Patent Publication Number: US-2004048249-A1

Title: Novel nucleic acids and secreted polypeptides

Description:
1. CROSS REFERENCE TO RELATED APPLICATIONS  
     [0001] This application is a continuation-in-part application of U.S. application Ser. No. 09/488,725 filed Jan. 21, 2000 entitled “Novel Contigs Obtained from Various Libraries”, Attorney Docket No. 784; U.S. application Ser. No. 09/491,404 filed Jan. 25, 2000 entitled “Novel Contigs Obtained from Various Libraries”, Attorney Docket No. 785; U.S. application Ser. No. 09/496,914 filed Feb. 3, 2000 entitled “Novel Contigs Obtained from Various Libraries”, Attorney Docket No. 787; U.S. application Ser. No. 09/515,126 filed Feb. 28, 2000 entitled “Novel Contigs Obtained from Various Libraries”, Attorney Docket No. 798; U.S. application Ser. No. 09/519,705 filed Mar. 7, 2000 entitled “Novel Contigs Obtained from Various Libraries”, Attorney Docket No. 789; U.S. application Ser. No. 09/540,217 filed Mar. 31, 2000 entitled “Novel Contigs Obtained from Various Libraries”, Attorney Docket No. 790; U.S. application Ser. No. 09/552,929 filed Apr. 18, 2000 entitled “Novel Contigs Obtained from Various Libraries”, Attorney Docket No. 791; U.S. application Ser. No. 09/577,408 filed May 18, 2000 entitled “Novel Contigs Obtained from Various Libraries”, Attorney Docket No. 792; all of which are incorporated herein by reference in their entirety. 
    
    
     
       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 &amp; 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 NaHPO 4 , 7% sodium dodecyl sulfate (SDS), 1 mM EDTA at 65° C., and washing in 0.1×SSC/0.1% SDS at 68° C.), and moderately stringent conditions (i.e., washing in 0.2×SSC/0.1% SDS at 42° C.). Other exemplary hybridization conditions are described herein in the examples.  
       [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&#39;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&#39;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&#39;s existing regulatory region with a regulatory sequence isolated from a different gene or a novel regulatory sequence synthesized by genetic engineering methods. Such regulatory sequences may be comprised of promoters, enhancers, scaffold-attachment regions, negative regulatory elements, transcriptional initiation sites, and regulatory protein binding sites or combinations of said sequences. Alternatively, sequences which affect the structure or stability of the RNA or protein produced may be replaced, removed, added, or otherwise modified by targeting. These sequence include polyadenylation signals, mRNA stability elements, splice sites, leader sequences for enhancing or modifying transport or secretion properties of the protein, or other sequences which alter or improve the function or stability of protein or RNA molecules.  
       [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.) C URRENT  P ROTOCOLS IN  M OLECULAR  B IOLOGY,  John Wiley &amp; Sons, 1992). Moreover, many expression vectors are commercially available that already encode a fusion moiety (e.g., a GST polypeptide). A nucleic acid encoding a polypeptide of the invention can be cloned into such an expression vector such that the fusion moiety is linked in-frame to the protein of the invention.  
       [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&#39;s existing regulatory region with a regulatory sequence isolated from a different gene or a novel regulatory sequence synthesized by genetic engineering methods. Such regulatory sequences may be comprised of promoters, enhancers, scaffold-attachment regions, negative regulatory elements, transcriptional initiation sites, regulatory protein binding sites or combinations of said sequences. Alternatively, sequences which affect the structure or stability of the RNA or protein produced may be replaced, removed, added, or otherwise modified by targeting. These sequences include polyadenylation signals, mRNA stability elements, splice sites, leader sequences for enhancing or modifying transport or secretion properties of the protein, or other sequences which alter or improve the function or stability of protein or RNA molecules.  
       [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&#39;s, Alzheimer&#39;s and other neurodegenerative diseases; tissues for grafting such as bone marrow, skin, cartilage, tendons, bone, muscle (including cardiac muscle), blood vessels, cornea, neural cells, gastrointestinal cells and others; and organs for transplantation such as kidney, liver, pancreas (including islet cells), heart and lung.  
       [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&#39;s, Parkinson&#39;s disease, Huntington&#39;s disease, amyotrophic lateral sclerosis, and Shy-Drager syndrome. Further conditions which may be treated in accordance with the present invention include mechanical and traumatic disorders, such as spinal cord disorders, head trauma and cerebrovascular diseases such as stroke. Peripheral neuropathies resulting from chemotherapy or other medical therapies may also be treatable using a composition of the invention.  
       [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&#39;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&#39;s disease or resulting from over production of cytokines such as TNF or IL-1. Compositions of the invention may also be useful to treat anaphylaxis and hypersensitivity to an antigenic substance or material. Compositions of this invention may be utilized to prevent or treat conditions such as, but not limited to, sepsis, acute pancreatitis, endotoxin shock, cytokine induced shock, rheumatoid arthritis, chronic inflammatory arthritis, pancreatic cell damage from diabetes mellitus type 1, graft versus host disease, inflammatory bowel disease, inflamation associated with pulmonary disease, other autoimmune disease or inflammatory disease, an antiproliferative agent such as for acute or chronic mylegenous leukemia or in the prevention of premature labor secondary to intrauterine infections.  
       [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&#39;s disease, Alzheimer&#39;s disease, Huntington&#39;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&#39;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&#39;s adjuvant (CFA). The route of injection can vary, but rats may be injected at the base of the tail with an adjuvant mixture. The polypeptide is administered in phosphate buffered solution (PBS) at a dose of about 1-5 mg/kg. The control consists of administering PBS only.  
       [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&#39;s solution, dextrose solution, and solutions consisting of small amounts of the human serum albumin. The vehicle may contain minor amounts of additives that maintain the isotonicity and stability of the polypeptide or other active ingredient. The preparation of such solutions is within the skill of the art.  
       [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&#39;s Pharmaceutical Sciences,” Mack Publishing Co., Easton, Pa., latest edition. A therapeutically effective dose further refers to that amount of the compound sufficient to result in amelioration of symptoms, e.g., treatment, healing, prevention or amelioration of the relevant medical condition, or an increase in rate of treatment, healing, prevention or amelioration of such conditions. When applied to an individual active ingredient, administered alone, a therapeutically effective dose refers to that ingredient alone. When applied to a combination, a therapeutically effective dose refers to combined amounts of the active ingredients that result in the therapeutic effect, whether administered in combination, serially or simultaneously.  
       [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&#39;s Injection, Dextrose Injection, Dextrose and Sodium Chloride Injection, Lactated Ringer&#39;s Injection, or other vehicle as known in the art. The pharmaceutical composition of the present invention may also contain stabilizers, preservatives, buffers, antioxidants, or other additives known to those of skill in the art. For injection, the agents of the invention may be formulated in aqueous solutions, preferably in physiologically compatible buffers such as Hanks&#39;s solution, Ringer&#39;s solution, or physiological saline buffer. For transmucosal administration, penetrants appropriate to the barrier to be permeated are used in the formulation. Such penetrants are generally known in the art.  
       [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&#39;s response. Larger doses of protein or other active ingredient of the present invention may be administered until the optimal therapeutic effect is obtained for the patient, and at that point the dosage is not increased further. It is contemplated that the various pharmaceutical compositions used to practice the method of the present invention should contain about 0.01 μg to about 100 mg (preferably about 0.1 μg to about 10 mg, more preferably about 0.1 μg to about 1 mg) of protein or other active ingredient of the present invention per kg body weight. For compositions of the present invention which are useful for bone, cartilage, tendon or ligament regeneration, the therapeutic method includes administering the composition topically, systematically, or locally as an implant or device. When administered, the therapeutic composition for use in this invention is, of course, in a pyrogen-free, physiologically acceptable form. Further, the composition may desirably be encapsulated or injected in a viscous form for delivery to the site of bone, cartilage or tissue damage. Topical administration may be suitable for wound healing and tissue repair. Therapeutically useful agents other than a protein or other active ingredient of the invention which may also optionally be included in the composition as described above, may alternatively or additionally, be administered simultaneously or sequentially with the composition in the methods of the invention. Preferably for bone and/or cartilage formation, the composition would include a matrix capable of delivering the protein-containing or other active ingredient-containing composition to the site of bone and/or cartilage damage, providing a structure for the developing bone and cartilage and optimally capable of being resorbed into the body. Such matrices may be formed of materials presently in use for other implanted medical applications.  
       [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&#39;s age, sex, and diet, the severity of any infection, time of administration and other clinical factors. The dosage may vary with the type of matrix used in the reconstitution and with inclusion of other proteins in the pharmaceutical composition. For example, the addition of other known growth factors, such as IGF I (insulin like growth factor I), to the final composition, may also effect the dosage. Progress can be monitored by periodic assessment of tissue/bone growth and/or repair, for example, X-rays, histomorphometric determinations and tetracycline labeling.  
       [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 IC 50  as determined in cell culture (i.e., the concentration of the test compound which achieves a half-maximal inhibition of the protein&#39;s biological activity). Such information can be used to more accurately determine useful doses in humans.  
       [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 LD 50  (the dose lethal to 50% of the population) and the ED 50  (the dose therapeutically effective in 50% of the population). The dose ratio between toxic and therapeutic effects is the therapeutic index and it can be expressed as the ratio between LD 50  and ED 50 . Compounds which exhibit high therapeutic indices are preferred. The data obtained from these cell culture assays and animal studies can be used in formulating a range of dosage for use in human. The dosage of such compounds lies preferably within a range of circulating concentrations that include the ED 50  with little or no toxicity. The dosage may vary within this range depending upon the dosage form employed and the route of administration utilized. The exact formulation, route of administration and dosage can be chosen by the individual physician in view of the patient&#39;s condition. See, e.g., Fingl et al., 1975, in “The 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&#39;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, F ab , F ab′ , and F (ab′)2  fragments, and an F ab  expression library. In general, an antibody molecule obtained from humans relates to any of the classes IgG, IgM, IgA, IgE and IgD, which differ from one another by the nature of the heavy chain present in the molecule. Certain classes have subclasses as well, such as IgG 1,  IgG 2 , and others. Furthermore, in humans, the light chain may be a kappa chain or a lambda chain. Reference herein to antibodies includes a reference to all such classes, subclasses and types of human antibody species.  
       [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&#39;s (complete and incomplete), mineral gels (e.g., aluminum hydroxide), surface-active substances (e.g., lysolecithin, pluronic polyols, polyanions, peptides, oil emulsions, dinitrophenol, etc.), adjuvants usable in humans such as Bacille Calmette-Guerin and  Corynebacterium parvum , or similar immunostimulatory agents. Additional examples of adjuvants that can be employed include MPL-TDM adjuvant (monophosphoryl Lipid A, synthetic trehalose dicorynomycolate).  
       [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&#39;s Modified Eagle&#39;s Medium and RPMI-1640 medium. Alternatively, the hybridoma cells can be grown in vivo as ascites in a mammal.  
       [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&#39;s endogenous antibodies in response to challenge by an antigen. (See PCT publication WO94/02602). The endogenous genes encoding the heavy and light immunoglobulin chains in the nonhuman host have been incapacitated, and active loci encoding human heavy and light chain immunoglobulins are inserted into the host&#39;s genome. The human genes are incorporated, for example, using yeast artificial chromosomes containing the requisite human DNA segments. An animal which provides all the desired modifications is then obtained as progeny by crossbreeding intermediate transgenic animals containing fewer than the full complement of the modifications. The preferred embodiment of such a nonhuman animal is a mouse, and is termed the Xenomouse™ as disclosed in PCT publications WO 96/33735 and WO 96/34096. This animal produces B cells that secrete fully human immunoglobulins. The antibodies can be obtained directly from the animal after immunization with an immunogen of interest, as, for example, a preparation of a polyclonal antibody, or alternatively from immortalized B cells derived from the animal, such as hybridomas producing monoclonal antibodies. Additionally, the genes encoding the immunoglobulins with human variable regions can be recovered and expressed to obtain the antibodies directly, or can be 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 F ab  fragment generated by reducing the disulfide bridges of an F (ab′)2  fragment; (iii) an F ab  fragment generated by the treatment of the antibody molecule with papain and a reducing agent and (iv) F v  fragments.  
       [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 (V H ) connected to a light-chain variable domain (V L ) by a linker which is too short to allow pairing between the two domains on the same chain. Accordingly, the V H  and V L  domains of one fragment are forced to pair with the complementary V L  and V H  domains of another fragment, thereby forming two antigen-binding sites. Another strategy for making bispecific antibody fragments by the use of single-chain Fv (sFv) dimers has also been reported. See, Gruber et al., J. Immunol. 152, 5368 (1994).  
       [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  212 Bi,  131 I,  131 In,  90 Y, and  186 Re.  
       [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&#39;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 &amp; Hondo, (1990) J. Clin. Microbiol. 28(6), 1469-72); using UV light (Nagata et al., 1985; Dahlen et al., 1987; Morrissey &amp; Collins, (1989) Mol. Cell Probes 3(2) 189-207) or by covalent binding of base modified DNA (Keller et al., 1988; 1989); all references being specifically incorporated herein.  
       [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 (&gt;NH) that serve as bridgeheads for further covalent coupling. CovaLink Modules may be purchased from Nunc Laboratories. DNA molecules may be bound to CovaLink exclusively at the 5′-end by a phosphoramidate bond, allowing immobilization of more than 1 pmol of DNA (Rasmussen et al., (1991) Anal. Biochem. 198(1) 138-42).  
       [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-MeIm 7 ), is then added to a final concentration of 10 mM 1-MeIm 7 . A ss DNA solution is then dispensed into CovaLink NH strips (75 μl/well) standing on ice.  
       [0430] Carbodiimide 0.2 M 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide (EDC), dissolved in 10 mM 1-MeIm 7 , is made fresh and 25 μl added per well. The strips are incubated for 5 hours at 50° C. After incubation the strips are washed using, e.g., Nunc-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 &amp; Maskos), incorporated herein by reference. This method of preparing an oligonucleotide bound to a support involves attaching a nucleoside 3′-reagent through the phosphate group by a covalent phosphodiester link to aliphatic hydroxyl groups carried by the support. The oligonucleotide is then synthesized on the supported nucleoside and protecting groups removed from the synthetic oligonucleotide chain under standard conditions that do not cleave the oligonucleotide from the support. Suitable reagents include nucleoside phosphoramidite and nucleoside hydrogen phosphorate.  
       [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 &amp; 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&#39;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 mm 2 , depending on the type of label used. By avoiding spotting in some preselected number of rows and columns, separate subsets (subarrays) may be formed. Samples in one subarray may be the same genomic segment of DNA (or the same gene) from different individuals, or may be different, overlapped genomic clones. Each of the subarrays may represent replica spotting of the same samples. In one example, a selected gene segment may be amplified from 64 patients. For each patient, the amplified gene segment may be in one 96-well plate (all 96 wells containing the same sample). A plate for each of the 64 patients is prepared. By using a 96-pin device, all samples may be spotted on one 8×12 cm membrane. Subarrays may contain 64 samples, one from each patient. Where the 96 subarrays are identical, the dot span may be 1 mm 2  and there may be a 1 mm space between subarrays.  
       [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&#39;s database containing EST sequences, dbEST, gb pri, and UniGene, and exons from public domain genomic sequences predicated by GenScan) that belong to this assemblage. The algorithm terminated when there were no additional sequences from the above databases that would extend the assemblage. Further, inclusion of component sequences into the assemblage was based on a BLASTN hit to the extending assemblage with BLAST score greater than 300 and percent identity greater than 95%.  
     [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&#39;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&#39;s Profile-3D threading program developed in Dr. David Eisenberg&#39;s laboratory (U.S. Pat. No. 5,436,850 and Luthy, Bowie, and Eisenberg, Nature, 356:83-85 (1992)) and a publication by R. Sanchez and A. Sali, Proc. Natl. Acad. Sci. USA, 95:13597-12502. The verify score produced by GeneAtlas normalizes the verify score for proteins with different lengths so that a unified cutoff can be used to select good models as follows:  
     [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                       # 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&#39;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.                            
     [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&#39;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&#39;S TYROSINE   “TRANSFERASE BRUTON&#39;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&#39;                                               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&#39;,                                               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&#39; 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&#39;                                               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&#39; 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&#39;; 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&#39;; 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&#39;; 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.  
 
    
     
       
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                 SEQUENCE LISTING 
               
            
           
           
               
            
               
                 The patent application contains a lengthy “Sequence Listing” section. A copy of the “Sequence Listing” is available in electronic form from the USPTO 
               
               
                 web site (http://seqdata.uspto.gov/sequence.html?DocID=20040048249). An electronic copy of the “Sequence Listing” will also be available from the 
               
               
                 USPTO upon request and payment of the fee set forth in 37 CFR 1.19(b)(3).