“CHAPERONE HOP, TPR-DOMAIN,
									CHAIN: A, B; HSC70-	PEPTIDE-COMPLEX, HELICAL REPEAT,
									PEPTIDE; CHAIN: C, D;”	HSC70, 2 HSP70, PROTEIN BINDING”
265	1elw	A	455	587	3.40E−06	0.19	0.57		“TPR1-DOMAIN OF HOP;	“CHAPERONE HOP, TPR-DOMAIN,
									CHAIN: A, B; HSC70-	PEPTIDE-COMPLEX, HELICAL REPEAT,
									PEPTIDE; CHAIN: C, D;”	HSC70, 2 HSP70, PROTEIN BINDING”
265	1elw	A	221	347	6.80E−06	−0.13	0.07		“TPR1 -DOMAIN OF HOP;	“CHAPERONE HOP, TPR-DOMAIN,
									CHAIN: A, B; HSC70-	PEPTIDE-COMPLEX, HELICAL REPEAT,
									PEPTIDE; CHAIN: C, D;”	HSC70, 2 HSP70, PROTEIN BINDING”
265	1elw	A	367	453	0.00068	−0.03	0.76		“TPR1-DOMAIN OF HOP;	“CHAPERONE HOP, TPR-DOMAIN,
									CHAIN: A, B; HSC70-	PEPTIDE-COMPLEX, HELICAL REPEAT,
									PEPTIDE; CHAIN: C, D;”	HSC70, 2 HSP70, PROTEIN BINDING”
265	1elw	A	376	505	0.0019	0.08	0.7		“TPR1-DOMAIN OF HOP;	“CHAPERONE HOP, TPR-DOMAIN,
									CHAIN: A, B; HSC70-	PEPTIDE-COMPLEX, HELICAL REPEAT,
									PEPTIDE; CHAIN: C, D;”	HSC70, 2 HSP70, PROTEIN BINDING”
265	1fch	A	209	577	1.30E−37	0.06	1		“PEROXISOMAL	“SIGNALING PROTEIN PEROXISMORE
									TARGETING SIGNAL 1	RECEPTOR 1, PTS1-BP, PEROXIN-5, PTS1
									RECEPTOR; CHAIN: A, B;	PROTEIN-PEPTIDE COMPLEX,
									PTS1-CONTAINING	TETRATRICOPEPTIDE REPEAT, TPR, 2
									PEPTIDE; CHAIN: C, D;”	HELICAL REPEAT”
265	1fch	A	366	607	5.10E−14	−0.29	0.64		“PEROXISOMAL	“SIGNALING PROTEIN PEROXISMORE
									TARGETING SIGNAL 1	RECEPTOR 1, PTS1-BP, PEROXIN-5, PTS1
									RECEPTOR; CHAIN: A, B;	PROTEIN-PEPTIDE COMPLEX,
									PTS1-CONTAINING	TETRATRICOPEPTIDE REPEAT, TPR, 2
									PEPTIDE; CHAIN: C, D;”	HELICAL REPEAT”
265	1qja	A	310	497	1.70E−06	−0.1	0.82		“14-3-3 PROTEIN ZETA;	“COMPLEX (SIGNAL
									CHAIN: A, B;	TRANSDUCTION/PEPTIDE) COMPLEX, 14-
									PHOSPHOPEPTIDE; CHAIN:	3-3, PHOSPHOPEPTIDE, SIGNAL
									Q, R”	TRANSDUCTION”
265	1qqe	A	397	582	2.60E−22	0.17	0.76		VESICULAR TRANSPORT	“PROTEIN TRANSPORT HELIX-TURN-
									PROTEIN SEC17; CHAIN: A;	HELIX TPR-LIKE REPEAT, PROTEIN
										TRANSPORT”
266	1air		370	658	1.20E−22	0.26	0.19		PECTATE LYASE C; CHAIN:	“PECTATE CLEAVAGE PELC; PECTATE
									NULL;	CLEAVAGE, PECTINOLYITC ACTIVITY,
										TRANS-ELIMINATION”
266	1fqv	A	71	118	1.50E−14	−0.24	0.4		“SKP2; CHAIN: A, C, E, G, I,	“LIGASE CYCLIN A/CDK2-ASSOCIATED
									K, M, O; SKP1; CHAIN: B, D,	PROTEIN P45; CYCLIN A/CDK2-
									F, H, J, L, N, P;”	ASSOCIATED PROTEIN P19; SKP1, SKP2,
										F-BOX, LRR, LEUCINE-RICH REPEAT, SCF,
										UBIQUITIN, 2 E3, UBIQUITIN PROTEIN
										LIGASE”
266	1fs1	A	72	112	1.70E−13	−0.28	0.82		“CYCLIN A/CDK2-	“LIGASE SKP2 F-BOX; SKP1; SKP1, SKP2,
									ASSOCIATED P19; CHAIN:	F-BOX, LRR, LEUCINE-RICH REPEAT, SCF,
									A, C; CYCLIN A/CDK2-	UBIQUITIN, 2 E3, UBIQUITIN PROTEIN
									ASSOCIATED P45; CHAIN: B,	LIGASE”
									D;”
266	1fs2	A	69	115	1.50E−14	−0.32	0.53		“SKP2; CHAIN: A, C; SKP1;	“LIGASE CYCLIN A/CDK2-ASSOCIATED
									CHAIN: B, D;”	P45; CYCLIN A/CDK2-ASSOCIATED P19;
										SKP1, SKP2, F-BOX, LRRS, LEUCINE-RICH
										REPEATS, SCF, 2 UBIQUITIN, E3,
										UBIQUITIN PROTEIN LIGASE”
267	1btn		453	527	5.20E−14	0.53	0.6		BETA-SPECTRIN; 1BTN 4	SIGNAL TRANSDUCTION PROTEIN
									CHAIN: NULL; 1BTN 5
267	1dro		252	334	0.00013	−0.15	0.63		BETA-SPECTRIN; 1DRO 6	CYTOSKELETON
									CHAIN: NULL; 1DRO 7
267	1ez3	A	639	726	5.20E−08	0.03	−0.14		“SYNTAXIN-1A; CHAIN: A,	“ENDOCYTOSIS/EXOCYTOSIS
									B, C;”	SYNAPTOTAGMIN ASSOCIATED 35 KDA
										PROTEIN, P35A, THREE HELIX BUNDLE”
267	1fao	A	446	530	6.50E−10	0.69	0.66		DUAL ADAPTOR OF	“SIGNALING PROTEIN DAPP1, PHISH,
									PHOSPHOTYROSINE AND 3-	BAM32; PLECKSTRIN, 3-
									CHAIN: A;	PHOSPHOINOSITIDES, INOSITOL
										TETRAKISPHOSPHATE 2 SIGNAL
										TRANSDUCTION PROTEIN, ADAPTOR
										PROTEIN”
267	1fb8	A	439	530	1.30E−11	0.33	0.57		DUAL ADAPTOR OF	“SIGNALING PROTEIN DAPP1, PHISH,
									PHOSPHOTYROSINE AND 3-	BAM32; PLECKSTRIN, 3-
									CHAIN: A;	PHOSPHOINOSITIDES, INOSITOL
										TETRAKISPHOSPHATE 2 SIGNAL
										TRANSDUCTION PROTEIN, ADAPTOR
										PROTEIN”
267	1fgy	A	444	527	1.20E−12	−0.36	0.1		GRP1; CHAIN: A;	SIGNALING PROTEIN ARF1 GUANINE
										NUCLEOTIDE EXCHANGE FACTOR AND
										PH DOMAIN
267	1pls		249	345	3.90E−13	0.58	0.59			“PHOSPHORYLATION PLECKSTRIN (N-
										TERMINAL PLECKSTRIN HOMOLOGY
										DOMAIN) MUTANT 1PLS 3 WITH LEU GLU
										(HIS)6 ADDED TO THE C TERMINUS 1PLS
										4 (INS(G105-LEHHHHHH)) (NMR, 25
										STRUCTURES) 1PLS 5”
267	1pls		439	527	3.90E−11	0.26	0.41			“PHOSPHORYLATION PLECKSTRIN (N-
										TERMINAL PLECKSTRIN HOMOLOGY
										DOMAIN) MUTANT 1PLS 3 WITH LEU GLU
										(HIS)6 ADDED TO THE C TERMINUS 1PLS
										4 (INS(G105-LEHHHHHH)) (NMR, 25
										STRUCTURES) 1PLS 5”
267	1pms		242	337	6.50E−08	−0.11	0.41		SOS 1; CHAIN: NULL;	“SIGNAL TRANSDUCTION SON OF
										SEVENLESS; PLECKSTRIN, SON OF
										SEVENLESS, SIGNAL TRANSDUCTION”
270	1apm	E	1049	1351	3.40E−100			100		“TRANSFERASE(PHOSPHOTRANSFERASE)
										$C-/AMP$-DEPENDENT PROTEIN
										KINASE (E.C.2.7.1.37) ($C/APK$) 1APM 3
										(CATALYTIC SUBUNIT) ““ALPHA””
										ISOENZYME MUTANT WITH SER 139
										1APM 4 REPLACED BY ALA (/S139A$)
										COMPLEX WITH THE PEPTIDE 1APM 5
										INHIBITOR PKI(5-24) AND THE
										DETERGENT MEGA-8 1APM 6”
270	1aql		1080	1350	1.00E−56			100.26	CYCLIN-DEPENDENT	“PROTEIN KINASE CDK2; PROTEIN
									PROTEIN KINASE 2; CHAIN:	KINASE, CELL CYCLE,
									NULL;	PHOSPHORYLATION, STAUROSPORINE, 2
										CELL DIVISION, MITOSIS, INHIBITION”
270	1blx	A	1074	1350	3.40E−49			119.61	CYCLIN-DEPENDENT	“COMPLEX (INHIBITOR
									KINASE 6; CHAIN: A;	PROTEIN/KINASE) INHIBITOR PROTEIN,
									P19INK4D; CHAIN: B;	CYCLIN-DEPENDENT KINASE, CELL
										CYCLE 2 CONTROL, ALPHA/BETA,
										COMPLEX (INHIBITOR
										PROTEIN/KINASE)”
270	1cmk	E	1040	1351	0			102.82		PHOSPHOTRANSFERASE CAMP-
										DEPENDENT PROTEIN KINASE
										CATALYTIC SUBUNIT 1CMK 3
										(E.C.2.7.1.37) 1CMK 4
270	1ctp	E	1046	1351	0			105.55		TRANSFERASE(PHOSPHOTRANSFERASE)
										CAMP-DEPENDENT PROTEIN KINASE
										(E.C.2.7.1.37) (CAPK) 1CTP 3 (CATALYTIC
										SUBUNIT) 1CTP 4
270	1fgk	B	1062	1350	8.50E−39			117.87	“FGF RECEPTOR 1; CHAIN:	“PHOSPHOTRANSFERASE FGFR1K,
									A, B;”	FIBROBLAST GROWTH FACTOR
										RECEPTOR 1; TRANSFERASE, TYROSINE-
										PROTEIN KINASE, ATP-BINDING, 2
										PHOSPHORYLATION, RECEPTOR,
										PHOSPHOTRANSFERASE”
270	1fgk	A	1075	1350	6.80E−33			115.09	“FGF RECEPTOR 1; CHAIN:	“PHOSPHOTRANSFERASE FGFR1K,
									A, B;”	FIBROBLAST GROWTH FACTOR
										RECEPTOR 1; TRANSFERASE, TYROSINE-
										PROTEIN KINASE, ATP-BINDING, 2
										PHOSPHORYLATION, RECEPTOR,
										PHOSPHOTRANSFERASE”
270	1hcl		1080	1350	1.00E−58			122.13	HUMAN CYCLIN-	“PROTEIN KINASE CDK2; TRANSFERASE,
									DEPENDENT KINASE 2;	SERINE/THREONINE PROTEIN KINASE,
									CHAIN: NULL;	ATP-BINDING, 2 CELL CYCLE, CELL
										DIVISION, MITOSIS, PHOSPHORYLATION”
270	1ir3	A	1068	1351	6.80E−30			99.63	INSULIN RECEPTOR;	“COMPLEX (TRANSFERASE/SUBSTRATE)
									CHAIN: A; PEPTIDE	TYROSINE KINASE, SIGNAL
									SUBSTRATE; CHAIN: B;	TRANSDUCTION,
										PHOSPHOTRANSFERASE, 2 COMPLEX
										(KINASE/PEPTIDE SUBSTRATE/ATP
										ANALOG), ENZYME, 3 COMPLEX
										(TRANSFERASE/SUBSTRATE)”
270	1phk		1076	1351	3.40E−86			114.42	PHOSPHORYLASE KINASE;	“KINASE RABBIT MUSCLE
									CHAIN: NULL;	PHOSPHORYLASE KINASE; GLYCOGEN
										METABOLISM, TRANSFERASE,
										SERINE/THREONINE-PROTEIN, 2 KINASE,
										ATP-BINDING, CALMODULIN-BINDING”
271	1aql		251	447	6.80E−24	−0.18	0.23		CYCLIN-DEPENDENT	“PROTEIN KINASE CDK2; PROTEIN
									PROTEIN KINASE 2; CHAIN:	KINASE, CELL CYCLE,
									NULL;	PHOSPHORYLATION, STAUROSPORINE, 2
										CELL DIVISION, MITOSIS, INHIBITION”
271	1b6c	B	191	548	1.20E−55	0.38	0.45		“FK506-BINDING PROTEIN;	“COMPLEX (ISOMERASE/PROTEIN
									CHAIN: A, C, E, G; TGF-B	KINASE) FKBP12; SERINE/THREONINE-
									SUPERFAMILY RECEPTOR	PROTEIN KINASE RECEPTOR R4;
									TYPE I; CHAIN: B, D, F, H;”	COMPLEX (ISOMERASE/PROTEIN
										KINASE), RECEPTOR 2
										SERINE/THREONINE KINASE”
271	1b6c	B	259	443	3.40E−27	−0.08	0.13		“FK506-BINDING PROTEIN;	“COMPLEX (ISOMERASE/PROTEIN
									CHAIN: A, C, E, G; TGF-B	KINASE) FKBP12; SERINE/THREONINE-
									SUPERFAMILY RECEPTOR	PROTEIN KINASE RECEPTOR R4;
									TYPE I; CHAIN: B, D, F, H;”	COMPLEX (ISOMERASE/PROTEIN
										KINASE), RECEPTOR 2
										SERINE/THREONINE KINASE”
271	1byg	A	259	449	3.40E−31	0.02	0.52		C-TERMINAL SRC KINASE;	“TRANSFERASE CSK; PROTEIN KINASE,
									CHAIN: A;	C-TERMINAL SRC KINASE,
										PHOSPHORYLATION, 2 STAUROSPORINE,
										TRANSFERASE”
271	1byg	A	194	233	5.20E−06	0.06	0.15		C-TERMINAL SRC KINASE;	“TRANSFERASE CSK; PROTEIN KINASE,
									CHAIN: A;	C-TERMINAL SRC KINASE,
										PHOSPHORYLATION, 2 STAUROSPORINE,
										TRANSFERASE”
271	1f3m	C	258	449	5.10E−28	0.16	0.18		“SERINE/THREONINE-	“TRANSFERASE KINASE DOMAIN,
									PROTEIN KINASE PAK-	AUTOINHIBITORY FRAGMENT,
									ALPHA; CHAIN: A, B;	HOMODIMER”
									SERINE/THREONINE-
									PROTEIN KINASE PAK-
									ALPHA; CHAIN: C, D;”
271	1fgk	B	259	445	5.10E−32	0.13	0.34		“FGF RECEPTOR 1; CHAIN:	“PHOSPHOTRANSFERASE FGFR1K,
									A, B;”	FIBROBLAST GROWTH FACTOR
										RECEPTOR 1; TRANSFERASE, TYROSINE-
										PROTEIN KINASE, ATP-BTNDING, 2
										PHOSPHORYLATION, RECEPTOR,
										PHOSPHOTRANSFERASE”
271	1fgk	A	275	445	1.70E−30	0.33	0.55		“FGF RECEPTOR 1; CHAIN:	“PHOSPHOTRANSFERASE FGFR1K,
									A, B;”	FIBROBLAST GROWTH FACTOR
										RECEPTOR 1; TRANSFERASE, TYROSINE-
										PROTEIN KINASE, ATP-BINDING, 2
										PHOSPHORYLATION, RECEPTOR,
										PHOSPHOTRANSFERASE”
271	1fgk	B	191	547	3.90E−29	−0.2	0.68		“FGF RECEPTOR 1; CHAIN:	“PHOSPHOTRANSFERASE FGFR1K,
									A, B;”	FIBROBLAST GROWTH FACTOR
										RECEPTOR 1; TRANSFERASE, TYROSINE-
										PROTEIN KINASE, ATP-BINDING, 2
										PHOSPHORYLATION, RECEPTOR,
										PHOSPHOTRANSFERASE”
271	1fmk		258	449	5.10E−34	0.23	0.24		TYROSINE-PROTEIN	“PHOSPHOTRANSFERASE C-SRC, P60-
									KINASE SRC; CHAIN: NULL;	SRC; SRC, TYROSINE KINASE,
										PHOSPHORYLATION, SH2, SH3, 2
										PHOSPHOTYROSINE, PROTO-ONCOGENE,
										PHOSPHOTRANSFERASE”
271	1fmk		193	547	1.30E−30	0.03	0.18		TYROSINE-PROTEIN	“PHOSPHOTRANSFERASE C-SRC, P60-
									KINASE SRC; CHAIN: NULL;	SRC; SRC, TYROSINE KINASE,
										PHOSPHORYLATION, SH2, SH3, 2
										PHOSPHOTYROSINE, PROTO-ONCOGENE,
										PHOSPHOTRANSFERASE”
271	1fpu	A	256	445	6.80E−33	−0.09	0.54		“PROTO-ONCOGENE	“TRANSFERASE P150, C-ABL; KINASE,
									TYROSINE-PROTEIN	KINASE INHIBITOR, STI-571, ACTIVATION
									KINASE ABL; CHAIN: A, B;”	LOOP”
271	1hcl		251	447	1.70E−27	0.38	0.49		HUMAN CYCLIN-	“PROTEIN KINASE CDK2; TRANSFERASE,
									DEPENDENT KINASE 2;	SERINE/THREONINE PROTEIN KINASE,
									CHAIN: NULL;	ATP-BINDING, 2 CELL CYCLE, CELL
										DIVISION, MITOSIS, PHOSPHORYLATION”
271	1ir3	A	259	445	3.40E−30	0.03	0.22		INSULIN RECEPTOR;	“COMPLEX (TRANSFERASE/SUBSTRATE)
									CHAIN: A; PEPTIDE	TYROSINE KINASE, SIGNAL
									SUBSTRATE; CHAIN: B;	TRANSDUCTION,
										PHOSPHOTRANSFERASE, 2 COMPLEX
										(KINASE/PEPTIDE SUBSTRATE/ATP
										ANALOG), ENZYME, 3 COMPLEX
										(TRANSFERASE/SUBSTRATE)”
271	1ir3	A	290	547	2.60E−28	0.44	0.24		INSULIN RECEPTOR;	“COMPLEX (TRANSFERASE/SUBSTRATE)
									CHAIN: A; PEPTIDE	TYROSINE KINASE, SIGNAL
									SUBSTRATE; CHAIN: B;	TRANSDUCTION,
										PHOSPHOTRANSFERASE, 2 COMPLEX
										(KINASE/PEPTIDE SUBSTRATE/ATP
										ANALOG), ENZYME, 3 COMPLEX
										(TRANSFERASE/SUBSTRATE)”
271	1ir3	A	193	233	0.0026	−0.32	0.07		INSULIN RECEPTOR;	“COMPLEX (TRANSFERASE/SUBSTRATE)
									CHAIN: A; PEPTIDE	TYROSINE KINASE, SIGNAL
									SUBSTRATE; CHAIN: B;	TRANSDUCTION,
										PHOSPHOTRANSFERASE, 2 COMPLEX
										(KINASE/PEPTIDE SUBSTRATE/ATP
										ANALOG), ENZYME, 3 COMPLEX
										(TRANSFERASE/SUBSTRATE)”
271	1phk		251	449	5.10E−24	0.16	0.47		PHOSPHORYLASE KINASE;	“KINASE RABBIT MUSCLE
									CHAIN: NULL;	PHOSPHORYLASE KINASE; GLYCOGEN
										METABOLISM, TRANSFERASE,
										SERINE/THREONINE-PROTEIN, 2 KINASE,
										ATP-BINDING, CALMODULIN-BINDING”
271	1qcf	A	256	449	1.70E−31	0.21	0.83		HAEMATOPOETIC CELL	“TYROSINE KINASE TYROSINE KINASE-
									KINASE (HCK); CHAIN: A;	INHIBITOR COMPLEX, DOWN-
										REGULATED KINASE, 2 ORDERED
										ACTIVATION LOOP”
271	1qcf	A	290	547	1.20E−28	0.53	0.88		HAEMATOPOETIC CELL	“TYROSINE KINASE TYROSINE KINASE-
									KINASE (HCK); CHAIN: A;	INHIBITOR COMPLEX, DOWN-
										REGULATED KINASE, 2 ORDERED
										ACTIVATION LOOP”
271	1qcf	A	194	233	0.00039	0.16	0.42		HAEMATOPOETIC CELL	“TYROSINE KINASE TYROSINE KINASE-
									KINASE (HCK); CHAIN: A;	INHIBITOR COMPLEX, DOWN-
										REGULATED KINASE, 2 ORDERED
										ACTIVATION LOOP”
271	1qpc	A	259	449	3.40E−35	0.33	0.29		LCK KINASE; CHAIN: A;	TRANSFERASE ALPHA BETA FOLD
271	1qpc	A	290	547	5.20E−30	0.5	0.74		LCK KINASE; CHAIN: A;	TRANSFERASE ALPHA BETA FOLD
271	1qpc	A	187	233	0.00039	−0.53	0.16		LCK KINASE; CHAIN: A;	TRANSFERASE ALPHA BETA FOLD
271	1vr2	A	259	445	5.10E−25	0.15	−0.06		VASCULAR ENDOTHELIAL	TRANSFERASE KDR; TYROSINE KINASE
									GROWTH FACTOR
									RECEPTOR CHAIN: A;
272	1got	B	837	1188	1.70E−63			141.57	GT-ALPHA/GI-ALPHA	“COMPLEX (GTP-BINDING/TRANSDUCER)
									CHIMERA; CHAIN: A; GT-	BETA1, TRANSDUCIN BETA SUBUNIT;
									BETA; CHAIN: B; GT-	GAMMA1, TRANSDUCIN GAMMA
									GAMMA; CHAIN: G;	SUBUNIT; COMPLEX (GTP-
										BINDING/TRANSDUCER), G PROTEIN,
										HETEROTRIMER 2 SIGNAL
										TRANSDUCTION”
273	1got	B	502	861	1.70E−59			140.82	GT-ALPHA/GI-ALPHA	“COMPLEX (GTP-BINDING/TRANSDUCER)
									CHIMERA; CHAIN: A; GT-	BETA1, TRANSDUCIN BETA SUBUNIT;
									BETA; CHAIN: B; GT-	GAMMA1, TRANSDUCIN GAMMA
									GAMMA; CHAIN: G;	SUBUNIT; COMPLEX (GTP-
										BINDING/TRANSDUCER), G PROTEIN,
										HETEROTRIMER 2 SIGNAL
										TRANSDUCTION”
277	1rgp		161	364	6.80E−36			86.57	RHOGAP; CHAIN: NULL;	“G-PROTEIN CDC42 GTPASE-ACTIVATING
										PROTEIN; G-PROTEIN, GAP, SIGNAL-
										TRANSDUCTION”
277	1tx4	A	166	378	1.00E−34			85.18	P50-RHOGAP; CHAIN: A;	“COMPLEX(GTPASE ACTIVATN/PROTO-
									TRANSFORMING PROTEIN	ONCOGENE) GTPASE-ACTIVATING
									RHOA; CHAIN: B;	PROTEIN RHOGAP; COMPLEX (GTPASE
										ACTIVATION/PROTO-ONCOGENE),
										GTPASE, 2 TRANSITION STATE, GAP”
278	1ctq	A	4	177	6.30E−22	0.49	1		TRANSFORMING PROTEIN	“SIGNALING PROTEIN G PROTEIN, GTP
									P21/H-RAS-1; CHAIN: A;	HYDROLYSIS, KINETIC
										CRYSTALLOGRAPHY, 2 SIGNALING
										PROTEIN”
278	1ctq	A	2	180	6.30E−22			77.6	TRANSFORMING PROTEIN	“SIGNALING PROTEIN G PROTEIN, GTP
									P21/H-RAS-1; CHAIN: A;	HYDROLYSIS, KINETIC
										CRYSTALLOGRAPHY, 2 SIGNALING
										PROTEIN”
278	1cxz	A	1	177	6.30E−22	−0.1	0.75		HIS-TAGGED	“SIGNALING PROTEIN PROTEIN-PROTEIN
									TRANSFORMING PROTEIN	COMPLEX, ANTIPARALLEL COILED-
									RHOA(0-181); CHAIN: A;	COIL”
									PKN; CHAIN: B;
278	1ds6	A	2	177	2.10E−22	0.31	0.93		RAS-RELATED C3	“SIGNALING PROTEIN P21-RAC2; RHO
									BOTULINUM TOXIN	GDI 2, RHO-GDI BETA, LY-GDI; BETA
									SUBSTRATE 2; CHAIN: A;	SANDWHICH, PROTEIN-PROTEIN
									RHO GDP-DISSOCIATION	COMPLEX, G-DOMAIN, 2
									INHIBITOR 2; CHAIN: B;	IMMUNOGLOBULIN FOLD, WALKER
										FOLD, GTP-BINDING PROTEIN”
278	1hur	A	5	175	4.20E−17	0.16	0.03		“HUMAN ADP-	“PROTEIN TRANSPORT GDP-BINDING,
									RIBOSYLATION FACTOR 1;	MEMBRANE TRAFFICKIN, NON-
									1HUR 5 CHAIN: A, B; 1HUR	MYRISTOYLATED 1HUR 16”
									7”
278	1ibr	A	5	177	1.10E−23	0.08	0.8		“RAN; CHAIN: A, C;	“SMALL GTPASE KARYOPHERIN BETA,
									IMPORTIN BETA SUBUNIT;	P95 SMALL GTPASE, NUCLEAR
									CHAIN: B, D;”	TRANSPORT RECEPTOR”
278	1ibr	A	3	184	1.10E−23			56.34	“RAN; CHAIN: A, C;	“SMALL GTPASE KARYOPHERIN BETA,
									IMPORTIN BETA SUBUNIT;	P95 SMALL GTPASE, NUCLEAR
									CHAIN: B, D;”	TRANSPORT RECEPTOR”
278	1kao		19	177	1.90E−18	0.45	1		RAP2A; CHAIN: NULL;	“GTP-BINDING PROTEIN GTP-BINDING
										PROTEIN, SMALL G PROTEIN, RAP2, GDP,
										RAS”
278	1kao		2	180	1.90E−18			89.76	RAP2A; CHAIN: NULL;	“GTP-BINDING PROTEIN GTP-BINDING
										PROTEIN, SMALL G PROTEIN, RAP2, GDP,
										RAS”
278	1rrp	C	5	177	1.50E−23	0.37	0.9		“RAN; CHAIN: A, C;	“COMPLEX (SMALL GTPASE/NUCLEAR
									NUCLEAR PORE COMPLEX	PROTEIN) COMPLEX (SMALL
									PROTEIN NUP358; CHAIN: B,	GTPASE/NUCLEAR PROTEIN), SMALL
									D;”	GTPASE, 2 NUCLEAR TRANSPORT”
278	1rrp	C	2	195	1.50E−23			57.02	“RAN; CHAIN: A, C;	“COMPLEX (SMALL GTPASE/NUCLEAR
									NUCLEAR PORE COMPLEX	PROTEIN) COMPLEX (SMALL
									PROTEIN NUP358; CHAIN: B,	GTPASE/NUCLEAR PROTEIN), SMALL
									D;”	GTPASE, 2 NUCLEAR TRANSPORT”
278	1zbd	A	5	177	4.20E−26	0.49	1		RAB-3A; CHAIN: A;	“COMPLEX (GTP-BINDING/EFFECTOR)
									RABPHILIN-3A; CHAIN: B;	RAS-RELATED PROTEIN RAB3A;
										COMPLEX (GTP-BINDING/EFFECTOR), G
										PROTEIN, EFFECTOR, RABCDR, 2
										SYNAPTIC EXOCYTOSIS, RAB PROTEIN,
										RAB3A, RABPHILIN”
278	1zbd	A	1	186	4.20E−26			57	RAB-3A; CHAIN: A;	“COMPLEX (GTP-BINDING/EFFECTOR)
									RABPHILIN-3A; CHAIN: B;	RAS-RELATED PROTEIN RAB3A;
										COMPLEX (GTP-BINDING/EFFECTOR), G
										PROTEIN, EFFECTOR, RABCDR, 2
										SYNAPTIC EXOCYTOSIS, RAB PROTEIN,
										RAB3A, RABPHILIN”
278	2ngr	A	4	203	6.30E−22	0.02	0.53		GTP BINDING PROTEIN	“HYDROLASE CDC42/CDC42GAP;
									(G25K); CHAIN: A; GTPASE	CDC42/CDC42GAP; TRANSITION STATE,
									ACTIVATING PROTEIN	G-PROTEIN, GAP, CDC42, ALF3.,
									(RHG); CHAIN: B;	HYDROLASE”
278	2ngr	A	2	191	6.30E−22			55.9	GTP BINDING PROTEIN	“HYDROLASE CDC42/CDC42GAP;
									(G25K); CHAIN: A; GTPASE	CDC42/CDC42GAP; TRANSITION STATE,
									ACTIVATING PROTEIN	G-PROTEIN, GAP, CDC42, ALF3.,
									(RHG); CHAIN: B;	HYDROLASE”
278	3rab	A	5	177	4.20E−26	0.44	1		RAB3A; CHAIN: A;	“HYDROLASE G PROTEIN, VESICULAR
										TRAFFICKING, GTP HYDROLYSIS, RAB 2
										PROTEIN, NEUROTRANSMITTER
										RELEASE, HYDROLASE”
278	3rab	A	1	181	4.20E−26			64.51	RAB3A; CHAIN: A;	“HYDROLASE G PROTEIN, VESICULAR
										TRAFFICKING, GTP HYDROLYSIS, RAB 2
										PROTEIN, NEUROTRANSMITTER
										RELEASE, HYDROLASE”
284	1qqe	A	201	485	1.20E−10			81.84	VESICULAR TRANSPORT	“PROTEIN TRANSPORT HELIX-TURN-
									PROTEIN SEC17; CHAIN: A;	HELIX TPR-LIKE REPEAT, PROTEIN
										TRANSPORT”
292	1cly	A	11	142	3.20E−44			59.45	RAS-RELATED PROTEIN	“SIGNALING PROTEIN GTP-BINDING
									RAP-1A; CHAIN: A; PROTOONKOGENE	PROTEINS, PROTEIN-PROTEIN COMPLEX,
									SERINE/THREONINE	EFFECTORS”
									PROTEIN KINASE CHAIN: B;
292	1ctq	A	11	143	4.80E−47			73.8	TRANSFORMING PROTEIN	“SIGNALING PROTEIN G PROTEIN, GTP
									P21/H-RAS-1; CHAIN: A;	HYDROLYSIS, KINETIC
										CRYSTALLOGRAPHY, 2 SIGNALING
										PROTEIN”
292	1ibr	A	11	148	3.20E−30			51.93	“RAN; CHAIN: A, C;	“SMALL GTPASE KARYOPHERIN BETA,
									IMPORTIN BETA SUBUNIT;	P95 SMALL GTPASE, NUCLEAR
									CHAIN: B, D;”	TRANSPORT RECEPTOR”
292	1kao		11	143	8.00E−42			59.64	RAP2A; CHAIN: NULL;	“GTP-BINDING PROTEIN GTP-BINDING
										PROTEIN, SMALL G PROTEIN, RAP2, GDP,
										RAS”
292	1plj		11	142	9.60E−44			60.42		“ONCOGENE PROTEIN C-H-RAS P21
										PROTEIN MUTANT WITH GLY 12
										REPLACED BY PRO 1PLJ3 (G12P)
										COMPLEXED WITH P3-1-(2-
										NITROPHENYL)ETHYL- 1PLJ4
										GUANOSINE-5′-(B,G-IMIDO)-
										TRIPHOSPHATE 1PLJ5”
292	1rrp	C	9	158	1.30E−30			51.49	“RAN; CHAIN: A, C;	“COMPLEX (SMALL GTPASE/NUCLEAR
									NUCLEAR PORE COMPLEX	PROTEIN) COMPLEX (SMALL
									PROTEIN NUP358; CHAIN: B,	GTPASE/NUCLEAR PROTEIN), SMALL
									D;”	GTPASE, 2 NUCLEAR TRANSPORT”
292	1zbd	A	6	148	4.80E−45			101.23	RAB-3A; CHAIN: A;	“COMPLEX (GTP-BINDING/EFFECTOR)
									RABPHILIN-3A; CHAIN: B;	RAS-RELATED PROTEIN RAB3A;
										COMPLEX (GTP-BINDING/EFFECTOR), G
										PROTEIN, EFFECTOR, RABCDR, 2
										SYNAPTIC EXOCYTOSIS, RAB PROTEIN,
										RAB3A, RABPHILIN”
292	3rab	A	7	143	3.20E−44			107.28	RAB3A; CHAIN: A;	“HYDROLASE G PROTEIN, VESICULAR
										TRAFFICKING, GTP HYDROLYSIS, RAB 2
										PROTEIN, NEUROTRANSMITTER
										RELEASE, HYDROLASE”
293	1a06		274	582	8.00E−97			164.46	CALCIUM/CALMODULIN-	“KINASE KINASE, SIGNAL
									DEPENDENT PROTEIN	TRANSDUCTION,
									KINASE; CHAIN: NULL;	CALCIUM/CALMODULIN”
293	1apm	E	248	588	0			122.98		“TRANSFERASE(PHOSPHOTRANSFERASE)
										$C-/AMP$-DEPENDENT PROTEIN
										KINASE (E.C.2.7.1.37) ($C/APK$) 1APM 3
										(CATALYTIC SUBUNIT) ““ALPHA””
										ISOENZYME MUTANT WITH SER 139
										1APM 4 REPLACED BY ALA (/S139A$)
										COMPLEX WITH THE PEPTIDE 1APM 5
										INHIBITOR PKI(5-24) AND THE
										DETERGENT MEGA-8 1APM 6”
293	1cmk	E	231	588	0			122.96		PHOSPHOTRANSFERASE CAMP-
										DEPENDENT PROTEIN KINASE
										CATALYTIC SUBUNIT 1CMK 3
										(E.C.2.7.1.37) 1CMK 4
293	1ctp	E	235	585	0			125.4		TRANSFERASE(PHOSPHOTRANSFERASE)
										CAMP-DEPENDENT PROTEIN KINASE
										(E.C.2.7.1.37) (CAPK) 1CTP 3 (CATALYTIC
										SUBUNIT) 1CTP4
293	1koa		249	596	4.20E−95			178.83	TWITCHIN; CHAIN: NULL;	“KINASE KINASE, TWITCHIN,
										INTRASTERIC REGULATION”
293	1kob	A	251	590	8.00E−94			252.1	“TWITCHIN; CHAIN: A, B;”	“KINASE KINASE, TWITCHIN,
										INTRASTERIC REGULATION”
293	1tki	A	277	596	5.60E−95			226.87	“TITIN; CHAIN: A, B;”	“SERINE KINASE SERINE KINASE, TITIN,
										MUSCLE, AUTOINHIBITION”
294	1byl	A	92	315	2.80E−45			85.97	PIX; CHAIN: A;	“TRANSPORT PROTEIN RHO-GTPASE
										EXCHANGE FACTOR, TRANSPORT
										PROTEIN”
297	1got	B	227	546	6.40E−69			117.61	GT-ALPHA/GI-ALPHA	“COMPLEX (GTP-BINDING/TRANSDUCER)
									CHIMERA; CHAIN: A; GT-	BETA1, TRANSDUCIN BETA SUBUNIT;
									BETA; CHAIN: B; GT-	GAMMA1, TRANSDUCIN GAMMA
									GAMMA; CHAIN: G;	SUBUNIT; COMPLEX (GTP-
										BINDING/TRANSDUCER), G PROTEIN,
										HETEROTRIMER 2 SIGNAL
										TRANSDUCTION”
298	1got	B	180	514	1.60E−65			111.63	GT-ALPHA/GI-ALPHA	“COMPLEX (GTP-BINDING/TRANSDUCER)
									CHIMERA; CHAIN: A; GT-	BETA1, TRANSDUCIN BETA SUBUNIT;
									BETA; CHAIN: B; GT-	GAMMA1, TRANSDUCIN GAMMA
									GAMMA; CHAIN: G;	SUBUNIT; COMPLEX (GTP-
										BINDING/TRANSDUCER), G PROTEIN,
										HETEROTRIMER 2 SIGNAL
										TRANSDUCTION”
302	1alh	A	279	355	1.30E−26			51.07	“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
302	1mey	C	279	354	4.80E−46			58.97	“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
303	1a17		76	234	1.30E−26			95.13	SERINE/THREONINE	“HYDROLASE TETRATRICOPEPTIDE, TRP;
									PROTEIN PHOSPHATASE 5;	HYDROLASE, PHOSPHATASE, PROTEIN-
									CHAIN: NULL;	PROTEIN INTERACTIONS, TPR, 2 SUPER-
										HELIX, X-RAY STRUCTURE”
303	1qqe	A	1	290	6.40E−07			62.22	VESICULAR TRANSPORT	“PROTEIN TRANSPORT HELIX-TURN-
									PROTEIN SEC17; CHAIN: A;	HELIX TPR-LIKE REPEAT, PROTEIN
										TRANSPORT”
305	1aut	L	141	238	4.20E−25	0.27	0.11		“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)”
305	1aut	L	178	269	1.00E−11	0.21	0.19		“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)”
305	1aut	L	141	237	4.20E−25			59.69	“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)”
305	1dan	L	129	230	2.10E−27	0.07	0.54		“BLOOD COAGULATION	“BLOOD COAGULATION, SERINE
									FACTOR VIIA; CHAIN: L, H;	PROTEASE, COMPLEX, CO-FACTOR, 2
									SOLUBLE TISSUE FACTOR;	RECEPTOR ENZYME, INHIBITOR, GLA,
									CHAIN: T, U; D-PHE-PHE-	EGF, 3 COMPLEX (SERINE
									ARG-	PROTEASE/COFACTOR/LIGAND)”
									CHLOROMETHYLKETONE
									(DFFRCMK) WITH CHAIN:
									C;”
305	1dan	L	182	266	1.40E−12	0.02	−0.05		“BLOOD COAGULATION	“BLOOD COAGULATION, SERINE
									FACTOR VIIA; CHAIN: L, H;	PROTEASE, COMPLEX, CO-FACTOR, 2
									SOLUBLE TISSUE FACTOR;	RECEPTOR ENZYME, INHIBITOR, GLA,
									CHAIN: T, U; D-PHE-PHE-	EGF, 3 COMPLEX (SERINE
									ARG-	PROTEASE/COFACTOR/LIGAND)”
									CHLOROMETHYLKETONE
									(DFFRCMK) WITH CHAIN:
									C;”
305	1dan	L	119	232	2.10E−27			69.56	“BLOOD COAGULATION	“BLOOD COAGULATION, SERINE
									FACTOR VIIA; CHAIN: L, H;	PROTEASE, COMPLEX, CO-FACTOR, 2
									SOLUBLE TISSUE FACTOR;	RECEPTOR ENZYME, INHIBITOR, GLA,
									CHAIN: T, U; D-PHE-PHE-	EGF, 3 COMPLEX (SERINE
									ARG-	PROTEASE/COFACTOR/LIGAND)”
									CHLOROMETHYLKETONE
									(DFFRCMK) WITH CHAIN:
									C;”
305	1dva	L	142	230	1.50E−23	0.44	0.83		“DES-GLA FACTOR VIIA	HYDROLASE/HYDROLASE INHIBITOR
									(HEAVY CHAIN); CHAIN: H,	PROTEIN-PEPTIDE COMPLEX
									I; DES-GLA FACTOR VIIA
									(LIGHT CHAIN); CHAIN: L,
									M; (DPN)-PHE-ARG; CHAIN:
									C, D; PEPTIDE E-76; CHAIN:
									X, Y;”
305	1dx5	I	146	256	4.20E−20	0.12	−0.07		“THROMBIN LIGHT CHAIN;	“SERINE PROTEINASE COAGULATION
									CHAIN: A, B, C, D;	FACTOR II; COAGULATION FACTOR II;
									THROMBIN HEAVY CHAIN;	FETOMODULIN, TM, CD141 ANTIGEN;
									CHAIN: M, N, O, P;	EGR-CMK SERINE PROTEINASE, EGF-
									THROMBOMODULIN;	LIKE DOMAINS, ANTICOAGULANT
									CHAIN: I, J, K, L; THROMBIN	COMPLEX, 2 ANTIFIBRINOLYTIC
									INHIBITOR L-GLU-L-GLY-L-	COMPLEX”
									ARM; CHAIN: E, F, G, H;”
305	1dx5	I	143	257	1.50E−14	0.23	0.15		“THROMBIN LIGHT CHAIN;	“SERINE PROTEINASE COAGULATION
									CHAIN: A, B, C, D;	FACTOR II; COAGULATION FACTOR II;
									THROMBIN HEAVY CHAIN;	FETOMODULIN, TM, CD141 ANTIGEN;
									CHAIN: M, N, O, P;	EGR-CMK SERINE PROTEINASE, EGF-
									THROMBOMODULIN;	LIKE DOMAINS, ANTICOAGULANT
									CHAIN: I, J, K, L; THROMBIN	COMPLEX, 2 ANTIFIBRINOLYTIC
									INHIBITOR L-GLU-L-GLY-L-	COMPLEX”
									ARM; CHAIN: E, F, G, H;”
305	1dx5	I	181	275	1.70E−13	0.2	−0.18		“THROMBIN LIGHT CHAIN;	“SERINE PROTEINASE COAGULATION
									CHAIN: A, B, C, D;	FACTOR II; COAGULATION FACTOR II;
									THROMBIN HEAVY CHAIN;	FETOMODULIN, TM, CD141 ANTIGEN;
									CHAIN: M, N, O, P;	EGR-CMK SERINE PROTEINASE, EGF-
									THROMBOMODULIN;	LIKE DOMAINS, ANTICOAGULANT
									CHAIN: I, J, K, L; THROMBIN	COMPLEX, 2 ANTIFIBRINOLYTIC
									INHIBITOR L-GLU-L-GLY-L-	COMPLEX”
									ARM; CHAIN: E, F, G, H;”
305	1emn		182	260	8.50E−17	0.26	0.69		FIBRILLIN; CHAIN: NULL;	“MATRIX PROTEIN EXTRACELLULAR
										MATRIX, CALCIUM-BINDING,
										GLYCOPROTEIN, 2 REPEAT, SIGNAL,
										MULTIGENE FAMILY, DISEASE
										MUTATION, 3 EGF-LIKE DOMAIN,
										HUMAN FIBRILLIN-1 FRAGMENT,
										MATRIX PROTEIN”
305	1emn		141	219	3.40E−19			58.55	FIBRILLIN; CHAIN: NULL;	“MATRIX PROTEIN EXTRACELLULAR
										MATRIX, CALCIUM-BINDING,
										GLYCOPROTEIN, 2 REPEAT, SIGNAL,
										MULTIGENE FAMILY, DISEASE
										MUTATION, 3 EGF-LIKE DOMAIN,
										HUMAN FIBRILLIN-1 FRAGMENT,
										MATRIX PROTEIN”
305	1ext	A	18	176	8.40E−12			52.2	“TUMOR NECROSIS	“SIGNALLING PROTEIN BINDING
									FACTOR RECEPTOR;	PROTEIN, CYTOKINE, SIGNALLING
									CHAIN: A, B;”	PROTEIN”
305	1fak	L	142	232	8.40E−24	0.26	0.34		BLOOD COAGULATION	“BLOOD CLOTTING COMPLEX(SERINE
									FACTOR VIIA; CHAIN: L;	PROTEASE/COFACTOR/LIGAND), BLOOD
									BLOOD COAGULATION	COAGULATION, 2 SERINE PROTEASE,
									FACTOR VIIA; CHAIN: H;	COMPLEX, CO-FACTOR, RECEPTOR
									SOLUBLE TISSUE FACTOR;	ENZYME, 3 INHIBITOR, GLA, EGF,
									CHAIN: T; 5L15; CHAIN: I;	COMPLEX (SERINE 4
										PROTEASE/COFACTOR/LIGAND), BLOOD
										CLOTTING”
305	1fak	L	182	266	1.40E−12	0	−0.03		BLOOD COAGULATION	“BLOOD CLOTTING COMPLEX(SERINE
									FACTOR VIIA; CHAIN: L;	PROTEASE/COFACTOR/LIGAND), BLOOD
									BLOOD COAGULATION	COAGULATION, 2 SERINE PROTEASE,
									FACTOR VIIA; CHAIN: H;	COMPLEX, CO-FACTOR, RECEPTOR
									SOLUBLE TISSUE FACTOR;	ENZYME, 3 INHIBITOR, GLA, EGF,
									CHAIN: T; 5L15; CHAIN: I;	COMPLEX (SERINE 4
										PROTEASE/COFACTOR/LIGAND), BLOOD
										CLOTTING”
305	1klo		73	238	4.20E−29	0.14	0.39		LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
305	1klo		114	250	2.10E−26	0.09	−0.03		LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
305	1klo		34	198	1.10E−25	0.02	0.01		LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
305	1klo		71	238	4.20E−29			79.78	LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
305	1pfx	L	182	266	1.70E−12	0.34	0.42		“FACTOR IXA; CHAIN: C, L,;	“COMPLEX (BLOOD
									D-PHE-PRO-ARG; CHAIN: I;”	COAGULATION/INHIBITOR) CHRISTMAS
										FACTOR; COMPLEX, INHIBITOR,
										HEMOPHILIA/EGF, BLOOD
										COAGULATION, 2 PLASMA, SERINE
										PROTEASE, CALCIUM-BINDING,
										HYDROLASE, 3 GLYCOPROTEIN”
305	1pfx	L	116	243	3.40E−14			78.6	“FACTOR IXA; CHAIN: C, L,;	“COMPLEX (BLOOD
									D-PHE-PRO-ARG; CHAIN: I;”	COAGULATION/INHIBITOR) CHRISTMAS
										FACTOR; COMPLEX, INHIBITOR,
										HEMOPHILIA/EGF, BLOOD
										COAGULATION, 2 PLASMA, SERINE
										PROTEASE, CALCIUM-BINDING,
										HYDROLASE, 3 GLYCOPROTEIN”
305	1pp2	R	66	186	4.20E−28	0.03	−0.12			HYDROLASE CALCIUM-FREE
										PHOSPHOLIPASE A = 2 = (E.C.3.1.1.4) 1PP2 4
305	1qfk	L	148	238	4.20E−28	0.12	0.49		COAGULATION FACTOR	“SERINE PROTEASE FVIIA; FVIIA; BLOOD
									VIIA (LIGHT CHAIN);	COAGULATION, SERINE PROTEASE”
									CHAIN: L; COAGULATION
									FACTOR VIIA (HEAVY
									CHAIN); CHAIN: H;
									TRIPEPTIDYL INHIBITOR;
									CHAIN: C;
305	1qfk	L	147	234	4.20E−28			61.83	COAGULATION FACTOR	“SERINE PROTEASE FVIIA; FVIIA; BLOOD
									VIIA (LIGHT CHAIN);	COAGULATION, SERINE PROTEASE”
									CHAIN: L; COAGULATION
									FACTOR VIIA (HEAVY
									CHAIN); CHAIN: H;
									TRIPEPTIDYL INHIBITOR;
									CHAIN: C;
305	1skz		47	172	8.40E−11			50.59	ANTISTASIN; CHAIN: NULL;	“SERINE PROTEASE INHIBITOR FACTOR
										XA INHIBITOR; ANTISTASIN, CRYSTAL
										STRUCTURE, FACTOR XA INHIBITOR, 2
										SERINE PROTEASE INHIBITOR,
										THROMBOSIS”
305	1tpg		129	219	2.10E−26	0.48	0.54		T-PLASMINOGEN	PLASMINOGEN ACTIVATION
									ACTIVATOR F1-G; 1TPG 7
									CHAIN: NULL; 1TPG 8
305	1tpg		89	184	8.40E−25	0.3	−0.01		T-PLASMINOGEN	PLASMINOGEN ACTIVATION
									ACTIVATOR F1-G; 1TPG 7
									CHAIN: NULL; 1TPG 8
305	1tpg		166	250	1.10E−22	0.07	−0.14		T-PLASMINOGEN	PLASMINOGEN ACTIVATION
									ACTIVATOR F1-G; 1TPG 7
									CHAIN: NULL; 1TPG 8
305	1tpg		49	150	2.10E−22	0.45	−0.11		T-PLASMINOGEN	PLASMINOGEN ACTIVATION
									ACTIVATOR F1-G; 1TPG 7
									CHAIN: NULL; 1TPG 8
305	1tpg		27	105	6.30E−20	0.44	0.31		T-PLASMINOGEN	PLASMINOGEN ACTIVATION
									ACTIVATOR F1-G; 1TPG 7
									CHAIN: NULL; 1TPG 8
305	1tpg		23	108	2.10E−22			60.81	T-PLASMINOGEN	PLASMINOGEN ACTIVATION
									ACTIVATOR F1-G; 1TPG 7
									CHAIN: NULL; 1TPG 8
305	1urk		68	195	1.90E−20	0.05	0.04			“PLASMINOGEN ACTIVATION
										PLASMINOGEN ACTIVATOR
										(UROKINASE-TYPE) (AMINO TERMINAL
										FRAGMENT) (NMR, 15 STRUCTURES)”
305	1urk		63	196	1.90E−20			61.63		“PLASMINOGEN ACTIVATION
										PLASMINOGEN ACTIVATOR
										(UROKINASE-TYPE) (AMINO TERMINAL
										FRAGMENT) (NMR, 15 STRUCTURES)”
305	1vap	A	68	186	4.20E−24	0.05	−0.07		“PHOSPHOLIPASE A2;	“LIPID DEGRADATION PHOSPHOLIPASE
									CHAIN: A, B;”	A2, LIPID DEGRADATION, HYDROLASE”
305	1vap	A	35	143	4.20E−20	0.02	−0.17		“PHOSPHOLIPASE A2;	“LIPID DEGRADATION PHOSPHOLIPASE
									CHAIN: A, B;”	A2, LIPID DEGRADATION, HYDROLASE”
305	1vpi		68	186	4.20E−25	0	−0.15		PHOSPHOLIPASE A2	“NEUROTOXIN PHOSPHOLIPASE A2
									INHIBITOR; CHAIN: NULL	INHIBITOR, X-RAY STRUCTURE,
										RECOGNITION, 2 MOLECULAR
										EVOLUTION, NEUROTOXIN”
305	1whe		23	106	6.30E−18			53.94	COAGULATION FACTOR X;	“GLYCOPROTEIN GLYCOPROTEIN,
									CHAIN: NULL;	HYDROLASE, SERINE PROTEASE,
										PLASMA, BLOOD 2 COAGULATION
										FACTOR”
305	1xka	L	147	237	3.40E−14			71.79	“BLOOD COAGULATION	“BLOOD COAGULATION FACTOR
									FACTOR XA; CHAIN: L, C;”	STUART FACTOR; BLOOD
										COAGULATION FACTOR, SERINE
										PROTEINASE, EPIDERMAL 2 GROWTH
										FACTOR LIKE DOMAIN”
305	9wga	A	26	203	3.40E−13			75.4		LECTIN (AGGLUTININ) WHEAT GERM
										AGGLUTININ (ISOLECTIN 2) 9WGA 3
306	1a5e		1	116	8.50E−28	0.55	1		TUMOR SUPPRESSOR	“ANTI-ONCOGENE CELL CYCLE, ANTI-
									P16INK4A; CHAIN: NULL;	ONCOGENE, REPEAT, ANK REPEAT”
306	1awc	B	1	123	1.70E−36	0.2	0.99		“GA BINDING PROTEIN	“COMPLEX (TRANSCRIPTION
									ALPHA; CHAIN: A; GA	REGULATION/DNA) GABPALPHA;
									BINDING PROTEIN BETA 1;	GABPBETA1; COMPLEX (TRANSCRIPTION
									CHAIN: B; DNA; CHAIN: D,	REGULATION/DNA), DNA-BINDING, 2
									E;”	NUCLEAR PROTEIN, ETS DOMAIN,
										ANKYRIN REPEATS, TRANSCRIPTION 3
										FACTOR”
306	1bd8		1	154	6.80E−27			51.04	P19INK4D CDK4/6	“TUMOR SUPPRESSOR TUMOR
									INHIBITOR; CHAIN: NULL;	SUPPRESSOR, CDK4/6 INHIBITOR,
										ANKYRIN MOTIF”
306	1bi7	B	1	116	1.40E−28	0.38	1		CYCLIN-DEPENDENT	“COMPLEX (KINASE/ANTI-ONCOGENE)
									KINASE 6; CHAIN: A;	CDK6; P16INK4A, MTS1; CYCLIN
									MULTIPLE TUMOR	DEPENDENT KINASE, CYCLIN
									SUPPRESSOR; CHAIN: B;	DEPENDENT KINASE INHIBITORY 2
										PROTEIN, CDK, INK4, CELL CYCLE,
										MULTIPLE TUMOR SUPPRESSOR, 3 MTS1,
										COMPLEX (KINASE/ANTI-ONCOGENE)
										HEADER”
306	1bi7	B	1	120	1.40E−28			51.34	CYCLIN-DEPENDENT	“COMPLEX (KINASE/ANTI-ONCOGENE)
									KINASE 6; CHAIN: A;	CDK6; P16INK4A, MTS1; CYCLIN
									MULTIPLE TUMOR	DEPENDENT KINASE, CYCLIN
									SUPPRESSOR; CHAIN: B;	DEPENDENT KINASE INHIBITORY 2
										PROTEIN, CDK, INK4, CELL CYCLE,
										MULTIPLE TUMOR SUPPRESSOR, 3 MTS1,
										COMPLEX (KINASE/ANTI-ONCOGENE)
										HEADER”
306	1blx	B	4	149	3.40E−27	0.16	0.63		CYCLIN-DEPENDENT	“COMPLEX (INHIBITOR
									KINASE 6; CHAIN: A;	PROTEIN/KINASE) INHIBITOR PROTEIN,
									P19INK4D; CHAIN: B;	CYCLIN-DEPENDENT KINASE, CELL
										CYCLE 2 CONTROL, ALPHA/BETA,
										COMPLEX (INHIBITOR
										PROTEIN/KINASE)”
306	1blx	B	1	158	3.40E−27			50.47	CYCLIN-DEPENDENT	“COMPLEX (INHIBITOR
									KINASE 6; CHAIN: A;	PROTEIN/KINASE) INHIBITOR PROTEIN,
									P19INK4D; CHAIN: B;	CYCLIN-DEPENDENT KINASE, CELL
										CYCLE 2 CONTROL, ALPHA/BETA,
										COMPLEX (INHIBITOR
										PROTEIN/KINASE)”
306	1bu9	A	1	136	5.10E−33	0.18	0.57		CYCLIN-DEPENDENT	“HORMONE/GROWTH FACTOR P18-
									KINASE 6 INHIBITOR;	INK4C; CELL CYCLE INHIBITOR,
									CHAIN: A;	P18INK4C, TUMOR, SUPPRESSOR,
										CYCLIN-2 DEPENDENT KINASE,
										HORMONE/GROWTH FACTOR”
306	1d9s	A	1	116	1.70E−28	0.46	1		CYCLIN-DEPENDENT	“SIGNALING PROTEIN HELIX-TURN-
									KINASE 4 INHIBITOR B;	HELIX, ANKYRIN REPEAT”
									CHAIN: A;
306	1ihb	A	1	136	5.10E−33	0.28	0.88		“CYCLIN-DEPENDENT	“CELL CYCLE INHIBITOR P18-
									KINASE 6 INHIBITOR;	INK4C(INK6); CELL CYCLE INHIBITOR,
									CHAIN: A, B;”	P18-INK4C(INK6), ANKYRIN REPEAT, 2
										CDK 4/6 INHIBITOR”
306	1ihb	A	1	153	5.10E−33			51.52	“CYCLIN-DEPENDENT	“CELL CYCLE INHIBITOR P18-
									KINASE 6 INHIBITOR;	INK4C(INK6); CELL CYCLE INHIBITOR,
									CHAIN: A, B;”	P18-INK4C(INK6), ANKYRIN REPEAT, 2
										CDK 4/6 INHIBITOR”
306	1ikn	D	1	155	3.40E−32	−0.14	0.27		NF-KAPPA-B P65 SUBUNIT;	“TRANSCRIPTION FACTOR P65; P50D;
									CHAIN: A; NF-KAPPA-B	TRANSCRIPTION FACTOR, IKB/NFKB
									P50D SUBUNIT; CHAIN: C; I-	COMPLEX”
									KAPPA-B-ALPHA; CHAIN: D;
306	1myo		2	118	3.40E−27	−0.24	0.86		MYOTROPHIN; CHAIN:	“ANK-REPEAT MYOTROPHIN,
									NULL	ACETYLATION, NMR, ANK-REPEAT”
306	1nfi	E	1	155	3.40E−32	−0.01	0.49		“NF-KAPPA-B P65; CHAIN:	“COMPLEX (TRANSCRIPTION REG/ANK
									A, C; NF-KAPPA-B P50;	REPEAT) COMPLEX (TRANSCRIPTION
									CHAIN: B, D; I-KAPPA-B-	REGULATION/ANK REPEAT), ANKYRIN 2
									ALPHA; CHAIN: E, F;”	REPEAT HELIX”
307	1be9	A	357	449	1.10E−05	0.12	0.68		PSD-95; CHAIN: A; CRIPT;	“PEPTIDE RECOGNITION PEPTIDE
									CHAIN: B;	RECOGNITION, PROTEIN
										LOCALIZATION”
307	1faq		841	883	1.50E−13	0.32	0.64		RAF-1; CHAIN: NULL;	“SERINE/THREONINE PROTEIN KINASE
										TRANSFERASE, SERINE/THREONINE-
										PROTEIN KINASE, 2 PROTO-ONCOGENE,
										ZINC, ATP-BINDING, PHORBOL-ESTER
										BINDING”
307	1faq		841	888	1.70E−08	−0.11	0.95		RAF-1; CHAIN: NULL;	“SERINE/THREONINE PROTEIN KINASE
										TRANSFERASE, SERINE/THREONINE-
										PROTEIN KINASE, 2 PROTO-ONCOGENE,
										ZINC, ATP-BINDING, PHORBOL-ESTER
										BINDING”
307	1i16		364	451	8.40E−10	0.47	0.27		INTERLEUKIN 16; CHAIN:	“CYTOKINE LCF; CYTOKINE,
									NULL;	LYMPHOCYTE CHEMOATTRACTANT
										FACTOR, PDZ DOMAIN”
307	1pdr		361	422	1.30E−05	−0.23	0.01		HUMAN DISCS LARGE	“SIGNAL TRANSDUCTION HDLG, DHR3
									PROTEIN; CHAIN: NULL;	DOMAIN; SIGNAL TRANSDUCTION, SH3
										DOMAIN, REPEAT”
307	1ptq		841	888	1.70E−13	0.25	1		PROTEIN KINASE C DELTA	PHOSPHOTRANSFERASE
									TYPE; 1PTQ 4
307	1qau	A	364	448	6.30E−11	0.7	0.8		NEURONAL NITRIC OXIDE	OXIDOREDUCTASE BETA-FINGER
									SYNTHASE (RESIDUES 1-130);
									CHAIN: A;
307	1qlc	A	364	448	1.70E−10	0.41	0.76		POSTSYNAPTIC DENSITY	“PEPTIDE RECOGNITION PSD-95; PDZ
									PROTEIN 95; CHAIN: A;	DOMAIN, NEURONAL NITRIC OXIDE
										SYNTHASE, NMDA RECEPTOR 2
										BINDING”
307	1tbn		839	897	4.20E−14	−0.34	0.45		“PROTEIN KINASE C,	“CALCIUM-BINDING PROTEIN RAT
									GAMMA TYPE; CHAIN:	BRAIN PKC-G; CALCIUM-BINDING
									NULL;”	PROTEIN, PROTEIN KINASE C, PKC,
										TRANSFERASE”
307	1tbn		838	896	6.80E−14	−0.23	0.06		“PROTEIN KINASE C,	“CALCIUM-BINDING PROTEIN RAT
									GAMMA TYPE; CHAIN:	BRAIN PKC-G; CALCIUM-BINDING
									NULL;”	PROTEIN, PROTEIN KINASE C, PKC,
										TRANSFERASE”
307	3pdz	A	364	448	4.20E−10	0.49	1		“TYROSINE PHOSPHATASE	“HYDROLASE PDZ DOMAIN, HUMAN
									(PTP-BAS, TYPE 1); CHAIN:	PHOSPHATASE, HPTP1E, PTP-BAS,
									A;”	SPECIFICITY 2 OF BINDING”
308	1got	B	3	330	9.60E−80			120.96	GT-ALPHA/GI-ALPHA	“COMPLEX (GTP-BINDING/TRANSDUCER)
									CHIMERA; CHAIN: A; GT-	BETA1, TRANSDUCIN BETA SUBUNIT;
									BETA; CHAIN: B; GT-	GAMMA1, TRANSDUCIN GAMMA
									GAMMA; CHAIN: G;	SUBUNIT; COMPLEX (GTP-
										BINDING/TRANSDUCER), G PROTEIN,
										HETEROTRIMER 2 SIGNAL
										TRANSDUCTION”
311	1a06		1	292	3.20E−55			66.92	CALCIUM/CALMODULIN-	“KINASE KINASE, SIGNAL
									DEPENDENT PROTEIN	TRANSDUCTION,
									KINASE; CHAIN: NULL;	CALCIUM/CALMODULIN”
311	1a06		1	292	3.20E−55			66.92	CALCIUM/CALMODULIN-	“KINASE KINASE, SIGNAL
									DEPENDENT PROTEIN	TRANSDUCTION,
									KINASE; CHAIN: NULL;	CALCIUM/CALMODULIN”
311	1a6o		1	264	4.80E−77			129.41	PROTEIN KINASE	“TRANSFERASE TRANSFERASE,
									CK2/ALPHA-SUBUNIT;	SERINE/THREONINE-PROTEIN KINASE,
									CHAIN: NULL;	CASEIN KINASE, 2 SER/THR KINASE”
311	1a6o		1	264	4.80E−77			129.41	PROTEIN KINASE	“TRANSFERASE TRANSFERASE,
									CK2/ALPHA-SUBUNIT;	SERINE/THREONINE-PROTEIN KINASE,
									CHAIN: NULL;	CASEIN KINASE, 2 SER/THR KINASE”
311	1apm	E	1	296	3.20E−43			59.72		“TRANSFERASE(PHOSPHOTRANSFERASE)
										$C-/AMP$-DEPENDENT PROTEIN
										KINASE (E.C.2.7.1.37) ($C/APK$) 1APM 3
										(CATALYTIC SUBUNIT) ““ALPHA””
										ISOENZYME MUTANT WITH SER 139
										1APM 4 REPLACED BY ALA (/S139A$)
										COMPLEX WITH THE PEPTIDE 1APM 5
										INHIBITOR PKI(5-24) AND THE
										DETERGENT MEGA-8 1APM 6”
311	1apm	E	1	296	3.20E−43			59.72		“TRANSFERASE (PHOSPHOTRANSFERASE)
										$C-/AMP$-DEPENDENT PROTEIN
										KINASE (E.C.2.7.1.37) ($C/APK$) 1APM 3
										(CATALYTIC SUBUNIT) ““ALPHA””
										ISOENZYME MUTANT WITH SER 139
										1APM 4 REPLACED BY ALA (/S139A$)
										COMPLEX WITH THE PEPTIDE 1APM 5
										INHIBITOR PKI(5-24) AND THE
										DETERGENT MEGA-8 1APM 6”
311	1aql		1	265	0			142.91	CYCLIN-DEPENDENT	“PROTEIN KINASE CDK2; PROTEIN
									PROTEIN KINASE 2; CHAIN:	KINASE, CELL CYCLE,
									NULL;	PHOSPHORYLATION, STAUROSPORINE, 2
										CELL DIVISION, MITOSIS, INHIBITION”
311	1aql		1	265	0			142.91	CYCLIN-DEPENDENT	“PROTEIN KINASE CDK2; PROTEIN
									PROTEIN KINASE 2; CHAIN:	KINASE, CELL CYCLE,
									NULL;	PHOSPHORYLATION, STAUROSPORINE, 2
										CELL DIVISION, MITOSIS, INHIBITION”
311	1bi8	A	2	256	1.60E−88			160.58	“CYCLIN-DEPENDENT	“COMPLEX (KINASE/INHIBITOR) CDK6;
									KINASE 6; CHAIN: A, C;	P19INK4D; CYCLIN DEPENDENT KINASE,
									CYCLIN-DEPENDENT	CYCLIN DEPENDENT KINASE
									KINASE INHIBITOR; CHAIN:	INHIBITORY 2 PROTEIN, CDK, INK4, CELL
									B, D;”	CYCLE, COMPLEX (KINASE/INHIBITOR)
										HEADER HELIX”
311	1bi8	A	2	256	1.60E−88			160.58	“CYCLIN-DEPENDENT	“COMPLEX (KINASE/INHIBITOR) CDK6;
									KINASE 6; CHAIN: A, C;	P19INK4D; CYCLIN DEPENDENT KINASE,
									CYCLIN-DEPENDENT	CYCLIN DEPENDENT KINASE
									KINASE INHIBITOR; CHAIN:	INHIBITORY 2 PROTEIN, CDK, INK4, CELL
									B, D;”	CYCLE, COMPLEX (KINASE/INHIBITOR)
										HEADER HELIX”
311	1blx	A	2	264	3.20E−88			140.69	CYCLIN-DEPENDENT	“COMPLEX (INHIBITOR
									KINASE 6; CHAIN: A;	PROTEIN/KINASE) INHIBITOR PROTEIN,
									P19INK4D; CHAIN: B;	CYCLIN-DEPENDENT KINASE, CELL
										CYCLE 2 CONTROL, ALPHA/BETA,
										COMPLEX (INHIBITOR
										PROTEIN/KINASE)”
311	1blx	A	2	264	3.20E−88			140.69	CYCLIN-DEPENDENT	“COMPLEX (INHIBITOR
									KINASE 6; CHAIN: A;	PROTEIN/KINASE) INHIBITOR PROTEIN,
									P19INK4D; CHAIN: B;	CYCLIN-DEPENDENT KINASE, CELL
										CYCLE 2 CONTROL, ALPHA/BETA,
										COMPLEX (INHIBITOR
										PROTEIN/KINASE)”
311	1byg	A	1	232	3.20E−21			59.7	C-TERMINAL SRC KINASE;	“TRANSFERASE CSK; PROTEIN KINASE,
									CHAIN: A;	C-TERMINAL SRC KINASE,
										PHOSPHORYLATION, 2 STAUROSPORINE,
										TRANSFERASE”
311	1byg	A	1	232	3.20E−21			59.7	C-TERMINAL SRC KINASE;	“TRANSFERASE CSK; PROTEIN KINASE,
									CHAIN: A;	C-TERMINAL SRC KINASE,
										PHOSPHORYLATION, 2 STAUROSPORINE,
										TRANSFERASE”
311	1ctp	E	1	277	1.60E−44			60.57		TRANSFERASE(PHOSPHOTRANSFERASE)
										CAMP-DEPENDENT PROTEIN KINASE
										(E.C.2.7.1.37) (CAPK) 1CTP 3 (CATALYTIC
										SUBUNIT) 1CTP 4
311	1ctp	E	1	277	1.60E−44			60.57		TRANSFERASE(PHOSPHOTRANSFERASE)
										CAMP-DEPENDENT PROTEIN KINASE
										(E.C.2.7.1.37) (CAPK) 1CTP 3 (CATALYTIC
										SUBUNIT) 1CTP 4
311	1fgk	B	1	232	1.60E−27			59.38	“FGF RECEPTOR 1; CHAIN:	“PHOSPHOTRANSFERASE FGFR1K,
									A, B;”	FIBROBLAST GROWTH FACTOR
										RECEPTOR 1; TRANSFERASE, TYROSINE-
										PROTEIN KINASE, ATP-BINDING, 2
										PHOSPHORYLATION, RECEPTOR,
										PHOSPHOTRANSFERASE”
311	1fgk	A	1	233	1.60E−22			70.44	“FGF RECEPTOR 1; CHAIN:	“PHOSPHOTRANSFERASE FGFR1K,
									A, B;”	FIBROBLAST GROWTH FACTOR
										RECEPTOR 1; TRANSFERASE, TYROSINE-
										PROTEIN KINASE, ATP-BINDING, 2
										PHOSPHORYLATTON, RECEPTOR,
										PHOSPHOTRANSFERASE”
311	1fgk	B	1	232	1.60E−27			59.38	“FGF RECEPTOR 1; CHAIN:	“PHOSPHOTRANSFERASE FGFR1K,
									A, B;”	FIBROBLAST GROWTH FACTOR
										RECEPTOR 1; TRANSFERASE, TYROSINE-
										PROTEIN KINASE, ATP-BINDING, 2
										PHOSPHORYLATION, RECEPTOR,
										PHOSPHOTRANSFERASE”
311	1fgk	A	1	233	1.60E−22			70.44	“FGF RECEPTOR 1; CHAIN:	“PHOSPHOTRANSFERASE FGFR1K,
									A, B;”	FIBROBLAST GROWTH FACTOR
										RECEPTOR 1; TRANSFERASE, TYROSINE-
										PROTEIN KINASE, ATP-BINDING, 2
										PHOSPHORYLATION, RECEPTOR,
										PHOSPHOTRANSFERASE”
311	1hcl		1	265	0			155.25	HUMAN CYCLIN-	“PROTEIN KINASE CDK2; TRANSFERASE,
									DEPENDENT KINASE 2;	SERINE/THREONINE PROTEIN KINASE,
									CHAIN: NULL;	ATP-BINDING, 2 CELL CYCLE, CELL
										DIVISION, MITOSIS, PHOSPHORYLATION”
311	1hcl		1	265	0			155.25	HUMAN CYCLIN-	“PROTEIN KINASE CDK2; TRANSFERASE,
									DEPENDENT KINASE 2;	SERINE/THREONINE PROTEIN KINASE,
									CHAIN: NULL;	ATP-BINDING, 2 CELL CYCLE, CELL
										DIVISION, MITOSIS, PHOSPHORYLATION”
311	1ian		1	313	3.20E−94			118.83	P38 MAP KINASE; CHAIN:	“SERINE/THREONINE-PROTEIN KINASE
									NULL;	CSBP, RK, P38; PROTEIN SER/THR-
										KINASE, SERINE/THREONINE-PROTEIN
										KINASE”
311	1ian		1	313	3.20E−94			118.83	P38 MAP KINASE; CHAIN:	“SERINE/THREONINE-PROTEIN KINASE
									NULL;	CSBP, RK, P38; PROTEIN SER/THR-
										KINASE, SERINE/THREONINE-PROTEIN
										KINASE”
311	1jnk		1	297	6.40E−90			122.01	C-JUN N-TERMINAL	“TRANSFERASE JNK3; TRANSFERASE,
									KINASE; CHAIN: NULL;	JNK3 MAP KINASE, SERINE/THREONINE
										PROTEIN 2 KINASE”
311	1jnk		1	297	6.40E−90			122.01	C-JUN N-TERMINAL	“TRANSFERASE JNK3; TRANSFERASE,
									KINASE; CHAIN: NULL;	JNK3 MAP KINASE, SERINE/THREONINE
										PROTEIN 2 KINASE”
311	1kob	A	1	314	6.40E−51			86.64	“TWITCHIN; CHAIN: A, B;”	“KINASE KINASE, TWITCHIN,
										INTRASTERIC REGULATION”
311	1kob	A	1	314	6.40E−51			86.64	“TWITCHIN; CHAIN: A, B;”	“KINASE KINASE, TWITCHIN,
										INTRASTERIC REGULATION”
311	1p38		1	302	0			141.43	MAP KINASE P38; CHAIN:	“TRANSPERASE MITOGEN ACTIVATED
									NULL;	PROTEIN KINASE; TRANSFERASE, MAP
										KINASE, SERINE/THREONINE-PROTEIN
										KINASE, 2 P38”
311	1p38		1	302	0			141.43	MAP KINASE P38; CHAIN:	“TRANSFERASE MITOGEN ACTIVATED
									NULL;	PROTEIN KINASE; TRANSFERASE, MAP
										KINASE, SERINE/THREONINE-PROTEIN
										KINASE, 2 P38”
311	1phk		1	257	1.60E−57			75.22	PHOSPHORYLASE KINASE;	“KINASE RABBIT MUSCLE
									CHAIN: NULL;	PHOSPHORYLASE KINASE; GLYCOGEN
										METABOLISM, TRANSFERASE,
										SERINE/THREONINE-PROTEIN, 2 KINASE,
										ATP-BINDING, CALMODULIN-BINDING”
311	1phk		1	257	1.60E−57			75.22	PHOSPHORYLASE KINASE;	“KINASE RABBIT MUSCLE
									CHAIN: NULL;	PHOSPHORYLASE KINASE; GLYCOGEN
										METABOLISM, TRANSFERASE,
										SERINE/THREONINE-PROTEIN, 2 KINASE,
										ATP-BINDING, CALMODULIN-BINDING”
311	1pme		2	295	0			162.83	ERK2; CHAIN: NULL;	“TRANSFERASE MAP KINASE,
										SERINE/THREONINE PROTEIN KINASE,
										TRANSFERASE”
311	1pme		2	295	0			162.83	ERK2; CHAIN: NULL;	“TRANSFERASE MAP KINASE,
										SERINE/THREONINE PROTEIN KINASE,
										TRANSFERASE”
311	1tki	A	1	315	1.40E−43			88.24	“TITIN; CHAIN: A, B;”	“SERINE KINASE SERINE KINASE, TITIN,
										MUSCLE, AUTOINHIBITION”
311	1tki	A	1	315	1.40E−43			88.24	“TITIN; CHAIN: A, B;”	“SERINE KINASE SERINE KINASE, TITIN,
										MUSCLE, AUTOINHIBITION”
311	3erk		2	312	0			165.29	EXTRACELLULAR	“TRANSFERASE MITOGEN ACTIVATED
									REGULATED KINASE 2;	PROTEIN KINASE, MAP 2, ERK2;
									CHAIN: NULL;	TRANSFERASE, SERINE/THREONINE-
										PROTEIN KINASE, MAP KINASE, 2 ERK2”
311	3erk		2	312	0			165.29	EXTRACELLULAR	“TRANSFERASE MITOGEN ACTIVATED
									REGULATED KINASE 2;	PROTEIN KINASE, MAP 2, ERK2;
									CHAIN: NULL;	TRANSFERASE, SERINE/THREONINE-
										PROTEIN KINASE, MAP KINASE, 2 ERK2”
312	1a4y	A	385	874	1.60E−39			120.16	“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”
312	2bnh		389	874	1.10E−46			125.28	RIBONUCLEASE	“ACETYLATION RNASE INHIBITOR,
									INHIBITOR; CHAIN: NULL;	RIBONUCLEASE/ANGIOGENIN
										INHIBITOR ACETYLATION, LEUCINE-
										RICH REPEATS”
313	1bu2	A	35	189	4.20E−23	−0.27	0.33		CYCLIN HOMOLOG; CHAIN:	“CELL CYCLE REGULATION CELL CYCLE
									A;	REGULATION, HERPESVIRUS SAIMIRI,
										VIRAL CYCLIN”
313	1jkw		35	194	6.30E−14	−0.31	0.06		CYCLIN H; CHAIN: NULL;	“CELL DIVISION RCYCLIN H
										(RECOMBINANT); CYCLIN, CELL CYCLE,
										CELL DIVISION, NUCLEAR PROTEIN”
313	1qmz	B	80	230	1.70E−32	−0.32	0.57		“CELL DIVISION PROTEIN	“COMPLEX (PROTEIN KINASE/CYCLIN)
									KINASE 2; CHAIN: A, C;	CYCLIN-DEPENDENT KINASE-2, CDK2,
									G2/MITOTIC-SPECIFIC	P33 PROTEIN KINASE; CCNA, CCN1;
									CYCLIN A; CHAIN: B, D;	COMPLEX (PROTEIN KINASE/CYCLIN),
									SUBSTRATE PEPTIDE;	CYCLIN, CDK, 2 PHOSPHORYLATION,
									CHAIN: E, F;”	SUBSTRATE COMPLEX”
313	1vin		80	230	1.70E−33	−0.14	0.57		CYCLIN A; CHAIN: NULL;	“BINDING PROTEIN CYCLIN, CELL
										CYCLE, KINASE-REGULATORY-SUBUNIT,
										2 BINDING PROTEIN”
313	1vin		35	195	4.20E−21	0.01	0.92		CYCLIN A; CHAIN: NULL;	“BINDING PROTEIN CYCLIN, CELL
										CYCLE, KINASE-REGULATORY-SUBUNIT,
										2 BINDING PROTEIN”
315	1aut	L	431	532	4.20E−17	0.33	−0.01		“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)”
315	1aut	L	1054	1154	4.20E−15	−0.15	0.31		“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)”
315	1aut	L	1331	1423	2.10E−13	−0.31	0.45		“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)”
315	1aut	L	846	920	1.30E−12	0.19	0.19		“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)”
315	1cej	A	1054	1137	4.20E−16	0.04	0.11		MEROZOITE SURFACE	“SURFACE PROTEIN MEROZOITE
									PROTEIN 1; CHAIN: A;	SURFACE ANTIGEN 1, MAJOR BLOOD-
										STAGE EGF-LIKE DOMAIN,
										EXTRACELLULAR, MODULAR PROTEIN,
										SURFACE 2 ANTIGEN, MALARIA
										VACCINE COMPONENT, SURFACE
										PROTEIN”
315	1cej	A	1337	1420	6.30E−14	−0.05	0.54		MEROZOITE SURFACE	“SURFACE PROTEIN MEROZOITE
									PROTEIN 1; CHAIN: A;	SURFACE ANTIGEN 1, MAJOR BLOOD-
										STAGE EGF-LIKE DOMAIN,
										EXTRACELLULAR, MODULAR PROTEIN,
										SURFACE 2 ANTIGEN, MALARIA
										VACCINE COMPONENT, SURFACE
										PROTEIN”
315	1cej	A	848	920	1.90E−13	0.1	−0.06		MEROZOITE SURFACE	“SURFACE PROTEIN MEROZOITE
									PROTEIN 1; CHAIN: A;	SURFACE ANTIGEN 1, MAJOR BLOOD-
										STAGE EGF-LIKE DOMAIN,
										EXTRACELLULAR, MODULAR PROTEIN,
										SURFACE 2 ANTIGEN, MALARIA
										VACCINE COMPONENT, SURFACE
										PROTEIN”
315	1cej	A	244	332	4.20E−10	0.02	0.01		MEROZOITE SURFACE	“SURFACE PROTEIN MEROZOITE
									PROTEIN 1; CHAIN: A;	SURFACE ANTIGEN 1, MAJOR BLOOD-
										STAGE EGF-LIKE DOMAIN,
										EXTRACELLULAR, MODULAR PROTEIN,
										SURFACE 2 ANTIGEN, MALARIA
										VACCINE COMPONENT, SURFACE
										PROTEIN”
315	1dan	L	696	822	1.10E−27	0	0.15		“BLOOD COAGULATION	“BLOOD COAGULATION, SERINE
									FACTOR VIIA; CHAIN: L, H;	PROTEASE, COMPLEX, CO-FACTOR, 2
									SOLUBLE TISSUE FACTOR;	RECEPTOR ENZYME, INHIBITOR, GLA,
									CHAIN: T, U; D-PHE-PHE-	EGF, 3 COMPLEX (SERINE
									ARG-	PROTEASE/COFACTOR/LIGAND)”
									CHLOROMETHYLKETONE
									(DFFRCMK) WITH CHAIN:
									C;”
315	1dan	L	448	574	6.30E−26	0.13	0.15		“BLOOD COAGULATION	“BLOOD COAGULATION, SERINE
									FACTOR VIIA; CHAIN: L, H;	PROTEASE, COMPLEX, CO-FACTOR, 2
									SOLUBLE TISSUE FACTOR;	RECEPTOR ENZYME, INHIBITOR, GLA,
									CHAIN: T, U; D-PHE-PHE-	EGF, 3 COMPLEX (SERINE
									ARG-	PROTEASE/COFACTOR/LIGAND)”
									CHLOROMETHYLKETONE
									(DFFRCMK) WITH CHAIN:
									C;”
315	1dan	L	574	696	1.10E−25	0.12	0.07		“BLOOD COAGULATION	“BLOOD COAGULATION, SERINE
									FACTOR VIIA; CHAIN: L, H;	PROTEASE, COMPLEX, CO-FACTOR, 2
									SOLUBLE TISSUE FACTOR;	RECEPTOR ENZYME, INHIBITOR, GLA,
									CHAIN: T, U; D-PHE-PHE-	EGF, 3 COMPLEX (SERINE
									ARG-	PROTEASE/COFACTOR/LIGAND)”
									CELOROMETHYLKETONE
									(DFFRCMK) WITH CHAIN:
									C;”
315	1dan	L	738	865	2.10E−25	0.12	0.05		“BLOOD COAGULATION	“BLOOD COAGULATION, SERINE
									FACTOR VIIA; CHAIN: L, H;	PROTEASE, COMPLEX, CO-FACTOR, 2
									SOLUBLE TISSUE FACTOR;	RECEPTOR ENZYME, INHIBITOR, GLA,
									CHAIN: T, U; D-PHE-PHE-	EGF, 3 COMPLEX (SERINE
									ARG-	PROTEASE/COFACTOR/LIGAND)”
									CHLOROMETHYLKETONE
									(DFFRCMK) WITH CHAIN:
									C;”
315	1dan	L	490	613	6.30E−25	0.31	0.09		“BLOOD COAGULATION	“BLOOD COAGULATION, SERINE
									FACTOR VIIA; CHAIN: L, H;	PROTEASE, COMPLEX, CO-FACTOR, 2
									SOLUBLE TISSUE FACTOR;	RECEPTOR ENZYME, INHIBITOR, GLA,
									CHAIN: T, U; D-PHE-PHE-	EGF, 3 COMPLEX (SERINE
									ARG-	PROTEASE/COFACTOR/LIGAND)”
									CHLOROMETHYLKETONE
									(DFFRCMK) WITH CHAIN:
									C;”
315	1dan	L	781	903	1.90E−24	0.34	0.3		“BLOOD COAGULATION	“BLOOD COAGULATION, SERINE
									FACTOR VIIA; CHAIN: L, II;	PROTEASE, COMPLEX, CO-FACTOR, 2
									SOLUBLE TISSUE FACTOR;	RECEPTOR ENZYME, INHIBITOR, GLA,
									CHAIN: T, U; D-PHE-PHE-	EGF, 3 COMPLEX (SERINE
									ARG-	PROTEASE/COFACTOR/LIGAND)”
									CHLOROMETHYLKETONE
									(DFFRCMK) WITH CHAIN:
									C;”
315	1dan	L	613	732	2.10E−24	0.23	0.06		“BLOOD COAGULATION	“BLOOD COAGULATION, SERINE
									FACTOR VIIA; CHAIN: L, H;	PROTEASE, COMPLEX, CO-FACTOR, 2
									SOLUBLE TISSUE FACTOR;	RECEPTOR ENZYME, INHIBITOR, GLA,
									CHAIN: T, U; D-PHE-PHE-	EGF, 3 COMPLEX (SERINE
									ARG-	PROTEASE/COFACTOR/LIGAND)”
									CHLOROMETHYLKETONE
									(DFFRCMK) WITH CHAIN:
									C;”
315	1dan	L	1007	1148	1.70E−16	0.29	0.33		“BLOOD COAGULATION	“BLOOD COAGULATION, SERINE
									FACTOR VIIA; CHAIN: L, H;	PROTEASE, COMPLEX, CO-FACTOR, 2
									SOLUBLE TISSUE FACTOR;	RECEPTOR ENZYME, INHIBITOR, GLA,
									CHAIN: T, U; D-PHE-PHE-	EGF, 3 COMPLEX (SERINE
									ARG-	PROTEASE/COFACTOR/LIGAND)”
									CHLOROMETHYLKETONE
									(DFFRCMK) WITH CHAIN:
									C;”
315	1dan	L	822	920	1.70E−16	0.11	0.15		“BLOOD COAGULATION	“BLOOD COAGULATION, SERINE
									FACTOR VIIA; CHAIN: L, H;	PROTEASE, COMPLEX, CO-FACTOR, 2
									SOLUBLE TISSUE FACTOR;	RECEPTOR ENZYME, INHIBITOR, GLA,
									CHAIN: T, U; D-PHE-PHE-	EGF, 3 COMPLEX (SERINE
									ARG-	PROTEASE/COFACTOR/LIGAND)”
									CHLOROMETHYLKETONE
									(DFFRCMK) WITH CHAIN:
									C;”
315	1dan	L	436	527	4.20E−16	0.14	0.31		“BLOOD COAGULATION	“BLOOD COAGULATION, SERINE
									FACTOR VIIA; CHAIN: L, H;	PROTEASE, COMPLEX, CO-FACTOR, 2
									SOLUBLE TISSUE FACTOR;	RECEPTOR ENZYME, INHIBITOR, GLA,
									CHAIN: T, U; D-PHE-PHE-	EGF, 3 COMPLEX (SERINE
									ARG-	PROTEASE/COFACTOR/LIGAND)”
									CHLOROMETHYLKETONE
									(DFFRCMK) WITH CHAIN:
									C;”
315	1dan	L	207	292	3.40E−13	0.33	−0.06		“BLOOD COAGULATION	“BLOOD COAGULATION, SERINE
									FACTOR VIIA; CHAIN: L, H;	PROTEASE, COMPLEX, CO-FACTOR, 2
									SOLUBLE TISSUE FACTOR;	RECEPTOR ENZYME, INHIBITOR, GLA,
									CHAIN: T, U; D-PHE-PHE-	EGF, 3 COMPLEX (SERINE
									ARG-	PROTEASE/COFACTOR/LIGAND)”
									CHLOROMETHYLKETONE
									(DFFRCMK) WITH CHAIN:
									C;”
315	1dan	L	244	329	5.10E−13	−0.21	0.15		“BLOOD COAGULATION	“BLOOD COAGULATION, SERINE
									FACTOR VIIA; CHAIN: L, H;	PROTEASE, COMPLEX, CO-FACTOR, 2
									SOLUBLE TISSUE FACTOR;	RECEPTOR ENZYME, INHIBITOR, GLA,
									CHAIN: T, U; D-PHE-PHE-	EGF, 3 COMPLEX (SERINE
									ARG-	PROTEASE/COFACTOR/LIGAND)”
									CHLOROMETHYLKETONE
									(DFFRCMK) WITH CHAIN:
									C;”
315	1dan	L	1102	1200	1.40E−12	−0.21	0.52		“BLOOD COAGULATION	“BLOOD COAGULATION, SERINE
									FACTOR VIIA; CHAIN: L, H;	PROTEASE, COMPLEX, CO-FACTOR, 2
									SOLUBLE TISSUE FACTOR;	RECEPTOR ENZYME, INHIBITOR, GLA,
									CHAIN: T, U; D-PHE-PHE-	EGF, 3 COMPLEX (SERINE
									ARG-	PROTEASE/COFACTOR/LIGAND)”
									CHLOROMETHYLKETONE
									(DFFRCMK) WITH CHAIN:
									C;”
315	1dan	L	321	391	3.40E−10	0.07	−0.2		“BLOOD COAGULATION	“BLOOD COAGULATION, SERINE
									FACTOR VIIA; CHAIN: L, H;	PROTEASE, COMPLEX, CO-FACTOR, 2
									SOLUBLE TISSUE FACTOR;	RECEPTOR ENZYME, INHIBITOR, GLA,
									CHAIN: T, U; D-PHE-PHE-	EGF, 3 COMPLEX (SERINE
									ARG-	PROTEASE/COFACTOR/LIGAND)”
									CHLOROMETHYLKETONE
									(DFFRCMK) WITH CHAIN:
									C;”
315	1dva	L	555	650	2.10E−26	0.3	0.35		“DES-GLA FACTOR VIIA	HYDROLASE/HYDROLASE INHIBITOR
									(HEAVY CHAIN); CHAIN: H,	PROTEIN-PEPTIDE COMPLEX
									I; DES-GLA FACTOR VIIA
									(LIGHT CHAIN); CHAIN: L,
									M; (DPN)-PHE-ARG; CHAIN:
									C, D; PEPTIDE E-76; CHAIN:
									X, Y;”
315	1dva	L	1054	1148	4.20E−14	0.12	0.88		“DES-GLA FACTOR VIIA	HYDROLASE/HYDROLASE INHIBITOR
									(HEAVY CHAIN); CHAIN: H,	PROTEIN-PEPTIDE COMPLEX
									I; DES-GLA FACTOR VIIA
									(LIGHT CHAIN); CHAIN: L,
									M; (DPN)-PHE-ARG; CHAIN:
									C, D; PEPTIDE E-76; CHAIN:
									X, Y;”
315	1dva	L	207	292	3.40E−13	0.41	−0.06		“DES-GLA FACTOR VIIA	HYDROLASE/HYDROLASE INHIBITOR
									(HEAVY CHAIN); CHAIN: H,	PROTEIN-PEPTIDE COMPLEX
									I; DES-GLA FACTOR VIIA
									(LIGHT CHAIN); CHAIN: L,
									M; (DPN)-PHE-ARG; CHAIN:
									C, D; PEPTIDE E-76; CHAIN:
									X, Y;”
315	1dva	L	1338	1423	5.10E−13	−0.37	0.13		“DES-GLA FACTOR VIIA	HYDROLASE/HYDROLASE INHIBITOR
									(HEAVY CHAIN); CHAIN: H,	PROTEIN-PEPTIDE COMPLEX
									I; DES-GLA FACTOR VIIA
									(LIGHT CHAIN); CHAIN: L,
									M; (DPN)-PHE-ARG; CHAIN:
									C, D; PEPTIDE E-76; CHAIN:
									X, Y;”
315	1dva	L	244	329	5.10E−13	−0.2	0.11		“DES-GLA FACTOR VIIA	HYDROLASE/HYDROLASE INHIBITOR
									(HEAVY CHAIN); CHAIN: H,	PROTEIN-PEPTIDE COMPLEX
									I; DES-GLA FACTOR VIIA
									(LIGHT CHAIN); CHAIN: L,
									M; (DPN)-PHE-ARG; CHAIN:
									C, D; PEPTIDE E-76; CHAIN:
									X, Y;”
315	1dx5	I	557	679	4.20E−28	0	0.9		“THROMBIN LIGHT CHAIN;	“SERINE PROTEINASE COAGULATION
									CHAIN: A, B, C, D;	FACTOR II; COAGULATION FACTOR II;
									THROMBIN HEAVY CHAIN;	FETOMODULIN, TM, CD141 ANTIGEN;
									CHAIN: M, N, O, P;	EGR-CMK SERINE PROTEINASE, EGF-
									THROMBOMODULIN;	LIKE DOMAINS, ANTICOAGULANT
									CHAIN: I, J, K, L; THROMBIN	COMPLEX, 2 ANTIFIBRINOLYTIC
									INHIBITOR L-GLU-L-GLY-L-	COMPLEX”
									ARM; CHAIN: E, F, G, H;”
315	1dx5	I	721	846	1.90E−25	0.24	1		“THROMBIN LIGHT CHAIN;	“SERINE PROTEINASE COAGULATION
									CHAIN: A, B, C, D;	FACTOR II; COAGULATION FACTOR II;
									THROMBIN HEAVY CHAIN;	FETOMODULIN, TM, CD141 ANTIGEN;
									CHAIN: M, N, O, P;	EGR-CMK SERINE PROTEINASE, EGF-
									THROMBOMODULIN;	LIKE DOMAINS, ANTICOAGULANT
									CHAIN: I, J, K, L; THROMBIN	COMPLEX, 2 ANTIFIBRINOLYTIC
									INHIBITOR L-GLU-L-GLY-L-	COMPLEX”
									ARM; CHAIN: E, F, G, H;”
315	1dx5	I	596	721	1.30E−24	0.23	0.51		“THROMBIN LIGHT CHAIN;	“SERINE PROTEINASE COAGULATION
									CHAIN: A, B, C, D;	FACTOR II; COAGULATION FACTOR II;
									THROMBIN HEAVY CHAIN;	FETOMODULIN, TM, CD141 ANTIGEN;
									CHAIN: M, N, O, P;	EGR-CMK SERINE PROTEINASE, EGF-
									THROMBOMODULIN;	LIKE DOMAINS, ANTICOAGULANT
									CHAIN: I, J, K, L; THROMBIN	COMPLEX, 2 ANTIFIBRINOLYTIC
									INHIBITOR L-GLU-L-GLY-L-	COMPLEX”
									ARM; CHAIN: E, F, G, H;”
315	1dx5	I	680	805	2.10E−24	0.15	0.57		“THROMBIN LIGHT CHAIN;	“SERINE PROTEINASE COAGULATION
									CHAIN: A, B, C, D;	FACTOR II; COAGULATION FACTOR II;
									THROMBIN HEAVY CHAIN;	FETOMODULIN, TM, CD141 ANTIGEN;
									CHAIN: M, N, O, P;	EGR-CMK SERINE PROTEINASE, EGF-
									THROMBOMODULIN;	LIKE DOMAINS, ANTICOAGULANT
									CHAIN: I, J, K, L; THROMBIN	COMPLEX, 2 ANTIFIBRINOLYTIC
									INHIBITOR L-GLU-L-GLY-L-	COMPLEX”
									ARM; CHAIN: E, F, G, H;”
315	1dx5	I	474	592	4.20E−23	0.06	0.33		“THROMBIN LIGHT CHAIN;	“SERINE PROTEINASE COAGULATION
									CHAIN: A, B, C, D;	FACTOR II; COAGULATION FACTOR II;
									THROMBIN HEAVY CHAIN;	FETOMODULIN, TM, CD141 ANTIGEN;
									CHAIN: M, N, O, P;	EGR-CMK SERINE PROTEINASE, EGF-
									THROMBOMODULIN;	LIKE DOMAINS, ANTICOAGULANT
									CHAIN: I, J, K, L; THROMBIN	COMPLEX, 2 ANTIFIBRINOLYTIC
									INHIBITOR L-GLU-L-GLY-L-	COMPLEX”
									ARM; CHAIN: E, F, G, H;”
315	1dx5	I	436	556	1.30E−19	0.29	0.33		“THROMBIN LIGHT CHAIN;	“SERINE PROTEINASE COAGULATION
									CHAIN: A, B, C, D;	FACTOR II; COAGULATION FACTOR II;
									THROMBIN HEAVY CHAIN;	FETOMODULIN, TM, CD141 ANTIGEN;
									CHAIN: M, N, O, P;	EGR-CMK SERINE PROTEINASE, EGF-
									THROMBOMODULIN;	LIKE DOMAINS, ANTICOAGULANT
									CHAIN: I, J, K, L; THROMBIN	COMPLEX, 2 ANTIFIBRINOLYTIC
									INHIBITOR L-GLU-L-GLY-L-	COMPLEX”
									ARM; CHAIN: E, F, G, H;”
315	1dx5	I	807	920	8.40E−18	−0.01	0.05		“THROMBIN LIGHT CHAIN;	“SERINE PROTEINASE COAGULATION
									CHAIN: A, B, C, D;	FACTOR II; COAGULATION FACTOR II;
									THROMBIN HEAVY CHAIN;	FETOMODULIN, TM, CD141 ANTIGEN;
									CHAIN: M, N, O, P;	EGR-CMK SERINE PROTEINASE, EGF-
									THROMBOMODULIN;	LIKE DOMAINS, ANTICOAGULANT
									CHAIN: I, J, K, L; THROMBIN	COMPLEX, 2 ANTIFIBRINOLYTIC
									INHIBITOR L-GLU-L-GLY-L-	COMPLEX”
									ARM; CHAIN: E, F, G, H;”
315	1dx5	I	806	933	1.70E−16	0.02	0.55		“THROMBIN LIGHT CHAIN;	“SERINE PROTEINASE COAGULATION
									CHAIN: A, B, C, D;	FACTOR II; COAGULATION FACTOR II;
									THROMBIN HEAVY CHAIN;	FETOMODULIN, TM, CD141 ANTIGEN;
									CHAIN: M, N, O, P;	EGR-CMK SERINE PROTEINASE, EGF-
									THROMBOMODULIN;	LIKE DOMAINS, ANTICOAGULANT
									CHAIN: I, J, K, L; THROMBIN	COMPLEX, 2 ANTIFIBRINOLYTIC
									INHIBITOR L-GLU-L-GLY-L-	COMPLEX”
									ARM; CHAIN: E, F, G, H;”
315	1dx5	I	1022	1137	1.70E−15	−0.37	0.15		“THROMBIN LIGHT CHAIN;	“SERINE PROTEINASE COAGULATION
									CHAIN: A, B, C, D;	FACTOR II; COAGULATION FACTOR II;
									THROMBIN HEAVY CHAIN;	FETOMODULIN, TM, CD141 ANTIGEN;
									CHAIN: M, N, O, P;	EGR-CMK SERINE PROTEINASE, EGF-
									THROMBOMODULIN;	LIKE DOMAINS, ANTICOAGULANT
									CHAIN: I, J, K, L; THROMBIN	COMPLEX, 2 ANTIFIBRINOLYTIC
									INHIBITOR L-GLU-L-GLY-L-	COMPLEX”
									ARM; CHAIN: E, F, G, H;”
315	1dx5	I	168	279	1.70E−14	0.21	−0.13		“THROMBIN LIGHT CHAIN;	“SERINE PROTEINASE COAGULATION
									CHAIN: A, B, C, D;	FACTOR II; COAGULATION FACTOR II;
									THROMBIN HEAVY CHAIN;	FETOMODULIN, TM, CD141 ANTIGEN;
									CHAIN: M, N, O, P;	EGR-CMK SERINE PROTEINASE, EGF-
									THROMBOMODULIN;	LIKE DOMAINS, ANTICOAGULANT
									CHAIN: I, J, K, L; THROMBIN	COMPLEX, 2 ANTIFIBRINOLYTIC
									INHIBITOR L-GLU-L-GLY-L-	COMPLEX”
									ARM; CHAIN: E, F, G, H;”
315	1dx5	I	1319	1418	1.70E−13	−0.1	0.71		“THROMBIN LIGHT CHAIN;	“SERINE PROTEINASE COAGULATION
									CHAIN: A, B, C, D;	FACTOR II; COAGULATION FACTOR II;
									THROMBIN HEAVY CHAIN;	FETOMODULIN, TM, CD141 ANTIGEN;
									CHAIN: M, N, O, P;	EGR-CMK SERINE PROTEINASE, EGF-
									THROMBOMODULIN;	LIKE DOMAINS, ANTICOAGULANT
									CHAIN: I, J, K, L; THROMBIN	COMPLEX, 2 ANTIFIBRINOLYTIC
									INHIBITOR L-GLU-L-GLY-L-	COMPLEX”
									ARM; CHAIN: E, F, G, H;”
315	1dx5	I	243	357	1.40E−12	0.23	0.22		“THROMBIN LIGHT CHAIN;	“SERINE PROTEINASE COAGULATION
									CHAIN: A, B, C, D;	FACTOR II; COAGULATION FACTOR II;
									THROMBIN HEAVY CHAIN;	FETOMODULIN, TM, CD141 ANTIGEN;
									CHAIN: M, N, O, P;	EGR-CMK SERINE PROTEINASE, EGF-
									THROMBOMODULIN;	LIKE DOMAINS, ANTICOAGULANT
									CHAIN: I, J, K, L; THROMBIN	COMPLEX, 2 ANTIFIBRINOLYTIC
									INHIBITOR L-GLU-L-GLY-L-	COMPLEX”
									ARM; CHAIN: E, F, G, H;”
315	1dx5	I	1298	1419	1.40E−10	−0.17	0.23		“THROMBIN LIGHT CHAIN;	“SERINE PROTEINASE COAGULATION
									CHAIN: A, B, C, D;	FACTOR II; COAGULATION FACTOR II;
									THROMBIN HEAVY CHAIN;	FETOMODULIN, TM, CD141 ANTIGEN;
									CHAIN: M, N, O, P;	EGR-CMK SERINE PROTEINASE, EGF-
									THROMBOMODULIN;	LIKE DOMAINS, ANTICOAGULANT
									CHAIN: I, J, K, L; THROMBIN	COMPLEX, 2 ANTIFIBRINOLYTIC
									INHIBITOR L-GLU-L-GLY-L-	COMPLEX”
									ARM; CHAIN: E, F, G, H;”
315	1dx5	I	899	1018	5.10E−08	0.05	−0.17		“THROMBIN LIGHT CHAIN;	“SERINE PROTEINASE COAGULATION
									CHAIN: A, B, C, D;	FACTOR II; COAGULATION FACTOR II;
									THROMBIN HEAVY CHAIN;	FETOMODULIN, TM, CD141 ANTIGEN;
									CHAIN: M, N, O, P;	EGR-CMK SERINE PROTEINASE, EGF-
									THROMBOMODULIN;	LIKE DOMAINS, ANTICOAGULANT
									CHAIN: I, J, K, L; THROMBIN	COMPLEX, 2 ANTIFIBRINOLYTIC
									INHIBITOR L-GLU-L-GLY-L-	COMPLEX”
									ARM; CHAIN: E, F, G, H;”
315	1emn		763	825	6.30E−19	0.12	1		FIBRILLIN; CHAIN: NULL;	“MATRIX PROTEIN EXTRACELLULAR
										MATRIX, CALCIUM-BINDING,
										GLYCOPROTEIN, 2 REPEAT, SIGNAL,
										MULTIGENE FAMILY, DISEASE
										MUTATION, 3 EGF-LIKE DOMAIN,
										HUMAN FIBRILLIN-1 FRAGMENT,
										MATRIX PROTEIN”
315	1emn		207	278	1.00E−18	0.48	0.31		FIBRILLIN; CHAIN: NULL;	“MATRIX PROTEIN EXTRACELLULALR
										MATRIX, CALCIUM-BINDING,
										GLYCOPROTEIN, 2 REPEAT, SIGNAL,
										MULTIGENE FAMILY, DISEASE
										MUTATION, 3 EGF-LIKE DOMAIN,
										HUMAN FIBRILLIN-1 FRAGMENT,
										MATRIX PROTEIN”
315	1emn		472	535	2.10E−17	−0.01	0.99		FIBRILLIN; CHAIN: NULL;	“MATRIX PROTEIN EXTRACELLULAR
										MATRIX, CALCIUM-BINDING,
										GLYCOPROTEIN, 2 REPEAT, SIGNAL,
										MULTIGENE FAMILY, DISEASE
										MUTATION, 3 EGF-LIKE DOMAIN,
										HUMAN FIBRILLIN-1 FRAGMENT,
										MATRIX PROTEIN”
315	1emn		432	509	1.70E−16	0.72	1		FIBRILLIN; CHAIN: NULL;	“MATRIX PROTEIN EXTRACELLULAR
										MATRIX, CALCIUM-BINDING,
										GLYCOPROTEIN, 2 REPEAT, SIGNAL,
										MULTIGENE FAMILY, DISEASE
										MUTATION, 3 EGF-LIKE DOMAIN,
										HUMAN FIBRILLIN-1 FRAGMENT,
										MATRIX PROTEIN”
315	1emn		243	319	3.40E−16	0.25	0.76		FIBRILLIN; CHAIN: NULL;	“MATRIX PROTEIN EXTRACELLULAR
										MATRIX, CALCIUM-BINDING,
										GLYCOPROTEIN, 2 REPEAT, SIGNAL,
										MULTIGENE FAMILY, DISEASE
										MUTATION, 3 EGF-LIKE DOMAIN,
										HUMAN FIBRILLIN-1 FRAGMENT,
										MATRIX PROTEIN”
315	1emn		1338	1417	6.80E−15	−0.16	0.62		FIBRILLIN; CHAIN: NULL;	“MATRIX PROTEIN EXTRACELLULAR
										MATRIX, CALCIUM-BINDING,
										GLYCOPROTEIN, 2 REPEAT, SIGNAL,
										MULTIGENE FAMILY, DISEASE
										MUTATION, 3 EGF-LIKE DOMAIN,
										HUMAN FIBRILLIN-1 FRAGMENT,
										MATRIX PROTEIN”
315	1emn		1054	1117	1.10E−14	0.26	0.99		FIBRILLIN; CHAIN: NULL;	“MATRIX PROTEIN EXTRACELLULAR
										MATRIX, CALCIUM-BINDING,
										GLYCOPROTEIN, 2 REPEAT, SIGNAL,
										MULTIGENE FAMILY, DISEASE
										MUTATION, 3 EGF-LIKE DOMAIN,
										HUMAN FIBRILLIN-1 FRAGMENT,
										MATRIX PROTEIN”
315	1emn		1097	1177	1.20E−13	0.09	0.15		FIBRILLIN; CHAIN: NULL;	“MATRIX PROTEIN EXTRACELLULAR
										MATRIX, CALCIUM-BINDING,
										GLYCOPROTEIN, 2 REPEAT, SIGNAL,
										MULTIGENE FAMILY, DISEASE
										MUTATION, 3 EGF-LIKE DOMAIN,
										HUMAN FIBRILLIN-1 FRAGMENT,
										MATRIX PROTEIN”
315	1emn		848	923	5.10E−13	0.1	0.92		FIBRILLIN; CHAIN: NULL;	“MATRIX PROTEIN EXTRACELLULAR
										MATRIX, CALCIUM-BINDING,
										GLYCOPROTEIN, 2 REPEAT, SIGNAL,
										MULTIGENE FAMILY, DISEASE
										MUTATION, 3 EGF-LIKE DOMAIN,
										HUMAN FIBRILLIN-1 FRAGMENT,
										MATRIX PROTEIN”
315	1emn		322	391	3.40E−11	0.15	−0.2		FIBRILLIN; CHAIN: NULL;	“MATRIX PROTEIN EXTRACELLULAR
										MATRIX, CALCIUM-BINDING,
										GLYCOPROTEIN, 2 REPEAT, SIGNAL,
										MULTIGENE FAMILY, DISEASE
										MUTATION, 3 EGF-LIKE DOMAIN,
										HUMAN FIBRILLIN-1 FRAGMENT,
										MATRIX PROTEIN”
315	1esl		164	241	5.10E−10	0.02	−0.17			“CELL ADHESION PROTEIN E-SELECTIN
										(LECTIN AND EGF DOMAINS, RESIDUES 1-157)
										1ESL 3 (FORMERLY KNOWN AS
										ELAM-1) 1ESL 4”
315	1ext	A	176	283	1.50E−08	0.17	−0.18		“TUMOR NECROSIS	“SIGNALLING PROTEIN BINDING
									FACTOR RECEPTOR;	PROTEIN, CYTOKINE, SIGNALLING
									CHAIN: A, B;”	PROTEIN”
315	1ext	A	1005	1139	1.90E−08	0.37	−0.01		“TUMOR NECROSIS	“SIGNALLING PROTEIN BINDING
									FACTOR RECEPTOR;	PROTEIN, CYTOKINE, SIGNALLING
									CHAIN: A, B;”	PROTEIN”
315	1fak	L	552	650	8.40E−27	0.41	0.25		BLOOD COAGULATION	“BLOOD CLOTTING COMPLEX(SERINE
									FACTOR VIIA; CHAIN: L;	PROTEASE/COFACTOR/LIGAND), BLOOD
									BLOOD COAGULATION	COAGULATION, 2 SERINE PROTEASE,
									FACTOR VIIA; CHAIN: H;	COMPLEX, CO-FACTOR, RECEPTOR
									SOLUBLE TISSUE FACTOR;	ENZYME, 3 INHIBITOR, GLA, EGF,
									CHAIN: T; 5L15; CHAIN: I;	COMPLEX (SERINE 4
										PROTEASE/COFACTOR/LIGAND), BLOOD
										CLOTTING”
315	1fak	L	594	698	1.00E−20	0.11	0		BLOOD COAGULATION	“BLOOD CLOTTING COMPLEX(SERINE
									FACTOR VIIA; CHAIN: L;	PROTEASE/COFACTOR/LIGAND), BLOOD
									BLOOD COAGULATION	COAGULATION, 2 SERINE PROTEASE,
									FACTOR VIIA; CHAIN: H;	COMPLEX, CO-FACTOR, RECEPTOR
									SOLUBLE TISSUE FACTOR;	ENZYME, 3 INHIBITOR, GLA, EGF,
									CHAIN: T; 5L15; CHAIN: I;	COMPLEX (SERINE 4
										PROTEASE/COFACTOR/LIGAND), BLOOD
										CLOTTING”
315	1fak	L	763	867	4.20E−20	0.15	0.47		BLOOD COAGULATION	“BLOOD CLOTTING COMPLEX(SERINE
									FACTOR VIIA; CHAIN: L;	PROTEASE/COFACTOR/LIGAND), BLOOD
									BLOOD COAGULATION	COAGULATION, 2 SERINE PROTEASE,
									FACTOR VIIA; CHAIN: H;	COMPLEX, CO-FACTOR, RECEPTOR
									SOLUBLE TISSUE FACTOR;	ENZYME, 3 INHIBITOR, GLA, EGF,
									CHAIN: T; 5L15; CHAIN: I;	COMPLEX (SERINE 4
										PROTEASE/COFACTOR/LIGAND), BLOOD
										CLOTTING”
315	1fak	L	1054	1148	4.20E−14	0.42	1		BLOOD COAGULATION	“BLOOD CLOTTING COMPLEX(SERINE
									FACTOR VIIA; CHAIN: L;	PROTEASE/COFACTOR/LIGAND), BLOOD
									BLOOD COAGULATION	COAGULATION, 2 SERINE PROTEASE,
									FACTOR VIIA; CHAIN: H;	COMPLEX, CO-FACTOR, RECEPTOR
									SOLUBLE TISSUE FACTOR;	ENZYME, 3 INHIBITOR, GLA, EGF,
									CHAIN: T; 5L15; CHAIN: I;	COMPLEX (SERINE 4
										PROTEASE/COFACTOR/LIGAND), BLOOD
										CLOTTING”
315	1fak	L	207	292	3.40E−13	0.23	−0.07		BLOOD COAGULATION	“BLOOD CLOTTING COMPLEX(SERINE
									FACTOR VIIA; CHAIN: L;	PROTEASE/COFACTOR/LIGAND), BLOOD
									BLOOD COAGULATION	COAGULATION, 2 SERINE PROTEASE,
									FACTOR VIIA; CHAIN: H;	COMPLEX, CO-FACTOR, RECEPTOR
									SOLUBLE TISSUE FACTOR;	ENZYME, 3 INHIBITOR, GLA, EGF,
									CHAIN: T; 5L15; CHAIN: I;	COMPLEX (SERINE 4
										PROTEASE/COFACTOR/LIGAND), BLOOD
										CLOTTING”
315	1fak	L	1338	1423	5.10E−13	−0.55	0.09		BLOOD COAGULATION	“BLOOD CLOTTING COMPLEX(SERINE
									FACTOR VIIA; CHAIN: L;	PROTEASE/COFACTOR/LIGAND), BLOOD
									BLOOD COAGULATION	COAGULATION, 2 SERINE PROTEASE,
									FACTOR VIIA; CHAIN: H;	COMPLEX, CO-FACTOR, RECEPTOR
									SOLUBLE TISSUE FACTOR;	ENZYME, 3 INHIBITOR, GLA, EGF,
									CHAIN: T; 5L15; CHAIN: I;	COMPLEX (SERINE 4
										PROTEASE/COFACTOR/LIGAND), BLOOD
										CLOTTING”
315	1fak	L	244	329	5.10E−13	−0.09	0.31		BLOOD COAGULATION	“BLOOD CLOTTING COMPLEX(SERINE
									FACTOR VIIA; CHAIN: L;	PROTEASE/COFACTOR/LIGAND), BLOOD
									BLOOD COAGULATION	COAGULATION, 2 SERINE PROTEASE,
									FACTOR VIIA; CHAIN: H;	COMPLEX, CO-FACTOR, RECEPTOR
									SOLUBLE TISSUE FACTOR;	ENZYME, 3 INHIBITOR, GLA, EGF,
									CHAIN: T; 5L15; CHAIN: I;	COMPLEX (SERINE 4
										PROTEASE/COFACTOR/LIGAND), BLOOD
										CLOTTING”
315	1fjs	L	1338	1379	6.30E−09	−0.14	0		COAGULATION FACTOR	“BLOOD CLOTTING PROTEIN INHIBITOR
									XA; CHAIN: A;	COMPLEX, COAGULATION COFACTOR,
									COAGULATION FACTOR	PROTEASE”
									XA; CHAIN: L;
315	1igr	A	834	998	5.10E−09	0.13	−0.19		INSULIN-LIKE GROWTH	“HORMONE RECEPTOR HORMONE
									FACTOR RECEPTOR 1;	RECEPTOR, INSULIN RECEPTOR FAMILY”
									CHAIN: A;
315	1jia	A	485	601	1.90E−25	0.09	−0.14		“PHOSPHOLIPASE A2;	“PHOSPHOLIPASE PHOSPHOLIPASE A2,
									CHAIN: A, B;”	AGKISTRODON HALYS PALLAS
										CRYSTAL 2 STRUCTURE”
315	1klo		556	738	6.30E−22	0.26	−0.11		LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
315	1klo		649	811	1.00E−20	0.44	−0.07		LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
315	1klo		731	903	1.90E−20	0.18	−0.14		LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
315	1klo		157	296	3.40E−12	0.11	−0.2		LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
315	1klo		900	1056	1.20E−09	0.03	−0.2		LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
315	1klo		329	473	5.10E−09	0.07	−0.19		LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
315	1klo		1311	1420	1.10E−08	0.06	−0.15		LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
315	1ncf	A	1005	112	1.10E−07	0.06	0.05		“TUMOR NECROSIS	“SIGNALLING PROTEIN TYPE I
				6					FACTOR RECEPTOR; INCF 4	RECEPTOR, STNFR1; 1NCF 8 BINDING
									CHAIN: A, B; INCF 5”	PROTEIN, CYTOKINE 1NCF 19”
315	1pfx	L	38	114	6.80E−12	−0.36	0		“FACTOR IXA; CHAIN: C, L,;	“COMPLEX (BLOOD
									D-PHE-PRO-ARG; CHAIN: I;”	COAGULATION/INHIBITOR) CHRISTMAS
										FACTOR; COMPLEX, INHIBITOR,
										HEMOPHILIA/EGF, BLOOD
										COAGULATION, 2 PLASMA, SERINE
										PROTEASE, CALCIUM-BINDING,
										HYDROLASE, 3 GLYCOPROTEIN”
315	1pfx	L	241	320	6.80E−10	0.15	0.13		“FACTOR IXA; CHAIN: C, L,;	“COMPLEX (BLOOD
									D-PHE-PRO-ARG; CHAIN: I;”	COAGULATION/INHIBITOR) CHRISTMAS
										FACTOR; COMPLEX, INHIBITOR,
										HEMOPHILIA/EGF, BLOOD
										COAGULATION, 2 PLASMA, SERINE
										PROTEASE, CALCIUM-BINDING,
										HYDROLASE, 3 GLYCOPROTEIN”
315	1pp2	R	682	811	1.50E−26	0.39	−0.11			HYDROLASE CALCIUM-FREE
										PHOSPHOLIPASE A = 2 = (E.C.3.1.1.4) 1PP2 4
315	1qfk	L	600	691	1.30E−21	0.18	0.65		COAGULATION FACTOR	“SERINE PROTEASE FVIIA; FVIIA; BLOOD
									VIIA (LIGHT CHAIN);	COAGULATION, SERINE PROTEASE”
									CHAIN: L; COAGULATION
									FACTOR VIIA (HEAVY
									CHAIN); CHAIN: H;
									TRIPEPTIDYL INHIBITOR;
									CHAIN: C;
315	1qfk	L	768	860	4.20E−20	0.04	0.4		COAGULATION FACTOR	“SERINE PROTEASE FVIIA; FVIIA; BLOOD
									VIIA (LIGHT CHAIN);	COAGULATION, SERINE PROTEASE”
									CHAIN: L, COAGULATION
									FACTOR VIIA (HEAVY
									CHAIN); CHAIN: H;
									TRIPEPTIDYL INHIBITOR;
									CHAIN: C;
315	1qfk	L	436	543	8.40E−19	0.03	0.15		COAGULATION FACTOR	“SERINE PROTEASE FVIIA; FVIIA; BLOOD
									VIIA (LIGHT CHAIN);	COAGULATION, SERINE PROTEASE”
									CHAIN: L; COAGULATION
									FACTOR VIIA (HEAVY
									CHAIN); CHAIN: H;
									TRIPEPTIDYL INHIBITOR;
									CHAIN: C;
315	1qfk	L	1337	1420	1.10E−14	−0.48	0.03		COAGULATION FACTOR	“SERINE PROTEASE FVIIA; FVIIA; BLOOD
									VIIA (LIGHT CHAIN);	COAGULATION, SERINE PROTEASE”
									CHAIN: L; COAGULATION
									FACTOR VIIA (HEAVY
									CHAIN); CHAIN: H;
									TRIPEPTIDYL INHIBITOR;
									CHAIN: C;
315	1qfk	L	1057	1152	4.20E−14	−0.02	0.95		COAGULATION FACTOR	“SERINE PROTEASE FVIIA; FVIIA; BLOOD
									VIIA (LIGHT CHAIN);	COAGULATION, SERINE PROTEASE”
									CHAIN: L; COAGULATION
									FACTOR VIIA (HEAVY
									CHAIN); CHAIN: H;
									TRIPEPTIDYL INHIBITOR;
									CHAIN: C;
315	1qfk	L	1338	1423	5.10E−13	−0.17	0.55		COAGULATION FACTOR	“SERINE PROTEASE FVIIA; FVIIA; BLOOD
									VIIA (LIGHT CHAIN);	COAGULATION, SERINE PROTEASE”
									CHAIN: L; COAGULATION
									FACTOR VIIA (HEAVY
									CHAIN); CHAIN: H;
									TRIPEPTIDYL INHIBITOR;
									CHAIN: C;
315	1qfk	L	248	329	6.80E−12	−0.12	0.29		COAGULATION FACTOR	“SERINE PROTEASE FVIIA; FVIIA; BLOOD
									VIIA (LIGHT CHAIN);	COAGULATION, SERINE PROTEASE”
									CHAIN: L; COAGULATION
									FACTOR VIIA (HEAVY
									CHAIN); CHAIN: H;
									TRIPEPTIDYL INHIBITOR;
									CHAIN: C;
315	1tpg		619	727	1.50E−21	0.3	0.11		T-PLASMINOGEN	PLASMINOGEN ACTIVATION
									ACTIVATOR F1-G; 1TPG 7
									CHAIN: NULL; 1TPG 8
315	1tpg		455	562	2.10E−19	−0.18	0.16		T-PLASMINOGEN	PLASMINOGEN ACTIVATION
									ACTIVATOR F1-G; 1TPG 7
									CHAIN: NULL; 1TPG 8
315	1vap	A	485	601	4.20E−31	0.15	−0.09		“PHOSPHOLIPASE A2;	“LIPID DEGRADATION PHOSPHOLIPASE
									CHAIN: A, B;”	A2, LIPID DEGRADATION, HYDROLASE”
315	1vap	A	569	685	2.10E−26	0.09	−0.14		“PHOSPHOLIPASE A2;	“LIPID DEGRADATION PHOSPHOLIPASE
									CHAIN: A, B;”	A2, LIPID DEGRADATION, HYDROLASE”
315	1vap	A	732	852	2.10E−23	0	−0.19		“PHOSPHOLIPASE A2;	“LIPID DEGRADATION PHOSPHOLIPASE
									CHAIN: A, B;”	A2, LIPID DEGRADATION, HYDROLASE”
315	1vap	A	653	769	1.30E−21	0.18	−0.18		“PHOSPHOLIPASE A2;	“LIPID DEGRADATION PHOSPHOLIPASE
									CHAIN: A, B;”	A2, LIPID DEGRADATION, HYDROLASE”
315	1vap	A	692	811	2.10E−21	0.25	−0.14		“PHOSPHOLIPASE A2;	“LIPID DEGRADATION PHOSPHOLIPASE
									CHAIN: A, B;”	A2, LIPID DEGRADATION, HYDROLASE”
315	1vpi		685	811	2.10E−24	0.31	−0.15		PHOSPHOLIPASE A2	“NEUROTOXIN PHOSPHOLIPASE A2
									INHIBITOR; CHAIN: NULL	INHIBITOR, X-RAY STRUCTURE,
										RECOGNITION, 2 MOLECULAR
										EVOLUTION, NEUROTOXIN”
315	1xka	L	208	295	1.70E−13	0.03	−0.03		“BLOOD COAGULATION	“BLOOD COAGULATION FACTOR
									FACTOR XA; CHAIN: L, C;”	STUART FACTOR; BLOOD
										COAGULATION FACTOR, SERINE
										PROTEINASE, EPIDERMAL 2 GROWTH
										FACTOR LIKE DOMAIN”
315	1xka	L	248	322	1.50E−09	0.02	−0.07		“BLOOD COAGULATION	“BLOOD COAGULATION FACTOR
									FACTOR XA; CHAIN: L, C;”	STUART FACTOR; BLOOD
										COAGULATION FACTOR, SERINE
										PROTEINASE, EPIDERMAL 2 GROWTH
										FACTOR LIKE DOMAIN”
315	2not	A	808	921	2.10E−12	0.07	−0.13		“PHOSPHOLIPASE A2;	“HYDROLASE HYDROLASE, LIPID
									CHAIN: A, B;”	DEGRADATION, CALCIUM,
										PRESYNAPTIC 2 NEUROTOXIN, VENOM”
315	9wga	A	70	268	1.70E−12	0.02	−0.19			LECTIN (AGGLUTININ) WHEAT GERM
										AGGLUTININ (ISOLECTIN 2) 9WGA 3
315	9wga	A	286	468	5.10E−11	0.15	−0.2			LECTIN (AGGLUTININ) WHEAT GERM
										AGGLUTININ (ISOLECTIN 2) 9WGA 3
317	1ihb	A	72	223	1.10E−33			74.13	“CYCLIN-DEPENDENT	“CELL CYCLE INHIBITOR P18-
									KINASE 6 INHIBITOR;	INK4C(INK6); CELL CYCLE INHIBITOR,
									CHAIN: A, B;”	P18-INK4C(INK6), ANKYRIN REPEAT, 2
										CDK 4/6 INHIBITOR”
317	1ikn	D	103	337	4.80E−39			74.28	NF-KAPPA-B P65 SUBUNIT;	“TRANSCRIPTION FACTOR P65; P50D;
									CHAIN: A; NF-KAPPA-B	TRANSCRIPTION FACTOR, IKB/NFKB
									P50D SUBUNIT; CHAIN: C; I-	COMPLEX”
									KAPPA-B-ALPHA; CHAIN: D;
317	1nfi	E	100	326	3.20E−39			79.82	“NF-KAPPA-B P65; CHAIN:	“COMPLEX (TRANSCRIPTION REG/ANK
									A, C; NF-KAPPA-B P50;	REPEAT) COMPLEX (TRANSCRIPTION
									CHAIN: B, D; I-KAPPA-B-	REGULATION/ANK REPEAT), ANKYRIN 2
									ALPHA; CHAIN: E, F;”	REPEAT HELIX”
317	1ycs	B	71	276	4.80E−25			86.29	P53; CHAIN: A; 53BP2;	“COMPLEX (ANTI-ONCOGENE/ANKYRIN
									CHAIN: B;	REPEATS) P53BP2; ANKYRIN REPEATS,
										SH3, P53, TUMOR SUPPRESSOR,
										MULTIGENE 2 FAMILY, NUCLEAR
										PROTEIN, PHOSPHORYLATION, DISEASE
										MUTATION, 3 POLYMORPHISM,
										COMPLEX (ANTI-ONCOGENE/ANKYRIN
										REPEATS)”
319	1got	B	360	691	1.30E−67			82.31	GT-ALPHA/GI-ALPHA	“COMPLEX (GTP-BINDING/TRANSDUCER)
									CHIMERA; CHAIN: A; GT-	BETA1, TRANSDUCIN BETA SUBUNIT;
									BETA; CHAIN: B; GT-	GAMMA1, TRANSDUCIN GAMMA
									GAMMA; CHAIN: G;	SUBUNIT; COMPLEX (GTP-
										BINDING/TRANSDUCER), G PROTEIN,
										HETEROTRIMER 2 SIGNAL
										TRANSDUCTION”
324	1ilb		27	172	3.20E−52			68.78		CYTOKINE INTERLEUKIN-1*BETA (/IL$-
										1*BETA) 1I1B4
324	1ilt	A	28	172	1.30E−48			111.09		CYTOKINE INTERLEUKIN-1 RECEPTOR
										ANTAGONIST (IL-1RA) (ALPHA
										CARBONS) 1ILT 3
324	1irp		18	172	3.20E−50			113.23		“CYTOKINE INTERLEUKIN-1 RECEPTOR
										ANTAGONIST PROTEIN 1IRP 3 (NMR, 12
										STRUCTURES) 1IRP 4”
324	8ilb		29	172	4.80E−49			75.29		CYTOKINE INTERLEUKIN 1-*BETA 8I1B 3
325	1a5e		64	178	9.60E−25	0.45	1		TUMOR SUPPRESSOR	“ANTI-ONCOGENE CELL CYCLE, ANTI-
									P16INK4A; CHAIN: NULL;	ONCOGENE, REPEAT, ANK REPEAT”
325	1awc	B	30	178	1.40E−42	0.56	1		“GA BINDING PROTEIN	“COMPLEX (TRANSCRIPTION-
									ALPHA; CHAIN: A; GA	REGULATION/DNA) GABPALPHA;
									BINDING PROTEIN BETA 1;	GABPBETA1; COMPLEX (TRANSCRIPTION
									CHAIN: B; DNA; CHAIN: D,	REGULATION/DNA), DNA-BINDING, 2
									E;”	NUCLEAR PROTEIN, ETS DOMAIN,
										ANKYRIN REPEATS, TRANSCRIPTION 3
										FACTOR”
325	1awc	B	64	195	4.80E−37	0.56	1		“GA BINDING PROTEIN	“COMPLEX (TRANSCRIPTION
									ALPHA; CHAIN: A; GA	REGULATION/DNA) GABPALPHA;
									BINDING PROTEIN BETA 1;	GABPBETA1; COMPLEX (TRANSCRIPTION
									CHAIN: B; DNA; CHAIN: D,	REGULATION/DNA), DNA-BINDING, 2
									E;”	NUCLEAR PROTEIN, ETS DOMAIN,
										ANKYRIN REPEATS, TRANSCRIPTION 3
										FACTOR”
325	1awc	B	3	145	1.60E−34	0.39	1		“GA BINDING PROTEIN	“COMPLEX (TRANSCRIPTION
									ALPHA; CHAIN: A; GA	REGULATION/DNA) GABPALPHA;
									BINDING PROTEIN BETA 1;	GABPBETA1; COMPLEX (TRANSCRIPTION
									CHAIN: B; DNA; CHAIN: D,	REGULATION/DNA), DNA-BINDING, 2
									E;”	NUCLEAR PROTEIN, ETS DOMAIN,
										ANKYRIN REPEATS, TRANSCRIPTION 3
										FACTOR”
325	1awc	B	26	179	1.40E−42			61.33	“GA BINDING PROTEIN	“COMPLEX (TRANSCRIPTION
									ALPHA; CHAIN: A; GA	REGULATION/DNA) GABPALPHA;
									BINDING PROTEIN BETA 1;	GABPBETA1; COMPLEX (TRANSCRIPTION
									CHAIN: B; DNA; CHAIN: D,	REGULATION/DNA), DNA-BINDING, 2
									E;”	NUCLEAR PROTEIN, ETS DOMAIN,
										ANKYRIN REPEATS, TRANSCRIPTION 3
										FACTOR”
325	1bd8		28	181	9.60E−33			57.12	P19INK4D CDK4/6	“TUMOR SUPPRESSOR TUMOR
									INHIBITOR; CHAIN: NULL;	SUPPRESSOR, CDK4/6 INHIBITOR,
										ANKYRIN MOTIF”
325	1bi7	B	64	178	8.00E−26	0.4	1		CYCLIN-DEPENDENT	“COMPLEX (KINASE/ANTI-ONCOGENE)
									KINASE 6; CHAIN: A;	CDK6; P16INK4A, MTS1; CYCLIN
									MULTIPLE TUMOR	DEPENDENT KINASE, CYCLIN
									SUPPRESSOR; CHAIN: B;	DEPENDENT KINASE INHIBITORY 2
										PROTEIN, CDK, INK4, CELL CYCLE,
										MULTIPLE TUMOR SUPPRESSOR, 3 MTS1,
										COMPLEX (KINASE/ANTI-ONCOGENE)
										HEADER”
325	1blx	B	30	182	9.80E−36	0.57	1		CYCLIN-DEPENDENT	“COMPLEX (INHIBITOR
									KINASE 6; CHAIN: A;	PROTEIN/KINASE) INHIBITOR PROTEIN,
									P19INK4D; CHAIN: B;	CYCLIN-DEPENDENT KINASE, CELL
										CYCLE 2 CONTROL, ALPHA/BETA,
										COMPLEX (INHIBITOR
										PROTEIN/KINASE)”
325	1blx	B	62	195	4.20E−31	0.49	1		CYCLIN-DEPENDENT	“COMPLEX (INHIBITOR
									KINASE 6; CHAIN: A;	PROTEIN/KINASE) INHIBITOR PROTEIN,
									P19INK4D; CHAIN: B;	CYCLIN-DEPENDENT KINASE, CELL
										CYCLE 2 CONTROL, ALPHA/BETA,
										COMPLEX (INHIBITOR
										PROTEIN/KINASE)”
325	1blx	B	1	152	9.80E−36			54.31	CYCLIN-DEPENDENT	“COMPLEX (INHIBITOR
									KINASE 6; CHAIN: A;	PROTEIN/KINASE) INHIBITOR PROTEIN,
									P19INK4D; CHAIN: B;	CYCLIN-DEPENDENT KINASE, CELL
										CYCLE 2 CONTROL, ALPHA/BETA,
										COMPLEX (INHIBITOR
										PROTEIN/KINASE)”
325	1bu9	A	30	183	4.80E−37	0.65	1		CYCLIN-DEPENDENT	“HORMONE/GROWTH FACTOR P18-
									KINASE 6 INHIBITOR;	INK4C; CELL CYCLE INHIBITOR,
									CHAIN: A;	P18INK4C, TUMOR, SUPPRESSOR,
										CYCLIN-2 DEPENDENT KINASE,
										HORMONE/GROWTH FACTOR”
325	1bu9	A	64	195	6.40E−33	0.35	1		CYCLIN-DEPENDENT	“HORMONE/GROWTH FACTOR P18-
									KINASE 6 INHIBITOR;	INK4C; CELL CYCLE INHIBITOR,
									CHAIN: A;	P18INK4C, TUMOR, SUPPRESSOR,
										CYCLIN-2 DEPENDENT KINASE,
										HORMONE/GROWTH FACTOR”
325	1bu9	A	25	189	4.80E−37			59.82	CYCLIN-DEPENDENT	“HORMONE/GROWTH FACTOR P18-
									KINASE 6 INHIBITOR;	INK4C; CELL CYCLE INHIBITOR,
									CHAIN: A;	P18INK4C, TUMOR, SUPPRESSOR,
										CYCLIN-2 DEPENDENT KINASE,
										HORMONE/GROWTH FACTOR”
325	1d9s	A	83	195	7.00E−27	0.41	1		CYCLIN-DEPENDENT	“SIGNALING PROTEIN HELIX-TURN-
									KINASE 4 INHIBITOR B;	HELIX, ANKYRIN REPEAT”
									CHAIN: A;
325	1d9s	A	64	184	4.80E−26	0.24	1		CYCLIN-DEPENDENT	“SIGNALING PROTEIN HELIX-TURN-
									KINASE 4 INHIBITOR B;	HELIX, ANKYRIN REPEAT”
									CHAIN: A;
325	1ihb	A	30	182	1.60E−36	0.72	1		“CYCLIN-DEPENDENT	“CELL CYCLE INHIBITOR P18-
									KINASE 6 INHIBITOR;	INK4C(INK6); CELL CYCLE INHIBITOR,
									CHAIN: A, B;”	P18-INK4C(INK6), ANKYRIN REPEAT, 2
										CDK 4/6 INHIBITOR”
325	1ihb	A	64	195	6.40E−33	0.45	1		“CYCLIN-DEPENDENT	“CELL CYCLE INHIBITOR P18-
									KINASE 6 INHIBITOR;	INK4C(INK6); CELL CYCLE INHIBITOR,
									CHAIN: A, B;”	P18-INK4C(INK6), ANKYRIN REPEAT, 2
										CDK 4/6 INHIBITOR”
325	1ihb	A	27	182	1.60E−36			63.67	“CYCLIN-DEPENDENT	“CELL CYCLE INHIBITOR P18-
									KINASE 6 INHIBITOR;	INK4C(INK6); CELL CYCLE INHIBITOR,
									CHAIN: A, B;”	P18-INK4C(INK6), ANKYRIN REPEAT, 2
										CDK 4/6 INHIBITOR”
325	1ikn	D	25	195	1.60E−41	0.31	1		NF-KAPPA-B P65 SUBUNIT;	“TRANSCRIPTION FACTOR P65; P50D;
									CHAIN: A; NF-KAPPA-B	TRANSCRIPTION FACTOR, IKB/NFKB
									P50D SUBUNIT; CHAIN: C; I-	COMPLEX”
									KAPPA-B-ALPHA; CHAIN: D;
325	1ikn	D	17	162	4.80E−36	0.4	1		NF-KAPPA-B P65 SUBUNIT;	“TRANSCRIPTION FACTOR P65; P50D;
									CHAIN: A; NF-KAPPA-B	TRANSCRIPTION FACTOR, IKB/NFKB
									P50D SUBUNIT; CHAIN: C; I-	COMPLEX”
									KAPPA-B-ALPHA; CHAIN: D;
325	1ikn	D	2	193	1.60E−41			54.26	NF-KAPPA-B P65 SUBUNIT;	“TRANSCRIPTION FACTOR P65; P50D;
									CHAIN: A; NF-KAPPA-B	TRANSCRIPTION FACTOR, IKB/NFKB
									P50D SUBUNIT; CHAIN: C; I-	COMPLEX”
									KAPPA-B-ALPHA; CHAIN: D;
325	1myo		65	180	8.00E−26	0.13	0.71		MYOTROPHIN; CHAIN:	“ANK-REPEAT MYOTROPHIN,
									NULL	ACETYLATION, NMR, ANK-REPEAT”
325	1myo		95	195	1.10E−25	0.36	1		MYOTROPHIN; CHAIN:	“ANK-REPEAT MYOTROPHIN,
									NULL	ACETYLATION, NMR, ANK-REPEAT”
325	1myo		98	196	3.20E−24	0.14	1		MYOTROPHIN; CHAIN:	“ANK-REPEAT MYOTROPHIN,
									NULL	ACETYLATION, NMR, ANK-REPEAT”
325	1myo		27	143	1.40E−31			61.01	MYOTROPHIN; CHAIN:	“ANK-REPEAT MYOTROPHIN,
									NULL	ACETYLATION, NMR, ANK-REPEAT”
325	1nfi	E	24	195	1.30E−41	0.41	1		“NF-KAPPA-B P65; CHAIN:	“COMPLEX (TRANSCRIPTION REG/ANK
									A, C; NF-KAPPA-B P50;	REPEAT) COMPLEX (TRANSCRIPTION
									CHAIN: B, D; I-KAPPA-B-	REGULATION/ANK REPEAT), ANKYRIN 2
									ALPHA; CHAIN: E, F;”	REPEAT HELIX”
325	1ycs	B	62	192	4.20E−30	0.4	0.98		P53; CHAIN: A; 53BP2;	“COMPLEX (ANTI-ONCOGENE/ANKYRIN
									CHAIN: B;	REPEATS) P53BP2; ANKYRIN REPEATS,
										SH3, P53, TUMOR SUPPRESSOR,
										MULTIGENE 2 FAMILY, NUCLEAR
										PROTEIN, PHOSPHORYLATION, DISEASE
										MUTATION, 3 POLYMORPHISM,
										COMPLEX (ANTI-ONCOGENE/ANKYRIN
										REPEATS)”
326	1apm	E	76	302	6.40E−81			86.74		“TRANSFERASE(PHOSPHOTRANSFERASE)
										$C-/AMP$-DEPENDENT PROTEIN
										KINASE (E.C.2.7.1.37) ($C/APK$) 1APM 3
										(CATALYTIC SUBUNIT) ““ALPHA””
										ISOENZYME MUTANT WITH SER 139
										1APM 4 REPLACED BY ALA (/S139A$)
										COMPLEX WITH THE PEPTIDE 1APM 5
										INHIBITOR PKI(5-24) AND THE
										DETERGENT MEGA-8 1APM 6”
326	1cmk	E	60	302	3.20E−82			88.65		PHOSPHOTRANSFERASE CAMP-
										DEPENDENT PROTEIN KINASE
										CATALYTIC SUBUNIT 1CMK 3
										(E.C.2.7.1.37) 1CMK 4
326	1ctp	E	77	302	3.20E−82			95.33		TRANSFERASE(PHOSPHOTRANSFERASE)
										CAMP-DEPENDENT PROTEIN KINASE
										(E.C.2.7.1.37) (CAPK) 1CTP 3 (CATALYTIC
										SUBUNIT) 1CTP 4
326	1phk		104	302	1.60E−57			71.37	PHOSPHORYLASE KINASE;	“KINASE RABBIT MUSCLE
									CHAIN: NULL;	PHOSPHORYLASE KINASE; GLYCOGEN
										METABOLISM, TRANSFERASE,
										SERINE/THREONINE-PROTEIN, 2 KINASE,
										ATP-BINDING, CALMODULIN-BINDING”
327	1erj	A	118	435	3.20E−65	0.15	0.95		“TRANSCRIPTIONAL	TRANSCRIPTION INHIBITOR BETA-
									REPRESSOR TUP1; CHAIN:	PROPELLER
									A, B, C;”
327	1erj	A	262	542	8.00E−65	0.15	0.68		“TRANSCRIPTIONAL	TRANSCRIPTION INHIBITOR BETA-
									REPRESSOR TUP1; CHAIN:	PROPELLER
									A, B, C;”
327	1erj	A	215	524	1.60E−62	0.37	0.98		“TRANSCRIPTIONAL	TRANSCRIPTION INHIBITOR BETA-
									REPRESSOR TUP1; CHAIN:	PROPELLER
									A, B, C;”
327	1erj	A	166	471	2.80E−19	0.41	0.1		“TRANSCRIPTIONAL	TRANSCRIPTION INHIBITOR BETA-
									REPRESSOR TUP1; CHAIN:	PROPELLER
									A, B, C;”
327	1got	B	168	480	1.60E−74	0.07	0.6		GT-ALPHA/GI-ALPHA	“COMPLEX (GTP-BINDING/TRANSDUCER)
									CHIMERA; CHAIN: A; GT-	BETA1, TRANSDUCIN BETA SUBUNIT;
									BETA; CHAIN: B; GT-	GAMMA1, TRANSDUCIN GAMMA
									GAMMA; CHAIN: G;	SUBUNIT; COMPLEX (GTP-
										BINDING/TRANSDUCER), G PROTEIN,
										HETEROTRIMER 2 SIGNAL
										TRANSDUCTION”
327	1got	B	249	564	1.60E−63	0.1	0.82		GT-ALPHA/GI-ALPHA	“COMPLEX (GTP-BINDING/TRANSDUCER)
									CHIMERA; CHAIN: A; GT-	BETA1, TRANSDUCIN BETA SUBUNIT;
									BETA; CHAIN: B; GT-	GAMMA1, TRANSDUCIN GAMMA
									GAMMA; CHAIN: G;	SUBUNIT; COMPLEX (GTP-
										BINDING/TRANSDUCER), G PROTEIN,
										HETEROTRIMER 2 SIGNAL
										TRANSDUCTION”
327	1got	B	2	293	1.30E−56	−0.12	0		GT-ALPHA/GI-ALPHA	“COMPLEX (GTP-BINDING/TRANSDUCER)
									CHIMERA; CHAIN: A; GT-	BETA1, TRANSDUCIN BETA SUBUNIT;
									BETA; CHAIN: B; GT-	GAMMA1, TRANSDUCIN GAMMA
									GAMMA; CHAIN: G;	SUBUNIT; COMPLEX (GTP-
										BINDING/TRANSDUCER), G PROTEIN,
										HETEROTRIMER 2 SIGNAL
										TRANSDUCTION”
327	1got	B	358	576	4.80E−40	0.15	0.06		GT-ALPHA/GI-ALPHA	“COMPLEX (GTP-BINDING/TRANSDUCER)
									CHIMERA; CHAIN: A; GT-	BETA1, TRANSDUCIN BETA SUBUNIT;
									BETA; CHAIN: B; GT-	GAMMA1, TRANSDUCIN GAMMA
									GAMMA; CHAIN: G;	SUBUNIT; COMPLEX (GTP-
										BINDING/TRANSDUCER), G PROTEIN,
										HETEROTRIMER 2 SIGNAL
										TRANSDUCTION”
327	1got	B	121	480	1.60E−74			98.86	GT-ALPHA/GI-ALPHA	“COMPLEX (GTP-BINDING/TRANSDUCER)
									CHIMERA; CHAIN: A; GT-	BETA1, TRANSDUCIN BETA SUBUNIT;
									BETA; CHAIN: B; GT-	GAMMA1, TRANSDUCIN GAMMA
									GAMMA; CHAIN: G;	SUBUNIT; COMPLEX (GTP-
										BINDING/TRANSDUCER), G PROTEIN,
										HETEROTRIMER 2 SIGNAL
										TRANSDUCTION”
329	1a25	A	324	445	3.20E−25	0.37	0.99		“PROTEIN KINASE C	“CALCIUM-BINDING PROTEIN CALB;
									(BETA); CHAIN: A, B;”	CALCIUM++/PHOSPHOLIPID BINDING
										PROTEIN, 2 CALCIUM-BINDING PROTEIN”
329	1a25	A	186	295	8.00E−24	0.07	0.62		“PROTEIN KINASE C	“CALCIUM-BINDING PROTEIN CALB;
									(BETA); CHAIN: A, B;”	CALCIUM++/PHOSPHOLIPID BINDING
										PROTEIN, 2 CALCIUM-BINDING PROTEIN”
329	1a25	A	317	447	3.20E−25			53.2	“PROTEIN KINASE C	“CALCIUM-BINDING PROTEIN CALB;
									(BETA); CHAIN: A, B;”	CALCIUM++/PHOSPHOLIPID BINDING
										PROTEIN, 2 CALCIUM-BINDING PROTEIN”
329	1byn	A	186	308	9.60E−34	0.54	0.92		SYNAPTOTAGMIN I; CHAIN:	“ENDOCYTOSIS/EXOCYTOSIS
									A;	SYNAPTOTAGMIN, C2-DOMAIN,
										EXOCYTOSIS, NEUROTRANSMITTER 2
										RELEASE, ENDOCYTOSIS/EXOCYTOSIS”
329	1byn	A	325	441	4.80E−20	0.55	0.98		SYNAPTOTAGMIN I; CHAIN:	“ENDOCYTOSIS/EXOCYTOSIS
									A;	SYNAPTOTAGMIN, C2-DOMAIN,
										EXOCYTOSIS, NEUROTRANSMITTER 2
										RELEASE, ENDOCYTOSIS/EXOCYTOSIS”
329	1cjy	A	201	314	8.00E−14	0.23	0.11		“CYTOSOLIC	“HYDROLASE CPLA2; PHOSPHOLIPASE,
									PHOSPHOLIPASE A2;	LIPID-BINDING, HYDROLASE”
									CHAIN: A, B;”
329	1dqv	A	189	453	3.20E−65	0.46	1		SYNAPTOTAGMIN III;	“ENDOCYTOSIS/EXOCYTOSIS BETA
									CHAIN: A;	SANDWICH, CALCIUM ION, C2 DOMAIN”
329	1dsy	A	185	299	6.40E−27	0.34	0.89		“PROTEIN KINASE C,	“TRANSFERASE CALCIUM++,
									ALPHA TYPE; CHAIN: A;”	PHOSPHOLIPID BINDING PROTEIN,
										CALCIUM-BINDING 2 PROTEIN,
										PHOSPHATIDYLSERINE, PROTEIN
										KINASE C”
329	1dsy	A	324	445	4.80E−25	0.35	0.93		“PROTEIN KINASE C,	“TRANSFERASE CALCIUM++,
									ALPHA TYPE; CHAIN: A;”	PHOSPHOLIPID BINDING PROTEIN,
										CALCIUM-BINDING 2 PROTEIN,
										PHOSPHATIDYLSERINE, PROTEIN
										KINASE C”
329	1rlw		201	314	8.00E−14	−0.07	0.13		PHOSPHOLIPASE A2;	“HYDROLASE CALB DOMAIN;
									CHAIN: NULL;	HYDROLASE, C2 DOMAIN, CALB
										DOMAIN”
329	1rsy		186	308	9.60E−34	0.02	0.89			CALCIUM/PHOSPHOLIPID BINDING
										PROTEIN SYNAPTOTAGMIN I (FIRST C2
										DOMAIN) (CALB) 1RSY 3
329	1rsy		314	439	2.80E−25	0.46	0.98			CALCIUM/PHOSPHOLIPID BINDING
										PROTEIN SYNAPTOTAGMIN I (FIRST C2
										DOMAIN) (CALB) 1RSY 3
329	1rsy		325	441	4.80E−20	0.48	0.9			CALCIUM/PHOSPHOLIPID BINDING
										PROTEIN SYNAPTOTAGMIN I (FIRST C2
										DOMAIN) (CALB) 1RSY 3
329	1rsy		311	442	2.80E−25			65.47		CALCIUM/PHOSPHOLIPID BINDING
										PROTEIN SYNAPTOTAGMIN I (FIRST C2
										DOMAIN) (CALB) 1RSY 3
329	3rpb	A	322	454	1.60E−32	0.65	1		RABPHILIN 3-A; CHAIN: A;	“ENDOCYTOSIS/EXOCYTOSIS C2-
										DOMAINS, C2B-DOMAIN, RABPHILIN,
										ENDOCYTOSIS/EXOCYTOSIS”
329	3rpb	A	188	318	4.80E−25	0.32	0.84		RABPHILIN 3-A; CHAIN: A;	“ENDOCYTOSIS/EXOCYTOSIS C2-
										DOMAINS, C2B-DOMAIN, RABPHILIN,
										ENDOCYTOSIS/EXOCYTOSIS”
332	1a06		1	213	3.20E−62	−0.02	0.84		CALCIUM/CALMODULIN-	“KINASE KINASE, SIGNAL
									DEPENDENT PROTEIN	TRANSDUCTION,
									KINASE; CHAIN: NULL;	CALCIUM/CALMODULIN”
332	1apm	E	1	204	3.20E−74	0.22	0.89			“TRANSFERASE(PHOSPHOTRANSFERASE)
										$C-/AMP$-DEPENDENT PROTEIN
										KINASE (E.C.2.7.1.37) ($C/APK$) 1APM 3
										(CATALYTIC SUBUNIT) ““ALPHA””
										ISOENZYME MUTANT WITH SER 139
										1APM 4 REPLACED BY ALA (/S139A$)
										COMPLEX WITH THE PEPTIDE 1APM 5
										INHIBITOR PKI(5-24) AND THE
										DETERGENT MEGA-8 1APM 6”
332	1cmk	E	1	204	1.10E−75	0.16	0.88			PHOSPHOTRANSFERASE CAMP-
										DEPENDENT PROTEIN KINASE
										CATALYTIC SUBUNIT 1CMK 3
										(E.C.2.7.1.37) 1CMK 4
332	1ctp	E	1	204	1.10E−75	0.32	0.94			TRANSFERASE(PHOSPHOTRANSFERASE)
										CAMP-DEPENDENT PROTEIN KINASE
										(E.C.2.7.1.37) (CAPK) 1CTP 3 (CATALYTIC
										SUBUNIT) 1CTP 4
332	1f3m	C	1	213	1.30E−44	−0.17	0.1		“SERINE/THREONINE-	“TRANSFERASE KINASE DOMAIN,
									PROTEIN KINASE PAK-	AUTOINHIBITORY FRAGMENT,
									ALPHA; CHAIN: A, B;	HOMODIMER”
									SERINE/THREONINE-
									PROTEIN KINASE PAK-
									ALPHA; CHAIN: C, D;”
332	1koa		1	192	1.40E−47	0.36	0.98		TWITCHIN; CHAIN: NULL;	“KINASE KINASE, TWITCHIN,
										INTRASTERIC REGULATION”
332	1koa		1	213	1.60E−47	0.13	0.69		TWITCHIN; CHAIN: NULL;	“KINASE KINASE, TWITCHIN,
										INTRASTERIC REGULATION”
332	1kob	A	1	213	1.30E−46	0.13	0.94		“TWITCHIN; CHAIN: A, B;”	“KINASE KINASE, TWITCHIN,
										INTRASTERIC REGULATION”
332	1phk		1	213	1.30E−61	0.21	0.74		PHOSPHORYLASE KINASE;	“KINASE RABBIT MUSCLE
									CHAIN: NULL;	PHOSPHORYLASE KINASE; GLYCOGEN
										METABOLISM, TRANSFERASE,
										SERINE/THREONINE-PROTEIN, 2 KINASE,
										ATP-BINDING, CALMODULIN-BINDING”
332	1tki	A	1	192	1.10E−47	0.12	0.92		“TITIN; CHAIN: A, B;”	“SERINE KINASE SERINE KINASE, TITIN,
										MUSCLE, AUTOINHIBITION”
333	1a06		1	243	3.20E−69	0.14	1		CALCIUM/CALMODULIN-	“KINASE KINASE, SIGNAL
									DEPENDENT PROTEIN	TRANSDUCTION,
									KINASE; CHAIN: NULL;	CALCIUM/CALMODULIN”
333	1apm	E	1	246	1.60E−80	0.19	0.99			“TRANSFERASE(PHOSPHOTRANSFERASE)
										$C-/AMP$-DEPENDENT PROTEIN
										KINASE (E.C.2.7.1.37) ($C/APK$) 1APM 3
										(CATALYTIC SUBUNIT) ““ALPHA””
										ISOENZYME MUTANT WITH SER 139
										1APM 4 REPLACED BY ALA (/S139A$)
										COMPLEX WITH THE PEPTIDE 1APM 5
										INHIBITOR PKI(5-24) AND THE
										DETERGENT MEGA-8 1APM 6”
333	1cmk	E	1	246	8.00E−82	0.28	0.84			PHOSPHOTRANSFERASE CAMP-
										DEPENDENT PROTEIN KINASE
										CATALYTIC SUBUNIT 1CMK 3
										(E.C.2.7.1.37) 1CMK 4
333	1ctp	E	1	246	1.60E−82	0.17	0.92			TRANSFERASE(PHOSPHOTRANSFERASE)
										CAMP-DEPENDENT PROTEIN KINASE
										(E.C.2.7.1.37) (CAPK) 1CTP 3 (CATALYTIC
										SUBUNIT) 1CTP 4
333	1f3m	C	1	218	3.20E−46	0.23	0.57		“SERINE/THREONINE-	“TRANSFERASE KINASE DOMAIN,
									PROTEIN KINASE PAK-	AUTOINHIBITORY FRAGMENT,
									ALPHA; CHAIN: A, B;	HOMODIMER”
									SERINE/THREONINE-
									PROTEIN KINASE PAK-
									ALPHA; CHAIN: C, D;”
333	1koa		1	229	2.80E−54	0.49	1		TWITCHIN; CHAIN: NULL;	“KINASE KINASE, TWITCHIN,
										INTRASTERIC REGULATION”
333	1koa		1	221	3.20E−53	0.25	1		TWITCHIN; CHAIN: NULL;	“KINASE KINASE, TWITCHIN,
										INTRASTERIC REGULATION”
333	1kob	A	1	226	1.60E−51	0.26	1		“TWITCHIN; CHAIN: A, B;”	“KINASE KINASE, TWITCHIN,
										INTRASTERIC REGULATION”
333	1phk		1	220	8.00E−67	0.31	1		PHOSPHORYLASE KINASE;	“KINASE RABBIT MUSCLE
									CHAIN: NULL;	PHOSPHORYLASE KINASE; GLYCOGEN
										METABOLISM, TRANSFERASE,
										SERINE/THREONINE-PROTEIN, 2 KINASE,
										ATP-BINDING, CALMODULIN-BINDING”
333	1tki	A	1	229	9.80E−55	0.3	0.99		“TITIN; CHAIN: A, B;”	“SERINE KINASE SERINE KINASE, TITIN,
										MUSCLE, AUTOINHIBITION”
334	1a06		454	755	8.00E−84	0.17	0.35		CALCIUM/CALMODULIN-	“KINASE KINASE, SIGNAL
									DEPENDENT PROTEIN	TRANSDUCTION,
									KINASE; CHAIN: NULL;	CALCIUM/CALMODULIN”
334	1a06		16	295	1.60E−70	−0.04	0.95		CALCIUM/CALMODULIN-	“KINASE KINASE, SIGNAL
									DEPENDENT PROTEIN	TRANSDUCTION,
									KINASE; CHAIN: NULL;	CALCIUM/CALMODULIN”
334	1a6o		470	731	8.00E−38	0.17	0.51		PROTEIN KINASE	“TRANSFERASE TRANSFERASE,
									CK2/ALPHA-SUBUNIT;	SERINE/THREONINE-PROTEIN KINASE,
									CHAIN: NULL;	CASEIN KINASE, 2 SER/THR KINASE”
334	1a6o		23	271	1.30E−37	0.07	0.6		PROTEIN KINASE	“TRANSFERASE TRANSFERASE,
									CK2/ALPHA-SUBUNIT;	SERINE/THREONINE-PROTEIN KINASE,
									CHAIN: NULL;	CASEIN KINASE, 2 SER/THR KINASE”
334	1adj	A	790	1219	2.80E−57	0.08	1		“HISTIDYL-TRNA	“COMPLEX (TRNA
									SYNTHETASE; CHAIN: A, B,	SYNTHETASE/PEPTIDE) AMINO ACID,
									C, D; HISTIDINE; CHAIN: E,	HISTIDINE, COMPLEX (TRNA
									F, G, H;”	SYNTHETASE/PEPTIDE)”
334	1adj	A	1046	1219	4.80E−11	0.03	0.45		“HISTIDYL-TRNA	“COMPLEX (TRNA
									SYNTHETASE; CHAIN: A, B,	SYNTHETASE/PEPTIDE) AMINO ACID,
									C, D; HISTIDINE; CHAIN: E,	HISTIDINE, COMPLEX (TRNA
									F, G, H;”	SYNTHETASE/PEPTIDE)”
334	1apm	E	470	774	0	0.08	0.64			“TRANSFERASE(PHOSPHOTRANSFERASE)
										$C-/AMP$-DEPENDENT PROTEIN
										KINASE (E.C.2.7.1.37) ($C/APK$) 1APM 3
										(CATALYTIC SUBUNIT) ““ALPHA””
										ISOENZYME MUTANT WITH SER 139
										1APM 4 REPLACED BY ALA (/S139A$)
										COMPLEX WITH THE PEPTIDE 1APM 5
										INHIBITOR PKI(5-24) AND THE
										DETERGENT MEGA-8 1APM 6”
334	1apm	E	16	320	1.30E−97	0.32	0.98			“TRANSFERASE(PHOSPHOTRANSFERASE)
										$C-/AMP$-DEPENDENT PROTEIN
										KINASE (E.C.2.7.1.37) ($C/APK$) 1APM 3
										(CATALYTIC SUBUNIT) ““ALPHA””
										ISOENZYME MUTANT WITH SER 139
										1APM 4 REPLACED BY ALA (/S139A$)
										COMPLEX WITH THE PEPTIDE 1APM 5
										INHIBITOR PKI(5-24) AND THE
										DETERGENT MEGA-8 1APM 6″
334	1aq1		470	741	1.60E−53	−0.02	0.69		CYCLIN-DEPENDENT	“PROTEIN KINASE CDK2; PROTEIN
									PROTEIN KINASE 2; CHAIN:	KINASE, CELL CYCLE,
									NULL;	PHOSPHORYLATION, STAUROSPORINE, 2
										CELL DIVISION, MITOSIS, INHIBITION”
334	1aq1		22	274	3.20E−46	−0.05	0.25		CYCLIN-DEPENPENT	“PROTEIN KINASE CDK2; PROTEIN
									PROTEIN KINASE 2; CHAIN:	KINASE, CELL CYCLE,
									NULL;	PHOSPHORYLATION, STAUROSPORINE, 2
										CELL DIVISION, MITOSIS, INHIBITION”
334	1bi8	A	470	731	4.80E−41	0.1	0.77		“CYCLIN-DEPENDENT	“COMPLEX (KINASE/INHIBITOR) CDK6;
									KINASE 6; CHAIN: A, C;	P19INK4D; CYCLIN DEPENDENT KINASE,
									CYCLIN-DEPENDENT	CYCLIN DEPENDENT KINASE
									KINASE INHIBITOR; CHAIN:	INHIBITORY 2 PROTEIN, CDK, INK4, CELL
									B, D;”	CYCLE, COMPLEX (KINASE/INHIBITOR)
										HEADER HELIX”
334	1bi8	A	23	269	3.20E−38	−0.16	0.9		“CYCLIN-DEPENDENT	“COMPLEX (KINASE/INHIBITOR) CDK6;
									KINASE 6; CHAIN: A, C;	P19INK4D; CYCLIN DEPENDENT KINASE,
									CYCLIN-DEPENDENT	CYCLIN DEPENDENT KINASE
									KINASE INHIBITOR; CHAIN:	INHIBITORY 2 PROTEIN, CDK, INK4, CELL
									B, D;”	CYCLE, COMPLEX (KINASE/INHIBITOR)
										HEADER HELIX”
334	1blx	A	470	732	4.80E−43	0.01	0.99		CYCLIN-DEPENDENT	“COMPLEX (INHIBITOR
									KINASE 6; CHAIN: A;	PROTEIN/KINASE) INHIBITOR PROTEIN,
									P19INK4D; CHAIN: B;	CYCLIN-DEPENDENT KINASE, CELL
										CYCLE 2 CONTROL, ALPHA/BETA,
										COMPLEX (INHIBITOR
										PROTEIN/KINASE)”
334	1blx	A	23	270	1.60E−42	0.18	1		CYCLIN-DEPENDENT	“COMPLEX (INHIBITOR
									KINASE 6; CHAIN: A;	PROTEIN/KINASE) INHIBITOR PROTEIN,
									P19INK4D; CHAIN: B;	CYCLIN-DEPENDENT KINASE, CELL
										CYCLE 2 CONTROL, ALPHA/BETA,
										COMPLEX (INHIBITOR
										PROTEIN/KINASE)”
334	1cm8	A	477	740	1.60E−43	−0.02	0.71		“PHOSPHORYLATED MAP	“TRANSFERASE STRESS-ACTIVATED
									KINASE P38-GAMMA;	PROTEIN KINASE-3, ERK6, ERK5; P38-
									CHAIN: A, B;”	GAMMA, GAMMA, PHOSPHORYLATION,
										MAP KINASE”
334	1cm8	A	50	279	3.20E−36	0.23	0.76		“PHOSPHORYLATED MAP	“TRANSFERASE STRESS-ACTIVATED
									KINASE P38-GAMMA;	PROTEIN KINASE-3, ERK6, ERK5; P38-
									CHAIN: A, B;”	GAMMA, GAMMA, PHOSPHORYLATION,
										MAP KINASE”
334	1cmk	E	470	774	0	0.03	0.78			PHOSPHOTRANSFERASE CAMP-
										DEPENDENT PROTEIN KINASE
										CATALYTIC SUBUNIT 1CMK 3
										(E.C.2.7.1.37) 1CMK 4
334	1cmk	E	14	320	1.30E−99	0.2	1			PHOSPHOTRANSFERASE CAMP-
										DEPENDENT PROTEIN KINASE
										CATALYTIC SUBUNIT 1CMK 3
										(E.C.2.7.1.37) 1CMK 4
334	1ctp	E	470	752	0	0.16	0.94			TRANSFERASE(PHOSPHOTRANSFERASE)
										CAMP-DEPENDENT PROTEIN KINASE
										(E.C.2.7.1.37) (CAPK) 1CTP 3 (CATALYTIC
										SUBUNIT) 1CTP 4
334	1ctp	E	14	309	4.80E−97	0.16	0.98			TRANSFERASE(PHOSPHOTRANSFERASE)
										CAMP-DEPENDENT PROTEIN KINASE
										(E.C.2.7.1.37) (CAPK) 1CTP 3 (CATALYTIC
										SUBUNIT) 1CTP 4
334	1evl	A	1126	1222	0.0008	0.6	0.89		“THREONYL-TRNA	“LIGASE AMINO ACID RECOGNITION,
									SYNTHETASE; CHAIN: A, B,	ZINC ION, TRNA-SYNTHETASE, 2
									C, D;”	ADENYLATE ANALOG, DELETION
										MUTANT”
334	1f3m	C	470	731	6.40E−56	0.36	1		“SERINE/THREONINE-	“TRANSFERASE KINASE DOMAIN,
									PROTEIN KINASE PAK-	AUTOINHIBITORY FRAGMENT,
									ALPHA; CHAIN: A, B;	HOMODIMER”
									SERINE/THREONINE-
									PROTEIN KINASE PAK-
									ALPHA; CHAIN: C, D;”
334	1f3m	C	10	269	1.40E−51	0.06	0.88		“SERINE/THREONINE-	“TRANSFERASE KINASE DOMAIN,
									PROTEIN KINASE PAK-	AUTOINHIBITORY FRAGMENT,
									ALPHA; CHAIN: A, B;	HOMODIMER”
									SERINE/THREONINE-
									PROTEIN KINASE PAK-
									ALPHA; CHAIN: C, D;”
334	1fpu	A	470	736	3.20E−32	0.2	0.04		“PROTO-ONCOGENE	“TRANSFERASE P150, C-ABL; KINASE,
									TYROSINE-PROTEIN	KINASE INHIBITOR, STI-571, ACTIVATION
									KINASE ABL; CHAIN: A, B;”	LOOP”
334	1hcl		470	741	1.60E−55	0.17	0.94		HUMAN CYCLIN-	“PROTEIN KINASE CDK2; TRANSFERASE,
									DEPENDENT KINASE 2;	SERINE/THREONINE PROTEIN KINASE,
									CHAIN: NULL;	ATP-BINDING, 2 CELL CYCLE, CELL
										DIVISION, MITOSIS, PHOSPHORYLATION”
334	1hcl		22	274	3.20E−49	0.1	0.57		HUMAN CYCLIN-	“PROTEIN KINASE CDK2; TRANSFERASE,
									DEPENDENT KINASE 2;	SERINE/THREONINE PROTEIN KINASE,
									CHAIN: NULL;	ATP-BINDING, 2 CELL CYCLE, CELL
										DIVISION, MITOSIS, PHOSPHORYLATION”
334	1htt	A	986	1219	5.60E−30	−0.16	0.78		“HISTIDYL-TRNA	“COMPLEX (TRNA SYNTHETASE/HIS-
									SYNTHETASE; CHAIN: A, B,	ADENYLATE) HISTIDINE-TRNA LIGASE;
									C, D; HISTIDYL-	COMPLEX (TRNA SYNTHETASE/HIS-
									ADENYLATE; CHAIN: E, F,	ADENYLATE), AMINOACYL-TRNA 2
									G, H;”	SYNTHASE, LIGASE, SYNTHETASE”
334	1htt	A	1046	1219	1.60E−14	−0.29	0.29		“HISTIDYL-TRNA	“COMPLEX (TRNA SYNTHETASE/HIS-
									SYNTHETASE; CHAIN: A, B,	ADENYLATE) HISTIDINE-TRNA LIGASE;
									C, D; HISTIDYL-	COMPLEX (TRNA SYNTHETASE/HIS-
									ADENYLATE; CHAIN: E, F,	ADENYLATE), AMINOACYL-TRNA 2
									G, H;”	SYNTHASE, LIGASE, SYNTHETASE”
334	1ian		23	277	1.60E−33	−0.17	0.37		P38 MAP KINASE; CHAIN:	“SERINE/THREONINE-PROTEIN KINASE
									NULL;	CSBP, RK, P38; PROTEIN SER/THR-
										KINASE, SERINE/THREONINE-PROTEIN
										KINASE”
334	1jnk		470	748	1.60E−41	0.17	0.99		C-JUN N-TERMINAL	“TRANSFERASE JNK3; TRANSFERASE,
									KINASE; CHAIN: NULL;	JNK3 MAP KINASE, SERINE/THREONINE
										PROTEIN 2 KINASE”
334	1jnk		22	212	4.80E−33	−0.23	0.03		C-JUN N-TERMINAL	“TRANSFERASE JNK3; TRANSFERASE,
									KINASE; CHAIN: NULL;	JNK3 MAP KINASE, SERINE/THREONINE
										PROTEIN 2 KINASE”
334	1jnk		241	285	4.80E−07	−0.38	0.06		C-JUN N-TERMINAL	“TRANSFERASE JNK3; TRANSFERASE,
									KINASE; CHAIN: NULL;	JNK3 MAP KINASE, SERINE/THREONINE
										PROTEIN 2 KINASE”
334	1kmm	A	779	1219	1.40E−47	−0.03	1		“HISTIDYL-TRNA	“AMINOACYL-TRNA SYNTHASE
									SYNTHETASE; CHAIN: A, B,	HISTIDINE-TRNA LIGASE; AMINOACYL-
									C, D;”	TRNA SYNTHASE, LIGASE,
										SYNTHETASE”
334	1kmm	A	1046	1219	3.20E−15	−0.07	0.17		“HISTIDYL-TRNA	“AMINOACYL-TRNA SYNTHASE
									SYNTHETASE; CHAIN: A, B,	HISTIDINE-TRNA LIGASE; AMINOACYL-
									C, D;”	TRNA SYNTHASE, LIGASE,
										SYNTHETASE”
334	1koa		470	730	1.40E−64	0.07	0.93		TWITCHIN; CHAIN: NULL;	“KINASE KINASE, TWITCHIN,
										INTRASTERIC REGULATION”
334	1koa		22	281	4.80E−57	0.26	1		TWITCHIN; CHAIN: NULL;	“KINASE KINASE, TWITCHIN,
										INTRASTERIC REGULATION”
334	1kob	A	470	734	3.20E−65	0.14	1		“TWITCHIN; CHAIN: A, B;”	“KINASE KINASE, TWITCHIN,
										INTRASTERIC REGULATION”
334	1kob	A	23	270	1.60E−57	0.06	0.68		“TWITCHIN; CHAIN: A, B;”	“KINASE KINASE, TWITCHIN,
										INTRASTERIC REGULATION”
334	1p38		23	277	9.60E−40	0.17	0.99		MAP KINASE P38; CHAIN:	“TRANSFERASE MITOGEN ACTIVATED
									NULL;	PROTEIN KINASE; TRANSFERASE, MAP
										KINASE, SERINE/THREONINE-PROTEIN
										KINASE, 2 P38”
334	1phk		470	733	1.10E−81	0.22	0.99		PHOSPHORYLASE KINASE;	“KINASE RABBIT MUSCLE
									CHAIN: NULL;	PHOSPHORYLASE KINASE; GLYCOGEN
										METABOLISM, TRANSFERASE,
										SERINE/THREONINE-PROTEIN, 2 KINASE,
										ATP-BINDING, CALMODULIN-BINDING”
334	1phk		21	269	3.20E−70	0.3	0.96		PHOSPHORYLASE KINASE;	“KINASE RABBIT MUSCLE
									CHAIN: NULL;	PHOSPHORYLASE KINASE; GLYCOGEN
										METABOLISM, TRANSFERASE,
										SERINE/THREONINE-PROTEIN, 2 KINASE,
										ATP-BINDING, CALMODULIN-BINDING”
334	1pme		474	752	1.60E−43	−0.09	0.23		ERK2; CHAIN: NULL;	“TRANSFERASE MAP KINASE,
										SERINE/THREONINE PROTEIN KINASE,
										TRANSFERASE”
334	1pme		24	277	8.00E−34	0.13	0.82		ERK2; CHAIN: NULL;	“TRANSFERASE MAP KINASE,
										SERINE/THREONINE PROTEIN KINASE,
										TRANSFERASE”
334	1qcf	A	470	724	4.80E−30	0.05	0.65		HAEMATOPOETIC CELL	“TYROSINE KINASE TYROSINE KINASE-
									KINASE (HCK); CHAIN: A;	INHIBITOR COMPLEX, DOWN-
										REGULATED KINASE, 2 ORDERED
										ACTIVATION LOOP”
334	1qe0	A	779	1217	7.00E−25	−0.27	0.66		“HISTIDYL-TRNA	“LIGASE CLASS II TRNA SYNTHETASE,
									SYNTHETASE; CHAIN: A,	BETA SHEET”
									B;”
334	1qe0	B	975	1215	1.40E−22	−0.03	0.92		“HISTIDYL-TRNA	“LIGASE CLASS II TRNA SYNTHETASE,
									SYNTHETASE; CHAIN: A,	BETA SHEET”
									B;”
334	1qe0	A	1043	1217	8.00E−19	−0.23	0.59		“HISTIDYL-TRNA	“LIGASE CLASS II TRNA SYNTHETASE,
									SYNTHETASE; CHAIN: A,	BETA SHEET”
									B;”
334	1qe0	B	1043	1216	1.60E−18	−0.17	0.55		“HISTIDYL-TRNA	“LIGASE CLASS II TRNA SYNTHETASE,
									SYNTHETASE; CHAIN: A,	BETA SHEET”
									B;”
334	1qf6	A	1126	1222	0.0008	0.36	0.87		THREONYL-TRNA	“LIGASE/RNA THRRS; TRNA (THR);
									SYNTHETASE; CHAIN: A;	THREONYL-TRNA SYNTHETASE,
									THREONINE TRNA; CHAIN:	TRNA(THR), AMP, ZINC, MRNA, 2
									B;	AMINOACYLATION, TRANSLATIONAL
										REGULATION, PROTEIN/RNA”
334	1tki	A	470	731	3.20E−52	0.19	0.83		“TITIN; CHAIN: A, B;”	“SERINE KINASE SERINE KINASE, TITIN,
										MUSCLE, AUTOINHIBITION”
334	1tki	A	19	269	6.40E−45	0.24	0.89		“TITIN; CHAIN: A, B;”	“SERINE KINASE SERINE KINASE, TITIN,
										MUSCLE, AUTOINHIBITION”
334	3erk		458	751	1.60E−45	0	0.28		EXTRACELLULAR	“TRANSFERASE MITOGEN ACTIVATED
									REGULATED KINASE 2;	PROTEIN KINASE, MAP 2, ERK2;
									CHAIN: NULL;	TRANSFERASE, SERINE/THREONINE-
										PROTEIN KINASE, MAP KINASE, 2 ERK2”
334	3erk		24	304	1.10E−38	0.33	0.84		EXTRACELLULAR	“TRANSFERASE MITOGEN ACTIVATED
									REGULATED KINASE 2;	PROTEIN KINASE, MAP 2, ERK2;
									CHAIN: NULL;	TRANSFERASE, SERINE/THREONINE-
										PROTEIN KINASE, MAP KINASE, 2 ERK2”
335	1hcl		1291	1558	3.20E−59			124.84	HUMAN CYCLIN-	“PROTEIN KINASE CDK2; TRANSFERASE,
									DEPENDENT KINASE 2;	SERINE/THREONINE PROTEIN KINASE,
									CHAIN: NULL;	ATP-BINDING, 2 CELL CYCLE, CELL
										DIVISION, MITOSIS, PHOSPHORYLATION”
335	1phk		1291	1555	1.40E−77			117.56	PHOSPHORYLASE KINASE;	“KINASE RABBIT MUSCLE
									CHAIN: NULL;	PHOSPHORYLASE KINASE; GLYCOGEN
										METABOLISM, TRANSFERASE,
										SERINE/THREONINE-PROTEIN, 2 KINASE,
										ATP-BINDING, CALMODULIN-BINDING”
336	1btn		92	164	9.80E−07	0.66	0.52		BETA-SPECTRIN; 1BTN 4	SIGNAL TRANSDUCTION PROTEIN
									CHAIN: NULL; 1BTN 5
336	1dcq	A	173	311	7.00E−31	0.19	0.99		PYK2-ASSOCIATED	“METAL BINDING PROTEIN ZINC-
									PROTEIN BETA; CHAIN: A;	BINDING MODULE, ANKYRIN REPEATS,
										METAL BINDING PROTEIN”
336	1fao	A	75	165	1.40E−11	0.41	0.87		DUAL ADAPTOR OF	“SIGNALING PROTEIN DAPP1, PHISH,
									PHOSPHOTYROSINE AND 3-	BAM32; PLECKSTRIN, 3-
									CHAIN: A;	PHOSPHOINOSITIDES, INOSITOL
										TETRAKISPHOSPHATE 2 SIGNAL
										TRANSDUCTION PROTEIN, ADAPTOR
										PROTEIN”
336	1fao	A	1	61	1.40E−11	−0.01	0.17		DUAL ADAPTOR OF	“SIGNALING PROTEIN DAPP1, PHISH,
									PHOSPHOTYROSINE AND 3-	BAM32; PLECKSTRIN, 3-
									CHAIN: A;	PHOSPHOINOSITIDES, INOSITOL
										TETRAKISPHOSPHATE 2 SIGNAL
										TRANSDUCTION PROTEIN, ADAPTOR
										PROTEIN”
336	1fao	A	2	58	1.40E−05	−0.21	0.48		DUAL ADAPTOR OF	“SIGNALING PROTEIN DAPP1, PHISH,
									PHOSPHOTYROSINE AND 3-	BAM32; PLECKSTRIN, 3-
									CHAIN: A;	PHOSPHOINOSITIDES, INOSITOL
										TETRAKISPHOSPHATE 2 SIGNAL
										TRANSDUCTION PROTEIN, ADAPTOR
										PROTEIN”
336	1fb8	A	1	65	2.80E−12	−0.05	0.25		DUAL ADAPTOR OF	“SIGNALING PROTEIN DAPP1, PHISH,
									PHOSPHOTYROSINE AND 3-	BAM32; PLECKSTRIN, 3-
									CHAIN: A;	PHOSPHOINOSITIDES, INOSITOL
										TETRAKISPHOSPHATE 2 SIGNAL
										TRANSDUCTION PROTEIN, ADAPTOR
										PROTEIN”
336	1fb8	A	72	165	2.80E−12	0.45	0.52		DUAL ADAPTOR OF	“SIGNALING PROTEIN DAPP1, PHISH,
									PHOSPHOTYROSINE AND 3-	BAM32; PLECKSTRIN, 3-
									CHAIN: A;	PHOSPHOINOSITIDES, INOSITOL
										TETRAKISPHOSPHATE 2 SIGNAL
										TRANSDUCTION PROTEIN, ADAPTOR
										PROTEIN”
336	1fb8	A	2	58	1.40E−05	0.1	0.57		DUAL ADAPTOR OF	“SIGNALING PROTEIN DAPP1, PHISH,
									PHOSPHOTYROSINE AND 3-	BAM32; PLECKSTRIN, 3-
									CHAIN: A;	PHOSPHOINOSITIDES, INOSITOL
										TETRAKISPHOSPHATE 2 SIGNAL
										TRANSDUCTION PROTEIN, ADAPTOR
										PROTEIN”
336	1pls		1	67	1.40E−08	0.19	0.35			“PHOSPHORYLATION PLECKSTRIN (N-
										TERMINAL PLECKSTRIN HOMOLOGY
										DOMAIN) MUTANT 1PLS 3 WITH LEU GLU
										(HIS)6 ADDED TO THE C TERMINUS 1PLS
										4 (INS(G105-LEHHHHHH)) (NMR, 25
										STRUCTURES) 1PLS 5”
336	1pms		45	166	2.80E−09	0.16	0.12		SOS 1; CHAIN: NULL;	“SIGNAL TRANSDUCTION SON OF
										SEVENLESS; PLECKSTRIN, SON OF
										SEVENLESS, SIGNAL TRANSDUCTION”
336	1qqg	A	2	64	0.00064	−0.29	0.07		“INSULIN RECEPTOR	“SIGNAL TRANSDUCTION IRS-1; BETA-
									SUBSTRATE 1; CHAIN: A,	SANDWHICH, SIGNAL TRANSDUCTION”
									B;”
337	1a06		434	695	1.60E−78	0.24	1		CALCIUM/CALMODULIN-	“KINASE KINASE, SIGNAL
									DEPENDENT PROTEIN	TRANSDUCTION,
									KINASE; CHAIN: NULL;	CALCIUM/CALMODULIN”
337	1a06		426	723	1.60E−78			114.97	CALCIUM/CALMODULIN-	“KINASE KINASE, SIGNAL
									DEPENDENT PROTEIN	TRANSDUCTION,
									KINASE; CHAIN: NULL;	CALCIUM/CALMODULIN”
337	1apm	E	431	725	0	0.81	1			“TRANSFERASE(PHOSPHOTRANSFERASE
										) $C-/AMP$-DEPENDENT PROTEIN
										KINASE (E.C.2.7.1.37) ($C/APK$) 1APM 3
										(CATALYTIC SUBUNIT) ““ALPHA””
										ISOENZYME MUTANT WITH SER 139
										1APM 4 REPLACED BY ALA (/S139A$)
										COMPLEX WITH THE PEPTIDE 1APM 5
										INHIBITOR PKI(5-24) AND THE
										DETERGENT MEGA-8 1APM 6”
337	1apm	E	401	744	0			256.61		“TRANSFERASE(PHOSPHOTRANSFERASE
										) $C-/AMP$-DEPENDENT PROTEIN
										KINASE (E.C.2.7.1.37) ($C/APK$) 1APM 3
										(CATALYTIC SUBUNIT) ““ALPHA””
										ISOENZYME MUTANT WITH SER 139
										1APM 4 REPLACED BY ALA (/S139A$)
										COMPLEX WITH THE PEPTIDE 1APM 5
										INHIBITOR PKI(5-24) AND THE
										DETERGENT MEGA-8 1APM 6”
337	1cmk	E	431	725	0	0.96	1			PHOSPHOTRANSFERASE CAMP-
										DEPENDENT PROTEIN KINASE
										CATALYTIC SUBUNIT 1CMK 3
										(E.C.2.7.1.37) 1CMK 4
337	1cmk	E	392	744	0			261.92		PHOSPHOTRANSFERASE CAMP-
										DEPENDENT PROTEIN KINASE
										CATALYTIC SUBUNIT 1CMK 3
										(E.C.2.7.1.37) 1CMK 4
337	1ctp	E	431	716	0	0.74	1			TRANSFERASE(PHOSPHOTRANSFERASE)
										CAMP-DEPENDENT PROTEIN KINASE
										(E.C.2.7.1.37) (CAPK) 1CTP 3 (CATALYTIC
										SUBUNIT) 1CTP 4
337	1ctp	E	398	735	0			247.17		TRANSFERASE(PHOSPHOTRANSFERASE)
										CAMP-DEPENDENT PROTEIN KINASE
										(E.C.2.7.1.37) (CAPK) 1CTP 3 (CATALYTIC
										SUBUNIT) 1CTP 4
337	1hcl		431	694	1.40E−45	0.64	1		HUMAN CYCLIN-	“PROTEIN KINASE CDK2; TRANSFERASE,
									DEPENDENT KINASE 2;	SERINE/THREONINE PROTEIN KINASE,
									CHAIN: NULL;	ATP-BINDING, 2 CELL CYCLE, CELL
										DIVISION, MITOSIS, PHOSPHORYLATION”
337	1hcl		431	722	1.40E−45			120.53	HUMAN CYCLIN-	“PROTEIN KINASE CDK2; TRANSFERASE,
									DEPENDENT KINASE 2;	SERINE/THREONINE PROTEIN KINASE,
									CHAIN: NULL;	ATP-BINDING, 2 CELL CYCLE, CELL
										DIVISION, MITOSIS, PHOSPHORYLATION”
337	1koa		431	692	4.80E−66	0.52	1		TWITCHIN; CHAIN: NULL;	“KINASE KINASE, TWITCHIN,
										INTRASTERIC REGULATION”
337	1kob	A	432	704	6.40E−67	0.51	1		“TWITCHIN; CHAIN: A, B;”	“KINASE KINASE, TWITCHIN,
										INTRASTERIC REGULATION”
337	1kob	A	404	764	6.40E−67			133.81	“TWITCHIN; CHAIN: A, B;”	“KINASE KINASE, TWITCHIN,
										INTRASTERIC REGULATION”
337	1phk		433	694	2.80E−86	0.58	1		PHOSPHORYLASE KINASE;	“KINASE RABBIT MUSCLE
									CHAIN: NULL;	PHOSPHORYLASE KINASE; GLYCOGEN
										METABOLISM, TRANSFERASE,
										SERINE/THREONINE-PROTEIN, 2 KINASE,
										ATP-BINDING, CALMODULIN-BINDING”
337	1phk		431	695	2.80E−86			113.37	PHOSPHORYLASE KINASE;	“KINASE RABBIT MUSCLE
									CHAIN: NULL;	PHOSPHORYLASE KINASE; GLYCOGEN
										METABOLISM, TRANSFERASE,
										SERINE/THREONINE-PROTEIN, 2 KINASE,
										ATP-BINDING, CALMODULIN-BINDING”
338	1d0s	A	312	602	2.80E−11	0	−0.2		“NICOTINATE	“TRANSFERASE DINUCLEOTIDE-
									MONONUCLEOTIDE: 5, 6-	BINDING MOTIF, PHOSPHORIBOSYL
									CHAIN: A;”	TRANSFERASE”
344	1a5e		287	447	1.50E−21			53.64	TUMOR SUPPRESSOR	“ANTI-ONCOGENE CELL CYCLE, ANTI-
									P16INK4A; CHAIN: NULL;	ONCOGENE, REPEAT, ANK REPEAT”
344	1awc	B	298	451	3.40E−36			63.61	“GA BINDING PROTEIN	“COMPLEX (TRANSCRIPTION
									ALPHA; CHAIN: A; GA	REGULATION/DNA) GABPALPHA;
									BINDING PROTEIN BETA 1;	GABPBETA1; COMPLEX (TRANSCRIPTION
									CHAIN: B; DNA; CHAIN: D,	REGULATION/DNA), DNA-BINDING, 2
									E;”	NUCLEAR PROTEIN, ETS DOMAIN,
										ANKYRIN REPEATS, TRANSCRIPTION 3
										FACTOR”
344	1bd8		298	451	1.70E−28			63.55	P19INK4D CDK4/6	“TUMOR SUPPRESSOR TUMOR
									INHIBITOR; CHAIN: NULL;	SUPPRESSOR, CDK4/6 INHIBITOR,
										ANKYRIN MOTIF”
344	1blx	B	298	451	1.40E−28			59.76	CYCLIN-DEPENDENT	“COMPLEX (INHIBITOR
									KINASE 6; CHAIN: A;	PROTEIN/KINASE) INHIBITOR PROTEIN,
									P19INK4D; CHAIN: B;	CYCLIN-DEPENDENT KINASE, CELL
										CYCLE 2 CONTROL, ALPHA/BETA,
										COMPLEX (INHIBITOR
										PROTEIN/KINASE)”
344	1bu9	A	222	401	1.20E−31			60.09	CYCLIN-DEPENDENT	“HORMONE/GROWTH FACTOR P18-
									KINASE 6 INHIBITOR;	INK4C; CELL CYCLE INHIBITOR,
									CHAIN: A;	P18INK4C, TUMOR, SUPPRESSOR,
										CYCLIN-2 DEPENDENT KINASE,
										HORMONE/GROWTH FACTOR”
344	1ihb	A	299	450	1.20E−31			62.65	“CYCLIN-DEPENDENT	“CELL CYCLE INHIBITOR P18-
									KINASE 6 INHIBITOR;	INK4C(INK6); CELL CYCLE INHIBITOR,
									CHAIN: A, B;”	P18-INK4C(INK6), ANKYRIN REPEAT, 2
										CDK 4/6 INHIBITOR”
344	1ikn	D	193	410	1.70E−39			58.8	NF-KAPPA-B P65 SUBUNIT;	“TRANSCRIPTION FACTOR P65; P50D;
									CHAIN: A; NF-KAPPA-B	TRANSCRIPTION FACTOR, IKB/NFKB
									P50D SUBUNIT; CHAIN: C; I-	COMPLEX”
									KAPPA-B-ALPHA; CHAIN: D;
344	1myo		336	451	1.50E−25			65.72	MYOTROPHIN; CHAIN:	“ANK-REPEAT MYOTROPHIN,
									NULL	ACETYLATION, NMR, ANK-REPEAT”
344	1nfi	E	221	431	5.10E−39			56.51	“NF-KAPPA-B P65; CHAIN:	“COMPLEX (TRANSCRIPTION REG/ANK
									A, C; NF-KAPPA-B P50;	REPEAT) COMPLEX (TRANSCRIPTION
									CHAIN: B, D; I-KAPPA-B-	REGULATION/ANK REPEAT), ANKYRIN 2
									ALPHA; CHAIN: E, F;”	REPEAT HELIX”
344	1sw6	A	142	412	1.40E−17			56.82	“REGULATORY PROTEIN	“TRANSCRIPTION REGULATION
									SW16; CHAIN: A, B;”	TRANSCRIPTION REGULATION,
										ANKYRIN REPEATS, CELL-CYCLE”
345	1awc	B	336	489	3.40E−40			99.08	“GA BINDING PROTEIN	“COMPLEX (TRANSCRIPTION
									ALPHA; CHAIN: A; GA	REGULATION/DNA) GABPALPHA;
									BINDING PROTEIN BETA 1;	GABPBETA1; COMPLEX (TRANSCRIPTION
									CHAIN: B; DNA; CHAIN: D,	REGULATION/DNA), DNA-BINDING, 2
									E;”	NUCLEAR PROTEIN, ETS DOMAIN,
										ANKYRIN REPEATS, TRANSCRIPTION 3
										FACTOR”
345	1bd8		298	458	3.40E−30			86.24	P19INK4D CDK4/6	“TUMOR SUPPRESSOR TUMOR
									INHIBITOR; CHAIN: NULL;	SUPPRESSOR, CDK4/6 INHIBITOR,
										ANKYRIN MOTIF”
345	1blx	B	335	496	3.40E−29			86.17	CYCLIN-DEPENDENT	“COMPLEX (INHIBITOR
									KINASE 6; CHAIN: A;	PROTEIN/KINASE) INHIBITOR PROTEIN,
									P19INK4D; CHAIN: B;	CYCLIN-DEPENDENT KINASE, CELL
										CYCLE 2 CONTROL, ALPHA/BETA,
										COMPLEX (INHIBITOR
										PROTEIN/KINASE)”
345	1bu9	A	332	499	3.40E−36			92.28	CYCLIN-DEPENDENT	“HORMONE/GROWTH FACTOR P18-
									KINASE 6 INHIBITOR;	INK4C; CELL CYCLE INHIBITOR,
									CHAIN: A;	P18INK4C, TUMOR, SUPPRESSOR,
										CYCLIN-2 DEPENDENT KINASE,
										HORMONE/GROWRH FACTOR”
345	1ihb	A	336	492	1.00E−36			96.92	“CYCLIN-DEPENDENT	“CELL CYCLE INHIBITOR P18-
									KINASE 6 INHIBITOR;	INK4C(INK6); CELL CYCLE INHIBITOR,
									CHAIN: A, B;”	P18-INK4C(INK6), ANKYRIN REPEAT, 2
										CDK 4/6 INHIBITOR”
345	1ikn	D	330	543	5.10E−43			85.65	NF-KAPPA-B P65 SUBUNIT;	“TRANSCRIPTION FACTOR P65; P50D;
									CHAIN: A; NF-KAPPA-B	TRANSCRIPTION FACTOR, IKB/NFKB
									P50D SUBUNIT; CHAIN: C; I-	COMPLEX”
									KAPPA-B-ALPHA; CHAIN: D;
345	1nfi	E	329	540	3.40E−43			97.89	“NF-KAPPA-B P65; CHAIN:	“COMPLEX (TRANSCRIPTION REG/ANK
									A, C; NF-KAPPA-B P50;	REPEAT) COMPLEX (TRANSCRIPTION
									CHAIN: B, D; I-KAPPA-B-	REGULATION/ANK REPEAT), ANKYRIN 2
									ALPHA; CHAIN: E, F;”	REPEAT HELIX”
347	1dx5	I	495	619	1.30E−13	0.35	0.45		“THROMBIN LIGHT CHAIN;	“SERINE PROTEINASE COAGULATION
									CHAIN: A, B, C, D;	FACTOR II; COAGULATION FACTOR II;
									THROMBIN HEAVY CHAIN;	FETOMODULIN, TM, CD141 ANTIGEN;
									CHAIN: M, N, O, P;	EGR-CMK SERINE PROTEINASE, EGF-
									THROMBOMODULIN;	LIKE DOMAINS, ANTICOAGULANT
									CHAIN: I, J, K, L; THROMBIN	COMPLEX, 2 ANTIFIBRINOLYTIC
									INHIBITOR L-GLU-L-GLY-L-	COMPLEX”
									ARM; CHAIN: E, F, G, H;”
347	1dx5	I	2067	2170	8.40E−13	0.54	−0.19		“THROMBIN LIGHT CHAIN;	“SERINE PROTEINASE COAGULATION
									CHAIN: A, B, C, D;	FACTOR II; COAGULATION FACTOR II;
									THROMBIN HEAVY CHAIN;	FETOMODULIN, TM, CD141 ANTIGEN;
									CHAIN: M, N, O, P;	EGR-CMK SERINE PROTEINASE, EGF-
									THROMBOMODULIN;	LIKE DOMAINS, ANTICOAGULANT
									CHAIN: I, J, K, L; THROMBIN	COMPLEX, 2 ANTIFIBRINOLYTIC
									INHIBITOR L-GLU-L-GLY-L-	COMPLEX”
									ARM; CHAIN: E, F, G, H;”
347	1dx5	I	1831	1951	2.10E−11	0.07	0.03		“THROMBIN LIGHT CHAIN;	“SERINE PROTEINASE COAGULATION
									CHAIN: A, B, C, D;	FACTOR II; COAGULATION FACTOR II;
									THROMBIN HEAVY CHAIN;	FETOMODULIN, TM, CD141 ANTIGEN;
									CHAIN: M, N, O, P;	EGR-CMK SERINE PROTEINASE, EGF-
									THROMBOMODULIN;	LIKE DOMAINS, ANTICOAGULANT
									CHAIN: I, J, K, L; THROMBIN	COMPLEX, 2 ANTIFIBRINOLYTIC
									INHIBITOR L-GLU-L-GLY-L-	COMPLEX”
									ARM; CHAIN: E, F, G, H;”
347	1ext	A	2054	2169	2.10E−13	0.63	−0.14		“TUMOR NECROSIS	“SIGNALLING PROTEIN BINDING
									FACTOR RECEPTOR;	PROTEIN, CYTOKINE, SIGNALLING
									CHAIN: A, B;”	PROTEIN”
347	1ext	A	1438	1593	2.10E−13	0.2	−0.08		“TUMOR NECROSIS	“SIGNALLING PROTEIN BINDING
									FACTOR RECEPTOR;	PROTEIN, CYTOKINE, SIGNALLING
									CHAIN: A, B;”	PROTEIN”
347	1ext	A	1831	1954	1.90E−12	0.06	−0.06		“TUMOR NECROSIS	“SIGNALLING PROTEIN BINDING
									FACTOR RECEPTOR;	PROTEIN, CYTOKINE, SIGNALLING
									CHAIN: A, B;”	PROTEIN”
347	1klo		1913	2067	4.20E−40	0.66	1		LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
347	1klo		359	542	2.10E−36	0.46	0.8		LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
347	1klo		494	632	6.30E−35	0.52	1		LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
347	1klo		300	471	4.20E−34	0.5	0.29		LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
347	1klo		1457	1627	4.20E−33	0.5	1		LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
347	1klo		429	587	6.30E−33	0.39	1		LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
347	1klo		2023	2145	4.20E−32	1.3	1		LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
347	1klo		541	725	4.20E−32	0.51	0.57		LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
347	1klo		1831	1967	1.70E−31	0.47	0.99		LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
347	1klo		632	826	6.30E−31	0.45	0.99		LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
347	1klo		1922	2060	3.40E−29	0.47	1		LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
347	1klo		1438	1578	8.40E−29	0.96	1		LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
347	1klo		744	867	4.20E−25	0.72	0.98		LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
347	1klo		677	825	3.40E−24	0.66	1		LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
347	1klo		725	867	3.40E−23	0.52	1		LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
347	1klo		1478	1624	6.80E−23	0.72	0.99		LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
347	1klo		587	724	1.70E−21	0.76	1		LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
347	1klo		1814	1966	1.00E−19	0.26	0.01		LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
347	1klo		1344	1484	1.20E−19	−0.45	0.01		LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
347	1klo		1391	1526	5.10E−19	0.05	0.43		LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
347	1klo		293	417	1.10E−16	0.22	0.46		LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
347	1klo		1913	2069	4.20E−40			157.87	LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
347	1pp2	R	1831	1949	1.30E−11	0.04	−0.18			HYDROLASE CALCIUM-FREE
										PHOSPHOLIPASE A = 2 = (E.C.3.1.1.4) 1PP2 4
347	1pp2	R	394	527	2.10E−10	0.22	−0.18			HYDROLASE CALCIUM-FREE
										PHOSPHOLIPASE A = 2 = (E.C.3.1.1.4) 1PP2 4
347	1qfk	L	584	699	2.10E−15	0.35	−0.05		COAGULATION FACTOR	“SERINE PROTEASE FVIIA; FVIIA; BLOOD
									VIIA (LIGHT CHAIN);	COAGULATION, SERINE PROTEASE”
									CHAIN: L; COAGULATION
									FACTOR VIIA (HEAVY
									CHAIN); CHAIN: H;
									TRIPEPTIDYL INHIBITOR;
									CHAIN: C;
347	1qfk	L	1437	1534	1.30E−08	0.05	−0.07		COAGULATION FACTOR	“SERINE PROTEASE FVIIA; FVIIA; BLOOD
									VIIA (LIGHT CHAIN);	COAGULATION, SERINE PROTEASE”
									CHAIN: L; COAGULATION
									FACTOR VIIA (HEAVY
									CHAIN); CHAIN: H;
									TRIPEPTIDYL INHIBITOR;
									CHAIN: C;
347	1qu0	A	3516	3688	1.50E−25	0.76	0.3		“LAMININ ALPHA2 CHAIN;	“METAL BINDING PROTEIN BETA
									CHAIN: A, B, C, D;”	SANDWICH, CALCIUM-BINDING
										PROTEIN, METAL BINDING 2 PROTEIN”
347	1qu0	A	3338	3496	2.10E−15	0.85	0.77		“LAMININ ALPHA2 CHAIN;	“METAL BINDING PROTEIN BETA
									CHAIN: A, B, C, D;”	SANDWICH, CALCIUM-BINDING
										PROTEIN, METAL BINDING 2 PROTEIN”
347	1qu0	A	3124	3281	1.50E−08	0.8	0.99		“LAMININ ALPHA2 CHAIN;	“METAL BINDING PROTEIN BETA
									CHAIN: A, B, C, D;”	SANDWICH, CALCIUM-BINDING
										PROTEIN, METAL BINDING 2 PROTEIN”
347	1quu	A	2204	2457	1.30E−09	0.12	−0.03		HUMAN SKELETAL	“CONTRACTILE PROTEIN TRIPLE-HELIX
									MUSCLE ALPHA-ACTININ 2;	COILED COIL, CONTRACTILE PROTEIN”
									CHAIN: A;
347	1skz		1966	2074	1.30E−20	0.23	−0.09		ANTISTASIN; CHAIN: NULL;	“SERINE PROTEASE INHIBITOR FACTOR
										XA INHIBITOR; ANTISTASIN, CRYSTAL
										STRUCTURE, FACTOR XA INHIBITOR, 2
										SERINE PROTEASE INHIBITOR,
										THROMBOSIS”
347	1skz		2066	2168	4.20E−19	0.61	0.19		ANTISTASIN; CHAIN: NULL;	“SERINE PROTEASE INHIBITOR FACTOR
										XA INHIBITOR; ANTISTASIN, CRYSTAL
										STRUCTURE, FACTOR XA INHIBITOR, 2
										SERINE PROTEASE INHIBITOR,
										THROMBOSIS”
347	1skz		426	543	1.30E−14	−0.04	0.11		ANTISTASIN; CHAIN: NULL;	“SERINE PROTEASE INHIBITOR FACTOR
										XA INHIBITOR; ANTISTASIN, CRYSTAL
										STRUCTURE, FACTOR XA INHIBITOR, 2
										SERINE PROTEASE INHIBITOR,
										THROMBOSIS”
347	1skz		772	872	2.10E−14	0	−0.03		ANTISTASIN; CHAIN: NULL;	“SERINE PROTEASE INHIBITOR FACTOR
										XA INHIBITOR; ANTISTASIN, CRYSTAL
										STRUCTURE, FACTOR XA INHIBITOR, 2
										SERINE PROTEASE INHIBITOR,
										THROMBOSIS”
347	1skz		1481	1591	6.30E−14	0.33	0.53		ANTISTASIN; CHAIN: NULL;	“SERINE PROTEASE INHIBITOR FACTOR
										XA INHIBITOR; ANTISTASIN, CRYSTAL
										STRUCTURE, FACTOR XA INHIBITOR, 2
										SERINE PROTEASE INHIBITOR,
										THROMBOSIS”
347	1tle		357	429	1.30E−14	0.41	−0.11		LAMININ; CHAIN: NULL;	“GLYCOPROTEIN LAMININ-TYPE EGF-
										LIKE; GLYCOPROTEIN, EXTRACELLULAR
										MATRIX PROTEIN, NIDOGEN BINDING, 2
										LE-MODULE”
347	1tle		1575	1628	1.30E−12	0.03	0.89		LAMININ; CHAIN: NULL;	“GLYCOPROTEIN LAMININ-TYPE EGF-
										LIKE; GLYCOPROTEIN, EXTRACELLULAR
										MATRIX PROTEIN, NIDOGEN BINDING, 2
										LE-MODULE”
347	1tpg		603	711	1.90E−21	0.44	−0.15		T-PLASMINOGEN	PLASMINOGEN ACTIVATION
									ACTIVATOR F1-G; 1TPG 7
									CHAIN: NULL; 1TPG 8
347	1tpg		2037	2145	2.10E−21	0.54	0.09		T-PLASMINOGEN	PLASMINOGEN ACTIVATION
									ACTIVATOR F1-G; 1TPG 7
									CHAIN: NULL; 1TPG 8
347	1tpg		525	619	2.10E−20	0.49	−0.13		T-PLASMINOGEN	PLASMINOGEN ACTIVATION
									ACTIVATOR F1-G; 1TPG 7
									CHAIN: NULL; 1TPG 8
347	1tpg		757	864	6.30E−15	0.29	0.3		T-PLASMINOGEN	PLASMINOGEN ACTIVATION
									ACTIVATOR F1-G; 1TPG 7
									CHAIN: NULL; 1TPG 8
347	9wga	A	2085	2249	6.80E−14	0.04	−0.2			LECTIN (AGGLUTININ) WHEAT GERM
										AGGLUTININ (ISOLECTIN 2) 9WGA 3
347	9wga	A	45	179	1.40E−12	0.04	−0.19			LECTIN (AGGLUTININ) WHEAT GERM
										AGGLUTININ (ISOLECTIN 2) 9WGA 3
347	9wga	A	343	492	1.70E−11	0.11	−0.17			LECTIN (AGGLUTININ) WHEAT GERM
										AGGLUTININ (ISOLECTIN 2) 9WGA 3
347	9wga	A	3062	3225	1.40E−10	0.08	−0.19			LECTIN (AGGLUTININ) WHEAT GERM
										AGGLUTININ (ISOLECTIN 2) 9WGA 3
349	1a06		4	268	5.10E−86			106.26	CALCIUM/CALMODULIN-	“KINASE KINASE, SIGNAL
									DEPENDENT PROTEIN	TRANSDUCTION,
									KINASE; CHAIN: NULL;	CALCIUM/CALMODULIN”
349	1a6o		1	268	6.80E−45			61.59	PROTEIN KINASE	“TRANSFERASE TRANSFERASE,
									CK2/ALPHA-SUBUNIT;	SERINE/THREONINE-PROTEIN KINASE,
									CHAIN: NULL;	CASEIN KINASE, 2 SER/THR KINASE”
349	1apm	E	1	268	1.70E−96			87.78		“TRANSFERASE(PHOSPHOTRANSFERASE)
										$C-/AMP$-DEPENDENT PROTEIN
										KINASE (E.C.2.7.1.37) ($C/APK$) 1APM 3
										(CATALYTIC SUBUNIT) ““ALPHA””
										ISOENZYME MUTANT WITH SER 139
										1APM 4 REPLACED BY ALA (/S139A$)
										COMPLEX WITH THE PEPTIDE 1APM 5
										INHIBITOR PKI(5-24) AND THE
										DETERGENT MEGA-8 1APM 6”
349	1aq1		7	268	6.80E−58			76.79	CYCLIN-DEPENDENT	“PROTEIN KINASE CDK2; PROTEIN
									PROTEIN KINASE 2; CHAIN:	KINASE, CELL CYCLE,
									NULL;	PHOSPHORYLATION, STAUROSPORINE, 2
										CELL DIVISION, MITOSIS, INHIBITION”
349	1bi8	A	8	266	4.20E−45			67.07	“CYCLIN-DEPENDENT	“COMPLEX (KINASE/INHIBITOR) CDK6;
									KINASE 6; CHAIN: A, C;	P19INK4D; CYCLIN DEPENDENT KINASE,
									CYCLIN-DEPENDENT	CYCLIN DEPENDENT KINASE
									KINASE INHIBITOR; CHAIN:	INHIBITORY 2 PROTEIN, CDK, INK4, CELL
									B, D;”	CYCLE, COMPLEX (KINASE/INHIBITOR)
										HEADER HELIX”
349	1blx	A	3	268	6.80E−49			74.28	CYCLIN-DEPENDENT	“COMPLEX (INHIBITOR
									KINASE 6; CHAIN: A;	PROTEIN/KINASE) INHIBITOR PROTEIN,
									P19INK4D; CHAIN: B;	CYCLIN-DEPENDENT KINASE, CELL
										CYCLE 2 CONTROL, ALPHA/BETA,
										COMPLEX (INHIBITOR
										PROTEIN/KINASE)”
349	1byg	A	5	264	5.10E−35			75.19	C-TERMINAL SRC KINASE;	“TRANSFERASE CSK; PROTEIN KINASE,
									CHAIN: A;	C-TERMINAL SRC KINASE,
										PHOSPHORYLATION, 2 STAUROSPORINE,
										TRANSFERASE”
349	1cki	A	2	268	1.70E−23			64.03	“CASEIN KINASE I DELTA;	PHOSPHOTRANSFERASE PROTEIN
									1CKI 6 CHAIN: A, B; 1CKI 7”	KINASE 1CKI 18
349	1cmk	E	1	268	1.70E−97			83.18		PHOSPHOTRANSFERASE CAMP-
										DEPENDENT PROTEIN KINASE
										CATALYTIC SUBUNIT 1CMK 3
										(E.C.2.7.1.37) 1CMK 4
349	1csn		5	267	1.40E−52			56.94	CASEIN KINASE-1; 1CSN 4	PHOSPHOTRANSFERASE
349	1ctp	E	1	268	1.70E−97			91.57		TRANSFERASE(PHOSPHOTRANSFERASE)
										CAMP-DEPENDENT PROTEIN KINASE
										(E.C.2.7.1.37) (CAPK) 1CTP 3 (CATALYTIC
										SUBUNIT) 1CTP 4
349	1fgk	B	2	268	1.50E−41			85.3	“FGF RECEPTOR 1; CHAIN:	“PHOSPHOTRANSFERASE FGFR1K,
									A, B;”	FIBROBLAST GROWTH FACTOR
										RECEPTOR 1; TRANSFERASE, TYROSINE-
										PROTEIN KINASE, ATP-BINDING, 2
										PHOSPHORYLATION, RECEPTOR,
										PHOSPHOTRANSFERASE”
349	1fgk	A	5	268	6.80E−35			79.66	“FGF RECEPTOR 1; CHAIN:	“PHOSPHOTRANSFERASE FGFR1K,
									A, B;”	FIBROBLAST GROWTH FACTOR
										RECEPTOR 1; TRANSFERASE, TYROSINE-
										PROTEIN KINASE, ATP-BINDING, 2
										PHOSPHORYLATION, RECEPTOR,
										PHOSPHOTRANSFERASE”
349	1hcl		7	268	8.50E−62			100.67	HUMAN CYCLIN-	“PROTEIN KINASE CDK2; TRANSFERASE,
									DEPENDENT KINASE 2;	SERINE/THREONINE PROTEIN KINASE,
									CHAIN: NULL;	ATP-BINDING, 2 CELL CYCLE, CELL
										DIVISION, MITOSIS, PHOSPHORYLATION”
349	1ir3	A	2	268	5.10E−30			76.94	INSULIN RECEPTOR;	“COMPLEX (TRANSFERASE/SUBSTRATE)
									CHAIN: A; PEPTIDE	TYROSINE KINASE, SIGNAL
									SUBSTRATE; CHAIN: B;	TRANSDUCTION,
										PHOSPHOTRANSFERASE, 2 COMPLEX
										(KINASE/PEPTIDE SUBSTRATE/ATP
										ANALOG), ENZYME, 3 COMPLEX
										(TRANSFERASE/SUBSTRATE)”
349	1jnk		2	267	1.70E−46			61.32	C-JUN N-TERMINAL	“TRANSFERASE JNK3; TRANSFERASE,
									KINASE; CHAIN: NULL;	JNK3 MAP KINASE, SERINE/THREONINE
										PROTEIN 2 KINASE”
349	1kob	A	1	268	1.70E−76			72.77	“TWITCHIN; CHAIN: A, B;”	“KINASE KINASE, TWITCHIN,
										INTRASTERIC REGULATION”
349	1p38		4	268	7.00E−52			61.55	MAP KINASE P38; CHAIN:	“TRANSFERASE MITOGEN ACTIVATED
									NULL;	PROTEIN KINASE; TRANSFERASE, MAP
										KINASE, SERINE/THREONINE-PROTEIN
										KINASE, 2 P38”
349	1phk		6	268	1.70E−84			135.19	PHOSPHORYLASE KINASE;	“KINASE RABBIT MUSCLE
									CHAIN: NULL;	PHOSPHORYLASE KINASE; GLYCOGEN
										METABOLISM, TRANSFERASE,
										SERINE/THREONINE-PROTEIN, 2 KINASE,
										ATP-BINDING, CALMODULIN-BINDING”
349	1pme		9	268	1.00E−48			74.13	ERK2; CHAIN: NULL;	“TRANSFERASE MAP KINASE,
										SERINE/THREONINE PROTEIN KINASE,
										TRANSFERASE”
349	1tki	A	6	268	3.40E−60			79.78	“TITIN; CHAIN: A, B;”	“SERINE KINASE SERINE KINASE, TITIN,
										MUSCLE, AUTOINHIBITION”
349	3erk		2	268	1.40E−58			69.09	EXTRACELLULAR	“TRANSFERASE MITOGEN ACTIVATED
									REGULATED KINASE 2;	PROTEIN KINASE, MAP 2, ERK2;
									CHAIN: NULL;	TRANSFERASE, SERINE/THREONINE-
										PROTEIN KINASE, MAP KINASE, 2 ERK2”
353	1got	B	24	330	5.10E−39			90.99	GT-ALPHA/GI-ALPHA	“COMPLEX (GTP-BINDING/TRANSDUCER)
									CHIMERA; CHAIN: A; GT-	BETA1, TRANSDUCIN BETA SUBUNIT;
									BETA; CHAIN: B; GT-	GAMMA1, TRANSDUCIN GAMMA
									GAMMA; CHAIN: G;	SUBUNIT; COMPLEX (GTP-
										BINDING/TRANSDUCER), G PROTEIN,
										HETEROTRIMER 2 SIGNAL
										TRANSDUCTION”
358	1dqv	A	297	571	4.20E−98	0.84	1		SYNAPTOTAGMIN III;	“ENDOCYTOSIS/EXOCYTOSIS BETA
									CHAIN: A;	SANDWICH, CALCIUM ION, C2 DOMAIN”
358	1dqv	A	299	570	6.80E−69	0.8	1		SYNAPTOTAGMIN III;	“ENDOCYTOSIS/EXOCYTOSIS BETA
									CHAIN: A;	SANDWICH, CALCIUM ION, C2 DOMAIN”
358	1rsy		290	422	1.10E−38	0.56	1			CALCIUM/PHOSPHOLIPID BINDING
										PROTEIN SYNAPTOTAGMIN I (FIRST C2
										DOMAIN) (CALB) 1RSY 3
358	1rsy		290	425	1.10E−38			122.85		CALCIUM/PHOSPHOLIPID BINDING
										PROTEIN SYNAPTOTAGMIN I (FIRST C2
										DOMAIN) (CALB) 1RSY 3
359	1a06		370	689	6.80E−80			117.24	CALCIUM/CALMODULIN-	“KINASE KINASE, SIGNAL
									DEPENDENT PROTEIN	TRANSDUCTION,
									KINASE; CHAIN: NULL;	CALCIUM/CALMODULIN”
359	1apm	E	352	703	0			256.47		“TRANSFERASE(PHOSPHOTRANSFERASE)
										$C-/AMP$-DEPENDENT PROTEIN
										KINASE (E.C.2.7.1.37) ($C/APK$) 1APM 3
										(CATALYTIC SUBUNIT) ““ALPHA””
										ISOENZYME MUTANT WITH SER 139
										1APM 4 REPLACED BY ALA (/S139A$)
										COMPLEX WITH THE PEPTIDE 1APM 5
										INHIBITOR PKI(5-24) AND THE
										DETERGENT MEGA-8 1APM 6”
359	1blx	A	371	677	2.80E−55			134.02	CYCLIN-DEPENDENT	“COMPLEX (INHIBITOR
									KINASE 6; CHAIN: A;	PROTEIN/KINASE) INHIBITOR PROTEIN,
									P19INK4D; CHAIN: B;	CYCLIN-DEPENDENT KINASE, CELL
										CYCLE 2 CONTROL, ALPHA/BETA,
										COMPLEX (INHIBITOR
										PROTEIN/KINASE)”
359	1cmk	E	342	703	0			257.02		PHOSPHOTRANSFERASE CAMP-
										DEPENDENT PROTEIN KINASE
										CATALYTIC SUBUNIT 1CMK 3
										(E.C.2.7.1.37) 1CMK 4
359	1ctp	E	348	690	0			247.27		TRANSFERASE(PHOSPHOTRANSFERASE)
										CAMP-DEPENDENT PROTEIN KINASE
										(E.C.2.7.1.37) (CAPK) 1CTP 3 (CATALYTIC
										SUBUNIT) 1CTP 4
359	1hcl		376	673	1.40E−51			120.13	HUMAN CYCLIN-	“PROTEIN KINASE CDK2; TRANSFERASE,
									DEPENDENT KINASE 2;	SERINE/THREONINE PROTEIN KINASE,
									CHAIN: NULL;	ATP-BINDING, 2 CELL CYCLE, CELL
										DIVISION, MITOSIS, PHOSPHORYLATION”
359	1kob	A	349	727	8.50E−64			129.51	“TWITCHIN; CHAIN: A, B;”	“KINASE KINASE, TWITCHIN,
										INTRASTERIC REGULATION”
359	1phk		377	655	3.40E−73			129.95	PHOSPHORYLASE KINASE;	“KINASE RABBIT MUSCLE
									CHAIN: NULL;	PHOSPHORYLASE KINASE; GLYCOGEN
										METABOLISM, TRANSFERASE,
										SERINE/THREONINE-PROTEIN, 2 KINASE,
										ATP-BINDING, CALMODULIN-BINDING”
359	3erk		362	730	1.40E−51			123.05	EXTRACELLULAR	“TRANSFERASE MITOGEN ACTIVATED
									REGULATED KINASE 2;	PROTEIN KINASE, MAP 2, ERK2;
									CHAIN: NULL;	TRANSFERASE, SERINE/THREONINE-
										PROTEIN KINASE, MAP KINASE, 2 ERK2”
362	1got	B	1	328	5.10E−79			97.07	GT-ALPHA/GI-ALPHA	“COMPLEX (GTP-BINDING/TRANSDUCER)
									CHIMERA; CHAIN: A; GT-	BETA1, TRANSDUCIN BETA SUBUNIT;
									BETA; CHAIN: B; GT-	GAMMA1, TRANSDUCIN GAMMA
									GAMMA; CHAIN: G;	SUBUNIT; COMPLEX (GTP-
										BINDING/TRANSDUCER), G PROTEIN,
										HETEROTRIMER 2 SIGNAL
										TRANSDUCTION”
366	1aox	A	607	812	1.50E−44	0.54	1		“INTEGRIN ALPHA 2 BETA;	“INTEGRIN INTEGRIN, CELL ADHESION,
									CHAIN: A, B;”	GLYCOPROTEIN”
366	1atz	A	614	794	1.50E−25	0.43	1		“VON WILLEBRAND	“COLLAGEN-BINDING COLLAGEN-
									FACTOR; CHAIN: A, B;”	BINDING, HEMOSTASIS, DINUCLEOTIDE
										BINDING FOLD”
366	1atz	A	612	776	5.10E−20	0.21	1		“VON WILLEBRAND	“COLLAGEN-BINDING COLLAGEN-
									FACTOR; CHAIN: A, B;”	BINDING, HEMOSTASIS, DINUCLEOTIDE
										BINDING FOLD”
366	1atz	A	44	210	2.10E−07	0.59	0.9		“VON WILLEBRAND	“COLLAGEN-BINDING COLLAGEN-
									FACTOR; CHAIN: A, B;”	BINDING, HEMOSTASIS, DINUCLEOTIDE
										BINDING FOLD”
366	1auq		603	820	3.40E−65	0.44	0.96		A1 DOMAIN OF VON	“WILLEBRAND WILLEBRAND, BLOOD
									WILLEBRAND FACTOR;	COAGULATION, PLATELET,
									CHAIN: NULL;	GLYCOPROTEIN”
366	1auq		37	228	1.50E−06	0.28	0.86		A1 DOMAIN OF VON	“WILLEBRAND WILLEBRAND, BLOOD
									WILLEBRAND FACTOR;	COAGULATION, PLATELET,
									CHAIN: NULL;	GLYCOPROTEIN”
366	1ck4	A	614	807	6.80E−47	0.6	1		“INTEGRIN ALPHA-1;	“STRUCTURAL PROTEIN I-DOMAIN,
									CHAIN: A, B;”	METAL BINDING, COLLAGEN,
										ADHESION”
366	1ck4	A	44	243	1.70E−11	0.62	1		“INTEGRIN ALPHA-1;	“STRUCTURAL PROTEIN I-DOMAIN,
									CHAIN: A, B;”	METAL BINDING, COLLAGEN,
										ADHESION”
366	1fns	A	611	817	1.00E−62	0.3	1		IMMUNOGLOBULIN NMC-4	“IMMUNE SYSTEM VON WILLEBRAND
									IGG1; CHAIN: L;	FACTOR, GLYCOPROTEIN IBA (A: ALPHA)
									IMMUNOGLOBULIN NMC-4	BINDING, 2 COMPLEX
									IGG1; CHAIN: H; VON	(WILLEBRAND/IMMUNOGLOBULIN),
									WILLEBRAND FACTOR;	BLOOD COAGULATION TYPE 3 2B VON
									CHAIN: A;	WILLEBRAND DISEASE”
366	1ido		615	804	3.40E−49	0.3	1		INTEGRIN; CHAIN: NULL;	“CELL ADHESION PROTEIN A-DOMAIN
										INTEGRIN, CELL ADHESION PROTEIN,
										GLYCOPROTEIN, EXTRACELLULAR 2
										MATRIX, CYTOSKELETON”
366	1kap	P	313	549	4.20E−12	1.16	−0.18		ALKALINE PROTEASE;	ZINC METALLOPROTEASE P.
									1KAP 4 CHAIN: P; 1KAP 5	AERUGINOSA ALKALINE PROTEASE;
									TETRAPEPTIDE (GLY SER	1KAP 6 CALCIUM BINDING PROTEIN
									ASN SER); 1KAP 9 CHAIN: I;	1KAP 19
									1KAP 10
366	1kap	P	256	514	2.10E−11	1.18	−0.19		ALKALINE PROTEASE;	ZINC METALLOPROTEASE P.
									1KAP 4 CHAIN: P; 1KAP 5	AERUGINOSA ALKALINE PROTEASE;
									TETRAPEPTIDE (GLY SER	1KAP 6 CALCIUM BINDING PROTEIN
									ASN SER); 1KAP 9 CHAIN: I;	1KAP 19
									1KAP 10
366	1lfa	A	612	809	3.40E−44	0.48	1		“CD11A; 1LFA 5 CHAIN: A,	“CELL ADHESION LFA-1, ALPHA-L\, BETA-
									B; 1LFA 6”	2 INTEGRIN, A-DOMAIN; 1LFA 8”
366	1lfa	A	44	234	2.10E−09	0.51	0.98		“CD11A; 1LFA 5 CHAIN: A,	“CELL ADHESION LFA-1, ALPHA-L\, BETA-
									B; 1LFA 6”	2 INTEGRIN, A-DOMAIN; 1LFA 8”
366	1osm	A	256	585	2.10E−29	1.08	−0.2		“OMPK36; CHAIN: A, B, C;”	“OUTER MEMBRANE PROTEIN
										OSMOPORIN; OUTER MEMBRANE
										PROTEIN, NON-SPECIFIC PORIN,
										OSMOPORIN, 2 BETA-BARREL,
										TRANSMEMBRANE”
366	1qc5	A	614	805	1.70E−45	0.75	1		ALPHA1 BETA1 INTEGRIN;	“CELL ADHESION INTEGRIN, CELL
									CHAIN: A; ALPHA1 BETA1	ADHESION”
									INTEGRIN; CHAIN: B;
366	1qc5	A	44	236	1.00E−11	0.56	1		ALPHA1 BETA1 INTEGRIN;	“CELL ADHESION INTEGRIN, CELL
									CHAIN: A; ALPHA1 BETA1	ADHESION”
									INTEGRIN; CHAIN: B;
366	2omf		256	570	2.10E−22	1.2	−0.2		MATRIX PORIN OUTER	“INTEGRAL MEMBRANE PROTEIN PORIN
									MEMBRANE PROTEIN F;	MATRIX PORIN, OMPF PORIN; 2OMF 7
									2OMF 5 CHAIN: NULL;	PORIN, MEMBRANE PROTEIN 2OMF 12”
									2OMF 6
366	2omf		361	588	8.40E−15	1.07	−0.2		MATRIX PORIN OUTER	“INTEGRAL MEMBRANE PROTEIN PORIN
									MEMBRANE PROTEIN F;	MATRIX PORIN, OMPF PORIN; 2OMF 7
									2OMF 5 CHAIN: NULL;	PORIN, MEMBRANE PROTEIN 2OMF 12”
									2OMF 6
368	1faO	A	89	177	2.80E−13	0.22	0.64		DUAL ADAPTOR OF	“SIGNALING PROTEIN DAPP1, PHISH,
									PHOSPHOTYROSINE AND 3-	BAM32; PLECKSTRIN, 3-
									CHAIN: A;	PHOSPHOINOSITIDES, INOSITOL
										TETRAKISPHOSPHATE 2 SIGNAL
										TRANSDUCTION PROTEIN, ADAPTOR
										PROTEIN”
368	1fb8	A	90	177	5.60E−14	0.21	0.8		DUAL ADAPTOR OF	“SIGNALING PROTEIN DAPP1, PHISH,
									PHOSPHOTYROSINE AND 3-	BAM32; PLECKSTRIN, 3-
									CHAIN: A;	PHOSPHOINOSITIDES, INOSITOL
										TETRAKISPHOSPHATE 2 SIGNAL
										TRANSDUCTION PROTEIN, ADAPTOR
										PROTEIN”
368	1pls		89	177	7.00E−11	0.2	0			“PHOSPHORYLATION PLECKSTRIN (N-
										TERMINAL PLECKSTRIN HOMOLOGY
										DOMAIN) MUTANT 1PLS 3 WITH LEU GLU
										(HIS)6 ADDED TO THE C TERMINUS 1PLS
										4 (INS(G105-LEHHHHHH)) (NMR, 25
										STRUCTURES) 1PLS 5”
369	1b8q	A	359	472	1.40E−20	0.43	1		NEURONAL NITRIC OXIDE	“OXIDOREDUCTASE PDZ DOMAIN, NNOS,
									SYNTHASE; CHAIN: A;	NITRIC OXIDE SYNTHASE”
									HEPTAPEPTIDE; CHAIN: B;
369	1b8q	A	252	345	5.60E−17	0.16	0.64		NEURONAL NITRIC OXIDE	“OXIDOREDUCTASE PDZ DOMAIN, NNOS,
									SYNTHASE; CHAIN: A;	NITRIC OXIDE SYNTHASE”
									HEPTAPEPTIDE; CHAIN: B;
369	1b8q	A	459	562	8.40E−17	0.35	0.77		NEURONAL NITRIC OXIDE	“OXIDOREDUCTASE PDZ DOMAIN, NNOS,
									SYNTHASE; CHAIN: A;	NITRIC OXIDE SYNTHASE”
									HEPTAPEPTIDE; CHAIN: B;
369	1b8q	A	41	125	4.20E−15	0.23	0.31		NEURONAL NITRIC OXIDE	“OXIDOREDUCTASE PDZ DOMAIN, NNOS,
									SYNTHASE; CHAIN: A;	NITRIC OXIDE SYNTHASE”
									HEPTAPEPTIDE; CHAIN: B;
369	1b8q	A	31	155	3.40E−12	0.18	0.12		NEURONAL NITRIC OXIDE	“OXIDOREDUCTASE PDZ DOMAIN, NNOS,
									SYNTHASE; CHAIN: A;	NITRIC OXIDE SYNTHASE”
									HEPTAPEPTIDE; CHAIN: B;
369	1b8q	A	774	887	5.60E−10	0.11	−0.11		NEURONAL NITRIC OXIDE	“OXIDOREDUCTASE PDZ DOMAIN, NNOS,
									SYNTHASE; CHAIN: A;	NITRIC OXIDE SYNTHASE”
									HEPTAPEPTIDE; CHAIN: B;
369	1be9	A	35	118	6.80E−16	0.48	1		PSD-95; CHAIN: A; CRIPT;	“PEPTIDE RECOGNITION PEPTIDE
									CHAIN: B;	RECOGNITION, PROTEIN
										LOCALIZATION”
369	1be9	A	266	362	3.40E−15	0.06	0.58		PSD-95; CHAIN: A; CRIPT;	“PEPTIDE RECOGNITION PEPTIDE
									CHAIN: B;	RECOGNITION, PROTEIN
										LOCALIZATION”
369	1be9	A	774	874	1.40E−09	0.31	0.16		PSD-95; CHAIN: A; CRIPT;	“PEPTIDE RECOGNITION PEPTIDE
									CHAIN: B;	RECOGNITION, PROTEIN
										LOCALIZATION”
369	1be9	A	453	558	1.70E−09	0.83	1		PSD-95; CHAIN: A; CRIPT;	“PEPTIDE RECOGNITION PEPTIDE
									CHAIN: B;	RECOGNITION, PROTEIN
										LOCALIZATION”
369	1i16		459	551	1.40E−17	0.55	0.15		INTERLEUKIN 16; CHAIN:	“CYTOKINE LCF; CYTOKINE,
									NULL;	LYMPHOCYTE CHEMOATTRACTANT
										FACTOR, PDZ DOMAIN”
369	1i16		259	358	1.40E−14	0.1	−0.14		INTERLEUKIN 16; CHAIN:	“CYTOKINE LCF; CYTOKINE,
									NULL;	LYMPHOCYTE CHEMOATTRACTANT
										FACTOR, PDZ DOMAIN”
369	1i16		362	444	2.80E−13	0.36	0.77		INTERLEUKIN 16; CHAIN:	“CYTOKINE LCF; CYTOKINE,
									NULL;	LYMPHOCYTE CHEMOATTRACTANT
										FACTOR, PDZ DOMAIN”
369	1i16		266	333	1.70E−09	−0.04	0		INTERLEUKIN 16; CHAIN:	“CYTOKINE LCF; CYTOKINE,
									NULL;	LYMPHOCYTE CHEMOATTRACTANT
										FACTOR, PDZ DOMAIN”
369	1i16		778	859	1.10E−08	0.32	−0.02		INTERLEUKIN 16; CHAIN:	“CYTOKINE LCF; CYTOKINE,
									NULL;	LYMPHOCYTE CHEMOATTRACTANT
										FACTOR, PDZ DOMAIN”
369	1kwa	A	461	545	2.80E−18	0.88	1		“HCASK/LIN-2 PROTEIN;	“KINASE HCASK, GLGF REPEAT, DHR;
									CHAIN: A, B;”	PDZ DOMAIN, NEUREXIN, SYNDECAN,
										RECEPTOR CLUSTERING, KINASE”
369	1kwa	A	260	345	1.40E−15	0.53	0.95		“HCASK/LIN-2 PROTEIN;	“KINASE HCASK, GLGF REPEAT, DHR;
									CHAIN: A, B;”	PDZ DOMAIN, NEUREXIN, SYNDECAN,
										RECEPTOR CLUSTERING, KINASE”
369	1kwa	A	38	122	1.40E−14	0.35	1		“HCASK/LIN-2 PROTEIN;	“KINASE HCASK, GLGF REPEAT, DHR;
									CHAIN: A, B;”	PDZ DOMAIN, NEUREXIN, SYNDECAN,
										RECEPTOR CLUSTERING, KINASE”
369	1kwa	A	362	447	8.40E−14	0.74	0.99		“HCASK/LIN-2 PROTEIN;	“KINASE HCASK, GLGF REPEAT, DHR;
									CHAIN: A, B;”	PDZ DOMAIN, NEUREXIN, SYNDECAN,
										RECEPTOR CLUSTERING, KINASE”
369	1kwa	A	776	859	4.20E−12	0.1	0.37		“HCASK/LIN-2 PROTEIN;	“KINASE HCASK, GLGF REPEAT, DHR;
									CHAIN: A, B;”	PDZ DOMAIN, NEUREXIN, SYNDECAN,
										RECEPTOR CLUSTERING, KINASE”
369	1kwa	A	37	124	5.10E−12	0.2	1		“HCASK/LIN-2 PROTEIN;	“KINASE HCASK, GLGF REPEAT, DHR;
									CHAIN: A, B;”	PDZ DOMAIN, NEUREXIN, SYNDECAN,
										RECEPTOR CLUSTERING, KINASE”
369	1pdr		459	547	2.80E−16	0.72	1		HUMAN DISCS LARGE	“SIGNAL TRANSDUCTION HDLG, DHR3
									PROTEIN; CHAIN: NULL;	DOMAIN; SIGNAL TRANSDUCTION, SH3
										DOMAIN, REPEAT”
369	1pdr		37	123	3.40E−15	0.45	1		HUMAN DISCS LARGE	“SIGNAL TRANSDUCTION HDLG, DHR3
									PROTEIN; CHAIN: NULL;	DOMAIN; SIGNAL TRANSDUCTION, SH3
										DOMAIN, REPEAT”
369	1pdr		266	354	1.00E−13	0.05	0.23		HUMAN DISCS LARGE	“SIGNAL TRANSDUCTION HDLG, DHR3
									PROTEIN; CHAIN: NULL;	DOMAIN; SIGNAL TRANSDUCTION, SH3
										DOMAIN, REPEAT”
369	1pdr		362	453	1.30E−11	0.82	1		HUMAN DISCS LARGE	“SIGNAL TRANSDUCTION HDLG, DHR3
									PROTEIN; CHAIN: NULL;	DOMAIN; SIGNAL TRANSDUCTION, SH3
										DOMAIN, REPEAT”
369	1pdr		777	866	1.70E−09	0.14	0.34		HUMAN DISCS LARGE	“SIGNAL TRANSDUCTION HDLG, DHR3
									PROTEIN; CHAIN: NULL;	DOMAIN; SIGNAL TRANSDUCTION, SH3
										DOMAIN, REPEAT”
369	1qav	A	35	122	3.40E−17	0.58	1		ALPHA-1 SYNTROPHIN	“MEMBRANE
									(RESIDUES 77-171); CHAIN:	PROTEIN/OXIDOREDUCTASE BETA-
									A; NEURONAL NITRIC	FINGER, HETERODIMER”
									OXIDE SYNTHASE
									(RESIDUES 1-130); CHAIN: B;
369	1qav	A	269	346	1.50E−12	0.02	0.84		ALPHA-1 SYNTROPHIN	“MEMBRANE
									(RESIDUES 77-171); CHAIN:	PROTEIN/OXIDOREDUCTASE BETA-
									A; NEURONAL NITRIC	FINGER, HETERODIMER”
									OXIDE SYNTHASE
									(RESIDUES 1-130); CHAIN: B;
369	1qav	A	779	855	5.10E−06	0.21	0.11		ALPHA-1 SYNTROPHIN	“MEMBRANE
									(RESIDUES 77-171); CHAIN:	PROTEIN/OXIDOREDUCTASE BETA-
									A; NEURONAL NITRIC	FINGER, HETERODIMER”
									OXIDE SYNTHASE
									(RESIDUES 1-130); CHAIN: B;
369	1qlc	A	459	545	1.40E−18	1.01	1		POSTSYNAPTIC DENSITY	“PEPTIDE RECOGNITION PSD-95; PDZ
									PROTEIN 95; CHAIN: A;	DOMAIN, NEURONAL NITRIC OXIDE
										SYNTHASE, NMDA RECEPTOR 2
										BINDING”
369	1qlc	A	36	123	5.10E−16	0.66	0.93		POSTSYNAPTIC DENSITY	“PEPTIDE RECOGNITION PSD-95; PDZ
									PROTEIN 95; CHAIN: A;	DOMAIN, NEURONAL NITRIC OXIDE
										SYNTHASE, NMDA RECEPTOR 2
										BINDING”
369	1qlc	A	266	348	3.40E−14	0.35	0.55		POSTSYNAPTIC DENSITY	“PEPTIDE RECOGNITION PSD-95; PDZ
									PROTEIN 95; CHAIN: A;	DOMAIN, NEURONAL NITRIC OXIDE
										SYNTHASE, NMDA RECEPTOR 2
										BINDING”
369	1qlc	A	362	447	1.40E−13	0.36	1		POSTSYNAPTIC DENSITY	“PEPTIDE RECOGNITION PSD-95; PDZ
									PROTEIN 95; CHAIN: A;	DOMAIN, NEURONAL NITRIC OXIDE
										SYNTHASE, NMDA RECEPTOR 2
										BINDING”
369	1qlc	A	774	857	2.80E−10	0.48	0.74		POSTSYNAPTIC DENSITY	“PEPTIDE RECOGNITION PSD-95; PDZ
									PROTEIN 95; CHAIN: A;	DOMAIN, NEURONAL NITRIC OXIDE
										SYNTHASE, NMDA RECEPTOR 2
										BINDING”
369	1qlc	A	466	542	5.10E−07	0.84	1		POSTSYNAPTIC DENSITY	“PEPTIDE RECOGNITION PSD-95; PDZ
									PROTEIN 95; CHAIN: A;	DOMAIN, NEURONAL NITRIC OXIDE
										SYNTHASE, NMDA RECEPTOR 2
										BINDING”
369	3pdz	A	33	118	3.40E−15	0.71	0.87		“TYROSINE PHOSPHATASE	“HYDROLASE PDZ DOMAIN, HUMAN
									(PTP-BAS, TYPE 1); CHAIN:	PHOSPHATASE, HPTP1E, PTP-BAS,
									A;”	SPECIFICITY 2 OF BINDING”
369	3pdz	A	266	341	1.70E−13	0.15	0.54		“TYROSINE PHOSPHATASE	“HYDROLASE PDZ DOMAIN, HUMAN
									(PTP-BAS, TYPE 1); CHAIN:	PHOSPHATASE, HPTP1E, PTP-BAS,
									A;”	SPECIFICITY 2 OF BINDING”
369	3pdz	A	460	545	1.70E−07	0.95	1		“TYROSINE PHOSPHATASE	“HYDROLASE PDZ DOMAIN, HUMAN
									(PTP-BAS, TYPE 1); CHAIN:	PHOSPHATASE, HPTP1E, PTP-BAS,
									A;”	SPECIFICITY 2 OF BINDING”
369	3pdz	A	788	862	3.40E−07	0	0.12		“TYROSINE PHOSPHATASE	“HYDROLASE PDZ DOMAIN, HUMAN
									(PTP-BAS, TYPE 1); CHAIN:	PHOSPHATASE, HPTP1E, PTP-BAS,
									A;”	SPECIFICITY 2 OF BINDING”
370	1a17		1126	1263	9.80E−22	0.42	1		SERINE/THREONINE	“HYDROLASE TETRATRICOPEPTIDE, TRP;
									PROTEIN PHOSPHATASE 5;	HYDROLASE, PHOSPHATASE, PROTEIN-
									CHAIN: NULL;	PROTEIN INTERACTIONS, TPR, 2 SUPER-
										HELIX, X-RAY STRUCTURE”
370	1a5e		934	1063	9.80E−32	0.41	0.99		TUMOR SUPPRESSOR	“ANTI-ONCOGENE CELL CYCLE, ANTI-
									P16INK4A; CHAIN: NULL;	ONCOGENE, REPEAT, ANK REPEAT”
370	1a5e		740	856	3.40E−19	0.61	1		TUMOR SUPPRESSOR	“ANTI-ONCOGENE CELL CYCLE, ANTI-
									P16INK4A; CHAIN: NULL;	ONCOGENE, REPEAT, ANK REPEAT”
370	1awc	B	915	1066	1.40E−44	0.72	1		“GA BINDING PROTEIN	“COMPLEX (TRANSCRIPTION
									ALPHA; CHAIN: A; GA	REGULATION/DNA) GABPALPHA;
									BINDING PROTEIN BETA 1;	GABPBETA1; COMPLEX (TRANSCRIPTION
									CHAIN: B; DNA; CHAIN: D,	REGULATION/DNA), DNA-BINDING, 2
									E;”	NUCLEAR PROTEIN, ETS DOMAIN,
										ANKYRIN REPEATS, TRANSCRIPTION 3
										FACTOR”
370	1awc	B	951	1099	1.40E−42	0.35	1		“GA BINDING PROTEIN	“COMPLEX (TRANSCRIPTION
									ALPHA; CHAIN: A; GA	REGULATION/DNA) GABPALPHA;
									BINDING PROTEIN BETA 1;	GABPBETA1; COMPLEX (TRANSCRIPTION
									CHAIN: B; DNA; CHAIN: D,	REGULATION/DNA), DNA-BINDING, 2
									E;”	NUCLEAR PROTEIN, ETS DOMAIN,
										ANKYRIN REPEATS, TRANSCRIPTION 3
										FACTOR”
370	1awc	B	919	1066	5.10E−40	0.59	1		“GA BINDING PROTEIN	“COMPLEX (TRANSCRIPTION
									ALPHA; CHAIN: A; GA	REGULATION/DNA) GABPALPHA;
									BINDING PROTEIN BETA 1;	GABPBETA1; COMPLEX (TRANSCRIPTION
									CHAIN: B; DNA; CHAIN: D,	REGULATION/DNA), DNA-BINDING, 2
									E;”	NUCLEAR PROTEIN, ETS DOMAIN,
										ANKYRIN REPEATS, TRANSCRIPTION 3
										FACTOR”
370	1awc	B	952	1099	1.70E−38	0.27	1		“GA BINDING PROTEIN	“COMPLEX (TRANSCRIPTION
									ALPHA; CHAIN: A; GA	REGULATION/DNA) GABPALPHA;
									BINDING PROTEIN BETA 1;	GABPBETA1; COMPLEX (TRANSCRIPTION
									CHAIN: B; DNA; CHAIN: D,	REGULATION/DNA), DNA-BINDING, 2
									E;”	NUCLEAR PROTEIN, ETS DOMAIN,
										ANKYRIN REPEATS, TRANSCRIPTION 3
										FACTOR”
370	1awc	B	881	1033	1.70E−37	0.64	1		“GA BINDING PROTEIN	“COMPLEX (TRANSCRIPTION
									ALPHA; CHAIN: A; GA	REGULATION/DNA) GABPALPHA;
									BINDING PROTEIN BETA 1;	GABPBETA1; COMPLEX (TRANSCRIPTION
									CHAIN: B; DNA; CHAIN: D,	REGULATION/DNA), DNA-BINDING, 2
									E;”	NUCLEAR PROTEIN, ETS DOMAIN,
										ANKYRIN REPEATS, TRANSCRIPTION 3
										FACTOR”
370	1awc	B	985	1132	1.70E−37	0.4	1		“GA BINDING PROTEIN	“COMPLEX (TRANSCRIPTION
									ALPHA; CHAIN: A; GA	REGULATION/DNA) GABPALPHA;
									BINDING PROTEIN BETA 1;	GABPBETA1; COMPLEX (TRANSCRIPTION
									CHAIN: B; DNA; CHAIN: D,	REGULATION/DNA), DNA-BINDING, 2
									E;”	NUCLEAR PROTEIN, ETS DOMAIN,
										ANKYRIN REPEATS, TRANSCRIPTION 3
										FACTOR”
370	1awc	B	740	896	3.40E−36	0.59	1		“GA BINDING PROTEIN	“COMPLEX (TRANSCRIPTION
									ALPHA; CHAIN: A; GA	REGULATION/DNA) GABPALPHA;
									BINDING PROTEIN BETA 1;	GABPBETA1; COMPLEX (TRANSCRIPTION
									CHAIN: B; DNA; CHAIN: D,	REGULATION/DNA), DNA-BINDING, 2
									E;”	NUCLEAR PROTEIN, ETS DOMAIN,
										ANKYRIN REPEATS, TRANSCRIPTION 3
										FACTOR”
370	1awc	B	1018	1185	1.40E−32	−0.14	0.18		“GA BINDING PROTEIN	“COMPLEX (TRANSCRIPTION
									ALPHA; CHAIN: A; GA	REGULATION/DNA) GABPALPHA;
									BINDING PROTEIN BETA 1;	GABPBETA1; COMPLEX (TRANSCRIPTION
									CHAIN: B; DNA; CHAIN: D,	REGULATION/DNA), DNA-BINDING, 2
									E;”	NUCLEAR PROTEIN, ETS DOMAIN,
										ANKYRIN REPEATS, TRANSCRIPTION 3
										FACTOR”
370	1awc	B	808	967	1.70E−30	0.53	1		“GA BINDING PROTEIN	“COMPLEX (TRANSCRIPTION
									ALPHA; CHAIN: A; GA	REGULATION/DNA) GABPALPHA;
									BINDING PROTEIN BETA 1;	GABPBETA1; COMPLEX (TRANSCRIPTION
									CHAIN: B; DNA; CHAIN: D,	REGULATION/DNA), DNA-BINDING, 2
									E;”	NUCLEAR PROTEIN, ETS DOMAIN,
										ANKYRIN REPEATS, TRANSCRIPTION 3
										FACTOR”
370	1awc	B	697	823	1.20E−22	−0.11	0.82		“GA BINDING PROTEIN	“COMPLEX (TRANSCRIPTION
									ALPHA; CHAIN: A; GA	REGULATION/DNA) GABPALPHA;
									BINDING PROTEIN BETA 1;	GABPBETA1; COMPLEX (TRANSCRIPTION
									CHAIN: B; DNA; CHAIN: D,	REGULATION/DNA), DNA-BINDING, 2
									E;”	NUCLEAR PROTEIN, ETS DOMAIN,
										ANKYRIN REPEATS, TRANSCRIPTION 3
										FACTOR”
370	1bd8		922	1069	6.80E−32	0.74	1		P19INK4D CDK4/6	“TUMOR SUPPRESSOR TUMOR
									INHIBITOR; CHAIN: NULL;	SUPPRESSOR, CDK4/6 INHIBITOR,
										ANKYRIN MOTIF”
370	1bd8		988	1135	8.50E−31	0.23	0.94		P19INK4D CDK4/6	“TUMOR SUPPRESSOR TUMOR
									INHIBITOR; CHAIN: NULL;	SUPPRESSOR, CDK4/6 INHIBITOR,
										ANKYRIN MOTIF”
370	1bd8		743	900	1.20E−29	0.67	1		P19INK4D CDK4/6	“TUMOR SUPPRESSOR TUMOR
									INHIBITOR; CHAIN: NULL;	SUPPRESSOR, CDK4/6 INHIBITOR,
										ANKYRIN MOTIF”
370	1bd8		636	826	3.40E−20	0.01	0.29		P19INK4D CDK4/6	“TUMOR SUPPRESSOR TUMOR
									INHIBITOR; CHAIN: NULL;	SUPPRESSOR, CDK4/6 INHIBITOR,
										ANKYRIN MOTIF”
370	1bi7	B	740	856	8.50E−20	0.66	1		CYCLIN-DEPENDENT	“COMPLEX (KINASE/ANTI-ONCOGENE)
									KINASE 6; CHAIN: A;	CDK6; P16INK4A, MTS1; CYCLIN
									MULTIPLE TUMOR	DEPENDENT KINASE, CYCLIN
									SUPPRESSOR; CHAIN: B;	DEPENDENT KINASE INHIBITORY 2
										PROTEIN, CDK, INK4, CELL CYCLE,
										MULTIPLE TUMOR SUPPRESSOR, 3 MTS1,
										COMPLEX (KINASE/ANTI-ONCOGENE)
										HEADER”
370	1blx	B	917	1071	1.40E−42	0.67	1		CYCLIN-DEPENDENT	“COMPLEX (INHIBITOR
									KINASE 6; CHAIN: A;	PROTEIN/KINASE) INHIBITOR PROTEIN,
									P19INK4D; CHAIN: B;	CYCLIN-DEPENDENT KINASE, CELL
										CYCLE 2 CONTROL, ALPHA/BETA,
										COMPLEX (INHIBITOR
										PROTEIN/KINASE)”
370	1blx	B	952	1104	1.40E−40	0.51	1		CYCLIN-DEPENDENT	“COMPLEX (INHIBITOR
									KINASE 6; CHAIN: A;	PROTEIN/KINASE) INHIBITOR PROTEIN,
									P19INK4D; CHAIN: B;	CYCLIN-DEPENDENT KINASE, CELL
										CYCLE 2 CONTROL, ALPHA/BETA,
										COMPLEX (INHIBITOR
										PROTEIN/KINASE)”
370	1blx	B	806	1005	8.40E−31	0.05	0.93		CYCLIN-DEPENDENT	“COMPLEX (INHIBITOR
									KINASE 6; CHAIN: A;	PROTEIN/KINASE) INHIBITOR PROTEIN,
									P19INK4D; CHAIN: B;	CYCLIN-DEPENDENT KINASE, CELL
										CYCLE 2 CONTROL, ALPHA/BETA,
										COMPLEX (INHIBITOR
										PROTEIN/KINASE)”
370	1blx	B	743	900	1.70E−30	0.78	1		CYCLIN-DEPENDENT	“COMPLEX (INHIBITOR
									KINASE 6; CHAIN: A;	PROTEIN/KINASE) INHIBITOR PROTEIN,
									P19INK4D; CHAIN: B;	CYCLIN-DEPENDENT KINASE, CELL
										CYCLE 2 CONTROL, ALPHA/BETA,
										COMPLEX (INHIBITOR
										PROTEIN/KINASE)”
370	1blx	B	1323	1437	1.20E−10	0.13	−0.19		CYCLIN-DEPENDENT	“COMPLEX (INHIBITOR
									KINASE 6; CHAIN: A;	PROTEIN/KINASE) INHIBITOR PROTEIN,
									P19INK4D; CHAIN: B;	CYCLIN-DEPENDENT KINASE, CELL
										CYCLE 2 CONTROL, ALPHA/BETA,
										COMPLEX (INHIBITOR
										PROTEIN/KINASE)”
370	1bu9	A	915	1071	2.80E−41	1.03	1		CYCLIN-DEPENDENT	“HORMONE/GROWTH FACTOR P18-
									KINASE 6 INHIBITOR;	INK4C; CELL CYCLE INHIBITOR,
									CHAIN: A;	P18INK4C, TUMOR, SUPPRESSOR,
										CYCLIN-2 DEPENDENT KINASE,
										HORMONE/GROWTH FACTOR”
370	1bu9	A	951	1104	1.30E−36	0.63	1		CYCLIN-DEPENDENT	“HORMONE/GROWTH FACTOR P18-
									KINASE 6 INHIBITOR;	INK4C; CELL CYCLE INHIBITOR,
									CHAIN: A;	P18INK4C, TUMOR, SUPPRESSOR,
										CYCLIN-2 DEPENDENT KINASE,
										HORMONE/GROWTH FACTOR”
370	1bu9	A	919	1071	5.10E−36	0.99	1		CYCLIN-DEPENDENT	“HORMONE/GROWTH FACTOR P18-
									KINASE 6 INHIBITOR;	INK4C; CELL CYCLE INHIBITOR,
									CHAIN: A;	P18INK4C, TUMOR, SUPPRESSOR,
										CYCLIN-2 DEPENDENT KINASE,
										HORMONE/GROWTH FACTOR”
370	1bu9	A	985	1137	3.40E−35	0.07	0.24		CYCLIN-DEPENDENT	“HORMONE/GROWTH FACTOR P18-
									KINASE 6 INHIBITOR;	INK4C; CELL CYCLE INHIBITOR,
									CHAIN: A;	P18INK4C, TUMOR, SUPPRESSOR,
										CYCLIN-2 DEPENDENT KINASE,
										HORMONE/GROWTH FACTOR”
370	1bu9	A	738	901	1.00E−34	0.48	0.8		CYCLIN-DEPENDENT	“HORMONE/GROWTH FACTOR P18-
									KINASE 6 INHIBITOR;	INK4C; CELL CYCLE INHIBITOR,
									CHAIN: A;	P18INK4C, TUMOR, SUPPRESSOR,
										CYCLIN-2 DEPENDENT KINASE,
										HORMONE/GROWTH FACTOR”
370	1d9s	A	938	1071	7.00E−37	0.64	1		CYCLIN-DEPENDENT	“SIGNALING PROTEIN HELIX-TURN-
									KINASE 4 INHIBITOR B;	HELIX, ANKYRIN REPEAT”
									CHAIN: A;
370	1d9s	A	971	1104	5.60E−34	0.48	0.99		CYCLIN-DEPENDENT	“SIGNALING PROTEIN HELIX-TURN-
									KINASE 4 INHIBITOR B;	HELIX, ANKYRIN REPEAT”
									CHAIN: A;
370	1d9s	A	748	857	5.60E−20	0.19	0.8		CYCLIN-DEPENDENT	“SIGNALING PROTEIN HELIX-TURN-
									KINASE 4 INHIBITOR B;	HELIX, ANKYRIN REPEAT”
									CHAIN: A;
370	1d9s	A	740	856	6.80E−20	0.49	1		CYCLIN-DEPENDENT	“SIGNALING PROTEIN HELIX-TURN-
									KINASE 4 INHIBITOR B;	HELIX, ANKYRIN REPEAT”
									CHAIN: A;
370	1elr	A	1127	1255	7.00E−18	0.5	0.96		TPR2A-DOMAIN OF HOP;	“CHAPERONE HOP, TPR-DOMAIN,
									CHAIN: A; HSP90-PEPTIDE	PEPTIDE-COMPLEX, HELICAL REPEAT,
									MEEVD; CHAIN: B;	HSP90, 2 PROTEIN BINDING”
370	1elw	A	1126	1251	2.80E−22	0.52	1		“TPR1-DOMAIN OF HOP;	“CHAPERONE HOP, TPR-DOMAIN,
									CHAIN: A, B; HSC70-	PEPTIDE-COMPLEX, HELICAL REPEAT,
									PEPTIDE; CHAIN: C, D;”	HSC70, 2 HSP70, PROTEIN BINDING”
370	1ihb	A	919	1070	3.40E−35	1.03	1		“CYCLIN-DEPENDENT	“CELL CYCLE INHIBITOR P18-
									KINASE 6 INHIBITOR;	INK4C(INK6); CELL CYCLE INHIBITOR,
									CHAIN: A, B;”	P18-INK4C(INK6), ANKYRIN REPEAT, 2
										CDK 4/6 INHIBITOR”
370	1ihb	A	985	1136	1.40E−34	0.27	0.98		“CYCLIN-DEPENDENT	“CELL CYCLE INHIBITOR P18-
									KINASE 6 INHIBITOR;	TNK4C(INK6); CELL CYCLE INHIBITOR,
									CHAIN: A, B;”	P18-INK4C(INK6), ANKYRIN REPEAT, 2
										CDK 4/6 INHIBITOR”
370	1ihb	A	738	900	3.40E−34	0.81	1		“CYCLIN-DEPENDENT	“CELL CYCLE INHIBITOR P18-
									KINASE 6 INHIBITOR;	INK4C(INK6); CELL CYCLE INHIBITOR,
									CHAIN: A, B;”	P18-INK4C(INK6), ANKYRIN REPEAT, 2
										CDK 4/6 INHIBITOR”
370	1ikn	D	914	1099	3.40E−43	0.24	1		NF-KAPPA-B P65 SUBUNIT;	“TRANSCRIPTION FACTOR P65; P50D;
									CHAIN: A; NF-KAPPA-B	TRANSCRIPTION FACTOR, IKB/NFKB
									P50D SUBUNIT; CHAIN: C; I-	COMPLEX”
									KAPPA-B-ALPHA; CHAIN: D;
370	1ikn	D	770	951	5.10E−40	0.18	0.83		NF-KAPPA-B P65 SUBUNIT;	“TRANSCRIPTION FACTOR P65; P50D;
									CHAIN: A; NF-KAPPA-B	TRANSCRIPTION FACTOR, IKB/NFKB
									P50D SUBUNIT; CHAIN: C; I-	COMPLEX”
									KAPPA-B-ALPHA; CHAIN: D;
370	1ikn	D	876	1050	1.50E−33	0.15	0.95		NF-KAPPA-B P65 SUBUNIT;	“TRANSCRIPTION FACTOR P65; P50D;
									CHAIN: A; NF-KAPPA-B	TRANSCRIPTION FACTOR, IKB/NFKB
									P50D SUBUNIT; CHAIN: C; I-	COMPLEX”
									KAPPA-B-ALPHA; CHAIN: D;
370	1ikn	D	735	907	1.70E−30	0.29	0.54		NF-KAPPA-B P65 SUBUNIT;	“TRANSCRIPTION FACTOR P65; P50D;
									CHAIN: A; NF-KAPPA-B	TRANSCRIPTION FACTOR, IKB/NFKB
									P50D SUBUNIT; CHAIN: C; I-	COMPLEX”
									KAPPA-B-ALPHA; CHAIN: D;
370	1myo		741	858	3.40E−24	0.19	0.9		MYOTROPHIN; CHAIN:	“ANK-REPEAT MYOTROPHIN,
									NULL	ACETYLATION, NMR, ANK-REPEAT”
370	1nfi	E	915	1104	9.80E−51	0.67	1		“NF-KAPPA-B P65; CHAIN:	“COMPLEX (TRANSCRIPTION REG/ANK
									A, C; NF-KAPPA-B P50;	REPEAT) COMPLEX (TRANSCRIPTION
									CHAIN: B, D; I-KAPPA-B-	REGULATION/ANK REPEAT), ANKYRIN 2
									ALPHA; CHAIN: E, F;”	REPEAT HELIX”
370	1nfi	E	914	1099	1.70E−43	0.37	1		“NF-KAPPA-B P65; CHAIN:	“COMPLEX (TRANSCRIPTION REG/ANK
									A, C; NF-KAPPA-B P50;	REPEAT) COMPLEX (TRANSCRIPTION
									CHAIN: B, D; I-KAPPA-B-	REGULATION/ANK REPEAT), ANKYRIN 2
									ALPHA; CHAIN: E, F;”	REPEAT HELIX”
370	1nfi	E	833	1071	4.20E−42	0.34	1		“NF-KAPPA-B P65; CHAIN:	“COMPLEX (TRANSCRIPTION REG/ANK
									A, C; NF-KAPPA-B P50;	REPEAT) COMPLEX (TRANSCRIPTION
									CHAIN: B, D; I-KAPPA-B-	REGULATION/ANK REPEAT), ANKYRIN 2
									ALPHA; CHAIN: E, F;”	REPEAT HELIX”
370	1nfi	E	769	951	1.00E−39	0.46	1		“NF-KAPPA-B P65; CHAIN:	“COMPLEX (TRANSCRIPTION REG/ANK
									A, C; NF-KAPPA-B P50;	REPEAT) COMPLEX (TRANSCRIPTION
									CHAIN: B, D; I-KAPPA-B-	REGULATION/ANK REPEAT), ANKYRIN 2
									ALPHA; CHAIN: E, F;”	REPEAT HELIX”
370	1nfi	E	802	1013	2.80E−38	0.35	1		“NF-KAPPA-B P65; CHAIN:	“COMPLEX (TRANSCRIPTION REG/ANK
									A, C; NF-KAPPA-B P50;	REPEAT) COMPLEX (TRANSCRIPTION
									CHAIN: B, D; I-KAPPA-B-	REGULATION/ANK REPEAT), ANKYRIN 2
									ALPHA; CHAIN: E, F;”	REPEAT HELIX”
370	1nfi	E	876	1050	5.10E−34	0.58	1		“NF-KAPPA-B P65; CHAIN:	“COMPLEX (TRANSCRIPTION REG/ANK
									A, C; NF-KAPPA-B P50;	REPEAT) COMPLEX (TRANSCRIPTION
									CHAIN: B, D; I-KAPPA-B-	REGULATION/ANK REPEAT), ANKYRIN 2
									ALPHA; CHAIN: E, F;”	REPEAT HELIX”
370	1nfi	E	735	907	8.50E−31	0.55	0.96		“NF-KAPPA-B P65; CHAIN:	“COMPLEX (TRANSCRIPTION REG/ANK
									A, C; NF-KAPPA-B P50;	REPEAT) COMPLEX (TRANSCRIPTION
									CHAIN: B, D; I-KAPPA-B-	REGULATION/ANK REPEAT), ANKYRIN 2
									ALPHA; CHAIN: E, F;”	REPEAT HELIX”
370	1nfi	E	978	1126	1.10E−30	0.23	1		“NF-KAPPA-B P65; CHAIN:	“COMPLEX (TRANSCRIPTION REG/ANK
									A, C; NF-KAPPA-B P50;	REPEAT) COMPLEX (TRANSCRIPTION
									CHAIN: B, D; I-KAPPA-B-	REGULATION/ANK REPEAT), ANKYRIN 2
									ALPHA; CHAIN: E, F;”	REPEAT HELIX”
370	1sw6	A	873	1089	2.80E−31	0	0.66		“REGULATORY PROTEIN	“TRANSCRIPTION REGULATION
									SWI6; CHAIN: A, B;”	TRANSCRIPTION REGULATION,
										ANKYRIN REPEATS, CELL-CYCLE”
370	1ycs	B	951	1111	2.80E−35	0.11	0.96		P53; CHAIN: A; 53BP2;	“COMPLEX (ANTI-ONCOGENE/ANKYRIN
									CHAIN: B;	REPEATS) P53BP2; ANKYRIN REPEATS,
										SH3, P53, TUMOR SUPPRESSOR,
										MULTIGENE 2 FAMILY, NUCLEAR
										PROTEIN, PHOSPHORYLATION, DISEASE
										MUTATION, 3 POLYMORPHISM,
										COMPLEX (ANTI-ONCOGENE/ANKYRIN
										REPEATS)”
370	1ycs	B	917	1085	2.80E−34	0.23	0.99		P53; CHAIN: A; 53BP2;	“COMPLEX (ANTI-ONCOGENE/ANKYRIN
									CHAIN: B;	REPEATS) P53BP2; ANKYRIN REPEATS,
										SH3, P53, TUMOR SUPPRESSOR,
										MULTIGENE 2 FAMILY, NUCLEAR
										PROTEIN, PHOSPHORYLATION, DISEASE
										MUTATION, 3 POLYMORPHISM,
										COMPLEX (ANTI-ONCOGENE/ANKYRIN
										REPEATS)”
370	1ycs	B	983	1135	2.80E−32	0.37	1		P53; CHAIN: A; 53BP2;	“COMPLEX (ANTI-ONCOGENE/ANKYRIN
									CHAIN: B;	REPEATS) P53BP2; ANKYRIN REPEATS,
										SH3, P53, TUMOR SUPPRESSOR,
										MULTIGENE 2 FAMILY, NUCLEAR
										PROTEIN, PHOSPHORYLATION, DISEASE
										MUTATION, 3 POLYMORPHISM,
										COMPLEX (ANTI-ONCOGENE/ANKYRIN
										REPEATS)”
370	1ycs	B	1015	1159	2.80E−23	0.12	0.68		P53; CHAIN: A; 53BP2;	“COMPLEX (ANTI-ONCOGENE/ANKYRIN
									CHAIN: B;	REPEATS) P53BP2; ANKYRIN REPEATS,
										SH3, P53, TUMOR SUPPRESSOR,
										MULTIGENE 2 FAMILY, NUCLEAR
										PROTEIN, PHOSPHORYLATION, DISEASE
										MUTATION, 3 POLYMORPHISM,
										COMPLEX (ANTI-ONCOGENE/ANKYRIN
										REPEATS)”
370	1ycs	B	740	832	1.70E−19	0.26	0.81		P53; CHAIN: A; 53BP2;	“COMPLEX (ANTI-ONCOGENE/ANKYRIN
									CHAIN: B;	REPEATS) P53BP2; ANKYRIN REPEATS,
										SH3, P53, TUMOR SUPPRESSOR,
										MULTIGENE 2 FAMILY, NUCLEAR
										PROTEIN, PHOSPHORYLATION, DISEASE
										MUTATION, 3 POLYMORPHISM,
										COMPLEX (ANTI-ONCOGENE/ANKYRIN
										REPEATS)”
372	1a5e		730	857	9.80E−32	0.59	1		TUMOR SUPPRESSOR	“ANTI-ONCOGENE CELL CYCLE, ANTI-
									P16INK4A; CHAIN: NULL;	ONCOGENE, REPEAT, ANK REPEAT”
372	1a5e		684	794	1.40E−16	0.65	0.41		TUMOR SUPPRESSOR	“ANTI-ONCOGENE CELL CYCLE, ANTI-
									P16INK4A; CHAIN: NULL;	ONCOGENE, REPEAT, ANK REPEAT”
372	1awc	B	712	862	2.80E−41	0.82	1		“GA BINDING PROTEIN	“COMPLEX (TRANSCRIPTION
									ALPHA; CHAIN: A; GA	REGULATION/DNA) GABPALPHA;
									BINDING PROTEIN BETA 1;	GABPBETA1; COMPLEX (TRANSCRIPTION
									CHAIN: B; DNA; CHAIN: D,	REGULATION/DNA), DNA-BlNDING, 2
									E;”	NUCLEAR PROTEIN, ETS DOMAIN,
										ANKYRIN REPEATS, TRANSCRIPTION 3
										FACTOR”
372	1awc	B	743	932	8.40E−39	0.38	1		“GA BINDING PROTEIN	“COMPLEX (TRANSCRIPTION
									ALPHA; CHAIN: A; GA	REGULATION/DNA) GABPALPHA;
									BINDING PROTEIN BETA 1;	GABPBETA1; COMPLEX (TRANSCRIPTION
									CHAIN: B; DNA; CHAIN: D,	REGULATION/DNA), DNA-BINDING, 2
									E;”	NUCLEAR PROTEIN, ETS DOMAIN,
										ANKYRIN REPEATS, TRANSCRIPTION 3
										FACTOR”
372	1awc	B	714	862	6.80E−36	0.95	1		“GA BINDING PROTEIN	“COMPLEX (TRANSCRIPTION
									ALPHA; CHAIN: A; GA	REGULATION/DNA) GABPALPHA;
									BINDING PROTEIN BETA 1;	GABPBETA1; COMPLEX (TRANSCRIPTION
									CHAIN: B; DNA; CHAIN: D,	REGULATION/DNA), DNA-BINDING, 2
									E;”	NUCLEAR PROTEIN, ETS DOMAIN,
										ANKYRIN REPEATS, TRANSCRIPTION 3
										FACTOR”
372	1awc	B	748	899	5.10E−35	0.69	1		“GA BINDING PROTEIN	“COMPLEX (TRANSCRIPTION
									ALPHA; CHAIN: A; GA	REGULATION/DNA) GABPALPHA;
									BINDING PROTEIN BETA 1;	GABPBETA1; COMPLEX (TRANSCRIPTION
									CHAIN: B; DNA; CHAIN: D,	REGULATION/DNA), DNA-BINDING, 2
									E;”	NUCLEAR PROTEIN, ETS DOMAIN,
										ANKYRIN REPEATS, TRANSCRIPTION 3
										FACTOR”
372	1awc	B	847	1004	1.70E−31	0.13	0.33		“GA BINDING PROTEIN	“COMPLEX (TRANSCRIPTION
									ALPHA; CHAIN: A; GA	REGULATION/DNA) GABPALPHA;
									BINDING PROTEIN BETA 1;	GABPBETA1; COMPLEX (TRANSCRIPTION
									CHAIN: B; DNA; CHAIN: D,	REGULATION/DNA), DNA-BINDING, 2
									E;”	NUCLEAR PROTEIN, ETS DOMAIN,
										ANKYRIN REPEATS, TRANSCRIPTION 3
										FACTOR”
372	1awc	B	779	963	2.80E−29	0.54	1		“GA BINDING PROTEIN	“COMPLEX (TRANSCRIPTION
									ALPHA; CHAIN: A; GA	REGULATION/DNA) GABPALPHA;
									BINDING PROTEIN BETA 1;	GABPBETA1; COMPLEX (TRANSCRIPTION
									CHAIN: B; DNA; CHAIN: D,	REGULATION/DNA), DNA-BINDING, 2
									E;”	NUCLEAR PROTEIN, ETS DOMAIN,
										ANKYRIN REPEATS, TRANSCRIPTION 3
										FACTOR”
372	1awc	B	1211	1301	1.70E−21	0.29	−0.18		“GA BINDING PROTEIN	“COMPLEX (TRANSCRIPTION
									ALPHA; CHAIN: A; GA	REGULATION/DNA) GABPALPHA;
									BINDING PROTEIN BETA 1;	GABPBETA1; COMPLEX (TRANSCRIPTION
									CHAIN: B; DNA; CHAIN: D,	REGULATION/DNA), DNA-BINDING, 2
									E;”	NUCLEAR PROTEIN, ETS DOMAIN,
										ANKYRIN REPEATS, TRANSCRIPTION 3
										FACTOR”
372	1awc	B	617	763	1.70E−18	0.26	−0.06		“GA BINDING PROTEIN	“COMPLEX (TRANSCRIPTION
									ALPHA; CHAIN: A; GA	REGULATION/DNA) GABPALPHA;
									BINDING PROTEIN BETA 1;	GABPBETA1; COMPLEX (TRANSCRIPTION
									CHAIN: B; DNA; CHAIN: D,	REGULATION/DNA), DNA-BINDING, 2
									E;”	NUCLEAR PROTEIN, ETS DOMAIN,
										ANKYRIN REPEATS, TRANSCRIPTION 3
										FACTOR”
372	1awc	B	1212	1317	1.70E−16	0.17	−0.14		“GA BINDING PROTEIN	“COMPLEX (TRANSCRIPTION
									ALPHA; CHAIN: A; GA	REGULATION/DNA) GABPALPHA;
									BINDING PROTEIN BETA 1;	GABPBETA1; COMPLEX (TRANSCRIPTION
									CHAIN: B; DNA; CHAIN: D,	REGULATION/DNA), DNA-BINDING, 2
									E;”	NUCLEAR PROTEIN, ETS DOMAIN,
										ANKYRIN REPEATS, TRANSCRIPTION 3
										FACTOR”
372	1bd8		751	932	1.40E−25	0.38	1		P19INK4D CDK4/6	“TUMOR SUPPRESSOR TUMOR
									INHIBITOR; CHAIN: NULL;	SUPPRESSOR, CDK4/6 INHIBITOR,
										ANKYRIN MOTIF”
372	1bd8		817	968	8.50E−25	0.38	0.28		P19INK4D CDK4/6	“TUMOR SUPPRESSOR TUMOR
									INHIBITOR; CHAIN: NULL;	SUPPRESSOR, CDK4/6 INHIBITOR,
										ANKYRIN MOTIF”
372	1bd8		887	1050	5.10E−24	0.04	−0.03		P19INK4D CDK4/6	“TUMOR SUPPRESSOR TUMOR
									INHIBITOR; CHAIN: NULL;	SUPPRESSOR, CDK4/6 INHIBITOR,
										ANKYRIN MOTIF”
372	1bd8		686	829	1.50E−22	0.64	1		P19INK4D CDK4/6	“TUMOR SUPPRESSOR TUMOR
									INHIBITOR; CHAIN: NULL;	SUPPRESSOR, CDK4/6 INHIBITOR,
										ANKYRIN MOTIF”
372	1bd8		617	766	5.10E−15	0.33	0.74		P19INK4D CDK4/6	“TUMOR SUPPRESSOR TUMOR
									INHIBITOR; CHAIN: NULL;	SUPPRESSOR, CDK4/6 INHIBITOR,
										ANKYRIN MOTIF”
372	1bd8		1210	1293	8.50E−15	0.1	−0.01		P19INK4D CDK4/6	“TUMOR SUPPRESSOR TUMOR
									INHIBITOR; CHAIN: NULL;	SUPPRESSOR, CDK4/6 INHIBITOR,
										ANKYRIN MOTIF”
372	1bi7	B	712	832	5.60E−30	0.69	1		CYCLIN-DEPENDENT	“COMPLEX (KINASE/ANTI-ONCOGENE)
									KINASE 6; CHAIN: A;	CDK6; P16INK4A, MTS1; CYCLIN
									MULTIPLE TUMOR	DEPENDENT KINASE, CYCLIN
									SUPPRESSOR; CHAIN: B;	DEPENDENT KINASE INHIBITORY 2
										PROTEIN, CDK, INK4, CELL CYCLE,
										MULTIPLE TUMOR SUPPRESSOR, 3 MTS1,
										COMPLEX (KINASE/ANTI-ONCOGENE)
										HEADER”
372	1bi7	B	777	932	4.20E−20	0.45	1		CYCLIN-DEPENDENT	“COMPLEX (KINASE/ANTI-ONCOGENE)
									KINASE 6; CHAIN: A;	CDK6; P16INK4A, MTS1; CYCLIN
									MULTIPLE TUMOR	DEPENDENT KINASE, CYCLIN
									SUPPRESSOR; CHAIN: B;	DEPENDENT KINASE INHIBITORY 2
										PROTEIN, CDK, INK4, CELL CYCLE,
										MULTIPLE TUMOR SUPPRESSOR, 3 MTS1,
										COMPLEX (KINASE/ANTI-ONCOGENE)
										HEADER”
372	1blx	B	712	865	5.60E−41	0.84	1		CYCLIN-DEPENDENT	“COMPLEX (INHIBITOR
									KINASE 6; CHAIN: A;	PROTEIN/KINASE) INHIBITOR PROTEIN,
									P19INK4D; CHAIN: B;	CYCLIN-DEPENDENT KINASE, CELL
										CYCLE 2 CONTROL, ALPHA/BETA,
										COMPLEX (INHIBITOR
										PROTEIN/KINASE)”
372	1blx	B	747	936	5.60E−36	0.41	1		CYCLIN-DEPENDENT	“COMPLEX (INHIBITOR
									KINASE 6; CHAIN: A;	PROTEIN/KINASE) INHIBITOR PROTEIN,
									P19INK4D; CHAIN: B;	CYCLIN-DEPENDENT KINASE, CELL
										CYCLE 2 CONTROL, ALPHA/BETA,
										COMPLEX (INHIBITOR
										PROTEIN/KINASE)”
372	1blx	B	817	972	1.00E−23	0.3	0.28		CYCLIN-DEPENDENT	“COMPLEX (INHIBITOR
									KINASE 6; CHAIN: A;	PROTEIN/KINASE) INHIBITOR PROTEIN,
									P19INK4D; CHAIN: B;	CYCLIN-DEPENDENT KINASE, CELL
										CYCLE 2 CONTROL, ALPHA/BETA,
										COMPLEX (INHIBITOR
										PROTEIN/KINASE)”
372	1blx	B	686	829	5.10E−21	0.59	1		CYCLIN-DEPENDENT	“COMPLEX (INHIBITOR
									KINASE 6; CHAIN: A;	PROTEIN/KINASE) INHIBITOR PROTEIN,
									P19INK4D; CHAIN: B;	CYCLIN-DEPENDENT KINASE, CELL
										CYCLE 2 CONTROL, ALPHA/BETA,
										COMPLEX (INHIBITOR
										PROTEIN/KINASE)”
372	1blx	B	1210	1293	1.70E−15	0.27	−0.08		CYCLIN-DEPENDENT	“COMPLEX (INHIBITOR
									KINASE 6; CHAIN: A;	PROTEIN/KINASE) INHIBITOR PROTEIN,
									P19INK4D; CHAIN: B;	CYCLIN-DEPENDENT KINASE, CELL
										CYCLE 2 CONTROL, ALPHA/BETA,
										COMPLEX (INHIBITOR
										PROTEIN/KINASE)”
372	1bu9	A	742	936	5.60E−36	0.48	1		CYCLIN-DEPENDENT	“HORMONE/GROWTH FACTOR P18-
									KINASE 6 INHIBITOR;	INK4C; CELL CYCLE INHIBITOR,
									CHAIN: A;	P18INK4C, TUMOR, SUPPRESSOR,
										CYCLIN-2 DEPENDENT KINASE,
										HORMONE/GROWTH FACTOR”
372	1bu9	A	705	865	1.10E−35	0.74	1		CYCLIN-DEPENDENT	“HORMONE/GROWTH FACTOR P18-
									KINASE 6 INHIBITOR;	INK4C; CELL CYCLE INHIBITOR,
									CHAIN: A;	P18INK4C, TUMOR, SUPPRESSOR,
										CYCLIN-2 DEPENDENT KINASE,
										HORMONE/GROWTH FACTOR”
372	1bu9	A	714	867	1.40E−33	0.86	1		CYCLIN-DEPENDENT	“HORMONE/GROWTH FACTOR P18-
									KINASE 6 INHIBITOR;	INK4C; CELL CYCLE INHIBITOR,
									CHAIN: A;	P18INK4C, TUMOR, SUPPRESSOR,
										CYCLIN-2 DEPENDENT KINASE,
										HORMONE/GROWTH FACTOR”
372	1bu9	A	617	768	1.70E−17	0.05	−0.01		CYCLIN-DEPENDENT	“HORMONE/GROWTH FACTOR P18-
									KINASE 6 INHIBITOR;	INK4C; CELL CYCLE INHIBITOR,
									CHAIN: A;	P18INK4C, TUMOR, SUPPRESSOR,
										CYCLIN-2 DEPENDENT KINASE,
										HORMONE/GROWTH FACTOR”
372	1cun	A	84	268	5.60E−14	0.36	0.29		“ALPHA SPECTRIN; CHAIN:	“STRUCTURAL PROTEIN TWO REPEATS
									A, B, C;”	OF SPECTRIN, ALPHA HELICAL LINKER
										REGION, 22 TANDEM 3-HELIX COILED-
										COILS, STRUCTURAL PROTEIN”
372	1d9s	A	736	865	1.30E−36	0.37	1		CYCLIN-DEPENDENT	“SIGNALING PROTEIN HELIX-TURN-
									KINASE 4 INHIBITOR B;	HELIX, ANKYRIN REPEAT”
									CHAIN: A;
372	1d9s	A	712	833	1.40E−32	0.59	1		CYCLIN-DEPENDENT	“SIGNALING PROTEIN HELIX-TURN-
									KINASE 4 INHIBITOR B;	HELIX, ANKYRIN REPEAT”
									CHAIN: A;
372	1d9s	A	801	967	2.80E−20	0.64	1		CYCLIN-DEPENDENT	“SIGNALING PROTEIN HELIX-TURN-
									KINASE 4 INHIBITOR B;	HELIX, ANKYRIN REPEAT”
									CHAIN: A;
372	1dcq	A	1210	1295	1.00E−14	0.12	−0.13		PYK2-ASSOCIATED	“METAL BINDING PROTEIN ZINC-
									PROTEIN BETA; CHAIN: A;	BINDING MODULE, ANKYRIN REPEATS,
										METAL BINDING PROTEIN”
372	1dnl	B	18	240	2.80E−10	0	0.03		SYNTAXIN BINDING	“ENDOCYTOSIS/EXOCYTOSIS NSEC1;
									PROTEIN 1; CHAIN: A;	PROTEIN-PROTEIN COMPLEX, MULTI-
									SYNTAXIN 1A; CHAIN: B;	SUBUNIT”
372	1ez3	A	133	249	7.00E−14	0.3	−0.14		“SYNTAXIN-1A; CHAIN: A,	“ENDOCYTOSIS/EXOCYTOSIS
									B, C;”	SYNAPTOTAGMIN ASSOCIATED 35 KDA
										PROTEIN, P35A, THREE HELIX BUNDLE”
372	1ez3	A	150	270	1.40E−12	0.06	−0.14		“SYNTAXIN-1A; CHAIN: A,	“ENDOCYTOSIS/EXOCYTOSIS
									B, C;”	SYNAPTOTAGMIN ASSOCIATED 35 KDA
										PROTEIN, P35A, THREE HELIX BUNDLE”
372	1ez3	A	119	219	1.10E−09	0.03	−0.18		“SYNTAXIN-1A; CHAIN: A,	“ENDOCYTOSIS/EXOCYTOSIS
									B, C;”	SYNAPTOTAGMIN ASSOCIATED 35 KDA
										PROTEIN, P35A, THREE HELIX BUNDLE”
372	1ihb	A	714	866	6.80E−33	1.07	1		“CYCLIN-DEPENDENT	“CELL CYCLE INHIBITOR P18-
									KINASE 6 INHIBITOR;	INK4C(INK6); CELL CYCLE INHIBITOR,
									CHAIN: A, B;”	P18-INK4C(INK6), ANKYRIN REPEAT, 2
										CDK 4/6 INHIBITOR”
372	1ihb	A	617	767	6.80E−17	0.25	0.19		“CYCLIN-DEPENDENT	“CELL CYCLE INHIBITOR P18-
									KINASE 6 INHIBITOR;	INK4C(INK6); CELL CYCLE INHIBITOR,
									CHAIN: A, B;”	P18-INK4C(INK6), ANKYRIN REPEAT, 2
										CDK 4/6 INHIBITOR”
372	1ikn	D	709	870	5.10E−38	0.2	1		NF-KAPPA-B P65 SUBUNIT;	“TRANSCRIPTION FACTOR P65; P50D;
									CHAIN: A; NF-KAPPA-B	TRANSCRIPTION FACTOR, IKB/NFKB
									P50D SUBUNIT; CHAIN: C; I-	COMPLEX”
									KAPPA-B-ALPHA; CHAIN: D;
372	1ikn	D	776	965	5.10E−34	0.19	0.78		NF-KAPPA-B P65 SUBUNIT;	“TRANSCRIPTION FACTOR P65; P50D;
									CHAIN: A; NF-KAPPA-B	TRANSCRIPTION FACTOR, IKB/NFKB
									P50D SUBUNIT; CHAIN: C; I-	COMPLEX”
									KAPPA-B-ALPHA; CHAIN: D;
372	1ikn	D	678	846	1.40E−29	0.57	1		NF-KAPPA-B P65 SUBUNIT;	“TRANSCRIPTION FACTOR P65; P50D;
									CHAIN: A; NF-KAPPA-B	TRANSCRIPTION FACTOR, IKB/NFKB
									P50D SUBUNIT; CHAIN: C; I-	COMPLEX”
									KAPPA-B-ALPHA; CHAIN: D;
372	1ikn	D	842	1031	3.40E−28	0.04	−0.14		NF-KAPPA-B P65 SUBUNIT;	“TRANSCRIPTION FACTOR P65; P50D;
									CHAIN: A; NF-KAPPA-B	TRANSCRIPTION FACTOR, IKB/NFKB
									P50D SUBUNIT; CHAIN: C; I-	COMPLEX”
									KAPPA-B-ALPHA; CHAIN: D;
372	1ikn	D	617	780	6.80E−20	0.3	0.54		NF-KAPPA-B P65 SUBUNIT;	“TRANSCRIPTION FACTOR P65; P50D;
									CHAIN: A; NF-KAPPA-B	TRANSCRIPTION FACTOR, IKB/NFKB
									P50D SUBUNIT; CHAIN: C; I-	COMPLEX”
									KAPPA-B-ALPHA; CHAIN: D;
372	1myo		885	981	3.40E−20	0.22	0.39		MYOTROPHIN; CHAIN:	“ANK-REPEAT MYOTROPHIN,
									NULL	ACETYLATION, NMR, ANK-REPEAT”
372	1myo		1211	1278	3.40E−14	0.25	−0.09		MYOTROPHIN; CHAIN:	“ANK-REPEAT MYOTROPHIN,
									NULL	ACETYLATION, NMR, ANK-REPEAT”
372	1myo		1213	1297	6.80E−14	0.21	−0.13		MYOTROPHIN; CHAIN:	“ANK-REPEAT MYOTROPHIN,
									NULL	ACETYLATION, NMR, ANK-REPEAT”
372	1nfi	E	708	870	5.10E−39	0.6	1		“NF-KAPPA-B P65; CHAIN:	“COMPLEX (TRANSCRIPTION REG/ANK
									A, C; NF-KAPPA-B P50;	REPEAT) COMPLEX (TRANSCRIPTION
									CHAIN: B, D; I-KAPPA-B-	REGULATION/ANK REPEAT), ANKYRIN 2
									ALPHA; CHAIN: E, F;”	REPEAT HELIX”
372	1nfi	E	712	936	7.00E−43	0.54	1		“NF-KAPPA-B P65; CHAIN:	“COMPLEX (TRANSCRIPTION REG/ANK
									A, C; NF-KAPPA-B P50;	REPEAT) COMPLEX (TRANSCRIPTION
									CHAIN: B, D; I-KAPPA-B-	REGULATION/ANK REPEAT), ANKYRIN 2
									ALPHA; CHAIN: E, F;”	REPEAT HELIX”
372	1nfi	E	774	965	3.40E−34	0.47	1		“NF-KAPPA-B P65; CHAIN:	“COMPLEX (TRANSCRIPTION REG/ANK
									A, C; NF-KAPPA-B P50;	REPEAT) COMPLEX (TRANSCRIPTION
									CHAIN: B, D; I-KAPPA-B-	REGULATION/ANK REPEAT), ANKYRIN 2
									ALPHA; CHAIN: E, F;”	REPEAT HELIX”
372	1nfi	E	640	813	6.80E−30	0.64	1		“NF-KAPPA-B P65; CHAIN:	“COMPLEX (TRANSCRIPTION REG/ANK
									A, C; NF-KAPPA-B P50;	REPEAT) COMPLEX (TRANSCRIPTION
									CHAIN: B, D; I-KAPPA-B-	REGULATION/ANK REPEAT), ANKYRIN 2
									ALPHA; CHAIN: E, F;”	REPEAT HELIX”
372	1nfi	E	676	846	1.70E−29	0.82	1		“NF-KAPPA-B P65; CHAIN:	“COMPLEX (TRANSCRIPTION REG/ANK
									A, C; NF-KAPPA-B P50;	REPEAT) COMPLEX (TRANSCRIPTION
									CHAIN: B, D; I-KAPPA-B-	REGULATION/ANK REPEAT), ANKYRIN 2
									ALPHA; CHAIN: E, F;”	REPEAT HELIX”
372	1nfi	E	625	780	1.70E−19	0.36	0.74		“NF-KAPPA-B P65; CHAIN:	“COMPLEX (TRANSCRIPTION REG/ANK
									A, C; NF-KAPPA-B P50;	REPEAT) COMPLEX (TRANSCRIPTION
									CHAIN: B, D; I-KAPPA-B-	REGULATION/ANK REPEAT), ANKYRN 2
									ALPHA; CHAIN: E, F;”	REPEAT HELIX”
372	1sig		48	262	1.40E−07	−0.11	0.12		RNA POLYMERASE	“TRANSCRIPTION REGULATION
									PRIMARY SIGMA FACTOR;	SIGMA70; RNA POLYMERASE SIGMA
									CHAIN: NULL;	FACTOR, TRANSCRIPTION REGULATION”
372	1ycs	B	712	921	2.80E−34	0.53	1		P53; CHAIN: A; 53BP2;	“COMPLEX (ANTI-ONCOGENE/ANKYRIN
									CHAIN: B;	REPEATS) P53BP2; ANKYRIN REPEATS,
										SH3, P53, TUMOR SUPPRESSOR,
										MULTIGENE 2 FAMILY, NUCLEAR
										PROTEIN, PHOSPHORYLATION, DISEASE
										MUTATION, 3 POLYMORPHISM,
										COMPLEX (ANTI-ONCOGENE/ANKYRIN
										REPEATS)”
372	1ycs	B	1212	1297	3.40E−14	0.28	−0.13		P53; CHAIN: A; 53BP2;	“COMPLEX (ANTI-ONCOGENE/ANKYRIN
									CHAIN: B;	REPEATS) P53BP2; ANKYRIN REPEATS,
										SH3, P53, TUMOR SUPPRESSOR,
										MULTIGENE 2 FAMILY, NUCLEAR
										PROTEIN, PHOSPHORYLATION, DISEASE
										MUTATION, 3 POLYMORPHISM,
										COMPLEX (ANTI-ONCOGENE/ANKYRIN
										REPEATS)”
373	1btk	A	51	97	0.00056	−0.17	0.19		“BRUTON'S TYROSINE	“TRANSFERASE BRUTON'S
									KINASE; CHAIN: A, B;”	AGAMMAGLOBULINEMIA TYROSINE
										KINASE, BTK; TRANSFERASE, PH
										DOMAIN, BTK MOTIF, ZINC BINDING, X-
										LINKED 2 AGAMMAGLOBULINEMIA,
										TYROSINE-PROTEIN KINASE”
373	1btn		51	137	1.40E−06	0.1	0.37		BETA-SPECTRIN; 1BTN 4	SIGNAL TRANSDUCTION PROTEIN
									CHAIN: NULL; 1BTN 5
373	1fao	A	51	139	2.80E−14	0.25	0.86		DUAL ADAPTOR OF	“SIGNALING PROTEIN DAPP1, PHISH,
									PHOSPHOTYROSINE AND 3-	BAM32; PLECKSTRIN, 3-
									CHAIN: A;	PHOSPHOINOSITIDES, INOSITOL
										TETRAKISPHOSPHATE 2 SIGNAL
										TRANSDUCTION PROTEIN, ADAPTOR
										PROTEIN”
373	1fb8	A	51	139	2.80E−14	0.38	0.89		DUAL ADAPTOR OF	“SIGNALING PROTEIN DAPP1, PHISH,
									PHOSPHOTYROSINE AND 3-	BAM32; PLECKSTRIN, 3-
									CHAIN: A;	PHOSPHOINOSITDES, INOSITOL
										TETRAKISPHOSPHATE 2 SIGNAL
										TRANSDUCTION PROTEIN, ADAPTOR
										PROTEIN”
373	1pls		51	138	1.40E−11	0.17	0.06			“PHOSPHORYLATION PLECKSTRIN (N-
										TERMINAL PLECKSTRIN HOMOLOGY
										DOMAIN) MUTANT 1PLS 3 WITH LEU GLU
										(HIS)6 ADDED TO THE C TERMINUS 1PLS
										4 (INS(G105-LEHHHHHH)) (NMR, 25
										STRUCTURES) 1PLS 5”
374	1sp2		1813	1839	0.0028	−0.51	0.68		SP1F2; CHAIN: NULL;	“ZINC FINGER TRANSCRIPTION FACTOR
										SP1; ZINC FINGER, TRANSCRIPTION
										ACTIVATION, SP1”
374	1sp2		1813	1839	0.0028	−0.51	0.68		SP1F2; CHAIN: NULL;	“ZINC FINGER TRANSCRIPTION FACTOR
										SP1; ZINC FINGER, TRANSCRIPTION
										ACTIVATION, SP1”
375	1a81	A	123	205	4.20E−19	0.62	1		“SYK KINASE; CHAIN: A, C,	“COMPLEX (TRANSFERASE/PEPTIDE)
									E, G, I, K; T-CELL SURFACE	ITAM PEPTIDE; COMPLEX
									GLYCOPROTEIN CD3	(TRANSFERASE/PEPTIDE), SYK, KINASE,
									EPSILON CHAIN; CHAIN: B,	SH2 DOMAIN, ITAM”
									D, F, H, J, L;”
375	1a81	E	123	204	1.40E−18	0.57	0.92		“SYK KINASE; CHAIN: A, C,	“COMPLEX (TRANSFERASE/PEPTIDE)
									E, G, I, K; T-CELL SURFACE	ITAM PEPTIDE; COMPLEX
									GLYCOPROTEIN CD3	(TRANSFERASE/PEPTDE), SYK, KINASE,
									EPSILON CHAIN; CHAIN: B,	SH2 DOMAIN, ITAM”
									D, F, H, J, L;”
375	1ab2		120	221	1.40E−19	0.4	1			“TRANSFERASE(PHOSPHOTRANSFERASE)
										PROTO-ONCOGENE TYROSINE KINASE
										(E.C.2.7.1.112) 1AB2 3 (SRC HOMOLOGY 2
										DOMAIN) (““ABELSON””, SH2 ABL) 1AB2 4
										(NMR, 20 STRUCTURES 1AB2 5”
375	1ab2		112	220	1.40E−19			51.36		“TRANSFERASE(PHOSPHOTRANSFERASE)
										PROTO-ONCOGENE TYROSINE KINASE
										(E.C.2.7.1.112) 1AB2 3 (SRC HOMOLOGY 2
										DOMAIN) (““ABELSON””, SH2 ABL) 1AB2 4
										(NMR, 20 STRUCTURES) 1AB2 5”
375	1aya	A	124	217	4.20E−22	0.78	1			“HYDROLASE(SH2 DOMAIN) TYROSINE
										PHOSPHATASE SYP (N-TERMINAL SH2
										DOMAIN) 1AYA 3 (PTP1D, SHPTP2)
										(E.C.3.1.3.48) COMPLEXED WITH THE
										PEPTIDE 1AYA 4 PDGFR-1009 1AYA 5”
375	1dlz	B	127	219	4.20E−21	0.26	1		“SAP SH2 DOMAIN; CHAIN:	GENE REGULATION SH2 DOMAINS
									A, B, C, D;”
375	1d4t	A	123	219	4.20E−20	0.23	1		T CELL SIGNAL	“SIGNALING PROTEIN SLAM; SH2
									TRANSDUCTION	DOMAIN, TYROSINE KINASE, SIGNAL
									MOLECULE SAP; CHAIN: A;	TRANSDUCTION, PEPTIDE 2
									SIGNALING LYMPHOCYTIC	RECOGNITION”
									ACTIVATION MOLECULE;
									CHAIN: B;
375	1lkk	A	123	217	1.40E−18	0.26	1		HUMAN P56 TYROSINE	COMPLEX (TYROSINE KINASE/PEPTIDE)
									KINASE; 1LKK7 CHAIN: A;
									1LKK 8 PHOSPHOTYROSYL
									PEPTIDE AC-PTYR-GLU-
									GLU-ILE; 1LKK 11 CHAIN: B;
									1LKK 12
375	1qgl	E	123	219	8.40E−21	0.58	0.99		GROWTH FACTOR	“HORMONE/GROWTH FACTOR GRB2-SH2;
									RECEPTOR BINDING	SIGNAL TRANSDUCTION, SH2 DOMAIN,
									PROTEIN; CHAIN: E; SHC-	PHOSPHOTYROSYL PEPTIDE, 2 COMPLEX
									DERIVED PEPTIDE; CHAIN:	(SIGNAL TRANSDUCTION/PEPTIDE),
									I;	HORMONE/GROWTH FACTOR”
375	1qgl	E	123	224	8.40E−21			51.7	GROWTH FACTOR	“HORMONE/GROWTH FACTOR GRB2-SH2;
									RECEPTOR BINDING	SIGNAL TRANSDUCTION, SH2 DOMAIN,
									PROTEIN; CHAIN: E; SHC-	PHOSPHOTYROSYL PEPTIDE, 2 COMPLEX
									DERIVED PEPTIDE; CHAIN:	(SIGNAL TRANSDUCTION/PEPTIDE),
									I;	HORMONE/GROWTH FACTOR”
375	1sha	A	123	205	2.80E−18	0.52	1			“PHOSPHOTRANSFERASE V-SRC
										TYROSINE KINASE TRANSFORMING
										PROTEIN (PHOSPHOTYROSINE 1SHA 3
										RECOGNITION DOMAIN SH2)
										(E.C.2.7.1.112) COMPLEX WITH 1SHA 4
										PHOSPHOPEPTIDE A (TYR-VAL-PRO-MET-
										LEU, PHOSPHORYLATED TYR) 1SHA 5”
375	3hck		123	219	2.80E−18	0.31	0.99		HCK SH2; CHAIN: NULL;	“TRANSFERASE HCK, SH2, TYROSINE
										KINASE, SIGNAL TRANSDUCTION,
										TRANSFERASE”
376	1pbw	B	99	193	7.00E−20	−0.05	0.29		“PHOSPHATIDYLINOSITOL	“PHOSPHOTRANSFERASE RHOGAP
									3-KINASE; CHAIN: A, B;”	DOMAIN; PHOSPHOTRANSFERASE,
										TPASE ACTIVATING PROTEIN, GAP,
										CDC42, 2 PHOSPHOINOSITIDE 3-KINASE,
										SH3 DOMAIN, SH2 DOMAIN, 3 SIGNAL
										TRANSDUCTION”
376	1pbw	A	99	193	1.30E−19	−0.41	0.46		“PHOSPHATIDYLINOSITOL	“PHOSPHOTRANSFERASE RHOGAP
									3-KINASE; CHAIN: A, B;”	DOMAIN; PHOSPHOTRANSFERASE,
										TPASE ACTIVATING PROTEIN, GAP,
										CDC42, 2 PHOSPHOINOSITIDE 3-KINASE,
										SH3 DOMAIN, SH2 DOMAIN, 3 SIGNAL
										TRANSDUCTION”
376	1rgp		89	193	1.10E−23	−0.01	0.8		RHOGAP; CHAIN: NULL;	“G-PROTEIN CDC42 GTPASE-ACTIVATING
										PROTEIN; G-PROTEIN, GAP, SIGNAL-
										TRANSDUCTION”
376	1tx4	A	89	193	4.20E−24	0.38	0.99		P50-RHOGAP; CHAIN: A;	“COMPLEX(GTPASE ACTLVATN/PROTO-
									TRANSFORMING PROTEIN	ONCOGENE) GTPASE-ACTIVATING
									RHOA; CHAIN: B;	PROTEIN RHOGAP; COMPLEX (GTPASE
										ACTIVATION/PROTO-ONCOGENE),
										GTPASE, 2 TRANSITION STATE, GAP”
379	1cp2	A	97	310	6.80E−50	−0.02	0.43		“NITROGENASE IRON	“OXIDOREDUCTASE CP2;
									PROTEIN; CHAIN: A, B;”	OXIDOREDUCTASE, NITROGENASE IRON
										PROTEIN HEADER CONECT LINK”
379	1cp2	A	66	319	6.80E−50			56.94	“NITROGENASE IRON	“OXIDOREDUCTASE CP2;
									PROTEIN; CHAIN: A, B;”	OXIDOREDUCTASE, NITROGENASE IRON
										PROTEIN HEADER CONECT LINK”
379	1f48	A	61	251	2.60E−23	−0.05	0.58		ARSENITE-	“HYDROLASE ARSA ATPASE; P-LOOP,
									TRANSLOCATING ATPASE;	ANTIMONITE BINDING SITE, ATP
									CHAIN: A;	BINDING SITE”
379	2ffh	A	43	314	6.50E−31	−0.24	0.01		“FFH; CHAIN: A, B, C;”	“PROTEIN TRANSPORT FIFTY-FOUR
										HOMOLOG, P48; FFH, SRP54, SIGNAL
										RECOGNITION PARTICLE, GTPASE, M
										DOMAIN, 2 RNA-BINDING, SIGNAL
										SEQUENCE-BINDING, HELIX-TURN-
										HELIX, 3 PROTEIN TARGETING, PROTEIN
										TRANSPORT”
379	2nip	A	95	312	5.10E−51	−0.36	0.51		“NITROGENASE IRON	“IRON PROTEIN IRON PROTEIN,
									PROTEIN; CHAIN: A, B;”	OXIDOREDUCTASE”
379	2nip	B	95	312	5.10E−51	−0.17	0.36		“NITROGENASE IRON	“IRON PROTEIN IRON PROTEIN,
									PROTEIN; CHAIN: A, B;”	OXIDOREDUCTASE”
379	2nip	A	65	319	5.10E−51			50.57	“NITROGENASE IRON	“IRON PROTEIN IRON PROTEIN,
									PROTEIN; CHAIN: A, B;”	OXIDOREDUCTASE”
387	1b57	A	117	209	0.0014	−0.46	0.09		“FRUCTOSE-BISPHOSPHATE	“LYASE LYASE, ALDEHYDE,
									ALDOLASE II; CHAIN: A, B;”	GLYCOLYSIS”
387	2dub	A	119	348	2.60E−24	−0.16	0.25		“2-ENOYL-COA	“LYASE CROTONASE, ENOYL-COA
									HYDRATASE; CHAIN: A, B,	HYDRATASE 1; LYASE, HYDRATASE, B-
									C, D, E, F;”	OXIDATION, FATTY ACID
										DEGRADATION, COA, 2 LIGAND
										BINDING”
390	1a4i	A	37	332	1.00E−97	0.64	1		“METHYLENETETRAHYDROFOLATE	“OXIDOREDUCTASE METHYLENETHF
									DEHYDROGENASE/CHAIN:	DEHYDROGENASE/METHENYLTHF THF,
									A, B;”	BIFUNCTIONAL, DEHYDROGENASE,
										CYCLOHYDROLASE, FOLATE, 2
										OXIDOREDUCTASE HEADER”
390	1a4i	A	35	333	1.00E−97			206.73	“METHYLENETETRAHYDROFOLATE	“OXIDOREDUCTASE METHYLENETHF
									DEHYDROGENASE/CHAIN:	DEHYDROGENASE/METHENYLTHF THF,
									A, B;”	BIFUNCTIONAL, DEHYDROGENASE,
										CYCLOHYDROLASE, FOLATE, 2
										OXIDOREDUCTASE HEADER”
390	1b0a	A	37	328	0	0.83	1		FOLD BIFUNCTIONAL	“OXIDOREDUCTASE,HYDROLASE
									PROTEIN; CHAIN: A;	FOLATE, DEHYDROGENASE,
										CYCLCOHYDROLASE, BIFUNCTIONAL, 2
										CHANNELING,
										OXIDOREDUCTASE,HYDROLASE”
390	1b0a	A	36	337	0			247.92	FOLD BIFUNCTIONAL	“OXIDOREDUCTASE,HYDROLASE
									PROTEIN; CHAIN: A;	FOLATE, DEHYDROGENASE,
										CYCLCOHYDROLASE, BIFUNCTIONAL, 2
										CHANNELING,
										OXIDOREDUCTASE,HYDROLASE”
393	1poi	A	40	343	3.40E−41			59.13	“GLUTACONATE	“TRANSFERASE TRANSFERASE, COA,
									COENZYME A-	GLUTAMATE, PROTEIN FERMENTATION”
									TRANSFERASE; CHAIN: A,
									B, C, D;”
394	2abx	A	48	128	0.0021	−0.3	0.07			POSTSYNAPTIC NEUROTOXIN ALPHA-
										*BUNGAROTOXIN 2ABX 4
397	1ail	L	35	258	5.10E−78			55.09	“FAB59.1; CHAIN: L, H;	“COMPLEX (ANTIBODY/PEPTIDE)
									AIB142; CHAIN: P;”	COMPLEX (ANTIBODY/PEPTIDE),
										ANTIBODY, CONSTRAINED HIV-1 V3 2
										LOOP PEPTIDE, IMMUNOGLOBULIN”
397	1b4j	L	35	256	1.70E−73			55.27	“ANTIBODY; CHAIN: L, H;”	“ANTIBODY ENGINEERING ANTIBODY
										ENGINEERING, HUMANIZED AND
										CHIMERIC ANTIBODIES, 2 FAB, X-RAY
										STRUCTURES, GAMMA-INTERFERON”
397	1b6d	A	35	254	3.40E−82			54.84	“IMMUNOGLOBULIN;	“IMMUNOGLOBULIN
									CHAIN: A, B;”	IMMUNOGLOBULIN, KAPPA LIGHT-
										CHAIN DIMER HEADER”
397	1baf	L	35	261	1.70E−74			54.63		“IMMUNOGLOBULIN FAB FRAGMENT OF
										MURINE MONOCLONAL ANTIBODY AN02
										COMPLEX 1BAF 3 WITH ITS HAPTEN
										(2,2,6,6-TETRAMETHYL-1-
										PIPERIDINYLOXY-1BAF 4
										DINITROPHENYL) 1BAF 5”
397	1bj1	L	35	255	1.40E−84			59.19	“FAB FRAGMENT; CHAIN: L,	“COMPLEX (ANTIBODY/ANTIGEN)FAB-
									H, J, K; VASCULAR	12; VEGF; COMPLEX
									ENDOTHELIAL GROWTH	(ANTIBODY/ANTIGEN), ANGIOGENIC
									FACTOR; CHAIN: V, W;”	FACTOR”
397	1bjm	A	33	257	3.40E−43			53.97	“LOC-LAMBDA 1 TYPE	“IMMUNOGLOBULIN BENCE-JONES
									LIGHT-CHAIN DIMER; 1BJM	PROTEIN; 1BJM 8 BENCE JONES,
									6 CHAIN: A, B; 1BJM 7”	ANTIBODY, MULTIPLE QUATERNARY
										STRUCTURES 1BJM 13”
397	1bz7	B	34	253	3.40E−13			55.47	ANTIBODY R24 (LIGHT	“IMMUNE SYSTEM ANTIBODY (FAB
									CHAIN); CHAIN: A;	FRAGMENT), IMMUNE SYSTEM”
									ANTIBODY R24 (HEAVY
									CHAIN); CHAIN: B;
397	1cly	H	34	258	8.50E−13			55.85	“IGG FAB (HUMAN IGG1,	“IMMUNOGLOBULIN CBR96 FAB
									KAPPA); CHAIN: L, H;”	(IMMUNOGLOBULIN);
										IMMUNOGLOBULIN, IMMUNOGLOBULIN
										C REGION, GLYCOPROTEIN, ANTIB”
397	1fbi	H	34	253	1.40E−14			55.78		COMPLEX (ANTIBODY/ANTIGEN) FAB
										FRAGMENT OF THE MONOCLONAL
										ANTIBODY F9.13.7 (IGG1) 1FBI3
										COMPLEXED WITH LYSOZYME
										(E.C.3.2.1.17) 1FBI4
397	1fig	L	35	261	3.40E−79			56.99		IMMUNOGLOBULIN IMMUNOGLOBULIN
										G1 (KAPPA LIGHT CHAIN) FAB'
										FRAGMENT 1FIG 3
397	1gc1	L	35	255	1.40E−76			57.05	“ENVELOPE PROTEIN	“COMPLEX (HIV ENVELOPE
									GP120; CHAIN: G; CD4;	PROTEIN/CD4/FAB) COMPLEX (HIV
									CHAIN: C; ANTIBODY 17B;	ENVELOPE PROTEIN/CD4/FAB), HIV-1
									CHAIN: L, H;”	EXTERIOR 2 ENVELOPE GP120, T-CELL
										SURFACE GLYCOPROTEIN CD4, 3
										ANTIGEN-BINDING FRAGMENT OF
										HUMAN IMMUNOGLOBULIN 17B, 4
										GLYCOSYLATED PROTEIN”
397	1iai	L	35	261	5.10E−78			54.53	“IDIOTYPIC FAB 730.1.4	COMPLEX (IMMUNOGLOBULIN
									(IGG1) OF VIRUS 1IAI 5	IGG1/IGG2A)
									CHAIN: L, H; 1IAI 7 ANTI-
									IDIOTYPIC FAB 409.5.3
									(IGG2A); 1IAI 9 CHAIN: M, I
									1IAI 10”
397	1iai	H	35	249	3.40E−17			55.12	“IDIOTYPIC FAB 730.1.4	COMPLEX (IMMUNOGLOBULIN
									(IGG1) OF VIRUS 1IAI 5	IGG1/IGG2A)
									CHAIN: L, H; 1IAI 7 ANTI-
									IDIOTYPIC FAB 409.5.3
									(IGG2A); 1IAI 9 CHAIN: M, I
									1IAI 10”
397	1igc	H	34	256	3.40E−13			53.87		“COMPLEX (ANTIBODY/BINDING
										PROTEIN) IGG1 FAB FRAGMENT
										COMPLEXED WITH PROTEIN G (DOMAIN
										III) 1IGC 5 PROTEIN G, STREPTOCOCCUS
										1IGC 15”
397	1igt	A	35	261	1.70E−82			56.11	“IGG2A INTACT ANTIBODY-	“IMMUNOGLOBULIN INTACT
									MAB231; CHAIN: A, B, C,	IMMUNOGLOBULIN V REGION C
									D”	REGION, IMMUNOGLOBULIN”
397	1psk	L	35	261	6.80E−75			54.63	“ANTIBODY; CHAIN: L, H;”	“IMMUNOGLOBULIN FAB, GD2-
										GANGLIOSIDE, CARBOHYDRATE,
										MELANOMA, IMMUNOGLOBULIN”
397	1vge	H	34	261	3.40E−19			55.63	“TR1.9 FAB; CHAIN: L, H;”	“IMMUNOGLOBULIN TR1.9, ANTI-
										THYROID PEROXIDASE,
										AUTOANTIBODY, 2 IMMUNOGLOBULIN”
397	2fgw	L	35	261	3.40E−85			56.67		IMMUNOGLOBULIN FAB FRAGMENT OF
										A HUMANIZED VERSION OF THE ANTI-
										CD18 2FGW 3 ANTIBODY ‘H52’ (HUH52-OZ
										FAB) 2FGW 4
397	2hrp	H	34	255	5.10E−11			53.98	“MONOCLONAL ANTIBODY	“COMPLEX
									F11.2.32; CHAIN: L, H, M, N;	(IMMUNOGLOBULIN/PEPTIDE)
									HIV-1 PROTEASE PEPTIDE;	IMMUNOGLOBULIN, IGG1; FAB
									CHAIN: P, Q;”	FRAGMENT, CROSS-REACTIVITY, HIV1
										PROTEASE, ENZYME 2 INHIBITION,
										COMPLEX
										(IMMUNOGLOBULIN/PEPTIDE)”
397	2mcg	1	33	257	3.40E−45			56.28		IMMUNOGLOBULIN IMMUNOGLOBULIN
										LAMBDA LIGHT CHAIN DIMER (/MCG$)
										2MCG 3 (TRIGONAL FORM) 2MCG 4
403	1a4j	L	22	232	1.60E−39			75.47	“IMMUNOGLOBULIN, DIELS	“IMMUNOGLOBULIN
									ALDER CATALYTIC	IMMUNOGLOBULIN, ANTIBODY,
									ANTIBODY; CHAIN: L, H, A,	CATALYTIC ANTIBODY, DIELS ALDER, 2
									B;”	GERMLINE”
403	1afv	L	22	234	9.60E−40			74.25	“HUMAN	“COMPLEX (VIRAL
									IMMUNODEFICIENCY	CAPSID/IMMUNOGLOBULIN) HIV-1 CA,
									VIRUS TYPE 1 CAPSID	HIV CA, HIV P24, P24; FAB, FAB LIGHT
									CHAIN: A, B; ANTIBODY	CHAIN, FAB HEAVY CHAIN COMPLEX
									FAB25.3 FRAGMENT;	(VIRAL CAPSID/IMMUNOGLOBULIN),
									CHAIN: H, K, L, M;”	HIV, CAPSID PROTEIN, 2 P24”
403	1ai1	L	22	232	1.60E−42			76.61	“FAB59.1; CHAIN: L, H;	“COMPLEX (ANTIBODY/PEPTIDE)
									AIB142; CHAIN: P;”	COMPLEX (ANTIBODY/PEPTIDE),
										ANTIBODY, CONSTRAINED HIV-1 V3 2
										LOOP PEPTIDE, IMMUNOGLOBULIN”
403	1axt	L	22	232	1.60E−40			74.4	“IMMUNOGLOBULIN	“IMMUNOGLOBULIN
									IGG2A; CHAIN: L, H;”	IMMUNOGLOBULIN, ANTIBODY FAB',
										CATALYST, ALDOLASE REACTION”
403	1b2w	L	22	234	3.20E−39			74.47	ANTIBODY (LIGHT CHAIN);	“IMMUNE SYSTEM IMMUNOGLOBULIN;
									CHAIN: L; ANTIBODY	IMMUNOGLOBULIN ANTIBODY
									(HEAVY CHAIN); CHAIN: H;	ENGINEERING, HUMANIZED AND
										CHIMERIC ANTIBODY, FAB, 2 X-RAY
										STRUCTURE, THREE-DIMENSIONAL
										STRYCTURE, GAMMA-3 INTERFERON,
										IMMUNE SYSTEM”
403	1baf	H	22	237	9.60E−13			73.72		“IMMUNOGLOBULIN FAB FRAGMENT OF
										MURINE MONOCLONAL ANTIBODY AN02
										COMPLEX 1BAF 3 WITH ITS HAPTEN
										(2,2,6,6-TETRAMETHYL-1-
										PIPERIDINYLOXY-1BAF 4
										DINITROPHENYL) 1BAF 5”
403	1bbj	L	22	232	1.60E−37			75.08		IMMUNOGLOBULIN FAB' FRAGMENT OF
										MONOCLONAL ANTIBODY B72.3 1BBJ 3
										(MURINE/HUMAN CHIMERA) 1BBJ 4
403	1bog	A	22	234	3.20E-36			73.51	“ANTIBODY (CR 4-1);	“COMPLEX (ANTIBODY/PEPTIDE)
									CHAIN: A, B; PEPTIDE;	POLYSPECIFICITY, CROSS REACTIVITY,
									CHAIN: C;”	FAB-FRAGMENT, PEPTIDE, 2 HIV-1,
										COMPLEX (ANTIBODY/PEPTIDE)”
403	1bql	H	25	234	9.60E−15			73.27		COMPLEX (ANTIBODY/ANTIGEN)
										HYHEL-5 FAB COMPLEXED WITH
										BOBWHITE QUAIL LYSOZYME 1BQL 3
										1BQL 95
403	1cel	L	22	232	4.80E−38			72.4	CAMPATH-1H: LIGHT	“ANTIBODY THERAPEUTIC, ANTIBODY,
									CHAIN; CHAIN: L;	CD52”
									CAMPATH-1H: HEAVY
									CHAIN; CHAIN: H; PEPTIDE
									ANTIGEN; CHAIN: P;
403	1gcl	L	22	232	6.40E−38			75.21	“ENVELOPE PROTEIN	“COMPLEX (HIV ENVELOPE
									GP120; CHAIN: G; CD4;	PROTEIN/CD4/FAB) COMPLEX (HIV
									CHAIN: C; ANTIBODY 17B;	ENVELOPE PROTEIN/CD4/FAB), HIV-1
									CHAIN: L, H;”	EXTERIOR 2 ENVELOPE GP120, T-CELL
										SURFACE GLYCOPROTEIN CD4, 3
										ANTIGEN-BINDING FRAGMENT OF
										HUMAN IMMUNOGLOBULIN 17B, 4
										GLYCOSYLATED PROTEIN”
403	1hil	A	22	232	1.60E−41			73.4		IMMUNOGLOBULIN IGG2A FAB
										FRAGMENT (FAB 17/9) 1HIL 3
403	1hyx	L	22	232	9.60E−41			76.4	“IMMUNOGLOBULIN 6D9;	“CATALYTIC ANTIBODY CATALYTIC
									CHAIN: L, H;”	ANTIBODY 6D9 CATALYTIC ANTIBODY,
										ESTER HYDROLYSIS, ESTEROLYTIC, FAB,
										2 IMMUNOGLOBULIN”
403	1igc	L	22	234	8.00E−40			73.05		“COMPLEX (ANTIBODY/BINDING
										PROTEIN) IGG1 FAB FRAGMENT
										COMPLEXED WITH PROTEIN G (DOMAIN
										III) 1IGC 5 PROTEIN G, STREPTOCOCCUS
										1IGC 15”
403	1igf	L	22	234	4.80E−41			74.75		IMMUNOGLOBULIN IGG1 FAB'
										FRAGMENT (B13I2) 1IGF 3
403	1mcp	L	22	234	1.10E−42			73.12		IMMUNOGLOBULIN IMMUNOGLOBULIN
										FAB FRAGMENT (MC/PC$603) 1MCP 4
403	1nsn	L	22	234	3.20E−42			73.78	“IGG FAB (IGG1, KAPPA);	“COMPLEX
									1NSN 4 CHAIN: L, H; 1NSN 5	(IMMUNOGLOBULIN/HYDROLASE) N10
									STAPHYLOCOCCAL	FAB IMMUNOGLOBULIN; 1NSN 7
									NUCLEASE; 1NSN 9 CHAIN:	STAPHYLOCOCCAL NUCLEASE
									S; 1NSN 10”	RIBONUCLEATE, 1NSN 11
										IMMUNOGLOBULIN, STAPHYLOCOCCAL
										NUCLEASE 1NSN 25”
403	1qrn	D	24	239	3.20E−12			79.43	MHC CLASS I HLA-A;	“IMMUNE SYSTEM HUMAN
									CHAIN: A; BETA-2	TCR/PEPTIDE/MHC COMPLEX, HLA-A2,
									MICROGLOBULIN; CHAIN:	HTLV-1, TAX, TCR, T 2 CELL RECEPTOR,
									B; TAX PEPTIDE P6A;	IMMUNE SYSTEM”
									CHAIN: C; HMAN T-CELL
									RECEPTOR; CHAIN: D; HLA-
									A 0201; CHAIN: E;
403	7fab	H	20	232	6.40E−13			72.96		IMMUNOGLOBULIN IMMUNOGLOBULIN
										FAB' NEW (LAMBDA LIGHT CHAIN) 7FAB3
409	1bu7	A	50	523	3.20E−71			217.68	“CYTOCHROME P450;	“OXIDOREDUCTASE FATTY ACID
									CHAIN: A, B;”	HYDROXYLASE; FATTY ACID
										MONOOXYGENASE, HEMOPROTEIN, P450
										REMARK”
409	1oxa		101	518	1.40E−28			91.88	CYTOCHROME P450 ERYF;	OXIDOREDUCTASE (OXYGENASE)
									1OXA 5 CHAIN: NULL 1OXA 6
410	1c28	A	157	288	1.40E−39			113.24	“30 KD ADIPOCYTE	“SERUM PROTEIN ACRP30 C1Q TNF
									COMPLEMENT-RELATED	TRIMER ALL BETA, SERUM PROTEIN”
									PROTEIN CHAIN: A, B, C;”
410	1c28	B	162	274	3.20E−36			103.46	“30 KD ADIPOCYTE	“SERUM PROTEIN ACRP30 C1Q TNF
									COMPLEMENT-RELATED	TRIMER ALL-BETA, SERUM PROTEIN”
									PROTEIN CHAIN: A, B, C;”
410	1c28	C	159	287	3.20E−28			80.55	“30 KD ADIPOCYTE	“SERUM PROTEIN ACRP30 C1Q TNF
									COMPLEMENT-RELATED	TRIMER ALL-BETA, SERUM PROTEIN”
									PROTEIN CHAIN: A, B, C;”
412	1c28	A	199	333	3.20E−15			119.24	“30 KD ADIPOCYTE	“SERUM PROTEIN ACRP30 C1Q TNF
									COMPLEMENT-RELATED	TRIMER ALL-BETA, SERUM PROTEIN”
									PROTEIN CHAIN: A, B, C;”
412	1c28	B	199	319	3.20E−13			104.74	“30 KD ADIPOCYTE	“SERUM PROTEIN ACRP30 C1Q TNF
									COMPLEMENT-RELATED	TRIMER ALL-BETA, SERUM PROTEIN”
									PROTEIN CHAIN: A, B, C;”
412	1c28	C	199	332	3.20E−09			85.06	“30 KD ADIPOCYTE	“SERUM PROTEIN ACRP30 C1Q TNF
									COMPLEMENT-RELATED	TRIMER ALL-BETA, SERUM PROTEIN”
									PROTEIN CHAIN: A, B, C;”
413	1c28	A	171	306	4.80E−20			61.4	“30 KD ADIPOCYTE	“SERUM PROTEIN ACRP30 C1Q TNF
									COMPLEMENT-RELATED	TRIMER ALL-BETA, SERUM PROTEIN”
									PROTEIN CHAIN: A, B, C;”
413	1c28	B	180	292	8.00E−17			50.71	“30 KD ADIPOCYTE	“SERUM PROTEIN ACRP30 C1Q TNF
									COMPLEMENT-RELATED	TRIMER ALL-BETA, SERUM PROTEIN”
									PROTEIN CHAIN: A, B, C;”
414	1hlg	A	29	394	8.50E−89	0.83	1		“LIPASE, GASTRIC; CHAIN:	HYDROLASE LIPASE
									A, B;”
416	1a4y	A	45	204	2.10E−18	0.13	0.41		“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”
416	1a4y	A	48	232	6.30E−13	−0.1	0.31		“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”
416	1a9n	A	68	211	8.40E−21	0.64	0.7		“U2 RNA HAIRPIN IV;	“COMPLEX (NUCLEAR PROTEIN/RNA)
									CHAIN: Q, R; U2 A'; CHAIN:	COMPLEX (NUCLEAR PROTEIN/RNA),
									A, C; U2 B”; CHAIN: B, D;”	RNA, SNRNP, IBONUCLEOPROTEIN”
416	1a9n	C	68	211	1.00E−20	0.61	0.55		“U2 RNA HAIRPIN IV;	“COMPLEX (NUCLEAR PROTEIN/RNA)
									CHAIN: Q, R; U2 A'; CHAIN:	COMPLEX (NUCLEAR PROTEIN/RNA),
									A, C; U2 B”; CHAIN: B, D;”	RNA, SNRNP, IBONUCLEOPROTEIN”
416	1a9n	C	43	124	1.50E−07	−0.09	0.07		“U2 RNA HAIRPIN IV;	“COMPLEX (NUCLEAR PROTEIN/RNA)
									CHAIN: Q, R; U2 A'; CHAIN:	COMPLEX (NUCLEAR PROTEIN/RNA),
									A, C; U2 B”; CHAIN: B, D;”	RNA, SNRNP, IBONUCLEOPROTEIN”
416	1cs6	A	293	405	3.40E−12	0.01	0.37		AXONIN-1; CHAIN: A;	CELL ADHESION NEURAL CELL
										ADHESION
416	1cvs	D	292	372	3.40E−11	0.13	0.4		“FIBROBLAST GROWTH	“GROWTH FACTOR/GROWTH FACTOR
									FACTOR 2; CHAIN: A, B;	RECEPTOR FGF, FGFR,
									FIBROBLAST GROWTH	IMMUNOGLOBULIN-LIKE, SIGNAL
									FACTOR RECEPTOR 1;	TRANSDUCTION, 2 DIMERIZATION,
									CHAIN: C, D;”	GROWTH FACTOR/GROWTH FACTOR
										RECEPTOR”
416	1cvs	C	293	404	3.40E−10	0.04	−0.05		“FIBROBLAST GROWTH	“GROWTH FACTOR/GROWTH FACTOR
									FACTOR 2; CHAIN: A, B;	RECEPTOR FGF, FGFR,
									FIBROBLAST GROWTH	IMMUNOGLOBULIN-LIKE, SIGNAL
									FACTOR RECEPTOR 1;	TRANSDUCTION, 2 DIMERIZATION,
									CHAIN: C, D;”	GROWTH FACTOR/GROWTH FACTOR
										RECEPTOR”
416	1cvs	D	293	404	3.40E−10	0.01	−0.13		“FIBROBLAST GROWTH	“GROWTH FACTOR/GROWTH FACTOR
									FACTOR 2; CHAIN: A, B;	RECEPTOR FGF, FGFR,
									FIBROBLAST GROWTH	IMMUNOGLOBULIN-LIKE, SIGNAL
									FACTOR RECEPTOR 1;	TRANSDUCTION, 2 DIMERIZATION,
									CHAIN: C, D;”	GROWTH FACTOR/GROWTH FACTOR
										RECEPTOR”
416	1d0b	A	45	188	1.70E−18	0.7	1		INTERNALIN B; CHAIN: A;	“CELL ADHESION LEUCINE RICH
										REPEAT, CALCIUM BINDING, CELL
										ADHESION”
416	1d0b	A	54	225	1.00E−17	0.55	0.99		INTERNALIN B; CHAIN: A;	“CELL ADHESION LEUCINE RICH
										REPEAT, CALCIUM BINDING, CELL
										ADHESION”
416	1d0b	A	7	124	1.70E−13	0.59	0.76		INTERNALIN B; CHAIN: A;	“CELL ADHESION LEUCINE RICH
										REPEAT, CALCIUM BINDING, CELL
										ADHESION”
416	1dce	A	34	121	8.50E−09	0.26	0.28		“RAB	“TRANSFERASE CRYSTAL STRUCTURE,
									GERANYLGERANYLTRANSFERASE	RAB GERANYLGERANYLTRANSFERASE,
									ALPHA SUBUNIT;	2.0 A 2 RESOLUTION, N-
									CHAIN: A, C; RAB	FORMYLMETHIONINE, ALPHA SUBUNIT,
									GERANYLGERANYLTRANSFERASE	BETA SUBUNIT”
									BETA SUBUNIT;
									CHAIN: B, D;”
416	1ds9	A	65	173	4.20E−14	−0.32	0		OUTER ARM DYNEIN;	“CONTRACTILE PROTEIN LEUCINE-RICH
									CHAIN: A;	REPEAT, BETA-BETA-ALPHA CYLINDER,
										DYNEIN, 2 CHLAMYDOMONAS,
										FLAGELLA”
416	1ev2	G	288	376	3.40E−09	0.04	0.36		“FIBROBLAST GROWTH	“GROWTH FACTOR/GROWTH FACTOR
									FACTOR 2; CHAIN: A, B, C,	RECEPTOR FGF2; FGFR2;
									D; FIBROBLAST GROWTH	IMMUNOGLOBULIN (IG)LIKE DOMAINS
									FACTOR RECEPTOR 2;	BELONGING TO THE I-SET 2 SUBGROUP
									CHAIN: E, F, G, H;”	WITHIN IG-LIKE DOMAINS, B-TREFOIL
										FOLD”
416	1ev2	E	293	377	3.40E−09	0.06	−0.11		“FIBROBLAST GROWTH	“GROWTH FACTOR/GROWTH FACTOR
									FACTOR 2; CHAIN: A, B, C,	RECEPTOR FGF2; FGFR2;
									D; FIBROBLAST GROWTH	IMMUNOGLOBULIN (IG)LIKE DOMAINS
									FACTOR RECEPTOR 2;	BELONGING TO THE I-SET 2 SUBGROUP
									CHAIN: E, F, G, H;”	WITHIN IG-LIKE DOMAINS, B-TREFOIL
										FOLD”
416	1evt	C	293	404	3.40E−10	0.03	−0.09		“FIBROBLAST GROWTH	“GROWTH FACTOR/GROWTH FACTOR
									FACTOR 1; CHAIN: A, B;	RECEPTOR FGF1; FGFR1;
									FIBROBLAST GROWTH	IMMUNOGLOBULIN (IG) LIKE DOMAINS
									FACTOR RECEPTOR 1;	BELONGING TO THE I-SET 2 SUBGROUP
									CHAIN: C, D;”	WITHIN IG-LIKE DOMAINS, B-TREFOIL
										FOLD”
416	1fhg	A	291	372	3.40E−09	0.01	0.34		TELOKIN; CHAIN: A	“CONTRACTILE PROTEIN
										IMMUNOGLOBULIN FOLD, BETA
										BARREL”
416	1fo1	B	155	224	8.50E−06	−0.13	0.03		“NUCLEAR RNA EXPORT	“RNA BINDING PROTEIN TAP (NFX1);
									FACTOR 1; CHAIN: A, B;”	RIBONUCLEOPROTEIN (RNP, RBD OR
										RRM) AND LEUCINE-RICH-REPEAT 2
										(LRR)”
416	1fo1	A	155	224	8.50E−06	−0.21	0.23		“NUCLEAR RNA EXPORT	“RNA BINDING PROTEIN TAP (NFX1);
									FACTOR 1; CHAIN: A, B;”	RIBONUCLEOPROTEIN (RNP, RBD OR
										RRM) AND LEUCINE-RICH-REPEAT 2
										(LRR)”
416	1fs2	A	63	215	3.40E−06	−0.09	0.12		“SKP2; CHAIN: A, C; SKP1;	“LIGASE CYCLIN A/CDK2-ASSOCIATED
									CHAIN: B, D;”	P45; CYCLIN A/CDK2-ASSOCIATED P19;
										SKP1, SKP2, F-BOX, LRRS, LEUCINE-RICH
										REPEATS, SCF, 2 UBIQUITIN, E3,
										UBIQUITIN PROTEIN LIGASE”
416	1yrg	A	61	231	0.00051	0.4	0.27		“GTPASE-ACTIVATING	“TRANSCRIPTION RNA1P; RANGAP;
									PROTEIN RNA1_SCHPO;	GTPASE-ACTIVATING PROTEIN FOR SPI1,
									CHAIN: A, B;”	GTPASE-ACTIVATING PROTEIN, GAP,
										RNA1P, RANGAP, LRR, LEUCINE-2 RICH
										REPEAT PROTEIN, TWINNING,
										HEMIHEDRAL TWINNING, 3
										MEROHEDRAL TWINNING, MEROHEDRY”
417	1cew	I	131	228	1.30E−18	0.01	0.04			PROTEINASE INHIBITOR(CYSTEINE)
										CYSTATIN 1CEW 3
417	1cew	I	33	117	4.20E−05	−0.01	0.01			PROTEINASE INHIBITOR(CYSTEINE)
										CYSTATIN 1CEW 3
418	1cew	I	25	132	1.20E−23	−0.03	0.12			PROTEINASE INHIBITOR(CYSTEINE)
										CYSTATIN 1CEW 3
420	1buc	A	63	442	0	0.9	1			ACYL-COA DEHYDROGENASE
										(FLAVOPROTEIN) BUTYRYL-COA
										DEHYDROGENASE (BCAD) (BACTERIAL
										SHORT-CHAIN 1BUC 3 ACYL-COA
										DEHYDROGENASE) (E.C.1.3.99.2)
										COMPLEXED WITH 1BUC 4 FAD AND
										ACETOACETYL-COENZYME A 1BUC 5
420	1egd	A	57	444	0	0.71	1		“MEDIUM CHAIN ACYL-	“ELECTRON TRANSFER ACYL-COA
									COA DEHYDROGENASE;	DEHYDROGENASE, FLAVOPROTEIN,
									CHAIN: A, B, C, D;”	ELECTRON TRANSFER”
420	1ivh	A	63	439	0	0.76	1		“ISOVALERYL-COA	“OXIDOREDUCTASE OXIDOREDUCTASE,
									DEHYDROGENASE; CHAIN:	ACYL-COA DEHYDROGENASE,
									A, B, C, D;”	FLAVOPROTEIN, 2 ISOVALERYL-COA,
										ISOVALERIC ACIDEMIA”
420	3mdd	A	60	444	0	0.9	1			OXIDOREDUCTASE MEDIUM CHAIN
										ACYL-COA DEHYDROGENASE (MCAD)
										(E.C.1.3.99.3) 3MDD 3
421	1a88	A	144	373	3.40E−30	0.29	−0.17		“CHLOROPEROXIDASE L;	“HALOPEROXIDASE BROMOPEROXIDASE
									CHAIN: A, B, C;”	L, HALOPEROXIDASE L;
										HALOPEROXIDASE, OXIDOREDUCTASE”
421	1a8q		146	374	1.70E−27	0.18	−0.06		BROMOPEROXIDASE A1;	“HALOPEROXIDASE
									CHAIN: NULL;	CHLOROPEROXIDASE A1,
										HALOPEROXIDASE A1;
										HALOPEROXIDASE, OXIDOREDUCTASE”
421	1a8s		144	373	1.40E−30	0.38	0.1		CHLOROPEROXIDASE F;	“HALOPEROXIDASE HALOPEROXIDASE
									CHAIN: NULL;	F; HALOPEROXIDASE,
										OXIDOREDUCTASE, PROPIONATE
										COMPLEX”
421	1azw	A	135	333	5.10E−22	0.07	−0.14		“PROLINE	“AMINOPEPTIDASE AMINOPEPTIDASE,
									IMINOPEPTIDASE; CHAIN:	PROLINE IMINOPEPTIDASE, SERINE
									A, B;”	PROTEASE, 2 XANTHOMONAS
										CAMPESTRIS”
421	1b6g		159	273	1.40E−13	0.51	−0.07		HALOALKANE	“HYDROLASE HYDROLASE,
									DEHALOGENASE; CHAIN:	HALOALKANE DEHALOGENASE,
									NULL;	ALPHA/BETA-HYDROLASE”
421	1c4x	A	162	373	1.70E−25	0.17	−0.18		“2-HYDROXY-6-OXO-6-	“HYDROLASE BPHD; HYDROLASE, PCB
									PHENYLHEXA-2,4-	DEGRADATION”
									DIENOATE CHAIN: A;”
421	1cqw	A	150	303	8.50E−22	0.11	−0.15		HALOALKANE	“HYDROLASE A/B HYDROLASE FOLD,
									DEHALOGENASE; 1-	DEHALOGENASE I-S BOND”
									CHLOROHEXANE CHAIN: A;
421	1ehy	A	135	267	1.70E−18	0.22	−0.05		“SOLUBLE EPOXIDE	“HYDROLASE HYDROLASE, ALPHA/BETA
									HYDROLASE; CHAIN: A, B,	HYDROLASE FOLD, EPOXIDE
									C, D;”	DEGRADATION, 2 EPICHLOROHYDRIN”
421	1ehy	A	170	303	4.20E−06	−0.12	0.12		“SOLUBLE EPOXIDE	“HYDROLASE HYDROLASE, ALPHA/BETA
									HYDROLASE; CHAIN: A, B,	HYDROLASE FOLD, EPOXIDE
									C, D;”	DEGRADATION, 2 EPICHLOROHYDRIN”
421	1evq	A	130	286	1.00E−11	0.06	−0.15		SERINE HYDROLASE;	HYDROLASE ALPHA/BETA HYDROLASE
									CHAIN: A;	FOLD
421	1hlg	A	137	272	3.40E−09	0.31	−0.17		“LIPASE, GASTRIC; CHAIN:	HYDROLASE LIPASE
									A, B;”
421	1jkm	A	134	273	1.50E−12	0.49	0.07		“BREFELDIN A ESTERASE;	“SERINE HYDROLASE SERINE
									CHAIN: A, B;”	HYDROLASE, DEGRADATION OF
										BREFELDIN A, ALPHA/BETA 2
										HYDROLASE FAMILY”
421	1qfm	A	3	377	1.70E−42	0.07	−0.07		PROLYL OLIGOPEPTIDASE;	“HYDROLASE PROLYL ENDOPEPTIDASE,
									CHAIN: A;	POST-PROLINE CLEAVING PROLYL
										OLIGOPEPTIDASE, AMNESIA,
										ALPHA/BETA-HYDROLASE, BETA- 2
										PROPELLER”
421	1qtr	A	132	333	6.80E−22	0.07	−0.07		PROLYL AMINOPEPTIIDASE;	“HYDROLASE ALPHA BETA HYDROLASE
										HALOPEROXIDASE, OXIDOREDUCTASE”
421	1a8q		146	374	1.70E−27	0.18	−0.06		BROMOPEROXIDASE A1;	“HALOPEROXIDASE
									CHAIN: NULL;	CHLOROPEROXIDASE A1,
										HALOPEROXIDASE A1;
										HALOPEROXIDASE, OXIDOREDUCTASE”
421	1a8s		144	373	1.40E−30	0.38	0.1		CHLOROPEROXIDASE F;	“HALOPEROXIDASE HALOPEROXIDASE
									CHAIN: NULL;	F; HALOPEROXIDASE,
										OXIDOREDUCTASE, PROPIONATE
										COMPLEX”
421	1azw	A	135	333	5.10E−22	0.07	−0.14		“PROLINE	“AMINOPEPTIDASE AMINOPEPTIDASE,
									IMINOPEPTIDASE; CHAIN:	PROLINE IMINOPEPTIDASE, SERINE
									A, B;”	PROTEASE, 2 XANTHOMONAS
										CAMPESTRIS”
421	1b6g		159	273	1.40E−13	0.51	−0.07		HALOALKANE	“HYDROLASE HYDROLASE,
									DEHALOGENASE; CHAIN:	HALOALKANE DEHALOGENASE,
									NULL;	ALPHA/BETA-HYDROLASE”
421	1c4x	A	162	373	1.70E−25	0.17	−0.18		“2-HYDROXY-6-OXO-6-	“HYDROLASE BPHD; HYDROLASE, PCB
									PHENYLHEXA-2,4-	DEGRADATION”
									DIENOATE CHAIN: A;”
421	1cqw	A	150	303	8.50E−22	0.11	−0.15		HALOALKANE	“HYDROLASE A/B HYDROLASE FOLD,
									DEHALOGENASE; 1-	DEHALOGENASE I-S BOND”
									CHLOROHEXANE CHAIN: A;
421	1ehy	A	135	267	1.70E−18	0.22	−0.05		“SOLUBLE EPOXIDE	“HYDROLASE HYDROLASE, ALPHA/BETA
									HYDROLASE; CHAIN: A, B,	HYDROLASE FOLD, EPOXIDE
									C, D;”	DEGRADATION, 2 EPICHLOROHYDRIN”
421	1ehy	A	170	303	4.20E−06	−0.12	0.12		“SOLUBLE EPOXIDE	“HYDROLASE HYDROLASE, ALPHA/BETA
									HYDROLASE; CHAIN: A, B,	HYDROLASE FOLD, EPOXIDE
									C, D;”	DEGRADATION, 2 EPICHLOROHYDRIN”
421	1evq	A	130	286	1.00E−11	0.06	−0.15		SERINE HYDROLASE;	HYDROLASE ALPHA/BETA HYDROLASE
									CHAIN: A;	FOLD
421	1hlg	A	137	272	3.40E−09	0.31	−0.17		“LIPASE, GASTRIC; CHAIN:	HYDROLASE LIPASE
									A, B;”
421	1jkm	A	134	273	1.50E−12	0.49	0.07		“BREFELDIN A ESTERASE;	“SERINE HYDROLASE SERINE
									CHAIN: A, B;”	HYDROLASE, DEGRADATION OF
										BREFELDIN A, ALPHA/BETA 2
										HYDROLASE FAMILY”
421	1qfm	A	3	377	1.70E−42	0.07	−0.07		PROLYL OLIGOPEPTIDASE;	“HYDROLASE PROLYL ENDOPEPTIDASE,
									CHAIN: A;	POST-PROLINE CLEAVING PROLYL
										OLIGOPEPTIDASE, AMNESIA,
										ALPHA/BETA-HYDROLASE, BETA- 2
										PROPELLER”
421	1qtr	A	132	333	6.80E−22	0.07	−0.07		PROLYL AMINOPEPTIDASE;	“HYDROLASE ALPHA BETA HYDROLASE
									CHAIN: A;	FOLD, PROLINE, PROLYL
										AMINOPEPTIDASE, 2 SERRATIA,
										IMINOPEPTIDASE”
422	1deq	C	98	362	5.10E−74	0.35	0.75		“FIBRINOGEN (ALPHA	BLOOD CLOTTING COILED-COIL
									CHAIN); CHAIN: A, D, N, Q;
									FIBRINOGEN (BETA
									CHAIN); CHAIN: B, E, O, R;
									FIBRINOGEN (GAMMA
									CHAIN); CHAIN: C, F, P, S;
									FIBRINOGEN; CHAIN: M, Z;”
422	1ei3	C	98	361	6.80E−74	0.21	0.82		“FIBRINOGEN; CHAIN: A, D;	“BLOOD CLOTTING COILED COILS,
									FIBRINOGEN; CHAIN: B, E;	DISULFIDE RINGS, FIBRIN FORMING
									FIBRINOGEN; CHAIN: C, F;”	ENTITIES”
422	1ei3	B	39	361	2.10E−73	−0.04	0.19		“FIBRINOGEN; CHAIN: A, D;	“BLOOD CLOTTING COILED COILS,
									FIBRINOGEN; CHAIN: B, E;	DISULFIDE RINGS, FIBRIN FORMING
									FIBRINOGEN; CHAIN: C, F;”	ENTITIES”
422	1ei3	B	113	363	5.10E−69	0.33	0.95		“FIBRINOGEN; CHAIN: A, D;	“BLOOD CLOTTING COILED COILS,
									FIBRINOGEN; CHAIN: B, E;	DISULFIDE RINGS, FIBRIN FORMING
									FIBRINOGEN; CHAIN: C, F;”	ENTITIES”
422	1fib		139	361	8.50E−72	0.61	1		GAMMA-FIBRINOGEN	“BLOOD COAGULATION FACTOR BLOOD
									CARBOXYL TERMINAL	COAGULATION, GLYCOPROTEIN,
									FRAGMENT; CHAIN: NULL;	CALCIUM, PLATELET, PLASMA, 2
										ALTERNATIVE SPLICING, SIGNAL,
										DISEASE MUTATION, 3 POLYMORPHISM”
422	1fib		143	364	8.50E−72			127.21	GAMMA-FIBRINOGEN	“BLOOD COAGULATION FACTOR BLOOD
									CARBOXYL TERMINAL	COAGULATION, GLYCOPROTEIN,
									FRAGMENT; CHAIN: NULL;	CALCIUM, PLATELET, PLASMA, 2
										ALTERNATIVE SPLICING, SIGNAL,
										DISEASE MUTATION, 3 POLYMORPHISM”
422	1fzc	C	98	361	5.10E−76	0.22	1		“FIBRIN; CHAIN: A, B, C, D,	“BLOOD COAGULATION BLOOD
									E, F, G, H, I, J;”	COAGULATION, PLASMA PROTEIN,
										CROSSLINKING”
422	1fzc	B	99	363	5.10E−70	0.39	1		“FIBRIN; CHAIN: A, B, C, D,	“BLOOD COAGULATION BLOOD
									E, F, G, H, I, J;”	COAGULATION, PLASMA PROTEIN,
										CROSSLINKING”
422	1fzc	C	92	368	5.10E−76			143.39	“FIBRIN; CHAIN: A, B, C, D,	“BLOOD COAGULATION BLOOD
									E, F, G, H, I, J;”	COAGULATION, PLASMA PROTEIN,
										CROSSLINKING”
422	1fzc	B	95	362	5.10E−70			141.03	“FIBRIN; CHAIN: A, B, C, D,	“BLOOD COAGULATION BLOOD
									E, F, G, H, I, J;”	COAGULATION, PLASMA PROTEIN,
										CROSSLINKING”
422	1fzd	A	184	365	3.40E−70	0.99	1		“FIBRINOGEN-420; CHAIN:	“BLOOD COAGULATION BLOOD
									A, B, C, D, E, F, G, H;”	COAGULATION, FIBRINOGEN-420,
										ALPHAEC DOMAIN, 2 FIBRINOGEN
										RELATED DOMAIN, GLYCOSYLATED
										PROTEIN”
422	1fzd	A	184	365	3.40E−70			145.75	“FIBRINOGEN-420; CHAIN:	“BLOOD COAGULATION BLOOD
									A, B, C, D, E, F, G, H;”	COAGULATION, FIBRINOGEN-420,
										ALPHAEC DOMAIN, 2 FIBRINOGEN
										RELATED DOMAIN, GLYCOSYLATED
										PROTEIN”
422	1fzg	C	98	361	5.10E−76	0.16	1		“FIBRINOGEN; CHAIN: A, B,	“BLOOD COAGULATION BLOOD
									C, D, E, F, S, T, M, N;”	COAGULATION, PLASMA, PLATELET,
										FIBRINOGEN, FIBRIN”
422	1fzg	E	117	364	5.10E−70	0.37	1		“FIBRINOGEN; CHAIN: A, B,	“BLOOD COAGULATION BLOOD
									C, D, E, F, S, T, M, N;”	COAGULATION, PLASMA, PLATELET,
										FIBRINOGEN, FIBRIN”
422	1fzg	C	97	364	5.10E−76			143.75	“FIBRINOGEN; CHAIN: A, B,	“BLOOD COAGULATION BLOOD
									C, D, E, F, S, T, M, N;”	COAGULATION, PLASMA, PLATELET,
										FIBRINOGEN, FIBRIN”
422	1fzg	E	102	362	5.10E−70			136.26	“FIBRINOGEN; CHAIN: A, B,	“BLOOD COAGULATION BLOOD
									C, D, E, F, S, T, M, N;”	COAGULATION, PLASMA, PLATELET,
										FIBRINOGEN, FIBRIN”
423	1aln	A	26	249	0	0.43	1		“B*3501; CHAIN: A, B;	“COMPLEX (ANTIGEN/PEPTIDE) B35;
									PEPTIDE VPLRPMTY;	MAJOR HISTOCOMPATIBILITY ANTIGEN,
									CHAIN: C;”	MHC, HLA, HLA-B3501, HIV, 2NEF,
										COMPLEX (ANTIGEN/PEPTIDE)”
423	1aln	A	26	249	0			152.97	“B*3501; CHAIN: A, B;	“COMPLEX (ANTIGEN/PEPTIDE) B35;
									PEPTIDE VPLRPMTY;	MAJOR HISTOCOMPATIBILITY ANTIGEN,
									CHAIN: C;”	MHC, HLA, HLA-B3501, HIV, 2NEF,
										COMPLEX (ANTIGEN/PEPTIDE)”
423	1agd	A	26	249	0	0.35	1		B*0801; CHAIN: A; BETA-2	“HISTOCOMPATIBILITY COMPLEX B8;
									MICROGLOBULIN; CHAIN:	B2M; PEPTIDE HLA B8, HIV, MHC CLASS I,
									B; HIV-1 GAG PEPTIDE	HISTOCOMPATIBILITY COMPLEX”
									(GGKKKYKL-INDEX
									PEPTIDE); CHAIN: C;
423	1agd	A	26	249	0			149.07	B*0801; CHAIN: A; BETA-2	“HISTOCOMPATIBILITY COMPLEX B8;
									MICROGLOBULIN; CHAIN:	B2M; PEPTIDE HLA B8, HIV, MHC CLASS I,
									B; HIV-1 GAG PEPTIDE	HISTOCOMPATIBILITY COMPLEX”
									(GGKKKYKL-INDEX
									PEPTIDE); CHAIN: C;
423	1duz	A	26	248	0	0.37	1		“HLA-A*0201; CHAIN: A, D;	IMMUNE SYSTEM IMMUNOGLOBULIN
									BETA-2 MICROGLOBULIN;	FOLD
									CHAIN: B, E; HTLV-1
									OCTAMERIC TAX PEPTIDE;
									CHAIN: C, F;”
423	1efx	A	26	250	0	0.56	1		“HLA-CW3 (HEAVY CHAIN);	“IMMUNE SYSTEM MHC, HLA, CLASS I,
									CHAIN: A; BETA-2-	KIR, NK CELL RECEPTOR,
									MICROGLOBULIN; CHAIN:	IMMUNOGLOBULIN 2 FOLD,
									B; PEPTIDE FROM	RECEPTOR/MHC COMPLEX”
									IMPORTIN ALPHA-2;
									CHAIN: C; NATURAL
									KILLER CELL RECEPTOR
									KIR2DL2; CHAIN: D, E;”
423	1hoc	A	26	245	1.40E−96			132.01		“HISTOCOMPATIBILITY ANTIGEN
										MURINE CLASS I MAJOR
										HISTOCOMPATIBILITY COMPLEX
										CONSISTING 1HOC 3 OF H-2D═B═, B2-
										MICROGLOBULIN, AND A 9-RESIDUE
										PEPTIDE 1HOC 4”
423	1hsa	A	26	249	0	0.4	1			HISTOCOMPATIBILITY ANTIGEN HUMAN
										CLASS I HISTOCOMPATIBILITY ANTIGEN
										1HSA 3/HLA-B(ASTERISK)2705$ 1HSA 4
423	1hsa	A	26	249	0			148.54		HISTOCOMPATIBILITY ANTIGEN HUMAN
										CLASS I HISTOCOMPATIBILITY ANTIGEN
										1HSA 3 /HLA-B(ASTERISK)2705$ 1HSA 4
423	1hsb	A	26	243	0	0.44	1			HISTOCOMPATIBILITY ANTIGEN CLASS I
										HISTOCOMPATIBILITY ANTIGEN AW68.1
										(LEUCOCYTE 1HSB 3 ANTIGEN) 1HSB 4
423	1hsb	A	26	243	0			136.73		HISTOCOMPATIBILITY ANTIGEN CLASS I
										HISTOCOMPATIBILITY ANTIGEN AW68.1
										(LEUCOCYTE 1HSB 3 ANTIGEN) 1HSB 4
423	1ld9	A	26	241	3.40E−96			121.61	MHC CLASS IH-2LD HEAVY	“MAJOR HISTOCOMPATIBILITY
									CHAIN; CHAIN: A; BETA-2	COMPLEX LD; MAJOR
									MICROGLOBULIN; CHAIN:	HISTOCOMPATIBILITY COMPLEX, LD”
									B; NANO-PEPTIDE; CHAIN:
									C;
423	1mhc	A	26	249	1.00E−90			130.39	“MHC CLASS I ANTIGEN H2-	HISTOCOMPATIBILITY
									M3; 1MHC 6 CHAIN: A, B, D,	ANTIGEN/PEPTIDE MAJOR
									E; 1MHC 7 NONAPEPTIDE	HISTOCOMPATIBILITY COMPLEX; 1MHC
									FROM RAT NADH	8 ND1; 1MHC 15
									DEHYDROGENASE; 1MHC
									12 CHAIN: C, F; 1MHC 13”
423	1mhe	A	27	247	0	0.36	1		“HLA CLASS I	“MAJOR HISTOCOMPATIBILITY
									HISTOCOMPATIBILITY	COMPLEX MHC NONCLASSICAL CHAIN,
									ANTIGEN HLA-E; CHAIN: A,	MHC-E, HLA-E, MHC CLASS HLA-E, HLA
									C; BETA-2-	E, MAJOR HISTOCOMPATIBILITY
									MICROGLOBULIN; CHAIN:	COMPLEX, MHC, HLA, 2 BETA 2
									B, D; PEPTIDE	MICROGLOBULIN, PEPTIDE, LEADER
									(VMAPRTVLL); CHAIN: P,	PEPTIDE, 3 NON-CLASSICAL MHC, CLASS
									Q;”	IB MHC”
423	1mhe	A	27	247	0			137.71	“HLA CLASS I	“MAJOR HISTOCOMPATIBILITY
									HISTOCOMPATIBILITY	COMPLEX MHC NONCLASSICAL CHAIN,
									ANTIGEN HLA-E; CHAIN: A,	MHC-E, HLA-E, MHC CLASS HLA-E, HLA
									C; BETA-2-	E, MAJOR HISTOCOMPATIBILITY
									MICROGLOBULIN; CHAIN:	COMPLEX, MHC, HLA, 2 BETA 2
									B, D; PEPTIDE	MICROGLOBULIN, PEPTIDE, LEADER
									(VMAPRTVLL); CHAIN: P,	PEPTIDE, 3 NON-CLASSICAL MHC, CLASS
									Q;”	IB MHC”
423	1osz	A	26	247	8.50E−99	0.48	1		MHC CLASS I H-2KB HEAVY	“COMPLEX (MHC I/PEPTIDE) VSV-8;
									CHAIN; CHAIN: A; BETA-2	MHC/PEPTIDE COMPLEX,
									MICROGLOBULIN; CHAIN:	TRANSMEMBRANE PROTEIN, THYMIC 2
									B; VESICULAR STOMATITIS	SELECTION, COMPLEX (MHC I/PEPTIDE)”
									VIRUS NUCLEOPROTEIN;
									CHAIN: C;
423	1osz	A	26	247	8.50E−99			138.77	MHC CLASS I H-2KB HEAVY	“COMPLEX (MHC I/PEPTIDE) VSV-8;
									CHAIN; CHAIN: A; BETA-2	MHC/PEPTIDE COMPLEX,
									MICROGLOBULIN; CHAIN:	TRANSMEMBRANE PROTEIN, THYMIC 2
									B; VESICULAR STOMATITIS	SELECTION, COMPLEX (MHC I/PEPTIDE)”
									VIRUS NUCLEOPROTEIN;
									CHAIN: C;
423	1qo3	A	27	247	0	0.44	1		“MHC CLASS I H-2DD	“COMPLEX (NK RECEPTOR/MHC CLASS I)
									HEAVY CHAIN; CHAIN: A;	H-2 CLASS I HISTOCOMPATIBILITY
									BETA-2-MICROGLOBULIN;	ANTIGEN, B2M; NK-CELL SURFACE
									CHAIN: B; HIV ENVELOPE	GLYCOPROTEIN YE1/48, NK CELL,
									GLYCOPROTEIN 120	INHIBITORY RECEPTOR, MHC-I, C-TYPE
									PEPTIDE; CHAIN: P; LY49A;	LECTIN-LIKE, 2 HISTOCOMPATIBILITY,
									CHAIN: C, D;”	B2M, LY49, LY-49”
423	1qqd	A	27	247	0	0.36	1		HISTOCOMPATIBILITY	“IMMUNE SYSTEM IMMUNOGLOBULIN
									LEUKOCYTE ANTIGEN	(IG)-LIKE DOMAIN, ALPHA HELIX, BETA
									(HLA)-CW4 CHAIN: A;	SHEET, 2 IMMUNE SYSTEM”
									BETA-2 MICROGLOBULIN;
									CHAIN: B; HLA-CW4
									SPECIFIC PEPTIDE; CHAIN:
									C;
423	1zag	A	25	249	1.50E−71			344.18	“ZINC-ALPHA-2-	“LIPID MOBILIZATION FACTOR ZN-
									GLYCOPROTEIN; CHAIN: A,	ALPHA-2-GLYCOPROTEIN, ZAG LIPID
									B, C, D;”	MOBILIZATION FACTOR, SECRETED MHC
										CLASS I HOMOLOG”
425	1by2		304	411	5.10E−44	1.06	1		MAC-2 BINDING PROTEIN;	“EXTRACELLULAR MODULE TUMOR-
									CHAIN: NULL;	ASSOCIATED ANTIGEN 90K;
										EXTRACELLULAR MODULE,
										SCAVENGER RECEPTOR, TUMOR-
										ASSOCIATED 2 ANTIGEN,
										EXTRACELLULAR MATRIX,
										GLYCOSYLATED PROTEIN”
425	1by2		39	149	1.20E−42	1.45	1		MAC-2 BINDING PROTEIN;	“EXTRACELLULAR MODULE TUMOR-
									CHAIN; NULL;	ASSOCIATED ANTIGEN 90K,
										EXTRACELLULAR MODULE,
										SCAVENGER RECEPTOR, TUMOR-
										ASSOCIATED 2 ANTIGEN,
										EXTRACELLULAR MATRIX,
										GLYCOSYLATED PROTEIN”
425	1by2		165	281	1.70E−38	0.48	0.72		MAC-2 BINDING PROTEIN;	“EXTRACELLULAR MODULE TUMOR-
									CHAIN: NULL;	ASSOCIATED ANTIGEN 90K;
										EXTRACELLULAR MODULE,
										SCAVENGER RECEPTOR, TUMOR-
										ASSOCIATED 2 ANTIGEN,
										EXTRACELLULAR MATRIX,
										GLYCOSYLATED PROTEIN”
425	1by2		37	150	1.20E−42			106.68	MAC-2 BINDING PROTEIN;	“EXTRACELLULAR MODULE TUMOR-
									CHAIN: NULL;	ASSOCIATED ANTIGEN 90K;
										EXTRACELLULAR MODULE,
										SCAVENGER RECEPTOR, TUMOR-
										ASSOCIATED 2 ANTIGEN,
										EXTRACELLULAR MATRIX,
										GLYCOSYLATED PROTEIN”
426	1ail	L	32	213	3.20E−13	0.07	0.05		“FAB59.1; CHAIN: L, H;	“COMPLEX (ANTIBODY/PEPTIDE)
									AIB142; CHAIN: P;”	COMPLEX (ANTIBODY/PEPTIDE),
										ANTIBODY, CONSTRAINED HIV-1 V3 2
										LOOP PEPTIDE, IMMUNOGLOBULIN”
426	1ail	H	31	249	1.60E−08			50.16	“FAB59.1; CHAIN: L, H;	“COMPLEX (ANTIBODY/PEPTIDE)
									AIB142; CHAIN: P;”	COMPLEX (ANTIBODY/PEPTIDE),
										ANTIBODY, CONSTRAINED HIV-1 V3 2
										LOOP PEPTIDE, IMMUNOGLOBULIN”
426	1aif	L	35	213	6.40E−13	0.07	0.05		“ANTI-IDIOTYPIC FAB	“IMMUNOGLOBULIN
									409.5.3 (IGG2A) FAB; CHAIN:	IMMUNOGLOBULIN, C REGION, V
									A, B, L, H”	REGION”
426	1dn2	A	29	222	4.80E−42	−0.11	0.01		“IMMUNOGLOBULIN	IMMUNE SYSTEM FC IGG PHAGE
									LAMBDA HEAVY CHAIN;	DISPLAY PEPTIDE
									CHAIN: A, B; ENGINEERED
									PEPTIDE; CHAIN: E, F;”
426	1ejo	L	32	213	3.20E−13	−0.05	0.33		IGG2A MONOCLONAL	“IMMUNE SYSTEM FMDV, ANTIGENIC-
									ANTIBODY (LIGHT CHAIN);	ANTIBODY INTERACTIONS, RGD MOTIF,
									CHAIN: L; IGG2A	G-H LOOP 2 OF VP1.”
									MONOCLONAL ANTIBODY
									(HEAVY CHAIN); CHAIN: H;
									FMDV PEPTIDE; CHAIN: P;
426	1epf	A	37	209	4.80E−21	0.16	−0.07		“NEURAL CELL ADHESION	“CELL ADHESION NCAM; NCAM,
									MOLECULE; CHAIN: A, B, C,	IMMUNOGLOBULIN FOLD,
									D;”	GLYCOPROTEIN”
426	1fl1	A	32	213	6.40E−13	0.06	−0.02		“F124 IMMUNOGLOBULIN	“IMMUNE SYSTEM IMMUNOGLOBULIN,
									(KAPPA LIGHT CHAIN);	ANTIBODY, FAB, HEPATITIS B, PRES2”
									CHAIN: A, C; F124
									IMMUNOGLOBULIN (IGG1
									HEAVY CHAIN); CHAIN: B,
									D;”
426	1f58	L	32	213	1.10E−12	−0.04	0.01		IGG1 ANTIBODY 58.2	“IMMUNE SYSTEM FAB 58.2; FAB 58.2; V3
									(LIGHT CHAIN); CHAIN: L;	LOOP; IMMUNOGLOBULIN, FAB, HIV-1,
									IGG1 ANTIBODY 58.2	GP120, V3, IMMUNE SYSTEM”
									(HEAVY CHAIN); CHAIN: H;
									EXTERIOR MEMBRANE
									GLYCOPROTEIN(GP120);
									CHAIN: P;
426	1f58	H	31	251	4.80E−08			51.35	IGG1 ANTIBODY 58.2	“IMMUNE SYSTEM FAB 58.2; FAB 58.2; V3
									(LIGHT CHAIN); CHAIN: L;	LOOP; IMMUNOGLOBULIN, FAB, HIV-1,
									IGG1 ANTIBODY 58.2	GP120, V3, IMMUNE SYSTEM”
									(HEAVY CHAIN); CHAIN: H;
									EXTERIOR MEMBRANE
									GLYCOPROTEIN(GP120);
									CHAIN: P;
426	1fc2	D	29	222	3.20E−41	−0.12	0.19			IMMUNOGLOBULIN IMMUNOGLOBULIN
										FC AND FRAGMENT B OF PROTEIN A
										COMPLEX 1FC2 4
426	1fhg	A	28	125	4.80E−15	0.38	0.04		TELOKIN; CHAIN: A	“CONTRACTILE PROTEIN
										IMMUNOGLOBULIN FOLD, BETA
										BARREL”
426	1igt	B	29	220	1.60E−33	0.07	−0.07		“IGG2A INTACT ANTIBODY-	“IMMUNOGLOBULIN INTACT
									MAB231; CHAIN: A, B, C,	IMMUNOGLOBULIN V REGION C
									D”	REGION, IMMUNOGLOBULIN”
426	1lil	A	25	228	6.40E−15			52.92	“LAMBDA III BENCE JONES	“IMMUNOGLOBULIN
									PROTEIN CLE; CHAIN: A, B”	IMMUNOGLOBULIN, BENCE JONES
										PROTEIN”
426	1mco	H	29	222	3.20E−41	−0.11	0.06			IMMUNOGLOBULIN IMMUNOGLOBULIN
										G1 (IGG1) (MCG) WITH A HINGE
										DELETION 1MCO 3
426	1nct		33	124	6.40E−13	0.2	−0.15		TITIN; CHAIN: NULL;	“MUSCLE PROTEIN CONNECTIN,
										NEXTM5; CELL ADHESION,
										GLYCOPROTEIN, TRANSMEMBRANE,
										REPEAT, BRAIN, 2 IMMUNOGLOBULIN
										FOLD, ALTERNATIVE SPLICING, SIGNAL,
										3 MUSCLE PROTEIN”
426	1tnm		33	124	6.40E−13	0.26	−0.13			“MUSCLE PROTEIN TITIN MODULE M5
										(CONNECTIN) 1TNM 3 (NMR, MINIMIZED
										AVERAGE STRUCTURE) 1TNM 4 1TNM 58”
426	8fab	A	37	221	1.60E−15	0.16	0.71			“IMMUNOGLOBULIN FAB FRAGMENT
										FROM HUMAN IMMUNOGLOBULIN IGG1
										(LAMBDA, HIL) 8FAB 3”
431	1sac	A	150	355	3.40E−19			66.32		AMYLOID PROTEIN SERUM AMYLOID P
										COMPONENT (SAP) 1SAC 3
432	1bu7	A	39	499	6.80E−68	0.49	1		“CYTOCHROME P450;	“OXIDOREDUCTASE FATTY ACID
									CHAIN: A, B;”	HYDROXYLASE; FATTY ACID
										MONOOXYGENASE, HEMOPROTEIN, P450
										REMARK”
432	1bu7	A	34	499	6.80E−68			191.84	“CYTOCHROME P450;	“OXIDOREDUCTASE FATTY ACID
									CHAIN: A, B;”	HYDROXYLASE; FATTY ACID
										MONOOXYGENASE, HEMOPROTEIN, P450
										REMARK”
432	1cpt		236	460	3.40E−20	−0.68	0			OXIDOREDUCTASE(OXYGENASE)
										CYTOCHROME P450-TERP 1CPT 3
432	1dt6	A	38	495	0	0.56	1		CYTOCHROME P450 2C5;	“OXIDOREDUCTASE PROGESTERONE 21-
									CHAIN: A;	HYDROXYLASE, CYPIIC5 P450 1,
										MEMBRANE PROTEIN, PROGESTERONE
										21-HYDROXYLASE, BENZO(A) 2 PYRENE
										HYDROXYLASE, ESTRADIOL 2-
										HYDROXYLASE, P450, CYP2C5”
432	1f26	A	58	463	2.10E−72	0.39	1		NITRIC OXIDE REDUCTASE;	“OXIDOREDUCTASE NITRIC OXIDE
									CHAIN: A;	REDUCTASE, CYTOCHROME P450NOR”
432	1f26	A	128	463	6.80E−20	−0.11	0.63		NITRIC OXIDE REDUCTASE;	“OXIDOREDUCTASE NITRIC OXIDE
									CHAIN: A;	REDUCTASE, CYTOCHROME P450NOR”
432	1f4t	A	69	494	8.40E−71	0.09	1		“CYTOCHROME P450 119;	OXIDOREDUCTASE CYP119; P450 FOLD
									CHAIN: A, B;”
432	1f4t	A	287	474	3.40E−18	−0.6	0.25		“CYTOCHROME P450 119;	OXIDOREDUCTASE CYP119; P450 FOLD
									CHAIN: A, B;”
432	1oxa		70	463	8.50E−27	0.11	1		CYTOCHROME P450 ERYF;	OXIDOREDUCTASE (OXYGENASE)
									1OXA 5 CHAIN: NULL 1OXA 6
432	1oxa		15	494	8.50E−27			96.86	CYTOCHROME P450 ERYF;	OXIDOREDUCTASE (OXYGENASE)
									1OXA 5 CHAIN: NULL 1OXA 6
432	1qmq	A	245	473	5.10E−11	−0.63	0		CYTOCHROME P450;	“OXIDOREDUCTASE CAMPHOR 5-
									CHAIN: A;	MONOOXYGENASE
										OXIDOREDUCTASE(OXYGENASE), RU-
										SUBSTRATE,”
433	1am5		95	438	0	0.93	1		PEPSIN; CHAIN: NULL;	“ASPARTYL PROTEASE ACID
										PROTEINASE; ASPARTYL PROTEASE,
										ACID PROTEINASE, HYDROLASE”
433	1am5		94	438	0			303.61	PEPSIN; CHAIN: NULL;	“ASPARTYL PROTEASE ACID
										PROTEINASE; ASPARTYL PROTEASE,
										ACID PROTEINASE, HYDROLASE”
433	1dpj	A	93	437	0	0.61	1		PROTEINASE A; CHAIN: A;	“HYDROLASE/HYDROLASE INHIBITOR
									PROTEINASE INHIBITOR	ASPARTATE PROTEASE; IA3;
									IA3 PEPTIDE; CHAIN: B;	PROTEINASE A, IA3 PEPTIDE”
433	1hrn	A	91	437	0	0.75	1			ASPARTIC PROTEINASE RENIN
										COMPLEXED WITH
										POLYHYDROXYMONOAMIDE INHIBITOR
										BILA 980 1HRN 3
433	1hrn	A	91	438	0			337.47		ASPARTIC PROTEINASE RENIN
										COMPLEXED WITH
										POLYHYDROXYMONOAMIDE INHIBITOR
										BILA 980 1HRN 3
433	1htr	B	102	438	0	0.73	1			ASPARTYL PROTEASE PROGASTRICSIN
										(PEPSINOGEN C) (E.C.3.4.23.3) 1HTR 3
										1HTR 87
433	1htr	B	94	438	0			298.52		ASPARTYL PROTEASE PROGASTRICSIN
										(PEPSINOGEN C) (E.C.3.4.23.3) 1HTR 3
										1HTR 87
433	1lya	B	198	438	6.80E−96	0.85	1			LYSOSOMAL ASPARTIC PROTEASE
										CATHEPSIN D (E.C.3.4.23.5) 1LYA 3
433	1lya	A	94	189	4.20E−35	0.26	0.94			LYSOSOMAL ASPARTIC PROTEASE
										CATHEPSIN D (E.C.3.4.23.5) 1LYA 3
433	1lya	A	93	197	1.50E−33	−0.19	0.93			LYSOSOMAL ASPARTIC PROTEASE
										CATHEPSIN D (E.C.3.4.23.5) 1LYA 3
433	1lya	B	198	438	6.80E−96			412.02		LYSOSOMAL ASPARTIC PROTEASE
										CATHEPSIN D (E.C.3.4.23.5) 1LYA 3
433	1lya	A	93	189	4.20E−35			168.02		LYSOSOMAL ASPARTIC PROTEASE
										CATHEPSIN D (E.C.3.4.23.5) 1LYA 3
433	1qdm	A	43	353	3.40E−89	0.29	0.98		“PROPHYTEPSIN; CHAIN: A,	“HYDROLASE ASPARTIC PROTEINASES,
									B, C;”	PHYTEPSIN, SAPOSIN-LIKE DOMAIN, 2
										ZYMOGEN STRUCTURE, HYDROLASE”
433	1qdm	A	58	438	3.40E−89			290.18	“PROPHYTEPSIN; CHAIN: A,	“HYDROLASE ASPARTIC PROTEINASES,
									B, C;”	PHYTEPSIN, SAPOSIN-LIKE DOMAIN, 2
										ZYMOGEN STRUCTURE, HYDROLASE”
433	1qrp	E	94	438	0	1	1		PEPSIN 3A; CHAIN: E; IVA-	“HYDROLASE/HYDROLASE INHIBITOR
									VAL-VAL-LEU(P)-(O)PHE-	ASPARTIC PROTEINASE, PHOSPHONATE
									ALA-ALA-OME; CHAIN: I;	INHIBITOR, TRANSITION 2 STATE
										ANALOGUE”
433	1qrp	E	95	438	0			325.28	PEPSIN 3A; CHAIN: E; IVA-	“HYDROLASE/HYDROLASE INHIBITOR
									VAL-VAL-LEU(P)-(O)PHE-	ASPARTIC PROTEINASE, PHOSPHONATE
									ALA-ALA-OME; CHAIN: I;	INHIBITOR, TRANSITION 2 STATE
										ANALOGUE”
433	1smr	A	96	437	0	0.86	1			HYDROLASE(ASPARTIC PROTEINASE)
										RENIN (E.C.3.4.23.15) COMPLEX WITH
										THE INHIBITOR CH-66 1SMR 3
433	1smr	A	89	438	0			346.22		HYDROLASE(ASPARTIC PROTEINASE)
										RENIN (E.C.3.4.23.15) COMPLEX WITH
										THE INHIBITOR CH-66 1SMR 3
433	3cms		94	437	0	0.96	1			HYDROLASE (ACID PROTEINASE)
										CHYMOSIN B (FORMERLY KNOWN AS
										RENNIN) (E.C.3.4.23.4) MUTANT 3CMS 3
										WITH VAL 111 REPLACED BY PHE
										(/V111F$) 3CMS 4
433	3cms		93	438	0			292.24		HYDROLASE (ACID PROTEINASE)
										CHYMOSIN B (FORMERLY KNOWN AS
										RENNIN) (E.C.3.4.23.4) MUTANT 3CMS 3
										WITH VAL 111 REPLACED BY PHE
										(/V111F$) 3CMS 4
433	3psg		22	438	0	0.68	1			HYDROLASE(ACID PROTEINASE
										ZYMOGEN) PEPSINOGEN 3PSG 3
433	3psg		58	438	0			329.87		HYDROLASE(ACID PROTEINASE
										ZYMOGEN) PEPSINOGEN 3PSG 3
433	4pep		95	438	0	1.05	1			HYDROLASE (ACID PROTEINASE) PEPSIN
										(E.C.3.4.23.1) 4PEP 4
433	4pep		95	438	0			330.33		HYDROLASE (ACID PROTEINASE) PEPSIN
										(E.C.3.4.23.1) 4PEP 4
434	1a4j	L	32	238	5.10E−26			56.92	“IMMUNOGLOBULIN, DIELS	“IMMUNOGLOBULIN
									ALDER CATALYTIC	IMMUNOGLOBULIN, ANTIBODY,
									ANTIBODY; CHAIN: L, H, A,	CATALYTIC ANTIBODY, DIELS ALDER, 2
									B;”	GERMLINE”
434	1ad9	L	33	240	8.50E−27			53.79	“FAB FRAGMENT CTM01;	“IMMUNOGLOBULIN
									CHAIN: L, H, A, B;”	IMMUNOGLOBULIN, FAB FRAGMENT”
434	1ai1	L	32	248	6.80E−30			53.92	“FAB59.1; CHAIN: L, H;	“COMPLEX (ANTIBODY/PEPTIDE)
									AIB142; CHAIN: P;”	COMPLEX (ANTIBODY/PEPTIDE),
										ANTIBODY, CONSTRAINED HIV-1 V3 2
										LOOP PEPTIDE, IMMUNOGLOBULIN”
434	1b2w	L	33	240	1.70E−30			56.41	ANTIBODY (LIGHT CHAIN);	“IMMUNE SYSTEM IMMUNOGLOBULIN;
									CHAIN: L; ANTIBODY	IMMUNOGLOBULIN ANTIBODY
									(HEAVY CHAIN); CHAIN: H;	ENGINEERING, HUMANIZED AND
										CHIMERIC ANTIBODY, FAB, 2 X-RAY
										STRUCTURE, THREE−DIMENSIONAL
										STRYCTURE, GAMMA-3 INTERFERON,
										IMMUNE SYSTEM”
434	1b4j	L	33	240	8.50E−29			55.89	“ANTIBODY; CHAIN: L, H;”	“ANTIBODY ENGINEERING ANTIBODY
										ENGINEERING, HUMANIZED AND
										CHIMERIC ANTIBODIES, 2 FAB, X-RAY
										STRUCTURES, GAMMA-INTERFERON”
434	1bj1	L	33	239	5.10E−31			54.13	“FAB FRAGMENT; CHAIN: L,	“COMPLEX (ANTIBODY/ANTIGEN) FAB-
									H, J, K; VASCULAR	12; VEGF; COMPLEX
									ENDOTHELIAL GROWTH	(ANTIBODY/ANTIGEN), ANGIOGENIC
									FACTOR; CHAIN: V, W;”	FACTOR”
434	1bjm	A	34	250	1.20E−27			55.03	“LOC-LAMBDA 1 TYPE	“IMMUNOGLOBULIN BENCE-JONES
									LIGHT-CHAIN DIMER; 1BJM	PROTEIN; 1BJM 8 BENCE JONES,
									6 CHAIN: A, B; 1BJM 7”	ANTIBODY, MULTIPLE QUATERNARY
										STRUCTURES 1BJM 13”
434	1bog	A	33	240	1.00E−28			55.49	“ANTIBODY (CB 4-1);	“COMPLEX (ANTIBODY/PEPTIDE)
									CHAIN: A, B; PEPTIDE;	POLYSPECIFICITY, CROSS REACTIVITY,
									CHAIN: C;”	FAB-FRAGMENT, PEPTIDE, 2 HIV-1,
										COMPLEX (ANTIBODY/PEPTIDE)”
434	1ce1	L	33	237	3.40E−29			56.56	CAMPATH-1H: LIGHT	“ANTIBODY THERAPEUTIC, ANTIBODY,
									CHAIN; CHAIN: L;	CD52”
									CAMPATH-1H: HEAVY
									CHAIN; CHAIN: H; PEPTIDE
									ANTIGEN; CHAIN: P;
434	1cly	L	31	240	6.80E−27			55.41	“IGG FAB (HUMAN IGG1,	“IMMUNOGLOBULIN CBR96 FAB
									KAPPA); CHAIN: L, H;”	(IMMUNOGLOBULIN);
										IMMUNOGLOBULIN, IMMUNOGLOBULIN
										C REGION, GLYCOPROTEIN, ANTIB”
434	1clz	L	29	240	6.80E−28			54.08	“IGG FAB (IGG3, KAPPA);	“IMMUNOGLOBULIN MBR96 FAB
									CHAIN: L, H;”	(IMMUNOGLOBULIN);
										IMMUNOGLOBULIN C REGION,
										GLYCOPROTEIN, TRANSMEMBRANE”
434	1dfb	L	33	240	1.20E−29			54.53		IMMUNOGLOBULIN 3D6 FAB 1DFB 3
434	1fgn	L	33	240	1.20E−29			54.11	“IMMUNOGLOBULIN FAB	“IMMUNOGLOBULIN FAB, FAB LIGHT
									5G9; CHAIN: L, H;”	CHAIN, FAB HEAVY CHAIN; ANTIBODY,
										FAB, ANTI-TF, MONOCLONAL, MURINE,
										IMMUNOGLOBULIN”
434	1fvd	A	33	240	1.70E−30			60.53		“IMMUNOGLOBULIN FAB FRAGMENT OF
										HUMANIZED ANTIBODY 4D5, VERSION 4
										1FVD 3”
434	1gcl	L	33	237	3.40E−29			54.38	“ENVELOPE PROTEIN	“COMPLEX (HIV ENVELOPE
									GP120; CHAIN: G; CD4;	PROTEIN/CD4/FAB) COMPLEX (HIV
									CHAIN: C; ANTIBODY 17B;	ENVELOPE PROTEIN/CD4/FAB), HIV-1
									CHAIN: L, H;”	EXTERIOR 2 ENVELOPE GP 120, T-CELL
										SURFACE GLYCOPROTEIN CD4, 3
										ANTIGEN-BINDING FRAGMENT OF
										HUMAN IMMUNOGLOBULIN 17B, 4
										GLYCOSYLATED PROTEIN”
434	1mim	L	32	239	5.10E−28			54.32	“CHIMERIC SDZ CHI621;	“IMMUNOGLOBULIN
									CHAIN: H, L;”	IMMUNOGLOBULIN, C REGION”
434	1vca	A	33	243	4.20E−11			64.99	“HUMAN VASCULAR CELL	“CELL ADHESION PROTEIN VCAM-D1, 2;
									ADHESION MOLECULE-1;	1VCA 6 IMMUNOGLOBULIN
									1VCA 4 CHAIN: A, B; 1VCA	SUPERFAMILY, INTEGRIN-BINDING
									5”	1VCA 15”
434	2fb4	L	32	250	1.70E−26			55.72		IMMUNOGLOBULIN IMMUNOGLOBULIN
									FAB 2FB4 4
434	2fgw	L	33	240	3.40E−31			54.51		IMMUNOGLOBULIN FAB FRAGMENT OF
										A HUMANIZED VERSION OF THE ANTI-
										CD18 2FGW3 ANTIBODY ‘H52’ (HUH52-OZ
										FAB) 2FGW 4
434	2mcg	1	33	250	3.40E−29			58.41		IMMUNOGLOBULIN IMMUNOGLOBULIN
										LAMBDA LIGHT CHAIN DIMER (/MCG$)
										2MCG 3 (TRIGONAL FORM) 2MCG 4
434	3fct	A	33	239	3.40E−28			55.8	“METAL CHELATASE	“IMMUNE SYSTEM METAL CHELATASE,
									CATALYTIC ANTIBODY;	CATALYTIC ANTIBODY, FAB
									CHAIN: A, C; METAL	FRAGMENT, IMMUNE 2 SYSTEM”
									CHELATASE CATALYTIC
									ANTIBODY; CHAIN: B, D;”
440	1c0p	A	27	61	0.00017	−0.31	0.18		D-AMINO ACID OXIDASE;	“OXIDOREDUCTASE ALPHA-BETA-
									CHAIN: A;	ALPHA MOTIF, FLAVIN CONTAINING
										PROTEIN, OXIDASE”
440	1cjc	A	33	397	1.70E−09	−0.15	0.03		ADRENODOXIN	“OXIDOREDUCTASE ADR, NADPH:
									REDUCTASE; CHAIN: A;	ADRENODOXIN OXIDOREDUCTASE;
										FLAVOENZYME, MAD ANALYSIS,
										ELECTRON TRANSFERASE”
440	1d4d	A	32	67	3.40E−09	−0.13	0.12		FLAVOCYTOCHROME C	“OXIDOREDUCTASE TETRAHEME
									FUMARATE REDUCTASE;	FLAVOCYTOCHROME C FUMARATE
									CHAIN: A;	REDUCTASE, 2 OXIDOREDUCTASE”
440	1djn	A	28	429	1.00E−13	−0.01	0.27		“TRIMETHYLAMINE	“OXIDOREDUCTASE IRON-SULFUR
									DEHYDROGENASE; CHAIN:	FLAVOPROTEIN, ELECTRON TRANSFER,
									A, B;”	OXIDOREDUCTASE”
440	1el5	A	28	60	8.50E−07	−0.05	0.43		“SARCOSINE OXIDASE;	“OXIDOREDUCTASE FLAVOPROTEIN,
									CHAIN: A, B;”	OXIDASE”
440	1fum	A	32	61	0.00017	−0.49	0.05		“FUMARATE REDUCTASE	“OXIDOREDUCTASE COMPLEX II;
									FLAVOPROTEIN SUBUNIT;	COMPLEX II; COMPLEX II; COMPLEX II;
									CHAIN: A, M; FUMARATE	FUMARATE REDUCTASE, COMPLEX II,
									REDUCTASE IRON-SULFUR	SUCCINATE DEHYDROGENASE, 2
									PROTEIN; CHAIN: B, N;	RESPIRATION, OXIDOREDUCTASE”
									FUMARATE REDUCTASE 15
									KD HYDROPHOBIC
									PROTEIN; CHAIN: C, O;
									FUMARATE REDUCTASE 13
									KD HYDROPHOBIC
									PROTEIN; CHAIN: D, P;”
440	1ges	A	30	542	0			70.22		“OXIDOREDUCTASE(FLAVOENZYME)
										GLUTATHIONE REDUCTASE (E.C.1.6.4.2)
										NAD MUTANT WITH ALA 179 1GES 3
										REPLACED BY GLY, ALA 183 BY GLY,
										VAL 197 BY GLU, ARG 198 BY 1GES 4
										MET, LYS 199 BY PHE, HIS 200 BY ASP,
										AND ARG 204 BY PHE 1GES 5
										(A179G, A183G, V197E, R198M, K199F, H200D,
										R204P) COMPLEXED WITH 1GES 6 NAD
										1GES 7”
440	1lpf	A	28	560	0	−0.3	0			OXIDOREDUCTASE DIHYDROLIPOAMIDE
										DEHYDROGENASE (E.C.1.8.1.4) COMPLEX
										WITH 1LPF 3 FLAVIN-ADENINE-
										DINUCLEOTIDE (FAD) 1LPF 4
440	1pbe		27	62	0.00068	−0.25	0.04			OXIDOREDUCTASE P-
										HYDROXYBENZOATE HYDROXYLASE
										(PHBH) (E.C.1.14.13.2) 1PBE 3 COMPLEXED
										WITH P-HYDROXYBENZOIC ACID 1PBE 4
440	1qjd	A	32	423	8.50E−09	0.03	0.37		FLAVOCYTOCHROME C3;	“FUMARATE REDUCTASE FUMARATE
									CHAIN: A	REDUCTASE, RESPIRATORY FUMARATE
										REDUCTASE”
440	1qo8	A	33	185	1.70E−07	−0.08	0.8		“FLAVOCYTOCHROME C3	OXIDOREDUCTASE OXIDOREDUCTASE
									FUMARATE REDUCTASE;
									CHAIN: A, D;”
440	1trb		28	413	1.20E−56	−0.16	0.68			OXIDOREDUCTASE (FLAVOENZYME)
										THIOREDOXIN REDUCTASE (E.C.1.6.4.5)
										MUTANT WITH CYS 138 1TRB 3
										REPLACED BY SER (C138S) 1TRB 4
440	1vdc		32	412	1.20E−50	0.01	0.17		NADPH DEPENDENT	“OXIDOREDUCTASE NTR;
									THIOREDOXIN	HYPOTHETICAL PROTEIN, REDOX-
									REDUCTASE; CHAIN: NULL;	ACTIVE CENTER, OXIDOREDUCTASE, 2
										DISULFIDE OXIDOREDUCTASE,
										THIOREDOXIN REDUCTASE, FLAVIN 3
										ADENINE DINULEOTIDE”
440	3grs		28	548	0			78.44		“OXIDOREDUCTASE (FLAVOENZYME)
										GLUTATHIONE REDUCTASE (E.C.1.6.4.2),
										OXIDIZED FORM (E) 3GRS 4”
441	1bxk	A	94	397	8.40E−67	0.67	1		“DTDP-GLUCOSE 4,6-	“LYASE EPIMERASE, DEHYDRATASE,
									DEHYDRATASE; CHAIN: A,	DEHYDROGENASE, LYASE”
									B;”
441	1bxk	A	93	412	8.40E−67			150.09	“DTDP-GLUCOSE 4,6-	“LYASE EPIMERASE, DEHYDRATASE,
									DEHYDRATASE; CHAIN: A,	DEHYDROGENASE, LYASE”
									B;”
441	1db3	A	94	404	1.40E−68	0.54	1		“GDP-MANNOSE 4,6-	“LYASE DEHYDRATASE, NADP, GDP-
									DEHYDRATASE; CHAIN: A;”	MANNOSE, GDP-FUCOSE”
441	1db3	A	93	424	1.40E−68			97.96	“GDP-MANNOSE 4,6-	“LYASE DEHYDRATASE, NADP, GDP-
									DEHYDRATASE; CHAIN: A;”	MANNOSE, GDP-FUCOSE”
441	1ek6	A	94	398	5.60E−66	0.43	1		“UDP-GALACTOSE 4-	“ISOMERASE EPIMERASE, SHORT-CHAIN
									EPIMERASE; CHAIN: A, B;”	DEHYDROGENASE, GALACTOSEMIA”
445	1ile		6	55	0.0085	−0.9	0.06		ISOLEUCYL-TRNA	AMINOACYL-TRNA SYNTHETASE ILERS;
									SYNTHETASE; CHAIN:	AMINOACYL-TRNA SYNTHETASE
									NULL;
450	1alh	A	239	320	4.20E−45	0.34	1		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
450	1alh	A	295	376	4.20E−43	0.13	0.98		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
450	1alh	A	267	348	6.30E−43	0.2	1		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
450	1alh	A	435	516	4.20E−42	0.26	0.98		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
450	1alh	A	407	488	1 .30E−38	0.27	1		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
450	1alh	A	519	627	6.30E−38	−0.18	0.21		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
450	1alh	A	267	349	4.20E−45			81.01	“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
450	1ard		407	435	1.90E−10	0.36	0.82			“TRANSCRIPTION REGULATION YEAST
										TRANSCRIPTION FACTOR ADR1
										(RESIDUES 102-130) 1ARD 3 (AMINO
										TERMINAL ZINC FINGER DOMAIN) (NMR,
										10 STRUCTURES) 1ARD 4 (ADR1B) 1ARD
										5”
450	1ard		575	603	1.30E−09	−0.36	0.05			“TRANSCRIPTION REGULATION YEAST
										TRANSCRIPTION FACTOR ADR1
										(RESIDUES 102-130) 1ARD 3 (AMINO
										TERMINAL ZINC FINGER DOMAIN) (NMR,
										10 STRUCTURES) 1ARD 4 (ADR1B) 1ARD
										5”
450	1ard		547	575	2.10E−07	0.02	0.11			“TRANSCRIPTION REGULATION YEAST
										TRANSCRIPTION FACTOR ADR1
										(RESIDUES 102-130) 1ARD 3 (AMINO
										TERMINAL ZINC FINGER DOMAIN) (NMR,
										10 STRUCTURES) 1ARD 4 (ADR1B) 1ARD
										5”
450	1ubd	C	236	347	4.20E−54	0.31	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
450	1ubd	C	461	571	1.90E−53	−0.1	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
450	1ubd	C	488	628	8.40E−52	−0.33	0.52		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
450	1ubd	C	320	431	8.40E−51	0.18	0.99		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
450	1ubd	C	376	515	1.50E−49	−0.04	0.66		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
450	1ubd	C	348	460	1.30E−48	−0.19	0.99		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
450	1ubd	C	185	291	2.10E−46	0.06	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
450	1ubd	C	266	376	4.20E−54			87.98	“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
450	2gli	A	238	377	4.20E−71	0.32	1		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
450	2gli	A	350	517	8.40E−69	−0.04	0.96		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
450	2gli	A	266	432	4.20E−67	−0.34	0.95		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
450	2gli	A	406	572	1.10E−66	0.05	0.96		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
450	2gli	A	183	321	6.30E−63	0.18	0.98		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
450	2gli	A	462	628	4.20E−51	−0.01	0.57		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
450	2gli	A	103	265	2.10E−24	−0.47	0.06		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
450	2gli	A	238	377	4.20E−71			97.21	“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
450	3znf		547	575	0.0063	0.51	0.4			ZINC FINGER /DNA$ BINDING DOMAIN
										ZINC FINGER (/NMR$) 3ZNF 3
455	1chc		137	192	1.50E−05	0.11	0.43			“VIRUS EQUINE HERPES VIRUS-1 (C3HC4,
										OR RING DOMAIN) 1CHC 3 (NMR, 1
										STRUCTURE) 1CHC 4”
455	1dvp	A	142	170	0.0021	−0.12	0.15		HEPATOCYTE GROWTH	“TRANSFERASE HRS; HRS, VHS, FYVE,
									FACTOR-REGULATED	ZINC FINGER, SUPERHELIX”
									TYROSINE CHAIN: A;
455	1rmd		139	192	4.20E−07	−0.04	0.29		RAG1; CHAIN: NULL;	“DNA-BINDING PROTEIN V(D)J
										RECOMBINATION ACTIVATING PROTEIN
										1; RAG1, V(D)J RECOMBINATION,
										ANTIBODY, MAD, RING FINGER, 2 ZINC
										BINUCLEAR CLUSTER, ZINC FINGER,
										DNA-BINDING PROTEIN”
455	1vfy	A	142	170	0.0011	−0.21	0		PHOSPHATIDYLINOSITOL-	“TRANSPORT PROTEIN FYVE DOMAIN,
									3-PHOSPHATE BINDING	ENDOSOME MATURATION,
									FYVE CHAIN: A;	INTRACELLULAR TRAFFICKING, 2
										TRANSPORT PROTEIN”
456	1alh	A	206	287	2.10E−40	0.42	1		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
456	1alh	A	319	399	1.30E−38	0.37	1		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
456	1alh	A	153	230	6.30E−37	0.38	1		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
456	1alh	A	318	398	1.50E−30	0.55	1		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
456	1alh	A	122	202	5.10E−28	0.05	0.55		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
456	1alh	A	206	288	2.10E−40			74.69	“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
456	1mey	C	233	314	5.10E−51	0.5	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
456	1mey	C	261	342	6.80E−51	0.51	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
456	1mey	C	345	426	1.00E−50	0.51	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
456	1mey	C	289	370	1.00E−50	0.32	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
456	1mey	C	317	398	1.70E−50	0.64	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
456	1mey	C	205	286	6.80E−50	0.34	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
456	1mey	C	177	258	1.70E−49	0.59	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
456	1mey	C	149	230	1.50E−47	0.52	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
456	1mey	C	121	202	3.40E−46	0.11	0.92		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
456	1mey	C	373	429	1.00E−33	0.46	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
456	1mey	G	343	370	1.00E−12	0.27	0.99		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
456	1mey	C	317	399	1.00E−50			96.05	“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
456	1tf3	A	122	198	1.70E−18	0.25	−0.11		“TRANSCRIPTION FACTOR	“COMPLEX (TRANSCRIPTION
									IIIA; CHAIN: A; 5S RNA	REGULATION/DNA) TFIIIA; 5S GENE;
									GENE; CHAIN: E, F;”	NMR, TFIIIA, PROTEIN, DNA,
										TRANSCRIPTION FACTOR, 5S RNA 2
										GENE, DNA BINDING PROTEIN, ZINC
										FINGER, COMPLEX 3 (TRANSCRIPTION
										REGULATION/DNA)”
456	1tf6	A	178	323	3.40E−38	0.34	0.95		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
456	1tf6	A	290	428	1.20E−36	−0.17	1		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
456	1tf6	A	122	267	5.10E−36	0.05	0.75		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
456	1tf6	A	233	398	3.40E−38			110.2	“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, B, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
456	1ubd	C	154	258	2.10E−49	0.25	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN; A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
456	1ubd	C	315	426	6.30E−48	0.34	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
456	1ubd	C	294	398	1.70E−35	0.29	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
456	1ubd	C	325	426	8.50E−35	0.27	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
456	1ubd	C	115	202	5.10E−29	−0.23	0.22		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
456	1ubd	C	317	427	6.30E−48			87.65	“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
456	2gli	A	233	400	4.20E−65	0.2	1		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FTNGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
456	2gli	A	205	372	2.10E−63	0.16	1		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
456	2gli	A	177	344	1.90E−62	0	0.88		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
456	2gli	A	153	288	2.10E−60	0	0.93		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
456	2gli	A	317	426	1.30E−46	0.05	0.93		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
456	2gli	A	297	425	1.70E−34	0.52	1		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
456	2gli	A	261	400	4.20E−65			95.99	“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
458	1tub	A	10	94	1.40E−40	−0.25	0.46		“TUBULIN; CHAIN: A, B;”	“MICROTUBULES MICROTUBULES,
										ALPHA-TUBULIN, BETA-TUBULIN,
										GTPASE HELIX”
462	1tub	A	17	82	5.10E−31	−0.43	0.21		“TUBULIN; CHAIN: A, B;”	“MICROTUBULES MICROTUBULES,
										ALPHA-TUBULIN, BETA-TUBULIN,
										GTPASE HELIX”
463	1alh	A	514	595	1.30E−42	0.01	1		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
463	1alh	A	290	370	1.70E−24	0.14	1		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
463	1mey	C	625	706	5.10E−51	0.53	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
463	1mey	C	597	678	6.80E−51	0.46	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
463	1mey	C	569	650	1.20E−50	0.41	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
463	1mey	C	541	622	1.50E−50	0.03	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
463	1mey	C	653	734	1.50E−50	0.47	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
463	1mey	C	681	762	5.10E−50	0.27	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
463	1mey	C	709	790	1.70E−49	0.14	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
463	1mey	C	513	594	3.40E−49	0.22	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
463	1mey	C	485	566	5.10E−49	0.36	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
463	1mey	C	457	538	1.20E−47	0.06	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
463	1mey	C	429	510	8.50E−47	0.35	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
463	1mey	C	401	482	3.40E−46	−0.06	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
463	1mey	C	373	454	8.50E−46	0.33	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
463	1mey	C	184	265	1.00E−44	−0.29	0.24		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
463	1mey	C	345	426	1.70E−44	0.22	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
463	1mey	C	737	814	6.80E−43	0.03	0.57		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
463	1mey	C	317	398	1.40E−42	0.29	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
463	1mey	C	289	370	1.20E−41	0.47	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
463	1mey	C	163	237	3.40E−40	−0.27	0.27		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
463	1mey	C	212	286	3.40E−36	−0.58	0.24		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
463	1mey	C	268	342	1.50E−35	−0.29	0.88		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
463	1mey	G	182	209	1.70E−11	−0.42	0.21		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
463	1mey	G	238	265	1.70E−10	0.12	0.1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
463	1mey	C	681	763	1.50E−50			100.44	“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
463	1tf3	A	290	370	3.40E−17	0.42	0.94		“TRANSCRIPTION FACTOR	“COMPLEX (TRANSCRIPTION
									IIIA; CHAIN: A; 5S RNA	REGULATION/DNA) TFIIIA; 5S GENE;
									GENE; CHAIN: E, F;”	NMR, TFIIIA, PROTEIN, DNA,
										TRANSCRIPTION FACTOR, 5S RNA 2
										GENE, DNA BINDING PROTEIN, ZINC
										FINGER, COMPLEX 3 (TRANSCRIPTION
										REGULATION/DNA)”
463	1tf6	A	598	743	3.40E−38	0.32	0.99		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
463	1tf6	A	654	799	1.40E−36	0.09	1		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
463	1tf6	A	458	603	1.70E−36	−0.07	1		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
463	1tf6	A	346	491	1.70E−34	−0.21	1		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
463	1tf6	A	290	435	3.40E−34	0.17	1		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
463	1tf6	A	682	813	3.40E−32	−0.05	0.99		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
463	1tf6	A	569	731	3.40E−38			101.86	“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
463	1ubd	C	651	762	1.00E−57	0.23	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
463	1ubd	C	511	622	2.10E−55	0.01	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
463	1ubd	C	567	706	6.30E−55	−0.08	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
463	1ubd	C	343	454	1.10E−53	0.36	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
463	1ubd	C	427	538	1.50E−53	−0.09	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
463	1ubd	C	294	398	6.30E−45	−0.2	0.82		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
463	1ubd	C	521	622	1.50E−35	−0.01	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
463	1ubd	C	493	594	1.00E−34	0.29	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
463	1ubd	C	661	762	3.40E−34	0.23	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
463	1ubd	C	686	790	1.50E−33	0.2	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
463	1ubd	C	465	566	1.70E−32	0.11	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
463	1ubd	C	717	815	8.50E−32	−0.41	0.45		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
463	1ubd	C	353	454	1.70E−30	0.11	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
463	1ubd	C	165	265	1.00E−27	−0.45	0.01		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
463	1ubd	C	270	370	1.00E−25	−0.03	0.75		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
463	1ubd	C	243	342	6.80E−24	−0.51	0.05		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
463	1ubd	C	117	209	1.70E−23	−0.69	0.16		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
463	1ubd	C	655	763	1.00E−57			86.42	“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
463	2adr		164	211	6.80E−11	−0.58	0.25		ADR1; CHAIN: NULL;	“TRANSCRIPTION REGULATION
										TRANSCRIPTION REGULATION, ADR1,
										ZINC FINGER, NMR”
463	2adr		241	316	5.10E−09	−0.04	0.68		ADR1; CHAIN: NULL;	“TRANSCRIPTION REGULATION
										TRANSCRIPTION REGULATION, ADR1,
										ZINC FINGER, NMR”
463	2gli	A	597	763	1.50E−73	0.22	1		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
463	2gli	A	569	736	4.20E−71	0.17	1		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
463	2gli	A	373	540	1.30E−69	−0.02	1		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
463	2gli	A	401	596	8.40E−69	−0.05	0.96		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
463	2gli	A	292	428	6.30E−60	0.01	1		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
463	2gli	A	681	804	1.50E−47	0.13	0.77		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
463	2gli	A	465	593	1.70E−35	0.46	1		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
463	2gli	A	661	792	1.50E−33	0.12	1		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
463	2gli	A	521	649	1.70E−33	0.25	0.94		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
463	2gli	A	689	813	1.00E−31	0.08	0.74		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
463	2gli	A	317	453	3.40E−31	0.07	1		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
463	2gli	A	269	400	1.40E−27	−0.08	0.47		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
463	2gli	A	215	369	8.50E−26	−0.02	0.68		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
463	2gli	A	597	736	1.50E−73			90.28	“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
465	1du3	A	54	158	2.10E−09	0.03	−0.11		“DEATH RECEPTOR 5;	“APOPTOSIS TRAIL, DR5, COMPLEX”
									CHAIN: A, B, C, G, H, I; TNF-
									RELATED APOPTOSIS
									INDUCING LIGAND; CHAIN:
									D, E, F, J, K, L;”
465	1dx5	I	19	107	2.10E−07	−0.29	0.16		“THROMBIN LIGHT CHAIN;	“SERINE PROTEINASE COAGULATION
									CHAIN: A, B, C, D;	FACTOR II; COAGULATION FACTOR II;
									THROMBIN HEAVY CHAIN;	FETOMODULIN, TM, CD141 ANTIGEN;
									CHAIN: M, N, O, P;	EGR-CMK SERINE PROTEINASE, EGF-
									THROMBOMODULIN;	LIKE DOMAINS, ANTICOAGULANT
									CHAIN: I, J, K, L; THROMBIN	COMPLEX, 2 ANTIFIBRINOLYTIC
									INHIBITOR L-GLU-L-GLY-L-	COMPLEX”
									ARM; CHAIN: E, F, G, H;”
465	1ext	A	7	168	1.10E−13			57.05	“TUMOR NECROSIS	“SIGNALLING PROTEIN BINDING
									FACTOR RECEPTOR;	PROTEIN, CYTOKINE, SIGNALLING
									CHAIN: A, B;”	PROTEIN”
465	1fvl		24	102	6.30E−08	−0.2	0.06		FLAVORIDIN; 1FVL 4	BLOOD COAGULATION INHIBITOR GP
									CHAIN: NULL IFVL 5	IIB/IIIA ANTAGONIST 1FVL 9
465	1klo		66	221	4.20E−14	0.13	0.01		LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
465	1klo		27	205	4.20E−14			68.79	LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
465	1skz		26	127	6.30E−13	−0.51	0.06		ANTISTASIN; CHAIN: NULL;	“SERINE PROTEASE INHIBITOR FACTOR
										XA INHIBITOR; ANTISTASIN, CRYSTAL
										STRUCTURE, FACTOR XA INHIBITOR, 2
										SERINE PROTEASE INHIBITOR,
										THROMBOSIS”
465	1skz		47	154	4.20E−14			61.73	ANTISTASIN; CHAIN: NULL;	“SERINE PROTEASE INHIBITOR FACTOR
										XA INHIBITOR; ANTISTASIN, CRYSTAL
										STRUCTURE, FACTOR XA INHIBITOR, 2
										SERINE PROTEASE INHIBITOR,
										THROMBOSIS”
465	4mt2		168	221	1.00E−16	0	−0.15			METALLOTHIONEIN METALLOTHIONEIN
										ISOFORM II 4MT2 3
466	1alh	A	101	191	3.40E−26	−0.58	0.34		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
466	1alh	A	70	163	1.70E−25	−0.37	0.21		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
466	1alh	A	101	220	8.40E−25	−0.23	0.18		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
466	1mey	C	306	387	1.50E−50	0.49	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
466	1mey	C	194	275	1.50E−50	0.27	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
466	1mey	C	278	359	1.70E−50	0.48	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
466	1mey	C	166	247	1.70E−49	−0.12	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
466	1mey	C	138	219	1.20E−48	−0.31	0.92		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
466	1mey	C	100	191	3.40E−45	0.05	0.69		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
466	1mey	C	41	125	5.10E−42	−0.37	0.13		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
466	1mey	C	69	163	6.80E−42	−0.4	0.84		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
466	1mey	G	98	125	1.70E−11	−0.17	0.82		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
466	1mey	C	306	388	1.50E−50			105.46	“DNA, CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
466	1tf6	A	139	284	1.20E−38	0.27	0.9		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
466	1tf6	A	167	312	1.40E−36	−0.15	0.74		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
466	1tf6	A	70	228	1.70E−34	−0.36	0.25		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
466	1tf6	A	194	359	1.70E−39			107.88	“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
466	1ubd	C	220	331	6.30E−54	0.06	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
466	1ubd	C	192	304	4.20E−53	0.17	0.99		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
466	1ubd	C	248	359	1.70E−52	0.1	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
466	1ubd	C	276	385	2.10E−52	0.19	0.89		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
466	1ubd	C	135	275	4.20E−46	−0.06	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
466	1ubd	C	98	247	8.40E−38	−0.15	0.65		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
466	1ubd	C	174	275	1.70E−34	0.02	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
466	1ubd	C	108	219	1.00E−32	−0.74	0.54		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
466	1ubd	C	80	191	8.50E−32	−0.51	0.19		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
466	1ubd	C	44	163	1.00E−28	−0.25	0.49		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
466	1ubd	C	81	219	2.10E−27	−0.15	0.9		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
466	1ubd	C	224	332	6.30E−54			86.9	“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
466	2adr		101	165	5.10E−13	−0.38	0.42		ADR1; CHAIN: NULL;	“TRANSCRIPTION REGULATION
										TRANSCRIPTION REGULATION, ADR1,
										ZINC FINGER, NMR”
466	2adr		77	127	5.10E−13	−0.51	0.06		ADR1; CHAIN: NULL;	“TRANSCRIPTION REGULATION
										TRANSCRIPTION REGULATION, ADR1,
										ZINC FINGER, NMR”
466	2gli	A	222	361	2.10E−68	0.42	1		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
466	2gli	A	138	305	4.20E−59	0.07	0.96		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
466	2gli	A	101	277	1.30E−55	0.07	1		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
466	2gli	A	250	384	1.10E−52	0.01	0.83		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
466	2gli	A	81	249	2.10E−42	0.01	0.99		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
466	2gli	A	80	221	8.50E−33	−0.14	0.36		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
466	2gli	A	18	162	6.80E−30	−0.43	0.07		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
466	2gli	A	222	361	2.10E−68			98.19	“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
469	1a7a	A	2	113	3.20E−18	0.38	0.19		“S-	“HYDROLASE HYDROLASE, NAD
									ADENOSYLHOMOCYSTEINE	BINDING PROTEIN”
									HYDROLASE; CHAIN: A,
									B;”
469	1dxy		2	114	3.20E−21	−0.11	0.1		D-2-	“OXIDOREDUCTASE D-HICDH, R-HICDH,
									HYDROXYISOCAPROATE	R-2-HYDROXYISOCAPROATE D-2-
									DEHYDROGENASE; CHAIN:	HYDROXYCARBOXYLATE
									NULL;	DEHYDROGENASE, D-LACTATE 2
										DEHYDROGENASE, OXIDOREDUCTASE”
469	1f0y	A	3	113	3.20E−14	0.08	−0.17		“L-3-HYDROXYACYL-COA	OXIDOREDUCTASE HCDH; ABORTIVE
									DEHYDROGENASE; CHAIN:	TERNARY COMPLEX
									A, B;”
469	1gdh	A	2	114	3.20E−17	0.01	0.43			OXIDOREDUCTASE(CHOH (D)-NAD(P) + (A))
										D-GLYCERATE DEHYDROGENASE
										(APO FORM) (E.C.1.1.1.29) 1GDH 3
469	1pgj	A	1	109	4.80E−15	0.02	0.13		“6-PHOSPHOGLUCONATE	“OXIDOREDUCTASE 6PGDH, 6-PGDH;
									DEHYDROGENASE; CHAIN:	OXIDOREDUCTASE, CHOH(D)-NADP + (B)”
									A, B;”
469	1psd	A	2	114	1.60E−20	−0.3	0.1			OXIDOREDUCTASE (NAD(A)) D-3-
										PHOSPHOGLYCERATE
										DEHYDROGENASE
										(PHOSPHOGLYCERATE 1PSD 3
										DEHYDROGENASE) (E.C.1.1.1.95) 1PSD 4
469	2dld	A	3	113	1.40E−23	−0.15	0.12		“D-LACTATE	OXIDOREDUCTASE (CHOH(D)-NAD + (A))
									DEHYDROGENASE; 2DLD 5	R-LACTATE DEHYDROGENASE; 2DLD 7
									CHAIN: A, B; 2DLD 6”
469	2nac	A	1	114	6.40E−20	0.18	0.21			“OXIDOREDUCTASE(ALDEHYDE(D), NAD + (A))
										NAD-DEPENDENT FORMATE
										DEHYDROGENASE (E.C.1.2.1.2) 2NAC 3
										(APO FORM) 2NAC 4”
469	2pgd		3	113	6.40E−16	0.01	−0.15			OXIDOREDUCTASE (CHOH(D)-NADP + (A))
										6-PHOSPHOGLUCONATE
										DEHYDROGENASE (6-PGDH) (E.C.1.1.1.44)
										2PGD 3
470	1alh	A	178	251	8.50E−20	−0.38	0.19		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
470	1mey	C	493	574	6.80E−51	0.7	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
470	1mey	C	465	546	6.80E−51	0.4	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
470	1mey	C	577	658	1.70E−50	0.62	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
470	1mey	C	521	602	1.70E−50	0.29	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
470	1mey	C	605	686	1.70E−50	0.56	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
470	1mey	C	437	518	1.70E−50	0.24	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
470	1mey	C	549	630	3.40E−50	0.3	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)
470	1mey	C	409	490	1.70E−49	0.03	1		DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
470	1mey	C	381	462	5.10E−49	0.18	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
470	1mey	C	353	434	1.50E−48	0.62	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
470	1mey	C	325	406	1.00E−47	0.45	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
470	1mey	C	297	378	8.50E−46	0.51	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
470	1mey	C	254	350	3.40E−41	0.2	0.89		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
470	1mey	C	205	279	1.00E−34	−0.06	0.54		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
470	1mey	G	659	686	1.20E−12	0.57	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
470	1mey	G	203	229	8.50E−07	0.17	0.04		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA”
470	1mey	C	605	687	1.70E−50			100.88	“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
470	1sp1		205	233	0.0037	−0.16	0.04		SP1F3; CHAIN: NULL;	“ZINC FINGER TRANSCRIPTION FACTOR
										SP1; ZINC FINGER, TRANSCRIPTION
										ACTIVATION, SP1”
470	1tf3	A	178	245	5.10E−12	−0.37	0.24		“TRANSCRIPTION FACTOR	“COMPLEX (TRANSCRIPTION
									IIIA; CHAIN: A; 5S RNA	REGULATION/DNA) TFIIIA; 5S GENE;
									GENE; CHAIN: E, F;”	NMR, TFIIIA, PROTEIN, DNA,
										TRANSCRIPTION FACTOR, 5S RNA 2
										GENE, DNA BINDING PROTEIN, ZINC
										FINGER, COMPLEX 3 (TRANSCRIPTION
										REGULATION/DNA)”
470	1tf6	A	494	646	1.00E−37	−0.02	0.99		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
470	1tf6	A	522	668	3.40E−37	0.21	1		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
470	1tf6	A	438	583	8.50E−37	−0.03	0.99		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
470	1tf6	A	326	471	5.10E−36	0.14	0.99		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
470	1tf6	A	550	686	5.10E−36	0.07	1		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
470	1tf6	A	255	415	1.50E−31	0.18	0.39		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
470	1tf6	A	178	331	3.40E−26	−0.19	0.48		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
470	1tf6	A	437	599	1.00E−37			100.76	“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
470	1ubd	C	575	686	6.30E−53	0.29	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
470	1ubd	C	353	462	8.40E−52	0.43	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
470	1ubd	C	463	574	6.30E−51	0.06	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
470	1ubd	C	407	518	4.20E−50	0.19	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
470	1ubd	C	549	658	1.50E−49	0.17	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
470	1ubd	C	295	434	4.20E−46	0.34	0.7		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
470	1ubd	C	585	686	1.70E−34	0.06	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
470	1ubd	C	557	658	5.10E−34	0.13	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
470	1ubd	C	361	462	6.80E−33	0.45	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
470	1ubd	C	299	406	6.80E−32	0.18	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
470	1ubd	C	262	378	1.20E−29	0.13	0.54		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
470	1ubd	C	249	406	2.10E−26	−0.42	0.25		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
470	1ubd	C	185	279	3.40E−24	−0.75	0.18		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
470	1ubd	C	327	435	8.40E−52			85.18	“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
470	2adr		209	253	8.50E−09	0.05	−0.18		ADR1; CHAIN: NULL;	“TRANSCRIPTION REGULATION
										TRANSCRIPTION REGULATION, ADR1,
										ZINC FINGER, NMR”
470	2gli	A	493	660	4.20E−68	0.19	1		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
470	2gli	A	438	603	8.40E−67	0.03	1		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
470	2gli	A	381	520	2.10E−65	0.12	1		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
470	2gli	A	298	435	1.90E−54	0.32	0.99		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
470	2gli	A	529	657	6.80E−34	0.28	1		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
470	2gli	A	557	685	1.00E−33	−0.09	1		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
470	2gli	A	325	461	3.40E−33	0.28	0.78		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
470	2gli	A	232	377	6.80E−28	0.17	0.69		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
470	2gli	A	216	408	1.50E−26	−0.2	0.13		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
470	2gli	A	325	464	2.10E−65			87.39	“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
471	1a05	A	56	395	1.40E−92	0.3	1		“3-ISOPROPYLMALATE	“OXIDOREDUCTASE IPMDH, IMDH;
									DEHYDROGENASE; CHAIN:	OXIDOREDUCTASE, DECARBOXYLATING
									A, B;”	DEHYDROGENASE, LEUCINE 2
										BIOSYNTHESIS”
471	1a05	A	54	394	1.40E−92			159.71	“3-ISOPROPYLMALATE	“OXIDOREDUCTASE IPMDH, IMDII;
									DEHYDROGENASE; CHAIN:	OXIDOREDUCTASE, DECARBOXYLATING
									A, B;”	DEHYDROGENASE, LEUCINE 2
										BIOSYNTHESIS”
471	1ai2		54	395	8.40E−88	0.44	1		ISOCITRATE	“OXIDOREDUCTASE OXALOSUCCINATE
									DEHYDROGENASE; CHAIN:	DECARBOXYLASE, IDH;
									NULL,	OXIDOREDUCTASE (NAD(A)-CHOH(D)),
										NADP, PHOSPHORYLATION, 2
										GLYOXYLATE BYPASS”
471	1ai2		30	392	8.40E−88			124.43	ISOCITRATE	“OXIDOREDUCTASE OXALOSUCCINATE
									DEHYDROGENASE; CHAIN:	DECARBOXYLASE, IDH;
									NULL;	OXIDOREDUCTASE (NAD(A)-CHOH(D)),
										NADP, PHOSPHORYLATION, 2
										GLYOXYLATE BYPASS”
471	1cm7	A	55	395	1.10E−86	0.4	1		“3-ISOPROPYLMALATE	“OXIDOREDUCTASE IPMDH, IMDH;
									DEHYDROGENASE; CHAIN:	OXIDOREDUCTASE, DEHYDROGENASE,
									A, B;”	NAD-DEPENDANT ENZYME, 2 LEUCINE
										BIOSYNTHETIC PATHWAY”
471	1cm7	A	51	401	1.10E−86			160.94	“3-ISOPROPYLMALATE	“OXIDOREDUCTASE IPMDH, IMDH;
									DEHYDROGENASE; CHAIN:	OXIDOREDUCTASE, DEHYDROGENASE,
									A, B;”	NAD-DEPENDANT ENZYME, 2 LEUCINE
										BIOSYNTHETIC PATHWAY”
471	1idm		57	395	7.00E−90	0.41	1		3-ISOPROPYLMALATE	“OXIDOREDUCTASE IPMDH; 1IDM 7
									DEHYDROGENASE; 1IDM 5	CHIMERA 1IDM 20
									CHAIN: NULL; 1IDM 6
471	1idm		55	396	7.00E−90			165.49	3-ISOPROPYLMALATE	“OXIDOREDUCTASE IPMDH; 1IDM 7
									DEHYDROGENASE; 1IDM 5	CHIMERA 1IDM 20
									CHAIN: NULL; 1IDM 6
471	1xac		57	395	8.40E−87	0.48	1		3-ISOPROPYLMALATE	“OXIDOREDUCTASE IPMDH, IMDH; 1XAC
									DEHYDROGENASE 2T2M6T	10 OXIDOREDUCTASE, CHIMERA 1XAC
									S82R; 1XAC 8 CHAIN: NULL;	21”
									1XAC 9
471	1xac		55	396	8.40E−87			159.36	3-ISOPROPYLMALATE	“OXIDOREDUCTASE IPMDH, IMDH; 1XAC
									DEHYDROGENASE 2T2M6T	10 OXIDOREDUCTASE, CHIMERA 1XAC
									S82R; 1XAC 8 CHAIN: NULL;	21”
									1XAC 9
471	2ayq	A	54	395	1.40E−96	0.63	1		“3-ISOPROPYLMALATE	“OXIDOREDUCTASE OXIDOREDUCTASE,
									DEHYDROGENASE; CHAIN:	3-ISOPROPYLMALATE
									A, B;”	DEHYDROGENASE, LEUCINE 2
										BIOSYNTHESIS, MODERATE
										THERMOPHILE”
471	2ayq	A	54	396	1.40E−96			154.13	“3-ISOPROPYLMALATE	“OXIDOREDUCTASE OXIDOREDUCTASE,
									DEHYDROGENASE; CHAIN:	3-ISOPROPYLMALATE
									A, B;”	DEHYDROGENASE, LEUCINE 2
										BIOSYNTHESIS, MODERATE
										THERMOPHILE”
472	1alh	A	240	320	1.70E−29	−0.15	0.75		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
472	1alh	A	212	292	3.40E−29	−0.22	0.3		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN; B,
									C;”
472	1alh	A	352	460	3.40E−27	0	0.49		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
472	1alh	A	519	594	8.50E−27	−0.27	0.12		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
472	1alh	A	380	490	3.40E−23	−0.37	0.23		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
472	1alh	A	241	349	4.20E−23	−0.04	0.09		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
472	1mey	C	323	404	3.40E−51	0.33	0.99		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
472	1mey	C	295	376	1.00E−50	0.12	0.98		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
472	1mey	C	267	348	3.40E−50	0.14	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
472	1mey	C	239	320	1.20E−49	−0.16	0.96		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
472	1mey	C	211	292	1.00E−48	−0.08	0.78		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
472	1mey	C	183	264	1.20E−45	−0.29	0.04		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
472	1mey	C	518	594	3.40E−44	−0.46	0.06		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
472	1mey	C	351	432	1.00E−42	0.08	0.98		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
472	1mey	C	379	490	3.40E−42	−0.2	0.9		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
472	1mey	C	547	599	3.40E−29	−0.49	0.39		“DNA CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
472	1mey	G	433	460	3.40E−13	0.59	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
472	1mey	C	379	461	1.00E−42			95.61	“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
472	1tf6	A	240	385	6.80E−37	−0.26	0.54		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
472	1tf6	A	184	329	3.40E−35	−0.07	0.05		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
472	1tf6	A	352	497	1.20E−34	−0.23	0.11		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
472	1tf6	A	323	492	1.20E−34			82.32	“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
472	1ubd	C	349	460	6.30E−50	0.32	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
472	1ubd	C	303	404	3.40E−35	0.03	0.83		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
472	1ubd	C	275	376	1.00E−34	−0.09	0.49		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
472	1ubd	C	247	348	1.00E−33	−0.02	0.22		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
472	1ubd	C	219	320	1.40E−33	−0.26	0.58		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
472	1ubd	C	244	404	1.10E−32	−0.48	0.01		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
472	1ubd	C	191	292	1.20E−32	−0.15	0.22		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
472	1ubd	C	359	460	8.50E−29	0.2	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
472	1ubd	C	219	348	6.30E−25	−0.01	0.18		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
472	1ubd	C	527	599	6.80E−22	−0.63	0.16		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
472	1ubd	C	353	461	6.30E−50			75.48	“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
472	2gli	A	325	462	6.30E−64	0.17	0.96		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
472	2gli	A	380	571	1.50E−47	−0.14	0.43		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
472	2gli	A	211	406	1.30E−34	−0.24	0.28		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
472	2gli	A	275	403	1.40E−33	−0.17	0.66		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
472	2gli	A	183	319	1.70E−33	−0.1	0.01		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
472	2gli	A	359	517	6.80E−28	−0.25	0.05		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
472	2gli	A	323	462	6.30E−64			82.53	“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
474	1alh	A	182	262	1.20E−28	−0.3	0.19		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
474	1alh	A	126	206	1.70E−27	−0.37	0.13		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
474	1alh	A	154	234	1.70E−27	0.17	0.65		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
474	1mey	C	265	346	3.40E−51	0	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
474	1mey	C	349	430	1.20E−50	0.25	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
474	1mey	C	293	374	1.20E−50	0.01	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
474	1mey	C	377	458	1.20E−50	0.01	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
474	1mey	C	321	402	1.70E−50	0.38	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
474	1mey	C	237	318	1.70E−50	0.17	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
474	1mey	C	209	290	6.80E−50	0.08	0.98		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
474	1mey	C	181	262	1.20E−47	0.07	0.45		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
474	1mey	C	153	234	6.80E−47	0.2	0.94		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
474	1mey	C	125	206	3.40E−45	−0.52	0.19		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
474	1mey	C	405	461	1.70E−33	0.03	0.99		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
474	1mey	G	291	318	5.10E−13	0.42	0.95		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
474	1mey	C	349	431	1.20E−50			103.69	“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
474	1tf6	A	210	355	5.10E−38	−0.15	0.51		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
474	1tf6	A	322	460	1.70E−36	−0.05	0.8		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
474	1tf6	A	265	430	5.10E−38			117	“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
474	1ubd	C	347	458	1.90E−59	0.29	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
474	1ubd	C	321	430	2.10E−56	−0.01	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
474	1ubd	C	270	402	1.70E−52	−0.16	0.65		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
474	1ubd	C	240	374	2.10E−44	−0.3	0.63		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
474	1ubd	C	179	319	2.10E−40	−0.51	0.07		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
474	1ubd	C	301	402	1.70E−35	−0.22	0.95		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
474	1ubd	C	245	346	5.10E−35	−0.24	0.89		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
474	1ubd	C	357	458	1.70E−34	0.09	0.99		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
474	1ubd	C	189	290	3.40E−34	−0.33	0.24		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
474	1ubd	C	161	262	5.10E−32	−0.36	0.51		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
474	1ubd	C	351	459	1.90E−59			87.13	“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
474	2gli	A	293	459	2.10E−74	0.08	0.96		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
474	2gli	A	154	348	4.20E−53	−0.57	0.18		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
474	2gli	A	153	289	8.50E−34	−0.18	0.66		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
474	2gli	A	245	373	1.20E−33	−0.14	0.81		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
474	2gli	A	329	457	1.70E−33	0.34	0.99		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
474	2gli	A	265	404	2.10E−74			96.72	“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
475	1alh	A	132	240	2.10E−30	−0.25	0.36		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
475	1alh	A	160	240	3.40E−28	−0.17	0.83		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
475	1alh	A	132	212	1.70E−26	−0.21	0.23		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
475	1alh	A	104	184	8.50E−26	0.04	0.17		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
475	1alh	A	80	156	8.50E−20	−0.24	0.17		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
475	1mey	C	299	380	3.40E−51	0.66	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
475	1mey	C	327	408	6.80E−51	0.52	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
475	1mey	C	355	436	8.50E−51	0.45	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
475	1mey	C	411	492	1.20E−50	0.36	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
475	1mey	C	383	464	1.20E−50	0.38	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
475	1mey	C	271	352	1.70E−50	0.48	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
475	1mey	C	243	324	8.50E−50	0.36	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
475	1mey	C	215	296	3.40E−48	0.47	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
475	1mey	C	187	268	1.70E−47	−0.12	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
475	1mey	C	159	240	5.10E−46	−0.28	0.95		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
475	1mey	C	131	212	8.50E−45	−0.05	0.62		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
475	1mey	C	103	184	1.70E−42	0.26	0.76		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
475	1mey	C	439	498	8.50E−36	0.18	0.92		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
475	1mey	C	79	156	1.50E−33	0.08	−0.06		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
475	1mey	C	383	465	8.50E−51			107.97	“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
475	1tf3	A	80	156	1.40E−13	0.02	−0.14		“TRANSCRIPTION FACTOR	“COMPLEX (TRANSCRIPTION
									IIIA; CHAIN: A; 5S RNA	REGULATION/DNA) TFIIIA; 5S GENE;
									GENE; CHAIN: E, F;”	NMR, TFIIIA, PROTEIN, DNA,
										TRANSCRIPTION FACTOR, 5S RNA 2
										GENE, DNA BINDING PROTEIN, ZINC
										FINGER, COMPLEX 3 (TRANSCRIPTION
										REGULATION/DNA)”
475	1tf6	A	244	389	3.40E−38	0.05	0.99		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
475	1tf6	A	328	474	1.00E−37	0.43	1		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
475	1tf6	A	356	494	3.40E−37	0.15	1		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
475	1tf6	A	188	333	5.10E−37	0.17	0.98		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
475	1tf6	A	132	277	1.70E−35	0	0.88		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
475	1tf6	A	80	221	1.70E−30	−0.12	0.01		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
475	1tf6	A	299	467	3.40E−38			120.08	“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
475	1ubd	C	297	408	6.30E−59	0.55	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
475	1ubd	C	381	492	1.00E−57	0.22	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
475	1ubd	C	269	380	1.90E−57	0.25	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
475	1ubd	C	242	352	2.10E−56	0.28	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
475	1ubd	C	353	464	1.90E−55	−0.06	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
475	1ubd	C	192	324	1.50E−49	−0.3	0.18		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
475	1ubd	C	136	268	2.10E−40	−0.3	0.78		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
475	1ubd	C	360	464	3.40E−35	0.2	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
475	1ubd	C	335	436	8.50E−35	0.13	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
475	1ubd	C	167	268	1.70E−32	−0.09	0.95		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
475	1ubd	C	111	212	6.80E−30	−0.08	0.27		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
475	1ubd	C	355	465	1.00E−57			90.92	“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
475	2adr		104	158	3.40E−13	0.08	0.09		ADR1; CHAIN: NULL;	“TRANSCRIPTION REGULATION
										TRANSCRIPTION REGULATION, ADR1,
										ZINC FINGER, NMR”
475	2gli	A	271	410	8.40E−75	0.42	1		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
475	2gli	A	327	466	8.40E−74	0.16	1		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
475	2gli	A	188	326	2.10E−65	0.34	0.87		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
475	2gli	A	383	495	1.50E−56	0.3	0.93		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
475	2gli	A	363	494	6.80E−35	0.24	1		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
475	2gli	A	103	239	8.50E−33	−0.19	0.13		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
475	2gli	A	243	382	8.40E−75			105.12	“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
476	1klo		139	295	1.70E−16			70.8	LAMININ; CHAIN: NULL;	GLYCOPROTEIN GLYCOPROTEIN
476	1skz		63	181	2.10E−13	−0.33	0.34		ANTISTASIN; CHAIN: NULL;	“SERINE PROTEASE INHIBITOR FACTOR
										XA INHIBITOR; ANTISTASIN, CRYSTAL
										STRUCTURE, FACTOR XA INHIBITOR, 2
										SERINE PROTEASE INHIBITOR,
										THROMBOSIS”
476	1skz		88	191	6.30E−12	−0.41	0.04		ANTISTASIN; CHAIN: NULL;	“SERINE PROTEASE INHIBITOR FACTOR
										XA INHIBITOR; ANTISTASIN, CRYSTAL
										STRUCTURE, FACTOR XA INHIBITOR, 2
										SERINE PROTEASE INHIBITOR,
										THROMBOSIS”
476	1skz		179	279	8.40E−12	−0.64	0.09		ANTISTASIN; CHAIN: NULL;	“SERINE PROTEASE INHIBITOR FACTOR
										XA INHIBITOR; ANTISTASIN, CRYSTAL
										STRUCTURE, FACTOR XA INHIBITOR, 2
										SERINE PROTEASE INHIBITOR,
										THROMBOSIS”
476	1vmo	A	25	200	4.20E−21	0.04	−0.18			MEMBRANE PROTEIN VITELLINE
										MEMBRANE OUTER LAYER PROTEIN I
										1VMO 3
476	9wga	A	56	240	3.40E−16			84.52		LECTIN (AGGLUTININ) WHEAT GERM
										AGGLUTININ (ISOLECTIN 2) 9WGA 3
479	1chc		26	84	6.30E−10	0.23	0.21			“VIRUS EQUINE HERPES VIRUS-1 (C3HC4,
										OR RING DOMAIN) 1CHC 3 (NMR, 1
										STRUCTURE) 1CHC 4”
479	1fbv	A	28	92	4.20E−11	−0.06	0.15		SIGNAL TRANSDUCTION	“LIGASE CBL, UBCH7, ZAP-70, E2,
									PROTEIN CBL; CHAIN: A;	UBIQUITIN, E3, PHOSPHORYLATION, 2
									ZAP-70 PEPTIDE; CHAIN: B;	TYROSINE KINASE, UBIQUITINATION,
									UBIQUITIN-CONIUGATING	PROTEIN DEGRADATION,”
									ENZYME E12-18 KDA
									UBCH7; CHAIN: C;
479	1fbv	A	29	69	1.70E−08	0.26	0.53		SIGNAL TRANSDUCTION	“LIGASE CBL, UBCH7, ZAP-70, E2,
									PROTEIN CBL; CHAIN: A;	UBIQITIN, E3, PHOSPHORYLATION, 2
									ZAP-70 PEPTIDE; CHAIN: B;	TYROSINE KINASE, UBIQUITINATION,
									UBIQUITIN-CONJUGATING	PROTEIN DEGRADATION,”
									ENZYME E12-18 KDA
									UBCH7; CHAIN: C;
479	1fre		130	166	1.10E−13	0.07	0.89		NUCLEAR FACTOR XNF7;	“ZINC-BINDING PROTEIN ZINC-BINDING
									CHAIN: NULL;	PROTEIN, XNF7, BBOX, DEVELOPMENT, 3
										MID-BLASTULA-TRANSITION”
479	1fre		130	166	0.00051	0.07	0.89		NUCLEAR FACTOR XNF7;	“ZINC-BINDING PROTEIN ZINC-BINDING
									CHAIN: NULL;	PROTEIN, XNF7, BBOX, DEVELOPMENT, 3
										MID-BLASTULA-TRANSITION”
479	1rmd		16	103	1.30E−18	0.4	0.13		RAG1; CHAIN: NULL;	“DNA-BINDING PROTEIN V(D)J
										RECOMBINATION ACTIVATING PROTEIN
										1; RAG1, V(D)J RECOMBINATION,
										ANTIBODY, MAD, RING FINGER, 2 ZINC
										BINUCLEAR CLUSTER, ZINC FINGER,
										DNA-BINDING PROTEIN”
479	1rmd		29	107	1.70E−12	0.3	−0.07		RAG1; CHAIN: NULL;	“DNA-BINDING PROTEIN V(D)J
										RECOMBINATION ACTIVATING PROTEIN
										1; RAG1, V(D)J RECOMBINATION,
										ANTIBODY, MAD, RING FINGER, 2 ZINC
										BINUCLEAR CLUSTER, ZINC FINGER,
										DNA-BINDING PROTEIN”
479	1rmd		5	136	1.30E−18			54.99	RAG1; CHAIN: NULL;	“DNA-BINDING PROTEIN V(D)J
										RECOMBINATION ACTIVATING PROTEIN
										1; RAG1, V(D)J RECOMBINATION,
										ANTIBODY, MAD, RING FINGER, 2 ZINC
										BINUCLEAR CLUSTER, ZINC FINGER,
										DNA-BINDING PROTEIN”
480	1alh	A	210	290	6.80E−29	0.38	0.96		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
480	1alh	A	188	262	6.80E−23	−0.21	0.13		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
480	1mey	C	321	402	1.40E−50	0.19	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
480	1mey	C	349	430	1.40E−50	0.24	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
480	1mey	C	377	458	1.70E−50	0.17	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
480	1mey	C	433	514	1.70E−50	0.52	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
480	1mey	C	405	486	3.40E−50	0.42	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
480	1mey	C	293	374	8.50E−50	0.75	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
480	1mey	C	461	542	1.20E−49	0.54	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
480	1mey	C	265	346	6.80E−49	0.47	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
480	1mey	C	237	318	5.10E−48	0.54	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
480	1mey	C	209	290	6.80E−47	0.32	1		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
480	1mey	C	187	262	1.70E−40	0.08	0.74		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
480	1mey	C	161	234	5.10E−36	−0.51	0.03		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
480	1mey	C	111	184	6.80E−35	−0.15	0.03		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
480	1mey	C	405	487	1.70E−50			95.91	“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
480	1sp2		518	544	3.40E−07	0.23	0.7		SP1F2; CHAIN: NULL;	“ZINC FINGER TRANSCRIPTION FACTOR
										SP1; ZINC FINGER, TRANSCRIPTION
										ACTIVATION, SP1”
480	1tf6	A	350	502	1.70E−38	0.15	0.93		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
480	1tf6	A	238	383	1.70E−37	0.16	0.96		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
480	1tf6	A	406	544	8.50E−37	0.38	1		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
480	1tf6	A	188	327	3.40E−34	0.22	0.33		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
480	1tf6	A	89	248	1.70E−25	−0.53	0		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
480	1tf6	A	319	486	1.70E−38			105.3	“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
480	1ubd	C	319	459	2.10E−52	0.05	0.74		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
480	1ubd	C	242	347	4.20E−51	−0.02	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
480	1ubd	C	431	543	4.20E−51	0.52	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
480	1ubd	C	404	514	4.20E−50	0.06	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
480	1ubd	C	291	403	8.40E−50	0.28	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
480	1ubd	C	214	318	8.40E−47	0.1	0.87		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
480	1ubd	C	329	430	3.40E−36	0.45	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
480	1ubd	C	385	486	8.50E−35	0.22	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
480	1ubd	C	245	346	3.40E−34	0.27	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
480	1ubd	C	217	318	1.70E−33	0.12	0.86		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
480	1ubd	C	441	542	1.70E−33	0.48	1		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
480	1ubd	C	163	290	1.70E−30	−0.15	0.03		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
480	1ubd	C	295	403	2.10E−52			88.54	“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
480	2gli	A	265	432	4.20E−66	0.02	0.94		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
480	2gli	A	349	516	2.10E−65	0.2	0.98		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
480	2gli	A	187	376	1.90E−60	0	0.66		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
480	2gli	A	329	457	8.50E−35	0.42	1		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
480	2gli	A	413	544	3.40E−34	0.42	1		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
480	2gli	A	209	345	3.40E−34	0.19	0.82		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
480	2gli	A	385	513	1.40E−33	0.37	0.99		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
480	2gli	A	273	404	5.10E−33	0.49	0.95		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
480	2gli	A	119	264	3.40E−27	−0.4	0.17		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
480	2gli	A	349	488	4.20E−66			94.21	“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
481	1alh	A	350	438	8.50E−29	−0.07	0.03		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
481	1alh	A	319	402	5.10E−26	−0.49	0.19		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
481	1alh	A	551	635	1.70E−24	−0.23	0.4		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
481	1alh	A	579	660	3.40E−19	−0.02	0		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
481	1alh	A	444	573	1.40E−18	0.12	−0.17		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
481	1alh	A	307	375	2.10E−07	−0.02	0.13		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
481	1bbo		321	372	1.00E−07	−0.63	0.05			“DNA-BINDING PROTEIN HUMAN
										ENHANCER-BINDING PROTEIN MBP-1
										MUTANT WITH CYS 11 1BBO 3 REPLACED
										BY ABU (C11ABU) (NMR, 60
										STRUCTURES) 1BBO 4”
481	1mey	C	350	437	5.10E−47	−0.12	0.19		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
481	1mey	C	377	469	1.70E−45	−0.34	0.28		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
481	1mey	C	551	634	1.70E−39	−0.2	0.24		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
481	1mey	C	443	573	5.10E−34	0.24	−0.03		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
481	1mey	G	288	315	6.80E−13	−0.31	0.11		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
481	1mey	G	316	345	1.40E−11	0.03	−0.15		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
481	1mey	G	346	374	1.70E−11	0.15	0.22		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
481	1tf3	A	378	469	1.70E−18	−0.01	0.52		“TRANSCRIPTION FACTOR	“COMPLEX (TRANSCRIPTION
									IIIA; CHAIN: A; 5S RNA	REGULATION/DNA) TFIIIA; 5S GENE;
									GENE; CHAIN: E, F;”	NMR, TFIIIA, PROTEIN, DNA,
										TRANSCRIPTION FACTOR, 5S RNA 2
										GENE, DNA BINDING PROTEIN, ZINC
										FINGER, COMPLEX 3 (TRANSCRIPTION
										REGULATION/DNA)”
481	1tf3	A	551	640	1.70E−15	0.1	0.83		“TRANSCRIPTION FACTOR	“COMPLEX (TRANSCRIPTION
									IIIA; CHAIN: A; 5S RNA	REGULATION/DNA) TFIIIA; 5S GENE;
									GENE; CHAIN: E, F;”	NMR, TEIIIA, PROTEIN, DNA,
										TRANSCRIPTION FACTOR, 5S RNA 2
										GENE, DNA BINDING PROTEIN, ZINC
										FINGER, COMPLEX 3 (TRANSCRIPTION
										REGULATION/DNA)”
481	1tf3	A	473	604	5.10E−08	0.04	−0.19		“TRANSCRIPTION FACTOR	“COMPLEX (TRANSCRIPTION
									IIIA; CHAIN: A, 5S RNA	REGULATION/DNA) TFIIIA; 5S GENE;
									GENE; CHAIN: E, F;”	NMR, TFIIIA, PROTEIN, DNA,
										TRANSCRIPTION FACTOR, 5S RNA 2
										GENE, DNA BINDING PROTEIN, ZINC
										FINGER, COMPLEX 3 (TRANSCRIPTION
										REGULATION(DNA)”
481	1tf6	A	352	499	1.40E−28	0.01	−0.01		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
481	1tf6	A	319	469	8.50E−28	−0.5	0		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
481	1tf6	A	378	584	5.10E−23	−0.25	0.03		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
481	1tf6	A	551	686	6.80E−22	−0.08	0.68		“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
481	1ubd	C	266	374	3.40E−31	−0.33	0.49		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
481	1ubd	C	551	633	3.40E−24	−0.5	0.74		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
481	1ubd	C	556	652	5.10E−20	−0.58	0.15		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
481	1ubd	C	448	603	5.10E−18	0.08	−0.09		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
481	2adr		413	471	5.10E−16	−0.24	0.42		ADR1; CHAIN: NULL;	“TRANSCRIPTION REGULATION
										TRANSCRIPTION REGULATION, ADR1,
										ZINC FINGER, NMR”
481	2adr		579	639	8.50E−12	−0.48	0.47		ADR1; CHAIN: NULL;	“TRANSCRIPTION REGULATION
										TRANSCRIPTION REGULATION, ADR1,
										ZINC FINGER, NMR”
481	2drp	A	345	403	1.70E−08	−0.34	0.27			COMPLEX(TRANSCRIPTION
										REGULATION/DNA) TRAMTRACK
										PROTEIN (TWO ZINC-FINGER PEPTIDE)
										COMPLEXED WITH 2DRP 3 DNA 2DRP 4
481	2gli	A	266	404	1.70E−30	−0.12	0.12		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
481	2gli	A	420	604	1.70E−20	0.02	−0.08		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
481	2gli	A	385	575	3.40E−19	0.03	0.24		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
484	1nkl		33	97	1.20E−18	0.41	0.95		NK-LYSIN; CHAIN: NULL;	“SAPOSIN FOLD SAPOSIN FOLD,
										ANTIBACTERIAL PEPTIDE,
										TUMOUROLYTIC PEPTIDE”
485	1byu	A	3	169	1.70E−26	0.28	0.58		“GTP-BINDING PROTEIN	“TRANSPORT PROTEIN TC4; GTPASE,
									RAN; CHAIN: A, B;”	NUCLEAR TRANSPORT, TRANSPORT
										PROTEIN”
485	1byu	B	3	169	1.70E−26	0.36	0.52		“GTP-BINDING PROTEIN	“TRANSPORT PROTEIN TC4; GTPASE,
									RAN; CHAIN: A, B;”	NUCLEAR TRANSPORT, TRANSPORT
										PROTEIN”
485	1d5c	A	3	169	3.40E−32	0.22	0.05		RAB6 GTPASE; CHAIN: A;	“ENDOCYTOSIS/EXOCYTOSIS G-
										PROTEIN, GTPASE, RAB6, VESICULAR
										TRAFFICKING”
485	1e0s	A	3	170	6.80E−52	1	1		ADP-RIBOSYLATION	“G PROTEIN, G PROTEIN, RAS, ARF, ARF6,
									FACTOR 6; CHAIN: A;	MEMBRANE TRAFFIC”
485	1ek0	A	3	162	1.00E−33	0.13	0.21		GTP-BINDING PROTEIN	“ENDOCYTOSIS/EXOCYTOSIS G PROTEIN,
									YPT51; CHAIN: A;	VESICULAR TRAFFIC, GTP HYDROLYSIS,
										YPT/RAB 2 PROTEIN, ENDOCYTOSIS,
										HYDROLASE”
485	1fnm	A	10	139	3.40E−05	−0.41	0.04		ELONGATION FACTOR G;	“TRANSLATION EF-G; BENT
									CHAIN: A;	CONFORMATION, VISIBLE DOMAIN III,
										MUTATION HIS573ALA”
485	1fzq	A	3	168	1.00E−44	0.75	1		ADP-RIBOSYLATION	“SIGNALING PROTEIN ARF-LIKE
									FACTOR-LIKE PROTEIN 3;	PROTEIN 3, ARL3; PROTEIN-GDP
									CHAIN: A;	COMPLEX WITHOUT MAGNESIUM, ARF
										FAMILY, RAS 2 SUPERFAMILY, G-
										DOMAIN”
485	1hur	A	3	171	5.10E−55	1.03	1		“HUMAN ADP-	“PROTEIN TRANSPORT GDP-BINDING,
									RIBOSYLATION FACTOR 1;	MEMBRANE TRAFFICKIN, NON-
									1HUR 5 CHAIN: A, B; 1HUR	MYRISTOYLATED 1HUR 16”
									7”
485	1hur	A	2	173	5.10E−55			81.42	“HUMAN ADP-	“PROTEIN TRANSPORT GDP-BINDING,
									RIBOSYLATION FACTOR 1;	MEMBRANE TRAFFICKIN, NON-
									1HUR 5 CHAIN: A, B; 1HUR	MYRISTOYLATED 1HUR 16”
									7”
485	1rrp	C	3	169	3.40E−26	0.41	0.22		“RAN; CHAIN: A, C;	“COMPLEX (SMALL GTPASE/NUCLEAR
									NUCLEAR PORE COMPLEX	PROTEIN) COMPLEX (SMALL
									PROTEIN NUP358; CHAIN: B,	GTPASE/NUCLEAR PROTEIN), SMALL
									D;”	GTPASE, 2 NUCLEAR TRANSPORT”
485	1zbd	A	3	169	1.50E−34	0.15	0.37		RAB-3A; CHAIN: A;	“COMPLEX (GTP-BINDING/EFFECTOR)
									RABPHILIN-3A; CHAIN: B;	RAS-RELATED PROTEIN RAB3A;
										COMPLEX (GTP-BINDING/EFFECTOR), G
										PROTEIN, EFFECTOR, RABCDR, 2
										SYNAPTIC EXOCYTOSIS, RAB PROTEIN,
										RAB3A, RABPHILIN”
485	3rab	A	3	169	1.40E−35	0.02	0.29		RAB3A; CHAIN: A;	“HYDROLASE G PROTEIN, VESICULAR
										TRAFFICKING, GTP HYDROLYSIS, RAB 2
										PROTEIN, NEUROTRANSMITTER
										RELEASE, HYDROLASE”
486	1alh	A	99	179	3.40E−29	−0.1	0.58		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
486	1alh	A	127	200	1.20E−25	−0.36	0.21		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
486	1alh	A	91	151	5.10E−21	−0.28	0.83		“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
486	1alh	A	99	182	3.40E−29			59.69	“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
486	1ard		99	127	1.10E−08	−0.47	0.87			“TRANSCRIPTION REGULATION YEAST
										TRANSCRIPTION FACTOR ADR1
										(RESIDUES 102-130) 1ARD 3 (AMINO
										TERMINAL ZINC FINGER DOMAIN) (NMR,
										10 STRUCTURES) 1ARD 4 (ADR1B) 1ARD
										5”
486	1ard		99	127	3.40E−06	−0.47	0.87			“TRANSCRIPTION REGULATION YEAST
										TRANSCRIPTION FACTOR ADR1
										(RESIDUES 102-130) 1ARD 3 (AMINO
										TERMINAL ZINC FINGER DOMAIN) (NMR,
										10 STRUCTURES) 1ARD 4 (ADR1B) 1ARD
										5”
486	1mey	C	98	179	1.00E−49	−0.01	0.84		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
486	1mey	C	126	200	1.50E−42	−0.21	0.01		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
486	1mey	C	72	151	5.10E−37	−0.12	0.15		“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
486	1mey	C	98	180	1.00E−49			63.19	“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
486	1tf3	A	89	151	6.80E−16	−0.62	0.48		“TRANSCRIPTION FACTOR	“COMPLEX (TRANSCRIPTION
									IIIA; CHAIN: A; 5S RNA	REGULATION/DNA) TFIIIA; 5S GENE;
									GENE; CHAIN: E, F;”	NMR, TFIIIA, PROTEIN, DNA,
										TRANSCRIPTION FACTOR, 5S RNA 2
										GENE, DNA BINDING PROTEIN, ZINC
										FINGER, COMPLEX 3 (TRANSCRIPTION
										REGULATION/DNA)”
486	1tf3	A	98	184	1.70E−19			52.05	“TRANSCRIPTION FACTOR	“COMPLEX (TRANSCRIPTION
									IIIA; CHAIN: A; 5S RNA	REGULATION/DNA) TFIIIA; 5S GENE;
									GENE; CHAIN: E, F;”	NMR, TFIIIA, PROTEIN, DNA,
										TRANSCRIPTION FACTOR, 5S RNA 2
										GENE, DNA BINDING PROTEIN, ZINC
										FINGER, COMPLEX 3 (TRANSCRIPTION
										REGULATION/DNA)”
486	1tf6	A	9	183	1.70E−25			51.78	“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, E, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
486	1ubd	C	92	179	3.40E−31	−0.13	0.82		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
486	1ubd	C	106	202	1.70E−29	−0.37	0.07		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
486	1ubd	C	74	151	1.70E−21	−0.44	0.05		“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
486	1ubd	C	74	180	3.40E−31			64.55	“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA;	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
486	2adr		127	184	1.70E−15	−0.59	0.07		ADR1; CHAIN: NULL;	“TRANSCRIPTION REGULATION
										TRANSCRIPTION REGULATION, ADR1,
										ZINC FINGER, NMR”
486	2adr		99	157	1.00E−16			50.07	ADR1; CHAIN: NULL;	“TRANSCRIPTION REGULATION
										TRANSCRIPTION REGULATION, ADR1,
										ZINC FINGER, NMR”
486	2gli	A	89	202	1.00E−28	−0.19	0.27		“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
486	2gli	A	56	202	1.00E−28			53.72	“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”
488	1alh	A	145	227	1.50E−28			78.47	“QGSR ZINC FINGER	“COMPLEX (ZINC FINGER/DNA)
									PEPTIDE; CHAIN: A;	COMPLEX (ZINC FINGER/DNA), ZINC
									DUPLEX	FINGER, DNA-BINDING PROTEIN”
									OLIGONUCLEOTIDE
									BINDING SITE; CHAIN: B,
									C;”
488	1mey	C	144	226	3.40E−48			96.09	“DNA; CHAIN: A, B, D, E;	“COMPLEX (ZINC FINGER/DNA) ZINC
									CONSENSUS ZINC FINGER	FINGER, PROTEIN-DNA INTERACTION,
									PROTEIN; CHAIN: C, F, G;”	PROTEIN DESIGN, 2 CRYSTAL
										STRUCTURE, COMPLEX (ZINC
										FINGER/DNA)”
488	1tf6	A	172	337	3.40E−35			109.42	“TFIIIA; CHAIN: A, D; 5S	“COMPLEX (TRANSCRIPTION
									RIBOSOMAL RNA GENE;	REGULATION/DNA) COMPLEX
									CHAIN: B, C, B, F;”	(TRANSCRIPTION REGULATION/DNA),
										RNA POLYMERASE III, 2 TRANSCRIPTION
										INITIATION, ZINC FINGER PROTEIN”
488	1ubd	C	146	254	6.80E−34			93.51	“YY1; CHAIN: C; ADENO-	“COMPLEX (TRANSCRIPTION
									ASSOCIATED VIRUS P5	REGULATION/DNA) YING-YANG 1;
									INITIATOR ELEMENT DNA	TRANSCRIPTION INITIATION, INITIATOR
									CHAIN: A, B;”	ELEMENT, YY1, ZINC 2 FINGER PROTEIN,
										DNA-PROTEIN RECOGNITION, 3
										COMPLEX (TRANSCRIPTION
										REGULATION/DNA)”
488	2gli	A	111	255	1.70E−34			87.07	“ZINC FINGER PROTEIN	“COMPLEX (DNA-BINDING
									GLI1; CHAIN: A; DNA;	PROTEIN/DNA) FIVE-FINGER GLI; GLI,
									CHAIN: C, D;”	ZINC FINGER, COMPLEX (DNA-BINDING
										PROTEIN/DNA)”

[0474]

TABLE 6
	Position of Predicted
SEQ ID NO:	Signal peptide	Maximum Score	Mean Score
250	1-27	0.954	0.795
251	1-22	0.918	0.708
260	1-27	0.961	0.814
261	1-34	0.976	0.676
296	1-21	0.934	0.774
305	1-25	0.994	0.957
307	1-21	0.997	0.955
309	1-22	0.967	0.839
339	1-16	0.907	0.560
347	1-35	0.897	0.663
355	1-32	0.973	0.750
357	1-18	0.970	0.815
366	1-20	0.963	0.907
377	1-15	0.904	0.734
378	1-17	0.924	0.598
379	1-19	0.958	0.843
380	1-20	0.976	0.945
381	1-19	0.916	0.649
382	1-13	0.956	0.798
383	1-19	0.916	0.649
384	1-26	0.991	0.949
385	1-20	0.961	0.880
386	1-20	0.961	0.880
387	1-15	0.931	0.773
388	1-38	0.986	0.856
389	1-22	0.987	0.824
390	1-20	0.914	0.671
391	1-15	0.905	0.594
392	1-25	0.958	0.903
393	1-17	0.902	0.762
394	1-22	0.963	0.931
395	1-23	0.973	0.917
396	1-17	0.903	0.663
397	1-26	0.990	0.876
398	1-17	0.911	0.652
399	1-33	0.985	0.912
400	1-24	0.928	0.580
401	1-24	0.958	0.812
402	1-16	0.947	0.770
403	1-21	0.933	0.880
404	1-21	0.961	0.912
405	1-17	0.883	0.585
406	1-19	0.888	0.591
407	1-20	0.978	0.830
408	1-17	0.984	0.922
409	1-36	0.993	0.929
410	1-19	0.954	0.791
411	1-19	0.954	0.791
412	1-19	0.954	0.791
413	1-19	0.954	0.791
414	1-18	0.995	0.926
415	1-19	0.923	0.605
416	1-19	0.995	0.936
417	1-18	0.980	0.930
418	1-18	0.980	0.930
419	1-18	0.980	0.930
420	1-16	0.923	0.710
421	1-21	0.961	0.731
422	1-25	0.952	0.848
423	1-20	0.981	0.933
424	1-48	0.905	0.599
425	1-25	0.989	0.949
426	1-26	0.960	0.869
427	1-22	0.942	0.855
428	1-19	0.955	0.846
429	1-20	0.978	0.835
430	1-19	0.925	0.759
431	1-37	0.977	0.782
432	1-29	0.911	0.708
433	1-20	0.974	0.922
434	1-33	0.904	0.641
435	1-13	0.880	0.581
436	1-30	0.946	0.787
437	1-15	0.975	0.886
438	1-19	0.981	0.916
439	1-15	0.988	0.973
440	1-26	0.956	0.748
441	1-35	0.972	0.737

[0475]

TABLE 7
SEQ ID NO: Chromsomal location
1          19
2          17
4          17
6          10
7          17
8          1p36.33-p36.12
10         19p13.3
11         4q21-q23
12         17
13         1p36.33-p36.12
16         6
17         4q12-q21
19         5
20         17
22         2p16
24         17
25         11q13
26         5
27         Xq28
28         12q23
29         12q23
30         7q34
31         17
34         17
35         5
36         17
37         17
38         17
39         7
41         17
42         Xp11.3-p11.23
43         11p15.3-p15.1
47         10
48         2
49         20
51         19p13.3
52         9
53         10q24
54         10q24
55         3p26
57         15
58         21q11.1
59         5
60         1q42.12-q43
61         12p13
62         4
64         Xp11.3-p11.23
65         p21
66         17
67         14q32
68         11
69         17
71         19q13.1-q13.2
75         6
79         16
82         17
83         17q25
88         14
89         14
90         15
91         6
92         5
93         9
94         11
95         17
96         4
98         7q21-q22
99         1
102        19
103        20
106        17
108        12
110        14
112        3
113        17
115        5
116        17
117        15q14
118        12q22
120        16
122        21q22.3
125        12
127        6q22.1-23.3
129        17
130        17
131        15q21
132        20q11.2
133        1q23
134        1
135        17
136        18q12.1
137        1
138        1
139        1
140        19q13.2-q13.4
141        16
142        16
143        5
144        1p36.3-p36.2
146        2
147        17
149        17
150        2
153        7
154        17
155        7q22
156        1p36.1-p35
164        9q34
165        19p13.1
170        10
171        1
172        3p
173        3q27
174        3q27
175        3q27
176        3
177        20
178        19
179        7q22.1
181        22q12.1-q12.3
185        13
186        11p15.5
187        q23.1-24.3
188        7q21.1
189        11p15.5
191        17
193        14
195        2p12-q11
196        17
197        12q13.12-q13.13
201        4
204        17
206        19
209        15
213        7
216        X
217        6q14.1-15
220        9
224        5
225        1
226        19
227        Xq28
229        17
230        3
232        17
235        5
236        19p13.3
237        17
238        17
240        2p12-q11
243        16
244        17

[0476]

TABLE 8
			Location
			of first
			nucleotide	Amino acid sequence (A = Alanine, C = Cysteine, D = Aspartic
		Nucleotide	of codon	Acid, E = Glutamic Acid, F = Phenylalanine, G = Glycine,
		location	corresp.	H = Histidine, I = Isoleucine, K = Lysine, L = Leucine,
		corresp. to	to last	M = Methionine, N = Asparagine, P = Proline, Q = Glutamine,
SEQ		first residue	residue of	R = Arginine, S = Serine, T = Threonine, V = Valine,
ID		of peptide	peptide	W = Tryptophan, Y = Tyrosine, X = Unknown, * = Stop codon, / = possible
NO:	Method	sequence	sequence	nucleotide deletion, = possible nucleotide insertion)
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
708	A	45	1078	CWGRWGRGTPTPSPSPRDAEEKAGGGWGRDQAPTPRRGDEGSMG
				AKESRIGFLSYEEALRRVTDVELKRLKDAFKRTCGLSYYMGQHC
				FIREVLGDGVPPKVAEVIYCSFGGTSKGLHFNNLIVGLVLLTRG
				KDEEKAKYIFSLFSSESGNYVIREEMERMLHVVDGKVPDTLRKC
				FSEGEKVNYEKFRNWLFLNKDAFTFSRWLLSGGVYVTLTDDSDT
				PTFYQTLAGVTHLEESDIIDLEKRYWLLKAQSRTGRFDLETFGP
				LVSPPIRPSLSEGLFNAFDENRDNHIDFKEISCGLSACCRGPLA
				ERQKFCFKVFDVDRG*VLSRVELRDNMGALLEVWKD
709	A	276	2588	NKHFSFQTPKKSHQKSLSFSKTTPRRISHTPQTPLYTPERLQKS
				PAKMTPTKQAAFKESLKDSSSPGHDSPLDSKITPQKRHTQAGEG
				TSLETKTPRTPKRQGTQPPGFLPNCTWPHSVNSSPESPSCPAPP
				TSSTAQPRRECLTPIRDPLRTPPRAAAFMGTPQNQTHQQPHVLR
				AARAEEPAQKLKDKAIKTPKRPGNSTVTSSPPVTPKKLFTSPLC
				DVSKKSPFRKSKIECPSPGELDQKEPQMSPSVAASLSCPVPSTP
				PELSQRATLDTVPPPPPSKVGKRCRKTSDP/MKEAS/SECQLDA
				SATPGVGTADSPAAPTDSRDDQKGLSLSPQSPPERRGYPGPGLR
				SDWHASSPLLITSDTEHVTLLSEAEHHGIGDLKSNVLSVEEGEG
				LRTADAEKSSLSHPGIPPSPPSCGPGSPLMPSRDVHCTTDGRQC
				QASAQLDNLPASAWHSTDSASPQTYEVELEMQASGLPKLRIKKI
				DPSSSLEAEPLSKEESSLGEESFLPALSMPRASRSLSKPEPTYV
				SPPCPRLSHSTPGK\TGGKPTSARPVPPPT/SPSSTPSPFQTDG
				VPWTPSPKHSGKTTPDIIK\TGPGGRGRWAVAPAPLPGGARSVQ\
				PSWEPVTA*VRGQGPRP*TQHPQDAHLGGF*ARGSVPAPRPVA
				SQE/PACLRPRKPLPGDSLG*VPGRESCWPRKKLTVEPKGSVT*
				EKIQKLVRVKRGLQVGVHGSYPPRETKRCLFPAPPHLPAVPCGA
				PSPASALQALTQSPLLFQGKTPSSQSKDPR
710	A	2	1510	EIELPCSEDLNLETLSQAHVYIIAGACLSLGFRFAGSENLSAFN
				CLHKFAKDFMTYLSAPNASVTGPHNLETCLSVVLLSLAMVMAGS
				GNLKVLQLCRFLHMKTGGEMNYGFHLAHHMALGLLFLGGGRYSL
				STSNSSIAALLCALYPHFPAHSTDNRYHLQALRHLYVLAAEPRL
				LVPVDVDTNTPCYALLEVTYKGTQWYEQTKEELMAPTLLPELHL
				LKQIKVKGPRYWELLIDLSKGTQHLKSILSKDGVLYVKLRAGQL
				SYKEDPMGWQSLLAQTVANRNSEARAFKPETISAFTSDPALLSF
				AEYFCKPTVNMGQKQEILDLFSSVLYECVTQETPEMLPAYIAMD
				QAIRRLGRREMSETSELWQIKLVLEFFSSRSHQERLQNHPKRGL
				FMNSEFLPVVKCTIDNTLDQWLQVGGDMCVHAYLSGQPLEESQL
				SMLACFLVYHSVPAPQHLPPIGLEGSTSFAELLFKFKQLKMPVR
				ALLRLAPLLLGNPQPMVM
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
711	A	536	126	TPPVPTAKKQPAFPASYIPPSPPTPPVPVPPPTLPKQQSFCAKP
				PPSPLSPVPSVVKQIASQFPPPPTPPAMESQPLKPVPANVAPQS
				PPAVKAKPKWQPSSIPVPSPDFPPPPPESSKVFPPXPPXPVPAX
				PXXPP
712	A	1	1642	MDYIRTDLTTAAPSPPRRLGPPPPGEQPPSGSGHVRPPGARPPH
				RGGGRGGGGGDPAAPPARGGGGGGKARPPGGGAAPCEPGCQCRA
				PMVSVSSERHPLYNRVKTGQIANCALPCHNPFFSQDERAFTVFW
				IGLWSVLCFVSTFATVSTFLIDMERFKYPERPIIFLSACYLFVS
				VGYLVRLVAGHEKVACSGGAPGAGGAGGAGGAAAGAGAAGAGAG
				GPGGRGEYEELGAVEQHVRYETTGPALCTVVFLLVYFFGMASSI
				WWVILSLTWFLAAGMKWGNEAIAGYSQYFHLAAWLVPSVKSIAV
				LALSSVDGDPVAGICYVGNQSLDNLRGFVLAPLVIYLFIGTMFL
				LAGFVSLFRIRSVIKQQDGPTKTHKLEKLMIRLGLFTVLYTVPA
				AVVACLFYEQHNRPRWEATHNCPCLRDLQPDQARRPDYAVFML
				KYFMCLVVGITSGVWVWSGKTLESWRSLCTRCCWASKGAAVGGG
				AGATAAGGGGGPGGGGGGGPGGGGGPGGGGGSLYSDVS\TGLTW
				RSGTASSVSYPK\QMPLSQV
713	A	3	586	GTIITPDEYTGKIMMLCEARPAVQKNMIFIDQNRVMLKYLFPLN
				EIVVDFYDSLKSLSSGYASFDYEDAGYQTAELVKMDILLNGNTV
				EELVTVVHKDKAHSIGKAICERLKDSLPRQLFEIAIQAAIGSKI
				IARETVKAYRKNVLAKCYGGDITRKMKLLKRQAEGKKKLRKIGN
				VEVPKDAFIKVLKTQSSK
714	A	250	687	AATSLPFRASTIASANSILRVGVMTSIHHFVFSKRVCCNFTSKT
				YFMSQQSSRTCTDGGYQALPFSCSSVSPSQQQTQIKSVRPDYLL
				VEPPHHMGPSFFASSGLHYDQ*PHHRLHLYWVFSARPWNGDLNP
				SSAHDI*HE*PLHF
715	A	1	2649	MKILTKLGYSLITTAEWEIMHDKEKLCCPSSRRWPPPHPPPPWR
				IAVRCPWQVIAIGNKQFQCLEALFQPSFLGMECCSIHKTTFNSI
				MKCDVDICKDLYANTMQKEITALVPSTTKIKIIVPRPKHRYSVW
				IGSSILASLSTFQQMWISKQESTLEDPPMGLTDIPEMKARGNKD
				TRGLTAAKKPELSENQDNGHKRDQQSRRDGLGGSSRPPALKPRD
				YNSHSALAEGPGVDEVDPVHHDGDDAVPALEAPGQAVLDEEGVA
				EHKAVLLISEEDGAFTARADLEGHRRLRQPFPRLVTPNQNLFFR
				LFRVSWHKSASVNNGESGTGLSTYGLSLRIFFPKLACQQVDSRG
				PPGIKVRHDQDPGYMHHKFAIVDKRVLITGSLNWTTQAIQNNRE
				NVLITEDDEYVRLFLEEFERIWEQFNPTNHDLPRGAFMSVVRIL
				VWNRNFCYSTEKAQCLFQNTTEKSFDEDNRKSTQQRVVWTTQNA
				SLTHSMPTVNCDNDSNNNNNNKTTVQSLDSKSFNRSCTVRPSFR
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
				LWVETEQEEKINTPLDSLHWSGSDQTGTLVDASSVREPGAELAN
				ATFLFFRLLTLARTVLIPIPLRKWGVQHLRAEESAGAVELAEVA
				ESHDGIHGALETATGLRGTGDIAAYGPKPSVTEEAKSECQSMMS
				LSTLCSSANIVQQDFLLQQLLDVFIRDKLMERRNRRTGRTEKAR
				IWEVTDRTVRTWIGEAVARLLLTLACLQVDSRGSPVVGGVVGGG
				ADHHAALRPAVRVVGRHGFEQHLLDGFAGKDRESADLGSDGQNG
				QDLDWGGGCASAADGVTFSVPVTPHTFRHSYAMHMLYAGIPLKV
				LQSLMGHKSISSTEVYTKVFALDVAARHRVQFAMPESDAVAMLK
				QLY
716	A	1	1297	GLRHEVTLRVLLKDALLEPGAGVLSIYYLGKKFLGDLQPDGRIM
				WQETGQTFNSPSAWATHCKKLVNPAKKSGCGWASVKYKGQKLDK
				YKATWLRLHQLHTPATAADESPASEGEEEELMEEEEEDVLAGV
				SAEDKSRRPLGKSPSEPAHPEATTPGKRVDSKIRVPVRYCMLGS
				RLARNPHTLVEVTSFAAINKFQPFNVAVSSNVLFLLDFHSHLT
				RSEVVGYLGGRWDVNSQMLTVLRAFPCRSRLGDAKTAAAIEEEI
				YQSLFLRGLSLVGWYHSHPHSPALPSLQDIDAQMDYQLRLQGSS
				NGFQPCLALLCSPYYSGNPGPESKISPFWVMPPPEQRPSDYGIP
				MDVEMAYVQDSFLTNDILHEMMLLVEFYKGSPDLVRLQEPWSQE
				HTYLDKLKISLASRTPKDQSLCHVLEQVCGVLKQGS
717	A	2	219	KLVTGVIAVAQKGVEGAGSIAAATGFVKKDQLGKNEEGAPQEGI
				LEDMPVDPDNEAYEMPSEEGYQDYEPEA
718	A	1	619	IQVEQNR*HFYELSLEYVCKLQEIQERKKFEFVEPMLSFFQGMF
				TFYHQGHELAKDFNHYKMELQINIQNTRNRFEGTRSEVEELMNK
				IRQNPKDHKRASQFTAEGYLYVQEKRPAPFGSSWVKHYCMYRKA
				AKKFNMIPFEHRSGGKLGDGEVFFLKECTKRHTDSIDRRFCFDI
				EAADRPGVSLTMQAFSEEERKQWLEALGGK
719	A	250	687	AATSLPFRASTIASANSILRVGVMTSIHHFVFSKRVCCNFTSKT
				YFMSQQSSRTCTDGGYQALPFSCSSVSPSQQQTQIKSVRPDYLL
				VEPPHHMGPSFFASSGLHYDQ*PHHRLHLYWVFSARPWNGDLNP
				SSAHDI*HE*PLHF
720	A	32	370	PGQCPGALAMKSRQKGKKKGSAKERVFGCDLQEHLQHSGQEVPQ
				VLKSCAEFVEEYGVVDGIYRLSGVSSNIQKLRQEFESERKPDLR
				RDVYLQDIHCVSSLCKAYFRELPDP
721	A	2	403	EFPRLPDPNVVFPPTPRRWNTQQDSTLERPKTLEFLPRPRPSAN
				RQRLDPWWFVSPSHARSTSPANSSSTETPSNLDSCFASSSSTVE
				ERPGLPALLPFQAGPLPPTERTLLDLDAEGQSQDSTVPLCRAEL
				NT
722	A	203	359	ALRSCWKLCRSMSSAAGFCASRPGLLFLGLLLLPLVVAFASGKP
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
				CIPWRPTP
723	A	36	633	TNELIHRPQPDSQQRFVPVPTPAKRSARAPSLPAGHLASLPATM
				PNVLLPPKESNLFKRILKCYEQKQYKNGLKFCKMILSNPKFAEH
				GETLAMKGLTLNCLGKKEEAYEFVRKGLRNDVKSHVCWHVYGLL
				QRSDKKYDEAIKCYRNALKLDKDNLQILRDLSLLQIQMRDLEGY
				RETRYQLLQLRPTQRASWIGYAI
724	A	1784	674	APTPTGQRVVRATPAQSAPVRLRRRSYDVNNPIPSNLKSEAKKA
				AKILREFTEITSRNGPDKIIPAHVIAKAKGLAILSVIKAGFLVT
				ARGGSGIVVARLPDGKWSAPSAIGIAGLGGGFEIGIEVSDLVII
				LNYDRAVEAFAKGGNLTLGGNLTVAVGPLGRNLEGNVALRSSAA
				VFTYCKSRGLFAGVSLEGSCLIERKETNRKFYCQDIRAYDILFG
				DTPRPAQAEDLYEILDSFTEKYENEGQRINARKAAREQRKSSAK
				ELPPKPLSRPQQSSAPVQLNSGSQSNRNEYKLYPGLSSYHERVG
				NLNQPIEVTALYSFEGQQPGDLNFQAGDRITVISKTDSHFDWWE
				GKLRGQTGIFPANYVTMN
725	A	3	927	CGGIRELEALATLYQKQNKYEQAEHFRKKSFKIHQKAIKKKGNL
				YGFALLRRRALQLEELTLGKDTPDNARTLNELGVLYYLQNNLET
				ADQFLKRSLEMRERVLGPDHPDCAQSLNNLAALCNEKKQYDKAE
				ELYERALDIRRRALAPDHPSLAYTVKHLAILYKKMGKLDKAVPL
				YELAVEIRQKSFGPKHPSVATALVNLAVLYSQMKKHVEALPLYE
				RALKIYEDSLGRMHPRVGETLKNLAVLSYEGGDFEKAAELYKRA
				MEIKEAETSLLGGKAPSRHSSSGDTFSLKTAHSPNVFLQQGQR
726	A	242	1310	FLSLFRKRLYMEVFEYTRPMMHPEPGKFYQINPEEYGHPNTWKE
				SFQQLYKGAHVKPGFAEHFYSNPARYKGRENMLYYDTIEDALGG
				VQEAHFDGLIFVHSGIYTDEWIYIESPITMIGAAPGKVADKVII
				ENTRDSTFVFMEGSEDAYVGYMTIRFNPDDKSAQHHNAHHCLEI
				TVNCSPIIDHCIIRSTCTVGSAVCVSGQGACPTIKHCNISDCE\
				NVG\IYITDHAHGNYTDG*LKFPIMPLAGIWVKNHGNPIIRRNH
				IHHGRDVGVFTFDHGMGYFESCNIHRNRIAGFEVKAYANPTVVR
				CEIHHGQTGGIYVHEKGRGQFIENKIYANNFAGVWITSNSDPTI
				RGNSI
727	A	297	554	VKRHASSANQYKYGKNRAEEDARRYLVEKEKLEKEKETIRTELI
				ALRQEKRELKEAIRSSPGAKLKALEEAVATLEAQCRAKEERR
728	A	88	572	PHGPKTMEEGGSTGSAGSDSSTSGSGGAQQRELERMAEVLVTGE
				QLRLRLHEEKVIKDRRHHLKTYPNCFVAKELIDWLIEHKEASDR
				ETAIKLMQKLADRGIIHHVCDEHKEFKDVKLFYRFRKDDGTFPL
				DNEVKA/CYERTEAI*KVCSA*NPPCNLDL
729	A	1344	776	YSAVEFGPTDWLPQTLDSLPYVSQDCLDSGIGSLESQMSELWGV
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
				RGGGPGEPGPPRAPYTGYSPYGSELPATAAFSAFGRAMGAGHFS
				VPADYPPAPPAFPPREYWSEPYPLPPPTSVLQEPPVQSPGAGRS
				PWGRAG/TPGQGAGQRVY*AVWCVSPAPGGGCDGALPTAPGPPA
				AGCRDPLLQVPAPQ
730	A	1	4491	PSPEAGGGGGALKASSARAAAAGLLREAGSGGRERADWRRRQLR
				KVRSVELDQLPEQPLFLAASPPASSTSPSPEPADAAGSGTGFQP
				VAVPPPHGAASRRGAHLTESVAAPDSGASSPAAAEPGEKRAPAA
				EPSPAAAPAGREMENKETLKGLHKMDDRPEERMIREKLKATCMP
				AWKHEWLERRNRRGPVVVKPIPVKGDGSEMNHLAAESPGEVQAS
				AASPASKGRRSPSPGNSPSGRTVKSESPGVRRKRVSPVPFQSGR
				ITPPRRAPSPDGFSPYSPEETNRRVNKVMRARLYLLQQIGPNSF
				LIGGDSPDNKYRVFIGPQNCSCAHGTFCIHLLFVMLRVFQLEPS
				DPMLWRKTLKNFEVESLFQKYHSRRSSRIKAPSRNTIQKFVSRM
				SNSHTLSSSSTSTSSSENSIKDEEEQMCPICLLGMLDEESLTVC
				EDGCRNKLHHHCMSIWAEECRRNREPLICPLCRSKWRSHDFYSH
				ELSSPVDSPSSLRAAQQQTVQQQPLAGSRRNQESNFNLTHYGTQ
				QIPPAYKDLAEPWIQVFGMELVGCLFSRNWNVREMALRRLSHDV
				SGALLLANGESTGNSGGSSGSSPSGGATRGFSQTSISGDVVEAC
				CSVLSMVCADPVYKVYVAALKTLRAMLVYTPCHSLAERIKLQRL
				LQPVVDTILVKCADANSRTSQLSISTLLELCKGQAGKLAVGREI
				LKAGSIGIGGVDYVLNCILGNQTESNNWQELLGRLCLIDRLLLE
				FPAEFYPHIVSTDVSQAEPVEIRYKKLLSLLTFALQSIDNSHSM
				VGKLSRRIYLSSARMVTTVPHVFSKLLEMLSVSSVSTHFTRMRR
				RLMAYADEVEIAEAIQLGVEDTLQRQQHNSFCRHLFPTTIWKPQ
				RTVPLECTVHLEKTGKGLCATKLSASSEDISERLARISVGPSSS
				TTTTTTTTEQPKPMVQTKGRPHSQCLNSSPLSHHSQLMFPALST
				PSSSTPSVPAGTATDVSKHRLQGFIPCRIPSASPQTQRKFSLQF
				HRNCPENKDSDKLSPVFTQSRPLPSSNIHRPKPSRPTPGNTSKQ
				GDPSKNSMTLDLNSSSKCDDSFGCSSNSS/NCCYT\SDETVFTP
				VEEKCRLDVNTELNSSIEDLLEASMPSSDTTVTFKSEVAVLSPE
				KAENDDTYKDDVNHNQKCKEKMEAEEEEALAIAMAMSASQVALP
				IVPQLQVENGEDIIIIQQDTPETLPGHTKAKQPYREDTEWLKGQ
				QIGLGAFSSCYQAQDVGTGTLMAVKQGTYVRNTSSEQEEVVEAL
				REEIRMMSHLNHPNIIRMLGATCEKSNYNLFIEWMAGGSVAHLL
				SKYGAFKESVVINYTEQLLRGLSYLHENQIIHRDVKGANLLIDS
				TGQRLRIADFGAAARLASKGTGAGEFQGQLLGTIAFMAPEVLRG
				QQYGRSCDVWSVGCAIIEMACAKPPWNAEKHSNHLALIFKIASA
				TTAPSIPSHLSPGLR\DVALRCL\ELQPQDRPPSRELLKHPVFR
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
				TTW
731	A	30	1060	RSCPGLVVLGSPDMSEVKSRKKSGPKGAPAAEPGKRSEGGKTPV
				ARSSGGGGWADPRTCLSLLSLGTCLGLAWFVFQQSEKFAKVENQ
				YQLLKLETNEFQQLQSKISLISEKLESTESILQEATSSMSLMTQ
				FEQEVSNLQDIMHDIQNNEEVLTQRMQSLNEKFQNITDFWKRSL
				EEMNINTDIFKSEAKHIHSQVTVQINSAEQEIKLLTERLKDLED
				STLRNIRTVKRQEEEDLLRVEEQLGSDTKAIEKLEEEQHALFAR
				DEDLTNKLSDYEPKVEECKTHLPTIESAIHSVLRVSQDLIETEK
				KMEDLTMQMFNMEDDMLKAVSEIMEMQKTLEGFFL
732	A	30	1060	RSCPGLVVLGSPDMSEVKSRKKSGPKGAPAAEPGKRSEGGKTPV
				ARSSGGGGWADPRTCLSLLSLGTCLGLAWFVFQQSEKFAKVENQ
				YQLLKLETNEFQQLQSKISLISEKLESTESILQEATSSMSLMTQ
				FEQEVSNLQDIMHDIQNNEEVLTQRMQSLNEKFQNITDFWKRSL
				EEMNINTDIFKSEAKHIHSQVTVQINSAEQEIKLLTERLKDLED
				STLRNIRTVKRQEEEDLLRVEEQLGSDTKAIEKLEEEQHALFAR
				DEDLTNKLSDYEPKVEECKTHLPTIESAIHSVLRVSQDLIETEK
				KMEDLTMQMFNMEDDMLKAVSEIMEMQKTLEGFFL
733	A	2	1148	IVDRCGIPLKEAESLQVAVKASQMGAVSQSCEDSCGDSVLADTL
				SSHDVPGSPTASLVTGGREGRGCSDVDPGIQGVVTDLAVSDAGE
				KVECRNFPGSSQSEIIQAIQNLTRLLYSLQAALTIQDSHIEIHR
				LVLQQQEGLSLGHSILRGGPLQDQKSRDADRQHEELANVHQLQH
				QLQQEQRRWLRRCEQQQRAQATRESWLQERERECQSQEELLLRS
				RGELDLQLQEYQHSLERLREGQRLVEREQARMRAQQSLLGHWKH
				GRQRSLPAVLLPGGPEVMELNRSESLCHENSFFINEALVQMSFN
				TFNKLNPSVIHQDATYPTTQSHSDLVRTSEHQVDLKVDPSQPSN
				VSHKLWTAAGSGHQILPFHESSKDSCKNGN
734	A	1	1063	MPFYISDLSICGDRILRALCPQDLPTYSLHSRGKMRASCSRKFL
				DNNSSRLVSCNMGALISIWGTTTPPLHATILDSQPTVHPPLAKD
				CLPCGLQASASDLRARALQRLCQQLPWVGSQPHTRSPSPQRGGK
				TGLFAGLASSVSMRPASPPSPAADSCSACRFFARRPPLRVTWVK
				PSSALALCVSISDSIPGNLKALPAETRAQLHHAEASLSQPPLQL
				RPFPKTSQAGDLQDLGPYVCVRKAVGKGDKQIRAVVKEHSVRSQ
				ERIWHYPGITTANMPGHLGQNTESGRDKLPMFGVWFPGCRFWGL
				WVWRLP*LKLAAPCRPSRSLRSSPISRRASTTRCLTVSGCPAAP
				NL
735	A	1	1277	NEFTRRKHLELTATMQVEEATGQAAGRRRGNVVRRVFGRIRRFF
				SRRRNEPTLPREFTRRGRRGAVSVDSLAELEDGALLLQTLQLSK
				ISFPIGQRLLGSKRKMSLNPIAKQIPQVVEACCQFIEKHGLSAV
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
				GIFTLEYSVQRVRQLREEFDQGLDVVLDDNQNVHDVAALLKEFF
				RDMKDSLLPDDLYMSFLLTATLKPQDQLSALQLLVYLMPPCHSD
				TLERLLKALHKITENCEDSIGIDGQLVPGNRMTSTNLALVFGSA
				LLKKGKFGKRESRKTKLGIDHYVASVNVVRAMIDNWDVLFQVPP
				HIQRQVAKRVWKSSPEALDFIRRRNLRKIQSARIKMEEDALLSD
				PVETSAEARAAVLAQSKPSDEGSSEEPAVPSGTARSHDDEEGAG
				NPPIPEQDRPLLRVPREKEAKTGVSYFFP
736	A	40	317	LRVTAQWASHTLPDPVVGNPGSGWKEKDRDSEWGWRDLKSKTWV
				EVEAEGGLSGDTFQWLPQGSSQRPGLPLVNQGAGVQETKGAGPL*
				SPAPLPPGSPEGAQASGCSPVGAIGMYPLTGPLPPPPQPRSWI
				SGPSTPILSLCPSPSTRSQGFPPQGLEVCVTPIELLPEVRLKIR
				ECFPSFL
737	A	79	825	LTSWLLSPAHRRAGRLSSTVESGVRCLVARRSCFHVLASPQVKR
				EVMEGLSDVASFATKLKNTLIQYHSIEEDKWRVAKKTKDVTVWR
				KPSEEFNGYLYKAQGVIDDLVYSIIDHIRPGPCRLDWDSLMTSL
				DILENFEENCCVMRYTTAGQLWNIISPREFVDFSYTVGYKEGLL
				SCGISLDWDEKRPEFVRGYNHPCGWFCVPLKDNPNQSLLTGYIQ
				TDLRGMIPQSAVDTAMASTLTNFYGDLRK
738	A	10	914	GPGKETLESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLM
				LVDGIDPNFKMEHQNKRSPLHAAAEAGHVDICHMLVQAGANIDT
				CSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHL
				AAKKGHYEVVQYLLSNGQMDVNCQDDGGWTPMIWATEYKHVDLV
				KLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLH
				AVNIHGDSPLHIAARENRYDCVVLFLSRDSDVPLKNKEGETPLQ
				CASLNSQVWSALQMSKALQDSAPDRPSPVERIVSRDI
739	A	10	914	GPGKETLESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLM
				LVDGIDPNFKMEHQNKRSPLHAAAEAGHVDICHMLVQAGANIDT
				CSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHL
				AAKKGHYEVVQYLLSNGQMDVNCQDDGGWTPMIWATEYKHVDLV
				KLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLH
				AVNIHGDSPLHIAARENRYDCVVLFLSRDSDVPLKNKEGETPLQ
				CASLNSQVWSALQMSKALQDSAPDRPSPVERIVSRDI
740	A	10	914	GPGKETLESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLM
				LVDGIDPNFKMEHQNKRSPLHAAAEAGHVDICHMLVQAGANIDT
				CSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHL
				AAKKGHYEVVQYLLSNGQMDVNCQDDGGWTPMIWATEYKHVDLV
				KLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLH
				AVNIHGDSPLHIAARENRYDCVVLFLSRDSDVPLKNKEGETPLQ
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
				CASLNSQVWSALQMSKALQDSAPDRPSPVERIVSRDI
741	A	1	1227	MSRGPEEVNRLTESTYRNVMEQFNPGLRNLINLGKNYEKAVNAM
				ILAGKAYYDGVAKIGEIATGSPVST*TGTCPHRDFKYPQETSTR
				VFDGKFLKNSTKRLSMSWRRR*NLDVKYMNATLKRYQTEHKNKL
				ESLEKSQAELKKIRRKSQGSRNALKYEHKEIEYVETVTSRQSEI
				QKFIADGCKEALLEEKRRFCFLVDKHCGFANHIHYYHLQSAELL
				NSKLPRWQETCVDAIKVPEKIMNMIEEIKTPASTPVSGTPQASP
				MIERSNVVRKDYDTLSKCSPKMPPAPSGRAYTSPLIDMFNNPAT
				AAPNSQRVNNSTGTSEDPSLQRSVSVATGLNMMKKQKVKTIFPH
				TAGSNKTLLSFAQGDVITLLIPEEKDGWLYGEHDVSKARGWFPS
				SYTKLLEENETEA
742	A	27	800	RFSSFSLIVSALASLNPVTMSDPEGETLRSTFPSYMAEGERLYL
				CGEFSKAAQSFSNALYLQDGDKNCLVARSKCFLKMGDLERSLKD
				AEASLQSDPAFCKGILQKAETLYTMGDFEFALVFYHRGYKLRPD
				REFRVGIQKAQEAINNSVGSPSSIKLENKGDLSFLSKQAENIKA
				QQKPQPMKHLLHPTKGEPKWKASLKSEKTVRQLLGELYVDKEYL
				EKLLLDEGFGHFVGTGPWGKGNLGGCFMHELKAEPVI
743	A	458	51	AWAQCLPTSPPSCPRGSTSPLWPPLCWAFRAGHKGLGPSSAHDS
				AGSPAWP*NLPEGQGGLCPPPDPAPAAAGTGPPGYCRWPGRASS
				SPGRCGRWDWLWGCGCRGPRAAQVPHRAASGWPPAHTGSHRGAH
				CLGA
744	A	8	459	DTLSLNCTLPETLPMTPSF*LSFL*FPGLARAKSIPTKTYSNEV
				VTLWYRPPDILLGSTDYSTQIDMW*GQVEVWQGPCGKGGGLVTT
				ATQPAAFLFTVPSLPRGVGCIFYEMATGRPLFPGSTVEEQLHFI
				FRILSEEAWALCAVETHR
745	A	1848	568	CARVAAWGGKLRRGLAVSRQAVRSPGPLAAAVAGAALAGAGAAW
				HHSRVSVAARDGSFTVSAQKNVEHGIIYIGKPSLRKQRFMQFSS
				LEHEGEYYMTPRDFLFSVMFEQMERKTSVKKLTKKDIEDTLSGI
				QTAGCGSTFFRDLGDKGLISYTEYLFLLTILTKPHSGFHVAFKM
				LDTDGNEMIEKREFFKLQKIISKQDDLMTVKTNETGYQEAIVKE
				PEINTTLQMRFFGKRGQRKLHYKEFRRFMENLQTEIQEMEFLQF
				SKGLSFMRKEDFAEWLLFFTNTENKDIYWKNVREKLSAGESISL
				DEFKSFCHFTTHLEDFAIAMQMFSLAHRPVRLAEFKRAVKVATG
				QELSNNILDTVFKIFDLDGDECLSHEEFLGVLKNRMHRGLWVPQ
				HQSIQEYWKCVKKESIKGVKEVWKQAGKGLF
746	A	7	368	SSTWCPQPTTTPRKPTWSPSC*ALASSSSPGSSWPGSATCASS
				SSWTSRGWTRPGSGSSAPNCCSCWPSGPRPSQGTSRRSRLSGTL
				RTSWAASPPVT\SIPEEDASAPTGSAPEAGGSA
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
747	A	224	435	RGWALDWIGADLSLHLQEEVETEVAWEECGHVLLSLCYSSQQGG
				LLVGVLRCAHLAPMDANGYSDPFVRL
748	A	1	1760	MVHNQYGTCCLSSGMRECGHTYTSWPPRSLSLESSQIATNSIAQ
				GHQGRGAPQQLVVSRLSEGFITKAANNSAQVIEDMKDTNARCCL
				LMPHIFTPKSHPNQPTWENGATLRSHGEIYISARNPGIQVESST
				WELGVASLEEGINAFHIKNIYVKEDVNGSWVVQEHYHSSKDVES
				TQVPIHGGLDKENVVPMHDGILRSCKNRMKSCPLFFAATWMQQK
				AIILSKLMQKRKTKYHMFFITPDQSSQRTSFEVNGHCTSLRGGS
				KYRSGSVKTLRTIYNFSYHTRSVGRYPSSSAEDWGMKREKSALL
				ITDDTISNEAALVDDGYIIGEMLPPCGRCEKKSREQIVIPFFSL
				LIKDIYFLNEGCANRLPNGHVNFEKFWELAKQVSEFMTWKQVEC
				PFERDRKILQYLLTVPVFSEDVSGLPVCWRMSVCPSASVLPSVS
				SRRPAAPQTAPAKLRLIPPVCPACWHLSVCPAGVPFYQCAPLNV
				LSTTRHLRLLQQMCSSPRPATCVSVCRRSRVFIGPRWGRDHGGA
				GLCFLASRTTNTHEDPAVIGAPGSAKHTSSLKTRWRTYFLQLTD
				RLRFCETEMFTEDT
749	A	2	2331	AATHPQMVGPEDAGACSGRNPKLLPVPAPDPVGQDRKVTRATGG
				FGGGVGAVEPPEEADEEEETPPRQLLQRYLAAAGEQLEPGLCYC
				PLPAGQAGAPPPSAAPRSDACLLGSGSKHRGAEVADGRAPRHEG
				MTNGDSGFLPGRDCRDLEEARGLARAGGRESRRRRPYGRLRLEG
				PGDEDADGAGSPSDWASPLEDPLRSCCLVAADAQEPEGAGSDSG
				DSPASSCSSSEDSEQRGVGAGGPEEGAPPATSAERTNGGAEPRL
				GFSDIHFNSRNTFQVSRGQSARDHLPPAGPPVPLPAAEQGPAGA
				SARARRSGGFADFFTRNLFPKRTK\DLKSVVHSAPGWKLFGKVP
				PRENLQKTSKIIQQEYEARTGRTCKPPPQSSRRKNFEFEPLSTT
				ALILEDRPSNLPAKSVEEALRHRQEYDEMVAEAKKREIKEAHKR
				KRIMKERFKQEENIASAMVIWINEILPNWEVMRSTRRVRELWWQ
				GLPPSVRGKVWSLAVGNELNITPELYEIFLSRAKERWKSFSETS
				SENDTEGVSVADREASLELIKLDISRTFPSLYIFQKGGPYHDVL
				HSILGAYTCYRPDVGYVQGMSFIAAVLILNLEEADAFIAFANLL
				NKPCQLAFFRVDHSMMLKYFATFEVFFEENLSKLFLHFKSYSLT
				PDIYLIDWIFTLYSKSLPLDLACRVWDVFCRDGEEFLFRTGLGI
				LRLYEDILLQMDFIHIAQFLTKLPEDITSEKLFSCIAAIQMQNS
				TKKWTQVFASVMKDIKEGDKNSSPALKS
750	C	41	318	MSSMNPEYDYLFKLLLRFADDTYTESYISTIGVDFKIRTIELDG
				KTIKLQIWDTAGQXRFRTITSSYYRGAHGIIVVYDVTDQGSFNN
				VKQW
751	A	3	522	RAAWHEGKFGAVCTCMEKATGLKLSAKVIKKQTPKDKEMVLLEI
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
				EVMNQLNHRNLIQLYAAIETPHEIVLFMEYIEGGELFERIVDED
				YHLTEVDTMVFVRQICDGILFMHKMRVLHLDLKPENILCVNTTG
				HLVKIIDFGLARRYNPNEKLKVNFGTPEFLSPEVVNYDQIF
752	A	183	473	EKLASVSNLVTVFENSRTPEAAPRGHRLEDVHHRPECRPPESPG
				PREKTNVGEAVGSEPRTVSRRYLNSLKNKLSSEAWRKSCQPVTL
				SRSXTHVPE
753	A	15	416	ASVLGKETGFSLSELPRESSYDIYRVPSSQSMEDRGYSPDTRVV
				RFLKGKSIGLRLAGGNDVGIFVSGVQAGSPADGQGIQEGDQILQ
				VNDVPFQNLTREEAVQFLLGLPPGEEMELVTQRKQDIFWKMVQS
				RV
754	A	2	2180	KLLGSRGPRLLPPECRSVACVQALKGSKKLVLSVYSAGRIPGGY
				VTNHIYTWVDPQGRSISPPSGLPQPHGGALRQQEGDRRSTLHLL
				QGGDEKKVNLVLGDGRSLGLTIRGGAEYGLGIYITGVDPGSEAE
				GSGLKVGDQILEVNGRSFLNILHDEAVRLLKSSRHLILTVKDVG
				RLPHARTTVDETKWIASSRIRETMANSAGFLGDLTTEGINKPGF
				YKGPAGSQVTLSSLGNQTRVLLEEQARHLLNEQEHATMAYYLDE
				YRGGSVSVEALVMALFKLLNTHAKFSLLSEVRGTISPQDLERFD
				HLVLRREIESMK\ARQPPGPGAGEHLVPWCSYS*HGFHSTGSHG
				TSTTVSSARNTLDLEETGEAVQGNINALPDVSVDDVRSTSQGLS
				SFKPLPRPPPLAQGNDLPLGQPRKLGREDLQPPSSMPSCSGTVF
				SAPQNRSPPAGTAPTPGTSSAQDLPSSPIYASVSPANPSSKRPL
				DAHLALVNQHPIGPFPRVQSPPHLKSPSAKATVAGGCLLPPSPS
				GHPDQTGTNQHFVMGEVHRPDSEPDVNEVRALPQTRTASTLSQL
				SDSGQTLSEDSGVDAGEAEASAPGRGRQSASTKSRSSKELPRKE
				RPTDGANKPPGLLEPTSTLVRVKKSAATLGIAIEGGANTRQPLP
				RIVTIQRGGSAHNCGQLKVGHVILEVNGLTLRGKEHREAARIIA
				EAFKTKDRDYIDFLVTEFNVML
755	A	1812	1402	PAAGPALWRLPEELLLLICSYLDMRALGRLAQVCHWLRRFTSCD
				LLWRRIARASLNSGFTRLGTDLMTSVPVKERVKVSQNWRLGRCR
				EGILLKWRCSQMPWMQLEDDSLYISQANFILAYQFRPDGASLNR
				RPLGV
756	A	1812	1402	PAAGPALWRLPEELLLLICSYLDMRALGRLAQVCHWLRRFTSCD
				LLWRRIARASLNSGFTRLGTDLMTSVPVKERVKVSQNWRLGRCR
				EGILLKWRCSQMPWMQLEDDSLYISQANFILAYQFRPDGASLNR
				RPLGV
757	A	1	375	VLNPRKKCKKKKYVNSGTVTLLSFSVDSEFTFVDYIKGGTQLNF
				TVAIDFTASNGETRMSEKVGGNPLQPTSLHYMSPYQLSAYAMAL
				KAVGEIIQDYDSDKLFPAYGFGAKLPPEGRISHQFPL
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
758	A	5	658	QSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQL
				KQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKELGQKDR
				LLQQHQAKLEEALRKLSDVSYHQVDLERELEHKDVLLAHCMKRE
				ADEATNYNSHNSQSNGFLLPTAGKGATSVSNRGTSDLQLVRDAL
				RSLRNSFSGHDPQHHTIDSLEQGISSLMERLHVMETXKKKKK
759	A	1319	2694	LARPAQPVLLREPEGAGPPVPAGHLVHHLQGGHLRERAHPDLEA
				HEHPLPCDQMFWRQMGGHLRMVEANSRGVVWGIGYDHTAWVYTG
				GYGGGCFQGLASSTSNIYTQSDVKCVHIYENQRWNPVTGYTSRG
				LPTDRYMWSDASGLQECTKAGTKPPSLQWAWVSDWFVDFSVPGG
				TDQEGWQYASDFPASYHGSKTMKDFVRRRCWARKCKLVTSGPWL
				EVPPIALRDVSIIPESPGAEGSGHSIALWAVSDKGDVLCRLGVS
				ELNPAGSSWLHVGTDQPFASISIGACYQVWAVARDGSAFYRGSV
				YPSQPAGDCWYHIPSPPRQRLKQVSAGQTSVYALDENGNLWYRQ
				GITPSYPQGSSWEHVSNNVCRVSVGPLDQVWVIANKVQGSHSLS
				RGTVCHRTGVQPHEPKGHGWDYGIGGGWDHISVRANATRAPRSS
				SQEQEPSAPPEAHGPVCC
760	A	3	1015	SSRPVRPRPAARLSAMSSTQFNKGPSYGL\SAQ\VKNRLL\SKY
				DPQKE\AELRTW\IEGLTGLSIGPDFQKG\LKDG\TIL\CTLMN
				KLQPG\SVPKINRSMQN\WHQLENLSNFIK\AMVSYGMNP\VDL
				FEANDLF\ESGNMT\QVQVSLLALGGKRPKTKGAAEGGLDIGVK
				YSEKQERNFDDATMKAGQCVIG\LQMGT\NKCASQSGMTAYGTR
				RHLYDPKNHILPPMDHSTISLQMGT\NKCASQVG\MTA\PGTRR
				HIYEYQAGNPTSCDNFSM\SLQ\MGYTQGAQTQSGQVF\GPGRP
				DI*TPSTCPQGTI\ADGAPSGTGDCPDPGEVPEYPPYYQEEAGY
761	A	3	674	SLVGSGVYGLGAGEVCAAATSAAIPSRAPAPRTRGRAGLPTEPR
				GPAAVVSRPPAWKSV*ASKMSSIKHLVYAVIRFLREQSQMDTYT
				SDEQESLEVAIQCLETVFKISPEDTHLAVSQPLTEMFTSSFCKN
				DVLPLSNSVPEDVGKADQLKDEGNNHMKEENYAAAVDCYTQAIE
				LDPNNAVYYCNRAAAQSKLRHYTDAIKDCEKAIAIDSQYSKAYG
				RMGL
762	A	2	854	RPPAARARRWLPKPSPARRSRRPAHRCSRRRRTCTPQATRPGMR*
				APAAACGPTGRRS/RLPALKLALEYIVPCMNKHGICVVDDFLG
				KETGQQIGDEVRALHDTGKFTDGQLVSQKSDSSKDIRGDKITWI
				EGKEPGCETIGLLMSSMDDLIRHCNGKLGSYKINGRTKAMVACY
				PGNGTGYVRHVDNPNGDGRCVTCIYYLNKDWDAKVSGGILRIFP
				EGKAQFADIEPKFDRLLFFWSDRRNPHEVQPAYATRYAITVWYF
				DADERARAKVKY/RNR*KRCEG
763	A	1813	986	MPALRPALLWALLALWLCCATPAHALQCRDGYEPCVNEGMCVTY
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
				HNGTGYCKCPEGFLGEYCQHRDPCEKNRCQNGGTCVAQAMLGKA
				TCRCASGFTGEDCQYSTSHPCFVSRPCLNGGTCHMLSRDTYECT
				CQVGFTGKECQWTDACLSHPCANGSTCTTVANQFSCKCLTGFTG
				QKCETDVNECDIPGHCQHGGICLNLPGSYQCQCLQGFTGQYCDS
				LYVPCAPSPCVNGGTCRQTGDFTFECNCLPETVRRGTELWERDR
				EVWNGKEHDEN*
764	A	3	1505	IPGSTISSPLQGRPAELLGRCQRPCHRHVADMVISESMDILFRI
				RGGLDLAFQLATPNEIFLKKALKHVLSDLSTKLSSNALVFRICH
				SSVYIWPSSDINTIPGELTDASACKNILRFIQFEPEEDIKRKFM
				RKKDKKLSDMHQIVNIDLMLEMSTSLAAVTPIIERESGGHHYVN
				MTLPVDAVISVAPEETWGKVRKLLVDAIHNQLTDMEKCILKYMK
				GTSIVVPEPLHFLLPGKKNLVTISYPSGIPDGQLQAYRKELHDL
				FNLPHDRPYFKRSNAYHFPDEPYKDGYIRNPHTYLNPPNMETGM
				IYVVQGIYGYHHYMQDRIDDNGWGCAYRSLQTICSWFKHQGYTE
				RSIPTHREIQQALVDAGDKPATFVGSRQWIGSIEVQLVLNQLIG
				ITSKILFVSQGSEIASQGRELANHFQSEGTPVMIGGGVLAHTIL
				GVAWNEITGQIKFLILDPHYTGAEDLQVILEKGWCGWKGPDFWN
				KDAYYNLCLPQRPNMI
765	A	1391	730	RTRGINTSSRLLNLRQVSKTRLSEPGTDLVEPSPKHTPNTSDNE
				GSDTEVCGPNSPSKRGNSTGIKLVRKEGGLDDSVFIAVKEIGRD
				LYRGLPTEERIQKLEFMLDKLQNEIDQELEHNNSLVREEKETTD
				TRKKSLLSAALAKSGERLQALTLLMIHYRAGIEDIETLESLSLD
				QHSKKISKYTDDTEEDLDNEISQLIDSQPFSSISDDLFGPSESV
766	A	276	1421	GSHQKQMLVPCFLYSLQNRKPSLYGSLTCQGIGLDGIPEVTASE
				GFTVNEINKKSIHISCPKENASSKFLAPYTTFSRIHTKSITCLD
				ISSRGGLGVSSSTDGTMKIWQASNGELRRVLEGHVFDVNCCRFF
				PSGLVVLSGGMDAQLKIWSAEDASCVVTFKGHKGGILDTAIVDR
				GRNVVSASRDGTARLWDCGRSACLGVLADCGSSINGVAVGAADN
				SINLGSPEQMPSEREVGTEAKMLLLAREDKKLQCLGLQSRQLVF
				LFIGSDAFNCCTFLSGFLLLAGTQDGNIYQLDVRSPRAPVQVIH
				RSGAPVLSLLSVRDGFIASQGDGSCFIVQQDLDYVTELTGADCD
				PVYKVATWEKQIYTCCRDGLVRRYQLSDL
767	A	528	971	HPLGSGSAPGNHYLLTLVSSCPSVAPVLEGAGDRHSHLSGLELL
				LCPHALVDTVPAPPSALHGDTHAHTHTHVHTHCPIAQETCRGPP
				LGASRLSPQGPGHLTLAPQEGSYLDFWDTHRGDPKPRRRRKSL\
				KTFSLTPATFRGIWAL
768	A	1802	1413	PEKATVVNQDGQPLIE*KLKEKQVRWKFIKRWKTRYFTLAGNQL
				LFQKGKSKDDPDDCPIELIKVQSVKAVAKKRRDRSLPRAFEIFT
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
				DNKTYVFKAKDEKNAEEWLQCINVAVAQAKERESREVTTYL
769	A	1674	479	RSPSRDHHGDPSAGPRLREVESRGTTFLLLSFPSSVGKGLSPAS
				ASKMKNYKAIGKIGEGTFSEVMKMQSLRDGNYYACKQMKQRFES
				DRKSGSLALICELMDMNIYELIRGRRYPLSEKKIMHYMYQLCKS
				LDHIHRNGIFHRDVKPENILIKDVLKLGDFGSCRSVYSKQPYTE
				YISTRWYRAPECLLTDGFYTYKMDLWSAGCVFYEIASLQPLFPG
				VNELDQISKIHDVIGTPAQKILTKFKQSRAMNFDFPFKKGSGIP
				LLTTNLSPQCLSLLHAMVGYD\PDERIAAHQALQHPYFQEQ/QK
				QSLKQEEDRPKRRGPAYVMEL\PKLKLSG\VVRLSSYSSPTL\Q
				SVLGSGTNGRVRLLRP*KCIPASKKTDPRK\DLKPAPQQCRLPT
				IVRKGGR
770	A	3	1795	LGLGSGTLLSVSEYKKKYREHVLQLHARVKERNARSVKITKRFT
				KLLIAPESAAPEEALGPAEEPEPGRARRSDTHTFNRLFRRDEEG
				RRPLTVVLQGPAGIGKTMAAKKILYDWAAGKLYQGQVDFAFFMP
				CGELLERPGTRSLADLILDQCPDRGAPVPQMLAQPQRLLFILDG
				ADELPALGGPEAAPCTDPFEAASGARVLGGLLSKALLPTALLLV
				TTRAAAPGRLQGRLCSPQCAEVRGFSDKDKKKYFYKFFRDERRA
				ERAYRFVKENETLFALCFVPFVCWIVCTVLRQQLELGRDLSRTS
				KTTTSVYLLFITSVLSSAPVADGPRLQGDLRNLCRLAREGVLGR
				RAQFAEKELEQLELRGSKVQTLFLSKKELPGVLETEVTYQFIDQ
				SFQEFLAALSYLLEDGGVPRTAAGGVGTLLRGDAQPHSHLVLTT
				RFLFGLLSAERMRDIERHFGCMVSERVKQEALRWVQGQGQGCPG
				VAPEVTEGAKGLEDTEEPEEEEEGEEPNYPLELLYCLYETQEDA
				FVRQALCRFPELALQRVRFCRMDVAVLSYCVRCCPAGQALRLIS
				CRLVAAQEKKKKSLGKRLQASLGGG
771	A	2	464	EDREDHVPKLEQINSTRILSSQNFTLTKKELLSTELLLLEAFSW
				NLCLPTPAHFLDYYLLASVSQKDHHCHTWPTTCPRKTKECLKEY
				AHYFLEVTLQDHIFYKFQPSVVAAACVGASRICLQLSPYWTRDL
				QRISSYSLEHLSTCIEILLVVY
772	A	101	857	GQCPGCIQFTKLSSGRCMELEMCIITEENREDLVQRGDECGRAT
				ASLVFHIYIWYMYFLYIYLYILHPGIPVICTISQGDMGASKARQ
				ERVRQGRGSDGAGWGLAHRSCRSFSDCKRAPGS/GRRQV/PGSK
				ASPPAPRPACDPPPSPQTSSSSGPASCRSSCAACRTAPPPRCPA
				AAPARAEAPTAGTAARAWPRRCGYA*WGRPPVADVPAAAGRVSR
				GTARAAAAGPPAGSLSPAAGRAPRTGWVGAAARR
773	A	3139	3792	DFAAKKRRENLRAGEILTLDLASEGSPHARQASEIRQHVLNTTR
				LVNNLLDMARIQSGGFNLKKEWLTLEEVVGSALQMLEPGLSSPI
				NLSLPEPLTLIHVDGPLFERVLINLLENAVKYAGAQAEIGIDAH
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
				VEGENLQLDVWDNGPGLPPGQEQTIFDKFARGNKESAVPGVGLG
				LAICRAIVDVHGGTITASTDRKVVPVFVLHFPQQMALNLKIS
774	A	915	435	LRQYSVKMRIVPTILLNFGADPDLRDIRYNTVLHYAVCGQSL\S
				LVEKL\LEYEADLEAKNKDGYTPLLVARY*QLIPKLVKFLLE\K
				GADVNASDNYQRTALILAVSGEPPCLVKLLLQQGGEICNEG\MV
				DSQLRNMFISMVLLHRYPQFTASHGK\QKHAK
775	A	1554	233	EFLGSGVSPDLANEDGLTALHQCCIDDFREMVQQLLEAGANINA
				CDSECWTPLHAAATCGHLHLVELLIASGANLLAVNTDGNMPYDL
				CDDEQTLDCLETAMADRGITQDSIEAARAVPELRMLDDIRSRLQ
				AGADLHAPLDHGATLLHVAAANGFSEAAALLLEHRASLSAKDQD
				GWEPLHAAAYWGQVPLVELLVAHGADLNAKSLMDETPLDVCGDE
				EVRAKLLELKHKHDALLRAQSRQRSLLRRRTSSAGSRGKVVRRV
				SLTQRTDLYRKQHAQEAIVWQQPPPTSPEPPEDNDDRQTGAELR
				PPPPEEDNPEVVRPHNGRVGGSPVRHLYSKRLDRSVSYQLSPLD
				STTPHTLVHDKAHHTLADLKRQRAAAKLQRPPPEGPESPETAEP
				GLPGDTVTPQPDCGFRAGGDPPLLKLTAPAVEAPVERRPCCLLM
776	A	710	169	PLSPCQGPLSVFSAKNRWRLVGPVHLTRGEGGFGLTLRGDSPVL
				IAAVIPGSQAAAAGLKEGDYIVSVNGQPCRWWRHAEVVTELKAA
				GEAGASLQVVSLLPSSRLPSLGDRRPVLLGPRGLLRSQREHGCK
				TPASTWASPRPLLNWSRKAQQGKTGGCPQPCAPVKPAPPSSLKH
				PGWP
777	A	3	1049	TRDELDQFLDKMDDPDYWRTVQDPMTGRDLRLTDEQVALVRRLQ
				SGQFGDVGFNPYEPAVDFFSGDVMIHPVTNRPADKRSFIPSLVE
				KEKVSRMVHAIKMGWIQPRRPRDPTPSFYDLWAQEDPNAVLGRH
				KMHVPAPKLALPGHAESYNPPPEYLLSEEERLAWEQQEPGERKL
				SFLPRKFPSLRAVPAYGRFIQERFERCLDLYLCPRQRKMRVNVD
				PEDLIPKLPRPRDLQPFPTCQALVYRGHSDLVRCLSVSPGGQWL
				VSGSDDGSLRLWEVATARCVRTVPVGGVVKSVAWNPNPAVCLVA
				AAVEDSVLLLNPTLGDRLVAGSTDQLLSAFVPPEEPPLQPA
778	A	208	784	THLWPHQRPFLFAFLRWQDCKFTCHPECRSLIQLDCSQQEGLSR
				DRPSPESTLTVTFSQNVCKPVEETQRPPTLQEIKQKIDSYNTRE
				KNCLGMKLSEDGTYTGFIKVHLKLRRPVTVPAGIRPQSIYDAIK
				EVNLAATTDKRTSFYLPLDAIKQLHISSTTTVSEVIQGLLKKFM
				VVDNPQKFALFKRIHK
779	A	3	845	IRVIGESDIMQEFLSESDENYNGVSDVELRVALPDGTTVTVRVK
				KNSTTDQVYQAIAAKVGMDSTTVNYFALFEVISHSFVRKLAPNE
				FPHKLYIQNYTSAVPGTCLTIRKWLFTTEEEILLNDNDLAVTYF
				FHQAVDDVKKGYIKAEEKSYQLQKLYEQRKMVMYLNMLRTCEGY
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
				NEIIFPHCACDSRRKGHVITAISITHFKLHACTEEGQLENQVIA
				FEWDEMQRWDTDEEGMAFCFEYARGEKKPRWVKIFTPYFNYMHE
				CFERVFCELKWRKEEY
780	A	3	1197	VLSDLCLFYYRDEKEEGILGSILLPSFQIALLTSEDHINRKYAF
				KAAHPNMRTYYFCTDTGKEMELWMKAMLDAALVQTEPVKRVDKI
				TSENAPTKETNNIPNHRVLIKPEIQNNQKTKEMSKIEEKKALEA
				EKYGFQKDGQDRPLTKINSVKLNSLPSEYESGSACPAQTVHYRP
				INLSSSENKIVNVSLADLRGGNRPNTGPLYTEADRVIQRTNSMQ
				QLEQWIKIQKGRGHEEETRGVISYQTLPRNMPSHRAQIMARYPE
				GYRTLPRNSKTRPESICSVTPSTHDKTLGPGAEEKRRSMRDDTM
				WQLYEWQQRQFYNKQSTLPRHSTLSSPKTMVNISDQTMHSIPTS
				PSHGSIAAYQGYSPQRTYRSEVSSPIQRGDVTIDRRHRAHHPKVK
781	A	1	542	SGSSHASDGSGFQELRICSEDQTPLIAGMCSLPMARYYIIKYAD
				QKALYTRDGQLLVGDPVADNCCAEKICTLPNRGLDRTKVPIFLG
				IQGGSRCLACVETEEGPSLQLEDVNIEELYKGGEEATRFTFFQS
				SSGSAFRLEAAAWPGWFLCGPAEPQQPVQLTKESEPSARTKFYF
				EQSW
782	A	1140	467	VNSATEDRRSIRGLDSTPPQSRRCCAMPGVGNSGPSTFSSETAH
				PCSRKKVHFGSIHDAVRAGDVKQLSEIVVRGASINELDVLHKFT
				PLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQD
				ACVQALIMNGANLTAQDDRGCTPLHLAATHGHSFTLQIMLRSGV
				DPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCSIEDVDYNGNL
				PEPP
783	A	2	770	PLELEQTIRFR\KKVEKDENYVNAIMQLGSIMEHCIKQNNAIDI
				YEEYFNDEEAMEVMEEDPSAKTINVFRDPQEIKRAATHLSWHPD
				GNRKLAGAYSCLDFQRAPVGMSSDSYIWDLENPNKPELALKPSS
				PLVTLEFNPKDSHVLLGGCYNGQIACWDTRKGSLVAELSTIESS
				HRDPVYGTIWLQSKTGTECFSASTDGQVMWWDIRKMSEPTEVVI
				LDITKKEQLENALGAISLEFESTLVSVPCCPFPDLH
784	A	45	456	FKGIRSLEIKGFMHHWSYPCAVLQLRQPGSALTPLKLPCQSPGG
				LPGAEVTYMNMTAYNKGRLQSSFWIVDKQHVYIGSAGLDWQSLG
				QMKELGVIFYNCSCLVLDLQRIFALYSSLKFKSRVPQTWSKRLY
				GVYDN
785	A	411	17	NKGPGDWRQDGGFPYLTQPWPSPKARLSTLWPQQEVSPGPGDTW
				LDKALQPGRPRLSLTQWLCGAGH*LPPCPLPSLPPP\TA*HVNC
				VPRTAVVGTGYANWNDSRTKIKLGQEEGASQGALLGPESPSSLL
786	A	4	549	EGTAEAFVNSINAPASERTLWARERTQDLAPLEKHSVGENTMVT
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
				KTHDQPVEEEDRYQGEDPESPFTQSDEGSSETPNSLASEEGNSS
				SETGELPVQGDSQSQGDQHGESVQGGHNNNPDTQRQGTPGEKNR
				ALEAVVPAVRGEDVQLTEDQEQPARGEHKNQGPRTKGPGAAVEL
				NVHSDP
787	A	214	916	RLPTGHQFSGVEGLILLQSPKSVAEGRRRLGVQSGFSLPRFDGS
				FFWGQVMKVLRHKYLINFYRAIESTSRVYIILELAQGGDVLEWI
				QRYGACSEPLAGKWFSQLTLGIAYLHSKSIVHR*GRCHPDWGLC
				PQGGFMHISHFLSFFPLS/TLPPQYLAYSCTLF*SYGQGY**ST
				HCMQSIL*NTMVSSRWSSDTILCLSPYFGLCSQLHGFPSSLPCA
				IIMVSTSHFLCPHLY
788	A	214	916	RLPTGHQFSGVEGLILLQSPKSVAEGRRRLGVQSGFSLPRFDGS
				FFWGQVMKVLRHKYLINFYRAIESTSRVYIILELAQGGDVLEWI
				QRYGACSEPLAGKWFSQLTLGIAYLHSKSIVHR*GRCHPDWGLC
				PQGGFMHISHFLSFFPLS/TLPPQYLAYSCTLF*SYGQGY**ST
				HCMQSIL*NTMVSSRWSSDTILCLSPYFGLCSQLHGFPSSLPCA
				IIMVSTSHFLCPHLY
789	A	3	379	YNQKVDLFSLGIIFFEMSYHPMVTASERIFVLNQLRDPTSPKFP
				EDFDDGEHAKQKSVISWLLNHDPAKRPTATELLKSELLPPPQME
				ESELHEVLHHTLTNVDGKAYRTIDGPRSFRQRISPAI
790	A	2	4966	RWPRRARLLRRGRGGGGVESLPHFGAPVPRARLQLTARRGHAGL
				RARMREAAAALVPPPAFAVTPAAAMEEPPPPPPPPPPPPEPETE
				SEPECCLAARQEGTLGDSACKSPESDLEDFSDETNTENLYGTSP
				PSTPRQMKRMSTKHQRNNVGRPASRSNLKEKMNAPNQPPHKDTG
				KTVENVEEYSYKQEKKIRAALRTTERDHKKNVQCSFMLDSVGGS
				LPKKSIPDVDLNKPYLSLGCSNAKLPVSVPMPIARPARQTSRTD
				CPADRLKFFETLRLLLKLTSVSKKKDREQRGQENTSGFWLNRSN
				ELIWLELQAWHAGRTINDQDFFLYTARQAIPDIINEILTFKVDY
				GSFAFVRDRAGFNGTSVEGQCKATPGTKIVGYSTHHEHLQRQRV
				SFEQVKRIMELLEYIEALYPSLQALQKDYEKYAAKDFQDRVQAL
				CLWLNITKDLNQKLRIMGTVLGIKNLSDIGWPVFEIPSPRPSKG
				NEPEYEGDDTEGELKELESSTDESEEEQISDPRVPEIRQPIDNS
				FDIQSRDCISKKLERLESEDDSLGWGAPDWSTEAGFSRHCLTSI
				YRPFVDKALKQMGLRKLILRLHKLMDGSLQRARIALVKNDRPVE
				FSEFPDPMWGSDYVQLSRTPPSSEEKCSAVSWEELKAMDLPSFE
				PAFLVLCRVLLNVIHECLKLRLEQRPAGEPSLLSIKQLVRECKE
				VLKGGLLMKQYYQFMLQEVLEDLEKPDCNIDAFEEDLHKMLMVY
				FDYMRSWIQMLQQLPQASHSLKNLLEEEWNFTKEITHYIRGGEA
				QAGKLFCDIAGMLLKSTGSFLEFGLQESCAEFWTSADDSSASDE
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQPRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
				IIRSVIEISRALKELFHEARERASKALGFAKMLRKDLEIAAEFR
				LSAPVRDLLDVLKSKQYVKVQIPGLENLQMFVPDTLAEEKSIIL
				QLLNAAAGKDCSKDSDDVLIDAYLLLTKHGDRARDSEDSWGTWE
				AQPVKVVPQVETVDTLRSMQVDNLLLVVMQSAHLTIQRKAFQQS
				IEGLMTLCQEQTSSQPVIAKALQQLKNDALELCNRISNAIDRVD
				HMFTSEFDAEVDESESVTLQQYYREAMIQGYNFGFEYHKEVVRL
				MSGEFRQKIGDKYISFARKWMNYVLTKCESGRGTRPRWATQGFD
				FLQAIEPAFISALPEDDFLSLQALMNECIGHVIGKPHSPVTGLY
				LAIHRNSPRPMKVPRCHSDPPNPHLIIPTPEGFSTRSMPSDARS
				HGSPAAAAAAAAAVAASRPSPSGGDSVLPKSISSAHDTRGSSVP
				ENDRLASIAAELQFRSLSRHSSPTEERDEPAYPRGDSSGSTRRS
				WELRTLISQSKDTASKLGPIEAIQKSVRLFEEKRYREMRRKNII
				GQVCDTPKSYDNVMHVGLRKVTFKWQRGNKIGEGQYGKVYTCIS
				VDTGELMAMKEIRFQPNDHKTIKETADELKIFEGIKHPNLVRYF
				GVELHREEMYIFMEYCDEGTLEEVSRLGLQEHVIRLYSKQITIA
				INVLHEHGIVHRDIKGANIFLTSSGLIKLGDFGCSVKLKNNAQT
				MPGEVNSTLGTAAYMAPEVITRAKGEGHGRAADIWSLGCVVIEM
				VTGKRPWHEYEHNFQIMYKVGMGHKPPIPERLSPEGKDFLSHCL
				ESDPKMRWTASQLLDHSFVKVCTDEE
791	A	20	432	SRAAALLEAVTETLFYYEVAEKIWSNRANRQCADCGSSRPDWAA
				VNLGVVICKQCAGQHRALGSGISKVQSLKLDTSVWSNEIVQLFI
				VLGNDRANRFWAGTLPPGEGLHPDATPGPRGEFISRKYRLGLFR
				KPHPQ
792	A	1121	320	SSCFQTSSHACFVTEFVPGGDPMMQIHEDVFPEPQARFYVACVV
				LGLQFLHEKKIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFG
				DRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGEC
				PFPGDTEEEVFDCIRLHGRPPTPAFLSVQG\VKFIQKLLQKCPE
				KPLGAGDQNAEEIKVQPFFRPTNWQALLARTIQPPFVPTLCGPA
				DLRYFEGEFHRAA\PALTPPAPHSLLTARQQAAFRDFDFVSERF
				LEP
793	A	2480	385	HLLIAQELADRVGEGRACWSLGNAYVSMGRPAQALTFAKKHLQI
				SQEIGDRHGELTARMNVAQLQLVLGRLTSPAASEKPDLAGYEAQ
				GARPKRTQRLSAETWDLLRLPLEREQNGDSHHSGDWRGPSRDSL
				PLPVRSRKYQEGPDAERRPREGSHSPLDSADVRVHVPRTSIPRA
				PSSDEECFFDLLTKFQSSRMDDQRCPLDDGQAGAAEATAAPTLE
				DRIAQPSMTASPQTEEFFDLIASSQSRRLDDQRASVGSLPGLRI
				THSNAGHLRGHGEPQEPGDDFFNMLIKYQSSRIDDQRCPPPDVL
				PRGPTMPDEDFFSLIQRVQAKRMDEQRVDLAGGPGAGGRRPARA
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
				PAAVPAWCELRPCAHRQAHPAPTPGRRSHSHSHVLPRPLPRTGT
				GHAAPRPPRPRATGSGQAARGGRACFHPGLAPMALSFLPSAPAA
				GRTGPSACRPRPGAVRLPHPLPQALPVLPCPAKCETLLSPSPSP
				KVSLSRLLGPPRTGPCSVPPELVLGWPCDRHAPPLQLRPGAGLP
				PSLSPHSPARGQQPQKAPQTTHGRPGCSGSPEVPPAESQGPAGA
				STGAGPISKAEGMAGHELRHSKTPSQEKGQGLVLGMLTGSKSSA
				QSGWEVAPGSVTLTQVGGWSVEAGEASLSSTLQTPHMRTPLLPP
				AGGDDITALSMGRGLTGHQVRDPRTGRTCWSLRWAPGA
794	A	543	1307	PSSIPSPELPQKNQRLEKYKDVIGCLPRVTRRTLATLIGHLYRV
				QKCAALNQMCTRNLALLFAPSVFQTDGRGEHEVRVLQELIDGYI
				SVFDIDSDQVAQIDLEVSLITTWKDVQLSQAGDLIMEVYIEQQL
				PDNCVTLKVSPTLTAEELTNQVLEMRGTAAGMDLWVTFEIREHG
				ELERPLHPKEKVLEQALQWCQLPEPCSASLLLKKVPLAQAGCLF
				TGIRRESPRVGLFAVFVRSHLACWGSRFQERFFLV
795	A	3	312	PSECAGIRRLKKTDIPLLQRLLQGPSEKNARIFLMDKDAEEISS
				DVAQYINFHFSLLESILQRLNEEEKREIQRIVTKFNKEKAIILK
				CLQNKLVIKTETTV
796	A	631	488	MHLLCFLDFPLLMQQTFLHHVKRMRPFSSQNFYLAITFHHRLTM
				TSR*
797	A	1	396	FRGTPVSGLTNRDTLAVIRHFREPIRLKTVKPGKVINKDLRHYL
				SLQFQKGSIDHKLQQVIRDNLYLRTIPCTTRAPRDGEVPGVDYN
				FISVEQFKALEESGALLESGTYDGNFYGTPKPPAEPSPFQPDPV
798	A	1100	1741	RRTFSRASVRRREFLQAISKPCGSATAPRGCPPPWPLSGIS/HT
				PNVKVSRLLILGGANVNYRTEVLNNAPILCVQSHLGHEEVVTLL
				LEFGACLDGTSENGMTALCYAAAAGHMKLVCLLTKKGVRVDHLD
				KKGQCALVHSALRGHGDILQYLLTCEWSPGPPQPGTLRKSHALQ
				QALTAAASMGHSSVVQCLLGMEKEHEVEVNGTDTLWGET
799	A	1100	1741	RRTFSRASVRRREFLQAISKPCGSATAPRGCPPPWPLSGIS/HT
				PNVKVSRLLILGGANVNYRTEVLNNAPILCVQSHLGHEEVVTLL
				LEFGACLDGTSENGMTALCYAAAAGHMKLVCLLTKKGVRVDHLD
				KKGQCALVHSALRGHGDILQYLLTCEWSPGPPQPGTLRKSHALQ
				QALTIAAASMGHSSVVQCLLGMEKEHEVEVNGTDTLWGET
800	A	1	496	FRKVECTPSREHLKHQTVYRLLKCAPRGKNGFTPLHMAVDKDTT
				NVGRYPVGRFPSLHVVKVLLDCGADPDSRDFDNNTPLHIAAQNN
				CPAIMNALIEAGAHMDATNAFKKTAYELLDEKLLARGTMQPFNY
				VTLQCLAARALDKNKIPYKGFIPEDLEAFIELH
801	A	5405	370	CDRCQEGHFGFNGCGGCRPCACGPAAEGSECHPQSGQCHCRPGT
				MGPQCRECAPGYWGLPEQGCRRCQCPGGRCDPHTGRCNCPPGLS
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
				GERCDTCSQQHQVPVPGGPVGHSIHCEVCDHCVVLLLDDLERAG
				ALLPAIHEQLRGINASSMAWARLHRLNASIADLQSQLRSPLGPR
				HETAQQLEVLEQQSTSLGQDARRLGGQAVGTRDQASQLLAGTEA
				TLGHAKTLLAAIRAVDRTLSELMSQTGHLGLANASAPSGEQLLR
				TLAEVERLLWEMRARDLGAPQAAAEAELAAAQRLLARVQEQLSS
				LWEENQALATQTRDRLAQHEAGLMDLREALNRAVDATREAQELN
				SRNQERLEEALQRKQELSRDNATLQATLHAARDTLASVFRLLHS
				LDQAKEELERLAASLDGARTPLLQRMQTFSPAGSKLRLVEAAEA
				HAQQLGQLALNLSSIILDVNQDRLTQRAIEASNAYSRILQAVQA
				AEDAAGQALQQADHTWATVVRQGLVDRAQQLLANSTALEEAMLQ
				EQQRLGLVWAALQGARTQLRDVRAKKDQLEAHIQAAQAMLAMDT
				DETSKKIAHAKAVAAEAQDTATRVQSQLQAMQENVERWQGQYEG
				LRGQDLGQAVLDAGHSVSTLEKTLPQLLAKLSILENRGVHNASL
				ALSASIGRVRELIAQARGAASKVKVPMKFNGRSGVQLRTPRDLA
				DLAAYTALKFYLQGPEPEPGQGTEDRFVMYMGSRQATGDYMGVS
				LRDKKVHWVYQLGEAGPAVLSIDEDIGEQFAAVSLDRTLQFGHM
				SVTVERQMIQETKGDTVAPGAEGLLNLRPDDFVFYVGGYPSTFT
				PPPLLRFPGYRGCIEMDTLNEEVVSLYNFERTFQLDTAVDRPCA
				RSKSTGDPWLTDGSYLDGTGFARISFDSQISTTKRFEQELRLVS
				YSGVLFFLKQQSQFLCLAVQEGSLVLLYDFGAGLKKAVPLQPPP
				PLTSASKAIQVFLLGGSRKRVLVRVERATVYSVEQDNDLELADA
				YYLGGVPPDQLPPSLRRLFPTGGSVRGCVKGIKALGKYVDLKRL
				NTTGVSAGCTADLLVGRAMTFHGHGFLRLALSNVAPLTGNVYSG
				FGFHSAQDSALLYYRASPDGLCQVSLQQGRVSLQLLRTEVKTQA
				GFADGAPHYVAFYSNATGVWLYVDDQLQQMKPHRGPPPELQPQP
				EGPPRLLLGGLPESGTIYNFSGCISNVFVQRLLGPQRVFDLQQN
				LGSVNVSTGCAPALQAQTPGLGPRGLQATARKASRRSRQPARHP
				ACMLPPHLRTTRDSYQFGGSLSSHLEFVGILARHRNWPSLSMHV
				LPRSSRGLLLFTARLRPGSPSLALFLSNGHFVAQMEGLGTRLRA
				QSRQRSRPGRWHKVSVRWEKNRILLVTDGARAWSQEGPHRQHQG
				AEHPQPHTLFVGGLPASSHSSKLPVTVGFSGCVKRLRLHGRPLG
				APTRMAGVTPCILGPLEAGLFFPGSGGVITLDLPGATLPDVGLE
				LEVRPLAVTGLIFHLGQARTPPYLQLQVTEKQVLLRADDGAGEF
				STSVTRPSVLCDGQWHRLAVMKSGNVLRLEVDAQSNHTVGPLLA
				AAAGAPAPLYLGGLPEPMAV\QP\WPPAYCGCMRRLAVNR/SPP
				VAMTRSVEVHGAVGASGCPSPTRTQPTPAPGQAPAAASHRPLCS
				PHRCLFGL
802	A	3	574	DAWADAWAVVCPDSQEDSETRAQEDSGSEQPPDSVLPDKLKVSW
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
				ENPSPQEAPAA*SAEPFQAPCSETSEAAPREGGKPPTPPPKILS
				EKLKASMGEMQASGPPAPGTVQVSVNGMDDSPEPAKPSQAEGTP
				GTPPKDATTSTALPPWDLPP/PVPSPLLLPWGLAWGRPAASLAA
				QGTAISGPAGGEGGL
803	A	321	542	MGVVLYVMLCASLPFDDTDIPKMLWQQQKGVSFPTHLSISADCQ
				DLLKRLLEPDMILRPSIEEVSWHPWLAST*
804	A	1	513	MKSTSGEDAVNIIEMTTKDLEYYINSVDTAAPGFERTECNFERS
				STGGTLQTLPRPLPLRHFRFRRRSHISGVLSSGAGASNPCPYCV
				CEEASKRGSHVQRGISEGLSGVEKRGGLLFFHLTLKRHAGSTES
				DTSEPVSTVWFGLDFHWYSGVLDKSLDLAFVICEVDRFQ
805	A	4	549	EGTAEAFVNSINAPASERTLWARERTQDLAPLEKHSVGENTMVT
				KTHDQPVEEEDRYQGEDPESPFTQSDEGSSETPNSLASEEGNSS
				SETGELPVQGDSQSQGDQHGESVQGGHNNNPDTQRQGTPGEKNR
				ALEAVVPAVRGEDVQLTEDQEQPARGEHKNQGPRTKGPGAAVEL
				NVHSDP
806	A	1	913	AHASAEGDAEGEAEGPVGSTLGSYATLTRRPGRSALVRTSPSVT
				PTPARGTPRSQSFALRARRKGPPPPPPKRLSSVSGPSPEPPPLD
				GSPGPKEGATGPRRRTLSEPAGPSEPPGPPAPAGPASDTEEEEP
				GPEGTPPSRGSSGEGLPFAEEGNLTIKQRPKPAGPPPRETPVPP
				GLDFNLTESDTVKRRPKCREREPLQTALLAFGVASATPGPAAPL
				PSPTPGESPPASSLPQPEPSSLPAQGVPTPLAPSPAMQPPVPPC
				PGPGLESSAASRWNGETEPPAAPAALLKVPGAGTAPKPVS
807	B	361	1371	MTKTHVIAASKEAFYTWQYRVAKKLTALEINQITRSRKEGRESR
				LAIIDISGVLTFFDLDARVTDSTGQQVVGELLKLERRDVWDMKW
				AKDNPDLFAMMEKTRMYVFRNLDPEEPIQTSGYICNFEDLEIKS
				VLLDEILKDPEHPNKDYLINFEIRSLRDSRALIEKVGIKDASQF
				IEDNPHPRLWRLLAEAALQKLDLYTAEQAFVRCKDYQGIKFVKR
				LGKLLSESMKQAEVVGYFGRFEEAERTYLEMDRRNTLELDCGLG
				RTGSVNFHTFLTLAKLFMALQQRHGIGSLSLAKESLLNVKDLLS
				IEPWHSEVYMVDPEEGVPELAIDKAAVA
808	A	214	916	RLPTGHQFSGVEGLILLQSPKSVAEGRRRLGVQSGFSLPRFDGS
				FFWGQVMKVLRHKYLINFYRAIESTSRVYIILELAQGGDVLEWI
				QRYGACSEPLAGKWFSQLTLGIAYLHSKSIVHR*GRCHPDWGLC
				PQGGFMHISHFLSFFPLS/TLPPQYLAYSCTLF*SYGQGY**ST
				HCMQSIL*NTMVSSRWSSDTILCLSPYFGLCSQLHGFPSSLPCA
				IIMVSTSHFLCPHLY
809	A	2	3708	FVPDCSVRTSESARRRDQRAQRSGRSPPTSAPSASRAGRRLEAS
				EEVFKMKKFNFRKVLDGLTASSPGSGSSSGSNSGGGAGSGSVHP
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
				AGTAGVLREEIQETLTSEYFQICKTVRHGFPHQPTALAFDPVQK
				ILAIGTRTGAIRILGRPGVDCYCQHESGAAVLQLQFLINEGALV
				SASSDDTLHLWNLRQKRPAILHSLKFNRERITYCHLPFQSKWLY
				VGTERGNTHIVNIESFILSGYVIMWNKAIELSTKTHPGPVVHLS
				DSPRDEGKLLIGYENGTVVFWDLKSKRAELRVYYDEAIHSIDWH
				HEGKQFMCSHSDGSLTLWNLKSPSRPFQTTIPHGKSQREGRKSE
				SCKPILKVEYKTCKNSEPFIIFSGGLSYDKACRRPSLTIMHGKA
				ITVLEMDHPTVEFLTLCETPYPNEFQEPYAVVVLLEKDLIVVDL
				TQSNFPIFENPYPMDIHESPVTCTAYFADCPPDLILVLYSIGVK
				HKKQGYSNKEWPISGGAWILGAQTYPEIIITGHADGSIKFWDAS
				AITLQMLYKLKTSKVFEKQKVGEGKQTCEIVEEDPFAIQMIYWC
				PESRIFCVSGVSAYVIIYKFSRHEITTEIVSLEVRLQYDVEDII
				TPEPETSPPFPDLSAQLPSSRSLSGSTNTVASEGVTKDSIPCLN
				VKTRPVRMPPGYQAELVIQLVWVDGEPPQQITSLAVSSAYGIVA
				FGNCNGLAVVDFIQKTVLLSMGTIDLYRSSDLYQRQPRSPRKNK
				QFIADNFCMRGLSNFYPDLTKRIRTSYQSLTELNDSPVPLELER
				CKSPTSDHVNGHCTSPTSQSCSSGKRLSSADVSKVNRWGPGRPP
				FRKAQSAACMEISLPVTTEENRENSYNRSRSSSISSIDKDSKEA
				ITALYFMDSFARKNDSTISPCLFVGTSLGMVLIISLNLPLADEQ
				RFTEPVMVLPSGTFLSLKGAVLTFSCMDRMGGLMQPPYEVWRDP
				NNIDENEKSWRRKVVMNSSSASQEIGDHQYTIICSEKQAKVFSL
				PSQTCLYVHNITETSFILQANVVVMCSSACLACFCANGHIMIMS
				LPSLRPMLDVNYLPLTDMRIARTFCFTNEGQALYLVSPTEIQRL
				TYSQEMCDNLQDMLGDLFTPIETPEAQNRGFLKGLFGGSGQTFD
				REELFGEASAGKASRSLAQHIPGPGSIEGMKGAAGGVMGELTRA
				RIALDERGQRLGELEEKTAGMMTSAEAFSKHAHELMLKYKDKKW
				YQF
810	A	1	993	MPSGWSGSPIDWLAWDNLEQPPLYPKKLVQTYSVFPNQDEMSDV
				VVQPYNSLLTLKRLTQNADCVEIKDYGPAKGGKKKDPNAPKRPP
				SGFFLFCSEFCPKSKSTNPGIPIGDVAKKLGEMWKNLNDSEKQP
				YITQAAKLKEKYEKDVAVYKSKGKSDGAKGPAKVAQKKVEEEDE
				DEEFCILHSAAELGGDLEPHPEKGLPEDDPDIVVKGWLYREPRG
				GGARPWLPPRRAWFVLTRDSLDQFSSSGKGARRLGSLVLTSLCS
				VTGPERRRKETGLWSVTVSGRKHSVRLCSPRQAEAERWGVALRE
				VIASKAPLETPTQLLLRDIQPPE
811	A	1	641	SLRLAWHEGKLHFSVYDFDRFSRHDLIGQVVLDNLLELAEQPPD
				RPLWRDIVEGGSEKADLGELNFSLCYLPTAGRLTVTIIKASNLK
				AMDLTGFSDPYVKASLISEGRRLKKRKTSIKKNTLNPTYNEALV
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
				FDVAPESVENVGLSIAVVDYDCIGHNEVIGVCRVGPDAADPHGR
				EHWAEMLANPRKPVEHWHQLVEEKTVTSFTKGSKGLS
812	A	340	509	REKEMDMSDPNFWTVLSNFTLPHLRSGNRLRRTQSCRTSNRKSL
				IGNGQSPALPRP
813	A	37	372	MSFGPYFYVCFIPILLYSLNTKGYGNPYPCFPSTPPKFPFGQPR
				ERSQPQPQPLLPLPWFCRAVLACWEGLTRSVCSSRCLQGEGRKA
				KWGGRQPPQALWPQPAEGRRQPA*
814	A	3	379	YNQKVDLFSLGIIFFEMSYHPMVTASERIFVLNQLRDPTSPKFP
				EDFDDGEHAKQKSVISWLLNHDPAKRPTATELLKSELLPPPQME
				ESELHEVLHHTLTNVDGKAYRTIDGPRSFRQRISPAI
815	A	139	445	SVRHLKYSLFKKSLLGSVSDNGIVTLWDVNSQSPYHNFDRVHKA
				PASGICFSPVNELLFVTIGLDKRIILYDTSSKKLVKTLVADTPL
				TAVDFMPDGATLAI
816	A	264	799	WESDVGEGLRPPPPPPPPGRRRTQEPRARDAATVIFACPAALLE
				TLIAYGSSSPSFCKHRAARPLIFLLHRLTAEATARCPICALEAR
				NPGRWGICASWPGMKTPFGKAAAGQRSRTGAGHGSVSVTMIKRK
				AAHKKHRSRPTSQPRGNIVGCIIQHGWKDGDEPLTQWKGTVLDQ
				LL
817	A	127	1271	TFTSGKTAVGKLAQPYKATLVSSAGASQVKWNKKNANCLATSHD
				GDVRIWDKRKPSTAVEYLAAHLSKIHGLDWHPDSEHILATSSQD
				NSVKIWDYRQPRKYLNILPCQVPVWKARYTPFSNGLVTVMVPQL
				RRENSLLLWNVFDLNTPVHTFVGHDDVVLEFQWRKQKEGSKDYQ
				LVTWSRDQTLRMW/PVDSQMQRLCANDILDGVDEFIESISLLPE
				PEKTLHTEDTDHQHTASHGEEEALKEDPPRNLLEERKSDQLGLP
				QTLQQEFSLINVQIRNVNVEMDAADRSCTVSVHCSNHRVKMLVK
				FPAQYPNNAAPSFQFINPTTITSTMKAKLLKILKDTALQKVKRG
				QSCLEPCLRQLVSCLESFVNQEDSASSNPFA
818	A	398	1	DLVCKISGFGRGPRDRSEAVYTTMSGRSPALWAAPETLQFGHFS
				SASDVWSFGIIMWEVMAFGERPYWDMSGQDVIKAVEDGFRLPPP
				RNCPNLMHRLMLDCWQKDPGERPRFSQIHSILSKMVQDPEPPNV
819	A	2619	326	GPSGPKGYRGQKGAKGNMGEPGEPGQKGRQGDRGIEGPIGFPGP
				KGVPGFKGEKGEFGADGRKGAPGLAGKNGTDGQKGKLGRIGPPG
				CKGDPGNRGPDGYPGEAGSPGERGDQGGKGDPWPP\GRRGPPGE
				IGAKGSKGYQGNNGAPGSPGVKGAKGGPGPRGPKGEPGRRGDPG
				TKGSPGSDGPKGEKGDPGPEGPRGLAGEVGNKGAKGDRGLPGPR
				GPQGALGEPGKQGSRGDPGDAGPRGDSGQPGPKGDPGRPGFSYP
				GPRGAPGEKGEPGPRGPEGGRGDFGLKGEPGRKGEKGEPADPGP
				PGEPGPRGPRGVPGPEGEPGPPGDPGLTECDVMTYVRETCGCCD
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
				CEKRCGALDVVFVIDSSESIGYTNFTLEKNFVINVVNRLGAIAK
				DPKSETGTRVGVVQYSHEGTFEAIQLDDERIDSLSSFKEAVKNL
				EWIAGGTWTPSALKFAYDPLIKESRRQKTRVFAVVITDGRHDPR
				DDDLNLRALCDRDVTVTAIGIGDMFHEKHESENLYSIACDKPQQ
				VRNMTLFSDLVAEKFIDDMEDVLCPDPQIVCPDLFCQTELSVAQ
				CTQRPVDIVFLLDGSERLGEQNFHKARRFVEQVARRLTLARRDD
				DPLNARVALLQFGGPGEQQVAFPLSHNLTAIHEALETTQYLNSF
				SHVGAGVVHAINAIVRSPRGGARRHAELSFVFLTDGVTGNDSLH
				ESAHSMRKQNVVPTVLALGSDVDMDVLTTLSLGDRAAVFHEKDY
				DSLAQPGFFDRFIRWIC
820	A	2	860	PRVRELKEILDRKGHFSENETRWIIQSLASAIAYLHNNDIVHRD
				LKLENIMVKSSLIDDNNEINLNIKVTDFGLAVKKQSRSEAMLQA
				TCGTPIYMAPEVISAHDYSQQCDIWSIGVVMYMLLRGEPPFLAS
				SEEKLFELIRKGELHFENAVWNSISDCAKSVLKQLMKVDPAHRI
				TAKELLDNQWLTGNKLSSVRPTNVLEMMKEWKNNPESVEENTTE
				EKNKPSTEEKLKSYQPWGNVPETNYTSDEEEEKQVGRIIAAFLP
				SVKYPHHTWNIFLQICLFVVSL
821	A	1	1003	LQDSAREYSELLDKASETDDPYERMVLVAAFAVSGYCSTYFRAG
				SKPFNPVLGETYECIREDKGFRFFSEQVSHHPPISACHCESKNF
				VFWQDIRWKNKFWGKSMEILPVGTLNVMLPKYGDYYVWNKVTTC
				IHNILSGRRWIEHYGEVTIRNTKSSVCICKLTFVKVNYWNSNMN
				EVQGVVIDQEGKAVYRLFGKWHEGLYCGVAPSAKCIWRPGSMPT
				NYELYYGFTRFAIELNELDPVLKDLLPPTDARFRPDQRFLEEGN
				LEAAASEKQRVEELQRSRRRYMEENNLEHIPKFFKKVIDANQRE
				AWVSNDTYWELRKDPGFSKVDSPVLW
822	A	3038	476	VALTTSMCCNKQVIVIDKIKSASIADRCGALHVGDHILSIDGTS
				MEYCTLAEATQFLANTTDQVKLEILPHHQTRLALKGPDHVKIQR
				SDRQLTWDSWASNHSSLHTNHHYNTYHPDHCRVPALTFPKAPPP
				NSPPALVSSSFSPTSMSAYSLSSLNMGTLPRSLYSTSPRGTMMR
				RRLKKKDFKSSLSLASSTVGLAGQVVHTETTEVVLTADPVTGFG
				IQLQGSVFATETLSSPPLISYIEADSPAERCGVLQIGDRVMAIN
				GIPTEDSTFEEASQLLRDSSITSKVTLEIEFDVAESVIPSSGTF
				HVKLPKKHNVELGITISSPSSRKPGDPLVISDIKKGSVAHRTGT
				LELGDKLLAIDNIRLDNCSMEDAVQILQQCEDLVKLKIRKDEDN
				SDEQESSGAIIYTVELKRYGGPLG\ITISGTEEP\FDL*IISSL
				TKGGLAERTGAIHIGDRIL\AINSSSLKGKPLSEAIHLLQMAGE
				TVTLKIKKQTDAQSASSPKKFPISSHLSDLGDVEEDSSPAQKPG
				KLSDMYPSHGCPSVDSAVDSWDGSA\IDTS\YGTEGT\SFQASG
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
				Y\NFNTYDWRSPKQRGS\LSPVT\KPRSQTYPDVGLSYEDWDRS
				TASGFAGAA\DSAETEQEENFWSQALEDLETCGQSGILRELEAT
				IMSGSTMSLNHEAPTPRSPAGSDRPSFQERSSSRPHYSQTTRSN
				TLPSDVGRKSVTLRKMKQEIKEIMSPTPVELHKVTLYKDSDMED
				FGFSVADGLLEKGVYVKNIRPAGPGDLGGLKPYDRLLQVNHVRT
				RDFDCCLVVPLIAESGNKLDLVISRNPLASQKSIDQQSLPGD*S
				EQNSAFFQQPSHGGNLETREPTNTL
823	A	1100	1741	RRTFSRASVRRREFLQAISKPCGSATAPRGCPPPWPLSGIS/HT
				PNVKVSRLLILGGANVNYRTEVLNNAPILCVQSHLGHEEVVTLL
				LEFGACLDGTSENGMTALCYAAAAGHMKLVCLLTKKGVRVDHLD
				KKGQCALVHSALRGHGDILQYLLTCEWSPGPPQPGTLRKSHALQ
				QALTAAASMGHSSVVQCLLGMEKEHEVEVNGTDTLWGET
824	A	998	276	EEGEERQGEGEEEEDGEELRRGLLRPAGVGGRMASVSSATFSGH
				GARSLLQFLRLVGQLKRVPRTGWVYRNVQRPESVSDHMYRMAVM
				AMVIKDDRLNKDRCVRLALVHDMAECIVGDIAPADNIPKEEKHR
				REEEAMKQITQLLPEDLRKELYELWE\EVYMEYETQSSAEAKFV
				KQLDQCEMILQASEYEDLEHKPGRLQDFYDSTAGKFNHPEIVQL
				VSELEAERSTNIAAAASEPHS
825	A	2	454	SVKRQPGFGQTTAKRHPSQGQQAVVKAALSILLNKAVLHGCPLP
				RAELDQHTADFKGGSFPLSIVSSYNTCNKKKGESGAWRKVNNSP
				RRKSGRFSLPTWNKPDLSTEGMKNKTISQLNCNRNASLSKQKSL
				ENDLSLTLNLDQRLSLGSD
826	A	2	414	GSGLYRGPTPGGQCIWKPNSMPPDHERNFGFTQFALELNELTAE
				LKRSLPSTDTRLRPDQRYLEEGNIQAAEAQKRRIEQLQRDRRKV
				MEENNIVHQARFFRRQTDSSGKEWWVTNNTYWRLRAEPGYGNMD
				GAVLW
827	A	16	691	RFVEDRIPYQDRESYSQPAWHHRGPPQRDWKWEKDGFNNTRKNS
				FPHSLRNGGGPRGRSGWHKGVAGGSSTWFHNHSNSGGGWLSNSG
				AVDWNHNGTGRNSSWLSEGTGGFSSWHMNNSNGNWKSSVRSTNN
				WNYSGPGDKFQPGRNRNSNCQMEDMTMLWNKKSNKSNKYSHDRY
				NWQRQENDKLGTVATYRGPSEGFTSDKFPSEGLLDFNFEQLESQ
				TTKQA
828	A	1	522	RGGVSDMLIKVQATEQMGYCPIQCEKLCYLPGNSKCSSVYENCL
				EQSRAIGNVHPRGVQSQRDTSLLKHTCRVDLFDDPCYINTQALQ
				STPGSAGNQ\GQPNHWGAHGTAERH/LETVQPGATAQPASSHSL
				PHIKQQLWSEECYHGKLSRKAAESLLVKDGDFLVRESATSPGQN
829	A	3	500	RVVEFEAFNMDSAYSEQAAVLLQRSRPSRGGTSAWGKCSLPKFT
				VPKGRLGVTRIGDLSLQDMRKVPSLALIELTALCDILGLDLKRS
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
				KAGKWKAAETRLFGVPLDSLLEADHKVLPSTQVPLVLQALLSCL
				EKRGLDMEGILRVPGSQARVKVHPEAADTFAHG
830	A	3	232	HEQDKNKYNTPKYRMIVRVTNRDIICQIAYARIEGDMIVCATYA
				HELPKYGVKVGLTYYACTYSTVVLVARTLLDT
831	A	3	497	WRGLMVMSAIEKLLRQVDWGQLDYLVVDMPPGTGDVQLSVSQNI
				PITGAVIVSTPQDIALMDAHKGAEMFRRVHVPVLGLVQNMSVFQ
				CPKCKHKTHIFGADGARKLAQTLGLEVLGDIPLHLNIREASDTG
				QPIVFSQPESDEAKAYLRIAVEVVRRLPSPSE
832	A	196	545	GLSRAAMVWWQQAQPSLEMQNDAGEFVDLYVPRKCSASNRIIGA
				KDHASIQMNVA\RLTRSQAGLMASLKLMLSAGPFVGWVSQMIPF
				SDWPR\RWHRLKELLTGENHRCGIFVINK
833	A	2	877	GTRNGQFEPRRGRAWEGSAGGLRAPGAAAGGPGVQPRGSG/LPG
				NAIRAGVNPGRGPASPFWDLSLPWDLWPPPTDHAPGAPDFPAVE
				GR\PWAGGRPPWPVSGVLGSRVCGPLYSTSPAGPG/SGGLSPSQ
				GGPAGAGGDAG/LPGRCPSAPWRAGSRPAASCPDWIPGPQGLWL
				HRNPTS/GPPSQIGEGAEQGDEGVADAPQIQCKN/GAEDPPAED
				EPPQVPEAGEEDAVPAEEGPGGTPETQADQVRERPEAHLAEGGA
				KGSPRRLADPQDLPAGQMSLAPPFPPVAAVIRSNK
834	A	2	877	GTRNGQFEPRRGRAWEGSAGGLRAPGAAAGGPGVQPRGSG/LPG
				NAIRAGVNPGRGPASPFWDLSLPWDLWPPPTDHAPGAPDFPAVE
				GR\PWAGGRPPWPVSGVLGSRVCGPLYSTSPAGPG/SGGLSPSQ
				GGPAGAGGDAG/LPGRCPSAPWRAGSRPAASCPDWIPGPQGLWL
				HRNPTS/GPPSQIGEGAEQGDEGVADAPQIQCKN/GAEDPPAED
				EPPQVPEAGEEDAVPAEEGPGGTPETQADQVRERPEAHLAEGGA
				KGSPRRLADPQDLPAGQMSLAPPFPPVAAVIRSNK
835	A	2	877	GTRNGQFEPRRGRAWEGSAGGLRAPGAAAGGPGVQPRGSG/LPG
				NAIRAGVNPGRGPASPFWDLSLPWDLWPPPTDHAPGAPDFPAVE
				GR\PWAGGRPPWPVSGVLGSRVCGPLYSTSPAGPG/SGGLSPSQ
				GGPAGAGGDAG/LPGRCPSAPWRAGSRPAASCPDWIPGPQGLWL
				HRNPTS/GPPSQIGEGAEQGDEGVADAPQIQCKN/GAEDPPAED
				EPPQVPEAGEEDAVPAEEGPGGTPETQADQVRERPEAHLAEGGA
				KGSPRRLADPQDLPAGQMSLAPPFPPVAAVIRSNK
836	A	167	691	MGWVWTLCTASACLTLLFWSQTPGKAFQIPCPPPHLSHWCLSPM
				QMDDGCARLCVLWTAWMRWRVLMCSCRVWATDLGIFLGVALGNE
				PLEMWPLTQNEECTVTGFLRDKLQYRSRLQYMKHYFPINYKIRV
				PYEGVFRIANVTRLRAQGSERELRYLGVLVSLSATESVHDELL
837	A	167	691	MGWVWTLCTASACLTLLFWSQTPGKAFQIPCPPPHLSHWCLSPM
				QMDDGCARLCVLWTAWMRWRVLMCSCRVWATDLGIFLGVALGNE
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
				PLEMWPLTQNEECTVTGFLRDKLQYRSRLQYMKHYFPINYKIRV
				PYEGVFRIANVTRLRAQGSERELRYLGVLVSLSATESVHDELL
838	A	145	1815	PCGRVPAPLPPGRAPITGTRWP/PLGTQPDLGSALYQENYKQMK
				ALVNQLHERVEHIKLGGGEKARALHISRGKLLPRERIDNLIDPG
				SPFLELSQFAGYQLYDNEEVPGGGIITGIGRVSGVECMIIANDA
				TVKGGAYYPVTVKKQLRAQEIAMQNRLPCIYLVDSGGAYLPRQA
				DVFPDRDHFGRTFYNQAIMSSKNIAQIAVVMGSCTAGGAYVPAM
				ADENIIVRKQGTIFLAGPPLVKAATGEEVSAEDLGGADLHCRKS
				GVSDHWALDDHHALHLTRKVVRNLNYQKKLDVTIEPSEEPLFPA
				DELYGIVGANLKRSFDVREVIARIVDGSRFTEFKAFYGDTLVTG
				FARIFGYPVGIVGNNGVLFSESAKKGTHFVQLCCQRNIPLLFLQ
				NITGFMVGREYEAEGIAKDGAKMVAAVACAQVPKITLIIGGSYG
				AGNYGMCGRAYSPRFLYIWPNARISVMGGEQAANVLATITKDQR
				AREGKQFSSADEAALKEPIIKKFEEEGNPYYSSARVWDDGIIDP
				ADTRLVLGLSFSAALNAPIEKTDFGIFRM
839	A	1401	1731	RRSLLRPPPQALPMMAPSHHPSPAPLPASPPPPAPPPPLAPPRD
				PLALRAPPVPQAPRAPPAPRALQAPPAPRARPPARGRRGGTAPG
				PRWPRPGARVPGARGQAPGSRP
840	A	2	1081	FVTDFPARSMAATSLMSALAARLLQPAHSCSLRLRPFHLAAVRN
				EAVVISGRKLAQQIKQEVRQEVEEWVASGNKRPHLSVILVGENP
				ASHSYVLNKTRAAAVVGINSETIMKPASISEEELLNLINKLNND
				DNVDGLLVQLPLPEHIDERRICNAVSPDKDVDGFHVINVGRMCL
				DQYSMLPATPWGVWEIIKRTGIPTLGKNVVVAGRSKNVGMPIAM
				LLHTDGAHERPGGDATVTISHRYTPKEQLKKHTILADIVISAAG
				IPNLITADMIKEGAAVIDVGINRVHDPVTAKPKLVGDVDFEGVR
				QKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLRLEEREVLKSK
				ELGVATN
841	A	1	1197	MAWPCISRLCCLARRWNQLDRSDVAVPLTLHGYSDLDSEEPGTG
				GAASRRGQPPAGARDSGRDVPLTQYQRDFGLWTTPAGPKDPPPG
				RGPGAGGRRGKSSAQSSAPPAPGARGVYVLPIGDADAAAAVTTS
				YRYGLGRDRNESPPCGGRTRRPGARGMGWAAERRRLEPGSHATS
				ELPAASEVTPVWSVGTAGGAFAAPCPETVLEHPRAGSAPLPSQP
				PSWGQPSEWPAFSRVGTGLPLTPTAGPSRARGARRPCPPALPGH
				CLLDRTYTGLQTLGAETLLAVVNSAAMNVGVQVVDVELHRHSLG
				EDCIYPQSSESDISDAPPSLPLTIPAPVKASSPIKQSHEPVPDT
				SVEKGS\PGSCPFHL*GPLSHLGSSPGFLLWRPPGLLSSVALVA
				SCS
842	A	1	2775	MHVERRVCHAVSKYNVTLSCVAGGLAAKSSGLELIWLCDLLVRE
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
				LGQLTGPVCKVRTPALIYGRHHQPPLPRPLPTLTCAASRWPQPE
				EATAPPGEGGQKDRALLPGIPAGPKDQCQNRRKISSRTATRPEP
				EPPQDRSQNRRKTSARTAEPQGLSLPEDDDPAPLSCRLGCLLTH
				CLPSWVPCCPPESTTLDVVEVESYDPYTDSWTPVSPALKYVSNF
				SAAGCRGRLYLVGSSACKYNALALQCYNPVTDAWSVIASPFLPK
				YLSSPRCAALHGELYLIGDNTKKVYVYDPGANLWQKVQSQHSLH
				ENGALVPLGDALYVTGGRWQGMEGDYHVEMEAYDTVRDTWTRHG
				ALPRLWLYHGASTVFLDVSNKKTEGYRPLLQLVGPSVDPAESMC
				MDGECANGLRREGTATYTGKMLHLRGRVIHRPSPVPGVVSADRS
				EVWLLLPDSAAPGTWQGSQSLLPHPVNQDRVRPPFPSGLFSKEF
				PGNSSPRCECKGFGAWTAEQRVVRLGRLLGTAAPIFPPQHPGLR
				IGQPAPKRRPCIPPDQPGTKGSDLAAGFVSDKRAQSALKSQGPS
				LAALPGAQIAQGLSQEGPSQNCAQCQHQSGCSADRNGNFRKHHC
				PCFGLPGPPGPPGPQGPPGPIIPPEALLKEFQLLLKGAVRQRER
				AEPEPCTCGPAGPVAASLAPVSATAGEDDDDVAAFLCRLRRDAL
				VERRALHELGVYYLPDAEGAFRRGPGLNLTSGQYRAPVAGFYAL
				AATLHVALGEPPRRGPPRPRDHLRLLICIQSRCQRNACRQAPEE
				RPRPLGGSPGLSQHGEHGSRGSVCMREVLRPCRAGTRWRKSLAL
				QKLGSHPLHTHYQGRGRKHQGSHLLSSEREVTAKNLNYECRSRT
				GGKGRLRLILLFVQPVEVAGLPVPGRYLQGSSVPWNLGDTFKSKY
843	A	1204	193	PDGHLALMSQPREVREFNGDHFLLERAIRADFALVKGWKADRAG
				NVVFRRSARNFNVPMCKAADVTAVEVG/AFPPEDIHVPNIYVGR
				VIKGQKYEKRIERLTIRKEEDGDAGKEEDARTRIIRRAALEFED
				GMYANLGIGIPLLASNFISPSMTVHLHSENGILGLGPFPTEDEV
				DADLINAGKQTVTVLPGGCFFASDDSFAMIRGGHIQLTMLGAMQ
				VSKYGDLANWMIPGKKVKGMGGAMDLVSSQKTRVVVTMQHCTKD
				NTPK\IMEKCTMPLTGK\RCVDRIITEKPVFDVHRKKELTLREL
				WEGLRVDD\IKKSTGCAFAVSPNLRPMQQVAP
844	A	707	858	MSRFLLPREGCLLIVFMLCEKTLPFLFTLKEYTFIPEHRTTDIN
				CVNTHE
845	A	3	372	MSPGIIQQLLSCSCHLPKDQQAKLPPTTLEKYGYSTGAVTLLTL
				GSMLGTALVLFHSCEENYRLILQLFVGLAVGTLSGDALLHLIPQ
				VLGLHKQEAPEFGHFHESKGHIWKLMGLIGGIHGF
846	A	1420	1855	KAQGLTKKVKSEKQPVKRLPAKFLQLW*EKQKRSSSSQDKDKDS
				RCTRQHCTEEDEEEDEEEEEESFMTSREMIPERNKQEKESDDAS
				TVNEETSEENNEMEESDVSQ/D*ERFTTFWKVVKTKALKVSGSS
				DCRETEELVGSNSQ
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ* KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
847	A	384	3	GGGID/SDASLVIAGVRLEDEGRYRCELINGIEDESVALTLSLE
				GEALPLPPHSCVAAGPPRLGLPGLLPSISSAPLGTPAPSPRPRR
				PSSPSAPIRWPSPGSPPPPRCGVSVPTQPGPVPVQLLRGVY
848	A	581	367	QDSALLQLHGL*SLVDKLSPPGQRRLDLFSCLLRHRLKLSTSEG
				VRIQSALQAFNAKLPNTMDYDTTKLCS
849	A	33	512	TAARCQGGPTHVPAFVGTACPTRIPGHAPARQCREYYY*YYYDF/
				WKEPRRCHALLLPPWAGLEVGMPPSHTQLGMHPAPPPPHLEVK
				AQG\PSNRQRTDGCRWCSGRASALGGGRQDSRLRERGGGYDH/H
				CPICRSLKIQLKCHPASGPQTVGLGRLASVS
850	A	108	440	MQATSNLLNLLLLSLFAGLNPSKTHINPKEGWQVYSSAQDPDGR
				GICTVVAPEQNLCSRDAKSRQLRQLLEKVQNMSQSIEVLNLRTQ
				RDFQYVLKMETQMKGLKAKFRQI
851	A	108	440	MQATSNLLNLLLLSLFAGLNPSKTHINPKEGWQVYSSAQDPDGR
				GICTVVAPEQNLCSRDAKSRQLRQLLEKVQNMSQSIEVLNLRTQ
				RDFQYVLKMETQMKGLKAKFRQI
852	A	112	861	QSQLCAGNSGPALGVGGPGCPKSAETHARSSPVATGSRVGGRRA
				PCGPGMTSQRSPLAPLLLLSLHGVAASLEVSESPGSIQVARGQT
				SSLACTFTTSAALINLNVIWMVTPLSNANQPEQVILYQGGQMFD
				GAPRFHGRVGFTGTMPATNVSIFINNTQLSDTGTYQCLVNNLPD
				IGGRNIGVTGLTVLVPPSAPHCQIQGSQDIGSDVILLCSSEEGI
				PRPTYLWEKLDNTLKLPPTATQDLGDDLEQ
853	A	1	247	IEDDGEIISDVLKIPVQLVFKNKIKLYWSKVKAEPSEKVSLRIS
				VTQPDSIVGIVAVDKSVNLMNASNDITMENVSLAIFSL
854	A	2	640	VVAVEYALSNYLFAAVGNPKDLFEVCLMAQDLDTAASYLIILQN
				MEVPAVSRQHATLLFNTALEQGKWDLCRHMIRFLKAIGSGESET
				PPSTPTAQEPSSSGGFEFFRNRSISLSQSAENVPASKFSLQKTL
				SMPSGPSGKRWSKDSDCAENMYIDMMLWRHARRLLEDVRLKDLG
				CFAAQLGFELISWLCKERTRAARVDNFVIALKRLHKD
855	A	1	1326	RTRMFLEEKIPSISDLKLAIRRATLKRSFTPVFLGSALKNKGVQ
				PLLDAVLEYLPNPSEVQNYAILNKEDDSKEKTKILMNSSRDNSH
				PFVGLAFKLEVGRFGQLTYVRSYQGELKKGDTIYNTRTRKKVRL
				QRLARMHADMMEDVEEVYAGDICALFGIDCASGDTFTDKANSGL
				SMESIHVPDPVISIAMKPSNKNDLEKFSKGIGRFTREDPTFKVY
				FDTE/RQRDSYIWNGRITP\EIYAQRLEREYGCPCITGK/TKSC/
				RFERPLLPLSRLTLHIKNNQVVQAS/MGKVIGVLEPLDPEGL\
				PKLEFSDETFGSNI\PKQFVPAVEKGFLDACEKGPLSGHKLSGL
				RFVLQDGAHHMVDSNEISFIRAGEGALKQALANATLCIL\EPIM
				AVEVVAPNEFQGTS/ILAGINRRHGVITGQDGVEDYFTLYADVS
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
				SLGHWQSCFY
856	A	673	122	PQSPQTDQTAQGQQALAPPAGRSGQ*GRPGRRARLGPGERHS*A
				PPPLSQLLLQTFPHLQALPSAHARPSGQPHADRGHSRSPSGTSA
				PALSAGA*APARGPEQARCPQAGRVCHCPRGGRRGPESSG*RPE
				APQASPEKGPLGFGPVPRTARTRAQASSRCQVAPRPEALCCPPP
				KGGRHPSQ
857	A	116	632	WHWPTSTNPRGQHL*CSAS*PLLCGSTMTDGATGCTRAPSAQPS
				SSSRQSGYRR*RRRRACTQTRASTPSR*APASASGRWP*CYASS
				LRTGTTLTSTASTTVPWLCPLFCCCPSKQPAPPFPASQQQHMES
				WRRQATPSRAATRALPSAKGHTGRLLTAAIYEGRPKPGQV
858	A	2	476	FVQHCPSLPLSTVLGASWALPWASGSHPPSRLPCRMPQLSLSWL
				GLGPVAASPWLLLLLVGGSWLLARVLAWTYTFYDNCRRLQCFPQ
				PPKQNWFWGHQGLVTPTEEGMKTLTQLVTTYPQGFKLWLGPTFP
				LLILCHPDIIRPITSASAAVAPKDMI
859	A	739	792	ASFLLQMCP*GPVQSLSSEP*GSGGFCLPLKSAQGT*T/PQDTC
				RQGHPGIPGNPGHNGLPGRDGRDGAKGDKGDAGEPGRPGSPGKD
				GTSGEKGERGADGKVEAKGIKGDQGS\*GSPGKHGPKGLAGPMG
				EKGLRGETGPQGQKGNKGDVGPTGPEGPRGNIGPLGPTGLPGPM
				GPIGKPGPKGEAGPTGPQGEPGVRGIRGWKGDRGEKGKIGETLV
				LPKSAFTVGLTVLSKFPSSDVPIKFDKIHIT
860	A	739	792	ASFLLQMCP*GPVQSLSSEP*GSGGFCLPLKSAQGT*T/PQDTC
				RQGHPGIPGNPGHNGLPGRDGRDGAKGDKGDAGEPGRPGSPGKD
				GTSGEKGERGADGKVEAKGIKGDQGS\*GSPGKHGPKGLAGPMG
				EKGLRGETGPQGQKGNKGDVGPTGPEGPRGNIGPLGPTGLPGPM
				GPIGKPGPKGEAGPTGPQGEPGVRGIRGWKGDRGEKGKIGETLV
				LPKSAFTVGLTVLSKFPSSDVPIKFDKIHIT
861	A	739	792	ASFLLQMCP*GPVQSLSSEP*GSGGFCLPLKSAQGT*T/PQDTC
				RQGHPGIPGNPGHNGLPGRDGRDGAKGDKGDAGEPGRPGSPGKD
				GTSGEKGERGADGKVEAKGIKGDQGS\*GSPGKHGPKGLAGPMG
				EKGLRGETGPQGQKGNKGDVGPTGPEGPRGNIGPLGPTGLPGPM
				GPIGKPGPKGEAGPTGPQGEPGVRGIRGWKGDRGEKGKIGETLV
				LPKSAFTVGLTVLSKFPSSDVPIKFDKIHIT
862	A	739	792	ASFLLQMCP*GPVQSLSSEP*GSGGFCLPLKSAQGT*T/PQDTC
				RQGHPGIPGNPGHNGLPGRDGRDGAKGDKGDAGEPGRPGSPGKD
				GTSGEKGERGADGKVEAKGIKGDQGS\*GSPGKHGPKGLAGPNG
				EKGLRGETGPQGQKGNKGDVGPTGPEGPRGNIGPLGPTGLPGPM
				GPIGKPGPKGEAGPTGPQGEPGVRGIRGWKGDRGEKGKIGETLV
				LPKSAFTVGLTVLSKFPSSDVPIKFDKIHIT
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
863	A	2	394	SFKYPTGIFTRFFLLPNSIIKAGFGTKGFFLEDKKTKIASTKIC
				NNKILWLICSEFMSLWAGSNKKNMNQSRMDVYMSHAPTGSSVHN
				ILHIKQLYHSDEFRAYDWGNDADNMKHYNQSHPPIYDLTAMKV
864	A	1	1692	FRGEAERMAL*QPGRSPRVPTPRPGRWARRDGVHSLPSQFEPER
				RGRGRRDSEPGTRGRPGRHAESTNLL*GRMENEESDVKPPDWPN
				PMNATSQSPQPQHFDSFGLRLPRDITELPEWSEGYPFYMAMGFP
				GYDLSADDIAGKFQFSRGMRRTYDAGFKLMVVEYAESTNNCQAA
				KQFGVLEKNVRDWRKVKPQLQNAHAMRRAFRGPKNGRFALVDQR
				VAEYVRYMQAKGDPITREAMQLKALEIAQEMNIPEKGFKASLGW
				CRRMMRRYDLSLRHKVPVPQHLPEDLTEKLVTYQRSVLALRRAH
				DYEVAQMGNADETPICLEVPSRVTVDNQGEKPVLVKTPGREKLK
				ITALLGVLADGRKLPPYIILRGTYIPPGKFPSGMEIRCHRYGWM
				TEDLMQDWLEVVWRRRTGAVPKQRGMLILNGFRGHATDSVKNSM
				ESMNTDMVIIPGGLTSQLQVLDVVVYKPLNDSVRAQYSNWLLAG
				NLALSPTGNAKKPPLGLFLEWVMVAWNSISSESIVQGFKKCHIS
				SNLEEEDDVLWEIESELPGGGEPPKDCDTESMAESN
865	A	367	2	MTWLVLLGTLLCMLRVGLGTPDSEGFPPRALHNCPYKCICAADL
				LSCTGLGLQDVPAELPAGTADLDLSHNALQRMRPGWLAPLFQLR
				ALHLDHNELHALDRGVFVNASGLRLLDLSSNAEF
866	B	68	391	MKSLVLLLCLAQLWGCHSAPHGPGLIYRQPNCDDPETEEYKEAR
				LVLDSVKLEA
867	B	68	391	MKSLVLLLCLAQLWGCHSAPHGPGLIYRQPNCDDPETEEYKEAR
				LVLDSVKLEA
868	B	68	391	MKSLVLLLCLAQLWGCHSAPHGPGLIYRQPNCDDPETEEYKEAR
				LVLDSVKLEA
869	A	17	1904	GWGTSGSMSGCGLFLRTTAAARACRGLVVSTANRRLLRTSPPVR
				AFAKELFLGKIKKKEVFPFPEVSQDELNEINQFLGPVEKFFTEE
				VDSRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMY
				SRLGETISMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKL
				ASGEA\LAAFCLTEPANGSDAA*IRSRATLSEDKKHYILNGSKV
				WITNGGLANIFTVFAKTEVVDSDGSVKDKITAFIVERDFGGVTN
				GKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNIL
				NSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQE
				KFALMAQKAYVMESMTYLTAGMLDQPGFPDCSIEAAMVKVFSSE
				AAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEIL
				RMYIALTGLQHAGRILTTRIHELKQAKVSTVMDTVGRRLRDSLG
				RTVDLGLTGNHGVVHPSLADSANKFEENTYCFGRTVETLLLRFG
				KTIMEEQLVLKRVANILINLYGMTAVLSRASRSIRIGLRNHDHE
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
				VLLANTFCVEAYLQNLFSLSQLDKYAPENLDEQIKKVSQQILEK
				RAYICAHPLDRTC
870	A	25	1396	ADPHTTVIRFFPAASATKRVLPPVLRVSSPRTWNPNVPESPRIP
				APRLPKRMSGAPTAGAALMLCAATAVLLSAQGGPVQSKSPRFAS
				WDEMNVLAHGLLQLGQG\CANT\GAHPQSAERAGA\RLSACGSA
				CQGTEGSTDLPLAPESRVDPEVLHSLQTQLKAQNSRIQQLFHKV
				AQQQRHLEKQHLRIQHLQSQFGLLDHKHLDHEVAKPARRKRLPE
				MAQPVDPAHNVSRLHRLPRDCQELFQVGERQSGLFEIQPQGSPP
				FLVNCKMTSDGGWTVIQRRHDGSVDFNRPWEAYKAGFGDPHGEF
				WLGLEKVHSITGDRNSRLAVQLRDWDGNAELLQFSVHLGGEDTA
				YSLQLTAPVAGQLGATTVPPSGLSVPFSTWDQDHDLRRDKNCAK
				SLSGGWWFGTCSHSNLNGQYFRSIPQQRQKLKKGIFWKTWRGRY
				YPLQATTMLIQPMAAEAAS
871	A	1	1140	TARTGSELPGRATRPMVRMVPVLLSLLLLLGPAVPQENQDGRYS
				LTYIYTGL\SKHVEDVPAFQALGSLNDLQFFRYNSTD\RKSQPM
				GLW\RQVGREWEDWEARTSQLSGRPGGGTFFYGRPWKDIVGVIY
				QRQ*TGSSRICRGRFGC\EIEINRSSGISWEF\YYDGKDYIEF\
				NK\EIPAW/VSPFDPAAQITKQKW\EAEPVYVQRA\KAYLEEEC
				PATLRK\YLKYSKNIL\DRQ\DPPSV\VVTSHQGPRE/KKRRNL
				KCLGLTTFYPRGKFDV\HWDFGAGRGCREP*VYGGDVL\HNGKW
				AFYPVPGVVV/VQCPPAGTQPPLLPA\TCSTASPGPAPSWCPWG
				GQARKQG\LEAMWDLQTQLACPFLALMLGS*THRNHSQWV\HKA
872	A	80	403	MLWFSGVGALAERYCRRSPGITCCVLLLLNCSGVPMSLASSFLT
				GSVAKCENEGEVLQIPFITDNPCIMCVCLNKEVTCKREKCPVLS
				RDCALAIKQRGACCEQCKGC
873	A	46	594	SPGPALFSQPLGSCSAKAFPAMRPVSVWQWSPWGLLLCLLCSSC
				LGSPSPSTGPEKKAGSQGLRFRLAGFPRKPYEGRVEIQRAGEWG
				TICDDDFTLQAAHILCRELGFTEATGWTHSAKYGPGTGRIWLDN
				LSCSGTEQSVTECASRGWGNSDCTHDEDAGVICKDQRLPGFSDS
				NVIEVEH
874	A	3	538	LLYAQAGVQ*LNLSSLQPQPAGLKQSSHPSLPSSWDYRYSTPHP
				ANFFVEMEFHHVAQAGLELLGSGDLPTSTSHSAGITGV\SHHAP
				PRLISSEGSLLGHLLCLPMVFPLLCVFVLISSSLAGEEAAGLRV
				QKLWPAVVLSHLPVCWFHCSGIWSEVIELKVGREGHVLPWQAHV
				VEF
875	A	993	848	TRYATPLAPGPGHPFSCSRRMATHHTLWMGLALLGVLGDLQAAP
				EAQVSVQPNFQQDKFLGRWFSAGLASNSSWLREKKAALSMCKSV
				VAPATDGGLNLTSTFLRKNQCETRTMLLQPAGSLGSYSYRSPHW
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
				GSTYSVSVVETDYDQYALLYSQGSKGPGEDFRMATLYSRTQTPR
				AELKEKFTAFCKAQGFTEDTIVFLPQTDKCMTEQ
876	A	2	1624	WDFIPDNSKAAFQASTRVYFELDLTDPYTISALASCQLLPHGEN
				LQDVLPHELYWRLKRHLDYVKLMMPSWMTPAQRGKGLYADYLFN
				AIAGNWERKRPVWVMLMVNSLTERDVRFRGVPVLDLYLAQQAEK
				MKKTTGAVEQVEEQCHPLNNGLNFSQVLFALNQTLLQQESVRAG
				SLQASYTTEDLIKHYNCGDLSAVIFNHDTSQLPNFINTTLPPHE
				QVTAQEIDSYFRQELIYKRNERMGKRVMALLRENEDKICFFAFG
				AGHFLGNNTVHSTFLAGRQGLGGGPPHPPGRPIHSPAPQSPAPS
				PEGTSTSPAPVTPAAAVPEAPSVTPTAPPEDEDPALSPHLLLPD
				SLSQLEEFGRQRKWHKRQSTHQRPRQFNDLWVRIEDRARQRGSV
				WTLELSQAGCVALGCPVCLLKLLVPFSIVLGKIDLKKSDLSPKA
				SAQDEAADGDSAMCFLLSSTTASPPPLPLQPTHSSGTAKPPFQL
				SDPATTAGPRQGPPAARHPPWAFSPPSPPTHRCLLPACIALGPP
				DLGPPQVEKPEK
877	A	2572	208	QRNLFLKAFTDFLAFMVLFNYIIPVSMYVTVEMQKFLGSYFITW
				DEDMFDEETGEGPLVNTSDLNEELGQVEYIFTDKTGTLTENNME
				FKECCIEGHVYVPHVICNGQVLPESSGIDMIDSSPSVNGREREE
				LFFRALCLCHTVQVKDDDSVDGPRKSPDGGKSCVYISSSPDEVA
				LVEGVQRLGFTYLRLKDNYMEILNRENHIERFELLEILSFDSVR
				RRMSVIVKSATGEIYLFCKGADSSIFPRVIEGKVDQIRARVERN
				AVEGLRTLCVAYKRLIQEEYEGICKLLQAAKVALQDREKKLAEA
				YEQIEKDLTLLGATAVEDRLQEKAADTIEALQKAGIKVWVLTGD
				KMETAAATCYACKLFRRNTQLLELTTKRIEEQSLHDVLFELSKT
				VLRHSGSLTRDNLSGLSADMQDYGLIIDGAALSLIMKPREDGSS
				GNYRELFLEICRSCSAVLCCRMAPLQKAQIVKLIKFSKEHPITL
				AIGDGANDVSMILEAHVGIGVIGKEGRQAARNSDYAIPKFKHLK
				KMLLVHGHFYYIRISELVQYFFYKNVCFIFPQFLYQFFCGFSQQ
				TLYDTAYLTLYNISFTSLPILLYSLMEQHVGIDVLKRDPTLYRD
				VAKNALLRWRVFIYWTLLGLFDALVFFFGAYFVFENTTVTSNGQ
				IFGNWTFGTLVFTVMVFTVTLKLALDTHYWTWINHFVIWGSLLF
				YVVFSLLWGGVIWPFLNYQRMYYVFIQMLSSGPAWLAIVLLVTI
				SLLPDVLKKVLCRQLWPTATERVQVRSVPSRGGGASGPWP
878	A	2887	3537	HLDRSGLFNIQVIPVCRKLGKEGNDEKQCVTTSRSNAAFFLLHF
				FLLATFTWMGLEAIHMYIALVKVFNTYIRRYILKFCIIGWGKPL
				KIFLVLFFPHENCQVYGKESYGKEKGDEL*VIKTFCDE*ISFVS*
				SGVMFFLNIAMFIVVMVQICGRNGKRSNRTLREEVLRNLRSVV
				SLTFLLGMTWGFAFFAWGPLNIPFMYLFSIFNSLQGKINCT
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
879	A	1	369	QMIDSQNSKETKSHKALSDLELVAQSIIIIFAAYDTTSTTLPFI
				MYELATHPDVQQKLQEEIDAVLANKAPVTYDALVQMEYLDMVVN
				ETLRLFPVVSRVTRVCKKDIEINGVFIPKGLAVMV
880	A	335	1105	MKRERGALSRASRALRLAPFVYLLLIQTDPLEGVNITSPVRLIH
				GTVGKSALLSVQYSSTSSDRPVVKWQLKRDKPVTVVQSIGTEVI
				GTLRPDYRDRIRLFENGSLLLSDLQLADEGTYEVEISITDDTFT
				GEKTINLTVDVPISRPQVLGASTTVLELSEAFTLNCSHENGTKP
				SYTWLKDGKPLLNDSRMLLSPDQKVLTITRVLMEDDDLYSCVVE
				NPINQGRTLPCKITEYRKSSLSSIWLQEAFSSLGPW*
881	A	3818	65	RLRLLLLESVSGLLQPRTGSAVAPVHPPNRSAPHLPGLMCLLRL
				HGSVGGAQNLSALGALVSLSNARLSSIKTRFEGLCLLSLLVGES
				PTELFQQHCVSWLRSIQQVLQTQDPPATMELAVAVLRDLLRYAA
				QLPALFRDISMNHLPGLLTSLLGLRPECEQSALEGMKACMTYFP
				RACGSLKGKLASFFLSRVDALSPQLQQLACECYSRLPSLGAGFS
				QGLKHTESWEQELHSLLASLHTLLGALYEGAETAPVQNEGPGVE
				MLLSSEDGDAHVLLQLRQRFSGLARCLGLMLSSEFGAPVSVPVQ
				EILDFICRTLSVSSKNIVSGICHLFRALAQDTRQPGKYWGPESP
				QTVSSWSPSQRASTFVQITSLPMCRDTGAQCQSVANASLGEGEF
				GDSAESLLRGPAILLTFHPGSILEDRGLILLGEMRSGVGFLTYV
				YICKWSFPVSVSLWLSLSSSTLYLCPFFLQSLHGDGPCGCCCCP
				LSTLKALDLLSALILACGSRLLRFGILIGRLLPQVLNSWSIGRD
				SLSPGQERPYSTVRTKVYAILELWVQVCGASAGMLQGGASGEAL
				LTHLLSDISPPADALKLRSPRGSPDGSLQTGKPSAPKKLKLDVG
				EAMAPPSHRKGDSNANSDVCAAALRGLSRTILMCGPLIKEETHR
				RLHDLVLPLVMGVQQGEVLGSSPYTSSRCRRELYCLLLALLLAP
				SPRCP\LLLPVPCKPSPSASEKIALRSPLSCSEALVTCAALTHP
				RVPPLQPMGPTCPTPAPVPLLRPHRPSGPHRSILRAPCPQWAPC
				PQQAPCPSAGPMPSAGPVPSEPWTSTTANLLGLLSRPSVCPPRL
				LPGPENHRAGSNEDPILAPSGTPPPTIPPDETFGGRVPRPAFVH
				YDKEEASDVEISLESDSDDSVVIVPEGLPPLPPPPPSGATPPPI
				APTGPPTASPPVPAKEEPEELPAAPGPLPPPPPPPPPVPGPVTL
				PPPQLVPEGTPGGGGPPALEEDLTVININSSDEEEEEEEEEEEE
				EEEEEEEEEDFEEEEEEEDFEEEEEDEEEYFEEEEEEEEEFEEE
				FEEEEGELEEEEEEEDEEEEEELEEVEDLEFGTAGGEVEEGAPP
				PSTLPPALPPPESPPKVQPEPEPEPGLLLEVEEPGTEEERGADT
				APTLAPEALPSQGEVEREGESPAAGPPPQELVEEEPSAPPTLLE
				EETEDGSDKVQPPPETPAEEEMETETEAEALQEKEQDDTAAMLA
				DFIDCPPDDEKPPPPSEPDS
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
882	A	311	790	YTMLRGTMTAWRGMRPEVTLACLLLATAGCFADLNEVPQVTVQP
				ASTVQKPGGTVILGCVVEPPRMNVTWRLNGKELNGSDDALGVLI
				THGTLVITALNNHTVGRYQCVARMPAGAVASVPATVTLASESAP
				LPPCHGAVPPHLSHPEAPTIHAASCYS
883	A	54	419	ITPLGLGAADMCAFPWLLLLLLLQEGSQRRLWRWCGSEEVVAVL
				QESISLPLEIPPDEEVENIIWSSHKSLATVVPGKEGHPATIMVT
				NPHYQGQILTMLLRSLQQPSASWPRDCSSSCSW
884	A	240	461	GLVFSRLSPEYYDLARAHLRDEEKSCPCLAQEGPQGDLLTKTQE
				LGRDYRTCLTIVQKLKKMVDKPTQRSVSNA
885	A	167	919	SAAGWASPLRPRCGVPRGCSWPSPCTQRCRCPRAGTTACWALGP
				RACRWPTSCSALDATTQCSSGPRGPAASSHATRGTASSSASTSG
				TPARLTPSSTSATTGTLCSATTPGCSSDTTRVPTSPTPATWCAT
				WVTSRTRWGSVSSTTPPSPTSLWTRTDRPGMATTSRD*AIFPLS
				PPAASSL*PLVYQSPTRLTSLAPNMQRVTSPCPWTLRTL*ARMC*
				SWVVGTRPLRQQRTSWVSQTLSICSAAPGS
886	A	2049	730	RAPARQGPGPARLPGMVSKALLRLVSAVNRRRMKLLLGIALLAY
				VASVWGNFVNMSFLLNRSIQENGELKIESKIEEVEPLREKIRD
				LEKSFTQKYPPVKFLSEKDRKRILITGGAGFVGSHLTDKLMMDG
				HEVTVVDNFFTGRKRNVEHWIGHENFELINHDVVEPLYIEVDQI
				YHLASPASPPNYMYNPIKTLKTNTIGTLNMLGLAKRVGARLLLA
				STSEVYGDPEVHBQSEDYWGHVNPIGPRACYDEGKRVAETMCYA
				YMKQEGVEVRVARIFNTFGPRMHMNDGRVVSNFILQALQGEPLT
				VYGSGSQTRAFQYVSDLVNGLVALMNSNVSSPVNLGNPEEHTIL
				EFAQLIKNLVGSGSEIQFLSEAQDDPQKRKPDIKKAKLMLGWEP
				VVPLEEGLNKAIHYFRKELEYQANNQYIPKPKPARIKKGRTRHS
887	A	203	1772	HLFLEFSVTQQEVQFKPESLCKKLFSDHKELEGLMKTLIHPCSQ
				GIVIFSRSWAGDVGFRKEQNVLWDALLIAVNSPVVLYTILIDPN
				WPGGLEYARNTAHQLKQKLQTVGGYTGKVCIIPRLIHLSSTQSR
				PGEIPLRYPRSYRLADEEEMEDLLQALVVVSLSSRSLLSDQMGC
				EFFNLLIMEQSQLLSESLQKTRELFIYCFPGVRKTALAIKIMEK
				IKDLFHCKPKEILYVCESDSLKDFVTQQTTCQAVTRKTFMQGEF
				LKIKHIVMDETENFCSKYGNWYMKAKNITHPKAKGTGSENLHHG
				ILWLFLDPFQIHHADVNGLPPPSAQFPRKTITSGIHCALEIAKV
				MKEEMKRIKENPPSNMSPDTLALFSETAYEEATCAQALPGVCET
				KTNLTTEQIANYVARKCHSLFQCGYLPKDIAILCRRGEDRGRYR
				LALLKAMELIETHRPSEVVFSPATGVWGSHIVLDSIQQFSGLER
				TVVFGLSPECDQSEEFHKLCFASRAIKHLYLLYEKRAAY
888	A	79	480	PAGIRRSIAKQTGHPGSWETGLWIFRDAAIEFSPEEWSYLDPAQ
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
				QNLYRDGMLENYRNLVSLGIAVSKPDLITCLEQPRNEPWNVKKHE
				TVARHPAVSSHFTQDLLPEHGIKDSFQKVILRRYGSYGIENLQL
				KK
889	A	523	989	GARRQAHTMALKRINKELSDLARDPPAQCSAGPVGDDMFHWQAT
				IMGPNDSPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPNINS
				NGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVPEIA
				RIYKTDRDKYNRISREWTQKYAM
890	A	310	2	LVCFFSVLMGPFYPPVSPERSVAQSEAREGRGPRGLPPLSLPRG
				PFGARAHRVGRPGSSVPHSPPSRGRGRKNPASARQQQRLAGNGA
				QEGRQRLAASKSTP
891	A	2280	3000	EAWCSWVWDFTRAYSGAPIFLLHMGSAPLPSRAEGKSLARVPNA
				TGLRMAFCLEASLGPDFCCWYQSPETLPPWSPCNAQLVSYCFSK
				PLKASTSPLSPGQDCGEASQPLLS*LPLSCPTLGCPFPSFPSKG
				FHGPPSVGSGPARSRLGSSSCF*ATTLGKLNVPSTLSPFPRTNH
				FCAHPWRRDELLAEGQSKCKSWSAGRGVHGFPSPGRVSVSFILS
				PLTGYGFRAMPRAPLCSPA
892	A	355	861	PLTTTPAAPRAPCPPSRLSGQPLTGPTEGSRSRLSPNISEQGEP
				PLALTVGHPLSTQPGPTVPSELEPIQGPRG*GDCPTPSQSA*GG
				VLSCTPESHTEFKPPPTGGGRRWARLGLNGAT*GREEPLQTRLP
				AEYPGPGPIDPLQPPPISTASMATAFSDFLLLGRDPA
893	A	15	800	FSDLTAHFLFHSGEKPYECKECGKVFRYKSSLTSHHRIHTGEKP
				YKCNRCGKVFSRSSNLVCHQKIHTGEKPYKCNQCGKVFNQASYL
				TRHQIIHTGERPYRCSKCGKAFRGCSGLTAHLAIHTEKKSHECK
				ECGKIFTQKSSLTNHHRIHIGEKPYKCTLCSKVFSHNSDLAQHQ
				RVHS*ESLQTVYGKTIIMSSSINQHQ*VHTKWKSYK*NVCDTGF
				IKACQITGHHHITVEDESTQMNCVYLGYYSRTIAIEHDRIYT
894	A	6222	7046	RTVTTFLSKDSHGVYCAQGGKIPDHQNPQCNRKQHPVSTILMLD
				KASFCQLRKRKHNLSVNCINRNPFMSLKNTSWHSSLSVTQRHQQ
				QSKLHFQGSILLH*PSQNIL/SNI*KCINYC*HCSSVLLSYLFI
				ETESYSVAQAGVQWHDLGLLQLLPLRFKQFSCFSLPSSWDYRSA
				PSCPANFCILVEMGFCHVGQAGLKLLASSDPPALASQSAGITGV
				SHYTQPCSPFLKSTGLFSCKVLSNPYHKGRIYLGRMCFLNSTWH
				LVKSTLFCPLFI
895	A	246	717	KRQSEEGVFSCCQGWNESLLLKSKVLEYP*FLHFPSFSFDLYLF
				NYVFIYLFIYFCSIQSQTQSKAERAYIYIYLYMCCRQNTVNFTT
				TTTKQLFCHLNIHLRRRNEKRWGCHFLVYAFEARSMFIYFFSLC
				INENDPEWRLAERSMYWSKHHKSC
896	A	3	1007	AWHEGLVSSPAIGAYLSASYGDSLVVLVATVVALLDICFILVAV
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
				PESLPEKMRPVSWGAQISWKQADPFASLKKVGKDSTVLL\ICIT
				VCLSYLPEAG\QYSSFF\LYLR\QVIGFG\TVKIAAFIAMVGIL
				SIVAQTAFLSILMRSLGNKNTVLLGLGFQMLQLAWYGFGSQAWM
				MWAAGTVAAMSSITFPAISALVSRNAESDQQGVAQGIITGIRGL
				CNGLGPALYGFIFYMFHVELTETGPKLNSNNVPLQGAVIPGPPF
				LFGACIVLMSFLAALFIPEYSKASGVQKHSNSSSGSLTNTPERG
				SDEDIEPLLQDSSIWELSSFEEPGNQCTEL
897	A	953	614	TPIRGTDDEHEECTVQEYSAGKNTCLRPGAVAHTCNPCTLGGRG
				RWIT*GSGVQDQPGPTWQNPVFLERRPRALHSSPGLTTQRILWA
				QGLWVGAGSTGCSRGPRGEGVFREG
898	A	1	412	FFFFECG*SFTNSFSVTIHRRIHNGEKSYECSDCGKSFNVLSSV
				KKHMRTHTGKKPYECNYCGKSFTSNSYLSVHTRMHNRQM*IQ*L/
				CGKAFIDLSCLR*HEQTLTRCMNHLLLCNKLPPKILWLQTKTL
				VISKFL
899	A	2	2865	ALPDGGASVASDRAEGRPAKPSKTAAREKTEGAVAAVGGGPSSF
				RCCYGCCHEARLGRTSLPRGVIMLTEASLSIWGWGSLGIVLFLI
				TFGPFVIFYLTFYILCFVGGGLVVTLLFGKTNSEKYLEQCEHSF
				LPPTSPGVPKCLEEMKREARTIKIDRRLTGANIIDEPLQQVIQF
				SLRDYVQYWYYTLSDDESFLLEIRQTLQNALIQFATRSKEIDWQ
				PYFTTRIVDDFGTHLRVFRKAQQKITEKDDQVKGTAEDLVDTFF
				EVEVEMEKEVCRDLVCTSPKDEEGFLRDLCEVLLYLLLPPGDFQ
				NKIMRYFVREILARGILLPLINQLSDPDYINQYVIWMIRDSNCN
				YEAFMNIIKLSDNIGELEAVRDKAAEELQYLRSLDTAGDDINTI
				KNQINSLLFVKKVCDSRIQRLQSGKEINTVKLAANFGKLCTVPL
				DSILVDNVALQFFMDYMQQTGGQAHLFFWMTVEGYRVTAQQQLE
				VLLSRQRDGKHQTNQTKGLLRAAAVGIYEQYLSEKASPRVTVDD
				YLVAKLADTLNHEDPTPEIFDDIQRKVYELMLRDERFYPSFRQN
				ALYVRMLAELDMLKDPSFRGSDDGDGESFNGSPTGSINLSLDDL
				SNVSSDDSVQLHAYISDTVYADYDPYAVAGVCNDHGKTYALYAI
				TVHRRNLNSEEMWKTYRRYSDFHDFHMRITEQFESLSSILKLPE
				KKTFNNMDRDFLEKRKKDLNAYLQLLLAPEMMKASPALAHYVYD
				FLENKAYSKGKGDFARKMDTFVNPLRNSMRNVSNAVKSLPDSLA
				EGMTKMSDNMGKMSERLGQDIKQSFFKVPPLIPKTDSDPEHRRV
				SAQLDDNVDDNIPLRVMLLLMDEVFDLKERNQWLRRNIKNLLQQ
				LIRATYGDTINRKIVDHVDWMTSPEQVADSVKRFRDAFWPNGIL
				AEAVPCRDKSIRMRTRVAGKTKLLAIMPGE
900	A	305	592	MGSLLCSCSQRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQ
				MPSDKPIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVGRCL
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
				GTGWQLS
901	A	60	388	GLDSFSATETRRTHTNTEPHSQSQEPSNGEPQKEEPAAESRDPT
				PGQQTEEDQDTAEIPVRDMEGDLQELASVKHRG*ILDLGS\SVK
				VKIIPKEEHCKMPEAGEEQPQV
902	A	1	885	MSPTREAPYLTLYCTLSAYGSAWPMVGLSKYLQKEKFLNEHRED
				FSNAFGLGEDKGGNFLRLSPPSSGRQGHHTRRAEALLGGAAGSN
				PGKATSERAHLLSPGGAALVSEESNADKRVENWPLMQSPWPTLS
				ISTLYLLFVWLGPKWMKDREPFQMRLVLIIYNFGMVLLNLFIFR
				ELFMGSYNAGYSYICQSVDYSNNVHEVRIQFHVTIGHTALSLYT
				DCPFPKWMHWALIAYAISFIFLFLNFYIRTYKEPKKPKAGKTAM
				NGISANGVSKSEKQLMIENGKKQKNGKAKGD
903	A	68	398	GPASNRALGFVVLLETRMVSAVSDPPTSTTGSTMCECISIHVGQ
				AGVQMGNACWELYCLEHDIQPSGTMPSHKALGSSDNSFNTFFRE
				TQPGRHV\PGLSVDLEPAVIAQ
904	A	3	416	EKPYECSDCGKSFIKKSQLHVHQRIHTGENPFICSECGKVFTHK
				TNLIIHQKIHTGERPYICTVCGKAFTDRSNLIKHQKIHTGEKPY
				KCSDCGKSFTWKSRLRIHQKCHTGER/HYECSECGKAFIQKSTL
				SMHQRIH
905	B	373	389	MPLEVVVELQIRAISCPGVFLPGKQDVYLGVYLMNQYLETNSFP
				SAFPIMIQESMRFEKVFESAVDPGAVVDLLENGDPSKAETEAAG
				HREEYIGTGRTTRSLAGAVGREPGLPSGPTPGENHLPAGSPIC
906	A	832	1885	AEWDAADKAHVGPGRSPRQPLPHVGRRRAAHTTGRGRRTAGCAP
				APARTLCILSILGPWCVLPHLPTLCLGQAQAASCSQGAHGCFAG
				CSCT/GTSASHPV/CCKCPLHPVCTLADVHGCITSGFSVISLPQ
				TCAPWTSWRKWSLSDSWQVDACPESCCEPPCCATSCCAPAPCLT
				LVCTPVSCVSSPCCQAACEPSPCQSGCTSSCTPSCCQQSSCQPA
				CCTSSPCQQACCVPVCCKPVCCVPVCCKPVCCKPCCVPVCSGA
				SSSCCQQSSRQPACCTTSCCRPSSSVSLLCRPVCRSTCCVPIPS
				CCAPASTCQPSCCRPASCVSLLCRPTCSRLSSACCGLSSGQKSSC
907	A	2	480	RIPGRRFRAAFVLGSANVASSVRLRCSFPLSLGGPSGPAAASVA
				LGPAGPGRSLGRTPDTGDWEMDSVSFEDVAVAFTQEEWALLDPS
				QKNLYRDVMQEIFRNLASVGNKSEDQNQDDFKNPGRNLSSHVV
				ERLFEIKEGSQYGETFSQDSNLNLNKI
908	A	1970	1677	FFLRRSFAVVAQAGVQWHDLNSPQPPPPGFKQFSCLSLPSS*DY
				RRMPPRPANFVFLVEMGFLHVGQAGLKLPTSGDPPASASQSAGI
				TGVSHRAQP
909	A	1982	958	RYFRSLAEGVRAAPRRREPRTMSVGFIGAGQLAYALARGFTAAG
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTIIHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRIICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQPRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
				ILSAHKIIASSPEMNLPTVSALRKMGVNLTRSNKETVKHSDVLF
				LAVKPHIIPFILDEIGADVQARHIVVSCAAGVTISSVEKKLMAF
				QPAPKVIRCMTNTPVVVQEGATVYATGTHALVEDGQLLEQLMSS
				VGFCTEVEEDLIDAVTGLSGSGPAYAFMALDALADGGVKMGLPR
				RLAIQLGAQALLGAAKMLLDSEQHPCQLKDNVCSPGGATIHALH
				FLESGGFRSLLINAVEASCIRTRELQSMADQEKISPAALKKTLL
				DRVKLESPTVSTLTPSSPGKLLTRSLALGGKKD
910	A	88	331	QLCSCLRPDRPPLPARSAQSPMAAALRAPTQVFVAFEDVAIYFS
				QEEWELLDEMQRLLYRDVMLENFAVMASLGIIECFQE
911	A	429	2	QDIAAWQSLTQVLTPESWRKANIMTEPQKSQERYKGIYVKEKLY
				RRARHDESLNWTSCDHHESQECKGEDPGRHPNCGKNLGMKSTVE
				QHHVVHVLPQPFTCNNCGVAFADDTDPRAHPSTHLGEKSYKCDQ
				YGKILSQSLY
912	A	1	415	PIGTLFSVAEFLVEHQRSHTGEKPYECNDCGKVFSQSTHLIQHQ
				RIHTGEKPYKCSECGKAFHNSSRLIHHQRLHHGEKPYRCSDCKK
				AFSQSTYLIQHRRIHTGEKPYKCSECGKAFRHSSNMCQHQRIHL
				REDFSM
913	A	3	562	SSCQAVCCDPSPCEPTCSESSICQPATCVALVCEPVCLRPVCCV
				QSSCEPPSVPSTCQEPSCCVSSICQPICSEPSPCSPAVCVSSPC
				QPTCYVVKRCRSVCPEPVSCPSTSCRPLSCSPGS\LHLPSRPTC
				PRTFYIFSSSKRPCSATISYRPVSRPICRPICSGLLTYRQPYMT
				SISYRPACYRP
914	A	2	1028	FFFLSQYISVYYNLPRLRDLARAAKTDSDRPSPPGACSQPGPKR
				KQASEGTAECRVLATELQECALAPTRATVLPPPGLPGLRQQPPA
				HGGSPPPGAARPSHRSAGPQALHLPGPPPAAAAALSPGAGGLLH
				SSW*EAGPPPQKAPGGGTPSPPGPVAQVDTTHDSQHPLAGRNPR
				APQRSPARPPLEAAGKAERGRQSSRTGVASGHGT*DQWMWCKGH
				GHPAVRGPGIGAAEAGAEGGQGGQDTGRAHGQPPGVHTAVLPHG
				SAAPESRWAPAPPAGASTLGVGP*PDGTPGSAVPGPVPPAPSVL
				PQSPGSRPPVKRPVQVRQARGPGPPPTWVLPGVP
915	A	1	1071	MVQVIRKDAPTPRTREPSLSDKGICPKPQEALKFFCEVDEEAIC
				VVCREFRSHKQHSVVPLEEVVQEYKELLESRLRVLKKELEDCEV
				FRSTEKKESKELLRILLTNAHPHNLAVKLEHTGLDAHLDLLLST
				HTFGYPKEDQRLWHAVAEATGLKAERTLFIDDSEAILDAAAQFG
				DAMKEKPAVEVRLDKWLWAARFYKTRALAREMIEGGKVHYNGQR
				SKPSKIVELNATLTLRQGNDERTVIVKAITEQRRPASTDRNRKP
				QYLEIIDIWDLSTSSVKIDVLVDRNARLISVLLKFGVHTVEIQA
				QSTGIIFQSRHPFMHPVTSPGTCRPSLNCLTGSPGTELECINSR
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
				VITGY
916	A	1	432	VLSCSPAPVAGPRGANPGEPRSGRDMDCVIFEEVAVNFTPEEWA
				LLDHAQRSLYRDVMLETCRNLASLDCYIYVRTSGSSSQRDVFGN
				GISNDEEIVKFTGSDSWSIFGENWRFDNTGDQHQIPQRHLRSQL
				GRLCESMKVIMR
917	A	1	703	PAPLAEGAFLAEASLLKGLSPATPTSEGPKVVSVQLGDGTRLKGT
				VLPVATIQNASTAMLMAASVARKAVVLPGGTATSPKMIAKNVLG
				LVPQALPKADGRAGLGTGGQKVNGASVVMVQPSKTATGPSTGGG
				TVISRTQSSLVEAFNKILNSKNLLPAYRPNLSPPAEAGLALPPT
				GYRCLECGDAFSLEKSLARHYDRRSMRIEVTCNHCARRLVFFNK
				CSLLLHAREHKDKG
918	A	1389	211	TGQGSGPMRAGSQSHQILSSPPSRMHAKDTPFPTHLIGAPKPLA
				CCVDGGEARPAVLWPGEKKIKRRPCPWGRPLSGPPFPP\PNLPG
				PRTPLPAPTPLEVSRPFLCHLVGQMA*WASAWGIE*GSP*PPEP\
				NPGPRCKQHPSRALPQYPQGIHTPPLLPQPRTDRLPGPEPN/R
				PSASETHGGPHTPYILPH*GSPGPTGASGKPPKLATALGRALCP
				PHHRPRSRVLVGALHPNPRSPWPPIFLGPIGACFSPAGWTP*RA
				VPRGSPGGSRLGAYVVVSGPRLQPPAPTPE/LYPLSRMSAIFHS
				RWMSGEVVGRGPA*GSGIRTMSSEEKCTGAC*ATGVPERAEEGA
				ATEVGSSAPPPRPRPASAGFRFVPGFFLFFSVCVRMVRPLPSHRG
919	A	243	428	MHGLFGQCFQEALGFLLLPRFPQSSQMLKFLKVDVTGSLTTNKL
				AVTVFETQYLWQLTSNQ*
920	A	240	461	GLVFSRLSPEYYDLARAHLRDEEKSCPCLAQEGPQGDLLTKTQE
				LGRDYRTCLTIVQKLKKMVDKPTQRSVSNA
921	A	1252	1190	FFQVFIFLFLIFFKTEFHSCCPGAVQWHDLDSLQPPPPRFKGFS
				CLSLPSSWDYRHAPAHPANFVFLVETGFLHV\GQ\ASLELPTSG
				DTPAS\ASQSAGITGVSHHA*PRASGRRCW
922	A	3	414	HASGLSEASHSKKTVKKVVVVEQNGSFQVKIPKNFVCEHCFGAF
				RSSYHLKRHILIHTGEKPFECDICDMRFIQKYHLERHKRVHSGE
				KPYQCERCHQVRLIPATIPHTHFSFPKNQGHPPLLPDKRATSVT
				RHNS
923	A	221	935	REAEGWVGWKDCPARLQLLGPTPHVGPVARSAAALSLEPWDLDH
				SPP*SAEGCCSSPDVYTGADWRPSLGYQGNSSWAHSGPGQLPHA
				MPAAGGAGGERLTGGRRALVHHCSRPRPRPSNEPTVAEGATTVA/
				ASARAAADRPA/P*GRQGKGRRP/AP*ERGPPQHSGGRGTGVRP
				SAAATGNQGRVVACPPTGSVLEPRSLRRPPEAAVHLAPALTTGR
				RTRLGESRGSADPAVTPASG
707	A	609	785	LGLEHISSSGEKYYYNCRTEVSQWGKTPKSGLERGQRQKEANKM
				AVNSFPKDRDYRREVMQATATSGFASGKSTSGDKPVSHSCTTPS
				TSSASGLNPTSAPPTSASAGPCFSVFHSSPIP/TLTSGPKSS*T
				IAVLLWKPRCSLIILMWT*SIINEVLTGDVTQASLQTTTHKCLT
				AGPSVFKITSLISQAAQLSTQAQASNQSPMSLTSDASSPRTICF
				SKE*GTPQT*\PVPIQTFGFSTPPVSSQPKVSTPVVKQGPVSQS
				ATQQPVTADKQQGHEPVSPRSLQRSSSQRSPSPGPNHTSNSSNA
				SNATVVPQNSSARSTCSLTP/VTSSTLQ*KSTTTIVEQKFHNGE
				KPQRVAWKEDRDKKKQTRWQSTASQKIGITEER
924	A	3	473	PAPAARSRELLKELRNGQDMDTVVFEDVVVDFTLEEWALLNPAQ
				RKLYRDVMLETFKHLASVDNEAQLKASGSISQQDTSGEKLSLKQ
				KIEKFTRKNIWASLLGKNWEEHSVKDKHNTKERHLSRNPRVERP
				CKSSKGNKRGRTFRKTRNCNRHLRR

[0477]

TABLE 9
				Identification of Priority
SEQ ID NO:	SEQ ID NO: of			Application that contig
of full-length	full-length	SEQ ID NO: of	SEQ ID NO: of	nucleotide sequence was
nucleotide	peptide	contig nucleotide	contig peptide	filed (Attorney Docket
sequence	sequence	sequence	sequence	No._SEQ_ID_NO.) *
1	245	489	707	784_740
2	246	490	708	784_9374
3	247	491	709	792_5634
4	248	492	710	784_4647
5	249	493	711	787_1136
6	250	494	712	790_10073
7	251	495	713	784_5294
8	252	496	714	790_28178
9	253	497	715	791_3741
10	254	498	716	784_4126
11	255	499	717	789_4043
12	256	500	718	784_1461
13	257	501	719	790_28178
14	258	502	720	784_10077
15	259	503	721	784_4160
16	260
17	261	504	722	790_19526
18	262	505	723	784_9991
19	263
20	264	506	724	784_7685
21	265	507	725	784_5439
22	266	508	726	784_682
23	267	509	727	784_900
24	268	510	728	784_455
25	269	511	729	784_5952
26	270	512	730	784_3473
27	271
28	272	513	731	784_2029
29	273	514	732	784_2029
30	274
31	275	515	733	784_2133
32	276	516	734	790_6724
33	277	517	735	784_2405
34	278	518	736	792_748
35	279	519	737	784_2231
36	280	520	738	784_2406
37	281	521	739	784_2406
38	282	522	740	784_2406
39	283	523	741	787_4493
40	284	524	742	784_5207
41	285	525	743	787_3535
42	286	526	744	784_1319
43	287	527	745	784_4272
44	288	528	746	787_132
45	289	529	747	784_2533
46	290	530	748	790_27260
47	291	531	749	784_3514
48	292	532	750	790_19778
49	293	533	751	784_1931
50	294	534	752	784_10013
51	295	535	753	784_2073
52	296	536	754	784_3028
53	297	537	755	787_3541
54	298	538	756	787_3541
55	299	539	757	787_2068
56	300	540	758	784_2127
57	301	541	759	784_8309
58	302	542	760	790_18776
59	303	543	761	784_9362
60	304	544	762	790_8075
61	305	545	763	785_242
62	306	546	764	784_4775
63	307	547	765	784_4325
64	308	548	766	784_7365
65	309	549	767	787_6838
66.	310	550	768	787_4689
67	311	551	769	784_5834
68	312	552	770	787_6059
69	313	553	771	787_2566
70	314	554	772	784_5823
71	315	555	773	790_23066
72	316	556	774	787_6376
73	317	557	775	784_7830
74	318	558	776	784_5371
75	319	559	777	789_1692
76	320
77	321	560	778	784_2629
78	322	561	779	784_4490
79	323	562	780	784_1862
80	324	563	781	787_6106
81	325	564	782	784_5283
82	326
83	327	565	783	784_1050
84	328	566	784	787_2903
85	329	567	785	784_5693
86	330
87	331	568	786	787_2946
88	332	569	787	784_8877
89	333	570	788	784_8877
90	334	571	789	784_2265
91	335	572	790	791_5470
92	336	573	791	788_5773
93	337	574	792	788_7171
94	338	575	793	784_4872
95	339	576	794	784_262
96	340	577	795	787_4845
97	341
98	342	578	796	785_82
99	343	579	797	787_2256
100	344	580	798	787_3416
101	345	581	799	787_3416
102	346	582	800	787_5278
103	347	583	801	784_3751
104	348	584	802	784_2890
105	349	585	803	785_411
106	350	586	804	790_12090
107	351	587	805	787_2946
108	352	588	806	787_8399
109	353	589	807	790_3720
110	354	590	808	784_8877
111	355
112	356	591	809	784_7066
113	357	592	810	790_23188
114	358	593	811	784_2661
115	359	594	812	784_10060
116	360	595	813	785_1267
117	361	596	814	784_2265
118	362	597	815	784_1914
119	363	598	816	784_9888
120	364	599	817	784_1120
121	365	600	818	787_2628
122	366	601	819	787_4552
123	367	602	820	784_2259
124	368	603	821	784_5456
125	369	604	822	787_3961
126	370	605	823	787_3416
127	371	606	824	784_6744
128	372	607	825	784_2191
129	373	608	826	784_4923
130	374	609	827	784_1956
131	375	610	828	784_961
132	376	611	829	784_2535
133	377
134	378	612	830	784_1653
135	379	613	831	784_5353
136	380	614	832	784_6636
137	381	615	833	784_958
138	382	616	834	784_958
139	383	617	835	784_958
140	384
141	385	618	836	785_1586
142	386	619	837	785_1586
143	387	620	838	784_3692
144	388	621	839	784_9667
145	389
146	390	622	840	787_7648
147	391	623	841	790_22282
148	392	624	842	790_12724
149	393	625	843	784_3455
150	394	626	844	785_502
151	395	627	845	787_5414
152	396	628	846	789_4462
153	397	629	847	788_2519
154	398
155	399	630	848	784_3923
156	400	631	849	790_23386
157	401	632	850	785_3574
158	402	633	851	785_3574
159	403	634	852	790_16843
160	404	635	853	787_2319
161	405	636	854	784_2529
162	406	637	855	784_3379
163	407	638	856	784_8979
164	408	639	857	787_1720
165	409	640	858	784_10082
166	410	641	859	787_181
167	411	642	860	787_181
168	412	643	861	787_181
169	413	644	862	787_181
170	414	645	863	787_2807
171	415	646	864	784_4061
172	416	647	865	785_707
173	417	648	866	790_13676
174	418	649	867	790_13676
175	419	650	868	790_13676
176	420	651	869	784_2932
177	421
178	422	652	870	784_6075
179	423	653	871	789_5561
180	424	654	872	785_582
181	425	655	873	784_9706
182	426	656	874	787_4158
183	427	657	875	784_8264
184	428	658	876	787_5843
185	429	659	877	784_4210
186	430
187	431	660	878	790_16312
188	432	661	879	784_1531
189	433
190	434	662	880	785_3606
191	435	663	881	784_3336
192	436	664	882	784_9961
193	437
194	438	665	883	787_6063
195	439	666	884	791_1603
196	440	667	885	787_4796
197	441	668	886	784_4453
198	442	669	887	790_11226
199	443	670	888	784_9645
200	444
201	445	671	889	787_8691
202	446	672	890	787_10237
203	447
204	448	673	891	789_6142
205	449	674	892	788_13275
206	450	675	893	784_546
207	451	676	894	791_3434
208	452	677	895	791_2649
209	453	678	896	784_3405
210	454	679	897	787_4674
211	455
212	456	680	898	784_3103
213	457	681	899	788_14055
214	458	682	900	784_9636
215	459
216	460	683	901	792_2618
217	461	684	902	790_27561
218	462	685	903	784_9032
219	463	686	904	787_1260
220	464	687	905	790_2677
221	465	688	906	790_23824
222	466	689	907	784_9794
223	467
224	468	690	908	784_4057
225	469	691	909	784_8449
226	470	692	910	784_9744
227	471
228	472	693	911	788_5898
229	473
230	474
231	475	694	912	784_4762
232	476	695	913	784_3767
233	477	696	914	784_1377
234	478
235	479	697	915	790_16072
236	480	698	916	784_9963
237	481	699	917	784_2480
238	482	700	918	784_355
239	483	701	919	785_2433
240	484	702	920	791_1603
241	485	703	921	787_4174
242	486	704	922	787_2367
243	487	705	923	789_4494
244	488	706	924	784_9639

[0478] 784_XXX=SEQ ID NO: XXX of Attorney Docket No. 784, U.S. Ser. No. 09/488,725 filed Jan. 21, 2000, the entire disclosure of which, including sequence listing, is incorporated herein by reference.

[0479] 785_XXX=SEQ ID NO: XXX of Attorney Docket No. 785, U.S. Ser. No. 09/491,404 filed Jan. 25, 2000, the entire disclosure of which, including sequence listing, is incorporated herein by reference.

[0480] 787_XXX=SEQ ID NO: XXX of Attorney Docket No. 787, U.S. Ser. No. 09/496,914 filed 03, 2000, the entire disclosure of which, including sequence listing, is incorporated herein by reference.

Table 9

[0481] 788_XXX=SEQ ID NO: XXX of Attorney Docket No. 788, U.S. Ser. No. 09/515,126 filed Feb. 28, 2000, the entire disclosure of which, including sequence listing, is incorporated herein by reference.

[0482] 789_XXX=SEQ ID NO: XXX of Attorney Docket No. 789, U.S. Ser. No. 09/519,705 filed Mar. 07, 2000, the entire disclosure of which, including sequence listing, is incorporated herein by reference.

[0483] 790_XXX=SEQ ID NO: XXX of Attorney Docket No. 790, U.S. Ser. No. 09/540,217 filed Mar, 31, 2000, the entire disclosure of which, including sequence listing, is incorporated herein by

[0484] 791_XXX=SEQ ID NO: XXX of Attorney Docket No. 791, U.S. Ser. No. 09/552,929 filed Apr. 18, 2000, the entire disclosure of which, including sequence listing, is incorporated herein by reference.

[0485] 792_XXX=SEQ ID NO: XXX of Attorney Docket No. 792, U.S. Ser. No. 09/577,408 filed May 18, 2000, the entire disclosure of which, including sequence listing, is incorporated herein by reference.

Claims

1. An isolated polynucleotide comprising a nucleotide sequence selected from the group consisting of SEQ ID NO: 1-244.

2. An isolated polynucleotide encoding a polypeptide with biological activity, wherein said polynucleotide hybridizes to the polynucleotide of claim 1 under stringent hybridization conditions.

3. An isolated polynucleotide encoding a polypeptide with biological activity, wherein said polynucleotide has greater than about 99% sequence identity with the polynucleotide of claim 1.

4. The polynucleotide of claim 1 wherein said polynucleotide is DNA.

5. An isolated polynucleotide of claim 1 wherein said polynucleotide comprises the complementary sequences.

6. A vector comprising the polynucleotide of claim 1.

7. An expression vector comprising the polynucleotide of claim 1.

8. A host cell genetically engineered to comprise the polynucleotide of claim 1.

9. A host cell genetically engineered to comprise the polynucleotide of claim 1 operatively associated with a regulatory sequence that modulates expression of the polynucleotide in the host cell.

10. An isolated polypeptide, wherein the polypeptide is selected from the group consisting of (a) a polypeptide encoded by any one of the polynucleotides of claim 1; and (b) a polypeptide encoded by a polynucleotide hybridizing under stringent conditions with any one of SEQ ID NO: 1-244.

11. A composition comprising the polypeptide of claim 10 and a carrier.

12. An antibody directed against the polypeptide of claim 10.

13. A method for detecting the polynucleotide of claim 1 in a sample, comprising: a) contacting the sample with a compound that binds to and forms a complex with the polynucleotide of claim 1 for a period sufficient to form the complex; and b) detecting the complex, so that if a complex is detected, the polynucleotide of claim 1 is detected.

14. A method for detecting the polynucleotide of claim 1 in a sample, comprising: a) contacting the sample under stringent hybridization conditions with nucleic acid primers that anneal to the polynucleotide of claim 1 under such conditions; b) amplifying a product comprising at least a portion of the polynucleotide of claim 1; and c) detecting said product and thereby the polynucleotide of claim 1 in the sample.

15. The method of claim 14, wherein the polynucleotide is an RNA molecule and the method further comprises reverse transcribing an annealed RNA molecule into a cDNA polynucleotide.

16. A method for detecting the polypeptide of claim 10 in a sample, comprising: a) 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 b) detecting formation of the complex, so that if a complex formation is detected, the polypeptide of claim 10 is detected.

17. A method for identifying a compound that binds to the polypeptide of claim 10, comprising: a) contacting the compound with the polypeptide of claim 10 under conditions sufficient to form a polypeptide/compound complex; and b) detecting the complex, so that if the polypeptide/compound complex is detected, a compound that binds to the polypeptide of claim 10 is identified.

18. A method for identifying a compound that binds to the polypeptide of claim 10, comprising: a) contacting the compound with the polypeptide of claim 10, in a cell, under conditions sufficient to form a polypeptide/compound complex, wherein the complex drives expression of a reporter gene sequence in the cell; and b) detecting the complex by detecting reporter gene sequence expression, so that if the polypeptide/compound complex is detected, a compound that binds to the polypeptide of claim 10 is identified.

19. A method of producing the polypeptide of claim 10, comprising, a) culturing a host cell comprising a polynucleotide sequence selected from the group consisting of any of the polynucleotides from SEQ ID NO: 1-244, under conditions sufficient to express the polypeptide in said cell; and b) isolating the polypeptide from the cell culture or cells of step (a).

20. An isolated polypeptide comprising an amino acid sequence selected from the group consisting of any one of the polypeptides SEQ ID NO: 245-488.

21. The polypeptide of claim 20 wherein the polypeptide is provided on a polypeptide array.

22. A collection of polynucleotides, wherein the collection comprising of at least one of SEQ ID NO: 1-244.

23. The collection of claim 22, wherein the collection is provided on a nucleic acid array.

24. The collection of claim 23, wherein the array detects full-matches to any one of the polynucleotides in the collection.

25. The collection of claim 23, wherein the array detects mismatches to any one of the polynucleotides in the collection.

26. The collection of claim 22, wherein the collection is provided in a computer-readable format.