Compositions for inhibition of membrane fusion-associated events, including human parainfluenza virus transmission

The present invention relates to peptides which exhibit potent anti-retroviral activity. The peptides of the invention comprise DP178 (SEQ ID NO:1) peptide corresponding to amino acids 638 to 673 of the HIV-1.sub.LAI gp41 protein, and fragments, analogs and homologs of DP178. The invention further relates to the uses of such peptides as inhibitory of human and non-human retroviral, especially HIV, transmission to uninfected cells.

1. INTRODUCTION
 The present invention relates, first, to DP178 (SEQ ID NO:1), a peptide
 corresponding to amino acids 638 to 673 of the HIV-1.sub.LAI transmembrane
 protein (TM) gp41, and portions or analogs of DP178 (SEQ ID NO:1), which
 exhibit anti-membrane fusion capability, antiviral activity, such as the
 ability to inhibit HIV transmission to uninfected CD-4.sup.+ cells, or an
 ability to modulate intracellular processes involving coiled-coil peptide
 structures. Further, the invention relates to the use of DP178 (SEQ ID
 NO:1) and DP178 portions and/or analogs as antifusogenic or antiviral
 compounds or as inhibitors of intracellular events involving coiled-coil
 peptide structures. The present invention also relates to peptides
 analogous to DP107, a peptide corresponding to amino acids 558 to 595 of
 the HIV-1.sub.LAI transmembrane protein (TM) gp41, having amino acid
 sequences present in other viruses, such as enveloped viruses, and/or
 other organisms, and further relates to the uses of such peptides. These
 peptides exhibit anti-membrane fusion capability, antiviral activity, or
 the ability to modulate intracellular processes involving coiled-coil
 peptide structures. The present invention additionally relates to methods
 for identifying compounds that disrupt the interaction between DP178 and
 DP107, and/or between DP107-like and DP178-like peptides. Further, the
 invention relates to the use of the peptides of the invention as
 diagnostic agents. For example, a DP178 peptide may be used as an HIV
 subtype-specific diagnostic. The invention is demonstrated, first, by way
 of an Example wherein DP178 (SEQ ID NO:1), and a peptide whose sequence is
 homologous to DP178 are each shown to be potent, non-cytotoxic inhibitors
 of HIV-1 transfer to uninfected CD-4.sup.+ cells. The invention is further
 demonstrated by Examples wherein peptides having structural and/or amino
 acid motif similarity to DP107 and DP178 are identified in a variety of
 viral and nonviral organisms, and in examples wherein a number of such
 identified peptides derived from several different viral systems are
 demonstrated to exhibit antiviral activity.
 2. BACKGROUND OF THE INVENTION
 2.1 Membrane Fusion Events
 Membrane fusion is a ubiquitous cell biological process (for a review, see
 White, J. M., 1992, Science 258:917-924). Fusion events which mediate
 cellular housekeeping functions, such as endocytosis, constitutive
 secretion, and recycling of membrane components, occur continuously in all
 eukaryotic cells.
 Additional fusion events occur in specialized cells. Intracellularly, for
 example, fusion events are involved in such processes as occur in
 regulated exocytosis of hormones, enzymes and neurotransmitters.
 Intercellularly, such fusion events feature prominently in, for example,
 sperm-egg fusion and myoblast fusion.
 Fusion events are also associated with disease states. For example, fusion
 events are involved in the formation of giant cells during inflammatory
 reactions, the entry of all enveloped viruses into cells, and, in the case
 of human immunodeficiency virus (HIV), for example, are responsible for
 the virally induced cell-cell fusion which leads to cell death.
 2.2. The Human Immunodeficiency Virus
 The human immunodeficiency virus (HIV) has been implicated as the primary
 cause of the slowly degenerative immune system disease termed acquired
 immune deficiency syndrome (AIDS) (Barre-Sinoussi, F. et al., 1983,
 Science 220:868-870; Gallo, R. et al., 1984, Science 224:500-503). There
 are at least two distinct types of HIV: HIV-1 (Barre-Sinoussi, F. et al.,
 1983, Science 220:868-870; Gallo R. et al., 1984, Science 224:500-503) and
 HIV-2 (Clavel, F. et al., 1986, Science 233:343-346; Guyader, M. et al.,
 1987, Nature 326:662-669). Further, a large amount of genetic
 heterogeneity exists within populations of each of these types. Infection
 of human CD-4.sup.+ T-lymphocytes with an HIV virus leads to depletion of
 the cell type and eventually to opportunistic infections, neurological
 dysfunctions, neoplastic growth, and ultimately death.
 HIV is a member of the lentivirus family of retroviruses (Teich, N. et al.,
 1984, RNA Tumor Viruses, Weiss, R. et al., eds., CSH-Press, pp. 949-956).
 Retroviruses are small enveloped viruses that contain a diploid,
 single-stranded RNA genome, and replicate via a DNA intermediate produced
 by a virally-encoded reverse transcriptase, an RNA-dependent DNA
 polymerase (Varmus, H., 1988, Science 240:1427-1439). Other retroviruses
 include, for example, oncogenic viruses such as human T-cell leukemia
 viruses (HTLV-I,-II,-III), and feline leukemia virus.
 The HIV viral particle consists of a viral core, composed of capsid
 proteins, that contains the viral RNA genome and those enzymes required
 for early replicative events. Myristylated Gag protein forms an outer
 viral shell around the viral core, which is, in turn, surrounded by a
 lipid membrane enveloped derived from the infected cell membrane. The HIV
 enveloped surface glycoproteins are synthesized as a single 160 Kd
 precursor protein which is cleaved by a cellular protease during viral
 budding into two glycoproteins, gp41 and gp120. gp41 is a transmembrane
 protein and gp120 is an extracellular protein which remains non-covalently
 associated with gp41, possibly in a trimeric or multimeric form
 (Hammarskjold, M. and Rekosh, D., 1989, Biochem. Biophys. Acta
 989:269-280).
 HIV is targeted to CD-4.sup.+ cells because the CD-4 cell surface protein
 acts as the cellular receptor for the HIV-1 virus (Dalgleish, A. et al.,
 1984, Nature 312:763-767; Klatzmann et al., 1984, Nature 312:767-768;
 Maddon et al., 1986, Cell 47:333-348). Viral entry into cells is dependent
 upon gp120 binding the cellular CD-4.sup.+ receptor molecules (McDougal,
 J. S. et al., 1986, Science 231:382-385; Maddon, P. J. et al., 1986, Cell
 47:333-348) and thus explains HIV's tropism for CD-4.sup.+ cells, while
 gp41 anchors the enveloped glycoprotein complex in the viral membrane.
 2.3. HIV Treatment
 HIV infection is pandemic and HIV associated diseases represent a major
 world health problem. Although considerable effort is being put into the
 successful design of effective therapeutics, currently no curative
 anti-retroviral drugs against AIDS exist. In attempts to develop such
 drugs, several stages of the HIV life cycle have been considered as
 targets for therapeutic intervention (Mitsuya, H. et al., 1991, FASEB J.
 5:2369-2381). For example, virally encoded reverse transcriptase has been
 one focus of drug development. A number of reverse-transcriptase-targeted
 drugs, including 2',3'-dideoxynucleoside analogs such as AZT, ddI, ddC,
 and d4T have been developed which have been shown to been active against
 HIV (Mitsuya, H. et al., 1991, Science 249:1533-1544). While beneficial,
 these nucleoside analogs are not curative, probably due to the rapid
 appearance of drug resistant HIV mutants (Lander, B. et al., 1989, Science
 243:1731-1734). In addition, the drugs often exhibit toxic side effects
 such as bone marrow suppression, vomiting, and liver function
 abnormalities.
 Attempts are also being made to develop drugs which can inhibit viral entry
 into the cell, the earliest stage of HIV infection. Here, the focus has
 thus far been on CD4, the cell surface receptor for HIV. Recombinant
 soluble CD4, for example, has been shown to inhibit infection of
 CD-4.sup.+ T-cells by some HIV-1 strains (Smith, D. H. et al., 1987,
 Science 238:1704-1707). Certain primary HIV-1 isolates, however, are
 relatively less sensitive to inhibition by recombinant CD-4 (Daar, E. et
 al., 1990, Proc. Natl. Acad. Sci. USA 87:6574-6579). In addition,
 recombinant soluble CD-4 clinical trials have produced inconclusive
 results (Schooley, R. et al., 1990, Ann. Int. Med. 112:247-253; Kahn, J.
 O. et al., 1990, Ann. Int. Med. 112:254-261; Yarchoan, R. et al., 1989,
 Proc. Vth Int. Conf. on AIDS, p. 564, MCP 137).
 The late stages of HIV replication, which involve crucial virus-specific
 secondary processing of certain viral proteins, have also been suggested
 as possible anti-HIV drug targets. Late stage processing is dependent on
 the activity of a viral protease, and drugs are being developed which
 inhibit this protease (Erickson, J., 1990, Science 249:527-533). The
 clinical outcome of these candidate drugs is still in question.
 Attention is also being given to the development of vaccines for the
 treatment of HIV infection. The HIV-1 enveloped proteins (gp160, gp120,
 gp41) have been shown to be the major antigens for anti-HIV antibodies
 present in AIDS patients (Barin, et al., 1985, Science 228:1094-1096).
 Thus far, therefore, these proteins seem to be the most promising
 candidates to act as antigens for anti-HIV vaccine development. To this
 end, several groups have begun to use various portions of gp160, gp120,
 and/or gp41 as immunogenic targets for the host immune system. See for
 example, Ivanoff, L. et al., U.S. Pat. No. 5,141,867; Saith, G. et al., WO
 92/22,654; Shafferman, A., WO 91/09,872; Formoso, C. et al., WO 90/07,119.
 Clinical results concerning these candidate vaccines, however, still
 remain far in the future.
 Thus, although a great deal of effort is being directed to the design and
 testing of anti-retroviral drugs, a truly effective, non-toxic treatment
 is still needed.
 3. SUMMARY OF THE INVENTION
 The present invention relates, first, to DP178 (SEQ ID NO:1), a 36-amino
 acid synthetic peptide corresponding to amino acids 638 to 673 of the
 transmembrane protein (TM) gp41 from the HIV-1 isolate LAI
 (HIV-.sub.1.sub.LAI), which exhibits potent anti-HIV-1 activity. As
 evidenced by the Example presented below, in Section 6, the DP178 (SEQ ID
 NO:1) antiviral activity is so high that, on a weight basis, no other
 known anti-HIV agent is effective at concentrations as low as those at
 which DP178 (SEQ ID NO:1) exhibits its inhibitory effects.
 The invention further relates to those portions and analogs of DP178 which
 also show such antiviral activity, and/or show anti-membrane fusion
 capability, or an ability to modulate intracellular processes involving
 coiled-coil peptide structures. The term "DP178 analog" refers to a
 peptide which contains an amino acid sequence corresponding to the DP178
 peptide sequence present within the gp41 protein of HIV-1.sub.LAI, but
 found in viruses and/or organisms other than HIV-1.sub.LAI. Such DP178
 analog peptides may, therefore, correspond to DP178-like amino acid
 sequences present in other viruses, such as, for example, enveloped
 viruses, such as retroviruses other than HIV-1.sub.LAI, as well as
 non-enveloped viruses. Further, such analogous DP178 peptides may also
 correspond to DP178-like amino acid sequences present in nonviral
 organisms.
 The invention further relates to peptides DP107 analogs. DP107 is a peptide
 corresponding to amino acids 558-595 of the HIV-1.sub.LAI transmembrane
 protein (TM) gp41. The term "DP107 analog" as used herein refers to a
 peptide which contains an amino acid sequence corresponding to the DP107
 peptide sequence present within the gp41 protein of HIV-1.sub.LAI, but
 found in viruses and organisms other than HIV-1.sub.LAI. Such DP107 analog
 peptides may, therefore, correspond to DP107-like amino acid sequences
 present in other viruses, such as, for example, enveloped viruses, such as
 retroviruses other than HIV-1.sub.LAI, as well as non-enveloped viruses.
 Further, such DP107 analog peptides may also correspond to DP107-like
 amino acid sequences present in nonviral organisms.
 Further, the peptides of the invention include DP107 analog and DP178
 analog peptides having amino acid sequences recognized or identified by
 the 107.times.178.times.4, ALLMOTI5 and/or PLZIP search motifs described
 herein.
 The peptides of the invention may, for example, exhibit antifusogenic
 activity, antiviral activity, and/or may have the ability to modulate
 intracellular processes which involve coiled-coil peptide structures. With
 respect to the antiviral activity of the peptides of the invention, such
 an antiviral activity includes, but is not limited to the inhibition of
 HIV transmission to uninfected CD-4.sup.+ cells. Additionally, the
 antifusogenic capability, antiviral activity or intracellular modulatory
 activity of the peptides of the invention merely requires the presence of
 the peptides of the invention, and, specifically, does not require the
 stimulation of a host immune response directed against such peptides.
 The peptides of the invention may be used, for example, as inhibitors of
 membrane fusion-associated events, such as, for example, the inhibition of
 human and non-human retroviral, especially HIV, transmission to uninfected
 cells. It is further contemplated that the peptides of the invention may
 be used as modulators of intracellular events involving coiled-coil
 peptide structures.
 The peptides of the invention may, alternatively, be used to identify
 compounds which may themselves exhibit antifusogenic, antiviral, or
 intracellular modulatory activity. Additional uses include, for example,
 the use of the peptides of the invention as organism or viral type and/or
 subtype-specific diagnostic tools.
 The terms "antifusogenic" and "anti-membrane fusion", as used herein, refer
 to an agent's ability to inhibit or reduce the level of membrane fusion
 events between two or more moieties relative to the level of membrane
 fusion which occurs between said moieties in the absence of the peptide.
 The moieties may be, for example, cell membranes or viral structures, such
 as viral envelopes or pili. The term "antiviral", as used herein, refers
 to the compound's ability to inhibit viral infection of cells, via, for
 example, cell-cell fusion or free virus infection. Such infection may
 involve membrane fusion, as occurs in the case of enveloped viruses, or
 some other fusion event involving a viral structure and a cellular
 structure (e.g., such as the fusion of a viral pilus and bacterial
 membrane during bacterial conjugation).
 It is also contemplated that the peptides of the invention may exhibit the
 ability to modulate intracellular events involving coiled-coil peptide
 structures. "Modulate", as used herein, refers to a stimulatory or
 inhibitory effect on the intracellular process of interest relative to the
 level or activity of such a process in the absence of a peptide of the
 invention.
 Embodiments of the invention are demonstrated below wherein an extremely
 low concentration of DP178 (SEQ ID NO:1), and very low concentrations of a
 DP178 homolog (SEQ ID NO:3) are shown to be potent inhibitors of HIV-1
 mediated CD-4.sup.+ cell-cell fusion (i.e., syncytial formation) and
 infection of CD-4.sup.+ cells by cell-free virus. Further, it is shown
 that DP178 (SEQ ID NO:1) is not toxic to cells, even at concentrations 3
 logs higher than the inhibitory DP-178 (SEQ ID NO:1) concentration.
 The present invention is based, in part, on the surprising discovery that
 the DP107 and DP178 domains of the HIV gp41 protein non-covalently complex
 with each other, and that their interaction is required for the normal
 infectivity of the virus. This discovery is described in the Example
 presented, below, in Section 8. The invention, therefore, further relates
 to methods for identifying antifusogenic, including antiviral, compounds
 that disrupt the interaction between DP107 and DP178, and/or between
 DP107-like and DP178-like peptides.
 Additional embodiments of the invention (specifically, the Examples
 presents in Sections 9-16 and 19-25, below) are demonstrated, below,
 wherein peptides, from a variety of viral and nonviral sources, having
 structural and/or amino acid motif similarity to DP107 and DP178 are
 identified, and search motifs for their identification are described.
 Further, Examples (in Sections 17, 18, 25-29) are presented wherein a
 number of the peptides of the invention are demonstrated exhibit
 substantial antiviral activity or activity predictive of antiviral
 activity.
 3.1. DEFINITIONS
 Peptides are defined herein as organic compounds comprising two or more
 amino acids covalently joined by peptide bonds. Peptides may be referred
 to with respect to the number of constituent amino acids, i.e., a
 dipeptide contains two amino acid residues, a tripeptide contains three,
 etc. Peptides containing ten or fewer amino acids may be referred to as
 oligopeptides, while those with more than ten amino acid residues are
 polypeptides. Such peptides may also include any of the modifications and
 additional amino and carboxy groups as are described herein.
 Peptide sequences defined herein are represented by one-letter symbols for
 amino acid residues as follows:
 A (alanine)
 R (arginine)
 N (asparagine)
 D (aspartic acid)
 C (cysteine)
 Q (glutamirie)
 E (glutamic acid)
 G (glycine)
 H (histidine)
 I (isoleucine)
 L (leucine)
 K (lysine)
 M (methionine)
 F (phenylalanine)
 P (proline)
 S (serine)
 T (threonine)
 W (tryptophan)
 Y (tyrosine)
 V (valine)

5. DETAILED DESCRIPTION OF THE INVENTION
 Described herein are peptides which may exhibit antifusogenic activity,
 antiviral capability, and/or the ability to modulate intracellular
 processes involving coiled-coil peptide structures. The peptides described
 include, first, DP178 (SEQ ID NO:1), a gp41-derived 36 amino acid peptide
 and fragments and analogs of DP178.
 In addition, the peptides of the invention described herein include
 peptides which are DP107 analogs. DP107 (SEQ ID NO:99) is a 38 amino acid
 peptide corresponding to residues 558 to 595 of the HIV-1.sub.LAI
 transmembrane (TM) gp41 protein. Such DP107 analogs may exhibit
 antifusogenic capability, antiviral activity or an ability to modulate
 intracellular processes involving coiled-coil structures.
 Further, peptides of the invention include DP107 and DP178 are described
 herein having amino acid sequences recognized by the
 107.times.178.times.4, ALLMOTI5, and PLZIP search motifs. Such motifs are
 also discussed.
 Also described here are antifusogenic, antiviral, intracellular modulatory,
 and diagnostic uses of the peptides of the invention. Further, procedures
 are described for the use of the peptides of the invention for the
 identification of compounds exhibiting antifusogenic, antiviral or
 intracellular modulatory activity.
 While not limited to any theory of operation, the following model is
 proposed to explain the potent anti-HIV activity of DP178, based, in part,
 on the experiments described in the Examples, infra. In the HIV protein,
 gp41, DP178 corresponds to a putative .alpha.-helix region located in the
 C-terminal end of the gp41 ectodomain, and appears to associate with a
 distal site on gp41 whose interactive structure is influenced by the
 leucine zipper motif, a coiled-coil structure, referred to as DP107. The
 association of these two domains may reflect a molecular linkage or
 "molecular clasp" intimately involved in the fusion process. It is of
 interest that mutations in the C-terminal .alpha.-helix motif of gp41
 (i.e., the D178 domain) tend to enhance the fusion ability of gp41,
 whereas mutations in the leucine zipper region (i.e., the DP107 domain)
 decrease or abolish the fusion ability of the viral protein. It may be
 that the leucine zipper motif is involved in membrane fusion while the
 C-terminal .alpha.-helix motif serves as a molecular safety to regulate
 the availability of the leucine zipper during virus-induced membrane
 fusion.
 On the basis of the foregoing, two models are proposed of gp41-mediated
 membrane fusion which are schematically shown in FIGS. 11A-B. The reason
 for proposing two models is that the temporal nature of the interaction
 between the regions defined by DP107 and DP178 cannot, as yet, be
 pinpointed. Each model envisions two conformations for gp41--one in a
 "native" state as it might be found on a resting virion. The other in a
 "fusogenic" state to reflect conformational changes triggered following
 binding of gp120 to CD4 and just prior to fusion with the target cell
 membrane. The strong binding affinity between gp120 and CD4 may actually
 represent the trigger for the fusion process obviating the need for a pH
 change such as occurs for viruses that fuse within intracellular vesicles.
 The two major features of both models are: (1) the leucine zipper
 sequences (DP107) in each chain of oligomeric enveloped are held apart in
 the native state and are only allowed access to one another in the
 fusogenic state so as to form the extremely stable coiled-coils, and (2)
 association of the DP178 and DP107 sites as they exist in gp41 occur
 either in the native or fusogenic state. FIGS. 11A depicts DP178/DP107
 interaction in the native state as a molecular clasp. On the other hand,
 if one assumes that the most stable form of the enveloped occurs in the
 fusogenic state, the model in FIG. 11B can be considered.
 When synthesized as peptides, both DP107 and DP178 are potent inhibitors of
 HIV infection and fusion, probably by virtue of their ability to form
 complexes with viral gp41 and interfere with its fusogenic process; e.g.,
 during the structural transition of the viral protein from the native
 structure to the fusogenic state, the DP178 and DP107 peptides may gain
 access to their respective binding sites on the viral gp41, and exert a
 disruptive influence. DP107 peptides which demonstrate anti-HIV activity
 are described in Applicants' co-pending application Ser. No. 08/264,531,
 filed Jun. 23, 1994, which is incorporated by reference herein in its
 entirety.
 As shown in the Examples, infra, a truncated recombinant gp41 protein
 corresponding to the ectodomain of gp41 containing both DP107 and DP178
 domains (excluding the fusion peptide, transmembrane region and
 cytoplasmic domain of gp41) did not inhibit HIV-1 induced fusion. However,
 when a single mutation was introduced to disrupt the coiled-coil structure
 of the DP107 domain--a mutation which results in a total loss of
 biological activity of DP107 peptides--the inactive recombinant protein
 was transformed to an active inhibitor of HIV-1 induced fusion. This
 transformation may result from liberation of the potent DP178 domain from
 a molecular clasp with the leucine zipper, DP107 domain.
 For clarity of discussion, the invention will be described primarily for
 DP178 peptide inhibitors of HIV. However, the principles may be
 analogously applied to other viruses, both enveloped and nonenveloped, and
 to other non-viral organisms.
 5.1. DP178 and DP178-Like Peptides
 The DP178 peptide (SEQ ID NO:1) of the invention corresponds to amino acid
 residues 638 to 673 of the transmembrane protein gp41 from the
 HIV-1.sub.LAI isolate, and has the 36 amino acid sequence (reading from
 amino to carboxy terminus):
 NH.sub.2 -YTSLIHSLIEESQNQQEKNEQELLELDKWASLWNWF-COOH (SEQ ID NO:1)
 In addition to the full-length DP178 (SEQ ID NO:1) 36-mer, the peptides of
 the invention may include truncations of the DP178 (SEQ ID NO:1) peptide
 which exhibit antifusogenic activity, antiviral activity and/or the
 ability to modulate intracellular processes involving coiled-coil peptide
 structures. Truncations of DP178 (SEQ ID NO:1) peptides may comprise
 peptides of between 3 and 36 amino acid residues (i.e., peptides ranging
 in size from a tripeptide to a 36-mer polypeptide) with the following
 amino acid sequence X-YTSLIHSLIEESQNQQEKNEQELLELDKWASLWNWF-Y (SEQ ID
 NO:1). Peptide sequences in these tables are listed from amino (left) to
 carboxy (right) terminus. "X" may represent an amino group (--NH.sub.2)
 and "Z" may represent a carboxyl (--COOH) group. Alternatively, "X" may
 represent a hydrophobic group, including but not limited to carbobenzyl,
 dansyl, or T-butoxycarbonyl; an acetyl group; a
 9-fluorenylmethoxy-carbonyl (FMOC) group; or a covalently attached
 macromolecular group, including but not limited to a lipid-fatty acid
 conjugate, polyethylene glycol, carbohydrate or peptide group. Further,
 "Z" may represent an amido group; a T-butoxycarbonyl group; or a
 covalently attached macromolecular group, including but not limited to a
 lipid-fatty acid conjugate, polyethylene glycol, carbohydrate or peptide
 group. A preferred "X" or "Z" macromolecular group is a peptide group.
 The peptides of the invention also include DP178-like peptides.
 "DP178-like", as used herein, refers, first, to DP178 and DP178
 truncations which contain one or more amino acid substitutions, insertions
 and/or deletions. Second, "DP-178-like" refers to peptide sequences
 identified or recognized by the ALLMOTI5, 107.times.178.times.4 and PLZIP
 search motifs described herein, having structural and/or amino acid motif
 similarity to DP178. The DP178-like peptides of the invention may exhibit
 antifusogenic or antiviral activity, or may exhibit the ability to
 modulate intracellular processes involving coiled-coil peptides. Further,
 such DP178-like peptides may possess additional advantageous features,
 such as, for example, increased bioavailability, and/or stability, or
 reduced host immune recognition.
 HIV-1 and HIV-2 enveloped proteins are structurally distinct, but there
 exists a striking amino acid conservation within the DP178-corresponding
 regions of HIV-1 and HIV-2. The amino acid conservation is of a periodic
 nature, suggesting some conservation of structure and/or function.
 Therefore, one possible class of amino acid substitutions would include
 those amino acid changes which are predicted to stabilize the structure of
 the DP178 peptides of the invention. Utilizing the DP178 and DP178 analog
 sequences described herein, the skilled artisan can readily compile DP178
 consensus sequences and ascertain from these, conserved amino acid
 residues which would represent preferred amino acid substitutions.
 The amino acid substitutions may be of a conserved or non-conserved nature.
 Conserved amino acid substitutions consist of replacing one or more amino
 acids of the DP178 (SEQ ID NO:1) peptide sequence with amino acids of
 similar charge, size, and/or hydrophobicity characteristics, such as, for
 example, a glutamic acid (E) to aspartic acid (D) amino acid substitution.
 Non-conserved substitutions consist of replacing one or more amino acids
 of the DP178 (SEQ ID NO:1) peptide sequence with amino acids possessing
 dissimilar charge, size, and/or hydrophobicity characteristics, such as,
 for example, a glutamic acid (E) to valine (V) substitution.
 Amino acid insertions may consist of single amino acid residues or
 stretches of residues. The insertions may be made at the carboxy or amino
 terminal end of the DP178 or DP178 truncated peptides, as well as at a
 position internal to the peptide. Such insertions will generally range
 from 2 to 15 amino acids in length. It is contemplated that insertions
 made at either the carboxy or amino terminus of the peptide of interest
 may be of a broader size range, with about 2 to about 50 amino acids being
 preferred. One or more such insertions may be introduced into DP178 (SEQ
 ID NO:1) or DP178 truncations, as long as such insertions result in
 peptides which may still be recognized by the 107.times.178.times.4,
 ALLMOTI5 or PLZIP search motifs described herein, or may, alternatively,
 exhibit antifusogenic or antiviral activity, or exhibit the ability to
 modulate intracellular processes involving coiled-coil peptide structures.
 Preferred amino or carboxy terminal insertions are peptides ranging from
 about 2 to about 50 amino acid residues in length, corresponding to gp41
 protein regions either amino to or carboxy to the actual DP178 gp41 amino
 acid sequence, respectively. Thus, a preferred amino terminal or carboxy
 terminal amino acid insertion would contain gp41 amino acid sequences
 found immediately amino to or carboxy to the DP178 region of the gp41
 protein.
 Deletions of DP178 (SEQ ID NO:1) or DP178 truncations are also within the
 scope of the invention. Such deletions consist of the removal of one or
 more amino acids from the DP178 or DP178-like peptide sequence, with the
 lower limit length of the resulting peptide sequence being 4 to 6 amino
 acids. Such deletions may involve a single contiguous or greater than one
 discrete portion of the peptide sequences. One or more such deletions may
 be introduced into DP178 (SEQ ID NO:1) or DP178 truncations, as long as
 such deletions result in peptides which may still be recognized by the
 107.times.178.times.4, ALLMOTI5 or PLZIP search motifs described herein,
 or may, alternatively, exhibit antifusogenic or antiviral activity, or
 exhibit the ability to modulate intracellular processes involving
 coiled-coil peptide structures.
 DP178 analogs are further described, below, in Section 5.3.
 5.2. DP107 and DP107-Like Peptides
 Further, the peptides of the invention include peptides having amino acid
 sequences corresponding to DP107 analogs. DP107 is a 38 amino acid peptide
 which exhibits potent antiviral activity, and corresponds to residues 558
 to 595 of HIV-1.sub.LAI transmembrane (TM) gp41 protein, as shown here:
 NH.sub.2 -NNLLRAIEAQQHLLQLTVWQIKQLQARILAVERYLKDQ-COOH
 In addition to the full-length DP107 38-mer, the peptides of the invention
 may include truncations of the DP107 peptide which exhibit antifusogenic
 activity, antiviral activity and/or the ability to modulate intracellular
 processes involving coiled-coil peptide structures. Truncations of DP107
 peptides may comprise peptides of between 3 and 38 amino acid residues
 (i.e., peptides ranging in size from a tripeptide to a 38-mer
 polypeptide), with the following amino acid sequence
 X-NNLLRAIEAQQHLLQLTVWQIKQLQARILAVERYLKDQ-Y (SEQ ID NO:25) including
 C-terminally truncated fragments containing at least three amino acids or
 N-terminal fragments containing at least three amino acids. Peptide
 sequences in these tables are listed from amino (left) to carboxy (right)
 terminus. "X" may represent an amino group (--NH.sub.2) and "Z" may
 represent a carboxyl (--COOH) group. Alternatively, "X" may represent a
 hydrophobic group, including but not limited to carbobenzyl, dansyl, or
 T-butoxycarbonyl; an acetyl group; a 9-fluorenylmethoxy-carbonyl (FMOC)
 group; or a covalently attached macromolecular group, including but not
 limited to a lipid-fatty acid conjugate, polyethylene glycol, carbohydrate
 or peptide group. Further, "Z" may represent an amido group; a
 T-butoxycarbonyl group; or a covalently attached macromolecular group,
 including but not limited to a lipid-fatty acid conjugate, polyethylene
 glycol, carbohydrate or peptide group. A preferred "X" or "Z"
 macromolecular group is a peptide group.
 The peptides of the invention also include DP107-like peptides.
 "DP107-like", as used herein, refers, first, to DP107 and DP107
 truncations which contain one or more amino acid substitutions, insertions
 and/or deletions. Second, "DP-107-like" refers to peptide sequences
 identified or recognized by the ALLMOTI5, 107.times.178.times.4 and PLZIP
 search motifs described herein, having structural and/or amino acid motif
 similarity to DP107. The DP107-like peptides of the invention may exhibit
 antifusogenic or antiviral activity, or may exhibit the ability to
 modulate intracellular processes involving coiled-coil peptides. Further,
 such DP107-like peptides may possess additional advantageous features,
 such as, for example, increased bioavailability, and/or stability, or
 reduced host immune recognition.
 HIV-1 and HIV-2 enveloped proteins are structurally distinct, but there
 exists a striking amino acid conservation within the DP107-corresponding
 regions of HIV-1 and HIV-2. The amino acid conservation is of a periodic
 nature, suggesting some conservation of structure and/or function.
 Therefore, one possible class of amino acid substitutions would include
 those amino acid changes which are predicted to stabilize the structure of
 the DP107 peptides of the invention. Utilizing the DP107 and DP107 analog
 sequences described herein, the skilled artisan can readily compile DP107
 consensus sequences and ascertain from these, conserved amino acid
 residues which would represent preferred amino acid substitutions.
 The amino acid substitutions may be of a conserved or non-conserved nature.
 Conserved amino acid substitutions consist of replacing one or more amino
 acids of the DP107 peptide sequence with amino acids of similar charge,
 size, and/or hydrophobicity characteristics, such as, for example, a
 glutamic acid (E) to aspartic acid (D) amino acid substitution.
 Non-conserved substitutions consist of replacing one or more amino acids
 of the DP107 (SEQ ID NO:25) peptide sequence with amino acids possessing
 dissimilar charge, size, and/or hydrophobicity characteristics, such as,
 for example, a glutamic acid (E) to valine (V) substitution.
 Amino acid insertions may consist of single amino acid residues or
 stretches of residues. The insertions may be made at the carboxy or amino
 terminal end of the DP107 or DP107 truncated peptides, as well as at a
 position internal to the peptide. Such insertions will generally range
 from 2 to 15 amino acids in length. It is contemplated that insertions
 made at either the carboxy or amino terminus of the peptide of interest
 may be of a broader size range, with about 2 to about 50 amino acids being
 preferred. One or more such insertions may be introduced into DP107 or
 DP107 truncations, as long as such insertions result in peptides which may
 still be recognized by the 107.times.178.times.4, ALLMOTI5 or PLZIP search
 motifs described herein, or may, alternatively, exhibit antifusogenic or
 antiviral activity, or exhibit the ability to modulate intracellular
 processes involving coiled-coil peptide structures.
 Preferred amino or carboxy terminal insertions are peptides ranging from
 about 2 to about 50 amino acid residues in length, corresponding to gp41
 protein regions either amino to or carboxy to the actual DP107 gp41 amino
 acid sequence, respectively. Thus, a preferred amino terminal or carboxy
 terminal amino acid insertion would contain gp41 amino acid sequences
 found immediately amino to or carboxy to the DP107 region of the gp41
 protein.
 Deletions of DP107 or DP178 truncations are also within the scope of the
 invention. Such deletions consist of the removal of one or more amino
 acids from the DP107 or DP107-like peptide sequence, with the lower limit
 length of the resulting peptide sequence being 4 to 6 amino acids. Such
 deletions may involve a single contiguous or greater than one discrete
 portion of the peptide sequences. One or more such deletions may be
 introduced into DP107 or DP107 truncations, as long as such deletions
 result in peptides which may still be recognized by the
 107.times.178.times.4, ALLMOTI5 or PLZIP search motifs described herein,
 or may, alternatively, exhibit antifusogenic or antiviral activity, or
 exhibit the ability to modulate intracellular processes involving
 coiled-coil peptide structures.
 DP107 and DP107 truncations are more fully described in Applicants'
 co-pending U.S. patent application Ser. No. 08/374,666, filed Jan. 27,
 1995, and which is incorporated herein by reference in its entirety. DP107
 analogs are further described, below, in Section 5.3.
 5.3. DP107 and DP178 Analogs
 Peptides corresponding to analogs of the DP178, DP178 truncations, DP107
 and DP107 truncation sequences of the invention, described, above, in
 Sections 5.1 and 5.2 may be found in other viruses, including, for
 example, non-HIV-1.sub.LAI enveloped viruses, non-enveloped viruses and
 other non-viral organisms.
 The term "analog", as used herein, refers to a peptide which is recognized
 or identified via the 107.times.178.times.4, ALLMOTI5 and/or PLZIP search
 strategies discussed below. Further, such peptides may exhibit
 antifusogenic capability, antiviral activity, or the ability to modulate
 intracellular processes involving coiled-coil structures.
 Such DP178 and DP107 analogs may, for example, correspond to peptide
 sequences present in TM proteins of enveloped viruses and may,
 additionally correspond to peptide sequences present in non enveloped and
 non-viral organisms. Such peptides may exhibit antifusogenic activity,
 antiviral activity, most particularly antiviral activity which is specific
 to the virus in which their native sequences are found, or may exhibit an
 ability to modulate intracellular processes involving coiled-coil peptide
 structures.
 DP178 analogs are peptides whose amino acid sequences are comprised of the
 amino acid sequences of peptide regions of, for example, other (i.e.,
 other than HIV-1.sub.LAI) viruses that correspond to the gp41 peptide
 region from which DP178 (SEQ ID NO:1) was derived. Such viruses may
 include, but are not limited to, other HIV-1 isolates and HIV-2 isolates.
 DP178 analogs derived from the corresponding gp41 peptide region of other
 (i.e., non HIV-1.sub.LAI) HIV-1 isolates may include, for example, peptide
 sequences as shown below.
 NH.sub.2 -YTNTIYTLLEESQNQQEKNEQELLELDKWASLWNWF-COOH (DP-185; SEQ ID NO:3);
 NH.sub.2 -YTGIIYNLLEESQNQQEKNEQELLELDKWANLWNWF-COOH (SEQ ID NO:4);
 NH.sub.2 -YTSLIYSLLEKSQIQQEKNEQELLELDKWASLWNWF-COOH (SEQ ID NO:5).
 SEQ ID NO:3 (DP-185), SEQ ID NO:4, and SEQ ID NO:5 are derived from
 HIV-1.sub.SF2, HIV-1.sub.RF, and HIV-1.sub.MN isolates, respectively.
 Underlined amino acid residues refer to those residues that differ from
 the corresponding position in the DP178 (SEQ ID NO:1) peptide. One such
 DP178 analog, DP-185 (SEQ ID NO:3), is described in the Example presented
 in Section 6, below, where it is demonstrated that DP-185 (SEQ ID NO:3)
 exhibits antiviral activity. The DP178 analogs of the invention may also
 include truncations, as described above. Further, the analogs of the
 invention modifications such those described for DP178 analogs in Section
 5.1., above. It is preferred that the DP178 analogs of the invention
 represent peptides whose amino acid sequences correspond to the DP178
 region of the gp41 protein, it is also contemplated that the peptides of
 the invention may, additionally, include amino sequences, ranging from
 about 2 to about 50 amino acid residues in length, corresponding to gp41
 protein regions either amino to or carboxy to the actual DP178 amino acid
 sequence.
 Striking similarities, as shown in FIG. 1, exist within the regions of
 HIV-1 and HIV-2 isolates which correspond to the DP178 sequence. A DP178
 analog derived from the HIV-2.sub.NIHZ isolate has the 36 amino acid
 sequence (reading from amino to carboxy terminus):
 NH.sub.2 -LEANISQSLEQAQIQQEKNMYELQKLNSWDVFTNWL-COOH (SEQ ID NO:7)
 Possible truncations of the HIV-2.sub.NIHZ DP178 analog may comprise
 peptides of between 3 and 36 amino acid residues (i.e., peptides ranging
 in size from a tripeptide to a 36-mer polypeptide) with the following
 amino acid sequence:
 X-LEANISQSLEQAQIQQEKNMYELQKLNSWDVFTNWL-Y (SEQ ID NO:7) including
 C-terminally truncated fragments containing at least three amino acids or
 N-terminal fragments containing at least three amino acids. Peptide
 sequences in these tables are listed from amino (left) to carboxy (right)
 terminus. "X" may represent an amino group (--NH.sub.2) and "Z" may
 represent a carboxyl (--COOH) group. Alternatively, "X" may represent a
 hydrophobic group, including but not limited to carbobenzyl, dansyl, or
 T-butoxycarbonyl; an acetyl group; a 9-fluorenylmethoxy-carbonyl (FMOC)
 group; or a covalently attached macromolecular group, including but not
 limited to a lipid-fatty acid conjugate, polyethylene glycol, carbohydrate
 or peptide group. Further, "Z" may represent an amido group; a
 T-butoxycarbonyl group; or a covalently attached macromolecular group,
 including but not limited to a lipid-fatty acid conjugate, polyethylene
 glycol, carbohydrate or peptide group. A preferred "X" or "Z"
 macromolecular group is a peptide group.
 DP178 and DP107 analogs are recognized or identified, for example, by
 utilizing one or more of the 107.times.178.times.4, ALLMOTI5 or PLZIP
 computer-assisted search strategies described and demonstrated, below, in
 the Examples presented in Sections 9 through 16 and 19 through 25. The
 search strategy identifies additional peptide regions which are predicted
 to have structural and/or amino acid sequence features similar to those of
 DP107 and/or DP178.
 The search strategies are described fully, below, in the Example presented
 in Section 9. While this search strategy is based, in part, on a primary
 amino acid motif deduced from DP107 and DP178, it is not based solely on
 searching for primary amino acid sequence homologies, as such protein
 sequence homologies exist within, but not between major groups of viruses.
 For example, primary amino acid sequence homology is high within the TM
 protein of different strains of HIV-1 or within the TM protein of
 different isolates of simian immunodeficiency virus (SIV). Primary amino
 acid sequence homology between HIV-1 and SIV, however, is low enough so as
 not to be useful. It is not possible, therefore, to find peptide regions
 similar to DP107 or DP178 within other viruses, or within non-viral
 organisms, whether structurally, or otherwise, based on primary sequence
 homology, alone.
 Further, while it would be potentially useful to identify primary sequence
 arrangements of amino acids based on, for example, the physical chemical
 characteristics of different classes of amino acids rather than based on
 the specific amino acids themselves, such search strategies have, until
 now, proven inadequate. For example, a computer algorithm designed by
 Lupas et al. to identify coiled-coil propensities of regions within
 proteins (Lupas, A., et al., 1991 Science 252:1162-1164) is inadequate for
 identifying protein regions analogous to DP107 or DP178.
 Specifically, analysis of HIV-1 gp160 (containing both gp120 and gp41)
 using the Lupas algorithm does not identify the coiled-coil region within
 DP107. It does, however, identify a region within DP178 beginning eight
 amino acids N-terminal to the start of DP178 and ending eight amino acids
 from the C-terminus. The DP107 peptide has been shown experimentally to
 form a stable coiled coil. A search based on the Lupas search algorithm,
 therefore, would not have identified the DP107 coiled-coil region.
 Conversely, the Lupas algorithm identified the DP178 region as a potential
 coiled-coil motif. However, the peptide derived from the DP178 region
 failed to form a coiled coil in solution.
 A possible explanation for the inability of the Lupas search algorithm to
 accurately identify coiled-coil sequences within the HIV-1 TM, is that the
 Lupas algorithm is based on the structure of coiled coils from proteins
 that are not structurally or functionally similar to the TM proteins of
 viruses, antiviral peptides (e.g. DP107 and DP178) of which are an object
 of this invention.
 The computer search strategy of the invention, as demonstrated in the
 Examples presented below, in Sections 9 through 16 and 19 through 25,
 successfully identifies regions of proteins similar to DP107 or DP178.
 This search strategy was designed to be used with a commercially-available
 sequence database package, preferably PC/Gene.
 A series of search motifs, the 107.times.178.times.4, ALLMOTI5 and PLZIP
 motifs, were designed and engineered to range in stringency from strict to
 broad, as discussed in this Section and in Section 9, with
 107.times.178.times.4 being preferred. The sequences identified via such
 search motifs, such as those listed in Tables V-XIV, below, potentially
 exhibit antifusogenic, such as antiviral, activity, may additionally be
 useful in the identification of antifusogenic, such as antiviral,
 compounds, and are intended to be within the scope of the invention.
 Coiled-coiled sequences are thought to consist of heptad amino acid
 repeats. For ease of description, the amino acid positions within the
 heptad repeats are sometimes referred to as A through G, with the first
 position being A, the second B, etc. The motifs used to identify
 DP107-like and DP178-like sequences herein are designed to specifically
 search for and identify such heptad repeats. In the descriptions of each
 of the motifs described, below, amino acids enclosed by brackets , i.e., [
 ], designate the only amino acid residues that are acceptable at the given
 position, while amino acids enclosed by braces, i.e., { }, designate the
 only amino acids which are unacceptable at the given heptad position. When
 a set of bracketed or braced amino acids is followed by a number in
 parentheses i.e., ( ), it refers to the number of subsequent amino acid
 positions for which the designated set of amino acids hold, e.g, a (2)
 means "for the next two heptad amino acid positions".
 The ALLMOTI5 is written as follows:
 {CDGHP}-{CFP}(2)-{CDGHP}-{CFP}(3)--
 {CDGHP}-{CFP}(2)-{CDGHP}-{CFP}(3)--
 {CDGHP}-{CFP}(2)-{CDGHP}-{CFP}(3)--
 {CDGHP}-{CFP}(2)-{CDGHP}-{CFP}(3)--
 {CDGHP}-{CFP}(2)-{CDGHP}-{CFP}(3)--
 Translating this motif, it would read: "at the first (A) position of the
 heptad, any amino acid residue except C, D, G, H, or P is acceptable, at
 the next two (B,C) amino acid positions, any amino acid residue except C,
 F, or P is acceptable, at the fourth heptad position (D), any amino acid
 residue except C, D, G, H, or P is acceptable, at the next three (E, F, G)
 amino acid positions, any amino acid residue except C, F, or P is
 acceptable. This motif is designed to search for five consecutive heptad
 repeats (thus the repeat of the first line five times), meaning that it
 searches for 35-mer sized peptides. It may also be designed to search for
 28-mers, by only repeating the initial motif four times. With respect to
 the ALLMOTI5 motif, a 35-mer search is preferred. Those viral
 (non-bacteriophage) sequences identified via such an ALLMOTI5 motif are
 listed in Table V, below, at the end of this Section. The viral sequences
 listed in Table V potentially exhibit antiviral activity, may be useful in
 the identification of antiviral compounds, and are intended to be within
 the scope of the invention. In those instances wherein a single gene
 exhibits greater than one sequence recognized by the ALLMOTI5 search
 motif, the amino acid residue numbers of these sequences are listed under
 "Area 2", Area 3", etc. This convention is used for each of the Tables
 listed, below, at the end of this Section.
 The 107.times.178.times.4 motif is written as follows:
 [EFIKLNQSTVWY]-{CFMP}(2)-[EFIKLNQSTVWY]-{CFMP}(3)--
 [EFIKLNQSTVWY]-{CFMP}(2)-[EFIKLNQSTVWY]-{CFMP}(3)--
 [EFIKLNQSTVWY]-{CFMP}(2)-[EFIKLNQSTVWY]-{CFMP}(3)--
 [EFIKLNQSTVWY]-{CFMP}(2)-[EFIKLNQSTVWY]-{CFMP}(3)--
 Translating this motif, it would read: "at the first (A) position of the
 heptad, only amino acid residue E, F, I, K, L, N, Q, S, T, V, W, or Y is
 acceptable, at the next two (B,C) amino acid positions, any amino acid
 residue except C, F, M or P is acceptable, at the fourth position (D),
 only amino acid residue E, F, I, K, L, N, Q, S, T, V, W, or Y is
 acceptable, at the next three (E, F, G) amino acid positions, any amino
 acid residue except C, F, M or P is acceptable. This motif is designed to
 search for four consecutive heptad repeats (thus the repeat of the first
 line four times), meaning that it searches for 28-mer sized peptides. It
 may also be designed to search for 35-mers, by repeating the initial motif
 five times. With respect to the 107.times.178.times.4 motif, a 28-mer
 search is preferred.
 Those viral (non-bacteriophage) sequences identified via such a
 107.times.178.times.4 motif are listed in Table II, below, at the end of
 this Section, with those viral (non-bacteriophage) sequences listed in
 Table III, below at the end of this Section, being preferred.
 The 107.times.178.times.4 search motif was also utilized to identify
 non-viral procaryotic protein sequences, as listed in Table IV, below, at
 the end of this Section. Further, this search motif was used to reveal a
 number of human proteins. The results of this human protein
 107.times.178.times.4 search is listed in Table V, below, at the end of
 this Section. The sequences listed in Tables IV and V, therefore, reveal
 peptides which may be useful as antifusogenic compounds or in the
 identification of antifusogenic compounds, and are intended to be within
 the scope of the invention.
 The PLZIP series of motifs are as listed in FIG. 19. These motifs are
 designed to identify leucine zipper coiled-coil like heptads wherein at
 least one proline residue is present at some predefined distance
 N-terminal to the repeat. These PLZIP motifs find regions of proteins with
 similarities to HIV-1 DP178 generally located just N-terminal to the
 transmembrane anchor. These motifs may be translated according to the same
 convention described above. Each line depicted in FIG. 19 represents a
 single, complete search motif. "X" in these motifs refers to any amino
 acid residue. In instances wherein a motif contains two numbers within
 parentheses, this refers to a variable number of amino acid residues. For
 example, X (1,12) is translated to "the next one to twelve amino acid
 residues, inclusive, may be any amino acid".
 Tables VI through IX below, at the end of this Section, list sequences
 identified via searches conducted with such PLZIP motifs. Specifically,
 Table VI lists viral sequences identified via PCTLZIP, P1CTLZIP and
 P2CTLZIP search motifs, Table VII lists viral sequences identified via
 P3CTLZIP, P4CTLZIP, P5CTLZIP and P6CTLZIP search motifs, Table VIII lists
 viral sequences identified via P7CTLZIP, P8CTLZIP and P9CTLZIP search
 motifs, Table IX lists viral sequences identified via P12LZIPC searches
 and Table X lists viral sequences identified via P23TLZIPC search motifs
 The viral sequences listed in these tables represent peptides which
 potentially exhibit antiviral activity, may be useful in the
 identification of antiviral compounds, and are intended to be within the
 scope of the invention.
 The Examples presented in Sections 17, 18, 26 and 27 below, demonstrate
 that viral sequences identified via the motif searches described herein
 identify substantial antiviral characteristics. Specifically, the Example
 presented in Section 17 describes peptides with anti-respiratory syncytial
 virus activity, the Example presented in Section 18 describes peptides
 with anti-parainfluenza virus activity, the Example presented in Section
 26 describes peptides with anti-measles virus activity and the Example
 presented in Section 27 describes peptides with anti-simian
 immunodeficiency virus activity.
 The DP107 and DP178 analogs may, further, contain any of the additional
 groups described for DP178, above, in Section 5.1. For example, these
 peptides may include any of the additional amino-terminal groups as
 described above for "X" groups, and may also include any of the
 carboxy-terminal groups as described, above, for "Z" groups.
 Additionally, truncations of the identified DP107 and DP178 peptides are
 among the peptides of the invention. Further, such DP107 and DP178 analogs
 and DP107/DP178 analog truncations may exhibit one or more amino acid
 substitutions, insertion, and/or deletions. The DP178 analog amino acid
 substitutions, insertions and deletions, are as described, above, for
 DP178-like peptides in Section 5.1. The DP-107 analog amino acid
 substitutions, insertions and deletions are also as described, above, for
 DP107-like peptides in Section 5.2.
 Truncations of Respiratory Syncytial Virus region DP107 peptides may
 comprise peptides of between 3 and 36 amino acid residues (i.e., peptides
 ranging in size from a tripeptide to a 36 mer polypeptide) with the
 following amino acid sequence:
 X-YTSVITIELSNIKENKCNGTDAKVKLIKQELDKYKNAVTELQLLMZQST-Z (SEQ ID NO:16)
 including C-terminally truncated fragments containing at least three amino
 acids or N-terminal fragments containing at least three amino acids.
 Truncations of Respiratory Syncytial Virus region DP178 peptides may
 comprise peptides of between 3 and 36 amino acid residues (i.e., peptides
 ranging in size from a tripeptide to a 36 mer polypeptide) with the
 following amino acid sequence:
 X-FYDPLVFPSDEFDASISQVNEKINQSLAFIRKSDELL-Z (SEQ ID NO:17) including
 C-terminally truncated fragments containing at least three amino acids or
 N-terminal fragments containing at least three amino acids. Truncations of
 Human Parainfluenza Virus 3 region DP107 peptides may comprise peptides of
 between 3 and 36 amino acid residues (i.e., peptides ranging in size from
 a tripeptide to a 36 mer polypeptide) with the following amino acid
 sequence:
 X-ALGVATSAQITAAVALVEAKQARSDIEKLKEAIR-Z (SEQ ID NO:19) including
 C-terminally truncated fragments containing at least three amino acids or
 N-terminal fragments containing at least three amino acids. Truncations of
 Human Parainfluenza Virus 3 region DP178 peptides may comprise peptides of
 between 3 and 36 amino acid residues (i.e., peptides ranging in size from
 a tripeptide to a 36 mer polypeptide) with the following amino acid
 sequence:
 X-ITLNNSVALDPIDISIELNKAKSDLEESKEWIRRS-Z (SEQ ID NO:18) including
 C-terminally truncated fragments containing at least three amino acids or
 N-terminal fragments containing at least three amino acids. Further, Table
 XI, below, presents DP107/DP178 analogs and analog truncations which
 exhibit substantial antiviral activity. These antiviral peptides are
 grouped according to the specific virus which they inhibit, including
 respiratory syncytial virus, human parainfluenza virus 3, simian
 immunodeficiency virus and measles virus. ##SPC1##
 ##SPC2##
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 ##SPC267##
 TABLE XI
 REPRESENTATIVE DP107/DP178 ANALOG ANTIVIRAL PEPTIDES
 Anti-Respiratory Syncytial Virus Peptides
 X-TSVITIELSNIKENKCNGTDAKVKLIKQELDKYKN-Z (SEQ ID NO:125)
 X-SVITIELSNIKENKCNGTDAKVKLIKQELDKYKNA-Z (SEQ ID NO:126)
 X-VITIELSNIKENKCNGTDAKVKLIKQELDKYKNAV-Z (SEQ ID NO:213)
 X-VAVSKVLHLEGEVNKIALLSTNKAVVSLSNGVS-Z (SEQ ID NO:20)
 X-AVSKVLHLEGEVNKIALLSTNKAVVSLSNGVSV-Z (SEQ ID NO:21)
 X-VSKVLHLEGEVNKIALLSTNKAVVSLSNGVSVL-Z (SEQ ID NO:22)
 X-SKVLHLEGEVNKIALLSTNKAVVSLSNGVSVLT-Z (SEQ ID NO:23)
 X-KVLHLEGEVNKIALLSTNKAVVSLSNGVSVLTS-Z (SEQ ID NO:24)
 X-LEGEVNKIALLSTNKAVVSLSNGVSVLTSKVLD-Z (SEQ ID NO:25)
 X-GEVNKIALLSTNKAVVSLSNGVSVLTSKVLDLK-Z (SEQ ID NO:26)
 X-EVNKIALLSTNKAVVSLSNGVSVLTSKVLDLKN-Z (SEQ ID NO:27)
 X-VNKIALLSTNKAVVSLSNGVSVLTSKVLDLKNY-Z (SEQ ID NO:28)
 X-NKIALLSTNKAVVSLSNGVSVLTSKVLDLKNYI-Z (SEQ ID NO:29)
 X-KIALLSTNKAVVSLSNGVSVLTSKVLDLKNYID-Z (SEQ ID NO:30)
 X-IALLSTNKAVVSLSNGVSVLTSKVLDLKNYIDK-Z (SEQ ID NO:31)
 X-ALLSTNKAVVSLSNGVSVLTSKVLDLKNYIDKQ-Z (SEQ ID NO:32)
 Anti-human Parainfluenza Virus 3 Peptides
 X-TLNNSVALDPIDISIELNKAKSDLEESKEWIRRSN-Z (SEQ ID NO:33)
 X-LNNSVALDPIDISIELNKAKSDLEESKEWIRRSNQ-Z (SEQ ID NO:34)
 X-NNSVALDPIDISIELNKAKSDLEESKEWIRRSNQK-Z (SEQ ID NO:35)
 X-NSVALDPIDISIELNKAKSDLEESKEWIRRSNQKL-Z (SEQ ID NO:36)
 X-SVALDPIDISIELNKAKSDLEESKEWIRRSNQKLD-Z (SEQ ID NO:37)
 X-VALDPIDISIELNKAKSDLEESKEWIRRSNQKLDS-Z (SEQ ID NO:38)
 X-ALDPIDISIELNKAKSDLEESKEWIRRSNQKLDSI-Z (SEQ ID NO:39)
 X-LDPIDISIELNKAKSDLEESKEWIRRSNQKLDSIG-Z (SEQ ID NO:40)
 X-DPIDISIELNKAKSDLEESKEWIRRSNQKLDSIGN-Z (SEQ ID NO:41)
 X-PIDISIELNKAKSDLEESKEWIRRSNQKLDSIGNW-Z (SEQ ID NO:42)
 X-IDISIELNKAKSDLEESKEWIRRSNQKLDSIGNWH-Z (SEQ ID NO:43)
 X-DISIELNKAKSDLEESKEWIRRSNQKLDSIGNWHQ-Z (SEQ ID NO:44)
 X-ISIELNKAKSDLEESKEWIRRSNQKLDSIGNWHQS-Z (SEQ ID NO:45)
 X-SIELNKAKSDLEESKEWIRRSNQKLDSIGNWHQSS-Z (SEQ ID NO:46)
 X-IELNKAKSDLEESKEWIRRSNQKLDSIGNWHQSST-Z (SEQ ID NO:47)
 X-ELNKAKSDLEESKEWIRRSNQKLDSIGNWHQSSTT-Z (SEQ ID NO:48)
 X-TAAVALVEAKQARSDIEKLKEAIRDTNKAVQSVQS-Z (SEQ ID NO:49)
 X-AVALVEAKQARSDIEKLKEAIRDTNKAVQSVQSSI-Z (SEQ ID NO:50)
 X-LVEAKQARSDIEKLKEAIRDTNKAVQSVQSSIGNL-Z (SEQ ID NO:51)
 X-VEAKQARSDIEKLKEAIRDTNKAVQSVQSSIGNLI-Z (SEQ ID NO:52)
 X-EAKQARSDIEKLKEAIRDTNKAVQSVQSSIGNLIV-Z (SEQ ID NO:53)
 X-AKQARSDIEKLKEAIRDTNKAVQSVQSSIGNLIVA-Z (SEQ ID NO:54)
 X-KQARSDIEKLKEAIRDTNKAVQSVQSSIGNLIVAI-Z (SEQ ID NO:55)
 X-QARSDIEKLKEAIRDTNKAVQSVQSSIGNLIVAIK-Z (SEQ ID NO:56)
 X-ARSDIEKLKEAIRDTNKAVQSVQSSIGNLIVAIKS-Z (SEQ ID NO:57)
 X-RSDIEKLKEAIRDTNKAVQSVQSSIGNLIVAIKSV-Z (SEQ ID NO:58)
 X-SDIEKLKEAIRDTNKAVQSVQSSIGNLIVAIKSVQ-Z (SEQ ID NO:59)
 X-KLKEAIRDTNKAVQSVQSSIGNLIVAIKSVQDYVN-Z (SEQ ID NO:60)
 X-LKEAIRDTNKAVQSVQSSIGNLIVAIKSVQDYVNK-Z (SEQ ID NO:61)
 X-AIRDTNKAVQSVQSSIGNLIVAIKSVQDYVNKEIV-Z (SEQ ID NO:62)
 Anti-simian Immunodeficiency Virus Peptides
 X-WQEWERKVDFLEENITALLEEAQIQQEKNMYELQK-Z (SEQ ID NO:63)
 X-QEWERKVDFLEENITALLEEAQIQQEKNMYELQKL-Z (SEQ ID NO:64)
 X-EWERKVDFLEENITALLEEAQIQQEKNMYELQKLN-Z (SEQ ID NO:65)
 X-WERKVDFLEENITALLEEAQIQQEKNMYELQKLNS-Z (SEQ ID NO:66)
 X-ERKVDFLEENITALLEEAQIQQEKNMYELQKLNSW-Z (SEQ ID NO:67)
 X-RKVDFLEENITALLEEAQIQQEKNMYELQKLNSWD-Z (SEQ ID NO:68)
 X-KVDFLEENITALLEEAQIQQEKNMYELQKLNSWDV-Z (SEQ ID NO:69)
 X-VDFLEENITALLEEAQIQQEKNMYELQKLNSWDVF-Z (SEQ ID NO:70)
 X-DFLEENITALLEEAQIQQEKNMYELQKLNSWDVFG-Z (SEQ ID NO:71)
 X-FLEENITALLEEAQIQQEKNMYELQKLNSWDVFGN-Z (SEQ ID NO:72)
 Anti-measles Virus Peptides
 X-LHRIDLGPPISLERLDVGTNLGNAIAKLEAKELL-Z (SEQ ID NO:73)
 X-HRIDLGPPISLERLDVGTNLGNAIAKLEAKELLE-Z (SEQ ID NO:74)
 X-RIDLGPPISLERLDVGTNLGNAIAKLEAKELLES-Z (SEQ ID NO:75)
 X-IDLGPPISLERLDVGTNLGNAIAKLEAKELLESS-Z (SEQ ID NO:76)
 X-DLGPPISLERLDVGTNLGNAIAKLEAKELLESSD-Z (SEQ ID NO:77)
 X-LGPPISLERLDVGTNLGNAIAKLEAKELLESSDQ-Z (SEQ ID NO:78)
 X-GPPISLERLDVGTNLGNAIAKLEAKELLESSDQI-Z (SEQ ID NO:79)
 X-PPISLERLDVGTNLGNAIAKLEAKELLESSDQIL-Z (SEQ ID NO:80)
 X-PISLERLDVGTNLGNAIAKLEAKELLESSDQILR-Z (SEQ ID NO:81)
 X-SLERLDVGTNLGNAIAKLEAKELLESSDQILRSM-Z (SEQ ID NO:82)
 X-LERLDVGTNLGNAIAKLEAKELLESSDQILRSMK-Z (SEQ ID NO:83)
 The one Letter Amino Acid Code is used.
 Additionally,
 "X" may represent an amino group, a hydrophobic group, including but not
 limited to carbobenzoxyl, dansyl, or T-butyloxycarbonyl; an acetyl group;
 a 9-fluorenylmethoxy-carbonyl (FMOC) group; a macromolecular carrier group
 including but not limited to lipid-fatty acid conjugates, polyethylene
 glycol, or carbohydrates.
 "Z" may represent a carboxyl group; an amido group; a T-butyloxycarbonyl
 group; a macromolecular carrier group including but not limited to
 lipid-fatty acid conjugates, polyethylene glycol, or carbohydrates.
 5.4. Synthesis of Peptides
 The peptides of the invention may be synthesized or prepared by techniques
 well known in the art. See, for example, Creighton, 1983, Proteins:
 Structures and Molecular Principles, W.H. Freeman and Co., NY, which is
 incorporated herein by reference in its entirety. Short peptides, for
 example, can be synthesized on a solid support or in solution. Longer
 peptides may be made using recombinant DNA techniques. Here, the
 nucleotide sequences encoding the peptides of the invention may be
 synthesized, and/or cloned, and expressed according to techniques well
 known to those of ordinary skill in the art. See, for example, Sambrook,
 et al., 1989, Molecular Cloning, A Laboratory Manual, Vols. 1-3, Cold
 Spring Harbor Press, N.Y.
 The peptides of the invention may alternatively be synthesized such that
 one or more of the bonds which link the amino acid residues of the
 peptides are non-peptide bonds. These alternative non-peptide bonds may be
 formed by utilizing reactions well known to those in the art, and may
 include, but are not limited to imino, ester, hydrazide, semicarbazide,
 and azo bonds, to name but a few. In yet another embodiment of the
 invention, peptides comprising the sequences described above may be
 synthesized with additional chemical groups present at their amino and/or
 carboxy termini, such that, for example, the stability, bioavailability,
 and/or inhibitory activity of the peptides is enhanced. For example,
 hydrophobic groups such as carbobenzoxyl, dansyl, or t-butyloxycarbonyl
 groups, may be added to the peptides' amino termini. Likewise, an acetyl
 group or a 9-fluorenylmethoxy-carbonyl group may be placed at the
 peptides' amino termini. (See "X" in Tables I to IV, above.) Additionally,
 the hydrophobic group, t-butyloxycarbonyl, or an amido group may be added
 to the peptides' carboxy termini. (See "Z" in Tables I to IV, above.)
 Further, the peptides of the invention may be synthesized such that their
 steric configuration is altered. For example, the D-isomer of one or more
 of the amino acid residues of the peptide may be used, rather than the
 usual L-isomer.
 Still further, at least one of the amino acid residues of the peptides of
 the invention may be substituted by one of the well known non-naturally
 occurring amino acid residues. Alterations such as these may serve to
 increase the stability, bioavailability and/or inhibitory action of the
 peptides of the invention.
 Any of the peptides described above may, additionally, have a
 macromolecular carrier group covalently attached to their amino and/or
 carboxy termini. Such macromolecular carrier groups may include, for
 example, lipid-fatty acid conjugates, polyethylene glycol, carbohydrates
 or additional peptides. "X", in Tables I to IV, above, may therefore
 additionally represent any of the above macromolecular carrier groups
 covalently attached to the amino terminus of a peptide, with an additional
 peptide group being preferred. Likewise, "Z", in Tables I to IV, may
 additionally represent any of the macromolecular carrier groups described
 above.
 5.5. Assays for Anti-Membrane Fusion Activity
 Described herein, are methods for ability of a compound, such as the
 peptides of the invention, to inhibit membrane fusion events.
 Specifically, assays for cell fusion events are described in Section
 5.5.1, below, and assays for antiviral activity are described in Section
 5.5.2, below.
 5.5.1 Assays for Cell Fusion Events
 Assays for cell fusion events are well known to those of skill in the art,
 and may be used in conjunction, for example, with the peptides of the
 invention to test the peptides' antifusogenic capabilities.
 Cell fusion assays are generally performed in vitro. Such an assay may
 comprise culturing cells which, in the absence of any treatment would
 undergo an observable level of syncytial formation. For example,
 uninfected cells may be incubated in the presence of cells chronically
 infected with a virus that induces cell fusion. Such viruses may include,
 but are not limited to, HIV, SIV, or respiratory syncytial virus.
 For the assay, cells are incubated in the presence of a peptide to be
 assayed. For each peptide, a range of peptide concentrations may be
 tested. This range should include a control culture wherein no peptide has
 been added.
 Standard conditions for culturing cells, well known to those of ordinary
 skill in the art, are used. After incubation for an appropriate period (24
 hours at 37.degree. C., for example) the culture is examined
 microscopically for the presence of multinucleated giant cells, which are
 indicative of cell fusion and syncytial formation. Well known stains, such
 as crystal violet stain, may be used to facilitate the visualization of
 syncytial formation.
 5.5.2 Assays for Antiviral Activity
 The antiviral activity exhibited by the peptides of the invention may be
 measured, for example, by easily performed in vitro assays, such as those
 described below, which can test the peptides' ability to inhibit syncytia
 formation, or their ability to inhibit infection by cell-free virus. Using
 these assays, such parameters as the relative antiviral activity of the
 peptides, exhibit against a given strain of virus and/or the strain
 specific inhibitory activity of the peptide can be determined.
 A cell fusion assay may be utilized to test the peptides' ability to
 inhibit viral-induced, such as HIV-induced, syncytia formation in vitro.
 Such an assay may comprise culturing uninfected cells in the presence of
 cells chronically infected with a syncytial-inducing virus and a peptide
 to be assayed. For each peptide, a range of peptide concentrations may be
 tested. This range should include a control culture wherein no peptide has
 been added. Standard conditions for culturing, well known to those of
 ordinary skill in the art, are used. After incubation for an appropriate
 period (24 hours at 37.degree. C., for example) the culture is examined
 microscopically for the presence of multinucleated giant cells, which are
 indicative of cell fusion and syncytia formation. Well known stains, such
 as crystal violet stain, may be used to facilitate syncytial
 visualization. Taking HIV as an example, such an assay would comprise
 CD-4.sup.+ cells (such as Molt or CEM cells, for example) cultured in the
 presence of chronically HIV-infected cells and a peptide to be assayed.
 Other well known characteristics of viral infection may also be assayed to
 test a peptide's antiviral capabilities. Once again taking HIV as an
 example, a reverse transcriptase (RT) assay may be utilized to test the
 peptides' ability to inhibit infection of CD-4.sup.+ cells by cell-free
 HIV. Such an assay may comprise culturing an appropriate concentration
 (i.e., TCID.sub.50) of virus and CD-4.sup.+ cells in the presence of the
 peptide to be tested. Culture conditions well known to those in the art
 are used. As above, a range of peptide concentrations may be used, in
 addition to a control culture wherein no peptide has been added. After
 incubation for an appropriate period (e.g., 7 days) of culturing, a
 cell-free supernatant is prepared, using standard procedures, and tested
 for the present of RT activity as a measure of successful infection. The
 RT activity may be tested using standard techniques such as those
 described by, for example, Goff et al. (Goff, S. et al., 1981, J. Virol.
 38:239-248) and/or Willey et al. (Willey, R. et al., 1988, J. Virol.
 62:139-147). These references are incorporated herein by reference in
 their entirety.
 Standard methods which are well-known to those of skill in the art may be
 utilized for assaying non-retroviral activity. See, for example, Pringle
 et al. (Pringle, C. R. et al., 1985, J. Medical Virology 17:377-386) for a
 discussion of respiratory syncytial virus and parainfluenza virus activity
 assay techniques. Further, see, for example, "Zinsser Microbiology", 1988,
 Joklik, W. K. et al., eds., Appleton & Lange, Norwalk, Conn., 19th ed.,
 for a general review of such techniques. These references are incorporated
 by reference herein in their entirety. In addition, the Examples presented
 below, in Sections 17, 18, 26 and 27 each provide additional assays for
 the testing of a compound's antiviral capability.
 In vivo assays may also be utilized to test, for example, the antiviral
 activity of the peptides of the invention. To test for anti-HIV activity,
 for example, the in vivo model described in Barnett et al. (Barnett, S. W.
 et al., 1994, Science 266:642-646) may be used.
 Additionally, anti-RSV activity can be assayed in vivo via well known mouse
 models. For example, RSV can be administered intranasally to mice of
 various inbred strains. Virus replicates in lungs of all strains, but the
 highest titers are obtained in P/N, C57L/N and DBA/2N mice. Infection of
 BALB/c mice produces an asymptomatic bronchiolitis characterized by
 lymphocytic infiltrates and pulmonary virus titers of 10.sup.4 to 10.sup.5
 pfu/g of lung tissue (Taylor, G. et al., 1984, Infect. Immun. 43:649-655).
 Cotton rat models of RSV are also well known. Virus replicates to high
 titer in the nose and lungs of the cotton rat but produces few if any
 signs of inflammation.
 5.6. Uses of the Peptides of the Invention
 The peptides of the invention may be utilized as antifusogenic or antiviral
 compounds, or as compounds which modulate intracellular processes
 involving coiled coil peptide structures. Further, such peptides may be
 used to identify agents which exhibit antifusogenic, antiviral or
 intracellular modulatory activity. Still further, the peptides of the
 invention may be utilized as organism or viral type/subtype-specific
 diagnostic tools.
 The antifusogenic capability of the peptides of the invention may
 additionally be utilized to inhibit or treat/ameliorate symptoms caused by
 processes involving membrane fusion events. Such events may include, for
 example, virus transmission via cell-cell fusion, abnormal
 neurotransmitter exchange via cell-fusion, and sperm-egg fusion. Further,
 the peptides of the invention may be used to inhibit free viral, such as
 retroviral, particularly HIV, transmission to uninfected cells wherein
 such viral infection involves membrane fusion events or involves fusion of
 a viral structure with a cell membrane. Among the intracellular disorders
 involving coiled coil peptides structures which may be ameliorated by the
 peptides of the invention are disorders involving, for example, bacterial
 toxins.
 With respect to antiviral activity, the viruses whose transmission may be
 inhibited by the peptides of the invention include, but are not limited to
 all strains of the viruses listed above, in Tables V through VII, and IX
 through XIV.
 These viruses include, for example, human retroviruses, particularly HIV-1
 and HIV-2 and the human T-lymphocyte viruses (HTLV-I and II). The
 non-human retroviruses whose transmission may be inhibited by the peptides
 of the invention include, but are not limited to bovine leukosis virus,
 feline sarcoma and leukemia viruses, simian immunodeficiency, sarcoma and
 leukemia viruses, and sheep progress pneumonia viruses.
 Non retroviral viruses whose transmission may be inhibited by the peptides
 of the invention include, but are not limited to human respiratory
 syncytial virus, canine distemper virus, newcastle disease virus, human
 parainfluenza virus, influenza viruses, measles viruses, Epstein-Barr
 viruses, hepatitis B viruses, and simian Mason-Pfizer viruses.
 Non enveloped viruses whose transmission may be inhibited by the peptides
 of the invention include, but are not limited to picornaviruses such as
 polio viruses, hepatitis A virus, enterovirus, echoviruses and coxsackie
 viruses, papovaviruses such as papilloma virus, parvoviruses, adenoviruses
 and reoviruses.
 As discussed more fully, below, in Section 5.5.1 and in the Example
 presented, below, in Section 8, DP107, DP178, DP107 analog and DP178
 analog peptides form non-covalent protein-protein interactions which are
 required for normal activity of the virus. Thus, the peptides of the
 invention may also be utilized as components in assays for the
 identification of compounds that interfere with such protein-protein
 interactions and may, therefore, act as antiviral agents. These assays are
 discussed, below, in Section 5.5.1.
 As demonstrated in the Example presented below in Section 6, the antiviral
 activity of the peptides of the invention may show a pronounced type and
 subtype specificity, i.e., specific peptides may be effective in
 inhibiting the activity of only specific viruses. This feature of the
 invention presents many advantages. One such advantage, for example, lies
 in the field of diagnostics, wherein one can use the antiviral specificity
 of the peptide of the invention to ascertain the identity of a viral
 isolate. With respect to HIV, one may easily determine whether a viral
 isolate consists of an HIV-1 or HIV-2 strain. For example, uninfected
 CD-4.sup.+ cells may be co-infected with an isolate which has been
 identified as containing HIV the DP178 (SEQ ID NO:1) peptide, after which
 the retroviral activity of cell supernatants may be assayed, using, for
 example, the techniques described above in Section 5.2. Those isolates
 whose retroviral activity is completely or nearly completely inhibited
 contain HIV-1. Those isolates whose viral activity is unchanged or only
 reduced by a small amount, may be considered to not contain HIV-1. Such an
 isolate may then be treated with one or more of the other DP178 peptides
 of the invention, and subsequently be tested for its viral activity in
 order to determine the identify of the viral isolate. The DP107 and DP178
 analogs of the invention may also be utilized in a diagnostic capacity
 specific to the type and subtype of virus or organism in which the
 specific peptide sequence is found. A diagnostic procedure as described,
 above, for DP178, may be used in conjunction with the DP107/DP178 analog
 of interest.
 5.5.1. Screening Assays
 As demonstrated in the Example presented in Section 8, below, DP107 and
 DP178 portions of the TM protein gp41 form non-covalent protein-protein
 interactions. As is also demonstrated, the maintenance of such
 interactions is necessary for normal viral infectivity. Thus, compounds
 which bind DP107, bind DP178, and/or act to disrupt normal DP107/DP178
 protein-protein interactions may act as antifusogenic, antiviral or
 cellular modulatory agents. Described below are assays for the
 identification of such compounds. Note that, while, for ease and clarity
 of discussion, DP107 and DP178 peptides will be used as components of the
 assays described, but it is to be understood that any of the DP107 analog
 or DP178 analog peptides described, above, in Sections 5.1 through 5.3 may
 also be utilized as part of these screens for compounds.
 Compounds which may be tested for an ability to bind DP107, DP178, and/or
 disrupt DP107/DP178 interactions, and which therefore, potentially
 represent antifusogenic, antiviral or intracellular modulatory compounds,
 include, but are not limited to, peptides made of D- and/or
 L-configuration amino acids (in, for example, the form of random peptide
 libraries; see Lam, K. S. et al., 1991, Nature 354:82-84), phosphopeptides
 (in, for example, the form of random or partially degenerate, directed
 phosphopeptide libraries; see, for example, Songyang, Z. et al., 1993,
 Cell 72:767-778), antibodies, and small organic or inorganic molecules.
 Synthetic compounds, natural products, and other sources of potentially
 effective materials may be screened in a variety of ways, as described in
 this Section.
 The compounds, antibodies, or other molecules identified may be tested, for
 example, for an ability to inhibit cell fusion or viral activity,
 utilizing, for example, assays such as those described, above, in Section
 5.5.
 Among the peptides which may be tested are soluble peptides comprising
 DP107 and/or DP178 domains, and peptides comprising DP107 and/or DP178
 domains having one or more mutations within one or both of the domains,
 such as the M41-P peptide described, below, in the Example presented in
 Section 8, which contains a isoleucine to proline mutation within the
 DP178 sequence.
 In one embodiment of such screening methods is a method for identifying a
 compound to be tested for antiviral ability comprising:
 (a) exposing at least one compound to a peptide comprising a DP107 peptide
 for a time sufficient to allow binding of the compound to the DP107
 peptide;
 (b) removing non-bound compounds; and
 (c) determining the presence of the compound bound to the DP107 peptide,
 thereby identifying an agent to be tested for antiviral ability.
 In a second embodiment of such screening methods is a method for
 identifying a compound to be tested for antiviral ability comprising:
 (a) exposing at least one compound to a peptide comprising a DP178 peptide
 for a time sufficient to allow binding of the compound to the DP178
 peptide;
 (b) removing non-bound compounds; and
 (c) determining the presence of the compound bound to the DP178 peptide,
 thereby identifying an agent to be tested for antiviral ability.
 One method utilizing these types of approaches that may be pursued in the
 isolation of such DP107-binding or DP178-binding compounds is an assay
 which would include the attachment of either the DP107 or the DP178
 peptide to a solid matrix, such as, for example, agarose or plastic beads,
 microtiter plate wells, petri dishes, or membranes composed of, for
 example, nylon or nitrocellulose. In such an assay system, either the
 DP107 or DP178 protein may be anchored onto a solid surface, and the
 compound, or test substance, which is not anchored, is labeled, either
 directly or indirectly. In practice, microtiter plates are conveniently
 utilized. The anchored component may be immobilized by non-covalent or
 covalent attachments. Non-covalent attachment may be accomplished simply
 by coating the solid surface with a solution of the protein and drying.
 Alternatively, an immobilized antibody, preferably a monoclonal antibody,
 specific for the protein may be used to anchor the protein to the solid
 surface. The surfaces may be prepared in advance and stored.
 In order to conduct the assay, the labeled compound is added to the coated
 surface containing the anchored DP107 or DP178 peptide. After the reaction
 is complete, unreacted components are removed (e.g., by washing) under
 conditions such that any complexes formed will remain immobilized on the
 solid surface. The detection of complexes anchored on the solid surface
 can be accomplished in a number of ways. Where the compound is
 pre-labeled, the detection of label immobilized on the surface indicates
 that complexes were formed. Where the labeled component is not
 pre-labeled, an indirect label can be used to detect complexes anchored on
 the surface; e.g., using a labeled antibody specific for the compound (the
 antibody, in turn, may be directly labeled or indirectly labeled with a
 labeled anti-Ig antibody).
 Alternatively, such an assay can be conducted in a liquid phase, the
 reaction products separated from unreacted components, and complexes
 detected; e.g., using an immobilized antibody specific for DP107 or DP178,
 whichever is appropriate for the given assay, or ab antibody specific for
 the compound, i.e., the test substance, in order to anchor any complexes
 formed in solution, and a labeled antibody specific for the other member
 of the complex to detect anchored complexes.
 By utilizing procedures such as this, large numbers of types of molecules
 may be simultaneously screened for DP107 or DP178-binding capability, and
 thus potential antiviral activity.
 Further, compounds may be screened for an ability to inhibit the formation
 of or, alternatively, disrupt DP107/DP178 complexes. Such compounds may
 then be tested for antifusogenic, antiviral or intercellular modulatory
 capability. For ease of description, DP107 and DP178 will be referred to
 as "binding partners." Compounds that disrupt such interactions may
 exhibit antiviral activity. Such compounds may include, but are not
 limited to molecules such as antibodies, peptides, and the like described
 above.
 The basic principle of the assay systems used to identify compounds that
 interfere with the interaction between the DP107 and DP178 peptides
 involves preparing a reaction mixture containing peptides under conditions
 and for a time sufficient to allow the two peptides to interact and bind,
 thus forming a complex. In order to test a compound for disruptive
 activity, the reaction is conducted in the presence and absence of the
 test compound, i.e., the test compound may be initially included in the
 reaction mixture, or added at a time subsequent to the addition of one of
 the binding partners; controls are incubated without the test compound or
 with a placebo. The formation of any complexes between the binding
 partners is then detected. The formation of a complex in the control
 reaction, but not in the reaction mixture containing the test compound
 indicates that the compound interferes with the interaction of the DP107
 and DP178 peptides.
 The assay for compounds that interfere with the interaction of the binding
 partners can be conducted in a heterogeneous or homogeneous format.
 Heterogeneous assays involve anchoring one of the binding partners onto a
 solid phase and detecting complexes anchored on the solid phase at the end
 of the reaction. In homogeneous assays, the entire reaction is carried out
 in a liquid phase. In either approach, the order of addition of reactants
 can be varied to obtain different information about the compounds being
 tested. For example, test compounds that interfere with the interaction
 between the binding partners, e.g., by competition, can be identified by
 conducting the reaction in the presence of the test substance; i.e., by
 adding the test substance to the reaction mixture prior to or
 simultaneously with the binding partners. On the other hand, test
 compounds that disrupt preformed complexes, e.g. compounds with higher
 binding constants that displace one of the binding partners from the
 complex, can be tested by adding the test compound to the reaction mixture
 after complexes have been formed. The various formats are described
 briefly below.
 In a heterogeneous assay system, one binding partner, e.g., either the
 DP107 or DP178 peptide, is anchored onto a solid surface, and its binding
 partner, which is not anchored, is labeled, either directly or indirectly.
 In practice, microtiter plates are conveniently utilized. The anchored
 species may be immobilized by non-covalent or covalent attachments.
 Non-covalent attachment may be accomplished simply by coating the solid
 surface with a solution of the protein and drying. Alternatively, an
 immobilized antibody specific for the protein may be used to anchor the
 protein to the solid surface. The surfaces may be prepared in advance and
 stored.
 In order to conduct the assay, the binding partner of the immobilized
 species is added to the coated surface with or without the test compound.
 After the reaction is complete, unreacted components are removed (e.g., by
 washing) and any complexes formed will remain immobilized on the solid
 surface. The detection of complexes anchored on the solid surface can be
 accomplished in a number of ways. Where the binding partner was
 pre-labeled, the detection of label immobilized on the surface indicates
 that complexes were formed. Where the binding partner is not pre-labeled,
 an indirect label can be used to detect complexes anchored on the surface;
 e.g., using a labeled antibody specific for the binding partner (the
 antibody, in turn, may be directly labeled or indirectly labeled with a
 labeled anti-Ig antibody). Depending upon the order of addition of
 reaction components, test compounds which inhibit complex formation or
 which disrupt preformed complexes can be detected.
 Alternatively, the reaction can be conducted in a liquid phase in the
 presence or absence of the test compound, the reaction products separated
 from unreacted components, and complexes detected; e.g., using an
 immobilized antibody specific for one binding partner to anchor any
 complexes formed in solution, and a labeled antibody specific for the
 other binding partner to detect anchored complexes. Again, depending upon
 the order of addition of reactants to the liquid phase, test compounds
 which inhibit complex or which disrupt preformed complexes can be
 identified.
 In an alternate embodiment of the invention, a homogeneous assay can be
 used. In this approach, a preformed complex of the DP107 and DP178
 peptides is prepared in which one of the binding partners is labeled, but
 the signal generated by the label is quenched due to complex formation
 (see, e.g., U.S. Pat. No. 4,109,496 by Rubenstein which utilizes this
 approach for immunoassays). The addition of a test substance that competes
 with and displaces one of the binding partners from the preformed complex
 will result in the generation of a signal above background. In this way,
 test substances which disrupt DP-107/DP-178 protein-protein interaction
 can be identified.
 In an alternative screening assay, test compounds may be assayed for the
 their ability to disrupt a DP178/DP107 interaction, as measured
 immunometrically using an antibody specifically reactive to a DP107/DP178
 complex (i.e., an antibody that recognizes neither DP107 nor DP178
 individually). Such an assay acts as a competition assay, and is based on
 techniques well known to those of skill in the art.
 The above competition assay may be described, by way of example, and not by
 way of limitation, by using the DP178 and M41.DELTA.178 peptides and by
 assaying test compounds for the disruption of the complexes formed by
 these two peptides by immunometrically visualizing DP178/M41.DELTA.78
 complexes via the human recombinant Fab, Fab-d, as described, below, in
 the Example presented in Section 8. M41.DELTA.178 is a maltose binding
 fusion protein containing a gp41 region having its DP178 domain deleted,
 and is described, below, in the Example presented in Section 8.
 Utilizing such an assay, M41.DELTA.178 may be immobilized onto solid
 supports such as microtiter wells. A series of dilutions of a test
 compound may then be added to each M41.DELTA.178-containing well in the
 presence of a constant concentration of DP-178 peptide. After incubation,
 at, for example, room temperature for one hour, unbound DP-178 and test
 compound are removed from the wells and wells are then incubated with the
 DP178/M41.DELTA.178-specific Fab-d antibody. After incubation and washing,
 unbound Fab-d is removed from the plates and bound Fab-d is quantitated. A
 no-inhibitor control should also be conducted. Test compounds showing an
 ability to disrupt DP178/M41.DELTA.178 complex formation are identified by
 their concentration-dependent decrease in the level of Fab-d binding.
 A variation of such an assay may be utilized to perform a rapid,
 high-throughput binding assay which is capable of directly measuring DP178
 binding to M41.DELTA.178 for the determination of binding constants of the
 ligand of inhibitory constants for competitors of DP178 binding.
 Such an assay takes advantage of accepted radioligand and receptor binding
 principles. (See, for example, Yamamura, H. I. et al., 1985,
 "Neurotransmitter Receptor Binding", 2nd ed., Raven Press, NY.) As above,
 M41.DELTA.178 is immobilized onto a solid support such as a microtiter
 well. DP178 binding to M41.DELTA.178 is then quantitated by measuring the
 fraction of DP178 that is bound as .sup.125 I-DP178 and calculating the
 total amount bound using a value for specific activity (dpm/.mu.g peptide)
 determined for each labeled DP178 preparation. Specific binding to
 M41.DELTA.178 is defined as the difference of the binding of the labeled
 DP178 preparation in the microtiter wells (totals) and the binding in
 identical wells containing, in addition, excess unlabeled DP178
 (nonspecifics).
 5.5 Pharmaceutical Formulations, Dosages and Modes of Administration
 The peptides of the invention may be administered using techniques well
 known to those in the art. Preferably, agents are formulated and
 administered systemically. Techniques for formulation and administration
 may be found in "Remington's Pharmaceutical Sciences", 18th ed., 1990,
 Mack Publishing Co., Easton, Pa. Suitable routes may 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, just to name a few. For injection,
 the agents of the invention may be formulated in aqueous solutions,
 preferably in physiologically compatible buffers such as Hanks' solution,
 Ringer's solution, or physiological saline buffer. For such transmucosal
 administration, penetrants appropriate to the barrier to be permeated are
 used in the formulation. Such penetrants are generally known in the art.
 In instances wherein intracellular administration of the peptides of the
 invention or other inhibitory agents is preferred, techniques well known
 to those of ordinary skill in the art may be utilized. For example, such
 agents may be encapsulated into liposomes, then administered as described
 above. Liposomes are spherical lipid bilayers with aqueous interiors. All
 molecules present in an aqueous solution at the time of liposome formation
 are incorporated into the aqueous interior. The liposomal contents are
 both protected from the external microenvironment and, because liposomes
 fuse with cell membranes, are effectively delivered into the cell
 cytoplasm. Additionally, due to their hydrophobicity, when small molecules
 are to be administered, direct intracellular administration may be
 achieved.
 Nucleotide sequences encoding the peptides of the invention which are to be
 intracellularly administered may be expressed in cells of interest, using
 techniques well known to those of skill in the art. For example,
 expression vectors derived from viruses such as retroviruses, vaccinia
 viruses, adeno-associated viruses, herpes viruses, or bovine papilloma
 viruses, may be used for delivery and expression of such nucleotide
 sequences into the targeted cell population. Methods for the construction
 of such vectors and expression constructs are well known. See, for
 example, Sambrook et al., 1989, Molecular Cloning, A Laboratory Manual,
 Cold Spring Harbor Press, Cold Spring Harbor N.Y., and Ausubel et al.,
 1989, Current Protocols in Molecular Biology, Greene Publishing Associates
 and Wiley Interscience, NY.
 With respect to HIV, peptides of the invention, particularly DP107 and
 DP178, may be used as therapeutics in the treatment of AIDS. In addition,
 the peptides may be used as prophylactic measures in previously uninfected
 individuals after acute exposure to an HIV virus. Examples of such
 prophylactic use of the peptides may include, but are not limited to,
 prevention of virus transmission from mother to infant and other settings
 where the likelihood of HIV transmission exists, such as, for example,
 accidents in health care settings wherein workers are exposed to
 HIV-containing blood products. The successful use of such treatments do
 not rely upon the generation of a host immune response directed against
 such peptides.
 Effective dosages of the peptides of the invention to be administered may
 be determined through procedures well known to those in the art which
 address such parameters as biological half-life, bioavailability, and
 toxicity. Given the data presented below in Section 6, DP178, for example,
 may prove efficacious in vivo at doses required to achieve circulating
 levels of about 1 to about 10 ng per ml of peptide.
 A therapeutically effective dose refers to that amount of the compound
 sufficient to result 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.sub.50 (the dose
 lethal to 50% of the population) and the ED50 (the dose therapeutically
 effective in 50% of the population). The dose ratio between toxic and
 therapeutic effects is the therapeutic index and it can be expressed as
 the ratio LD.sub.50 /ED.sub.50. Compounds which exhibit large 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
 humans. The dosage of such compounds lies preferably within a range of
 circulating concentrations that include the ED50 with little or no
 toxicity. The dosage may vary within this range depending upon the dosage
 form employed and the route of administration utilized. For any compound
 used in the method of the invention, the therapeutically effective dose
 can be estimated initially from cell culture assays. A dose may be
 formulated in animal models to achieve a circulating plasma concentration
 range that includes the IC.sub.50 (e.g., the concentration of the test
 compound which achieves a half-maximal inhibition of the fusogenic event,
 such as a half-maximal inhibition of viral infection relative to the
 amount of the event in the absence of the test compound) as determined in
 cell culture. Such information can be used to more accurately determine
 useful doses in humans. Levels in plasma may be measured, for example, by
 high performance liquid chromatography (HPLC).
 The peptides of the invention may, further, serve the role of a
 prophylactic vaccine, wherein the host raises antibodies against the
 peptides of the invention, which then serve to neutralize HIV viruses by,
 for example, inhibiting further HIV infection.
 Administration of the peptides of the invention as a prophylactic vaccine,
 therefore, would comprise administering to a host a concentration of
 peptides effective in raising an immune response which is sufficient to
 neutralize HIV, by, for example, inhibiting HIV ability to infect cells.
 The exact concentration will depend upon the specific peptide to be
 administered, but may be determined by using standard techniques for
 assaying the development of an immune response which are well known to
 those of ordinary skill in the art. The peptides to be used as vaccines
 are usually administered intramuscularly.
 The peptides may be formulated with a suitable adjuvant in order to enhance
 the immunological response. Such adjuvants may include, but are not
 limited to mineral gels such as aluminum hydroxide; surface active
 substances such as lysolecithin, pluronic polyols, polyanions; other
 peptides; oil emulsions; and potentially useful human adjuvants such as
 BCG and Corynebacterium parvum. Many methods may be used to introduce the
 vaccine formulations described here. These methods include but are not
 limited to oral, intradermal, intramuscular, intraperitoneal, intravenous,
 subcutaneous, and intranasal routes.
 Alternatively, an effective concentration of polyclonal or monoclonal
 antibodies raised against the peptides of the invention may be
 administered to a host so that no uninfected cells become infected by HIV.
 The exact concentration of such antibodies will vary according to each
 specific antibody preparation, but may be determined using standard
 techniques well known to those of ordinary skill in the art.
 Administration of the antibodies may be accomplished using a variety of
 techniques, including, but not limited to those described in this section.
 For all such treatments described above, the exact formulation, route of
 administration and dosage can be chosen by the individual physician in
 view of the patient's condition. (See e.g. Fingl et al., 1975, in "The
 Pharmacological Basis of Therapeutics", Ch. 1 p1).
 It should be noted that the attending physician would know how to and when
 to terminate, interrupt, or adjust administration due to toxicity, or to
 organ dysfunctions. Conversely, the attending physician would also know to
 adjust treatment to higher levels if the clinical response were not
 adequate (precluding toxicity). The magnitude of an administrated dose in
 the management of the oncogenic disorder of interest will vary with the
 severity of the condition to be treated and the route of administration.
 The dose and perhaps dose frequency, will also vary according to the age,
 body weight, and response of the individual patient. A program comparable
 to that discussed above may be used in veterinary medicine.
 Use of pharmaceutically acceptable carriers to formulate the compounds
 herein disclosed for the practice of the invention into dosages suitable
 for systemic administration is within the scope of the invention. With
 proper choice of carrier and suitable manufacturing practice, the
 compositions of the present invention, in particular, those formulated as
 solutions, may be administered parenterally, such as by intravenous
 injection. The compounds can be formulated readily using pharmaceutically
 acceptable carriers well known in the art into dosages suitable for oral
 administration. Such carriers enable the compounds of the invention to be
 formulated as tablets, pills, capsules, liquids, gels, syrups, slurries,
 suspensions and the like, for oral ingestion by a patient to be treated.
 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. Determination of the
 effective amounts is well within the capability of those skilled in the
 art, especially in light of the detailed disclosure provided herein.
 In addition to the active ingredients, these pharmaceutical compositions
 may contain suitable pharmaceutically acceptable carriers comprising
 excipients and auxiliaries which facilitate processing of the active
 compounds into preparations which can be used pharmaceutically. The
 preparations formulated for oral administration may be in the form of
 tablets, dragees, capsules, or solutions.
 The pharmaceutical compositions of the present invention may be
 manufactured in a manner that is itself known, e.q., by means of
 conventional mixing, dissolving, granulating, dragee-making, levigating,
 emulsifying, encapsulating, entrapping or lyophilizing processes.
 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.
 Pharmaceutical preparations for oral use can be obtained by combining the
 active compounds with 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.
 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
 oi.ls, liquid paraffin, or liquid polyethylene glycols. In addition,
 stabilizers may be added.
 6. EXAMPLE: DP178 (SEQ ID NO:1) IS A POTENT INHIBITOR OF HIV-1 INFECTION
 In this example, DP178 (SEQ ID NO:1) is shown to be a potent inhibitor of
 HIV-1 mediated CD-4.sup.+ cell-cell fusion and infection by cell free
 virus. In the fusion assay, this peptide completely blocks virus induced
 syncytia formation at concentrations of from 1-10 ng/ml. In the
 infectivity assay the inhibitory concentration is somewhat higher,
 blocking infection at 90 ng/ml. It is further shown that DP178 (SEQ ID
 NO:1) shows that the antiviral activity of DP178 (SEQ ID NO:1) is highly
 specific for HIV-1. Additionally, a synthetic peptide, DP-185 (SEQ ID
 NO:3), representing a HIV-1-derived DP178 homolog is also found to block
 HIV-1-mediated syncytia formation.
 6.1. Materials and Methods
 6.1.1. Peptide Synthesis
 Peptides were synthesized using Fast Moc chemistry on an Applied Biosystems
 Model 431A peptide synthesizer. Generally, unless otherwise noted, the
 peptides contained amidated carboxy termini and acetylated amino termini.
 Amidated peptides were prepared using Rink resin (Advanced Chemtech) while
 peptides containing free carboxy termini were synthesized on Wang
 (p-alkoxy-benzyl-alcohol) resin (Bachem). First residues were double
 coupled to the appropriate resin and subsequent residues were single
 coupled. Each coupling step was followed by acetic anhydride capping.
 Peptides were cleaved from the resin by treatment with trifluoracetic acid
 (TFA) (10 ml), H.sub.2 O (0.5 ml), thioanisole (0.5 ml), ethanedithiol
 (0.25 ml), and crystalline phenol (0.75 g). Purification was carried out
 by reverse phase HPLC. Approximately 50 mg samples of crude peptide were
 chromatographed on a Waters Delta Pak C18 column (19 mm.times.30 cm,
 15.mu. spherical) with a linear gradient; H.sub.2 O/acetonitrile 0.1% TFA.
 Lyophilized peptides were stored desiccated and peptide solutions were
 made in water at about 1 mg/ml. Electrospray mass spectrometry yielded the
 following results: DP178 (SEQ ID NO:1):4491.87 (calculated 4491.94);
 DP-180 (SEQ ID NO:2):4491.45 (calculated 4491.94); DP-185 (SEQ ID
 NO:3):not done (calculated 4546.97).
 6.1.2. VIRUS
 The HIV-1.sub.LAI virus was obtained from R. Gallo (Popovic, M. et al.,
 1984, Science 224:497-508) and propagated in CEM cells cultured in RPMI
 1640 containing 10% fetal calf serum. Supernatant from the infected CEM
 cells was passed through a 0.2 .mu.m filter and the infectious titer
 estimated in a microinfectivity assay using the AA5 cell line to support
 virus replication. For this purpose, 25 .mu.l of serial diluted virus was
 added to 75 .mu.l AA5 cells at a concentration of 2.times.10.sup.5 /ml in
 a 96-well microtitre plate. Each virus dilution was tested in triplicate.
 Cells were cultured for eight days by addition of fresh medium every other
 day. On day 8 post infection, supernatant samples were tested for virus
 replication as evidenced by reverse transcriptase activity released to the
 supernatant. The TCID.sub.50 was calculated according to the Reed and
 Muench formula (Reed, L. J. et al., 1938, Am. J. Hyg. 27:493-497). The
 titer of the HIV-1.sub.LAI and HIV-1.sub.MN stocks used for these studies,
 as measured on the AA5 cell line, was approximately 1.4.times.10.sup.6 and
 3.8.times.10.sup.4 TCID.sub.50 /ml, respectively.
 6.1.3. Cell Fusion Assay
 Approximately 7.times.10.sup.4 Molt cells were incubated with
 1.times.10.sup.4 CEM cells chronically infected with the HIV-1.sub.LAI
 virus in 96-well plates (one-half area cluster plates; Costar, Cambridge,
 Mass.) in a final volume of 100 .mu.l culture medium as previously
 described (Matthews, T. J. et al., 1987, Proc. Natl. Acad. Sci. USA 84:
 5424-5428). Peptide inhibitors were added in a volume of 10 .mu.l and the
 cell mixtures were incubated for 24 hr. at 37.degree. C. At that time,
 multinucleated giant cells were estimated by microscopic examination at a
 40.times.magnification which allowed visualization of the entire well in a
 single field.
 6.1.4. Cell Free Virus Infection Assay
 Synthetic peptides were incubated at 37.degree. C. with either 247
 TCID.sub.50 (for experiment depicted in FIG. 2), or 62 TCID.sub.50 (for
 experiment depicted in FIG.3) units of HIV-1.sub.LAI virus or 25
 TCID.sub.50 units of HIV-2.sub.NIHZ and CEM CD4.sup.+ cells at peptide
 concentrations of 0, 0.04, 0.4, 4.0, and 40 .mu.g/ml for 7 days. The
 resulting reverse transcriptase (RT) activity in counts per minute was
 determined using the assay described, below, in Section 6.1.5. See, Reed,
 L. J. et al., 1938, Am. J. Hyg. 27: 493-497 for an explanation of
 TCID.sub.50 calculations.
 6.1.5. Reverse Transcriptase Assay
 The micro-reverse transcriptase (RT) assay was adapted from Goff et al.
 (Goff, S. et al., 1981, J. Virol. 38:239-248) and Willey et al. (Willey,
 R. et al., 1988, J. Virol. 62:139-147). Supernatants from virus/cell
 cultures are adjusted to 1% Triton-X100. A 10 .mu.l sample of supernatant
 was added to 50 .mu.l of RT cocktail in a 96-well U-bottom microtitre
 plate and the samples incubated at 37.degree. C. for 90 min. The RT
 cocktail contained 75 mM KCl, 2 mM dithiothreitol, 5 mM MgCl.sub.2, 5
 .mu.g/ml poly A (Pharmacia, cat. No. 27-4110-01), 0.25 units/ml oligo dT
 (Pharmacia, cat. No. 27-7858-01), 0.05% NP40, 50 mM Tris-HCl, pH 7.8, 0.5
 .mu.M non-radioactive dTTP, and 10 .mu.Ci/ml .sup.32 P-dTTP (Amersham,
 cat. No. PB.10167).
 After the incubation period, 40 .mu.l of reaction mixture was applied to a
 Schleicher and Schuell (S+S) NA45 membrane (or DE81 paper) saturated in
 2.times.SSC buffer (0.3M NaCl and 0.003M sodium citrate) held in a S+S
 Minifold over one sheet of GBOO3 (S+S) filter paper, with partial vacuum
 applied. Each well of the minifold was washed four times with 200 .mu.l
 2.times.SSC, under full vacuum. The membrane was removed from the minifold
 and washed 2 more times in a pyrex dish with an excess of 2.times.SSC.
 Finally, the membrane was drained on absorbent paper, placed on Whatman #3
 paper, covered with Saran wrap, and exposed to film overnight at
 -70.degree. C.
 6.2. Results
 6.2.1. Peptide Inhibition of Infected Cell-Induced Syncytia Formation
 The initial screen for antiviral activity assayed peptides' ability to
 block syncytium formation induced by overnight co-cultivation of
 uninfected Molt4 cells with chronically HIV-1 infected CEM cells. The
 results of several such experiments are presented herein. In the first of
 these experiments, serial DP178 (SEQ ID NO:1) peptide concentrations
 between 10 .mu.g/ml and 12.5 ng/ml were tested for blockade of the cell
 fusion process. For these experiments, CEM cells chronically infected with
 either HIV-1.sub.LAI, HIV-1.sub.MN, HIV-1.sub.RF, or HIV-1.sub.SF2 virus
 were cocultivated overnight with uninfected Molt 4 cells. The results
 (FIG. 4) show that DP178 (SEQ ID NO:1) afforded complete protection
 against each of the HIV-1 isolates down to the lowest concentration of
 DP178 (SEQ ID NO:1) used. For HIV.sub.LAI inhibition, the lowest
 concentration tested was 12.5 ng/ml; for all other HIV-1 viruses, the
 lowest concentration of DP178 (SEQ ID NO:1) used in this study was 100
 ng/ml. A second peptide, DP-180 (SEQ ID NO:2), containing the same amino
 acid residues as DP178 (SEQ ID NO:1) but arranged in a random order
 exhibited no evidence of anti-fusogenic activity even at the high
 concentration of 40 .mu.g/ml (FIG. 4). These observations indicate that
 the inhibitory effect of DP178 (SEQ ID NO:1) is primary sequence-specific
 and not related to non-specific peptide/protein interactions. The actual
 endpoint (i.e., the lowest effective inhibitory concentration) of DP178
 inhibitory action is within the range of 1-10 ng/ml.
 The next series of experiments involved the preparation and testing of a
 DP178 (SEQ ID NO:1) homolog for its ability to inhibit HIV-1-induced
 syncytia formation. As shown in FIG. 1, the sequence of DP-185 (SEQ ID
 NO:3) is slightly different from DP178 (SEQ ID NO:1) in that its primary
 sequence is taken from the HIV-1.sub.SF2 isolate and contains several
 amino acid differences relative to DP178 (SEQ ID NO:1) near the N
 terminus. As shown in FIG. 4, DP-185 (SEQ ID NO:3), exhibits inhibitory
 activity even at 312.5 ng/ml, the lowest concentration tested.
 The next series of experiments involved a comparison of DP178 (SEQ ID NO:1)
 HIV-1 and HIV-2 inhibitory activity. As shown in FIG. 5, DP178 (SEQ ID
 NO:1) blocked HIV-1-mediated syncytia formation at peptide concentrations
 below 1 ng/ml. DP178 (SEQ ID NO:1) failed, however, to block HIV-2
 mediated syncytia formation at concentrations as high as 10 .mu.g/ml. This
 striking 4 log selectivity of DP178 (SEQ ID NO:1) as an inhibitor of
 HIV-1-mediated cell fusion demonstrates an unexpected HIV-1 specificity in
 the action of DP178 (SEQ ID NO:1). DP178 (SEQ ID NO:1) inhibition of
 HIV-1-mediated cell fusion, but the peptide's inability to inhibit HIV-2
 medicated cell fusion in the same cell type at the concentrations tested
 provides further evidence for the high degree of selectivity associated
 with the antiviral action of DP178 (SEQ ID NO:1).
 6.2.2. Peptide Inhibition of Infection by Cell-Free Virus
 DP178 (SEQ ID NO:1) was next tested for its ability to block CD-4.sup.+ CEM
 cell infection by cell free HIV-1 virus. The results, shown in FIG. 2, are
 from an experiment in which DP178 (SEQ ID NO:1) was assayed for its
 ability to block infection of CEM cells by an HIV-1.sub.LAI isolate.
 Included in the experiment were three control peptides, DP-116 (SEQ ID
 NO:9), DP-125 (SEQ ID NO:8), and DP-118 (SEQ ID NO:10). DP-116 (SEQ ID
 NO:9) represents a peptide previously shown to be inactive using this
 assay, and DP-125 (SEQ ID NO:8; Wild, C. et al., 1992, Proc. Natl. Acad,
 Sci. USA 89:10,537) and DP-118 (SEQ ID NO:10) are peptides which have
 previously been shown to be active in this assay. Each concentration (0,
 0.04, 0.4, 4, and 40 .mu.g/ml) of peptide was incubated with 247
 TCID.sub.50 units of HIV-1.sub.LAI virus and CEM cells. After 7 days of
 culture, cell-free supernatant was tested for the presence of RT activity
 as a measure of successful infection. The results, shown in FIG. 2,
 demonstrate that DP178 (SEQ ID NO:1) inhibited the de novo infection
 process mediated by the HIV-1 viral isolate at concentrations as low as 90
 ng/ml (IC50=90 ng/ml). In contrast, the two positive control peptides,
 DP-125 (SEQ ID NO:8) and DP-118 (SEQ ID NO:10), had over 60-fold higher
 IC50 concentrations of approximately 5 .mu.g/ml.
 In a separate experiment, the HIV-1 and HIV-2 inhibitory action of DP178
 (SEQ ID NO:1) was tested with CEM cells and either HIV-1.sub.LAI or
 HIV-2.sub.NIHZ. 62 TCID.sub.50 HIV-1.sub.LAI or 25 GCID.sub.50
 HIV-2.sub.NIHZ were used in these experiments, and were incubated for 7
 days. As may be seen in FIG. 3, DP178 (SEQ ID NO:1) inhibited HIV-1
 infection with an IC50 of about 31 ng/ml. In contrast, DP178 (SEQ ID NO:1)
 exhibited a much higher IC50 for HIV-2.sub.NIHZ, thus making DP178 (SEQ ID
 NO:1) two logs more potent as a HIV-1 inhibitor than a HIV-2 inhibitor.
 This finding is consistent with the results of the fusion inhibition
 assays described, above, in Section 6.2.1, and further supports a
 significant level of selectivity (i.e., for HIV-1 over HIV-2).
 7. EXAMPLE: THE HIV-1 INHIBITOR, DP178 (SEQ ID NO:1) IS NON-CYTOTOXIC
 In this Example, the 36 amino acid synthetic peptide inhibitor DP178 (SEQ
 ID NO:1) is shown to be non-cytotoxic to cells in culture, even at the
 highest peptide concentrations (40 .mu.g/ml) tested.
 7.1. Materials and Methods
 Cell proliferation and toxicity assay: Approximately 3.8.times.10.sup.5 CEM
 cells for each peptide concentration were incubated for 3 days at
 37.degree. C. in T25 flasks. Peptides tested were DP178 (SEQ ID NO:1) and
 DP-116 (SEQ ID NO:9), as described in FIG. 1. Peptides were synthesized as
 described, above, in Section 6.1. The concentrations of each peptide used
 were 0, 2.5, 10, and 40 .mu.g/ml. Cell counts were taken at incubation
 times of 0, 24, 48, and 72 hours.
 7.2. RESULTS
 Whether the potent HIV-1 inhibitor DP178 (SEQ ID NO:1) exhibited any
 cytotoxic effects was assessed by assaying the peptide's effects on the
 proliferation and viability of cells in culture. CEM cells were incubated
 in the presence of varying concentrations of DP178 (SEQ ID NO:1), and
 DP-116 (SEQ ID NO:9), a peptide previously shown to be ineffective as a
 HIV inhibitor (Wild, C. et al., 1992, Proc. Natl. Acad. Sci. USA
 89:10,537-10,541). Additionally, cells were incubated in the absence of
 either peptide.
 The results of the cytotoxicity study demonstrate that DP178 (SEQ ID NO:1)
 exhibits no cytotoxic effects on cells in culture. As can be seen, below,
 in Table XXIV, even the proliferation and viability characteristics of
 cells cultured for 3 days in the presence of the highest concentration of
 DP178 (SEQ ID NO:1) tested (40 .mu.g/ml) do not significantly differ from
 the DP-116 (SEQ ID NO:9) or the no-peptide controls. The cell
 proliferation data is also represented in graphic form in FIG. 6. As was
 demonstrated in the Working Example presented above in Section 6, DP178
 (SEQ ID NO:1) completely inhibits HIV-1 mediated syncytia formation at
 peptide concentrations between 1 and 10 ng/ml, and completely inhibits
 cell-free viral infection at concentrations of at least 90 ng/ml. Thus,
 this study demonstrates that even at peptide concentrations greater than 3
 log higher than the HIV inhibitory dose, DP178 (SEQ ID NO:1) exhibits no
 cytotoxic effects.
 TABLE XII
 % Viability
 Peptide at time (hours)
 Peptide Concentration .mu.g/ml 0 24 48 72
 DP178 40 98 97 95 97
 (SEQ ID 10 98 97 98 98
 NO: 1) 2.5 98 93 96 96
 DP116 40 98 95 98 97
 (SEQ ID 10 98 95 93 98
 NO: 9) 2.5 98 96 98 99
 No 0 98 97 99 98
 Peptide
 8. EXAMPLE: THE INTERACTION OF DP178 AND DP107
 Soluble recombinant forms of gp41 used in the example described below
 provide evidence that the DP178 peptide associates with a distal site on
 gp41 whose interactive structure is influenced by the DP107 leucine zipper
 motif. A single mutation disrupting the coiled-coil structure of the
 leucine zipper domain transformed the soluble recombinant gp41 protein
 from an inactive to an active inhibitor of HIV-1 fusion. This
 transformation may result from liberation of the potent DP178 domain from
 a molecular clasp with the leucine zipper, DP107, determinant. The results
 also indicate that the anti-HIV activity of various gp41 derivatives
 (peptides and recombinant proteins) may be due to their ability to form
 complexes with viral gp41 and interfere with its fusogenic process.
 8.1. Maretials and Methods
 8.1.1. Construction of Fusion Protiens and GP41 Mutants
 Construction of fusion proteins and mutants shown in FIG. 7 was
 accomplished as follows: the DNA sequence corresponding to the
 extracellular domain of gp41 (540-686) was cloned into the Xmn I site of
 the expression vector pMal-p2 (New England Biolab) to give M41. The gp41
 sequence was amplified from pgtat (Malim et al., 1988, Nature 355:
 181-183) by using polymerase chain reaction (PCR) with upstream primer
 5'-ATGACGCTGACGGTACAGGCC-3' (primer A) (SEQ ID NO:11) and downstream
 primer 5'-TGACTAAGCTTAATACCACAGCCAATTTGTTAT-3' (SEQ ID NO:12) (primer B).
 M41-P was constructed by using the T7-Gen in vitro mutagenesis kit from
 United States Biochemicals (USB) following the supplier's instructions.
 The mutagenic primer (5'-GGAGCTGCTTGGGGCCCCAGAC-3') (SEQ ID NO:13)
 introduces an Ile to Pro mutation in M41 at position 578. M41.DELTA.107,
 from which the DP-107 region has been deleted, was made using a deletion
 mutagenic primer 5'-CCAAATCCCCAGGAGCTGCTCGAGCTGCACTATACCAGAC-3' (SEQ ID
 NO:14) (primer C) following the USB T7-Gen mutagenesis protocol.
 M41.DELTA.178, from which the DP-178 region has been deleted, was made by
 cloning the DNA fragment corresponding to gp41 amino acids 540-642 into
 the Xmn I site of pMal-p2. Primer A and
 5'-ATAGCTTCTAGATTAATTGTTAATTTCTCTGTCCC-3' (SEQ ID NO:15) (primer D) were
 used in the PCR with the template pgtat to generate the inserted DNA
 fragments. M41-P was used as the template with primer A and D in PCR to
 generate M41-P.DELTA.178. All inserted sequences and mutated residues were
 checked by restriction enzyme analysis and confirmed by DNA sequencing.
 8.1.2. Purification and Characterization of Fusion Proteins
 The fusion proteins were purified according to the protocol described in
 the manufacturer's brochure of protein fusion and purification systems
 from New England Biolabs (NEB). Fusion proteins (10 ng) were analyzed by
 electrophoresis on 8% SDS polyacrylamide gels. Western blotting analysis
 was performed as described by Sambrook et al., 1989, Molecular Cloning: A
 Laboratory Manual, 2d Ed, Cold Spring Harbor Laboratory Press, Cold Spring
 Harbor, N.Y., Ch. 18, pp. 64-75. An HIV-1 positive serum diluted
 1000-fold, or a human Fab derived from repertoire cloning was used to
 react with the fusion proteins. The second antibody was HRP-conjugated
 goat antihuman Fab. An ECL Western blotting detection system (Amersham)
 was used to detect the bound antibody. A detailed protocol for this
 detection system was provided by the manufacturer. Rainbow molecular
 weight markers (Amersham) were used to estimate the size of fusion
 proteins.
 8.1.3. Cell Fusion Assays For Anti-HIV Activity
 Cell fusion assays were performed as previously described (Matthews et al.,
 1987, Proc. Natl. Acad. Sci. USA 84: 5424-5481). CEM cells
 (7.times.10.sup.4) were incubated with HIV-1.sub.IIIB chronically infected
 CEM cells (10.sup.4) in 96-well flat-bottomed half-area plates (Costar) in
 100 .mu.l culture medium. Peptide and fusion proteins at various
 concentrations in 10 .mu.l culture medium were incubated with the cell
 mixtures at 37.degree. C. for 24 hours. Multinucleated syncytia were
 estimated with microscopic examination. Both M41 and M41-P did not show
 cytotoxicity at the concentrations tested and shown in FIG. 8.
 Inhibition of HIV-1 induced cell-cell fusion activity was carried out in
 the presence of 10 nM DP178 and various concentrations of M41.DELTA.178 or
 M41-P.DELTA.178 as indicated in FIG. 9. There was no observable syncytia
 in the presence of 10 nM DP178. No peptide or fusion protein was added in
 the control samples.
 8.1.4. Elisa Analysis of DP178 Binding to the Leucine Zipper Motif of gp41
 The amino acid sequence of DP178 used is:
 YTSLIHSLIEESQNQQEKNEQELLELDKWASLWNWF. For enzyme linked immunoassay
 (ELISA), M41.DELTA.78 or M41-P.DELTA.178 (5 .mu.g/ml) in 0.1M NaHCO.sub.3,
 pH 8.6, were coated on 96 wells Linbro ELISA plates (Flow Lab, Inc.)
 overnight. Each well was washed three times with distilled water then
 blocked with 3% bovine serum albumin (BSA) for 2 hours. After blocking,
 peptides with 0.5% BSA in TBST (40 mM Tris-HCl pH7.5, 150 mM NaCl, 0.05%
 Tween 20) were added to the ELISA plates and incubated at room temperature
 for 1 hour. After washing three times with TBST, Fab-d was added at a
 concentration of 10 ng/ml with 0.5% BSA in TBST. The plates were washed
 three times with TBST after incubation at room temperature for 1 hour.
 Horse radish peroxidase (HRP) conjugated goat antihuman Fab antiserum at a
 2000 fold dilution in TBST with 0.5% BSA was added to each well and
 incubated at room temperature for 45 minutes. The plates were then washed
 four times with TBST. The peroxidase substrate o-phenylene diamine (2.5
 mg/ml) and 0.15% H.sub.2 O.sub.2 were added to develop the color. The
 reaction was stopped with an equal volume of 4.5 N H.sub.2 SO.sub.4 after
 incubation at room temperature for 10 minutes. The optical density of the
 stopped reaction mixture was measured with a micro plate reader (Molecular
 Design) at 490 nm. Results are shown in FIG. 10.
 8.2. Results
 8.2.1. The Expression and Characterization of the Ectodomain of gp41
 As a step toward understanding the roles of the two helical regions in gp41
 structure and function, the ectodomain of gp41 was expressed as a maltose
 binding fusion protein (M41) (FIG. 7). The fusogenic peptide sequence at
 the N-terminal of gp41 was omitted from this recombinant protein and its
 derivatives to improve solubility. The maltose binding protein facilitated
 purification of the fusion proteins under relatively mild, non-denaturing
 conditions. Because the M41 soluble recombinant gp41 was not glycosylated,
 lacked several regions of the transmembrane protein (i.e., the fusion
 peptide, the membrane spanning, and the cytoplasmic domains), and was
 expressed in the absence of gp120, it was not expected to precisely
 reflect the structure of native gp41 on HIV-1 virions. Nevertheless,
 purified M41 folded in a manner that preserved certain discontinuous
 epitopes as evidenced by reactivity with human monoclonal antibodies,
 98-6, 126-6, and 50-69, previously shown to bind conformational epitopes
 on native gp41 expressed in eukaryotic cells (Xu et al., 1991, J. Virol.
 65: 4832-4838; Chen, 1994, J. Virol. 68:2002-2010). Thus, at least certain
 regions of native gp41 defined by these antibodies appear to be reproduced
 in the recombinant fusion protein M41. Furthermore, M41 reacted with a
 human recombinant Fab (Fab-d) that recognizes a conformational epitope on
 gp41 and binds HIV-1 virions as well as HIV-1 infected cells but not
 uninfected cells as analyzed by FACS. Deletion of either helix motif,
 i.e., DP107 or DP178, of the M41 fusion protein eliminated reactivity with
 Fab-d. These results indicate that both helical regions, separated by 60
 amino acids in the primary sequence, are required to maintain the Fab-d
 epitope.
 8.2.2. Anti-HIV Activity of the Recombinant Ectodomain of gp41
 The wild type M41 fusion protein was tested for anti-HIV-1 activity. As
 explained, supra, synthetic peptides corresponding to the leucine zipper
 (DP107) and the C-terminal putative helix (DP178) show potent anti-HIV
 activity. Despite inclusion of both these regions, the recombinant M41
 protein did not affect HIV-1 induced membrane fusion at concentrations as
 high as 50 .mu.M (Table XXV, below).
 TABLE XIII
 DISRUPTION OF THE LEUCINE ZIPPER OF
 GP41 FREES THE ANTI-HIV MOTIF
 DP107 DP178 M41 M41-P M41-P.DELTA.178
 Cell fusion 1 .mu.M 1 nM &gt;50 .mu.M 83 nM &gt;50 .mu.M
 (IC.sub.90)
 Fab-D -- -- 3.5 .times. 10.sup.-9 2.5 .times. 10.sup.-8
 --
 binding (k.sub.D)
 HIV infectivity 1 .mu.M 80 nM &gt;16 .mu.M 66 nM &gt;8 .mu.M
 (IC.sub.90)
 1 The affinity constants of Fab-d binding to the fusion proteins were
 determined using a protocol described by B. Friguet et al., 1985, J.
 Immunol. Method. 77:305-319.
 -- = No detectable binding of Fab-d to the fusion proteins.
 Antiviral Infectivity Assays. 20 .mu.l of serially diluted virus stock was
 incubated for 60 minutes at ambient temperature with 20 .mu.l of the
 indicated concentration of purified recombinant fusion protein in RPMI
 1640 containing 10% fetal bovine serum and antibiotics in a 96-well
 microtiter plate. 20 .mu.l of CEM4 cells at 6 .times. 10.sup.5 cells/ml
 were added to each well, and cultures were incubated at 37.degree. C. in a
 humidified CO.sub.2 incubator. Cells were cultured for 9
 # days by the addition of fresh medium every 2 to 3 days. On days 5, 7, and
 9 postinfection, supernatant samples were assayed for reverse
 transcriptase (RT) activity, as described below, to monitor viral
 replication. The 50% tissue culture infectious dose (TCID.sub.50) was
 calculated for each condition according to the formula of Reed & Muench,
 1937, Am. J. Hyg. 27:493-497. RT activity was determined by a modification
 of the published methods of Goff et al., 1981, J. Virol. 38:
 # 239-248 and Willey et al., 1988, J. Virol. 62:139-147 as described in
 Chen et al., 1993, AIDS Res. Human Retroviruses 9:1079-1086.
 Surprisingly, a single amino acid substitution, proline in place of
 isoleucine in the middle of the leucine zipper motif, yielded a fusion
 protein (M41-P) which did exhibit antiviral activity (Table XIII and FIG.
 8). As seen in Table XIII, M41-P blocked syncytia formation by 90% at
 approximately 85 nM and neutralized HIV-1.sub.IIIB infection by 90% at
 approximately 70 nM concentrations. The anti-HIV-1 activity of M41-P
 appeared to be mediated by the C-terminal helical sequence since deletion
 of that region from M41-P yielded an inactive fusion protein,
 M41-P.DELTA.178 (Table XIII). This interpretation was reinforced by
 experiments demonstrating that a truncated fusion protein lacking the
 DP178 sequence, M41.DELTA.178, abrogated the potent anti-fusion activity
 of the DP178 peptide in a concentration-dependent manner (FIG. 9). The
 same truncated fusion protein containing the proline mutation disrupting
 the leucine zipper, M41-P.DELTA.178, was not active in similar competition
 experiments (FIG. 9). The results indicate that the DP178 peptide
 associates with a second site on gp41 whose interactive structure is
 dependent on a wild type leucine zipper sequence. A similar interaction
 may occur within the wild type fusion protein, M41, and act to form an
 intramolecular clasp which sequesters the DP178 region, making it
 unavailable for anti-viral activity.
 A specific association between these two domains is also indicated by other
 human monoclonal Fab-d studies. For example, Fab-d failed to bind either
 the DP178 peptide or the fusion protein M41.DELTA.178, but its epitope was
 reconstituted by simply mixing these two reagents together (FIG. 10).
 Again, the proline mutation in the leucine zipper domain of the fusion
 protein, M41-P.DELTA.178, failed to reconstitute the epitope in similar
 mixing experiments.
 9. EXAMPLE: METHOD FOR COMPUTER-ASSISTED IDENTIFICATION OF DP107-LIKE AND
 DP178-LIKE SEOUENCES
 A number of known coiled-coil sequences have been well described in the
 literature and contain heptad repeat positioning for each amino acid.
 Coiled-coil nomenclature labels each of seven amino acids of a heptad
 repeat A through G, with amino acids A and D tending to be hydrophobic
 positions. Amino acids E and G tend to be charged. These four positions
 (A, D, E, and G) form the amphipathic backbone structure of a monomeric
 alpha-helix. The backbones of two or more amphipathic helices interact
 with each other to form di-, tri-, tetrameric, etc., coiled-coil
 structures. In order to begin to design computer search motifs, a series
 of well characterized coiled coils were chosen including yeast
 transcription factor GCN4, Influenza Virus hemagglutinin loop 36, and
 human proto-oncogenes c-Myc, c-Fos, and c-Jun. For each peptide sequence,
 a strict homology for the A and D positions, and a list of the amino acids
 which could be excluded for the B, C, E, F, and G positions (because they
 are not observed in these positions) was determined. Motifs were tailored
 to the DP107 and DP178 sequences by deducing the most likely possibilities
 for heptad positioning of the amino acids of HIV-1 Bru DP-107, which is
 known to have coiled-coil structure, and HIV-1 Bru DP178, which is still
 structurally undefined. The analysis of each of the sequences is contained
 in FIG. 12. For example, the motif for GCN4 was designed as follows:
 1. The only amino acids (using standard single letter amino acid codes)
 found in the A or D positions of GCN4 were [LMNV].
 2. All amino acids were found at B, C, E, F, and G positions except
 {CFGIMPTW}.
 3. The PESEARCH motif would, therefore, be written as follows:
 [LMNV]-{CFGIMPTW}(2)-[LMNV]-{CFGIMPTW}(3)--
 [LMNV]-{CFGIMPTW}(2)-[LMNV]-{CFGIMPTW}(3)--
 [LMNV]-{CFGIMPTW}(2)-[LMNV]-{CFGIMPTW}(3)--
 [LMNV]-{CFGIMPTW}(2)-[LMNV]-{CFGIMPTW}(3)
 Translating or reading the motif: "at the first A position either L, M, N,
 or V must occur; at positions B and C (the next two positions) accept
 everything except C, F, G, I, M, P, T, or W; at the D position either L,
 M, N, or V must occur; at positions E, F, and G (the next 3 positions)
 accept everything except C, F, G, I, M, P, T, or W." This statement is
 contained four times in a 28-mer motif and five times in a 35-mer motif.
 The basic motif key then would be: [LMNV]-{CFGIMPTW}. The motif keys for
 the remaining well described coiled-coil sequences are summarized in FIG.
 12.
 The motif design for DP107 and DP178 was slightly different than the 28-mer
 model sequences described above due to the fact that heptad repeat
 positions are not defined and the peptides are both longer than 28
 residues. FIG. 13 illustrates several possible sequence alignments for
 both DP107 and DP178 and also includes motif designs based on 28-mer,
 35-mer, and full-length peptides. Notice that only slight differences
 occur in the motifs as the peptides are lengthened. Generally, lengthening
 the base peptide results in a less stringent motif. This is very useful in
 broadening the possibilities for identifying DP107- or DP-178-like primary
 amino acid sequences referred to in this document as "hits". In addition
 to making highly specific motifs for each type peptide sequence to be
 searched, it is also possible to make "hybrid" motifs. These motifs are
 made by "crossing" two or more very stringent motifs to make a new search
 algorithm which will find not only both "parent" motif sequences but also
 any peptide sequences which have similarities to one, the other, or both
 "parents". For example, in FIG. 14 the "parent" sequence of GCN4 is
 crossed with each of the possible "parent" motifs of DP-107. Now the
 hybrid motif must contain all of the amino acids found in the A and D
 positions of both parents, and exclude all of the amino acids not found in
 either parent at the other positions. The resulting hybrid from crossing
 GCN4 or [LMNV]{CFGIMPTW} and DP107 (28-mer with the first L in the D
 position) or [ILQT]{CDFIMPST}, is [ILMNQTV]{CFIMPT}. Notice that now only
 two basic hybrid motifs exist which cover both framing possibilities, as
 well as all peptide lengths of the parent DP-107 molecule. FIG. 15
 represents the "hybridizations" of GCN4 with DP-178. FIG. 16 represents
 the "hybridizations" of DP107 and DP178. It is important to keep in mind
 that the represented motifs, both parent and hybrid, are motif keys and
 not the depiction of the full-length motif needed to actually do the
 computer search.
 Hybridizations can be performed on any combination of two or more motifs.
 FIG. 17 summarizes several three-motif hybridizations including GCN4,
 DP107 (both frames), and DP178 (also both frames). Notice that the
 resulting motifs are now becoming much more similar to each other. In
 fact, the first and third hybrid motifs are actually subsets of the second
 and fourth hybrid motifs respectively. This means that the first and third
 hybrid motifs are slightly more stringent than the second and fourth. It
 should also be noted that with only minor changes in these four motifs, or
 by hybridizing them, a single motif could be obtained which would find all
 of the sequences. However, it should be remembered that stringency is also
 reduced. Finally, the most broad-spectrum and least-stringent hybrid motif
 is described in FIG. 18 which summarizes the hybridization of GCN4, DP107
 (both frames), DP178 (both frames), c-Fos, c-Jun, c-Myc, and Flu loop 36.
 A special set of motifs was designed based on the fact that DP-178 is
 located only approximately ten amino acids upstream of the transmembrane
 spanning region of gp41 and just C-terminal to a proline which separates
 DP107 and DP178. It has been postulated that DP178 may be an amphipathic
 helix when membrane associated, and that the proline might aid in the
 initiation of the helix formation. The same arrangement was observed in
 Respiratory Syncytial Virus; however, the DP178-like region in this virus
 also had a leucine zipper just C-terminal to the proline. Therefore,
 N-terminal proline-leucine zipper motifs were designed to analyze whether
 any other viruses might contain this same pattern. The motifs are
 summarized in FIG. 19.
 The PC/Gene protein database contains 5879 viral amino acid sequences
 (library file PVIRUSES; CD-ROM release 11.0). Of these, 1092 are viral
 enveloped or glycoprotein sequences (library file PVIRUSE1). Tables V
 through XIV contain lists of protein sequence names and motif hit
 locations for all the motifs searched.
 10. EXAMPLE: COMPUTER-ASSISTED IDENTIFICATION OF DP107 AND DP178-LIKE
 SEQUENCES IN HUMAN IMMUNODEFICIENCY VIRUS
 FIG. 20 represents search results for HIV-1 BRU isolate gp41 (PC/Gene
 protein sequence PENV_HV1BR). Notice that the hybrid motif which crosses
 DP-107 and DP-178 (named 107.times.178.times.4; the same motif as found in
 FIG. 16 found three hits including amino acids 550-599, 636-688, and
 796-823. These areas include DP-107 plus eight N-terminal and four
 C-terminal amino acids; DP178 plus seven N-terminal and ten C-terminal
 amino acids; and an area inside the transmembrane region (cytoplasmic).
 FIG. 20 also contains the results obtained from searching with the motif
 named ALLMOTI5, for which the key is found in FIG. 17 ({CDGHP}
 {CFP}.times.5). This motif also found three hits including DP107 (amino
 acids 510-599), DP178 (615-717), and a cytoplasmic region (772-841). These
 hits overlap the hits found by the motif 107.times.178.times.4 with
 considerable additional sequences on both the amino and carboxy termini.
 This is not surprising in that 107.times.178.times.4 is a subset of the
 ALLMOTI5 hybrid motif. Importantly, even though the stringency of ALLMOTI5
 is considerably less than 107.times.178.times.4, it still selectively
 identifies the DP107 and DP178 regions of gp41 shown to contain sequences
 for inhibitory peptides of HIV-1. The results of these two motif searches
 are summarized in Table V under the PC/Gene protein sequence name PENV
 HV1BR. The proline-leucine zipper motifs also gave several hits in HIV-1
 BRU including 503-525 which is at the very C-terminus of gp120, just
 upstream of the cleavage site (P7LZIPC and P12LZIPC); and 735-768 in the
 cytoplasmic domain of gp41 (P23LZIPC). These results are found in Tables
 VIII, IX, and X under the same sequence name as mentioned above. Notice
 that the only area of HIV-1 BRU which is predicted by the Lupas algorithm
 to contain a coiled-coil region, is from amino acids 635-670. This begins
 eight amino acids N-terminal to the start and ends eight amino acids
 N-terminal to the end of DP178. DP107, despite the fact that it is a known
 coiled coil, is not predicted to contain a coiled-coil region using the
 Lupas method.
 11. EXAMPLE: COMPUTER-ASSISTED IDENTIFICATION OF DP107-LIKE AND DP178-LIKE
 SEQUENCES IN HUMAN RESPIRATORY SYNCYTIAL VIRUS
 FIG. 21 represents search results for Human Respiratory Syncytial Virus
 (RSV; Strain A2) fusion glycoprotein F1 (PC/Gene protein sequence name
 PVGLF_HRSVA). Motif 107.times.178.times.4 finds three hits including amino
 acids 152-202, 213-243, and 488-515. The arrangement of these hits is
 similar to what is found in HIV-1 except that the motif finds two regions
 with similarities to DP-178, one just downstream of what would be called
 the DP107 region or amino acids 213-243, and one just upstream of the
 transmembrane region (also similar to DP178) or amino acids 488-515. Motif
 ALLMOTI5 also finds three areas including amino acids 116-202, 267-302,
 and 506-549. The proline-leucine zipper motifs also gave several hits
 including amino acids 205-221 and 265-287 (PlLZIPC 265-280, P12LZIPC), and
 484-513 (P7LZIPC and P12LZIPC 484-506, P23LZIPC). Notice that the PLZIP
 motifs also identify regions which share location similarities with DP-178
 of HIV-1.
 12. EXAMPLE: COMPUTER-ASSISTED IDENTIFICATION OF DP107-LIKE AND DP178-LIKE
 SEQUENCES IN SIMIAN IMMUNODEFICIENCY VIRUS
 Motif hits for Simian immunodeficiency Virus gp41 (AGM3 isolate; PC/Gene
 protein sequence name PENV_SIVAG) are shown in FIG. 22. Motif
 107.times.178.times.4 finds three hits including amino acids 566-593,
 597-624, and 703-730. The first two hits only have three amino acids
 between them and could probably be combined into one hit from 566-624
 which would represent a DP107-like hit. Amino acids 703 to 730 would then
 represent a DP178-like hit. ALLMOTI5 also finds three hits including amino
 acids 556-628 (DP107-like), 651-699 (DP178-like), and 808-852 which
 represents the transmembrane spanning region. SIV also has one region from
 655-692 with a high propensity to form a coiled coil as predicted by the
 Lupas algorithm. Both 107.times.178.times.4 and ALLMOTI5 motifs find the
 same region. SIV does not have any PLZIP motif hits in gp41.
 The identification of DP178/DP107 analogs for a second SIV isolate (MM251)
 is demonstrated in the Example presented, below, in Section 19.
 13. EXAMPLE: COMPUTER-ASSISTED IDENTIFICATION OF DP107-LIKE AND DP178 LIKE
 SEQUENCES IN CANINE DISTEMPER VIRUS
 Canine Distemper Virus (strain Onderstepoort) fusion glycoprotein F1
 (PC/Gene Protein sequence name PVGLF_CDVO) has regions similar to Human
 RSV which are predicted to be DP107-like and DP178-like (FIG. 23). Motif
 107.times.178.times.4 highlights one area just C-terminal to the fusion
 peptide at amino acids 252-293. Amino acids 252-286 are also predicted to
 be coiled coil using the Lupas algorithm. Almost 100 amino acids
 C-terminal to the first region is a DP178-like area at residues 340-367.
 ALLMOTI5 highlights three areas of interest including: amino acids
 228-297, which completely overlaps both the Lupas prediction and the
 DP107-like 107.times.178.times.4 hit; residues 340-381, which overlaps the
 second 107.times.178.times.4 hit; and amino acids 568-602, which is
 DP178-like in that it is located just N-terminal to the transmembrane
 region. It also overlaps another region (residues 570-602) predicted by
 the Lupas method to have a high propensity to form a coiled coil. Several
 PLZIP motifs successfully identified areas of interest including P6 and
 P12LZIPC which highlight residues 336-357 and 336-361 respectively; P1 and
 P12LZIPC which find residues 398-414; and P12 and P23LZIPC which find
 residues 562-589 and 562-592 respectively.
 14. EXAMPLE: COMPUTER-ASSISTED IDENTIFICATION OF DP107-LIKE AND DP178-LIKE
 SEQUENCES IN NEWCASTLE DISEASE VIRUS
 FIG. 24 shows the motif hits found in Newcastle Disease Virus (strain
 Australia-Victoria/32; PC Gene protein sequence name PVGLF_NDVA). Motif
 107.times.178.times.4 finds two areas including a DP107-like hit at amino
 acids 151-178 and a DP178-like hit at residues 426-512. ALLMOTI5 finds
 three areas including residues 117-182, 231-272, and 426-512. The hits
 from 426-512 include a region which is predicted by the Lupas method to
 have a high coiled-coil propensity (460-503). The PLZIP motifs identify
 only one region of interest at amino acids 273-289 (P1 and 12LZIPC).
 15. EXAMPLE: COMPUTER-ASSISTED IDENTIFICATION OF DP107-LIKE AND DP178-LIKE
 SEQUENCES IN HUMAN AINFLUENZA VIRUS
 Both motifs 107.times.178.times.4 and ALLMOTI5 exhibit DP107-like hits in
 the same region, 115-182 and 117-182 respectively, of Human Parainfluenza
 Virus (strain NIH 47885; PC/Gene protein sequence name PVGLF_p13H4; (FIG.
 25). In addition, the two motifs have a DP178-like hit just slightly
 C-terminal at amino acids 207-241. Both motifs also have DP178-like hits
 nearer the transmembrane region including amino acids 457-497 and 462-512
 respectively. Several PLZIP motif hits are also observed including 283-303
 (P5LZIPC), 283-310 (P12LZIPC), 453-474 (P6LZIPC), and 453-481 (P23LZIPC).
 The Lupas algorithm predicts that amino acids 122-176 may have a
 propensity to form a coiled-coil.
 16. EXAMPLE: COMPUTER-ASSISTED IDENTIFICATION OF DP107-LIKE AND DP178-LIKE
 SEQUENCES OF INFLUENZA A VIRUS
 FIG. 26 illustrates the Lupas prediction for a coiled coil in Influenza A
 Virus (strain A/Aichi/2/68) at residues 379-436, as well as the motif hits
 for 107.times.178.times.4 at amino acids 387-453, and for ALLMOTI5 at
 residues 380-456. Residues 383-471 (38-125 of HA2) were shown by Carr and
 Kim to be an extended coiled coil when under acidic pH (Carr and Kim,
 1993, Cell 73: 823-832). The Lupas algorithm predicts a coiled-coil at
 residues 379-436. All three methods successfully predicted the region
 shown to actually have coiled-coil structure; however, ALLMOTI5 predicted
 the greatest portion of the 88 residue stretch.
 17. EXAMPLE: POTENTIAL RESPIRATORY SYNCYTIAL VIRUS DP178/DP107 ANALOGS: CD
 AND ANTIVIRAL CHARACTERIZATION
 In the Example presented herein, respiratory syncytial virus (RSV) peptides
 identified by utilizing the computer-assisted search motifs described in
 the Examples presented in Sections 9 and 11, above, were tested for
 anti-RSV activity. Additionally, circular dichroism (CD) structural
 analyses were conducted on the peptides, as discussed below. It is
 demonstrated that several of the identified peptides exhibit potent
 antiviral capability. Additionally, it is shown that several of these
 peptides exhibit a substantial helical character.
 17.1 Materials and Methods
 Structural analyses: The CD spectra were measured in a 10 mM sodium
 phosphate, 150 mM sodium chloride, pH 7.0, buffer at approximately 10 mM
 concentrations, using a 1 cm pathlength cell on a Jobin/Yvon
 Autodichrograph Mark V CD spectrophotometer. Peptides were synthesized
 according to the methods described, above, in Section 6.1. Peptide
 concentrations were determined from A.sub.280 using Edlehoch's method
 (1967, Biochemistry 6:1948).
 Anti-RSV antiviral activity assays: The assay utilized herein tested the
 ability of the peptides to disrupt the ability of HEp2 cells acutely
 infected with RSV (i.e., cells which are infected with a multiplicity of
 infection of greater than 2) to fuse and cause syncytial formation on a
 monolayer of uninfected an uninfected line of Hep-2 cells. The lower the
 observed level of fusion, the greater the antiviral activity of the
 peptide was determined to be.
 Uninfected confluent monolayers of Hep-2 cells were grown in microtiter
 wells in 3% EMEM (Eagle Minimum Essential Medium w/o L-glutamine [Bio
 Whittaker Cat. No. 12-125F], with fetal bovine serum [FBS; which had been
 heat inactivated for 30 minutes at 56.degree. C.; Bio Whittaker Cat. No.
 14-501F) supplemented at 3%, antibiotics (penicillin/streptomycin; Bio
 Whittaker Cat. No. 17-602E) added at 1%, and glutamine added at 1%.
 To prepare Hep2 cells for addition to uninfected cells, cultures of acutely
 infected Hep2 cells were washed with DPBS (Dulbecco's Phosphate Buffered
 Saline w/o calcium or magnesium; Bio Whittaker Cat. No. 17-512F) and cell
 monolayers were removed with Versene (1:5000; Gibco Life Technologies Cat.
 No. 15040-017). The cells were spun 10 minutes and resuspended in 3% FBS.
 Cell counts were performed using a hemacytometer. Persistent cells were
 added to the uninfected Hep-2 cells.
 The antiviral assay was conducted by, first, removing all media from the
 wells containing uninfected Hep-2 cells, then adding peptides (at the
 dilutions described below) in 3% EMEM, and 100 acutely RSV-infected Hep2
 cells per well. Wells were then incubated at 37.degree. C. for 48 hours.
 After incubation, cells in control wells were checked for fusion centers,
 media was removed from the wells, followed by addition, to each well, of
 either Crystal Violet stain or XTT. With respect to Crystal Violet,
 approximately 50 .mu.l 0.25% Crystal Violet stain in methanol were added
 to each well. The wells were rinsed immediately, to remove excess stain,
 and were allowed to dry. The number of syncytia per well were then
 counted, using a dissecting microscope.
 With respect to XTT
 (2,3-bis[2-Methoxy-4-nitro-5-sulfophenyl]-2H-tetrazolium-5-carboxyanilide
 inner salt), 50 .mu.l XTT (1 mg/ml in RPMI buffered with 100 mM HEPES, pH
 7.2-7.4, plus 5% DMS0) were added to each well. The OD.sub.450/690 was
 measured (after blanking against growth medium without cells or reagents,
 and against reagents) according to standard procedures.
 Peptides: The peptides characterized in the study presented herein were:
 1) peptides T-142 to T-155 and T-575, as shown in FIG. 27A, and peptides
 T-22 to T-27, T-68, T-334 and T-371 to T-375 and T-575, as shown in FIG.
 27B;
 2) peptides T-120 to T-141 and T-576, as shown in FIG. 27B, and peptides
 T-12, T-13, T-15, T-19, T-28 to T-30, T-66, T-69, T-70 and T-576, as shown
 in FIG. 27D; and
 3) peptides T-67 and T-104 to T-119 and T-384, as shown in FIG. 28A, and
 peptides T-71, T-613 to T-617, T-662 to T-676 and T-730, as shown in FIG.
 28B.
 The peptides of group 1 represent portions of the RSV F2 protein
 DP178/107-like region. The peptides of group 2 represent portions of the
 RSV F1 protein DP107-like region. The peptides of groups 3 represent
 portions of the RSV F1 protein DP178-like region.
 Each peptide was tested at 2-fold serial dilutions ranging from 100
 .mu.g/ml to approximately 100 ng/ml. For each of the assays, a well
 containing no peptide was also used. The IC.sub.50 data for each peptide
 represents the average of several experiments conducted utilizing that
 peptide.
 17.2 Results
 The data summarized in FIGS. 27A-B and 28A-B represent antiviral and
 structural information obtained from peptides derived from the RSV F2
 DP178/DP107-like F2 region (FIGS. 27A-B), the RSV F1 DP-107-like region
 (FIGS. 27C-D) and the RSV DP178-like F2 region (FIGS. 28A-B).
 As shown in FIGS. 27A-D, a number of the RSV DP178/DP107-like peptides
 exhibited a detectable level of antiviral activity. Peptides from the RSV
 DP178/DP107-like F2 region (FIGS. 27A-B), for example, T-142 to T-145 and
 T-334 purfied peptides, exhibited detectable levels of antiviral activity,
 as evidenced by their IC.sub.50 values. Further, a number of RSV F1
 DP107-like peptides (FIGS. 27C-D) exhibited a sizable level of antiviral
 activity as purified peptides, including, for example, peptides T-124 to
 T-127, T-131, T-135 and T-137 to T-139, as demonstrated by their low
 IC.sub.50 values. In addition, CD analysis FIGS. 27A, 27C) reveals that
 many of the peptides exhibit some detectable level of helical structure.
 The results summarized in FIGS. 28A-B demonstrate that a number of
 DP178-like purified peptides exhibit a range of potent anti-viral
 activity. These peptides include, for example, T-67, T-104, T-105 and
 T-107 to T-119, as listed in FIG. 28A, and T-665 to T-669 and T-671 to
 T-673, as listed in FIG. 28B. In addition, some of the DP178-like peptides
 exhibited some level of helicity.
 Thus, the computer assisted searches described, hereinabove, successfully
 identified viral peptide domains that represent highly promising anti-RSV
 antiviral compounds.
 18. EXAMPLE: POTENTIAL HUMAN AINFLUENZA VIRUS TYPE 3 DP178/DP107
 ANALOGS: CD AND ANTIVIRAL CHARACTERIZATION
 In the Example presented herein, human parainfluenza virus type 3 (HPIV3)
 peptides identified by utilizing the computer-assisted search motifs
 described in the Examples presented in Sections 9 and 15, above, were
 tested for anti-HPIV3 activity. Additionally, circular dichroism (CD)
 structural analyses were conducted on the peptides, as discussed below. It
 is demonstrated that several of the identified peptides exhibit potent
 antiviral capability. Additionally, it is shown that several of these
 peptides exhibit a substantial helical character.
 18.1 Materials and Methods
 Structural analyses: Structural analyses consisted of circular dichroism
 (CD) studies. The CD spectra were measured in a lOmM sodium phosphate, 150
 mM sodium chloride, pH 7.0, buffer at approximately 10 mM concentrations,
 using a 1 cm pathlength cell on a Jobin/Yvon Autodichrograph Mark V CD
 spectrophotometer. Peptide concentrations were determined from A.sub.280
 using Edlehoch's method (1967, Biochemistry 6:1948).
 Anti-HPIV3 antiviral activity assays: The assay utilized herein tested the
 ability of the peptides to disrupt the ability of Hep2 cells chronically
 infected with HPIV3 to fuse and cause syncytial formation on a monolayer
 of an uninfected line of CV-1W cells. The more potent the lower the
 observed level of fusion, the greater the antiviral activity of the
 peptide.
 Uninfected confluent monolayers of CV-1W cells were grown in microtiter
 wells in 3% EMEM (Eagle Minimum Essential Medium w/o L-glutamine [Bio
 Whittaker Cat. No. 12-125F], with fetal bovine serum [FBS; which had been
 heat inactivated for 30 minutes at 56.degree. C.; Bio Whittaker Cat. No.
 14-501F) supplemented at 3%, antibiotics/antimycotics (Gibco BRL Life
 Technologies Cat. No. 15040-017) added at 1%, and glutamine added at 1%.
 To prepare Hep2 cells for addition to uninfected cells, cultures of
 chronically infected Hep2 cells were washed with DPBS (Dulbecco's
 Phosphate Buffered Saline w/o calcium or magnesium; Bio Whittaker Cat. No.
 17-512F) and cell monolayers were removed with Versene (1:5000; Gibco Life
 Technologies Cat. No. 15040-017). The cells were spun 10 minutes and
 resuspended in 3% FBS. Cell counts were performed using a hemacytometer.
 Persistent cells were added to the uninfected CV-1W cells.
 The antiviral assay was conducted by, first, removing all media from the
 wells containing uninfected CV-1W cells, then adding peptides (at the
 dilutions described below) in 3% EMEM, and 500 chronically HPIV3-infected
 Hep2 cells per well. Wells were then incubated at 37.degree. C. for 24
 hours.
 On day 2, after cells in control wells were checked for fusion centers,
 media was removed from the wells, followed by addition, to each well, of
 approximately 50 .mu.l 0.25% Crystal Violet stain in methanol. Wells were
 rinsed immediately, to remove excess stain and were then allowed to dry.
 The number of syncytia per well were then counted, using a dissecting
 microscope.
 Alternatively, instead of Crystal Violet analysis, cells were assayed with
 XTT, as described, above, in Section 17.1.
 Peptides: The peptides characterized in the study presented herein were:
 1) Peptides 157 to 188, as shown in FIG. 29A, and peptides T-38 to T-40,
 T-42 to T-46 and T-582, as shown in FIG. 29B. These peptides are derived
 from the DP107 region of the HPIV3 F1 fusion protein (represented by HPF3
 107, as shown in FIG. 29A); and
 2) Peptides 189 to 210, as shown in FIG. 30A, and T-269, T-626, T-383 and
 T-577 to T-579, as shown in FIG. 30B. These peptides are primarily derived
 from the DP178 region of the HPIV3 F1 fusion protein (represented by HPF3
 178, as shown in FIG. 30A). Peptide T-626 contains two mutated amino acid
 resides (represented by a shaded background). Additionally, peptide T-577
 represents F1 amino acids 65-100, T-578 represents F1 amino acids 207-242
 and T-579 represents F1 amino acids 273-309.
 Each peptide was tested at 2-fold serial dilutions ranging from 500
 .mu.g/ml to approximately 500 ng/ml. For each of the assays, a well
 containing no peptide was also used.
 18.2 Results
 The data summarized in FIGS. 29A-C and 30A-B represent antiviral and
 structural information obtained from peptides derived from the HPIV3
 fusion protein DP107-like region (FIGS. 29A-C) and the HPIV3 fusion
 protein DP178-like region (FIGS. 30A-B).
 As shown in FIGS. 29A-B, a number of the HPIV3 DP107-like peptides
 exhibited potent levels of antiviral activity. These peptides include, for
 example, peptides T-40, T-172 to T-175, T-178, T-184 and T-185.
 CD analysis reveals that a number of the peptides exhibit detectable to
 substantial level of helical structure.
 The results summarized in FIGS. 30A-B demonstrate that a number of the
 DP178-like peptides tested exhibit a range of anti-viral activity. These
 peptides include, for example, peptides 194 to 211, as evidenced by their
 low IC.sub.50 values. In fact, peptides 201 to 205 exhibit IC.sub.50
 values in the nanogram/ml range. In addition, many of the DP178-like
 peptides exhibited some level of helicity.
 Thus, the computer assisted searches described, hereinabove, have
 successfully identified viral peptide domains that represent highly
 promising anti-HPIV3 antiviral compounds.
 19. EXAMPLE: COMPUTER-ASSISTED IDENTIFICATION OF DP178/DP107 ANALOGS IN
 SIMIAN IMMUNODEFICIENCY VIRUS
 FIG. 31 represents search results for SIV isolate MM251 (PC/Gene.RTM.
 protein sequence PENV_SIVM2). Both 107.times.178.times.4 and ALLMOTI5
 search motifs identified two regions with similarities to DP107 and/or
 DP178.
 The peptide regions found by 107.times.178.times.4 were located at amino
 acid residues 156-215 and 277-289. The peptide regions found by ALLMOTI5
 were located at amino acid residues 156-219 and 245-286. Both motifs,
 therefore, identify similar regions.
 Interestingly, the first SIV peptide region (i.e., from amino acid residue
 156 to approximately amino acid residue 219) correlates with a DP107
 region, while the second region identified (i.e., from approximately amino
 acid residue 245 to approximately amino acid residue 289) correlates with
 the DP178 region of HIV. In fact, an alignment of SIV isolate MM251 and
 HIV isolate BRU, followed by a selection of the best peptide matches for
 HIV DP107 and DP178, reveals that the best matches are found within the
 peptide regions identified by the 107.times.178.times.4 and ALLMOTI5
 search motifs.
 It should be noted that a potential coiled-coil region at amino acid
 residues 242-282 is predicted by the Lupas program. This is similar to the
 observation in HIV in which the coiled-coil is predicted by the Lupas
 program to be in the DP178 rather than in the DP107 region. It is
 possible, therefore, that SIV may be similar to HIV in that it may contain
 a coiled-coil structure in the DP107 region, despite such a structure
 being missed by the Lupas algorithm. Likewise, it may be that the region
 corresponding to a DP178 analog in SIV may exhibit an undefined structure,
 despite the Lupas program's prediction of a coiled-coil structure.
 20. EXAMPLE: COMPUTER-ASSISTED IDENTIFICATION OF DP178/DP107 ANALOGS IN
 EPSTEIN-BARR VIRUS
 The results presented herein describe the identification of DP178/DP107
 analogs within two different Epstein-Barr Virus proteins. Epstein-Barr is
 a human herpes virus which is the causative agent of, for example,
 infectious mononucleosis (IM), and is also associated with nasopharyngeal
 carcinomas (NPC), Burkitt's lymphoma and other diseases. The virus
 predominantly exists in the latent form and is activated by a variety of
 stimuli.
 FIG. 32 depicts the search motif results for the Epstein-Barr Virus (Strain
 B95-8; PC/Gene.RTM. protein sequence PVGLB_EBV) glycoprotein gp110
 precursor (gp115). The 107.times.178.times.4 motif identified two regions
 of interest, namely the regions covered by amino acid residues 95-122 and
 631-658. One PZIP region was identified at amino acid residue 732-752
 which is most likely a cytoplasmic region of the protein. The Lupas
 algorithm predicts a coiled-coil structure for amino acids 657-684. No
 ALLMOTI5 regions were identified.
 FIG. 33 depicts the search motif results for the Zebra (or EB1)
 trans-activator protein (BZLF1) of the above-identified Epstein-Barr
 virus. This protein is a transcription factor which represents the primary
 mediator of viral reactivation. It is a member of the b-ZIP family of
 transcription factors and shares significant homology with the basic
 DNA-binding and dimerization domains of the cellular oncogenes c-fos and
 C/EBP. The Zebra protein functions as a homodimer.
 Search results demonstrate that the Zebra protein exhibits a single region
 which is predicted to be either of DP107 or DP178 similarity, and is found
 between the known DNA binding and dimerization regions of the protein.
 Specifically, this region is located at amino acid residues 193-220, as
 shown in FIG. 33. The Lupas program predicted no coiled-coil regions.
 21. EXAMPLE: COMPUTER-ASSISTED IDENTIFICATION OF DP178IDP107 ANALOGS IN
 MEASLES VIRUS
 FIG. 34 illustrates the motif search results for the fusion protein F1 of
 measles virus, strain Edmonston (PC Gene.RTM. protein sequence
 PVGLF_MEASE), successfully identifying DP178/DP107 analogs.
 The 107.times.178.times.4 motif identifies a single region at amino acid
 residues 228-262. The ALLMOTI5 search motif identifies three regions,
 including amino acid residues 116-184, 228-269 and 452-500. Three regions
 containing proline residues followed by a leucine zipper-like sequence
 were found beginning at proline residues 214, 286 and 451.
 The Lupas program identified two regions it predicted had potential for
 coiled-coil structure, which include amino acid residues 141-172 and
 444-483.
 22. EXAMPLE: COMPUTER-ASSISTED IDENTIFICATION OF DP178/DP107 ANALOGS IN
 HEPATITIS B VIRUS
 FIG. 35 depicts the results of a PZIP motif search conducted on the
 Hepatitis B virus subtype AYW. Two regions of interest within the major
 surface antigen precursor S protein were identified. The first lies just
 C-terminal to the proposed fusion peptide of the major surface antigen
 (Hbs) which is found at amino acid residues 174-191. The second region is
 located at amino acid residues 233-267. The Lupas program predicts no
 coiled-coil repeat regions.
 In order to test the potential anti-HBV antiviral activity of these
 D178/DP107 analog regions, peptides derived from area around the analog
 regions are synthesized, as shown in FIGS. 52A-B. These peptides represent
 one amino acid peptide "walks" through the putative DP178/DP107 analog
 regions. The peptides are synthesized according to standard Fmoc chemistry
 on Rinkamide MBHA resins to provide for carboxy terminal blockade (Chang,
 C. D. and Meinhofer, J., 1978, Int. J. Pept. Protein Res. 11:246-249;
 Fields, G. B. and Noble, R. L., 1990, Int. J. Pept. Protein Res.
 35:161-214). Following complete synthesis, the peptide amino-terminus is
 blocked through automated acetylation and the peptide is cleaved with
 trifluoroacetic acid (TFA) and the appropriate scavengers (King, D. S. et
 al., 1990, Int. J. Pept. Res. 36:255-266). After cleavage, the peptide is
 precipitated with ether and dried under vacuum for 24 hours.
 The anti-HBV activity of the peptides is tested by utilizing standard
 assays to determine the test peptide concentration required to cause an
 acceptable (e.g., 90%) decrease in the amount of viral progeny formed by
 cells exposed to an HBV viral inoculum. Candidate antivial peptides are
 further characterized in model systems such as wood chuck tissue culture
 and animal systems, prior to testing on humans.
 23. EXAMPLE: COMPUTER-ASSISTED IDENTIFICATION OF DP178/DP107 ANALOGS IN
 SIMIAN MASON-PFIZER MONKEY VIRUS
 The results depicted herein illustrate the results of search motifs
 conducted on the Simian Mason-Pfizer monkey virus. The motifs reveal
 DP178/DP107 analogs within the enveloped (TM) protein GP20, as shown in
 FIG. 36.
 The 107.times.178.times.4 motifs identifies a region at amino acid residues
 422-470. The ALLMOTI5 finds a region at amino acid residues 408-474. The
 Lupas program predicted a coiled-coil structure a amino acids 424-459.
 24. EXAMPLE: COMPUTER-ASSISTED IDENTIFICATION OF DP178/DP107 ANALOGS IN
 BACTERIAL PROTEINS
 The results presented herein demonstrate the identification of DP178/DP107
 analogs corresponding to sequences present in proteins of a variety of
 bacterial species.
 FIG. 37 depicts the search motif results for the Pseudomonas aeruginosa
 fimbrial protein (Pilin). Two regions were identified by motifs
 107.times.178.times.4 and ALLMOTI5. The regions located at amino acid
 residues 30-67 and 80-144 were identified by the 107.times.178.times.4
 motif. The regions at amino acid residues 30-68 and 80-125 were identified
 by the ALLMOTI5.
 FIG. 38 depicts the search motif results for the Pseudomonas gonorrhoeae
 fimbrial protein (Pilin). A single region was identified by both the
 107.times.178.times.4 and the ALLMOTI5 motifs. The region located at amino
 acid residues 66-97 was identified by the 107.times.178.times.4 motif. The
 region located at amino acid residues 66-125 were identified by the
 ALLMOTI5 search motif. No coiled-coil regions were predicted by the Lupas
 program.
 FIG. 39 depicts the search motif results for the Hemophilus Influenza
 fimbrial protein (Pilin). A single region was identified by both the
 107.times.178.times.4 and the ALLMOTI5 motifs. The region located at amino
 acid residues 102-129 was identified by the 107.times.178.times.4 motif.
 The region located at amino acid residues 102-148 were identified by the
 ALLMOTI5 search motif. No coiled-coil regions were predicted by the Lupas
 program.
 FIG. 40 depicts the search motif results for the Staphylococcus aureus
 toxic shock syndrome Hemophilus Influenza fimbrial protein (Pilin). A
 single region was identified by both the 107.times.178.times.4 and the
 ALLMOTI5 motifs. The region located at amino acid residues 102-129 was
 identified by the 107.times.178.times.4 motif. The region located at amino
 acid residues 102-148 were identified by the ALLMOTI5 search motif. No
 coiled-coil regions were predicted by the Lupas program.
 FIG. 41 summarizes the motif search results conducted on the Staphylococcus
 aureus enterotoxin Type E protein. These results demonstrate the
 successful identification of DP178/DP107 analogs corresponding to peptide
 sequences within this protein, as described below.
 The ALLMOTI5 motif identified a region at amino acid residues 22-27. The
 107.times.178.times.4 motif identified two regions, with the first at
 amino acid residues 26-69 and the second at 88-115. A P12LZIPC motif
 search identified two regions, at amino acid residues 163-181 and 230-250.
 The Lupas program predicted a region with a high propensity for coiling at
 amino acid residues 25-54. This sequence is completely contained within
 the first region identified by both ALLMOTI5 and 107.times.178.times.4
 motifs.
 FIG. 42 depicts the search motif results conducted on a second
 Staphylococcus aureus toxin, enterotoxin A. Two regions were identified by
 the ALLMOTI5 motif, at amino acid residues 22-70 and amino acid residues
 164-205. The 107.times.178.times.4 motif found two regions, the first at
 amino acid residues 26-69 and the second at amino acid residues 165-192. A
 P23LZIPC motif search revealed a region at amino acid residues 216-250. No
 coiled-coil regions were predicted by the Lupas program.
 FIG. 43 shows the motif search results conducted on the E. coli heat labile
 enterotoxin A protein, demonstrating that identification of DP178/DP107
 analogs corresponding to peptides located within this protein. Two regions
 were identified by the ALLMOTI5 motif, with the first residing at amino
 acid residues 55-115, and the second residing at amino acid residues
 216-254. The 107.times.178.times.4 motif identified a single region at
 amino acid residues 78-105. No coiled-coil regions were predicted by the
 Lupas program.
 25. EXAMPLE: COMPUTER-ASSISTED IDENTIFICATION OF DP178/DP107 ANALOGS WITHIN
 VARIOUS HUMAN PROTEINS
 The results presented herein demonstrate the identification of DP178/DP107
 analogs corresponding to peptide sequences present within several
 different human proteins.
 FIG. 44 illustrates the search motif results conducted on the human c-fos
 oncoprotein. The ALLMOTI5 motif identified a single region at amino acid
 residues 155-193. The 107.times.178.times.4 motif identified one region at
 amino acid residues 162-193. The Lupas program predicted a region at amino
 acid residues 148-201 to have coiled-coil structure.
 FIG. 45 illustrates the search motif results conducted on the human lupus
 KU autoantigen protein P70. The ALLMOTI5 motif identified a single region
 at amino acid residues 229-280. The 107.times.178.times.4 motif identified
 one region at amino acid residues 235-292. The Lupas program predicted a
 region at amino acid residues 232-267 to have coiled-coil structure.
 FIG. 46 illustrates the search motif results conducted on the human zinc
 finger protein 10. The ALLMOTI5 motif identified a single region at amino
 acid residues 29-81. The 107.times.178.times.4 motif identified one region
 at amino acid residues 29-56. A P23LZIPC motif search found a single
 region at amino acid residues 420-457. The Lupas program predicted no
 coiled-coil regions.
 26. EXAMPLE: POTENTIAL MEASLES VIRUS DP178/DP107 ANALOGS: CD AND ANTIVIRAL
 CHARACTERIZATION
 In the Example presented herein, measles (MeV) virus DP178-like peptides
 identified by utilizing the computer-assisted search motifs described in
 the Examples presented in Sections 9 and 21, above, are tested for
 anti-MeV activity. Additionally, circular dichroism (CD) structural
 analyses are conducted on the peptides, as discussed below. It is
 demonstrated that several of the identified peptides exhibit potent
 antiviral capability. Additionally, it is shown that none of the these
 peptides exhibit a substantial helical character.
 26.1 Materials and Methods
 Structural analyses: The CD spectra were measured in a 10 mM sodium
 phosphate, 150 mM sodium chloride, pH 7.0, buffer at approximately 10 mM
 concentrations, using a 1 cm pathlength cell on a Jobin/Yvon
 Autodichrograph Mark V CD spectrophotometer. Peptide concentrations were
 determined from A.sub.280 using Edlehoch's method (1967, Biochemistry
 6:1948).
 Anti-MeV antiviral activity syncytial reduction assay: The assay utilized
 herein tested the ability of the peptides to disrupt the ability of Vero
 cells acutely infected with MeV (i.e., cells which are infected with a
 multiplicity of infection of 2-3) to fuse and cause syncytial formation on
 a monolayer of an uninfected line of Vero cells. The more potent the
 peptide, the lower the observed level of fusion, the greater the antiviral
 activity of the peptide.
 Uninfected confluent monolayers of Vero cells were grown in microtiter
 wells in 10% FBS EMEM (Eagle Minimum Essential Medium w/o L-glutamine [Bio
 Whittaker Cat. No. 12-125F], with fetal bovine serum [FBS; which had been
 heat inactivated for 30 minutes at 56.degree. C.; Bio Whittaker Cat. No.
 14-501F) supplemented at 10%, antibiotics/antimycotics (Bio Whittaker Cat.
 No. 17-602E) added at 1%, and glutamine added at 1%.
 To prepare acutely infected Vero cells for addition to the uninfected
 cells, cultures of acutely infected Vero cells were washed twice with HBSS
 (Bio Whittaker Cat. No. 10-543F) and cell monolayers were removed with
 trypsin (Bio Whittaker Cat. No. 17-161E). Once cells detached, media was
 added, any remaining clumps of cells were dispersed, and hemacytometer
 cell counts were performed.
 The antiviral assay was conducted by, first, removing all media from the
 wells containing uninfected Vero cells, then adding peptides (at the
 dilutions described below) in 10% FBS EMEM, and 50-100 acutely
 MeV-infected Vero cells per well. Wells were then incubated at 37.degree.
 C. for a maximum of 18 hours.
 On day 2, after cells in control wells were checked for fusion centers,
 media was removed from the wells, followed by addition, to each well, of
 approximately 50 .mu.l 0.25% Crystal Violet stain in methanol. Wells were
 rinsed twice with water immediately, to remove excess stain and were then
 allowed to dry. The number of syncytia per well were then counted, using a
 dissecting microscope.
 Anti-MeV antiviral activity plaque reduction assay: The assay utilized
 herein tested the ability of the peptides to disrupt the ability of MeV to
 infect permissive, uninfected Vero cells, leading to the infected cells'
 fusing with uninfected cells to produce syncytia. The lower the observed
 level of syncytial formation, the greater the antiviral activity of the
 peptide.
 Monolayers of uninfected Vero cells are grown as described above.
 The antiviral assay was conducted by, first, removing all media from the
 wells containing uninfected Vero cells, then adding peptides (at the
 dilutions described below) in 10% FBS EMEM, and MeV stock virus at a final
 concentration of 30 plaque forming units (PFU) per well. Wells were then
 incubated at 37.degree. C. for a minimum of 36 hours and a maximum of 48
 hours.
 On day 2, after cells in control wells were checked for fusion centers,
 media was removed from the wells, followed by addition, to each well, of
 approximately 50 .mu.l 0.25% Crystal Violet stain in methanol. Wells were
 rinsed twice with water immediately, to remove excess stain and were then
 allowed to dry. The number of syncytia per well were then counted, using a
 dissecting microscope.
 Peptides: The peptides characterized in the study presented herein were
 peptides T-252A0 to T-256A0, T-257B1/C1, and T-258B1 to T-265B0, and
 T-266A0 to T-268A0, as shown in FIG. 47. These peptides represent a walk
 through the DP178-like region of the MeV fusion protein.
 Each peptide was tested at 2-fold serial dilutions ranging from 100
 .mu.g/ml to approximately 100 ng/ml. For each of the assays, a well
 containing no peptide was also used.
 26.2 Results
 The data summarized in FIG. 47 represents antiviral and structural
 information obtained via "peptide walks" through the DP178-like region of
 the MeV fusion protein.
 As shown in FIG. 47, the MeV DP178-like peptides exhibited a range of
 antiviral activity as crude peptides. Several of these peptides were
 chosen for purification and further antiviral characterization. The
 IC.sub.50 values for such peptides were determined, as shown in FIG. 47,
 and ranged from 1.35 .mu.g/ml (T-257B1/C1) to 0.072 .mu.g/ml (T-265B1).
 None of the DP178-like peptides showed, by CD analysis, a detectable level
 of helicity.
 Thus, the computer assisted searches described, hereinabove, as in for
 example, the Example presented in Section 9, for example, successfully
 identified viral peptide domains that represent highly promising anti-MeV
 antiviral compounds.
 27. EXAMPLE: POTENTIAL SIV DP178/DP107 ANALOGS: ANTIVIRAL CHARACTERIZATION
 In the Example presented herein, simian immunodeficiency virus (SIV)
 DP178-like peptides identified by utilizing the computer-assisted search
 motifs described in the Examples presented in Sections 9, 12 and 19,
 above, were tested for anti-SIV activity. It is demonstrated that several
 of the identified peptides exhibit potent antiviral capability.
 27.1 Materials and Methods
 Anti-SIV antiviral assays: The assay utilized herein were as reported in
 Langolis et al. (Langolis, A. J. et al., 1991, AIDS Research and Human
 Retroviruses 7:713-720).
 Peptides: The peptides characterized in the study presented herein were
 peptides T-391 to T-400, as shown in FIG. 48. These peptides represent a
 walk through the DP178-like region of the SIV .TM. protein.
 Each peptide was tested at 2-fold serial dilutions ranging from 100
 .mu.g/ml to approximately 100 ng/ml. For each of the assays, a well
 containing no peptide was also used.
 27.2 Results
 The data summarized in FIG. 48 represents antiviral information obtained
 via "peptide walks" through the DP178-like region of the SIV .TM. protein.
 As shown in FIG. 48, peptides T-391 to T-400 were tested and exhibited a
 potent antiviral activity as crude peptides.
 Thus, the computer assisted searches described, hereinabove, as in for
 example, the Example presented in Section 9, for example, successfully
 identified viral peptide domains that represent highly promising anti-SIV
 antiviral compounds.
 28. EXAMPLE: ANTI-VIRAL ACTIVITY OF DP107 AND DP-178 PEPTIDE TRUNCATIONS
 AND MUTATIONS
 The Example presented in this Section represents a study of the antiviral
 activity of DP107 and DP178 truncations and mutations. It is demonstrated
 that several of these DP107 and DP178 modified peptides exhibit
 substantial antiviral activity.
 28.1 Materials and Methods
 Anti-HIV assays: The antiviral assays performed were as those described,
 above, in Section 6.1. Assays utilized HIV-1/IIIb and/or HIV-2 NIHZ
 isolates. Purified peptides were used, unless otherwise noted in FIGS.
 49A-C.
 Peptides: The peptides characterized in the study presented herein were:
 1) FIGS. 49A-C present peptides derived from 30 the region around and
 containing the DP178 region of the HIV-1 BRU isolate. Specifically, this
 region spanned from gp41 amino acid residue 615 to amino acid residue 717.
 The peptides listed contain truncations of this region and/or mutations
 which vary from the DP178 sequence amino acid sequence. Further, certain
 of the peptides have had amino- and/or carboxy-terminal groups either
 added or removed, as indicated in the figures; and
 2) FIG. 50. presents peptides which represent truncations of DP107 and/or
 the gp41 region surrounding the DP107 amino acid sequence of HIV-1 BRU
 isolate. Certain of the peptides are unblocked or biotinylated, as
 indicated in the figure.
 Blocked peptides contained an acyl N-terminus and an amido C-terminus.
 28.2 Results
 Anti-HIV antiviral data was obtained with the group 1 DP178-derived
 peptides listed in FIG. 49A-C. The full-length, non-mutant DP178 peptide
 (referred to in FIGS. 49A-C as T20) results shown are for 4 ng/ml.
 In FIG. 49A, a number of the DP178 truncations exhibited a high level of
 antiviral activity, as evidenced by their low IC.sub.50 values. These
 include, for example, test peptides T-50, T-624, T-636 to T-641, T-645 to
 T-650, T-652 to T-654 and T-656. T-50 represents a test peptide which
 contains a point mutation, as indicated by the residue's shaded
 background. The HIV-1-derived test peptides exhibited a distinct
 strain-specific antiviral activity, in that none of the peptides tested on
 the HIV-2 NIHZ isolate demonstrated appreciable anti-HIV-2 antiviral
 activity.
 Among the peptides listed in FIG. 49B, are test peptides representing the
 amino (T-4) and carboxy (T-3) terminal halves of DP178 were tested. The
 amino terminal peptide was not active (IC.sub.50 &gt;400 .mu.g/ml) whereas
 the carboxy terminal peptide showed potent antiviral activity (IC.sub.50
 =3 .mu.g/ml). A number of additional test peptides also exhibited a high
 level of antiviral activity. These included, for example, T-61/T-102,
 T-217 to T-221, T-235, T-381, T-677, T-377, T-590, T-378, T-591, T-271 to
 T-272, T-611, T-222 to T-223 and T-60/T-224. Certain of the antiviral
 peptides contain point mutations and/or amino acid residue additions which
 vary from the DP178 amino acid sequence.
 In FIG. 49C, point mutations and/or amino and/or carboxy-terminal
 modifications are introduced into the DP178 amino acid sequence itself. As
 shown in the figure, the majority of the test peptides listed exhibit
 potent antiviral activity.
 Truncations of the DP107 peptide (referred to in FIG. 50 as T21) were also
 produced and tested, as shown in FIG. 50. FIG. 50 also presents data
 concerning blocked and unblocked peptides which contain additional amino
 acid residues from the gp41 region in which the DP107 sequence resides.
 Most of these peptides showed antiviral activity, as evidenced by their
 low IC.sub.50 values.
 Thus, the results presented in this Section demonstrate that not only do
 the full length DP107 and DP178 peptides exhibit potent antiviral
 activity, but truncations and/or mutant versions of these peptides can
 also possess substantial antiviral character.
 29: EXAMPLE: POTENTIAL EPSTEIN-BARR DP178/DP107 ANALOGS: ANTIVIRAL
 CHARACTERIZATION
 In the Example presented herein, peptides derived from the Epstein-Barr
 (EBV) DP-178/DP107 analog region of the Zebra protein identified, above,
 in the Example presented in Section 20 are described and tested for
 anti-EBV activity. It is demonstrated that among these peptides are ones
 which exhibit potential antiviral activity.
 29.1 Materials and Methods
 Electrophoretic Mobility Shift Assays (EMSA)
 Briefly, an EBV Zebra protein was synthesized utilizing SP6 RNA polymerase
 in vitro transcription and wheat germ in vitro translation systems
 (Promega Corporation recommendations; Butler, E. T. and Chamberlain, M.
 J., 1984, J. Biol. Chem. 257:5772; Pelham, H. R. B. and Jackson, R. J.,
 1976, Eur. J. Biochem. 67:247). The in vitro translated Zebra protein was
 then preincubated with increasing amounts of peptide up to 250 ng/ml prior
 to the addition of 10,000 to 20,000 c.p.m. of a .sup.32 P-labeled Zebra
 response element DNA fragment. After a 20 minute incubation in the
 presence of the response element, the reaction was analyzed on a 4%
 non-denaturing polyacrylamide gel, followed by autoradiography, utilizing
 standard gel-shift procedures. The ability of a test peptide to prevent
 Zebra homodimer DNA binding was assayed by the peptide's ability to
 abolish the response element gel migration retardation characteristic of a
 protein-bound nucleic acid molecule.
 Peptides: The peptides characterized in this study represent peptide walks
 through the region containing, and flanked on both sides by, the
 DP178/DP107 analog region identified in the Example presented in Section
 20, above, and shown as shown in FIG. 33. Specifically, the peptide walks
 covered the region from amino acid residue 173 to amino acid residue 246
 of the EBV Zebra protein.
 Each of the tested peptides were analyzed at a range of concentrations,
 with 150 ng/ml being the lowest concentration at which any of the peptides
 exerted an inhibitory effect.
 29.2 Results
 The EBV Zebra protein transcription factor contains a DP178/DP107 analog
 region, as demonstrated in the Example presented, above, in Section 20.
 This protein appears to be the primary factor responsible for the
 reactivation capability of the virus. A method by which the DNA-binding
 function of the Zebra virus may be abolished may, therefore, represent an
 effective antiviral technique. In order to identify potential anti-EBV
 DP178/DP107 peptides, therefore, peptides derived from the region
 identified in Section 20, above, were tested for their ability to inhibit
 Zebra protein DNA binding.
 The test peptides' ability to inhibit Zebra protein DNA binding was assayed
 via the EMSA assays described, above, in Section 28.1. The data summarized
 in FIGS. 51A-B presents the results of EMSA assays of the listed EBV test
 peptides. These peptides represent one amino acid "walks" through the
 region containing, and flanked on both sides by, the DP178/DP107 analog
 region identified in the Example presented in Section 20, above, and shown
 as shown in FIG. 33. As shown in FIGS. 51A-B, the region from which these
 peptides are derived lies from EBV Zebra protein amino acid residue 173 to
 246. A number of the test peptides which were assayed exhibited an ability
 to inhibit Zebra protein homodimer DNA binding, including 439, 441, 444
 and 445.
 Those peptides which exhibit an ability to inhibit Zebra protein DNA
 binding represent potential anti-EBV antiviral compounds whose ability to
 inhibit EBV infection can be further characterized.
 The present invention is not to be limited in scope by the specific
 embodiments described which are intended as single illustrations of
 individual aspects of the invention, and functionally equivalent methods
 and components are within the scope of the invention. Indeed, various
 modifications of the invention, in addition to those shown and described
 herein will become apparent to those skilled in the art from the foregoing
 description and accompanying drawings. Such modifications are intended to
 fall within the scope of the appended claims.
 SEQUENCE LISTING
 (1) GENERAL INFORMATION:
 (iii) NUMBER OF SEQUENCES: 517
 (2) INFORMATION FOR SEQ ID NO: 1:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:1
 Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Ser Gln Asn Gln Gln
 1 5 10 15
 Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu
 20 25 30
 Trp Asn Trp Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 2:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:2
 Ser Ser Glu Ser Phe Thr Leu Leu Glu Gln Trp Asn Asn Trp Lys Leu
 1 5 10 15
 Gln Leu Ala Glu Gln Trp Leu Glu Gln Ile Asn Glu Lys His Tyr Leu
 20 25 30
 Glu Asp Ile Ser
 35
 (2) INFORMATION FOR SEQ ID NO: 3:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:3
 Tyr Thr Asn Thr Ile Tyr Thr Leu Leu Glu Glu Ser Gln Asn Gln Gln
 1 5 10 15
 Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu
 20 25 30
 Trp Asn Trp Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 4:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:4
 Tyr Thr Gly Ile Ile Tyr Asn Leu Leu Glu Glu Ser Gln Asn Gln Gln
 1 5 10 15
 Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala Asn Leu
 20 25 30
 Trp Asn Trp Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 5:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:5
 Tyr Thr Ser Leu Ile Tyr Ser Leu Leu Glu Lys Ser Gln Thr Gln Gln
 1 5 10 15
 Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu
 20 25 30
 Trp Asn Trp Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 6:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:6
 Leu Glu Ala Asn Ile Ser Lys Ser Leu Glu Gln Ala Gln Ile Gln Gln
 1 5 10 15
 Glu Lys Asn Met Tyr Glu Leu Gln Lys Leu Asn Ser Trp Asp Ile Phe
 20 25 30
 Gly Asn Trp Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 7:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:7
 Leu Glu Ala Asn Ile Ser Gln Ser Leu Glu Gln Ala Gln Ile Gln Gln
 1 5 10 15
 Glu Lys Asn Met Tyr Glu Leu Gln Lys Leu Asn Ser Trp Asp Val Phe
 20 25 30
 Thr Asn Trp Leu
 35
 (2) INFORMATION FOR SEQ ID NO: 8:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 41 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:8
 Cys Gly Gly Asn Asn Leu Leu Arg Ala Ile Glu Ala Gln Gln His Leu
 1 5 10 15
 Leu Gln Leu Thr Val Trp Gly Ile Lys Gln Leu Gln Ala Arg Ile Leu
 20 25 30
 Ala Val Glu Arg Tyr Leu Lys Asp Gln
 35 40
 (2) INFORMATION FOR SEQ ID NO: 9:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 17 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:9
 Leu Gln Ala Arg Ile Leu Ala Val Glu Arg Tyr Leu Lys Asp Gln Gln
 1 5 10 15
 Gln
 (2) INFORMATION FOR SEQ ID NO: 10:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 38 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:10
 Gln Gln Leu Leu Asp Val Val Lys Arg Gln Gln Glu Met Leu Arg Leu
 1 5 10 15
 Thr Val Trp Gly Thr Lys Asn Leu Gln Ala Arg Val Thr Ala Ile Glu
 20 25 30
 Lys Tyr Leu Lys Asp Gln
 35
 (2) INFORMATION FOR SEQ ID NO: 11:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 21 base pairs
 (B) TYPE: nucleic acid
 (C) STRANDEDNESS: single
 (D) TOPOLOGY: linear
 (ii) MOLECULE TYPE: DNA
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:11
 ATGACGCTGA CGGTACAGGC C 21
 (2) INFORMATION FOR SEQ ID NO: 12:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 base pairs
 (B) TYPE: nucleic acid
 (C) STRANDEDNESS: single
 (D) TOPOLOGY: linear
 (ii) MOLECULE TYPE: DNA
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:12
 TGACTAAGCT TAATACCACA GCCAATTTGT TAT 33
 (2) INFORMATION FOR SEQ ID NO: 13:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 22 base pairs
 (B) TYPE: nucleic acid
 (C) STRANDEDNESS: single
 (D) TOPOLOGY: linear
 (ii) MOLECULE TYPE: DNA
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:13
 GGAGCTGCTT GGGGCCCCAG AC 22
 (2) INFORMATION FOR SEQ ID NO: 14:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 40 base pairs
 (B) TYPE: nucleic acid
 (C) STRANDEDNESS: single
 (D) TOPOLOGY: linear
 (ii) MOLECULE TYPE: DNA
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:14
 CCAAATCCCC AGGAGCTGCT CGAGCTGCAC TATACCAGAC 40
 (2) INFORMATION FOR SEQ ID NO: 15:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 base pairs
 (B) TYPE: nucleic acid
 (C) STRANDEDNESS: single
 (D) TOPOLOGY: linear
 (ii) MOLECULE TYPE: DNA
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:15
 ATAGCTTCTA GATTAATTGT TAATTTCTCT GTCCC 35
 (2) INFORMATION FOR SEQ ID NO: 16:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 48 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:16
 Tyr Thr Ser Val Ile Thr Ile Glu Leu Ser Asn Ile Lys Glu Asn Lys
 1 5 10 15
 Cys Asn Gly Thr Asp Ala Lys Val Lys Leu Ile Lys Gln Glu Leu Asp
 20 25 30
 Lys Tyr Lys Asn Ala Val Thr Glu Leu Gln Leu Leu Met Gln Ser Thr
 35 40 45
 (2) INFORMATION FOR SEQ ID NO: 17:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 37 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:17
 Phe Tyr Asp Pro Leu Val Phe Pro Ser Asp Glu Phe Asp Ala Ser Ile
 1 5 10 15
 Ser Gln Val Asn Glu Lys Ile Asn Gln Ser Leu Ala Phe Ile Arg Lys
 20 25 30
 Ser Asp Glu Leu Leu
 35
 (2) INFORMATION FOR SEQ ID NO: 18:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:18
 Ile Thr Leu Asn Asn Ser Val Ala Leu Asp Pro Ile Asp Ile Ser Ile
 1 5 10 15
 Glu Leu Asn Lys Ala Lys Ser Asp Leu Glu Glu Ser Lys Glu Trp Ile
 20 25 30
 Arg Arg Ser
 35
 (2) INFORMATION FOR SEQ ID NO: 19:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 34 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:19
 Ala Leu Gly Val Ala Thr Ser Ala Gln Ile Thr Ala Ala Val Ala Leu
 1 5 10 15
 Val Glu Ala Lys Gln Ala Arg Ser Asp Ile Glu Lys Leu Lys Glu Ala
 20 25 30
 Ile Arg
 (2) INFORMATION FOR SEQ ID NO: 20:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:20
 Val Ala Val Ser Lys Val Leu His Leu Glu Gly Glu Val Asn Lys Ile
 1 5 10 15
 Ala Leu Leu Ser Thr Asn Lys Ala Val Val Ser Leu Ser Asn Gly Val
 20 25 30
 Ser
 (2) INFORMATION FOR SEQ ID NO: 21:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:21
 Ala Val Ser Lys Val Leu His Leu Glu Gly Glu Val Asn Lys Ile Ala
 1 5 10 15
 Leu Leu Ser Thr Asn Lys Ala Val Val Ser Leu Ser Asn Gly Val Ser
 20 25 30
 Val
 (2) INFORMATION FOR SEQ ID NO: 22:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:22
 Val Ser Lys Val Leu His Leu Glu Gly Glu Val Asn Lys Ile Ala Leu
 1 5 10 15
 Leu Ser Thr Asn Lys Ala Val Val Ser Leu Ser Asn Gly Val Ser Val
 20 25 30
 Leu
 (2) INFORMATION FOR SEQ ID NO: 23:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:23
 Ser Lys Val Leu His Leu Glu Gly Glu Val Asn Lys Ile Ala Leu Leu
 1 5 10 15
 Ser Thr Asn Lys Ala Val Val Ser Leu Ser Asn Gly Val Ser Val Leu
 20 25 30
 Thr
 (2) INFORMATION FOR SEQ ID NO: 24:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:24
 Lys Val Leu His Leu Glu Gly Glu Val Asn Lys Ile Ala Leu Leu Ser
 1 5 10 15
 Thr Asn Lys Ala Val Val Ser Leu Ser Asn Gly Val Ser Val Leu Thr
 20 25 30
 Ser
 (2) INFORMATION FOR SEQ ID NO: 25:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:25
 Leu Glu Gly Glu Val Asn Lys Ile Ala Leu Leu Ser Thr Asn Lys Ala
 1 5 10 15
 Val Val Ser Leu Ser Asn Gly Val Ser Val Leu Thr Ser Lys Val Leu
 20 25 30
 Asp
 (2) INFORMATION FOR SEQ ID NO: 26:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:26
 Gly Glu Val Asn Lys Ile Ala Leu Leu Ser Thr Asn Lys Ala Val Val
 1 5 10 15
 Ser Leu Ser Asn Gly Val Ser Val Leu Thr Ser Lys Val Leu Asp Leu
 20 25 30
 Lys
 (2) INFORMATION FOR SEQ ID NO: 27:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:27
 Glu Val Asn Lys Ile Ala Leu Leu Ser Thr Asn Lys Ala Val Val Ser
 1 5 10 15
 Leu Ser Asn Gly Val Ser Val Leu Thr Ser Lys Val Leu Asp Leu Lys
 20 25 30
 Asn
 (2) INFORMATION FOR SEQ ID NO: 28:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:28
 Val Asn Lys Ile Ala Leu Leu Ser Thr Asn Lys Ala Val Val Ser Leu
 1 5 10 15
 Ser Asn Gly Val Ser Val Leu Thr Ser Lys Val Leu Asp Leu Lys Asn
 20 25 30
 Tyr
 (2) INFORMATION FOR SEQ ID NO: 29:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:29
 Asn Lys Ile Ala Leu Leu Ser Thr Asn Lys Ala Val Val Ser Leu Ser
 1 5 10 15
 Asn Gly Val Ser Val Leu Thr Ser Lys Val Leu Asp Leu Lys Asn Tyr
 20 25 30
 Ile
 (2) INFORMATION FOR SEQ ID NO: 30:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:30
 Lys Ile Ala Leu Leu Ser Thr Asn Lys Ala Val Val Ser Leu Ser Asn
 1 5 10 15
 Gly Val Ser Val Leu Thr Ser Lys Val Leu Asp Leu Lys Asn Tyr Ile
 20 25 30
 Asp
 (2) INFORMATION FOR SEQ ID NO: 31:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:31
 Ile Ala Leu Leu Ser Thr Asn Lys Ala Val Val Ser Leu Ser Asn Gly
 1 5 10 15
 Val Ser Val Leu Thr Ser Lys Val Leu Asp Leu Lys Asn Tyr Ile Asp
 20 25 30
 Lys
 (2) INFORMATION FOR SEQ ID NO: 32:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:32
 Ala Leu Leu Ser Thr Asn Lys Ala Val Val Ser Leu Ser Asn Gly Val
 1 5 10 15
 Ser Val Leu Thr Ser Lys Val Leu Asp Leu Lys Asn Tyr Ile Asp Lys
 20 25 30
 Gln
 (2) INFORMATION FOR SEQ ID NO: 33:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:33
 Thr Leu Asn Asn Ser Val Ala Leu Asp Pro Ile Asp Ile Ser Ile Glu
 1 5 10 15
 Leu Asn Lys Ala Lys Ser Asp Leu Glu Glu Ser Lys Glu Trp Ile Arg
 20 25 30
 Arg Ser Asn
 35
 (2) INFORMATION FOR SEQ ID NO: 34:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:34
 Leu Asn Asn Ser Val Ala Leu Asp Pro Ile Asp Ile Ser Ile Glu Leu
 1 5 10 15
 Asn Lys Ala Lys Ser Asp Leu Glu Glu Ser Lys Glu Trp Ile Arg Arg
 20 25 30
 Ser Asn Gln
 35
 (2) INFORMATION FOR SEQ ID NO: 35:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:35
 Asn Asn Ser Val Ala Leu Asp Pro Ile Asp Ile Ser Ile Glu Leu Asn
 1 5 10 15
 Lys Ala Lys Ser Asp Leu Glu Glu Ser Lys Glu Trp Ile Arg Arg Ser
 20 25 30
 Asn Gln Lys
 35
 (2) INFORMATION FOR SEQ ID NO: 36:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:36
 Asn Ser Val Ala Leu Asp Pro Ile Asp Ile Ser Ile Glu Leu Asn Lys
 1 5 10 15
 Ala Lys Ser Asp Leu Glu Glu Ser Lys Glu Trp Ile Arg Arg Ser Asn
 20 25 30
 Gln Lys Leu
 35
 (2) INFORMATION FOR SEQ ID NO: 37:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:37
 Ser Val Ala Leu Asp Pro Ile Asp Ile Ser Ile Glu Leu Asn Lys Ala
 1 5 10 15
 Lys Ser Asp Leu Glu Glu Ser Lys Glu Trp Ile Arg Arg Ser Asn Gln
 20 25 30
 Lys Leu Asp
 35
 (2) INFORMATION FOR SEQ ID NO: 38:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:38
 Val Ala Leu Asp Pro Ile Asp Ile Ser Ile Glu Leu Asn Lys Ala Lys
 1 5 10 15
 Ser Asp Leu Glu Glu Ser Lys Glu Trp Ile Arg Arg Ser Asn Gln Lys
 20 25 30
 Leu Asp Ser
 35
 (2) INFORMATION FOR SEQ ID NO: 39:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:39
 Ala Leu Asp Pro Ile Asp Ile Ser Ile Glu Leu Asn Lys Ala Lys Ser
 1 5 10 15
 Asp Leu Glu Glu Ser Lys Glu Trp Ile Arg Arg Ser Asn Gln Lys Leu
 20 25 30
 Asp Ser Ile
 35
 (2) INFORMATION FOR SEQ ID NO: 40:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:40
 Leu Asp Pro Ile Asp Ile Ser Ile Glu Leu Asn Lys Ala Lys Ser Asp
 1 5 10 15
 Leu Glu Glu Ser Lys Glu Trp Ile Arg Arg Ser Asn Gln Lys Leu Asp
 20 25 30
 Ser Ile Gly
 35
 (2) INFORMATION FOR SEQ ID NO: 41:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:41
 Asp Pro Ile Asp Ile Ser Ile Glu Leu Asn Lys Ala Lys Ser Asp Leu
 1 5 10 15
 Glu Glu Ser Lys Glu Trp Ile Arg Arg Ser Asn Gln Lys Leu Asp Ser
 20 25 30
 Ile Gly Asn
 35
 (2) INFORMATION FOR SEQ ID NO: 42:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:42
 Pro Ile Asp Ile Ser Ile Glu Leu Asn Lys Ala Lys Ser Asp Leu Glu
 1 5 10 15
 Glu Ser Lys Glu Trp Ile Arg Arg Ser Asn Gln Lys Leu Asp Ser Ile
 20 25 30
 Gly Asn Trp
 35
 (2) INFORMATION FOR SEQ ID NO: 43:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:43
 Ile Asp Ile Ser Ile Glu Leu Asn Lys Ala Lys Ser Asp Leu Glu Glu
 1 5 10 15
 Ser Lys Glu Trp Ile Arg Arg Ser Asn Gln Lys Leu Asp Ser Ile Gly
 20 25 30
 Asn Trp His
 35
 (2) INFORMATION FOR SEQ ID NO: 44:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:44
 Asp Ile Ser Ile Glu Leu Asn Lys Ala Lys Ser Asp Leu Glu Glu Ser
 1 5 10 15
 Lys Glu Trp Ile Arg Arg Ser Asn Gln Lys Leu Asp Ser Ile Gly Asn
 20 25 30
 Trp His Gln
 35
 (2) INFORMATION FOR SEQ ID NO: 45:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:45
 Ile Ser Ile Glu Leu Asn Lys Ala Lys Ser Asp Leu Glu Glu Ser Lys
 1 5 10 15
 Glu Trp Ile Arg Arg Ser Asn Gln Lys Leu Asp Ser Ile Gly Asn Trp
 20 25 30
 His Gln Ser
 35
 (2) INFORMATION FOR SEQ ID NO: 46:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:46
 Ser Ile Glu Leu Asn Lys Ala Lys Ser Asp Leu Glu Glu Ser Lys Glu
 1 5 10 15
 Trp Ile Arg Arg Ser Asn Gln Lys Leu Asp Ser Ile Gly Asn Trp His
 20 25 30
 Gln Ser Ser
 35
 (2) INFORMATION FOR SEQ ID NO: 47:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:47
 Ile Glu Leu Asn Lys Ala Lys Ser Asp Leu Glu Glu Ser Lys Glu Trp
 1 5 10 15
 Ile Arg Arg Ser Asn Gln Lys Leu Asp Ser Ile Gly Asn Trp His Gln
 20 25 30
 Ser Ser Thr
 35
 (2) INFORMATION FOR SEQ ID NO: 48:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:48
 Glu Leu Asn Lys Ala Lys Ser Asp Leu Glu Glu Ser Lys Glu Trp Ile
 1 5 10 15
 Arg Arg Ser Asn Gln Lys Leu Asp Ser Ile Gly Asn Trp His Gln Ser
 20 25 30
 Ser Thr Thr
 35
 (2) INFORMATION FOR SEQ ID NO: 49:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:49
 Thr Ala Ala Val Ala Leu Val Glu Ala Lys Gln Ala Arg Ser Asp Ile
 1 5 10 15
 Glu Lys Leu Lys Glu Ala Ile Arg Asp Thr Asn Lys Ala Val Gln Ser
 20 25 30
 Val Gln Ser
 35
 (2) INFORMATION FOR SEQ ID NO: 50:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:50
 Ala Val Ala Leu Val Glu Ala Lys Gln Ala Arg Ser Asp Ile Glu Lys
 1 5 10 15
 Leu Lys Glu Ala Ile Arg Asp Thr Asn Lys Ala Val Gln Ser Val Gln
 20 25 30
 Ser Ser Ile
 35
 (2) INFORMATION FOR SEQ ID NO: 51:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:51
 Leu Val Glu Ala Lys Gln Ala Arg Ser Asp Ile Glu Lys Leu Lys Glu
 1 5 10 15
 Ala Ile Arg Asp Thr Asn Lys Ala Val Gln Ser Val Gln Ser Ser Ile
 20 25 30
 Gly Asn Leu
 35
 (2) INFORMATION FOR SEQ ID NO: 52:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:52
 Val Glu Ala Lys Gln Ala Arg Ser Asp Ile Glu Lys Leu Lys Glu Ala
 1 5 10 15
 Ile Arg Asp Thr Asn Lys Ala Val Gln Ser Val Gln Ser Ser Ile Gly
 20 25 30
 Asn Leu Ile
 35
 (2) INFORMATION FOR SEQ ID NO: 53:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:53
 Glu Ala Lys Gln Ala Arg Ser Asp Ile Glu Lys Leu Lys Glu Ala Ile
 1 5 10 15
 Arg Asp Thr Asn Lys Ala Val Gln Ser Val Gln Ser Ser Ile Gly Asn
 20 25 30
 Leu Ile Val
 35
 (2) INFORMATION FOR SEQ ID NO: 54:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:54
 Ala Lys Gln Ala Arg Ser Asp Ile Glu Lys Leu Lys Glu Ala Ile Arg
 1 5 10 15
 Asp Thr Asn Lys Ala Val Gln Ser Val Gln Ser Ser Ile Gly Asn Leu
 20 25 30
 Ile Val Ala
 35
 (2) INFORMATION FOR SEQ ID NO: 55:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:55
 Lys Gln Ala Arg Ser Asp Ile Glu Lys Leu Lys Glu Ala Ile Arg Asp
 1 5 10 15
 Thr Asn Lys Ala Val Gln Ser Val Gln Ser Ser Ile Gly Asn Leu Ile
 20 25 30
 Val Ala Ile
 35
 (2) INFORMATION FOR SEQ ID NO: 56:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:56
 Gln Ala Arg Ser Asp Ile Glu Lys Leu Lys Glu Ala Ile Arg Asp Thr
 1 5 10 15
 Asn Lys Ala Val Gln Ser Val Gln Ser Ser Ile Gly Asn Leu Ile Val
 20 25 30
 Ala Ile Lys
 35
 (2) INFORMATION FOR SEQ ID NO: 57:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:57
 Ala Arg Ser Asp Ile Glu Lys Leu Lys Glu Ala Ile Arg Asp Thr Asn
 1 5 10 15
 Lys Ala Val Gln Ser Val Gln Ser Ser Ile Gly Asn Leu Ile Val Ala
 20 25 30
 Ile Lys Ser
 35
 (2) INFORMATION FOR SEQ ID NO: 58:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:58
 Arg Ser Asp Ile Glu Lys Leu Lys Glu Ala Ile Arg Asp Thr Asn Lys
 1 5 10 15
 Ala Val Gln Ser Val Gln Ser Ser Ile Gly Asn Leu Ile Val Ala Ile
 20 25 30
 Lys Ser Val
 35
 (2) INFORMATION FOR SEQ ID NO: 59:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:59
 Ser Asp Ile Glu Lys Leu Lys Glu Ala Ile Arg Asp Thr Asn Lys Ala
 1 5 10 15
 Val Gln Ser Val Gln Ser Ser Ile Gly Asn Leu Ile Val Ala Ile Lys
 20 25 30
 Ser Val Gln
 35
 (2) INFORMATION FOR SEQ ID NO: 60:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:60
 Lys Leu Lys Glu Ala Ile Arg Asp Thr Asn Lys Ala Val Gln Ser Val
 1 5 10 15
 Gln Ser Ser Ile Gly Asn Leu Ile Val Ala Ile Lys Ser Val Gln Asp
 20 25 30
 Tyr Val Asn
 35
 (2) INFORMATION FOR SEQ ID NO: 61:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:61
 Leu Lys Glu Ala Ile Arg Asp Thr Asn Lys Ala Val Gln Ser Val Gln
 1 5 10 15
 Ser Ser Ile Gly Asn Leu Ile Val Ala Ile Lys Ser Val Gln Asp Tyr
 20 25 30
 Val Asn Lys
 35
 (2) INFORMATION FOR SEQ ID NO: 62:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:62
 Ala Ile Arg Asp Thr Asn Lys Ala Val Gln Ser Val Gln Ser Ser Ile
 1 5 10 15
 Gly Asn Leu Ile Val Ala Ile Lys Ser Val Gln Asp Tyr Val Asn Lys
 20 25 30
 Glu Ile Val
 35
 (2) INFORMATION FOR SEQ ID NO: 63:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:63
 Trp Gln Glu Trp Glu Arg Lys Val Asp Phe Leu Glu Glu Asn Ile Thr
 1 5 10 15
 Ala Leu Leu Glu Glu Ala Gln Ile Gln Gln Glu Lys Asn Met Tyr Glu
 20 25 30
 Leu Gln Lys
 35
 (2) INFORMATION FOR SEQ ID NO: 64:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:64
 Gln Glu Trp Glu Arg Lys Val Asp Phe Leu Glu Glu Asn Ile Thr Ala
 1 5 10 15
 Leu Leu Glu Glu Ala Gln Ile Gln Gln Glu Lys Asn Met Tyr Glu Leu
 20 25 30
 Gln Lys Leu
 35
 (2) INFORMATION FOR SEQ ID NO: 65:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:65
 Glu Trp Glu Arg Lys Val Asp Phe Leu Glu Glu Asn Ile Thr Ala Leu
 1 5 10 15
 Leu Glu Glu Ala Gln Ile Gln Gln Glu Lys Asn Met Tyr Glu Leu Gln
 20 25 30
 Lys Leu Asn
 35
 (2) INFORMATION FOR SEQ ID NO: 66:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:66
 Trp Glu Arg Lys Val Asp Phe Leu Glu Glu Asn Ile Thr Ala Leu Leu
 1 5 10 15
 Glu Glu Ala Gln Ile Gln Gln Glu Lys Asn Met Tyr Glu Leu Gln Lys
 20 25 30
 Leu Asn Ser
 35
 (2) INFORMATION FOR SEQ ID NO: 67:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:67
 Glu Arg Lys Val Asp Phe Leu Glu Glu Asn Ile Thr Ala Leu Leu Glu
 1 5 10 15
 Glu Ala Gln Ile Gln Gln Glu Lys Asn Met Tyr Glu Leu Gln Lys Leu
 20 25 30
 Asn Ser Trp
 35
 (2) INFORMATION FOR SEQ ID NO: 68:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:68
 Arg Lys Val Asp Phe Leu Glu Glu Asn Ile Thr Ala Leu Leu Glu Glu
 1 5 10 15
 Ala Gln Ile Gln Gln Glu Lys Asn Met Tyr Glu Leu Gln Lys Leu Asn
 20 25 30
 Ser Trp Asp
 35
 (2) INFORMATION FOR SEQ ID NO: 69:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:69
 Lys Val Asp Phe Leu Glu Glu Asn Ile Thr Ala Leu Leu Glu Glu Ala
 1 5 10 15
 Gln Ile Gln Gln Glu Lys Asn Met Tyr Glu Leu Gln Lys Leu Asn Ser
 20 25 30
 Trp Asp Val
 35
 (2) INFORMATION FOR SEQ ID NO: 70:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:70
 Val Asp Phe Leu Glu Glu Asn Ile Thr Ala Leu Leu Glu Glu Ala Gln
 1 5 10 15
 Ile Gln Gln Glu Lys Asn Met Tyr Glu Leu Gln Lys Leu Asn Ser Trp
 20 25 30
 Asp Val Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 71:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:71
 Asp Phe Leu Glu Glu Asn Ile Thr Ala Leu Leu Glu Glu Ala Gln Ile
 1 5 10 15
 Gln Gln Glu Lys Asn Met Tyr Glu Leu Gln Lys Leu Asn Ser Trp Asp
 20 25 30
 Val Phe Gly
 35
 (2) INFORMATION FOR SEQ ID NO: 72:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:72
 Phe Leu Glu Glu Asn Ile Thr Ala Leu Leu Glu Glu Ala Gln Ile Gln
 1 5 10 15
 Gln Glu Lys Asn Met Tyr Glu Leu Gln Lys Leu Asn Ser Trp Asp Val
 20 25 30
 Phe Gly Asn
 35
 (2) INFORMATION FOR SEQ ID NO: 73:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 34 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:73
 Leu His Arg Ile Asp Leu Gly Pro Pro Ile Ser Leu Glu Arg Leu Asp
 1 5 10 15
 Val Gly Thr Asn Leu Gly Asn Ala Ile Ala Lys Leu Glu Ala Lys Glu
 20 25 30
 Leu Leu
 (2) INFORMATION FOR SEQ ID NO: 74:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 34 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:74
 His Arg Ile Asp Leu Gly Pro Pro Ile Ser Leu Glu Arg Leu Asp Val
 1 5 10 15
 Gly Thr Asn Leu Gly Asn Ala Ile Ala Lys Leu Glu Ala Lys Glu Leu
 20 25 30
 Leu Glu
 (2) INFORMATION FOR SEQ ID NO: 75:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 34 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:75
 Arg Ile Asp Leu Gly Pro Pro Ile Ser Leu Glu Arg Leu Asp Val Gly
 1 5 10 15
 Thr Asn Leu Gly Asn Ala Ile Ala Lys Leu Glu Ala Lys Glu Leu Leu
 20 25 30
 Glu Ser
 (2) INFORMATION FOR SEQ ID NO: 76:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 34 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:76
 Ile Asp Leu Gly Pro Pro Ile Ser Leu Glu Arg Leu Asp Val Gly Thr
 1 5 10 15
 Asn Leu Gly Asn Ala Ile Ala Lys Leu Glu Ala Lys Glu Leu Leu Glu
 20 25 30
 Ser Ser
 (2) INFORMATION FOR SEQ ID NO: 77:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 34 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:77
 Asp Leu Gly Pro Pro Ile Ser Leu Glu Arg Leu Asp Val Gly Thr Asn
 1 5 10 15
 Leu Gly Asn Ala Ile Ala Lys Leu Glu Ala Lys Glu Leu Leu Glu Ser
 20 25 30
 Ser Asp
 (2) INFORMATION FOR SEQ ID NO: 78:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 34 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:78
 Leu Gly Pro Pro Ile Ser Leu Glu Arg Leu Asp Val Gly Thr Asn Leu
 1 5 10 15
 Gly Asn Ala Ile Ala Lys Leu Glu Ala Lys Glu Leu Leu Glu Ser Ser
 20 25 30
 Asp Gln
 (2) INFORMATION FOR SEQ ID NO: 79:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 34 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:79
 Gly Pro Pro Ile Ser Leu Glu Arg Leu Asp Val Gly Thr Asn Leu Gly
 1 5 10 15
 Asn Ala Ile Ala Lys Leu Glu Ala Lys Glu Leu Leu Glu Ser Ser Asp
 20 25 30
 Gln Ile
 (2) INFORMATION FOR SEQ ID NO: 80:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 34 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:80
 Pro Pro Ile Ser Leu Glu Arg Leu Asp Val Gly Thr Asn Leu Gly Asn
 1 5 10 15
 Ala Ile Ala Lys Leu Glu Ala Lys Glu Leu Leu Glu Ser Ser Asp Gln
 20 25 30
 Ile Leu
 (2) INFORMATION FOR SEQ ID NO: 81:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 34 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:81
 Pro Ile Ser Leu Glu Arg Leu Asp Val Gly Thr Asn Leu Gly Asn Ala
 1 5 10 15
 Ile Ala Lys Leu Glu Ala Lys Glu Leu Leu Glu Ser Ser Asp Gln Ile
 20 25 30
 Leu Arg
 (2) INFORMATION FOR SEQ ID NO: 82:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 34 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:82
 Ser Leu Glu Arg Leu Asp Val Gly Thr Asn Leu Gly Asn Ala Ile Ala
 1 5 10 15
 Lys Leu Glu Ala Lys Glu Leu Leu Glu Ser Ser Asp Gln Ile Leu Arg
 20 25 30
 Ser Met
 (2) INFORMATION FOR SEQ ID NO: 83:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 34 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /label= A
 /note= "Preceeding this amino acid, there may be an amino
 group, a hydrophobic group, an acetyl group, a
 9-fluorenylmethoxycarbonyl group, or a macromolecular
 carrier group."
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 48
 (D) OTHER INFORMATION: /label= B
 /note= "Following this amino acid, there may be a
 carboxyl group, an amido group, a T-butyloxycarbonyl
 group, or a macromolecular carrier group."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:83
 Leu Glu Arg Leu Asp Val Gly Thr Asn Leu Gly Asn Ala Ile Ala Lys
 1 5 10 15
 Leu Glu Ala Lys Glu Leu Leu Glu Ser Ser Asp Gln Ile Leu Arg Ser
 20 25 30
 Met Lys
 (2) INFORMATION FOR SEQ ID NO: 84:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 28 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:84
 Met Lys Gln Leu Glu Asp Lys Val Glu Glu Leu Leu Ser Lys Asn Tyr
 1 5 10 15
 His Leu Glu Asn Glu Val Ala Arg Leu Lys Lys Leu
 20 25
 (2) INFORMATION FOR SEQ ID NO: 85:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 28 amino acids
 (B) TYPE: am
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:85
 Thr Asp Thr Leu Gln Ala Glu Thr Asp Gln Leu Glu Asp Glu Lys Ser
 1 5 10 15
 Ala Leu Gln Thr Glu Ile Ala Asn Leu Leu Lys Glu
 20 25
 (2) INFORMATION FOR SEQ ID NO: 86:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 28 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:86
 Ile Ala Arg Leu Glu Glu Lys Val Lys Thr Leu Lys Ala Gln Asn Ser
 1 5 10 15
 Glu Leu Ala Ser Thr Ala Asn Met Leu Arg Glu Gln
 20 25
 (2) INFORMATION FOR SEQ ID NO: 87:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 28 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:87
 Glu Gln Lys Leu Ile Ser Glu Glu Asp Leu Leu Glu Lys Arg Arg Glu
 1 5 10 15
 Gln Leu Lys His Lys Leu Glu Gln Leu Arg Asn Ser
 20 25
 (2) INFORMATION FOR SEQ ID NO: 88:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 28 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:88
 Ile Glu Lys Thr Asn Glu Lys Phe His Gln Ile Glu Lys Glu Phe Ser
 1 5 10 15
 Glu Val Glu Gly Arg Ile Gln Asp Leu Glu Lys Tyr
 20 25
 (2) INFORMATION FOR SEQ ID NO: 89:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 38 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:89
 Asn Asn Leu Leu Arg Ala Ile Glu Ala Gln Gln His Leu Leu Gln Leu
 1 5 10 15
 Thr Val Trp Gly Ile Lys Gln Leu Gln Ala Arg Ile Leu Ala Val Glu
 20 25 30
 Arg Tyr Leu Lys Asp Gln
 35
 (2) INFORMATION FOR SEQ ID NO: 90:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 338 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: protein
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:90
 Phe Leu Gly Phe Leu Gly Ala Ala Gly Ser Thr Met Gly Ala Arg Ser
 1 5 10 15
 Met Thr Leu Thr Val Gln Ala Arg Gln Leu Leu Ser Gly Ile Val Gln
 20 25 30
 Gln Gln Asn Asn Leu Leu Arg Ala Ile Glu Ala Gln Gln His Leu Leu
 35 40 45
 Gln Leu Thr Val Trp Gly Ile Lys Gln Leu Gln Ala Arg Ile Leu Ala
 50 55 60
 Val Glu Arg Tyr Leu Lys Asp Gln Gln Leu Leu Gly Ile Trp Gly Cys
 65 70 75 80
 Ser Gly Lys Leu Ile Cys Thr Thr Ala Val Pro Trp Asn Ala Ser Trp
 85 90 95
 Ser Asn Lys Ser Leu Glu Gln Ile Trp Asn Asn Met Thr Trp Met Glu
 100 105 110
 Trp Asp Arg Glu Ile Asn Asn Tyr Thr Ser Leu Ile His Ser Leu Ile
 115 120 125
 Glu Glu Ser Gln Asn Gln Gln Glu Lys Asn Glu Gln Glu Leu Leu Glu
 130 135 140
 Leu Asp Lys Trp Ala Ser Leu Trp Asn Trp Phe Asn Ile Thr Asn Trp
 145 150 155 160
 Leu Trp Tyr Ile Lys Ile Phe Ile Met Ile Val Gly Gly Leu Val Gly
 165 170 175
 Leu Arg Ile Val Phe Ala Val Leu Ser Ile Val Asn Arg Val Arg Gln
 180 185 190
 Gly Tyr Ser Pro Leu Ser Phe Gln Thr His Leu Pro Thr Pro Arg Gly
 195 200 205
 Pro Asp Arg Pro Glu Gly Ile Glu Glu Glu Gly Gly Glu Arg Asp Arg
 210 215 220
 Asp Arg Ser Ile Arg Leu Val Asn Gly Ser Leu Ala Leu Ile Trp Asp
 225 230 235 240
 Asp Leu Arg Ser Leu Cys Leu Phe Ser Tyr His Arg Leu Arg Asp Leu
 245 250 255
 Leu Leu Ile Val Thr Arg Ile Val Glu Leu Leu Gly Arg Arg Gly Trp
 260 265 270
 Glu Ala Leu Lys Tyr Trp Trp Asn Leu Leu Gln Tyr Trp Ser Gln Glu
 275 280 285
 Leu Lys Asn Ser Ala Val Ser Leu Leu Asn Ala Thr Ala Ile Ala Val
 290 295 300
 Ala Glu Gly Thr Asp Arg Val Ile Glu Val Val Gln Gly Ala Cys Arg
 305 310 315 320
 Ala Ile Arg His Ile Pro Arg Arg Ile Arg Gln Gly Leu Glu Arg Ile
 325 330 335
 Leu Leu
 (2) INFORMATION FOR SEQ ID NO: 91:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 437 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: protein
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:91
 Phe Leu Gly Phe Leu Leu Gly Val Gly Ser Ala Ile Ala Ser Gly Val
 1 5 10 15
 Ala Val Ser Lys Val Leu His Leu Glu Gly Glu Val Asn Lys Ile Lys
 20 25 30
 Ser Ala Leu Leu Ser Thr Asn Lys Ala Val Val Ser Leu Ser Asn Gly
 35 40 45
 Val Ser Val Leu Thr Ser Lys Val Leu Asp Leu Lys Asn Tyr Ile Asp
 50 55 60
 Lys Gln Leu Leu Pro Ile Val Asn Lys Gln Ser Cys Ser Ile Ser Asn
 65 70 75 80
 Ile Glu Thr Val Ile Glu Phe Gln Gln Lys Asn Asn Arg Leu Leu Glu
 85 90 95
 Ile Thr Arg Glu Phe Ser Val Asn Ala Gly Val Thr Thr Pro Val Ser
 100 105 110
 Thr Met Leu Thr Asn Ser Glu Leu Leu Ser Leu Ile Asn Asp Met Pro
 115 120 125
 Ile Thr Asn Asp Gln Lys Lys Leu Met Ser Asn Asn Val Gln Ile Val
 130 135 140
 Arg Gln Gln Ser Tyr Ser Ile Met Ser Ile Ile Lys Glu Glu Val Leu
 145 150 155 160
 Ala Tyr Val Val Gln Leu Pro Leu Tyr Gly Val Ile Asp Thr Pro Cys
 165 170 175
 Trp Lys Leu His Thr Ser Pro Leu Cys Thr Thr Asn Thr Lys Glu Gly
 180 185 190
 Ser Asn Ile Cys Leu Thr Arg Thr Asp Arg Gly Trp Tyr Cys Asp Asn
 195 200 205
 Ala Gly Ser Val Ser Phe Phe Pro Gln Ala Glu Thr Cys Lys Val Gln
 210 215 220
 Ser Asn Arg Val Phe Cys Asp Thr Met Asn Ser Leu Thr Leu Pro Ser
 225 230 235 240
 Glu Ile Asn Leu Cys Asn Val Asp Ile Phe Asn Pro Lys Tyr Asp Cys
 245 250 255
 Lys Ile Met Thr Ser Lys Thr Asp Val Ser Ser Ser Val Ile Thr Ser
 260 265 270
 Leu Gly Ala Ile Val Ser Cys Tyr Gly Lys Thr Lys Cys Thr Ala Ser
 275 280 285
 Asn Lys Asn Arg Gly Ile Ile Lys Thr Phe Ser Asn Gly Cys Asp Tyr
 290 295 300
 Val Ser Asn Lys Gly Met Asp Thr Val Ser Val Gly Asn Thr Leu Tyr
 305 310 315 320
 Tyr Val Asn Lys Gln Glu Gly Lys Ser Leu Tyr Val Lys Gly Glu Pro
 325 330 335
 Ile Ile Asn Phe Tyr Asp Pro Leu Val Phe Pro Ser Asp Glu Phe Asp
 340 345 350
 Ala Ser Ile Ser Gln Val Asn Glu Lys Ile Asn Gln Ser Leu Ala Phe
 355 360 365
 Ile Arg Lys Ser Asp Glu Leu Leu His Asn Val Asn Ala Gly Lys Ser
 370 375 380
 Thr Thr Asn Ile Met Ile Thr Thr Ile Ile Ile Val Ile Ile Val Ile
 385 390 395 400
 Leu Leu Ser Leu Ile Ala Val Gly Leu Leu Leu Tyr Cys Lys Ala Arg
 405 410 415
 Ser Thr Pro Val Thr Leu Ser Lys Asp Gln Leu Ser Gly Ile Asn Asn
 420 425 430
 Ile Ala Phe Ser Asn
 435
 (2) INFORMATION FOR SEQ ID NO: 92:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 328 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: protein
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:92
 Phe Leu Gly Phe Leu Gly Ala Ala Gly Thr Ala Met Gly Ala Ala Ala
 1 5 10 15
 Thr Ala Leu Thr Val Gln Ser Gln His Leu Leu Ala Gly Ile Leu Gln
 20 25 30
 Gln Gln Lys Asn Leu Leu Ala Ala Val Glu Ala Gln Gln Gln Met Leu
 35 40 45
 Lys Leu Thr Ile Trp Gly Val Lys Asn Leu Asn Ala Arg Val Thr Ala
 50 55 60
 Leu Glu Lys Tyr Leu Glu Asp Gln Ala Arg Leu Asn Ala Trp Gly Cys
 65 70 75 80
 Ala Trp Lys Gln Val Cys His Thr Thr Val Pro Trp Gln Trp Asn Asn
 85 90 95
 Arg Thr Pro Asp Trp Asn Asn Met Thr Trp Leu Glu Trp Glu Arg Gln
 100 105 110
 Ile Ser Tyr Leu Glu Gly Asn Ile Thr Thr Gln Leu Glu Glu Ala Arg
 115 120 125
 Ala Gln Glu Glu Lys Asn Leu Asp Ala Tyr Gln Lys Leu Ser Ser Trp
 130 135 140
 Ser Asp Phe Trp Ser Trp Phe Asp Phe Ser Lys Trp Leu Asn Ile Leu
 145 150 155 160
 Lys Ile Gly Phe Leu Asp Val Leu Gly Ile Ile Gly Leu Arg Leu Leu
 165 170 175
 Tyr Thr Val Tyr Ser Cys Ile Ala Arg Val Arg Gln Gly Tyr Ser Pro
 180 185 190
 Leu Ser Pro Gln Ile His Ile His Pro Trp Lys Gly Gln Pro Asp Asn
 195 200 205
 Ala Glu Gly Pro Gly Glu Gly Gly Asp Lys Arg Lys Asn Ser Ser Glu
 210 215 220
 Pro Trp Gln Lys Glu Ser Gly Thr Ala Glu Trp Lys Ser Asn Trp Cys
 225 230 235 240
 Lys Arg Leu Thr Asn Trp Cys Ser Ile Ser Ser Ile Trp Leu Tyr Asn
 245 250 255
 Ser Cys Leu Thr Leu Leu Val His Leu Arg Ser Ala Phe Gln Tyr Ile
 260 265 270
 Gln Tyr Gly Leu Gly Glu Leu Lys Ala Ala Ala Gln Glu Ala Val Val
 275 280 285
 Ala Leu Ala Arg Leu Ala Gln Asn Ala Gly Tyr Gln Ile Trp Leu Ala
 290 295 300
 Cys Arg Ser Ala Tyr Arg Ala Ile Ile Asn Ser Pro Arg Arg Val Arg
 305 310 315 320
 Gln Gly Leu Glu Gly Ile Leu Asn
 325
 (2) INFORMATION FOR SEQ ID NO: 93:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 438 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: protein
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:93
 Phe Ala Gly Val Val Leu Ala Gly Val Ala Leu Gly Val Ala Thr Ala
 1 5 10 15
 Ala Gln Ile Thr Ala Gly Ile Ala Leu His Gln Ser Asn Leu Asn Ala
 20 25 30
 Gln Ala Ile Gln Ser Leu Arg Thr Ser Leu Glu Gln Ser Asn Lys Ala
 35 40 45
 Ile Glu Glu Ile Arg Glu Ala Thr Gln Glu Thr Val Ile Ala Val Gln
 50 55 60
 Gly Val Gln Asp Tyr Val Asn Asn Glu Leu Val Pro Ala Met Gln His
 65 70 75 80
 Met Ser Cys Glu Leu Val Gly Gln Arg Leu Gly Leu Arg Leu Leu Arg
 85 90 95
 Tyr Tyr Thr Glu Leu Leu Ser Ile Phe Gly Pro Ser Leu Arg Asp Pro
 100 105 110
 Ile Ser Ala Glu Ile Ser Ile Gln Ala Leu Ile Tyr Ala Leu Gly Gly
 115 120 125
 Glu Ile His Lys Ile Leu Glu Lys Leu Gly Tyr Ser Gly Ser Asp Met
 130 135 140
 Ile Ala Ile Leu Glu Ser Arg Gly Ile Lys Thr Lys Ile Thr His Val
 145 150 155 160
 Asp Leu Pro Gly Lys Phe Ile Ile Leu Ser Ile Ser Tyr Pro Thr Leu
 165 170 175
 Ser Glu Val Lys Gly Val Ile Val His Arg Leu Glu Ala Val Ser Tyr
 180 185 190
 Asn Ile Gly Ser Gln Glu Trp Tyr Thr Thr Val Pro Arg Tyr Ile Ala
 195 200 205
 Thr Asn Gly Tyr Leu Ile Ser Asn Phe Asp Glu Ser Ser Cys Val Phe
 210 215 220
 Val Ser Glu Ser Ala Ile Cys Ser Gln Asn Ser Leu Tyr Pro Met Ser
 225 230 235 240
 Pro Leu Leu Gln Gln Cys Ile Arg Gly Asp Thr Ser Ser Cys Ala Arg
 245 250 255
 Thr Leu Val Ser Gly Thr Met Gly Asn Lys Phe Ile Leu Ser Lys Gly
 260 265 270
 Asn Ile Val Ala Asn Cys Ala Ser Ile Leu Cys Lys Cys Tyr Ser Thr
 275 280 285
 Ser Thr Ile Ile Asn Gln Ser Pro Asp Lys Leu Leu Thr Phe Ile Ala
 290 295 300
 Ser Asp Thr Cys Pro Leu Val Glu Ile Asp Gly Ala Thr Ile Gln Val
 305 310 315 320
 Gly Gly Arg Gln Tyr Pro Asp Met Val Tyr Glu Gly Lys Val Ala Leu
 325 330 335
 Gly Pro Ala Ile Ser Leu Asp Arg Leu Asp Val Gly Thr Asn Leu Gly
 340 345 350
 Asn Ala Leu Lys Lys Leu Asp Asp Ala Lys Val Leu Ile Asp Ser Ser
 355 360 365
 Asn Gln Ile Leu Glu Thr Val Arg Arg Ser Ser Phe Asn Phe Gly Ser
 370 375 380
 Leu Leu Ser Val Pro Ile Leu Ser Cys Thr Ala Leu Ala Leu Leu Leu
 385 390 395 400
 Leu Ile Tyr Cys Cys Lys Arg Arg Tyr Gln Gln Thr Leu Lys Gln His
 405 410 415
 Thr Lys Val Asp Pro Ala Phe Lys Pro Asp Leu Thr Gly Thr Ser Lys
 420 425 430
 Ser Tyr Val Arg Ser Leu
 435
 (2) INFORMATION FOR SEQ ID NO: 94:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 436 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: protein
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:94
 Phe Ile Gly Ala Ile Ile Gly Ser Val Ala Leu Gly Val Ala Thr Ala
 1 5 10 15
 Ala Gln Ile Thr Ala Ala Ser Ala Leu Ile Gln Ala Asn Gln Asn Ala
 20 25 30
 Ala Asn Ile Leu Arg Leu Lys Glu Ser Ile Thr Ala Thr Ile Glu Ala
 35 40 45
 Val His Glu Val Thr Asp Gly Leu Ser Gln Leu Ala Val Ala Val Gly
 50 55 60
 Lys Met Gln Gln Phe Val Asn Asp Gln Phe Asn Asn Thr Ala Gln Glu
 65 70 75 80
 Leu Asp Cys Ile Lys Ile Thr Gln Gln Val Gly Val Glu Leu Asn Leu
 85 90 95
 Tyr Leu Thr Glu Leu Thr Thr Val Phe Gly Pro Gln Ile Thr Ser Pro
 100 105 110
 Ala Leu Thr Gln Leu Thr Ile Gln Ala Leu Tyr Asn Ala Gly Gly Asn
 115 120 125
 Met Asp Tyr Leu Leu Thr Lys Leu Gly Val Gly Asn Asn Gln Leu Ser
 130 135 140
 Ser Leu Ile Gly Ser Gly Leu Ile Thr Gly Asn Pro Ile Leu Tyr Asp
 145 150 155 160
 Ser Gln Thr Gln Leu Leu Gly Ile Gln Val Thr Leu Pro Ser Val Gly
 165 170 175
 Asn Leu Asn Asn Met Arg Ala Thr Tyr Leu Glu Thr Leu Ser Val Ser
 180 185 190
 Thr Thr Lys Gly Phe Ala Ser Ala Leu Val Pro Lys Val Val Thr Gln
 195 200 205
 Val Gly Ser Val Ile Glu Glu Leu Asp Thr Ser Tyr Cys Ile Glu Thr
 210 215 220
 Asp Leu Asp Leu Tyr Cys Thr Arg Ile Val Thr Phe Pro Met Ser Pro
 225 230 235 240
 Gly Ile Tyr Ser Cys Leu Asn Gly Asn Thr Ser Ala Cys Met Tyr Ser
 245 250 255
 Lys Thr Glu Gly Ala Leu Thr Thr Pro Tyr Met Thr Leu Lys Gly Ser
 260 265 270
 Val Ile Ala Asn Cys Lys Met Thr Thr Cys Arg Cys Ala Asp Pro Pro
 275 280 285
 Gly Ile Ile Ser Gln Asn Tyr Gly Glu Ala Val Ser Leu Ile Asp Arg
 290 295 300
 His Ser Cys Asn Val Leu Ser Leu Asp Gly Ile Thr Leu Arg Leu Ser
 305 310 315 320
 Gly Glu Phe Asp Ala Thr Tyr Gln Lys Asn Ile Ser Ile Leu Asp Ser
 325 330 335
 Gln Val Ile Val Thr Gly Asn Leu Asp Ile Ser Thr Glu Leu Gly Asn
 340 345 350
 Val Asn Asn Ser Ile Ser Asn Ala Leu Asp Lys Leu Glu Glu Ser Asn
 355 360 365
 Ser Lys Leu Asp Lys Val Asn Val Lys Leu Thr Ser Thr Ser Ala Leu
 370 375 380
 Ile Thr Tyr Ile Ala Leu Thr Ala Ile Ser Leu Val Cys Gly Ile Leu
 385 390 395 400
 Ser Leu Val Leu Ala Cys Tyr Leu Met Tyr Lys Gln Lys Ala Gln Gln
 405 410 415
 Lys Thr Leu Leu Trp Leu Gly Asn Asn Thr Leu Gly Gln Met Arg Ala
 420 425 430
 Thr Thr Lys Met
 435
 (2) INFORMATION FOR SEQ ID NO: 95:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 430 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: protein
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:95
 Phe Phe Gly Gly Val Ile Gly Thr Ile Ala Leu Gly Val Ala Thr Ser
 1 5 10 15
 Ala Gln Ile Thr Ala Ala Val Ala Leu Val Glu Ala Lys Gln Ala Arg
 20 25 30
 Ser Asp Ile Glu Lys Leu Lys Glu Ala Ile Arg Asp Thr Asn Lys Ala
 35 40 45
 Val Gln Ser Val Gln Ser Ser Ile Gly Asn Leu Ile Val Ala Ile Lys
 50 55 60
 Ser Val Gln Asp Tyr Val Asn Lys Glu Ile Val Pro Ser Ile Ala Arg
 65 70 75 80
 Leu Gly Cys Glu Ala Ala Gly Leu Gln Leu Gly Ile Ala Leu Thr Gln
 85 90 95
 His Tyr Ser Glu Leu Thr Asn Ile Phe Gly Asp Asn Ile Gly Ser Leu
 100 105 110
 Gln Glu Lys Gly Ile Lys Leu Gln Gly Ile Ala Ser Leu Tyr Arg Thr
 115 120 125
 Asn Ile Thr Glu Ile Phe Thr Thr Ser Thr Val Asp Lys Tyr Asp Ile
 130 135 140
 Tyr Asp Leu Leu Phe Thr Glu Ser Ile Lys Val Arg Val Ile Asp Val
 145 150 155 160
 Asp Leu Asn Asp Tyr Ser Ile Thr Leu Gln Val Arg Leu Pro Leu Leu
 165 170 175
 Thr Arg Leu Leu Asn Thr Gln Ile Tyr Arg Val Asp Ser Ile Ser Tyr
 180 185 190
 Asn Ile Gln Asn Arg Glu Trp Tyr Ile Pro Leu Pro Ser His Ile Met
 195 200 205
 Thr Lys Gly Ala Phe Leu Gly Gly Ala Asp Val Lys Glu Cys Ile Glu
 210 215 220
 Ala Phe Ser Ser Tyr Ile Cys Pro Ser Asp Pro Gly Phe Val Leu Asn
 225 230 235 240
 His Glu Met Glu Ser Cys Leu Ser Gly Asn Ile Ser Gln Cys Pro Arg
 245 250 255
 Thr Val Val Lys Ser Asp Ile Val Pro Arg Tyr Ala Phe Val Asn Gly
 260 265 270
 Gly Val Val Ala Asn Cys Ile Thr Thr Thr Cys Thr Cys Asn Gly Ile
 275 280 285
 Gly Asn Arg Ile Asn Gln Pro Pro Asp Gln Gly Val Lys Ile Ile Thr
 290 295 300
 His Lys Glu Cys Asn Thr Ile Gly Ile Asn Gly Met Leu Phe Asn Thr
 305 310 315 320
 Asn Lys Glu Gly Thr Leu Ala Phe Tyr Thr Pro Asn Asp Ile Thr Leu
 325 330 335
 Asn Asn Ser Val Ala Leu Asp Pro Ile Asp Ile Ser Ile Glu Leu Asn
 340 345 350
 Lys Ala Lys Ser Asp Leu Glu Glu Ser Lys Glu Trp Ile Arg Arg Ser
 355 360 365
 Asn Gln Lys Leu Asp Ser Ile Gly Asn Trp His Gln Ser Ser Thr Thr
 370 375 380
 Ile Ile Ile Val Leu Ile Met Ile Ile Ile Leu Phe Ile Ile Asn Val
 385 390 395 400
 Thr Ile Ile Ile Ile Ala Val Lys Tyr Tyr Arg Ile Gln Lys Arg Asn
 405 410 415
 Arg Val Asp Gln Asn Asp Lys Pro Tyr Val Leu Thr Asn Lys
 420 425 430
 (2) INFORMATION FOR SEQ ID NO: 96:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 221 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: protein
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:96
 Gly Leu Phe Gly Ala Ile Ala Gly Phe Ile Glu Asn Gly Trp Glu Gly
 1 5 10 15
 Met Ile Asp Gly Trp Tyr Gly Phe Arg His Gln Asn Ser Glu Gly Thr
 20 25 30
 Gly Gln Ala Ala Asp Leu Lys Ser Thr Gln Ala Ala Ile Asp Gln Ile
 35 40 45
 Asn Gly Lys Leu Asn Arg Val Ile Glu Lys Thr Asn Glu Lys Phe His
 50 55 60
 Gln Ile Glu Lys Glu Phe Ser Glu Val Glu Gly Arg Ile Gln Asp Leu
 65 70 75 80
 Glu Lys Tyr Val Glu Asp Thr Lys Ile Asp Leu Trp Ser Tyr Asn Ala
 85 90 95
 Glu Leu Leu Val Ala Leu Glu Asn Gln His Thr Ile Asp Leu Thr Asp
 100 105 110
 Ser Glu Met Asn Lys Leu Phe Glu Lys Thr Arg Arg Gln Leu Arg Glu
 115 120 125
 Asn Ala Glu Glu Met Gly Asn Gly Cys Phe Lys Ile Tyr His Lys Cys
 130 135 140
 Asp Asn Ala Cys Ile Glu Ser Ile Arg Asn Gly Thr Tyr Asp His Asp
 145 150 155 160
 Val Tyr Arg Asp Glu Ala Leu Asn Asn Arg Phe Gln Ile Lys Gly Val
 165 170 175
 Glu Leu Lys Ser Gly Tyr Lys Asp Trp Ile Leu Trp Ile Ser Phe Ala
 180 185 190
 Ile Ser Cys Phe Leu Leu Cys Val Val Leu Leu Gly Phe Ile Met Trp
 195 200 205
 Ala Cys Gln Arg Gly Asn Ile Arg Cys Asn Ile Cys Ile
 210 215 220
 (2) INFORMATION FOR SEQ ID NO: 97:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 46 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:97
 Tyr Thr Ser Val Ile Thr Ile Glu Leu Ser Asn Ile Lys Glu Asn Lys
 1 5 10 15
 Cys Asn Gly Ala Lys Val Lys Leu Ile Lys Gln Glu Leu Asp Lys Tyr
 20 25 30
 Lys Asn Ala Val Thr Glu Leu Gln Leu Leu Met Gln Ser Thr
 35 40 45
 (2) INFORMATION FOR SEQ ID NO: 98:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 54 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:98
 Ala Ser Gly Val Ala Val Ser Lys Val Leu His Leu Glu Gly Glu Val
 1 5 10 15
 Asn Lys Ile Ala Leu Leu Ser Thr Asn Lys Ala Val Val Ser Leu Ser
 20 25 30
 Asn Gly Val Ser Val Leu Thr Ser Lys Val Leu Asp Leu Lys Asn Tyr
 35 40 45
 Ile Asp Lys Gln Leu Leu
 50
 (2) INFORMATION FOR SEQ ID NO: 99:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 53 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:99
 Gly Glu Pro Ile Ile Asn Phe Tyr Asp Pro Leu Val Phe Pro Ser Asp
 1 5 10 15
 Glu Phe Asp Ala Ser Ile Ser Gln Val Asn Glu Lys Ile Asn Gln Ser
 20 25 30
 Leu Ala Phe Ile Arg Lys Ser Asp Glu Leu Leu His Asn Val Asn Ala
 35 40 45
 Gly Lys Ser Thr Thr
 50
 (2) INFORMATION FOR SEQ ID NO: 100:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 70 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:100
 Gly Thr Ile Ala Leu Gly Val Ala Thr Ser Ala Gln Ile Thr Ala Ala
 1 5 10 15
 Val Ala Leu Val Glu Ala Lys Gln Ala Arg Ser Asp Ile Glu Lys Leu
 20 25 30
 Lys Glu Ala Ile Arg Asp Thr Asn Lys Ala Val Gln Ser Val Gln Ser
 35 40 45
 Ser Ile Gly Asn Leu Ile Val Ala Ile Lys Ser Val Gln Asp Tyr Val
 50 55 60
 Asn Lys Glu Ile Val Pro
 65 70
 (2) INFORMATION FOR SEQ ID NO: 101:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 56 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:101
 Tyr Thr Pro Asn Asp Ile Thr Leu Asn Asn Ser Val Ala Leu Asp Pro
 1 5 10 15
 Ile Asp Ile Ser Ile Glu Leu Asn Lys Ala Lys Ser Asp Leu Glu Glu
 20 25 30
 Ser Lys Glu Trp Ile Arg Arg Ser Asn Gln Lys Leu Asp Ser Ile Gly
 35 40 45
 Asn Trp His Gln Ser Ser Thr Thr
 50 55
 (2) INFORMATION FOR SEQ ID NO: 102:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 249 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: protein
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:102
 Arg Asn Lys Arg Gly Val Phe Val Leu Gly Phe Leu Gly Phe Leu Ala
 1 5 10 15
 Thr Ala Gly Ser Ala Met Gly Ala Ala Ser Xaa Xaa Xaa Xaa Ala Gln
 20 25 30
 Ser Arg Thr Leu Leu Ala Gly Ile Val Gln Gln Gln Gln Gln Leu Leu
 35 40 45
 Asp Val Val Lys Arg Gln Gln Glu Leu Leu Arg Leu Thr Val Trp Gly
 50 55 60
 Thr Lys Asn Leu Gln Thr Arg Val Thr Ala Ile Glu Lys Tyr Leu Lys
 65 70 75 80
 Asp Gln Ala Gln Leu Asn Ala Trp Gly Cys Ala Phe Arg Gln Val Cys
 85 90 95
 His Thr Thr Val Pro Trp Pro Asn Ala Ser Leu Thr Pro Asp Trp Asn
 100 105 110
 Asn Asp Thr Trp Gln Glu Trp Glu Arg Lys Val Asp Phe Leu Glu Glu
 115 120 125
 Asn Ile Thr Ala Leu Leu Glu Glu Ala Gln Ile Gln Gln Glu Lys Asn
 130 135 140
 Met Tyr Glu Leu Gln Lys Leu Asn Ser Trp Asp Val Phe Gly Asn Xaa
 145 150 155 160
 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa
 165 170 175
 Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Xaa Ile Tyr Ile Val Met Leu
 180 185 190
 Ala Lys Leu Arg Gln Gly Tyr Arg Pro Val Phe Ser Ser Pro Pro Ser
 195 200 205
 Tyr Phe Gln Xaa Thr His Thr Gln Gln Asp Pro Ala Leu Pro Thr Arg
 210 215 220
 Glu Gly Lys Glu Gly Asp Gly Gly Glu Gly Gly Gly Asn Ser Ser Trp
 225 230 235 240
 Pro Trp Gln Ile Glu Tyr Ile His Phe
 245
 (2) INFORMATION FOR SEQ ID NO: 103:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 856 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: protein
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:103
 Met Thr Arg Arg Arg Val Leu Ser Val Val Val Leu Leu Ala Ala Leu
 1 5 10 15
 Ala Cys Arg Leu Gly Ala Gln Thr Pro Glu Gln Pro Ala Pro Pro Ala
 20 25 30
 Thr Thr Val Gln Pro Thr Ala Thr Arg Gln Gln Thr Ser Phe Pro Phe
 35 40 45
 Arg Val Cys Glu Leu Ser Ser His Gly Asp Leu Phe Arg Phe Ser Ser
 50 55 60
 Asp Ile Gln Cys Pro Ser Phe Gly Thr Arg Glu Asn His Thr Glu Gly
 65 70 75 80
 Leu Leu Met Val Phe Lys Asp Asn Ile Ile Pro Tyr Ser Phe Lys Val
 85 90 95
 Arg Ser Tyr Thr Lys Ile Val Thr Asn Ile Leu Ile Tyr Asn Gly Trp
 100 105 110
 Tyr Ala Asp Ser Val Thr Asn Arg His Glu Glu Lys Phe Ser Val Asp
 115 120 125
 Ser Tyr Glu Thr Asp Gln Met Asp Thr Ile Tyr Gln Cys Tyr Asn Ala
 130 135 140
 Val Lys Met Thr Lys Asp Gly Leu Thr Arg Val Tyr Val Asp Arg Asp
 145 150 155 160
 Gly Val Asn Ile Thr Val Asn Leu Lys Pro Thr Gly Gly Leu Ala Asn
 165 170 175
 Gly Val Arg Arg Tyr Ala Ser Gln Thr Glu Leu Tyr Asp Ala Pro Gly
 180 185 190
 Trp Leu Ile Trp Thr Tyr Arg Thr Arg Thr Thr Val Asn Cys Leu Ile
 195 200 205
 Thr Asp Met Met Ala Lys Ser Asn Ser Pro Phe Asp Phe Phe Val Thr
 210 215 220
 Thr Thr Gly Gln Thr Val Glu Met Ser Pro Phe Tyr Asp Gly Lys Asn
 225 230 235 240
 Lys Glu Thr Phe His Glu Arg Ala Asp Ser Phe His Val Arg Thr Asn
 245 250 255
 Tyr Lys Ile Val Asp Tyr Asp Asn Arg Gly Thr Asn Pro Gln Gly Glu
 260 265 270
 Arg Arg Ala Phe Leu Asp Lys Gly Thr Tyr Thr Leu Ser Trp Lys Leu
 275 280 285
 Glu Asn Arg Thr Ala Tyr Cys Pro Leu Gln His Trp Gln Thr Phe Asp
 290 295 300
 Ser Thr Ile Ala Thr Glu Thr Gly Lys Ser Ile His Phe Val Thr Asp
 305 310 315 320
 Glu Gly Thr Ser Ser Phe Val Thr Asn Thr Thr Val Gly Ile Glu Leu
 325 330 335
 Pro Asp Ala Phe Lys Cys Ile Glu Glu Gln Val Asn Lys Thr His Glu
 340 345 350
 Lys Tyr Glu Ala Val Gln Asp Arg Tyr Thr Lys Gly Gln Glu Ala Ile
 355 360 365
 Thr Tyr Phe Ile Thr Ser Gly Gly Leu Leu Leu Ala Trp Leu Pro Leu
 370 375 380
 Thr Pro Arg Ser Leu Ala Thr Val Lys Asn Leu Thr Glu Leu Thr Thr
 385 390 395 400
 Pro Thr Ser Ser Pro Pro Ser Ser Pro Ser Pro Pro Ala Pro Ser Ala
 405 410 415
 Ala Arg Gly Ser Thr Pro Ala Ala Val Leu Arg Arg Arg Arg Arg Asp
 420 425 430
 Ala Gly Asn Ala Thr Thr Pro Val Pro Pro Thr Ala Pro Gly Lys Ser
 435 440 445
 Leu Gly Thr Leu Asn Asn Pro Ala Thr Val Gln Ile Gln Phe Ala Tyr
 450 455 460
 Asp Ser Leu Arg Arg Gln Ile Asn Arg Met Leu Gly Asp Leu Ala Arg
 465 470 475 480
 Ala Trp Cys Leu Glu Gln Lys Arg Gln Asn Met Val Leu Arg Glu Leu
 485 490 495
 Thr Lys Ile Asn Pro Thr Thr Val Met Ser Ser Ile Tyr Gly Lys Ala
 500 505 510
 Val Ala Ala Lys Arg Leu Gly Asp Val Ile Ser Val Ser Gln Cys Val
 515 520 525
 Pro Val Asn Gln Ala Thr Val Thr Leu Arg Lys Ser Met Arg Val Pro
 530 535 540
 Gly Ser Glu Thr Met Cys Tyr Ser Arg Pro Leu Val Ser Phe Ser Phe
 545 550 555 560
 Ile Asn Asp Thr Lys Thr Tyr Glu Gly Gln Leu Gly Thr Asp Asn Glu
 565 570 575
 Ile Phe Leu Thr Lys Lys Met Thr Glu Val Cys Gln Ala Thr Ser Gln
 580 585 590
 Tyr Tyr Phe Gln Ser Gly Asn Glu Ile His Val Tyr Asn Asp Tyr His
 595 600 605
 His Phe Lys Thr Ile Glu Leu Asp Gly Ile Ala Thr Leu Gln Thr Phe
 610 615 620
 Ile Ser Leu Asn Thr Ser Leu Ile Glu Asn Ile Asp Phe Ala Ser Leu
 625 630 635 640
 Glu Leu Tyr Ser Arg Asp Glu Gln Arg Ala Ser Asn Val Phe Asp Leu
 645 650 655
 Glu Gly Ile Phe Arg Glu Tyr Asn Phe Gln Ala Gln Asn Ile Ala Gly
 660 665 670
 Leu Arg Lys Asp Leu Asp Asn Ala Val Ser Asn Gly Arg Asn Gln Phe
 675 680 685
 Val Asp Gly Leu Gly Glu Leu Met Asp Ser Leu Gly Ser Val Gly Gln
 690 695 700
 Ser Ile Thr Asn Leu Val Ser Thr Val Gly Gly Leu Phe Ser Ser Leu
 705 710 715 720
 Val Ser Gly Phe Ile Ser Phe Phe Lys Asn Pro Phe Gly Gly Met Leu
 725 730 735
 Ile Leu Val Leu Val Ala Gly Val Val Ile Leu Val Ile Ser Leu Thr
 740 745 750
 Arg Arg Thr Arg Gln Met Ser Gln Gln Pro Val Gln Met Leu Tyr Pro
 755 760 765
 Gly Ile Asp Glu Leu Ala Gln Gln His Ala Ser Gly Glu Gly Pro Gly
 770 775 780
 Ile Asn Pro Ile Ser Lys Thr Glu Leu Gln Ala Ile Met Leu Ala Leu
 785 790 795 800
 His Glu Gln Asn Gln Glu Gln Lys Arg Ala Ala Gln Arg Ala Ala Gly
 805 810 815
 Pro Ser Val Ala Ser Arg Ala Leu Gln Ala Ala Arg Asp Arg Phe Pro
 820 825 830
 Gly Leu Arg Arg Arg Arg Tyr His Asp Pro Glu Thr Ala Ala Ala Leu
 835 840 845
 Leu Gly Glu Ala Glu Thr Glu Phe
 850 855
 (2) INFORMATION FOR SEQ ID NO: 104:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 245 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: protein
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:104
 Met Met Asp Pro Asn Ser Thr Ser Glu Asp Val Lys Phe Thr Pro Asp
 1 5 10 15
 Pro Tyr Gln Val Pro Phe Val Gln Ala Phe Asp Gln Ala Thr Arg Val
 20 25 30
 Tyr Gln Asp Leu Gly Gly Pro Ser Gln Ala Pro Leu Pro Cys Val Leu
 35 40 45
 Trp Pro Val Leu Pro Glu Pro Leu Pro Gln Gly Gln Leu Thr Ala Tyr
 50 55 60
 His Val Ser Thr Ala Pro Thr Gly Ser Trp Phe Ser Ala Pro Gln Pro
 65 70 75 80
 Ala Pro Glu Asn Ala Tyr Gln Ala Tyr Ala Ala Pro Gln Leu Phe Pro
 85 90 95
 Val Ser Asp Ile Thr Gln Asn Gln Gln Thr Asn Gln Ala Gly Gly Glu
 100 105 110
 Ala Pro Gln Pro Gly Asp Asn Ser Thr Val Gln Thr Ala Ala Ala Val
 115 120 125
 Val Phe Ala Cys Pro Gly Ala Asn Gln Gly Gln Gln Leu Ala Asp Ile
 130 135 140
 Gly Val Pro Gln Pro Ala Pro Val Ala Ala Pro Ala Arg Arg Thr Arg
 145 150 155 160
 Lys Pro Gln Gln Pro Glu Ser Leu Glu Glu Cys Asp Ser Glu Leu Glu
 165 170 175
 Ile Lys Arg Tyr Lys Asn Arg Val Ala Ser Arg Lys Cys Arg Ala Lys
 180 185 190
 Phe Lys Gln Leu Leu Gln His Tyr Arg Glu Val Ala Ala Ala Lys Ser
 195 200 205
 Ser Glu Asn Asp Arg Leu Arg Leu Leu Leu Lys Gln Met Cys Pro Ser
 210 215 220
 Leu Asp Val Asp Ser Ile Ile Pro Arg Thr Pro Asp Val Leu His Glu
 225 230 235 240
 Asp Leu Leu Asn Phe
 245
 (2) INFORMATION FOR SEQ ID NO: 105:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 438 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: protein
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:105
 Phe Ala Gly Val Val Leu Ala Gly Ala Ala Leu Gly Val Ala Thr Ala
 1 5 10 15
 Ala Gln Ile Thr Ala Gly Ile Ala Leu His Gln Ser Met Leu Asn Ser
 20 25 30
 Gln Ala Ile Asp Asn Leu Arg Ala Ser Leu Glu Thr Thr Asn Gln Ala
 35 40 45
 Ile Glu Ala Ile Arg Gln Ala Gly Gln Glu Met Ile Leu Ala Val Gln
 50 55 60
 Gly Val Gln Asp Tyr Ile Asn Asn Glu Leu Ile Pro Ser Met Asn Gln
 65 70 75 80
 Leu Ser Cys Asp Leu Ile Gly Gln Lys Leu Gly Leu Lys Leu Leu Arg
 85 90 95
 Tyr Tyr Thr Glu Ile Leu Ser Leu Phe Gly Pro Ser Leu Arg Asp Pro
 100 105 110
 Ile Ser Ala Glu Ile Ser Ile Gln Ala Leu Ser Tyr Ala Leu Gly Gly
 115 120 125
 Asp Ile Asn Lys Val Leu Glu Lys Leu Gly Tyr Ser Gly Gly Asp Leu
 130 135 140
 Leu Gly Ile Leu Glu Ser Arg Gly Ile Lys Ala Arg Ile Thr His Val
 145 150 155 160
 Asp Thr Glu Ser Tyr Phe Ile Val Leu Ser Ile Ala Tyr Pro Thr Leu
 165 170 175
 Ser Glu Ile Lys Gly Val Ile Val His Arg Leu Glu Gly Val Ser Tyr
 180 185 190
 Asn Ile Gly Ser Gln Glu Trp Tyr Thr Thr Val Pro Lys Tyr Val Ala
 195 200 205
 Thr Gln Gly Tyr Leu Ile Ser Asn Phe Asp Glu Ser Ser Cys Thr Phe
 210 215 220
 Met Pro Glu Gly Thr Val Cys Ser Gln Asn Ala Leu Tyr Pro Met Ser
 225 230 235 240
 Pro Leu Leu Gln Glu Cys Leu Arg Gly Ser Thr Lys Ser Cys Ala Arg
 245 250 255
 Thr Leu Val Ser Gly Ser Phe Gly Asn Arg Phe Ile Leu Ser Gln Gly
 260 265 270
 Asn Leu Ile Ala Asn Cys Ala Ser Ile Leu Cys Lys Cys Tyr Thr Thr
 275 280 285
 Gly Thr Ile Ile Asn Gln Asp Pro Asp Lys Ile Leu Thr Tyr Ile Ala
 290 295 300
 Ala Asp His Cys Pro Val Val Glu Val Asn Gly Val Thr Ile Gln Val
 305 310 315 320
 Gly Ser Arg Arg Tyr Pro Asp Ala Val Tyr Leu His Arg Ile Asp Leu
 325 330 335
 Gly Pro Pro Ile Ser Leu Glu Arg Leu Asp Val Gly Thr Asn Leu Gly
 340 345 350
 Asn Ala Ile Ala Lys Leu Glu Asp Ala Lys Glu Leu Leu Glu Ser Ser
 355 360 365
 Asp Gln Ile Leu Arg Ser Met Lys Gly Leu Ser Ser Thr Ser Ile Val
 370 375 380
 Tyr Ile Leu Ile Ala Val Cys Leu Gly Gly Leu Ile Gly Ile Pro Ala
 385 390 395 400
 Leu Ile Cys Cys Cys Arg Gly Arg Cys Asn Lys Lys Gly Glu Gln Val
 405 410 415
 Gly Met Ser Arg Pro Gly Leu Lys Pro Asp Leu Thr Gly Thr Ser Lys
 420 425 430
 Ser Tyr Val Arg Ser Leu
 435
 (2) INFORMATION FOR SEQ ID NO: 106:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 389 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: protein
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:106
 Met Gly Gln Asn Leu Ser Thr Ser Asn Pro Leu Gly Phe Phe Pro Asp
 1 5 10 15
 His Gln Leu Asp Pro Ala Phe Arg Ala Asn Thr Ala Asn Pro Asp Trp
 20 25 30
 Asp Phe Asn Pro Asn Lys Asp Thr Trp Pro Asp Ala Asn Lys Val Gly
 35 40 45
 Ala Gly Ala Phe Gly Leu Gly Phe Thr Pro Pro His Gly Gly Leu Leu
 50 55 60
 Gly Trp Ser Pro Gln Ala Gln Gly Ile Leu Gln Thr Leu Pro Ala Asn
 65 70 75 80
 Pro Pro Pro Ala Ser Thr Asn Arg Gln Ser Gly Arg Gln Pro Thr Pro
 85 90 95
 Leu Ser Pro Pro Leu Arg Asn Thr His Pro Gln Ala Met Gln Trp Asn
 100 105 110
 Ser Thr Thr Phe His Gln Thr Leu Gln Asp Pro Arg Val Arg Gly Leu
 115 120 125
 Tyr Phe Pro Ala Gly Gly Ser Ser Ser Gly Thr Val Asn Pro Val Leu
 130 135 140
 Thr Thr Ala Ser Pro Leu Ser Ser Ile Phe Ser Arg Ile Gly Asp Pro
 145 150 155 160
 Ala Leu Asn Met Glu Asn Ile Thr Ser Gly Phe Leu Gly Pro Leu Leu
 165 170 175
 Val Leu Gln Ala Gly Phe Phe Leu Leu Thr Arg Ile Leu Thr Ile Pro
 180 185 190
 Gln Ser Leu Asp Ser Trp Trp Thr Ser Leu Asn Phe Leu Gly Gly Thr
 195 200 205
 Thr Val Cys Leu Gly Gln Asn Ser Gln Ser Pro Thr Ser Asn His Ser
 210 215 220
 Pro Thr Ser Cys Pro Pro Thr Cys Pro Gly Tyr Arg Trp Met Cys Leu
 225 230 235 240
 Arg Arg Phe Ile Ile Phe Leu Phe Ile Leu Leu Leu Cys Leu Ile Phe
 245 250 255
 Leu Leu Val Leu Leu Asp Tyr Gln Gly Met Leu Pro Val Cys Pro Leu
 260 265 270
 Ile Pro Gly Ser Ser Thr Thr Ser Thr Gly Pro Cys Arg Thr Cys Met
 275 280 285
 Thr Thr Ala Gln Gly Thr Ser Met Tyr Pro Ser Cys Cys Cys Thr Lys
 290 295 300
 Pro Ser Asp Gly Asn Cys Thr Cys Ile Pro Ile Pro Ser Ser Trp Ala
 305 310 315 320
 Phe Gly Lys Phe Leu Trp Glu Trp Ala Ser Ala Arg Phe Ser Trp Leu
 325 330 335
 Ser Leu Leu Val Pro Phe Val Gln Trp Phe Val Gly Leu Ser Pro Thr
 340 345 350
 Val Trp Leu Ser Val Ile Trp Met Met Trp Tyr Trp Gly Pro Ser Leu
 355 360 365
 Tyr Ser Ile Leu Ser Pro Phe Leu Pro Leu Leu Pro Ile Phe Phe Cys
 370 375 380
 Leu Trp Val Tyr Ile
 385
 (2) INFORMATION FOR SEQ ID NO: 107:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 192 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: protein
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:107
 Ala Ile Gln Leu Ile Pro Leu Phe Val Gly Leu Gly Ile Thr Thr Ala
 1 5 10 15
 Val Ser Thr Gly Ala Ala Gly Leu Gly Val Ser Ile Thr Gln Tyr Thr
 20 25 30
 Lys Leu Ser His Gln Leu Ile Ser Asp Val Gln Ala Ile Ser Ser Thr
 35 40 45
 Ile Gln Asp Leu Gln Asp Gln Val Asp Ser Leu Ala Glu Val Val Leu
 50 55 60
 Gln Asn Arg Arg Gly Leu Asp Leu Leu Thr Ala Glu Gln Gly Gly Ile
 65 70 75 80
 Cys Leu Ala Leu Gln Glu Lys Cys Cys Phe Tyr Ala Asn Lys Ser Gly
 85 90 95
 Ile Val Arg Asp Lys Ile Lys Asn Leu Gln Asp Asp Leu Glu Arg Arg
 100 105 110
 Arg Arg Gln Leu Ile Asp Asn Pro Phe Trp Thr Ser Phe His Gly Phe
 115 120 125
 Leu Pro Tyr Val Met Pro Leu Leu Gly Pro Leu Leu Cys Leu Leu Leu
 130 135 140
 Val Leu Ser Phe Gly Pro Ile Ile Phe Asn Lys Leu Met Thr Phe Ile
 145 150 155 160
 Lys His Gln Ile Glu Ser Ile Gln Ala Lys Pro Ile Gln Val His Tyr
 165 170 175
 His Arg Leu Glu Gln Glu Asp Ser Gly Gly Ser Tyr Leu Thr Leu Thr
 180 185 190
 (2) INFORMATION FOR SEQ ID NO: 108:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 154 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: protein
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:108
 Met Lys Ala Gln Lys Gly Phe Thr Leu Ile Glu Leu Met Ile Val Val
 1 5 10 15
 Ala Ile Ile Gly Ile Leu Ala Ala Ile Ala Ile Pro Gln Tyr Gln Asp
 20 25 30
 Tyr Thr Ala Arg Thr Gln Val Thr Arg Ala Val Ser Glu Val Ser Ala
 35 40 45
 Leu Lys Thr Ala Ala Glu Ser Ala Ile Leu Glu Gly Lys Glu Ile Val
 50 55 60
 Ser Ser Ala Thr Pro Lys Asp Thr Gln Tyr Asp Ile Gly Phe Thr Glu
 65 70 75 80
 Ser Thr Leu Leu Asp Gly Ser Gly Lys Ser Gln Ile Gln Val Thr Asp
 85 90 95
 Asn Gln Asp Gly Thr Val Glu Leu Val Ala Thr Leu Gly Lys Ser Ser
 100 105 110
 Gly Ser Ala Ile Lys Gly Ala Val Ile Thr Val Ser Arg Lys Asn Asp
 115 120 125
 Gly Val Trp Asn Cys Lys Ile Thr Lys Thr Pro Thr Ala Trp Lys Pro
 130 135 140
 Asn Tyr Ala Pro Ala Asn Cys Pro Lys Ser
 145 150
 (2) INFORMATION FOR SEQ ID NO: 109:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 167 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: protein
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:109
 Met Asn Thr Leu Gln Lys Gly Phe Thr Leu Ile Glu Leu Met Ile Val
 1 5 10 15
 Ile Ala Ile Val Gly Ile Leu Ala Ala Val Ala Leu Pro Ala Tyr Gln
 20 25 30
 Asp Tyr Thr Ala Arg Ala Gln Val Ser Glu Ala Ile Leu Leu Ala Glu
 35 40 45
 Gly Gln Lys Ser Ala Val Thr Glu Tyr Tyr Leu Asn His Gly Ile Trp
 50 55 60
 Pro Lys Asp Asn Thr Ser Ala Gly Val Ala Ser Ser Ser Ser Ile Lys
 65 70 75 80
 Gly Lys Tyr Val Lys Glu Val Lys Val Glu Asn Gly Val Val Thr Ala
 85 90 95
 Thr Met Asn Ser Ser Asn Val Asn Lys Glu Ile Gln Gly Lys Lys Leu
 100 105 110
 Ser Leu Trp Ala Lys Arg Gln Asp Gly Ser Val Lys Trp Phe Cys Gly
 115 120 125
 Gln Pro Val Thr Arg Asn Ala Lys Asp Asp Thr Val Thr Ala Asp Ala
 130 135 140
 Thr Gly Asn Asp Gly Lys Ile Asp Thr Lys His Leu Pro Ser Thr Cys
 145 150 155 160
 Arg Asp Asn Phe Asp Ala Ser
 165
 (2) INFORMATION FOR SEQ ID NO: 110:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 213 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: protein
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:110
 Met Lys Lys Thr Leu Leu Gly Ser Leu Ile Leu Leu Ala Phe Ala Gly
 1 5 10 15
 Asn Val Gln Ala Asp Ile Asn Thr Glu Thr Ser Gly Lys Val Thr Phe
 20 25 30
 Phe Gly Lys Val Val Glu Asn Thr Cys Lys Val Lys Thr Glu His Lys
 35 40 45
 Asn Leu Ser Val Val Leu Asn Asp Val Gly Lys Asn Ser Leu Ser Thr
 50 55 60
 Lys Val Asn Thr Ala Met Pro Thr Pro Phe Thr Ile Thr Leu Gln Asn
 65 70 75 80
 Cys Asp Pro Thr Thr Ala Asn Gly Thr Ala Asn Lys Ala Asn Lys Val
 85 90 95
 Gly Leu Tyr Phe Tyr Ser Trp Lys Asn Val Asp Lys Glu Asn Asn Phe
 100 105 110
 Thr Leu Lys Asn Glu Gln Thr Thr Ala Asp Tyr Ala Thr Asn Val Asn
 115 120 125
 Ile Gln Leu Met Glu Ser Asn Gly Thr Lys Ala Ile Ser Val Val Gly
 130 135 140
 Lys Glu Thr Glu Asp Phe Met His Thr Asn Asn Asn Gly Val Ala Leu
 145 150 155 160
 Asn Gln Thr His Pro Asn Asn Ala His Ile Ser Gly Ser Thr Gln Leu
 165 170 175
 Thr Thr Gly Thr Asn Glu Leu Pro Leu His Phe Ile Ala Gln Tyr Tyr
 180 185 190
 Ala Thr Asn Lys Ala Thr Ala Gly Lys Val Gln Ser Ser Val Asp Phe
 195 200 205
 Gln Ile Ala Tyr Glu
 210
 (2) INFORMATION FOR SEQ ID NO: 111:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 234 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: protein
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:111
 Met Asn Lys Lys Leu Leu Met Asn Phe Phe Ile Val Ser Pro Leu Leu
 1 5 10 15
 Leu Ala Thr Thr Ala Thr Asp Phe Thr Pro Val Pro Leu Ser Ser Asn
 20 25 30
 Gln Ile Ile Lys Thr Ala Lys Ala Ser Thr Asn Asp Asn Ile Lys Asp
 35 40 45
 Leu Leu Asp Trp Tyr Ser Ser Gly Ser Asp Thr Phe Thr Asn Ser Glu
 50 55 60
 Val Leu Asp Asn Ser Leu Gly Ser Met Arg Ile Lys Asn Thr Asp Gly
 65 70 75 80
 Ser Ile Ser Leu Ile Ile Phe Pro Ser Pro Tyr Tyr Ser Pro Ala Phe
 85 90 95
 Thr Lys Gly Glu Lys Val Asp Leu Asn Thr Lys Arg Thr Lys Lys Ser
 100 105 110
 Gln His Thr Ser Glu Gly Thr Tyr Ile His Phe Gln Ile Ser Gly Val
 115 120 125
 Thr Asn Thr Glu Lys Leu Pro Thr Pro Ile Glu Leu Pro Leu Lys Val
 130 135 140
 Lys Val His Gly Lys Asp Ser Pro Leu Lys Tyr Gly Pro Lys Phe Asp
 145 150 155 160
 Lys Lys Gln Leu Ala Ile Ser Thr Leu Asp Phe Glu Ile Arg His Gln
 165 170 175
 Leu Thr Gln Ile His Gly Leu Tyr Arg Ser Ser Asp Lys Thr Gly Gly
 180 185 190
 Tyr Trp Lys Ile Thr Met Asn Asp Gly Ser Thr Tyr Gln Ser Asp Leu
 195 200 205
 Ser Lys Lys Phe Glu Tyr Asn Thr Glu Lys Pro Pro Ile Asn Ile Asp
 210 215 220
 Glu Ile Lys Thr Ile Glu Ala Glu Ile Asn
 225 230
 (2) INFORMATION FOR SEQ ID NO: 112:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 257 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: protein
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:112
 Met Lys Lys Thr Ala Phe Ile Leu Leu Leu Phe Ile Ala Leu Thr Leu
 1 5 10 15
 Thr Thr Ser Pro Leu Val Asn Gly Ser Glu Lys Ser Glu Glu Ile Asn
 20 25 30
 Glu Lys Asp Leu Arg Lys Lys Ser Glu Leu Gln Arg Asn Ala Leu Ser
 35 40 45
 Asn Leu Arg Gln Ile Tyr Tyr Tyr Asn Glu Lys Ala Ile Thr Glu Asn
 50 55 60
 Lys Glu Ser Asp Asp Gln Phe Leu Glu Asn Thr Leu Leu Phe Lys Gly
 65 70 75 80
 Phe Phe Thr Gly His Pro Trp Tyr Asn Asp Leu Leu Val Asp Leu Gly
 85 90 95
 Ser Lys Asp Ala Thr Asn Lys Tyr Lys Gly Lys Lys Val Asp Leu Tyr
 100 105 110
 Gly Ala Tyr Tyr Gly Tyr Gln Cys Ala Gly Gly Thr Pro Asn Lys Thr
 115 120 125
 Ala Cys Met Tyr Gly Gly Val Thr Leu His Asp Asn Asn Arg Leu Thr
 130 135 140
 Glu Glu Lys Lys Val Pro Ile Asn Leu Trp Ile Asp Gly Lys Gln Thr
 145 150 155 160
 Thr Val Pro Ile Asp Lys Val Lys Thr Ser Lys Lys Glu Val Thr Val
 165 170 175
 Gln Glu Leu Asp Leu Gln Ala Arg His Tyr Leu His Gly Lys Phe Gly
 180 185 190
 Leu Tyr Asn Ser Asp Ser Phe Gly Gly Lys Val Gln Arg Gly Leu Ile
 195 200 205
 Val Phe His Ser Ser Glu Gly Ser Thr Val Ser Tyr Asp Leu Phe Asp
 210 215 220
 Ala Gln Gly Gln Tyr Pro Asp Thr Leu Leu Arg Ile Tyr Arg Asp Asn
 225 230 235 240
 Lys Thr Ile Asn Ser Glu Asn Leu His Ile Asp Leu Tyr Leu Tyr Thr
 245 250 255
 Thr
 (2) INFORMATION FOR SEQ ID NO: 113:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 257 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: protein
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:113
 Met Lys Lys Thr Ala Phe Thr Leu Leu Leu Phe Ile Ala Leu Thr Leu
 1 5 10 15
 Thr Thr Ser Pro Leu Val Asn Gly Ser Glu Lys Ser Glu Glu Ile Asn
 20 25 30
 Glu Lys Asp Leu Arg Lys Lys Ser Glu Leu Gln Gly Thr Ala Leu Gly
 35 40 45
 Asn Leu Lys Gln Ile Tyr Tyr Tyr Asn Glu Lys Ala Lys Thr Glu Asn
 50 55 60
 Lys Glu Ser His Asp Gln Phe Leu Gln His Thr Ile Leu Phe Lys Gly
 65 70 75 80
 Phe Phe Thr Asp His Ser Trp Tyr Asn Asp Leu Leu Val Asp Phe Asp
 85 90 95
 Ser Lys Asp Ile Val Asp Lys Tyr Lys Gly Lys Lys Val Asp Leu Tyr
 100 105 110
 Gly Ala Tyr Tyr Gly Tyr Gln Cys Ala Gly Gly Thr Pro Asn Lys Thr
 115 120 125
 Ala Cys Met Tyr Gly Gly Val Thr Leu His Asp Asn Asn Arg Leu Thr
 130 135 140
 Glu Glu Lys Lys Val Pro Ile Asn Leu Trp Leu Asp Gly Lys Gln Asn
 145 150 155 160
 Thr Val Pro Leu Glu Thr Val Lys Thr Asn Lys Lys Asn Val Thr Val
 165 170 175
 Gln Glu Leu Asp Leu Gln Ala Arg Arg Tyr Leu Gln Glu Lys Tyr Asn
 180 185 190
 Leu Tyr Asn Ser Asp Val Phe Asp Gly Lys Val Gln Arg Gly Leu Ile
 195 200 205
 Val Phe His Thr Ser Thr Glu Pro Ser Val Asn Tyr Asp Leu Phe Gly
 210 215 220
 Ala Gln Gly Gln Tyr Ser Asn Thr Leu Leu Arg Ile Tyr Arg Asp Asn
 225 230 235 240
 Lys Thr Ile Asn Ser Glu Asn Met His Ile Asp Ile Tyr Leu Tyr Thr
 245 250 255
 Ser
 (2) INFORMATION FOR SEQ ID NO: 114:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 254 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: protein
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:114
 Met Lys Asn Ile Thr Phe Ile Phe Phe Ile Leu Leu Ala Ser Pro Leu
 1 5 10 15
 Tyr Ala Asn Gly Asp Arg Leu Tyr Arg Ala Asp Ser Arg Pro Pro Asp
 20 25 30
 Glu Ile Lys Arg Phe Arg Ser Leu Met Pro Arg Gly Asn Glu Tyr Phe
 35 40 45
 Asp Arg Gly Thr Gln Met Asn Ile Asn Leu Tyr Asp His Ala Arg Gly
 50 55 60
 Thr Gln Thr Gly Phe Val Arg Tyr Asp Asp Gly Tyr Val Ser Thr Ser
 65 70 75 80
 Leu Ser Leu Arg Ser Ala His Leu Ala Gly Gln Tyr Ile Leu Ser Gly
 85 90 95
 Tyr Ser Leu Thr Ile Tyr Ile Val Ile Ala Asn Met Phe Asn Val Asn
 100 105 110
 Asp Val Ile Ser Val Tyr Ser Pro His Pro Tyr Glu Gln Glu Val Ser
 115 120 125
 Ala Leu Gly Gly Ile Pro Tyr Ser Gln Ile Tyr Gly Trp Tyr Arg Val
 130 135 140
 Asn Phe Gly Val Ile Asp Glu Arg Leu His Arg Asn Arg Glu Tyr Arg
 145 150 155 160
 Asp Arg Tyr Tyr Arg Asn Leu Asn Ile Ala Pro Ala Glu Asp Gly Tyr
 165 170 175
 Arg Leu Ala Gly Phe Pro Pro Asp His Gln Ala Trp Arg Glu Glu Pro
 180 185 190
 Trp Ile His His Ala Pro Gln Gly Cys Gly Asp Ser Ser Arg Thr Ile
 195 200 205
 Thr Gly Asp Thr Cys Asn Glu Glu Thr Gln Asn Leu Ser Thr Ile Tyr
 210 215 220
 Leu Arg Glu Tyr Gln Ser Lys Val Lys Arg Gln Ile Phe Ser Asp Tyr
 225 230 235 240
 Gln Ser Glu Val Asp Ile Tyr Asn Arg Ile Arg Asp Glu Leu
 245 250
 (2) INFORMATION FOR SEQ ID NO: 115:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 380 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: protein
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:115
 Met Met Phe Ser Gly Phe Asn Ala Asp Tyr Glu Ala Ser Ser Ser Arg
 1 5 10 15
 Cys Ser Ser Ala Ser Pro Ala Gly Asp Ser Leu Ser Tyr Tyr His Ser
 20 25 30
 Pro Ala Asp Ser Phe Ser Ser Met Gly Ser Pro Val Asn Ala Gln Asp
 35 40 45
 Phe Cys Thr Asp Leu Ala Val Ser Ser Ala Asn Phe Ile Pro Thr Val
 50 55 60
 Thr Ala Ile Ser Thr Ser Pro Asp Leu Gln Trp Leu Val Gln Pro Ala
 65 70 75 80
 Leu Val Ser Ser Val Ala Pro Ser Gln Thr Arg Ala Pro His Pro Phe
 85 90 95
 Gly Val Pro Ala Pro Ser Ala Gly Ala Tyr Ser Arg Ala Gly Val Val
 100 105 110
 Lys Thr Met Thr Gly Gly Arg Ala Gln Ser Ile Gly Arg Arg Gly Lys
 115 120 125
 Val Glu Gln Leu Ser Pro Glu Glu Glu Glu Lys Arg Arg Ile Arg Arg
 130 135 140
 Glu Arg Asn Lys Met Ala Ala Ala Lys Cys Arg Asn Arg Arg Arg Glu
 145 150 155 160
 Leu Thr Asp Thr Leu Gln Ala Glu Thr Asp Gln Leu Glu Asp Glu Lys
 165 170 175
 Ser Ala Leu Gln Thr Glu Ile Ala Asn Leu Leu Lys Glu Lys Glu Lys
 180 185 190
 Leu Glu Phe Ile Leu Ala Ala His Arg Pro Ala Cys Lys Ile Pro Asp
 195 200 205
 Asp Leu Gly Phe Pro Glu Glu Met Ser Val Ala Ser Leu Asp Leu Thr
 210 215 220
 Gly Gly Leu Pro Glu Val Ala Thr Pro Glu Ser Glu Glu Ala Phe Thr
 225 230 235 240
 Leu Pro Leu Leu Asn Asp Pro Glu Pro Lys Pro Ser Val Glu Pro Val
 245 250 255
 Lys Ser Ile Ser Ser Met Glu Leu Lys Thr Glu Pro Phe Asp Asp Phe
 260 265 270
 Leu Phe Pro Ala Ser Ser Arg Pro Ser Gly Ser Glu Thr Ala Arg Ser
 275 280 285
 Val Pro Asp Met Asp Leu Ser Gly Ser Phe Tyr Ala Leu Pro Leu Leu
 290 295 300
 Asn Asp Pro Glu Pro Lys Pro Ser Val Glu Pro Val Lys Ser Ile Ser
 305 310 315 320
 Ser Met Glu Leu Lys Thr Glu Pro Phe Asp Asp Phe Leu Phe Pro Ala
 325 330 335
 Ser Ser Arg Pro Ser Gly Ser Glu Thr Ala Arg Ser Val Pro Asp Met
 340 345 350
 Asp Leu Ser Gly Ser Phe Tyr Ala Gly Ser Ser Ser Asn Glu Pro Ser
 355 360 365
 Ser Asp Ser Leu Ser Ser Pro Thr Leu Leu Ala Leu
 370 375 380
 (2) INFORMATION FOR SEQ ID NO: 116:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 607 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: protein
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:116
 Ser Gly Trp Glu Ser Tyr Tyr Lys Thr Glu Gly Asp Glu Glu Ala Glu
 1 5 10 15
 Glu Glu Gln Glu Glu Asn Leu Glu Ala Ser Gly Asp Tyr Lys Tyr Ser
 20 25 30
 Gly Arg Asp Ser Leu Ile Phe Leu Val Asp Ala Ser Lys Ala Met Phe
 35 40 45
 Glu Ser Gln Ser Glu Asp Glu Leu Thr Pro Phe Asp Met Ser Ile Gln
 50 55 60
 Cys Ile Gln Ser Val Tyr Ile Ser Lys Ile Ile Ser Ser Asp Arg Asp
 65 70 75 80
 Leu Leu Ala Val Val Phe Tyr Gly Thr Glu Lys Asp Lys Asn Ser Val
 85 90 95
 Asn Phe Lys Asn Ile Tyr Val Leu Gln Glu Leu Asp Asn Pro Gly Ala
 100 105 110
 Lys Arg Ile Leu Glu Leu Asp Gln Phe Lys Gly Gln Gln Gly Gln Lys
 115 120 125
 Arg Phe Gln Asp Met Met Gly His Gly Ser Asp Tyr Ser Leu Ser Glu
 130 135 140
 Val Leu Trp Val Cys Ala Asn Leu Phe Ser Asp Val Gln Phe Lys Met
 145 150 155 160
 Ser His Lys Arg Ile Met Leu Phe Thr Asn Glu Asp Asn Pro His Gly
 165 170 175
 Asn Asp Ser Ala Lys Ala Ser Arg Ala Arg Thr Lys Ala Gly Asp Leu
 180 185 190
 Arg Asp Thr Gly Ile Phe Leu Asp Leu Met His Leu Lys Lys Pro Gly
 195 200 205
 Gly Phe Asp Ile Ser Leu Phe Tyr Arg Asp Ile Ile Ser Ile Ala Glu
 210 215 220
 Asp Glu Asp Leu Arg Val His Phe Glu Glu Ser Ser Lys Leu Glu Asp
 225 230 235 240
 Leu Leu Arg Lys Val Arg Ala Lys Glu Thr Arg Lys Arg Ala Leu Ser
 245 250 255
 Arg Leu Lys Leu Lys Leu Asn Lys Asp Ile Val Ile Ser Val Gly Ile
 260 265 270
 Tyr Asn Leu Val Gln Lys Ala Leu Lys Pro Pro Pro Ile Lys Leu Tyr
 275 280 285
 Arg Glu Thr Asn Glu Pro Val Lys Thr Lys Thr Arg Thr Phe Asn Thr
 290 295 300
 Ser Thr Gly Gly Leu Leu Leu Pro Ser Asp Thr Lys Arg Ser Gln Ile
 305 310 315 320
 Tyr Gly Ser Arg Gln Ile Ile Leu Glu Lys Glu Glu Thr Glu Glu Leu
 325 330 335
 Lys Arg Phe Asp Asp Pro Gly Leu Met Leu Met Gly Phe Lys Pro Leu
 340 345 350
 Val Leu Leu Lys Lys His His Leu Arg Pro Ser Leu Phe Val Tyr Pro
 355 360 365
 Glu Glu Ser Leu Val Ile Gly Ser Ser Thr Leu Phe Ser Ala Leu Leu
 370 375 380
 Ile Lys Cys Leu Glu Lys Glu Val Ala Ala Leu Cys Arg Tyr Thr Pro
 385 390 395 400
 Arg Arg Asn Ile Pro Pro Tyr Phe Val Ala Leu Val Pro Gln Glu Glu
 405 410 415
 Glu Leu Asp Asp Gln Lys Ile Gln Val Thr Pro Pro Gly Phe Gln Leu
 420 425 430
 Val Phe Leu Pro Phe Ala Asp Asp Lys Arg Lys Met Pro Phe Thr Glu
 435 440 445
 Lys Ile Met Ala Thr Pro Glu Gln Val Gly Lys Met Lys Ala Ile Val
 450 455 460
 Glu Lys Leu Arg Phe Thr Tyr Arg Ser Asp Ser Phe Glu Asn Pro Val
 465 470 475 480
 Leu Gln Gln His Phe Arg Asn Leu Glu Ala Leu Ala Leu Asp Leu Met
 485 490 495
 Glu Pro Glu Gln Ala Val Asp Leu Thr Leu Pro Lys Val Glu Ala Met
 500 505 510
 Asn Lys Arg Leu Gly Ser Leu Val Asp Glu Phe Lys Glu Leu Val Tyr
 515 520 525
 Pro Pro Asp Tyr Asn Pro Glu Gly Lys Val Thr Lys Arg Lys His Asp
 530 535 540
 Asn Glu Gly Ser Gly Ser Lys Arg Pro Lys Val Glu Tyr Ser Glu Glu
 545 550 555 560
 Glu Leu Lys Thr His Ile Ser Lys Gly Thr Leu Gly Lys Phe Thr Val
 565 570 575
 Pro Met Leu Lys Glu Ala Cys Arg Ala Tyr Gly Leu Lys Ser Gly Leu
 580 585 590
 Lys Lys Gln Glu Leu Leu Glu Ala Leu Thr Lys His Phe Gln Asp
 595 600 605
 (2) INFORMATION FOR SEQ ID NO: 117:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 462 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: protein
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:117
 Gly Gly Gly Ala Leu Ser Pro Gln His Ser Ala Val Thr Gln Gly Ser
 1 5 10 15
 Ile Ile Lys Asn Lys Glu Gly Met Asp Ala Lys Ser Leu Thr Ala Trp
 20 25 30
 Ser Arg Thr Leu Val Thr Phe Lys Asp Val Phe Val Asp Phe Thr Arg
 35 40 45
 Glu Glu Trp Lys Leu Leu Asp Thr Ala Gln Gln Ile Val Tyr Arg Asn
 50 55 60
 Val Met Leu Glu Asn Tyr Lys Asn Leu Val Ser Leu Gly Tyr Gln Leu
 65 70 75 80
 Thr Lys Pro Asp Val Ile Leu Arg Leu Glu Lys Gly Glu Glu Pro Trp
 85 90 95
 Leu Val Glu Arg Glu Ile His Gln Glu Thr His Pro Asp Ser Glu Thr
 100 105 110
 Ala Phe Glu Ile Lys Ser Ser Val Ser Ser Arg Ser Ile Phe Lys Asp
 115 120 125
 Lys Gln Ser Cys Asp Ile Lys Met Glu Gly Met Ala Arg Asn Asp Leu
 130 135 140
 Trp Tyr Leu Ser Leu Glu Glu Val Trp Lys Cys Arg Asp Gln Leu Asp
 145 150 155 160
 Lys Tyr Gln Glu Asn Pro Glu Arg His Leu Arg His Gln Leu Ile His
 165 170 175
 Thr Gly Glu Lys Pro Tyr Glu Cys Lys Glu Cys Gly Lys Ser Phe Ser
 180 185 190
 Arg Ser Ser His Leu Ile Gly His Gln Lys Thr His Thr Gly Glu Glu
 195 200 205
 Pro Tyr Glu Cys Lys Glu Cys Gly Lys Ser Phe Ser Trp Phe Ser His
 210 215 220
 Leu Val Thr His Gln Arg Thr His Thr Gly Asp Lys Leu Tyr Thr Cys
 225 230 235 240
 Asn Gln Cys Gly Lys Ser Phe Val His Ser Ser Arg Leu Ile Arg His
 245 250 255
 Gln Arg Thr His Thr Gly His Lys Pro Tyr Glu Cys Pro Glu Cys Gly
 260 265 270
 Lys Ser Phe Arg Gln Ser Thr His Leu Ile Leu His Gln Arg Thr His
 275 280 285
 Val Arg Val Arg Pro Tyr Glu Cys Asn Glu Cys Gly Lys Ser Tyr Ser
 290 295 300
 Gln Arg Ser His Leu Val Val His His Arg Ile His Thr Gly Leu Lys
 305 310 315 320
 Pro Phe Glu Cys Lys Asp Cys Gly Lys Cys Phe Ser Arg Ser Ser His
 325 330 335
 Leu Tyr Ser His Gln Arg Thr His Thr Gly Glu Lys Pro Tyr Glu Cys
 340 345 350
 His Asp Cys Gly Lys Ser Phe Ser Gln Ser Ser Ala Leu Ile Val His
 355 360 365
 Gln Arg Ile His Thr Gly Glu Lys Pro Tyr Glu Cys Cys Gln Cys Gly
 370 375 380
 Lys Ala Phe Ile Arg Lys Asn Asp Leu Ile Lys His Gln Arg Ile His
 385 390 395 400
 Val Gly Ala Glu Thr Tyr Lys Cys Asn Gln Cys Gly Ile Ile Phe Ser
 405 410 415
 Gln Asn Ser Pro Phe Ile Val His Gln Ile Ala His Thr Gly Glu Gln
 420 425 430
 Phe Leu Thr Cys Asn Gln Cys Gly Thr Ala Leu Val Asn Thr Ser Asn
 435 440 445
 Leu Ile Gly Tyr Gln Thr Asn His Ile Arg Glu Asn Ala Tyr
 450 455 460
 (2) INFORMATION FOR SEQ ID NO: 118:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:118
 Pro Asp Ala Val Tyr Leu His Arg Ile Asp Leu Gly Pro Pro Ile Ser
 1 5 10 15
 Leu Glu Arg Leu Asp Val Gly Thr Asn Leu Gly Asn Ala Ile Ala Lys
 20 25 30
 Leu Glu Asp
 35
 (2) INFORMATION FOR SEQ ID NO: 119:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 34 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:119
 Leu Glu Arg Leu Asp Val Gly Thr Asn Leu Gly Asn Ala Ile Ala Lys
 1 5 10 15
 Leu Glu Ala Lys Glu Leu Leu Glu Ser Ser Asp Gln Ile Leu Arg Ser
 20 25 30
 Met Lys
 (2) INFORMATION FOR SEQ ID NO: 120:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 47 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:120
 Thr Trp Gln Glu Trp Glu Arg Lys Val Asp Phe Leu Glu Glu Asn Ile
 1 5 10 15
 Thr Ala Leu Leu Glu Glu Ala Gln Ile Gln Gln Glu Lys Asn Met Tyr
 20 25 30
 Glu Leu Gln Lys Leu Asn Ser Trp Asp Val Phe Gly Asn Trp Phe
 35 40 45
 (2) INFORMATION FOR SEQ ID NO: 121:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 42 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:121
 Ile Glu Leu Ser Asn Ile Lys Glu Asn Lys Cys Asn Gly Thr Asp Ala
 1 5 10 15
 Lys Val Lys Leu Ile Lys Gln Glu Leu Asp Lys Tyr Lys Asn Ala Val
 20 25 30
 Thr Glu Leu Gln Leu Leu Met Gln Ser Thr
 35 40
 (2) INFORMATION FOR SEQ ID NO: 122:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 27 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:122
 Val Ser Lys Gly Tyr Ser Ala Leu Arg Thr Gly Trp Tyr Thr Ser Val
 1 5 10 15
 Ile Thr Ile Glu Leu Ser Asn Ile Lys Glu Asn
 20 25
 (2) INFORMATION FOR SEQ ID NO: 123:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 13 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:123
 Ala Phe Ile Arg Lys Ser Asp Glu Leu Leu His Asn Val
 1 5 10
 (2) INFORMATION FOR SEQ ID NO: 124:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 17
 (D) OTHER INFORMATION: /product= "OTHER"
 /note= "X represents U, the standard designation for
 C-abu, a modified cysteine."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:124
 Tyr Thr Ser Val Ile Thr Ile Glu Leu Ser Asn Ile Lys Glu Asn Lys
 1 5 10 15
 Xaa Asn Gly Thr Asp Ala Lys Val Lys Leu Ile Lys Gln Glu Leu Asp
 20 25 30
 Lys Tyr Lys
 35
 (2) INFORMATION FOR SEQ ID NO: 125:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 16
 (D) OTHER INFORMATION: /product= "OTHER"
 /note= "X represents U, the standard designation for
 C-abu, a modified cysteine."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:125
 Thr Ser Val Ile Thr Ile Glu Leu Ser Asn Ile Lys Glu Asn Lys Xaa
 1 5 10 15
 Asn Gly Thr Asp Ala Lys Val Lys Leu Ile Lys Gln Glu Leu Asp Lys
 20 25 30
 Tyr Lys Asn
 35
 (2) INFORMATION FOR SEQ ID NO: 126:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 15
 (D) OTHER INFORMATION: /product= "OTHER"
 /note= "X represents U, the standard designation for
 C-abu, a modified cysteine."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:126
 Ser Val Ile Thr Ile Glu Leu Ser Asn Ile Lys Glu Asn Lys Xaa Asn
 1 5 10 15
 Gly Thr Asp Ala Lys Val Lys Leu Ile Lys Gln Glu Leu Asp Lys Tyr
 20 25 30
 Lys Asn Ala
 35
 (2) INFORMATION FOR SEQ ID NO: 127:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /product= "OTHER"
 /note= "X represents U, the standard designation for
 C-abu, a modified cysteine."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:127
 Ser Asn Ile Lys Glu Asn Lys Xaa Asn Gly Thr Asp Ala Lys Val Lys
 1 5 10 15
 Leu Ile Lys Gln Glu Leu Asp Lys Tyr Lys Asn Ala Val Thr Glu Leu
 20 25 30
 Gln Leu Leu
 35
 (2) INFORMATION FOR SEQ ID NO: 128:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (D) OTHER INFORMATION: /product= "OTHER"
 /note= "X represents U, the standard designation for
 C-abu, a modified cysteine."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:128
 Lys Glu Asn Lys Xaa Asn Gly Thr Asp Ala Lys Val Lys Leu Ile Lys
 1 5 10 15
 Gln Glu Leu Asp Lys Tyr Lys Asn Ala Val Thr Glu Leu Gln Leu Leu
 20 25 30
 Met Gln Ser
 35
 (2) INFORMATION FOR SEQ ID NO: 129:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (ix) FEATURE:
 (A) NAME/KEY: Modified-site
 (B) LOCATION: 31
 (D) OTHER INFORMATION: /product= "OTHER"
 /note= "X represents U, the standard designation for
 C-abu, a modified cysteine."
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:129
 Ala Val Ser Lys Gly Tyr Leu Ser Ala Leu Arg Thr Gly Trp Tyr Thr
 1 5 10 15
 Ser Val Ile Thr Ile Glu Leu Ser Asn Ile Lys Glu Asn Lys Xaa Asn
 20 25 30
 Gly Thr Asp Ala
 35
 (2) INFORMATION FOR SEQ ID NO: 130:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 27 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:130
 Val Val Ser Leu Ser Asn Gly Val Ser Val Leu Thr Ser Lys Val Leu
 1 5 10 15
 Asp Leu Lys Asn Tyr Ile Asp Lys Gln Leu Leu
 20 25
 (2) INFORMATION FOR SEQ ID NO: 131:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 28 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:131
 Leu Leu Ser Thr Asn Lys Ala Val Val Ser Leu Ser Asn Gly Val Ser
 1 5 10 15
 Val Leu Thr Ser Lys Val Leu Asp Leu Lys Asn Tyr
 20 25
 (2) INFORMATION FOR SEQ ID NO: 132:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 28 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:132
 Val Leu His Leu Glu Gly Glu Val Asn Lys Ile Lys Ser Ala Leu Leu
 1 5 10 15
 Ser Thr Asn Lys Ala Val Val Ser Leu Ser Asn Gly
 20 25
 (2) INFORMATION FOR SEQ ID NO: 133:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 28 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:133
 Leu Leu Ser Thr Asn Lys Ala Val Val Ser Leu Ser Asn Gly Val Ser
 1 5 10 15
 Val Leu Thr Ser Lys Val Leu Asp Leu Lys Asn Tyr
 20 25
 (2) INFORMATION FOR SEQ ID NO: 134:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 37 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:134
 Ala Ser Gly Val Ala Val Ser Lys Val Leu His Leu Glu Gly Glu Val
 1 5 10 15
 Asn Lys Ile Lys Ser Ala Leu Leu Ser Thr Asn Lys Ala Val Val Ser
 20 25 30
 Leu Ser Asn Gly Val
 35
 (2) INFORMATION FOR SEQ ID NO: 135:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:135
 Val Leu His Leu Glu Gly Glu Val Asn Lys Ile Lys Ser Ala Leu Leu
 1 5 10 15
 Ser Thr Asn Lys Ala Val Val Ser Leu Ser Asn Gly Val Ser Val Leu
 20 25 30
 Thr Ser Lys
 35
 (2) INFORMATION FOR SEQ ID NO: 136:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 28 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:136
 Asn Asp Gln Lys Lys Leu Met Ser Asn Asn Val Gln Ile Val Arg Gln
 1 5 10 15
 Gln Ser Tyr Ser Ile Met Ser Ile Ile Lys Glu Glu
 20 25
 (2) INFORMATION FOR SEQ ID NO: 137:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:137
 Ser Ile Ser Asn Ile Glu Thr Val Ile Glu Phe Gln Gln Lys Asn Asn
 1 5 10 15
 Arg Leu Leu Glu Ile Thr Arg Glu Phe Ser Val Asn Ala Gly Val Thr
 20 25 30
 Thr Pro Val Ser
 35
 (2) INFORMATION FOR SEQ ID NO: 138:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:138
 Pro Ile Ile Asn Phe Tyr Asp Pro Leu Val Phe Pro Ser Asp Glu Phe
 1 5 10 15
 Asp Ala Ser Ile Ser Gln Val Asn Glu Lys Ile Asn Gln Ser Leu Ala
 20 25 30
 Phe Ile Arg
 35
 (2) INFORMATION FOR SEQ ID NO: 139:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 29 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:139
 Arg Met Lys Gln Leu Glu Asp Lys Val Glu Glu Leu Leu Ser Lys Leu
 1 5 10 15
 Ala Phe Ile Arg Lys Ser Asp Glu Leu Leu His Asn Val
 20 25
 (2) INFORMATION FOR SEQ ID NO: 140:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 19 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:140
 Ala Phe Ile Arg Lys Ser Asp Glu Leu Leu His Asn Val Asn Ala Gly
 1 5 10 15
 Lys Ser Thr
 (2) INFORMATION FOR SEQ ID NO: 141:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 19 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:141
 Phe Asp Ala Ser Ile Ser Gln Val Asn Glu Lys Ile Asn Gln Ser Leu
 1 5 10 15
 Ala Phe Ile
 (2) INFORMATION FOR SEQ ID NO: 142:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 21 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:142
 Ser Leu Ala Phe Ile Arg Lys Ser Asp Glu Leu Leu His Asn Val Asn
 1 5 10 15
 Ala Gly Lys Ser Thr
 20
 (2) INFORMATION FOR SEQ ID NO: 143:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:143
 Phe Asp Ala Ser Ile Ser Gln Val Asn Glu Lys Ile Asn Gln Ser Leu
 1 5 10 15
 Ala Phe Ile Arg Lys Ser Asp Glu Leu Leu His Asn Val Asn Ala Gly
 20 25 30
 Lys
 (2) INFORMATION FOR SEQ ID NO: 144:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:144
 Ala Ser Ile Ser Gln Val Asn Glu Lys Ile Asn Gln Ser Leu Ala Phe
 1 5 10 15
 Ile Arg Lys Ser Asp Glu Leu Leu His Asn Val Asn Ala Gly Lys Ser
 20 25 30
 Thr
 (2) INFORMATION FOR SEQ ID NO: 145:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:145
 Phe Asp Ala Ser Ile Ser Gln Val Asn Glu Lys Ile Asn Gln Ser Leu
 1 5 10 15
 Ala Phe Ile Arg Lys Ser Asp Glu Leu Leu His Asn Val Asn Ala Gly
 20 25 30
 Lys Ser Thr
 35
 (2) INFORMATION FOR SEQ ID NO: 146:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 28 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:146
 Ala Thr Ser Ala Gln Ile Thr Ala Ala Val Ala Leu Val Glu Ala Lys
 1 5 10 15
 Gln Ala Arg Ser Asp Ile Glu Lys Leu Lys Glu Ala
 20 25
 (2) INFORMATION FOR SEQ ID NO: 147:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:147
 Ala Ala Val Ala Leu Val Glu Ala Lys Gln Ala Arg Ser Asp Ile Glu
 1 5 10 15
 Lys Leu Lys Glu Ala Ile Arg Asp Thr Asn Lys Ala Val Gln Ser Val
 20 25 30
 Gln Ser Ser
 35
 (2) INFORMATION FOR SEQ ID NO: 148:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:148
 Ala Lys Gln Ala Arg Ser Asp Ile Glu Lys Leu Lys Glu Ala Ile Arg
 1 5 10 15
 Asp Thr Asn Lys Ala Val Gln Ser Val Gln Ser Ser Ile Gly Asn Leu
 20 25 30
 Ile Val Ala
 35
 (2) INFORMATION FOR SEQ ID NO: 149:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 28 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:149
 Ile Arg Asp Thr Asn Lys Ala Val Gln Ser Val Gln Ser Ser Ile Gly
 1 5 10 15
 Asn Leu Ile Val Ala Ile Lys Ser Val Gln Asp Tyr
 20 25
 (2) INFORMATION FOR SEQ ID NO: 150:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 28 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:150
 Ala Val Gln Ser Val Gln Ser Ser Ile Gly Asn Leu Ile Val Ala Ile
 1 5 10 15
 Lys Ser Val Gln Asp Tyr Val Asn Lys Glu Ile Val
 20 25
 (2) INFORMATION FOR SEQ ID NO: 151:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 28 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:151
 Leu Lys Glu Ala Ile Arg Asp Thr Asn Lys Ala Val Gln Ser Val Gln
 1 5 10 15
 Ser Ser Ile Gly Asn Leu Ile Val Ala Ile Lys Ser
 20 25
 (2) INFORMATION FOR SEQ ID NO: 152:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 13 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:152
 Glu Trp Ile Arg Arg Ser Asn Gln Lys Leu Asp Ser Ile
 1 5 10
 (2) INFORMATION FOR SEQ ID NO: 153:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:153
 Ile Asp Ile Ser Ile Glu Leu Asn Lys Ala Lys Ser Asp Leu Glu Glu
 1 5 10 15
 Ser Lys Glu Trp Ile Lys Lys Ser Asn Gln Lys Leu Asp Ser Ile Gly
 20 25 30
 Asn Trp His
 35
 (2) INFORMATION FOR SEQ ID NO: 154:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 29 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:154
 Arg Met Lys Gln Leu Glu Asp Lys Val Glu Glu Leu Leu Ser Lys Leu
 1 5 10 15
 Glu Trp Ile Arg Arg Ser Asn Gln Lys Leu Asp Ser Ile
 20 25
 (2) INFORMATION FOR SEQ ID NO: 155:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:155
 Asp Gln Gln Ile Lys Gln Tyr Lys Arg Leu Leu Asp Arg Leu Ile Ile
 1 5 10 15
 Pro Leu Tyr Asp Gly Leu Arg Gln Lys Asp Val Ile Val Ser Asn Gln
 20 25 30
 Glu Ser Asn
 35
 (2) INFORMATION FOR SEQ ID NO: 156:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:156
 Tyr Ser Glu Leu Thr Asn Ile Phe Gly Asp Asn Ile Gly Ser Leu Gln
 1 5 10 15
 Glu Lys Gly Ile Lys Leu Gln Gly Ile Ala Ser Leu Tyr Arg Thr Asn
 20 25 30
 Ile Thr Glu Ile
 35
 (2) INFORMATION FOR SEQ ID NO: 157:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:157
 Thr Ser Ile Thr Leu Gln Val Arg Leu Pro Leu Leu Thr Arg Leu Leu
 1 5 10 15
 Asn Thr Gln Ile Tyr Arg Val Asp Ser Ile Ser Tyr Asn Ile Gln Asn
 20 25 30
 Arg Glu Trp Tyr
 35
 (2) INFORMATION FOR SEQ ID NO: 158:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 57 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:158
 Asn Lys Ser Leu Glu Gln Ile Trp Asn Asn Met Thr Trp Met Glu Trp
 1 5 10 15
 Asp Arg Glu Ile Asn Asn Tyr Thr Ser Leu Ile His Ser Leu Ile Glu
 20 25 30
 Glu Gln Asn Gln Gln Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp
 35 40 45
 Lys Trp Ala Ser Leu Trp Asn Trp Phe
 50 55
 (2) INFORMATION FOR SEQ ID NO: 159:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:159
 Trp Met Glu Trp Asp Arg Glu Ile Asn Asn Tyr Thr Ser Leu Ile Gly
 1 5 10 15
 Ser Leu Ile Glu Glu Ser Gln Asn Gln Gln Glu Lys Asn Glu Gln Glu
 20 25 30
 Leu Leu Glu
 35
 (2) INFORMATION FOR SEQ ID NO: 160:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 49 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:160
 Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Ser Gln Asn Gln Gln
 1 5 10 15
 Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu
 20 25 30
 Trp Asn Trp Phe Asn Ile Thr Asn Trp Leu Trp Leu Ile Lys Ile Phe
 35 40 45
 Ile
 (2) INFORMATION FOR SEQ ID NO: 161:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 28 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:161
 Glu Ala Ala Ala Arg Glu Ala Ala Ala Arg Glu Ala Ala Ala Arg Leu
 1 5 10 15
 Glu Leu Asp Lys Trp Ala Ser Leu Trp Asn Trp Phe
 20 25
 (2) INFORMATION FOR SEQ ID NO: 162:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 28 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:162
 Arg Met Lys Gln Leu Glu Asp Lys Val Glu Glu Leu Leu Ser Lys Leu
 1 5 10 15
 Glu Leu Asp Lys Trp Ala Ser Leu Trp Asn Trp Phe
 20 25
 (2) INFORMATION FOR SEQ ID NO: 163:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 28 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:163
 Phe Trp Asn Trp Leu Ser Ala Trp Lys Asp Leu Glu Leu Lys Ser Leu
 1 5 10 15
 Leu Glu Glu Val Lys Asp Glu Leu Gln Lys Met Arg
 20 25
 (2) INFORMATION FOR SEQ ID NO: 164:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:164
 Arg Met Lys Gln Leu Glu Asp Lys Val Glu Glu Leu Leu Ser Lys Asn
 1 5 10 15
 Tyr His Leu Glu Asn Glu Leu Glu Leu Asp Lys Trp Ala Ser Leu Trp
 20 25 30
 Asn Trp Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 165:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 30 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:165
 Phe Trp Asn Trp Leu Ser Ala Trp Lys Asp Leu Glu Leu Tyr Pro Gly
 1 5 10 15
 Ser Leu Glu Leu Asp Lys Trp Ala Ser Leu Trp Asn Trp Phe
 20 25 30
 (2) INFORMATION FOR SEQ ID NO: 166:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 15 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:166
 Cys Leu Glu Leu Asp Lys Trp Ala Ser Leu Trp Asn Trp Phe Cys
 1 5 10 15
 (2) INFORMATION FOR SEQ ID NO: 167:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 15 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:167
 Cys Leu Glu Leu Asp Lys Trp Ala Ser Leu Ala Asn Trp Phe Cys
 1 5 10 15
 (2) INFORMATION FOR SEQ ID NO: 168:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 15 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:168
 Cys Leu Glu Leu Asp Lys Trp Ala Ser Leu Trp Asn Phe Phe Cys
 1 5 10 15
 (2) INFORMATION FOR SEQ ID NO: 169:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 13 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:169
 Leu Glu Leu Asp Lys Trp Ala Ser Leu Ala Asn Ala Phe
 1 5 10
 (2) INFORMATION FOR SEQ ID NO: 170:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 13 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:170
 Leu Glu Leu Asp Lys Trp Ala Ser Leu Phe Asn Phe Phe
 1 5 10
 (2) INFORMATION FOR SEQ ID NO: 171:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 13 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:171
 Leu Glu Leu Asp Lys Trp Ala Ser Leu Trp Asn Ala Phe
 1 5 10
 (2) INFORMATION FOR SEQ ID NO: 172:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 13 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:172
 Leu Glu Leu Asp Lys Trp Ala Ser Leu Trp Asn Trp Ala
 1 5 10
 (2) INFORMATION FOR SEQ ID NO: 173:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 13 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:173
 Leu Glu Leu Asp Lys Trp Ala Ser Ala Trp Asn Trp Phe
 1 5 10
 (2) INFORMATION FOR SEQ ID NO: 174:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 13 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:174
 Leu Glu Leu Asp Lys Ala Ala Ser Leu Trp Asn Trp Phe
 1 5 10
 (2) INFORMATION FOR SEQ ID NO: 175:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 13 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:175
 Leu Lys Leu Asp Lys Trp Ala Ser Leu Trp Asn Trp Phe
 1 5 10
 (2) INFORMATION FOR SEQ ID NO: 176:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 13 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:176
 Leu Glu Leu Lys Lys Trp Ala Ser Leu Trp Asn Trp Phe
 1 5 10
 (2) INFORMATION FOR SEQ ID NO: 177:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 39 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:177
 Cys Gly Gly Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Ser Gln
 1 5 10 15
 Asn Gln Gln Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp
 20 25 30
 Ala Ser Leu Trp Asn Trp Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 178:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:178
 Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Ser Gln Asn Gln Gln
 1 5 10 15
 Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu
 20 25 30
 Trp Asn Ala Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 179:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:179
 Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Ser Gln Asn Gln Gln
 1 5 10 15
 Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu
 20 25 30
 Ala Asn Trp Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 180:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:180
 Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Ser Gln Asn Gln Gln
 1 5 10 15
 Glu Lys Asn Glu Gln Gln Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu
 20 25 30
 Trp Asn Trp Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 181:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:181
 Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Ser Gln Asn Gln Gln
 1 5 10 15
 Glu Lys Asn Glu Gln Glu Leu Leu Gln Leu Asp Lys Trp Ala Ser Leu
 20 25 30
 Trp Asn Trp Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 182:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:182
 Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Ser Gln Asn Gln Gln
 1 5 10 15
 Glu Lys Asn Gln Gln Glu Leu Leu Gln Leu Asp Lys Trp Ala Ser Leu
 20 25 30
 Trp Asn Trp Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 183:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:183
 Tyr Thr Ser Leu Ile Gln Ser Leu Ile Glu Glu Ser Gln Asn Gln Gln
 1 5 10 15
 Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu
 20 25 30
 Trp Asn Trp Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 184:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:184
 Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Ser Gln Gln Gln Gln
 1 5 10 15
 Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu
 20 25 30
 Trp Asn Trp Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 185:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:185
 Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Ser Gln Asn Gln Gln
 1 5 10 15
 Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asn Lys Trp Ala Ser Leu
 20 25 30
 Trp Asn Trp Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 186:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:186
 Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Gln Ser Gln Asn Gln Gln
 1 5 10 15
 Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu
 20 25 30
 Trp Asn Trp Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 187:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:187
 Tyr Thr Ser Leu Ile His Ser Leu Ile Gln Glu Ser Gln Asn Gln Gln
 1 5 10 15
 Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu
 20 25 30
 Trp Asn Trp Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 188:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:188
 Tyr Thr Ser Leu Ile His Ser Leu Ile Gln Gln Ser Gln Asn Gln Gln
 1 5 10 15
 Gln Lys Asn Gln Gln Gln Leu Leu Gln Leu Asp Lys Trp Ala Ser Leu
 20 25 30
 Trp Asn Trp Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 189:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:189
 Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Ser Gln Asn Gln Gln
 1 5 10 15
 Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu
 20 25 30
 Ala Asn Ala Ala
 35
 (2) INFORMATION FOR SEQ ID NO: 190:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:190
 Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Ser Gln Asn Gln Gln
 1 5 10 15
 Glu Lys Asn Glu Gln Gln Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu
 20 25 30
 Trp Asn Trp Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 191:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:191
 Tyr Thr Ser Leu Ile Gln Ser Leu Ile Glu Glu Ser Gln Asn Gln Gln
 1 5 10 15
 Glu Lys Asn Glu Gln Gln Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu
 20 25 30
 Trp Asn Trp Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 192:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:192
 Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Ser Gln Asn Gln Gln
 1 5 10 15
 Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu
 20 25 30
 Phe Asn Phe Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 193:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:193
 Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Ser Gln Asn Leu Gln
 1 5 10 15
 Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu
 20 25 30
 Trp Asn Trp Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 194:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:194
 Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Ser Gln Asn Gln Gln
 1 5 10 15
 Glu Lys Leu Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu
 20 25 30
 Trp Asn Trp Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 195:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:195
 Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Ser Gln Asn Gln Gln
 1 5 10 15
 Glu Lys Asn Glu Gln Glu Leu Leu Glu Phe Asp Lys Trp Ala Ser Leu
 20 25 30
 Trp Asn Trp Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 196:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:196
 Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Ser Gln Asn Gln Gln
 1 5 10 15
 Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Pro Ala Ser Leu
 20 25 30
 Trp Asn Trp Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 197:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:197
 Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Ser Gln Asn Gln Gln
 1 5 10 15
 Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Pro
 20 25 30
 Trp Asn Trp Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 198:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:198
 Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Ser Gln Asn Gln Gln
 1 5 10 15
 Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu
 20 25 30
 Trp Asn Ser Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 199:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:199
 Leu Leu Asp Asn Phe Glu Ser Thr Trp Glu Gln Ser Lys Glu Leu Trp
 1 5 10 15
 Glu Gln Gln Glu Ile Ser Ile Gln Asn Leu His Lys Ser Ala Leu Gln
 20 25 30
 Glu Tyr Trp Asn
 35
 (2) INFORMATION FOR SEQ ID NO: 200:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:200
 Leu Ser Asn Leu Leu Gln Ile Ser Asn Asn Ser Asp Glu Trp Leu Glu
 1 5 10 15
 Ala Leu Glu Ile Glu His Glu Lys Trp Lys Leu Thr Gln Trp Gln Ser
 20 25 30
 Tyr Glu Gln Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 201:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 63 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:201
 Met Thr Leu Thr Val Gln Ala Arg Gln Leu Leu Ser Gly Ile Val Gln
 1 5 10 15
 Gln Gln Asn Asn Leu Leu Arg Ala Ile Glu Ala Gln Gln His Leu Leu
 20 25 30
 Gln Leu Thr Val Trp Gly Ile Lys Gln Leu Gln Ala Arg Ile Leu Ala
 35 40 45
 Val Glu Arg Tyr Leu Lys Asp Gln Gln Leu Leu Gly Ile Trp Gly
 50 55 60
 (2) INFORMATION FOR SEQ ID NO: 202:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 45 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:202
 Ser Glu Leu Glu Ile Lys Arg Tyr Lys Asn Arg Val Ala Ser Arg Lys
 1 5 10 15
 Cys Arg Ala Lys Phe Gln Leu Leu Gln His Tyr Arg Glu Val Ala Ala
 20 25 30
 Ala Lys Ser Ser Glu Asn Asp Arg Leu Arg Leu Leu Leu
 35 40 45
 (2) INFORMATION FOR SEQ ID NO: 203:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 45 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:203
 Ala Ser Arg Lys Cys Arg Ala Lys Phe Lys Gln Leu Leu Gln His Tyr
 1 5 10 15
 Arg Glu Val Ala Ala Ala Lys Ser Ser Glu Asn Asp Arg Leu Arg Leu
 20 25 30
 Leu Leu Lys Gln Met Cys Pro Ser Leu Asp Val Asp Ser
 35 40 45
 (2) INFORMATION FOR SEQ ID NO: 204:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:204
 Leu Leu Gln His Tyr Arg Glu Val Ala Ala Ala Lys Ser Ser Glu Asn
 1 5 10 15
 Asp Arg Leu Arg Leu Leu Leu Lys Gln Met Cys Pro Ser Leu Asp Val
 20 25 30
 Asp Ser Ile
 35
 (2) INFORMATION FOR SEQ ID NO: 205:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 45 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:205
 Leu Gln His Tyr Arg Glu Val Ala Ala Ala Lys Ser Ser Glu Asn Asp
 1 5 10 15
 Arg Leu Arg Leu Leu Leu Lys Gln Met Cys Pro Ser Leu Asp Val Asp
 20 25 30
 Ser Ile Ile Pro Arg Thr Pro Asp Val Leu His Glu Asp
 35 40 45
 (2) INFORMATION FOR SEQ ID NO: 206:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:206
 Ser Ser Glu Asn Asp Arg Leu Arg Leu Leu Leu Lys Gln Met Cys Pro
 1 5 10 15
 Ser Leu Asp Val Asp Ser Ile Ile Pro Arg Thr Pro Asp Val Leu His
 20 25 30
 Glu Asp Leu
 35
 (2) INFORMATION FOR SEQ ID NO: 207:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 37 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:207
 Ser Glu Asn Asp Arg Leu Arg Leu Leu Leu Lys Gln Met Cys Pro Ser
 1 5 10 15
 Leu Asp Val Asp Ser Ile Ile Pro Arg Thr Pro Asp Val Leu His Glu
 20 25 30
 Asp Leu Leu Asn Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 208:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 46 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:208
 Pro Leu Leu Val Leu Gln Ala Gly Phe Phe Leu Leu Thr Arg Ile Leu
 1 5 10 15
 Thr Ile Pro Gln Ser Leu Asp Ser Trp Trp Thr Ser Leu Asn Phe Leu
 20 25 30
 Gly Gly Thr Thr Val Cys Leu Gly Gln Asn Ser Gln Ser Pro
 35 40 45
 (2) INFORMATION FOR SEQ ID NO: 209:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 57 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:209
 Pro Gly Tyr Arg Trp Met Cys Leu Arg Arg Phe Ile Ile Phe Leu Phe
 1 5 10 15
 Ile Leu Leu Leu Cys Leu Ile Phe Leu Leu Val Leu Leu Asp Tyr Gln
 20 25 30
 Gly Met Leu Pro Val Cys Pro Leu Ile Pro Gly Ser Ser Thr Ser Thr
 35 40 45
 Gly Pro Cys Arg Thr Cys Met Thr Thr
 50 55
 (2) INFORMATION FOR SEQ ID NO: 210:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:210
 Tyr Thr Ser Val Ile Thr Ile Glu Leu Ser Asn Ile Lys Glu Asn Lys
 1 5 10 15
 Cys Asn Gly Ala Lys Val Lys Leu Ile Lys Gln Glu Leu Asp Lys Tyr
 20 25 30
 Lys
 (2) INFORMATION FOR SEQ ID NO: 211:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:211
 Thr Ser Val Ile Thr Ile Glu Leu Ser Asn Ile Lys Glu Asn Lys Cys
 1 5 10 15
 Asn Gly Ala Lys Val Lys Leu Ile Lys Gln Glu Leu Asp Lys Tyr Lys
 20 25 30
 Asn
 (2) INFORMATION FOR SEQ ID NO: 212:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:212
 Ser Val Ile Thr Ile Glu Leu Ser Asn Ile Lys Glu Asn Lys Cys Asn
 1 5 10 15
 Gly Ala Lys Val Lys Leu Ile Lys Gln Glu Leu Asp Lys Tyr Lys Asn
 20 25 30
 Ala
 (2) INFORMATION FOR SEQ ID NO: 213:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:213
 Val Ile Thr Ile Glu Leu Ser Asn Ile Lys Glu Asn Lys Cys Asn Gly
 1 5 10 15
 Ala Lys Val Lys Leu Ile Lys Gln Glu Leu Asp Lys Tyr Lys Asn Ala
 20 25 30
 Val
 (2) INFORMATION FOR SEQ ID NO: 214:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:214
 Ile Thr Ile Glu Leu Ser Asn Ile Lys Glu Asn Lys Cys Asn Gly Ala
 1 5 10 15
 Lys Val Lys Leu Ile Lys Gln Glu Leu Asp Lys Tyr Lys Asn Ala Val
 20 25 30
 Thr
 (2) INFORMATION FOR SEQ ID NO: 215:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:215
 Thr Ile Glu Leu Ser Asn Ile Lys Glu Asn Lys Cys Asn Gly Ala Lys
 1 5 10 15
 Val Lys Leu Ile Lys Gln Glu Leu Asp Lys Tyr Lys Asn Ala Val Thr
 20 25 30
 Glu
 (2) INFORMATION FOR SEQ ID NO: 216:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:216
 Ile Glu Leu Ser Asn Ile Lys Glu Asn Lys Cys Asn Gly Ala Lys Val
 1 5 10 15
 Lys Leu Ile Lys Gln Glu Leu Asp Lys Tyr Lys Asn Ala Val Thr Glu
 20 25 30
 Leu
 (2) INFORMATION FOR SEQ ID NO: 217:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:217
 Glu Leu Ser Asn Ile Lys Glu Asn Lys Cys Asn Gly Ala Lys Val Lys
 1 5 10 15
 Leu Ile Lys Gln Glu Leu Asp Lys Tyr Lys Asn Ala Val Thr Glu Leu
 20 25 30
 Gln
 (2) INFORMATION FOR SEQ ID NO: 218:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:218
 Leu Ser Asn Ile Lys Glu Asn Lys Cys Asn Gly Ala Lys Val Lys Leu
 1 5 10 15
 Ile Lys Gln Glu Leu Asp Lys Tyr Lys Asn Ala Val Thr Glu Leu Gln
 20 25 30
 Leu
 (2) INFORMATION FOR SEQ ID NO: 219:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:219
 Ser Asn Ile Lys Glu Asn Lys Cys Asn Gly Ala Lys Val Lys Leu Ile
 1 5 10 15
 Lys Gln Glu Leu Asp Lys Tyr Lys Asn Ala Val Thr Glu Leu Gln Leu
 20 25 30
 Leu
 (2) INFORMATION FOR SEQ ID NO: 220:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:220
 Asn Ile Lys Glu Asn Lys Cys Asn Gly Ala Lys Val Lys Leu Ile Lys
 1 5 10 15
 Gln Glu Leu Asp Lys Tyr Lys Asn Ala Val Thr Glu Leu Gln Leu Leu
 20 25 30
 Met
 (2) INFORMATION FOR SEQ ID NO: 221:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:221
 Ile Lys Glu Asn Lys Cys Asn Gly Ala Lys Val Lys Leu Ile Lys Gln
 1 5 10 15
 Glu Leu Asp Lys Tyr Lys Asn Ala Val Thr Glu Leu Gln Leu Leu Met
 20 25 30
 Gln
 (2) INFORMATION FOR SEQ ID NO: 222:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:222
 Lys Glu Asn Lys Cys Asn Gly Ala Lys Val Lys Leu Ile Lys Gln Glu
 1 5 10 15
 Leu Asp Lys Tyr Lys Asn Ala Val Thr Glu Leu Gln Leu Leu Met Gln
 20 25 30
 Ser
 (2) INFORMATION FOR SEQ ID NO: 223:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:223
 Glu Asn Lys Cys Asn Gly Ala Lys Val Lys Leu Ile Lys Gln Glu Leu
 1 5 10 15
 Asp Lys Tyr Lys Asn Ala Val Thr Glu Leu Gln Leu Leu Met Gln Ser
 20 25 30
 Thr
 (2) INFORMATION FOR SEQ ID NO: 224:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 28 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:224
 Ile Glu Leu Ser Asn Ile Lys Glu Asn Lys Cys Asn Gly Thr Asp Ala
 1 5 10 15
 Lys Val Lys Leu Ile Lys Gln Glu Leu Asp Lys Tyr
 20 25
 (2) INFORMATION FOR SEQ ID NO: 225:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 28 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:225
 Glu Asn Lys Cys Asn Gly Thr Asp Ala Lys Val Lys Leu Ile Lys Gln
 1 5 10 15
 Glu Leu Asp Lys Tyr Lys Asn Ala Val Thr Glu Leu
 20 25
 (2) INFORMATION FOR SEQ ID NO: 226:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 28 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:226
 Asp Ala Lys Val Lys Leu Ile Lys Gln Glu Leu Asp Lys Tyr Lys Asn
 1 5 10 15
 Ala Val Thr Glu Leu Gln Leu Leu Met Gln Ser Thr
 20 25
 (2) INFORMATION FOR SEQ ID NO: 227:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 28 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:227
 Cys Asn Gly Thr Asp Ala Lys Val Lys Leu Ile Lys Gln Glu Leu Asp
 1 5 10 15
 Lys Tyr Lys Asn Ala Val Thr Glu Leu Gln Leu Leu
 20 25
 (2) INFORMATION FOR SEQ ID NO: 228:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:228
 Ser Asn Ile Lys Glu Asn Lys Cys Asn Gly Thr Asp Ala Lys Val Lys
 1 5 10 15
 Leu Ile Lys Gln Glu Leu Asp Lys Tyr Lys Asn Ala Val Thr Glu Leu
 20 25 30
 Gln Leu Leu
 35
 (2) INFORMATION FOR SEQ ID NO: 229:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:229
 Ala Ser Gly Val Ala Val Ser Lys Val Leu His Leu Glu Gly Glu Val
 1 5 10 15
 Asn Lys Ile Ala Leu Leu Ser Thr Asn Lys Ala Val Val Ser Leu Ser
 20 25 30
 Asn
 (2) INFORMATION FOR SEQ ID NO: 230:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:230
 Ser Gly Val Ala Val Ser Lys Val Leu His Leu Glu Gly Glu Val Asn
 1 5 10 15
 Lys Ile Ala Leu Leu Ser Thr Asn Lys Ala Val Val Ser Leu Ser Asn
 20 25 30
 Gly
 (2) INFORMATION FOR SEQ ID NO: 231:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:231
 Gly Val Ala Val Ser Lys Val Leu His Leu Glu Gly Glu Val Asn Lys
 1 5 10 15
 Ile Ala Leu Leu Ser Thr Asn Lys Ala Val Val Ser Leu Ser Asn Gly
 20 25 30
 Val
 (2) INFORMATION FOR SEQ ID NO: 232:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:232
 Val Ala Val Ser Lys Val Leu His Leu Glu Gly Glu Val Asn Lys Ile
 1 5 10 15
 Ala Leu Leu Ser Thr Asn Lys Ala Val Val Ser Leu Ser Asn Gly Val
 20 25 30
 Ser
 (2) INFORMATION FOR SEQ ID NO: 233:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:233
 Ala Val Ser Lys Val Leu His Leu Glu Gly Glu Val Asn Lys Ile Ala
 1 5 10 15
 Leu Leu Ser Thr Asn Lys Ala Val Val Ser Leu Ser Asn Gly Val Ser
 20 25 30
 Val
 (2) INFORMATION FOR SEQ ID NO: 234:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:234
 Val Ser Lys Val Leu His Leu Glu Gly Glu Val Asn Lys Ile Ala Leu
 1 5 10 15
 Leu Ser Thr Asn Lys Ala Val Val Ser Leu Ser Asn Gly Val Ser Val
 20 25 30
 Leu
 (2) INFORMATION FOR SEQ ID NO: 235:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:235
 Ser Lys Val Leu His Leu Glu Gly Glu Val Asn Lys Ile Ala Leu Leu
 1 5 10 15
 Ser Thr Asn Lys Ala Val Val Ser Leu Ser Asn Gly Val Ser Val Leu
 20 25 30
 Thr
 (2) INFORMATION FOR SEQ ID NO: 236:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:236
 Lys Val Leu His Leu Glu Gly Glu Val Asn Lys Ile Ala Leu Leu Ser
 1 5 10 15
 Thr Asn Lys Ala Val Val Ser Leu Ser Asn Gly Val Ser Val Leu Thr
 20 25 30
 Ser
 (2) INFORMATION FOR SEQ ID NO: 237:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:237
 Val Leu His Leu Glu Gly Glu Val Asn Lys Ile Ala Leu Leu Ser Thr
 1 5 10 15
 Asn Lys Ala Val Val Ser Leu Ser Asn Gly Val Ser Val Leu Thr Ser
 20 25 30
 Lys
 (2) INFORMATION FOR SEQ ID NO: 238:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:238
 Leu His Leu Glu Gly Glu Val Asn Lys Ile Ala Leu Leu Ser Thr Asn
 1 5 10 15
 Lys Ala Val Val Ser Leu Ser Asn Gly Val Ser Val Leu Thr Ser Lys
 20 25 30
 Val
 (2) INFORMATION FOR SEQ ID NO: 239:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:239
 His Leu Glu Gly Glu Val Asn Lys Ile Ala Leu Leu Ser Thr Asn Lys
 1 5 10 15
 Ala Val Val Ser Leu Ser Asn Gly Val Ser Val Leu Thr Ser Lys Val
 20 25 30
 Leu
 (2) INFORMATION FOR SEQ ID NO: 240:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:240
 Leu Glu Gly Glu Val Asn Lys Ile Ala Leu Leu Ser Thr Asn Lys Ala
 1 5 10 15
 Val Val Ser Leu Ser Asn Gly Val Ser Val Leu Thr Ser Lys Val Leu
 20 25 30
 Asp
 (2) INFORMATION FOR SEQ ID NO: 241:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:241
 Glu Gly Glu Val Asn Lys Ile Ala Leu Leu Ser Thr Asn Lys Ala Val
 1 5 10 15
 Val Ser Leu Ser Asn Gly Val Ser Val Leu Thr Ser Lys Val Leu Asp
 20 25 30
 Leu
 (2) INFORMATION FOR SEQ ID NO: 242:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:242
 Gly Glu Val Asn Lys Ile Ala Leu Leu Ser Thr Asn Lys Ala Val Val
 1 5 10 15
 Ser Leu Ser Asn Gly Val Ser Val Leu Thr Ser Lys Val Leu Asp Leu
 20 25 30
 Lys
 (2) INFORMATION FOR SEQ ID NO: 243:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:243
 Glu Val Asn Lys Ile Ala Leu Leu Ser Thr Asn Lys Ala Val Val Ser
 1 5 10 15
 Leu Ser Asn Gly Val Ser Val Leu Thr Ser Lys Val Leu Asp Leu Lys
 20 25 30
 Asn
 (2) INFORMATION FOR SEQ ID NO: 244:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:244
 Val Asn Lys Ile Ala Leu Leu Ser Thr Asn Lys Ala Val Val Ser Leu
 1 5 10 15
 Ser Asn Gly Val Ser Val Leu Thr Ser Lys Val Leu Asp Leu Lys Asn
 20 25 30
 Tyr
 (2) INFORMATION FOR SEQ ID NO: 245:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:245
 Asn Lys Ile Ala Leu Leu Ser Thr Asn Lys Ala Val Val Ser Leu Ser
 1 5 10 15
 Asn Gly Val Ser Val Leu Thr Ser Lys Val Leu Asp Leu Lys Asn Tyr
 20 25 30
 Ile
 (2) INFORMATION FOR SEQ ID NO: 246:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:246
 Lys Ile Ala Leu Leu Ser Thr Asn Lys Ala Val Val Ser Leu Ser Asn
 1 5 10 15
 Gly Val Ser Val Leu Thr Ser Lys Val Leu Asp Leu Lys Asn Tyr Ile
 20 25 30
 Asp
 (2) INFORMATION FOR SEQ ID NO: 247:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:247
 Ile Ala Leu Leu Ser Thr Asn Lys Ala Val Val Ser Leu Ser Asn Gly
 1 5 10 15
 Val Ser Val Leu Thr Ser Lys Val Leu Asp Leu Lys Asn Tyr Ile Asp
 20 25 30
 Lys
 (2) INFORMATION FOR SEQ ID NO: 248:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:248
 Ala Leu Leu Ser Thr Asn Lys Ala Val Val Ser Leu Ser Asn Gly Val
 1 5 10 15
 Ser Val Leu Thr Ser Lys Val Leu Asp Leu Lys Asn Tyr Ile Asp Lys
 20 25 30
 Gln
 (2) INFORMATION FOR SEQ ID NO: 249:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:249
 Leu Leu Ser Thr Asn Lys Ala Val Val Ser Leu Ser Asn Gly Val Ser
 1 5 10 15
 Val Leu Thr Ser Lys Val Leu Asp Leu Lys Asn Tyr Ile Asp Lys Gln
 20 25 30
 Leu
 (2) INFORMATION FOR SEQ ID NO: 250:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:250
 Leu Ser Thr Asn Lys Ala Val Val Ser Leu Ser Asn Gly Val Ser Val
 1 5 10 15
 Leu Thr Ser Lys Val Leu Asp Leu Lys Asn Tyr Ile Asp Lys Gln Leu
 20 25 30
 Leu
 (2) INFORMATION FOR SEQ ID NO: 251:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:251
 Ser Gly Val Ala Val Ser Lys Val Leu His Leu Glu Gly Glu Val Asn
 1 5 10 15
 Lys Ile Lys Ser Ala Leu Leu Ser Thr Asn Lys Ala Val Val Ser Leu
 20 25 30
 Ser Asn Gly
 35
 (2) INFORMATION FOR SEQ ID NO: 252:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 27 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:252
 Val Val Ser Leu Ser Asn Gly Val Ser Val Leu Thr Ser Lys Val Leu
 1 5 10 15
 Asp Leu Lys Asn Tyr Ile Asp Lys Gln Leu Leu
 20 25
 (2) INFORMATION FOR SEQ ID NO: 253:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 28 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:253
 Val Asn Lys Ile Lys Ser Ala Leu Leu Ser Thr Asn Lys Ala Val Val
 1 5 10 15
 Ser Leu Ser Asn Gly Val Ser Val Leu Thr Ser Lys
 20 25
 (2) INFORMATION FOR SEQ ID NO: 254:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 28 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:254
 Asp Glu Phe Asp Ala Ser Ile Ser Gln Val Asn Glu Lys Ile Asn Gln
 1 5 10 15
 Ser Leu Ala Phe Ile Arg Lys Ser Asp Glu Leu Leu
 20 25
 (2) INFORMATION FOR SEQ ID NO: 255:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:255
 Ile Ile Asn Phe Tyr Asp Pro Leu Val Phe Pro Ser Asp Glu Phe Asp
 1 5 10 15
 Ala Ser Ile Ser Gln Val Asn Glu Lys Ile Asn Gln Ser Leu Ala Phe
 20 25 30
 Ile Arg Lys
 35
 (2) INFORMATION FOR SEQ ID NO: 256:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:256
 Ile Asn Phe Tyr Asp Pro Leu Val Phe Pro Ser Asp Glu Phe Asp Ala
 1 5 10 15
 Ser Ile Ser Gln Val Asn Glu Lys Ile Asn Gln Ser Leu Ala Phe Ile
 20 25 30
 Arg Lys Ser
 35
 (2) INFORMATION FOR SEQ ID NO: 257:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:257
 Asn Phe Tyr Asp Pro Leu Val Phe Pro Ser Asp Glu Phe Asp Ala Ser
 1 5 10 15
 Ile Ser Gln Val Asn Glu Lys Ile Asn Gln Ser Leu Ala Phe Ile Arg
 20 25 30
 Lys Ser Asp
 35
 (2) INFORMATION FOR SEQ ID NO: 258:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:258
 Phe Tyr Asp Pro Leu Val Phe Pro Ser Asp Glu Phe Asp Ala Ser Ile
 1 5 10 15
 Ser Gln Val Asn Glu Lys Ile Asn Gln Ser Leu Ala Phe Ile Arg Lys
 20 25 30
 Ser Asp Glu
 35
 (2) INFORMATION FOR SEQ ID NO: 259:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:259
 Tyr Asp Pro Leu Val Phe Pro Ser Asp Glu Phe Asp Ala Ser Ile Ser
 1 5 10 15
 Gln Val Asn Glu Lys Ile Asn Gln Ser Leu Ala Phe Ile Arg Lys Ser
 20 25 30
 Asp Glu Leu
 35
 (2) INFORMATION FOR SEQ ID NO: 260:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:260
 Asp Pro Leu Val Phe Pro Ser Asp Glu Phe Asp Ala Ser Ile Ser Gln
 1 5 10 15
 Val Asn Glu Lys Ile Asn Gln Ser Leu Ala Phe Ile Arg Lys Ser Asp
 20 25 30
 Glu Leu Leu
 35
 (2) INFORMATION FOR SEQ ID NO: 261:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:261
 Pro Leu Val Phe Pro Ser Asp Glu Phe Asp Ala Ser Ile Ser Gln Val
 1 5 10 15
 Asn Glu Lys Ile Asn Gln Ser Leu Ala Phe Ile Arg Lys Ser Asp Glu
 20 25 30
 Leu Leu His
 35
 (2) INFORMATION FOR SEQ ID NO: 262:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:262
 Leu Val Phe Pro Ser Asp Glu Phe Asp Ala Ser Ile Ser Gln Val Asn
 1 5 10 15
 Glu Lys Ile Asn Gln Ser Leu Ala Phe Ile Arg Lys Ser Asp Glu Leu
 20 25 30
 Leu His Asn
 35
 (2) INFORMATION FOR SEQ ID NO: 263:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:263
 Val Phe Pro Ser Asp Glu Phe Asp Ala Ser Ile Ser Gln Val Asn Glu
 1 5 10 15
 Lys Ile Asn Gln Ser Leu Ala Phe Ile Arg Lys Ser Asp Glu Leu Leu
 20 25 30
 His Asn Val
 35
 (2) INFORMATION FOR SEQ ID NO: 264:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:264
 Phe Pro Ser Asp Glu Phe Asp Ala Ser Ile Ser Gln Val Asn Glu Lys
 1 5 10 15
 Ile Asn Gln Ser Leu Ala Phe Ile Arg Lys Ser Asp Glu Leu Leu His
 20 25 30
 Asn Val Asn
 35
 (2) INFORMATION FOR SEQ ID NO: 265:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:265
 Pro Ser Asp Glu Phe Asp Ala Ser Ile Ser Gln Val Asn Glu Lys Ile
 1 5 10 15
 Asn Gln Ser Leu Ala Phe Ile Arg Lys Ser Asp Glu Leu Leu His Asn
 20 25 30
 Val Asn Ala
 35
 (2) INFORMATION FOR SEQ ID NO: 266:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:266
 Ser Asp Glu Phe Asp Ala Ser Ile Ser Gln Val Asn Glu Lys Ile Asn
 1 5 10 15
 Gln Ser Leu Ala Phe Ile Arg Lys Ser Asp Glu Leu Leu His Asn Val
 20 25 30
 Asn Ala Gly
 35
 (2) INFORMATION FOR SEQ ID NO: 267:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:267
 Asp Glu Phe Asp Ala Ser Ile Ser Gln Val Asn Glu Lys Ile Asn Gln
 1 5 10 15
 Ser Leu Ala Phe Ile Arg Lys Ser Asp Glu Leu Leu His Asn Val Asn
 20 25 30
 Ala Gly Lys
 35
 (2) INFORMATION FOR SEQ ID NO: 268:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:268
 Glu Phe Asp Ala Ser Ile Ser Gln Val Asn Glu Lys Ile Asn Gln Ser
 1 5 10 15
 Leu Ala Phe Ile Arg Lys Ser Asp Glu Leu Leu His Asn Val Asn Ala
 20 25 30
 Gly Lys Ser
 35
 (2) INFORMATION FOR SEQ ID NO: 269:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:269
 Phe Asp Ala Ser Ile Ser Gln Val Asn Glu Lys Ile Asn Gln Ser Leu
 1 5 10 15
 Ala Phe Ile Arg Lys Ser Asp Glu Leu Leu His Asn Val Asn Ala Gly
 20 25 30
 Lys Ser Thr
 35
 (2) INFORMATION FOR SEQ ID NO: 270:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:270
 Asp Ala Ser Ile Ser Gln Val Asn Glu Lys Ile Asn Gln Ser Leu Ala
 1 5 10 15
 Phe Ile Arg Lys Ser Asp Glu Leu Leu His Asn Val Asn Ala Gly Lys
 20 25 30
 Ser Thr Thr
 35
 (2) INFORMATION FOR SEQ ID NO: 271:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 12 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:271
 Glu Leu Leu His Asn Val Asn Ala Gly Lys Ser Thr
 1 5 10
 (2) INFORMATION FOR SEQ ID NO: 272:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 15 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:272
 Lys Ser Asp Glu Leu Leu His Asn Val Asn Ala Gly Lys Ser Thr
 1 5 10 15
 (2) INFORMATION FOR SEQ ID NO: 273:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 17 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:273
 Ile Arg Lys Ser Asp Glu Leu Leu His Asn Val Asn Ala Gly Lys Ser
 1 5 10 15
 Thr
 (2) INFORMATION FOR SEQ ID NO: 274:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 21 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:274
 Phe Asp Ala Ser Ile Ser Gln Val Asn Glu Lys Ile Asn Gln Ser Leu
 1 5 10 15
 Ala Phe Ile Arg Lys
 20
 (2) INFORMATION FOR SEQ ID NO: 275:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 31 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:275
 Phe Asp Ala Ser Ile Ser Gln Val Asn Glu Lys Ile Asn Gln Ser Leu
 1 5 10 15
 Ala Phe Ile Arg Lys Ser Asp Glu Leu Leu His Asn Val Asn Ala
 20 25 30
 (2) INFORMATION FOR SEQ ID NO: 276:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 29 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:276
 Phe Asp Ala Ser Ile Ser Gln Val Asn Glu Lys Ile Asn Gln Ser Leu
 1 5 10 15
 Ala Phe Ile Arg Lys Ser Asp Glu Leu Leu His Asn Val
 20 25
 (2) INFORMATION FOR SEQ ID NO: 277:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 27 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:277
 Phe Asp Ala Ser Ile Ser Gln Val Asn Glu Lys Ile Asn Gln Ser Leu
 1 5 10 15
 Ala Phe Ile Arg Lys Ser Asp Glu Leu Leu His
 20 25
 (2) INFORMATION FOR SEQ ID NO: 278:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 25 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:278
 Phe Asp Ala Ser Ile Ser Gln Val Asn Glu Lys Ile Asn Gln Ser Leu
 1 5 10 15
 Ala Phe Ile Arg Lys Ser Asp Glu Leu
 20 25
 (2) INFORMATION FOR SEQ ID NO: 279:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 23 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:279
 Phe Asp Ala Ser Ile Ser Gln Val Asn Glu Lys Ile Asn Gln Ser Leu
 1 5 10 15
 Ala Phe Ile Arg Lys Ser Asp
 20
 (2) INFORMATION FOR SEQ ID NO: 280:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 31 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:280
 Ile Ser Gln Val Asn Glu Lys Ile Asn Gln Ser Leu Ala Phe Ile Arg
 1 5 10 15
 Lys Ser Asp Glu Leu Leu His Asn Val Asn Ala Gly Lys Ser Thr
 20 25 30
 (2) INFORMATION FOR SEQ ID NO: 281:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 29 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:281
 Gln Val Asn Glu Lys Ile Asn Gln Ser Leu Ala Phe Ile Arg Lys Ser
 1 5 10 15
 Asp Glu Leu Leu His Asn Val Asn Ala Gly Lys Ser Thr
 20 25
 (2) INFORMATION FOR SEQ ID NO: 282:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 27 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:282
 Asn Glu Lys Ile Asn Gln Ser Leu Ala Phe Ile Arg Lys Ser Asp Glu
 1 5 10 15
 Leu Leu His Asn Val Asn Ala Gly Lys Ser Thr
 20 25
 (2) INFORMATION FOR SEQ ID NO: 283:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 25 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:283
 Lys Ile Asn Gln Ser Leu Ala Phe Ile Arg Lys Ser Asp Glu Leu Leu
 1 5 10 15
 His Asn Val Asn Ala Gly Lys Ser Thr
 20 25
 (2) INFORMATION FOR SEQ ID NO: 284:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 23 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:284
 Asn Gln Ser Leu Ala Phe Ile Arg Lys Ser Asp Glu Leu Leu His Asn
 1 5 10 15
 Val Asn Ala Gly Lys Ser Thr
 20
 (2) INFORMATION FOR SEQ ID NO: 285:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:285
 Ala Leu Gly Val Ala Thr Ser Ala Gln Ile Thr Ala Ala Val Ala Leu
 1 5 10 15
 Val Glu Ala Lys Gln Ala Arg Ser Asp Ile Glu Lys Leu Lys Glu Ala
 20 25 30
 Ile Arg Asp
 35
 (2) INFORMATION FOR SEQ ID NO: 286:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:286
 Leu Gly Val Ala Thr Ser Ala Gln Ile Thr Ala Ala Val Ala Leu Val
 1 5 10 15
 Glu Ala Lys Gln Ala Arg Ser Asp Ile Glu Lys Leu Lys Glu Ala Ile
 20 25 30
 Arg Asp Thr
 35
 (2) INFORMATION FOR SEQ ID NO: 287:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:287
 Gly Val Ala Thr Ser Ala Gln Ile Thr Ala Ala Val Ala Leu Val Glu
 1 5 10 15
 Ala Lys Gln Ala Arg Ser Asp Ile Glu Lys Leu Lys Glu Ala Ile Arg
 20 25 30
 Asp Thr Asn
 35
 (2) INFORMATION FOR SEQ ID NO: 288:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:288
 Val Ala Thr Ser Ala Gln Ile Thr Ala Ala Val Ala Leu Val Glu Ala
 1 5 10 15
 Lys Gln Ala Arg Ser Asp Ile Glu Lys Leu Lys Glu Ala Ile Arg Asp
 20 25 30
 Thr Asn Lys
 35
 (2) INFORMATION FOR SEQ ID NO: 289:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:289
 Ala Thr Ser Ala Gln Ile Thr Ala Ala Val Ala Leu Val Glu Ala Lys
 1 5 10 15
 Gln Ala Arg Ser Asp Ile Glu Lys Leu Lys Glu Ala Ile Arg Asp Thr
 20 25 30
 Asn Lys Ala
 35
 (2) INFORMATION FOR SEQ ID NO: 290:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:290
 Thr Ser Ala Gln Ile Thr Ala Ala Val Ala Leu Val Glu Ala Lys Gln
 1 5 10 15
 Ala Arg Ser Asp Ile Glu Lys Leu Lys Glu Ala Ile Arg Asp Thr Asn
 20 25 30
 Lys Ala Val
 35
 (2) INFORMATION FOR SEQ ID NO: 291:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:291
 Ser Ala Gln Ile Thr Ala Ala Val Ala Leu Val Glu Ala Lys Gln Ala
 1 5 10 15
 Arg Ser Asp Ile Glu Lys Leu Lys Glu Ala Ile Arg Asp Thr Asn Lys
 20 25 30
 Ala Val Gln
 35
 (2) INFORMATION FOR SEQ ID NO: 292:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:292
 Ala Gln Ile Thr Ala Ala Val Ala Leu Val Glu Ala Lys Gln Ala Arg
 1 5 10 15
 Ser Asp Ile Glu Lys Leu Lys Glu Ala Ile Arg Asp Thr Asn Lys Ala
 20 25 30
 Val Gln Ser
 35
 (2) INFORMATION FOR SEQ ID NO: 293:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:293
 Gln Ile Thr Ala Ala Val Ala Leu Val Glu Ala Lys Gln Ala Arg Ser
 1 5 10 15
 Asp Ile Glu Lys Leu Lys Glu Ala Ile Arg Asp Thr Asn Lys Ala Val
 20 25 30
 Gln Ser Val
 35
 (2) INFORMATION FOR SEQ ID NO: 294:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:294
 Ile Thr Ala Ala Val Ala Leu Val Glu Ala Lys Gln Ala Arg Ser Asp
 1 5 10 15
 Ile Glu Lys Leu Lys Glu Ala Ile Arg Asp Thr Asn Lys Ala Val Gln
 20 25 30
 Ser Val Gln
 35
 (2) INFORMATION FOR SEQ ID NO: 295:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:295
 Thr Ala Ala Val Ala Leu Val Glu Ala Lys Gln Ala Arg Ser Asp Ile
 1 5 10 15
 Glu Lys Leu Lys Glu Ala Ile Arg Asp Thr Asn Lys Ala Val Gln Ser
 20 25 30
 Val Gln Ser
 35
 (2) INFORMATION FOR SEQ ID NO: 296:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:296
 Ala Ala Val Ala Leu Val Glu Ala Lys Gln Ala Arg Ser Asp Ile Glu
 1 5 10 15
 Lys Leu Lys Glu Ala Ile Arg Asp Thr Asn Lys Ala Val Gln Ser Val
 20 25 30
 Gln Ser Ser
 35
 (2) INFORMATION FOR SEQ ID NO: 297:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:297
 Ala Val Ala Leu Val Glu Ala Lys Gln Ala Arg Ser Asp Ile Glu Lys
 1 5 10 15
 Leu Lys Glu Ala Ile Arg Asp Thr Asn Lys Ala Val Gln Ser Val Gln
 20 25 30
 Ser Ser Ile
 35
 (2) INFORMATION FOR SEQ ID NO: 298:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:298
 Val Ala Leu Val Glu Ala Lys Gln Ala Arg Ser Asp Ile Glu Lys Leu
 1 5 10 15
 Lys Glu Ala Ile Arg Asp Thr Asn Lys Ala Val Gln Ser Val Gln Ser
 20 25 30
 Ser Ile Gly
 35
 (2) INFORMATION FOR SEQ ID NO: 299:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:299
 Ala Leu Val Glu Ala Lys Gln Ala Arg Ser Asp Ile Glu Lys Leu Lys
 1 5 10 15
 Glu Ala Ile Arg Asp Thr Asn Lys Ala Val Gln Ser Val Gln Ser Ser
 20 25 30
 Ile Gly Asn
 35
 (2) INFORMATION FOR SEQ ID NO: 300:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:300
 Leu Val Glu Ala Lys Gln Ala Arg Ser Asp Ile Glu Lys Leu Lys Glu
 1 5 10 15
 Ala Ile Arg Asp Thr Asn Lys Ala Val Gln Ser Val Gln Ser Ser Ile
 20 25 30
 Gly Asn Leu
 35
 (2) INFORMATION FOR SEQ ID NO: 301:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:301
 Val Glu Ala Lys Gln Ala Arg Ser Asp Ile Glu Lys Leu Lys Glu Ala
 1 5 10 15
 Ile Arg Asp Thr Asn Lys Ala Val Gln Ser Val Gln Ser Ser Ile Gly
 20 25 30
 Asn Leu Ile
 35
 (2) INFORMATION FOR SEQ ID NO: 302:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:302
 Glu Ala Lys Gln Ala Arg Ser Asp Ile Glu Lys Leu Lys Glu Ala Ile
 1 5 10 15
 Arg Asp Thr Asn Lys Ala Val Gln Ser Val Gln Ser Ser Ile Gly Asn
 20 25 30
 Leu Ile Val
 35
 (2) INFORMATION FOR SEQ ID NO: 303:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:303
 Ala Lys Gln Ala Arg Ser Asp Ile Glu Lys Leu Lys Glu Ala Ile Arg
 1 5 10 15
 Asp Thr Asn Lys Ala Val Gln Ser Val Gln Ser Ser Ile Gly Asn Leu
 20 25 30
 Ile Val Ala
 35
 (2) INFORMATION FOR SEQ ID NO: 304:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:304
 Lys Gln Ala Arg Ser Asp Ile Glu Lys Leu Lys Glu Ala Ile Arg Asp
 1 5 10 15
 Thr Asn Lys Ala Val Gln Ser Val Gln Ser Ser Ile Gly Asn Leu Ile
 20 25 30
 Val Ala Ile
 35
 (2) INFORMATION FOR SEQ ID NO: 305:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:305
 Gln Ala Arg Ser Asp Ile Glu Lys Leu Lys Glu Ala Ile Arg Asp Thr
 1 5 10 15
 Asn Lys Ala Val Gln Ser Val Gln Ser Ser Ile Gly Asn Leu Ile Val
 20 25 30
 Ala Ile Lys
 35
 (2) INFORMATION FOR SEQ ID NO: 306:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:306
 Ala Arg Ser Asp Ile Glu Lys Leu Lys Glu Ala Ile Arg Asp Thr Asn
 1 5 10 15
 Lys Ala Val Gln Ser Val Gln Ser Ser Ile Gly Asn Leu Ile Val Ala
 20 25 30
 Ile Lys Ser
 35
 (2) INFORMATION FOR SEQ ID NO: 307:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:307
 Arg Ser Asp Ile Glu Lys Leu Lys Glu Ala Ile Arg Asp Thr Asn Lys
 1 5 10 15
 Ala Val Gln Ser Val Gln Ser Ser Ile Gly Asn Leu Ile Val Ala Ile
 20 25 30
 Lys Ser Val
 35
 (2) INFORMATION FOR SEQ ID NO: 308:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:308
 Ser Asp Ile Glu Lys Leu Lys Glu Ala Ile Arg Asp Thr Asn Lys Ala
 1 5 10 15
 Val Gln Ser Val Gln Ser Ser Ile Gly Asn Leu Ile Val Ala Ile Lys
 20 25 30
 Ser Val Gln
 35
 (2) INFORMATION FOR SEQ ID NO: 309:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:309
 Asp Ile Glu Lys Leu Lys Glu Ala Ile Arg Asp Thr Asn Lys Ala Val
 1 5 10 15
 Gln Ser Val Gln Ser Ser Ile Gly Asn Leu Ile Val Ala Ile Lys Ser
 20 25 30
 Val Gln Asp
 35
 (2) INFORMATION FOR SEQ ID NO: 310:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:310
 Ile Glu Lys Leu Lys Glu Ala Ile Arg Asp Thr Asn Lys Ala Val Gln
 1 5 10 15
 Ser Val Gln Ser Ser Ile Gly Asn Leu Ile Val Ala Ile Lys Ser Val
 20 25 30
 Gln Asp Tyr
 35
 (2) INFORMATION FOR SEQ ID NO: 311:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:311
 Glu Lys Leu Lys Glu Ala Ile Arg Asp Thr Asn Lys Ala Val Gln Ser
 1 5 10 15
 Val Gln Ser Ser Ile Gly Asn Leu Ile Val Ala Ile Lys Ser Val Gln
 20 25 30
 Asp Tyr Val
 35
 (2) INFORMATION FOR SEQ ID NO: 312:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:312
 Lys Leu Lys Glu Ala Ile Arg Asp Thr Asn Lys Ala Val Gln Ser Val
 1 5 10 15
 Gln Ser Ser Ile Gly Asn Leu Ile Val Ala Ile Lys Ser Val Gln Asp
 20 25 30
 Tyr Val Asn
 35
 (2) INFORMATION FOR SEQ ID NO: 313:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:313
 Leu Lys Glu Ala Ile Arg Asp Thr Asn Lys Ala Val Gln Ser Val Gln
 1 5 10 15
 Ser Ser Ile Gly Asn Leu Ile Val Ala Ile Lys Ser Val Gln Asp Tyr
 20 25 30
 Val Asn Lys
 35
 (2) INFORMATION FOR SEQ ID NO: 314:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:314
 Lys Glu Ala Ile Arg Asp Thr Asn Lys Ala Val Gln Ser Val Gln Ser
 1 5 10 15
 Ser Ile Gly Asn Leu Ile Val Ala Ile Lys Ser Val Gln Asp Tyr Val
 20 25 30
 Asn Lys Glu
 35
 (2) INFORMATION FOR SEQ ID NO: 315:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:315
 Glu Ala Ile Arg Asp Thr Asn Lys Ala Val Gln Ser Val Gln Ser Ser
 1 5 10 15
 Ile Gly Asn Leu Ile Val Ala Ile Lys Ser Val Gln Asp Tyr Val Asn
 20 25 30
 Lys Glu Ile
 35
 (2) INFORMATION FOR SEQ ID NO: 316:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:316
 Ala Ile Arg Asp Thr Asn Lys Ala Val Gln Ser Val Gln Ser Ser Ile
 1 5 10 15
 Gly Asn Leu Ile Val Ala Ile Lys Ser Val Gln Asp Tyr Val Asn Lys
 20 25 30
 Glu Ile Val
 35
 (2) INFORMATION FOR SEQ ID NO: 317:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:317
 Ile Arg Asp Thr Asn Lys Ala Val Gln Ser Val Gln Ser Ser Ile Gly
 1 5 10 15
 Asn Leu Ile Val Ala Ile Lys Ser Val Gln Asp Tyr Val Asn Lys Glu
 20 25 30
 Ile Val Pro
 35
 (2) INFORMATION FOR SEQ ID NO: 318:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 28 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:318
 Ala Ala Val Ala Leu Val Glu Ala Lys Gln Ala Arg Ser Asp Ile Glu
 1 5 10 15
 Lys Leu Lys Glu Ala Ile Arg Asp Thr Asn Lys Ala
 20 25
 (2) INFORMATION FOR SEQ ID NO: 319:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 28 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:319
 Ala Lys Gln Ala Arg Ser Asp Ile Glu Lys Leu Lys Glu Ala Ile Arg
 1 5 10 15
 Asp Thr Asn Lys Ala Val Gln Ser Val Gln Ser Ser
 20 25
 (2) INFORMATION FOR SEQ ID NO: 320:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 28 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:320
 Ile Glu Lys Leu Lys Glu Ala Ile Arg Asp Thr Asn Lys Ala Val Gln
 1 5 10 15
 Ser Val Gln Ser Ser Ile Gly Asn Leu Ile Val Ala
 20 25
 (2) INFORMATION FOR SEQ ID NO: 321:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:321
 Tyr Thr Pro Asn Asp Ile Thr Leu Asn Asn Ser Val Ala Leu Asp Pro
 1 5 10 15
 Ile Asp Ile Ser Ile Glu Leu Asn Lys Ala Lys Ser Asp Leu Glu Glu
 20 25 30
 Ser Lys Glu
 35
 (2) INFORMATION FOR SEQ ID NO: 322:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:322
 Thr Pro Asn Asp Ile Thr Leu Asn Asn Ser Val Ala Leu Asp Pro Ile
 1 5 10 15
 Asp Ile Ser Ile Glu Leu Asn Lys Ala Lys Ser Asp Leu Glu Glu Ser
 20 25 30
 Lys Glu Trp
 35
 (2) INFORMATION FOR SEQ ID NO: 323:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:323
 Pro Asn Asp Ile Thr Leu Asn Asn Ser Val Ala Leu Asp Pro Ile Asp
 1 5 10 15
 Ile Ser Ile Glu Leu Asn Lys Ala Lys Ser Asp Leu Glu Glu Ser Lys
 20 25 30
 Glu Trp Ile
 35
 (2) INFORMATION FOR SEQ ID NO: 324:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:324
 Asn Asp Ile Thr Leu Asn Asn Ser Val Ala Leu Asp Pro Ile Asp Ile
 1 5 10 15
 Ser Ile Glu Leu Asn Lys Ala Lys Ser Asp Leu Glu Glu Ser Lys Glu
 20 25 30
 Trp Ile Arg
 35
 (2) INFORMATION FOR SEQ ID NO: 325:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:325
 Asp Ile Thr Leu Asn Asn Ser Val Ala Leu Asp Pro Ile Asp Ile Ser
 1 5 10 15
 Ile Glu Leu Asn Lys Ala Lys Ser Asp Leu Glu Glu Ser Lys Glu Trp
 20 25 30
 Ile Arg Arg
 35
 (2) INFORMATION FOR SEQ ID NO: 326:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:326
 Ile Thr Leu Asn Asn Ser Val Ala Leu Asp Pro Ile Asp Ile Ser Ile
 1 5 10 15
 Glu Leu Asn Lys Ala Lys Ser Asp Leu Glu Glu Ser Lys Glu Trp Ile
 20 25 30
 Arg Arg Ser
 35
 (2) INFORMATION FOR SEQ ID NO: 327:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:327
 Thr Leu Asn Asn Ser Val Ala Leu Asp Pro Ile Asp Ile Ser Ile Glu
 1 5 10 15
 Leu Asn Lys Ala Lys Ser Asp Leu Glu Glu Ser Lys Glu Trp Ile Arg
 20 25 30
 Arg Ser Asn
 35
 (2) INFORMATION FOR SEQ ID NO: 328:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:328
 Leu Asn Asn Ser Val Ala Leu Asp Pro Ile Asp Ile Ser Ile Glu Leu
 1 5 10 15
 Asn Lys Ala Lys Ser Asp Leu Glu Glu Ser Lys Glu Trp Ile Arg Arg
 20 25 30
 Ser Asn Gln
 35
 (2) INFORMATION FOR SEQ ID NO: 329:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:329
 Asn Asn Ser Val Ala Leu Asp Pro Ile Asp Ile Ser Ile Glu Leu Asn
 1 5 10 15
 Lys Ala Lys Ser Asp Leu Glu Glu Ser Lys Glu Trp Ile Arg Arg Ser
 20 25 30
 Asn Gln Lys
 35
 (2) INFORMATION FOR SEQ ID NO: 330:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:330
 Asn Ser Val Ala Leu Asp Pro Ile Asp Ile Ser Ile Glu Leu Asn Lys
 1 5 10 15
 Ala Lys Ser Asp Leu Glu Glu Ser Lys Glu Trp Ile Arg Arg Ser Asn
 20 25 30
 Gln Lys Leu
 35
 (2) INFORMATION FOR SEQ ID NO: 331:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:331
 Ser Val Ala Leu Asp Pro Ile Asp Ile Ser Ile Glu Leu Asn Lys Ala
 1 5 10 15
 Lys Ser Asp Leu Glu Glu Ser Lys Glu Trp Ile Arg Arg Ser Asn Gln
 20 25 30
 Lys Leu Asp
 35
 (2) INFORMATION FOR SEQ ID NO: 332:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:332
 Val Ala Leu Asp Pro Ile Asp Ile Ser Ile Glu Leu Asn Lys Ala Lys
 1 5 10 15
 Ser Asp Leu Glu Glu Ser Lys Glu Trp Ile Arg Arg Ser Asn Gln Lys
 20 25 30
 Leu Asp Ser
 35
 (2) INFORMATION FOR SEQ ID NO: 333:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:333
 Ala Leu Asp Pro Ile Asp Ile Ser Ile Glu Leu Asn Lys Ala Lys Ser
 1 5 10 15
 Asp Leu Glu Glu Ser Lys Glu Trp Ile Arg Arg Ser Asn Gln Lys Leu
 20 25 30
 Asp Ser Ile
 35
 (2) INFORMATION FOR SEQ ID NO: 334:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:334
 Leu Asp Pro Ile Asp Ile Ser Ile Glu Leu Asn Lys Ala Lys Ser Asp
 1 5 10 15
 Leu Glu Glu Ser Lys Glu Trp Ile Arg Arg Ser Asn Gln Lys Leu Asp
 20 25 30
 Ser Ile Gly
 35
 (2) INFORMATION FOR SEQ ID NO: 335:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:335
 Asp Pro Ile Asp Ile Ser Ile Glu Leu Asn Lys Ala Lys Ser Asp Leu
 1 5 10 15
 Glu Glu Ser Lys Glu Trp Ile Arg Arg Ser Asn Gln Lys Leu Asp Ser
 20 25 30
 Ile Gly Asn
 35
 (2) INFORMATION FOR SEQ ID NO: 336:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:336
 Pro Ile Asp Ile Ser Ile Glu Leu Asn Lys Ala Lys Ser Asp Leu Glu
 1 5 10 15
 Glu Ser Lys Glu Trp Ile Arg Arg Ser Asn Gln Lys Leu Asp Ser Ile
 20 25 30
 Gly Asn Trp
 35
 (2) INFORMATION FOR SEQ ID NO: 337:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:337
 Ile Asp Ile Ser Ile Glu Leu Asn Lys Ala Lys Ser Asp Leu Glu Glu
 1 5 10 15
 Ser Lys Glu Trp Ile Arg Arg Ser Asn Gln Lys Leu Asp Ser Ile Gly
 20 25 30
 Asn Trp His
 35
 (2) INFORMATION FOR SEQ ID NO: 338:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:338
 Asp Ile Ser Ile Glu Leu Asn Lys Ala Lys Ser Asp Leu Glu Glu Ser
 1 5 10 15
 Lys Glu Trp Ile Arg Arg Ser Asn Gln Lys Leu Asp Ser Ile Gly Asn
 20 25 30
 Trp His Gln
 35
 (2) INFORMATION FOR SEQ ID NO: 339:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:339
 Ile Ser Ile Glu Leu Asn Lys Ala Lys Ser Asp Leu Glu Glu Ser Lys
 1 5 10 15
 Glu Trp Ile Arg Arg Ser Asn Gln Lys Leu Asp Ser Ile Gly Asn Trp
 20 25 30
 His Gln Ser
 35
 (2) INFORMATION FOR SEQ ID NO: 340:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:340
 Ser Ile Glu Leu Asn Lys Ala Lys Ser Asp Leu Glu Glu Ser Lys Glu
 1 5 10 15
 Trp Ile Arg Arg Ser Asn Gln Lys Leu Asp Ser Ile Gly Asn Trp His
 20 25 30
 Gln Ser Ser
 35
 (2) INFORMATION FOR SEQ ID NO: 341:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:341
 Ile Glu Leu Asn Lys Ala Lys Ser Asp Leu Glu Glu Ser Lys Glu Trp
 1 5 10 15
 Ile Arg Arg Ser Asn Gln Lys Leu Asp Ser Ile Gly Asn Trp His Gln
 20 25 30
 Ser Ser Thr
 35
 (2) INFORMATION FOR SEQ ID NO: 342:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:342
 Glu Leu Asn Lys Ala Lys Ser Asp Leu Glu Glu Ser Lys Glu Trp Ile
 1 5 10 15
 Arg Arg Ser Asn Gln Lys Leu Asp Ser Ile Gly Asn Trp His Gln Ser
 20 25 30
 Ser Thr Thr
 35
 (2) INFORMATION FOR SEQ ID NO: 343:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 34 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:343
 Asp Ala Val Tyr Leu His Arg Ile Asp Leu Gly Pro Pro Ile Ser Leu
 1 5 10 15
 Glu Arg Leu Asp Val Gly Thr Asn Leu Gly Asn Ala Ile Ala Lys Leu
 20 25 30
 Glu Ala
 (2) INFORMATION FOR SEQ ID NO: 344:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 34 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:344
 Ala Val Tyr Leu His Arg Ile Asp Leu Gly Pro Pro Ile Ser Leu Glu
 1 5 10 15
 Arg Leu Asp Val Gly Thr Asn Leu Gly Asn Ala Ile Ala Lys Leu Glu
 20 25 30
 Ala Lys
 (2) INFORMATION FOR SEQ ID NO: 345:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 34 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:345
 Val Tyr Leu His Arg Ile Asp Leu Gly Pro Pro Ile Ser Leu Glu Arg
 1 5 10 15
 Leu Asp Val Gly Thr Asn Leu Gly Asn Ala Ile Ala Lys Leu Glu Ala
 20 25 30
 Lys Glu
 (2) INFORMATION FOR SEQ ID NO: 346:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 34 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:346
 Tyr Leu His Arg Ile Asp Leu Gly Pro Pro Ile Ser Leu Glu Arg Leu
 1 5 10 15
 Asp Val Gly Thr Asn Leu Gly Asn Ala Ile Ala Lys Leu Glu Ala Lys
 20 25 30
 Glu Leu
 (2) INFORMATION FOR SEQ ID NO: 347:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 34 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:347
 Leu His Arg Ile Asp Leu Gly Pro Pro Ile Ser Leu Glu Arg Leu Asp
 1 5 10 15
 Val Gly Thr Asn Leu Gly Asn Ala Ile Ala Lys Leu Glu Ala Lys Glu
 20 25 30
 Leu Leu
 (2) INFORMATION FOR SEQ ID NO: 348:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 34 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:348
 His Arg Ile Asp Leu Gly Pro Pro Ile Ser Leu Glu Arg Leu Asp Val
 1 5 10 15
 Gly Thr Asn Leu Gly Asn Ala Ile Ala Lys Leu Glu Ala Lys Glu Leu
 20 25 30
 Leu Glu
 (2) INFORMATION FOR SEQ ID NO: 349:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 34 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:349
 Arg Ile Asp Leu Gly Pro Pro Ile Ser Leu Glu Arg Leu Asp Val Gly
 1 5 10 15
 Thr Asn Leu Gly Asn Ala Ile Ala Lys Leu Glu Ala Lys Glu Leu Leu
 20 25 30
 Glu Ser
 (2) INFORMATION FOR SEQ ID NO: 350:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 34 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:350
 Ile Asp Leu Gly Pro Pro Ile Ser Leu Glu Arg Leu Asp Val Gly Thr
 1 5 10 15
 Asn Leu Gly Asn Ala Ile Ala Lys Leu Glu Ala Lys Glu Leu Leu Glu
 20 25 30
 Ser Ser
 (2) INFORMATION FOR SEQ ID NO: 351:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 34 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:351
 Asp Leu Gly Pro Pro Ile Ser Leu Glu Arg Leu Asp Val Gly Thr Asn
 1 5 10 15
 Leu Gly Asn Ala Ile Ala Lys Leu Glu Ala Lys Glu Leu Leu Glu Ser
 20 25 30
 Ser Asp
 (2) INFORMATION FOR SEQ ID NO: 352:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 34 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:352
 Leu Gly Pro Pro Ile Ser Leu Glu Arg Leu Asp Val Gly Thr Asn Leu
 1 5 10 15
 Gly Asn Ala Ile Ala Lys Leu Glu Ala Lys Glu Leu Leu Glu Ser Ser
 20 25 30
 Asp Gln
 (2) INFORMATION FOR SEQ ID NO: 353:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 34 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:353
 Gly Pro Pro Ile Ser Leu Glu Arg Leu Asp Val Gly Thr Asn Leu Gly
 1 5 10 15
 Asn Ala Ile Ala Lys Leu Glu Ala Lys Glu Leu Leu Glu Ser Ser Asp
 20 25 30
 Gln Ile
 (2) INFORMATION FOR SEQ ID NO: 354:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 34 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:354
 Pro Pro Ile Ser Leu Glu Arg Leu Asp Val Gly Thr Asn Leu Gly Asn
 1 5 10 15
 Ala Ile Ala Lys Leu Glu Ala Lys Glu Leu Leu Glu Ser Ser Asp Gln
 20 25 30
 Ile Leu
 (2) INFORMATION FOR SEQ ID NO: 355:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 34 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:355
 Pro Ile Ser Leu Glu Arg Leu Asp Val Gly Thr Asn Leu Gly Asn Ala
 1 5 10 15
 Ile Ala Lys Leu Glu Ala Lys Glu Leu Leu Glu Ser Ser Asp Gln Ile
 20 25 30
 Leu Arg
 (2) INFORMATION FOR SEQ ID NO: 356:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 34 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:356
 Ile Ser Leu Glu Arg Leu Asp Val Gly Thr Asn Leu Gly Asn Ala Ile
 1 5 10 15
 Ala Lys Leu Glu Ala Lys Glu Leu Leu Glu Ser Ser Asp Gln Ile Leu
 20 25 30
 Arg Ser
 (2) INFORMATION FOR SEQ ID NO: 357:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 34 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:357
 Ser Leu Glu Arg Leu Asp Val Gly Thr Asn Leu Gly Asn Ala Ile Ala
 1 5 10 15
 Lys Leu Glu Ala Lys Glu Leu Leu Glu Ser Ser Asp Gln Ile Leu Arg
 20 25 30
 Ser Met
 (2) INFORMATION FOR SEQ ID NO: 358:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:358
 Thr Trp Gln Glu Trp Glu Arg Lys Val Asp Phe Leu Glu Glu Asn Ile
 1 5 10 15
 Thr Ala Leu Leu Glu Glu Ala Gln Ile Gln Gln Glu Lys Asn Met Tyr
 20 25 30
 Glu Leu Gln
 35
 (2) INFORMATION FOR SEQ ID NO: 359:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:359
 Trp Gln Glu Trp Glu Arg Lys Val Asp Phe Leu Glu Glu Asn Ile Thr
 1 5 10 15
 Ala Leu Leu Glu Glu Ala Gln Ile Gln Gln Glu Lys Asn Met Tyr Glu
 20 25 30
 Leu Gln Lys
 35
 (2) INFORMATION FOR SEQ ID NO: 360:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:360
 Gln Glu Trp Glu Arg Lys Val Asp Phe Leu Glu Glu Asn Ile Thr Ala
 1 5 10 15
 Leu Leu Glu Glu Ala Gln Ile Gln Gln Glu Lys Asn Met Tyr Glu Leu
 20 25 30
 Gln Lys Leu
 35
 (2) INFORMATION FOR SEQ ID NO: 361:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:361
 Glu Trp Glu Arg Lys Val Asp Phe Leu Glu Glu Asn Ile Thr Ala Leu
 1 5 10 15
 Leu Glu Glu Ala Gln Ile Gln Gln Glu Lys Asn Met Tyr Glu Leu Gln
 20 25 30
 Lys Leu Asn
 35
 (2) INFORMATION FOR SEQ ID NO: 362:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:362
 Trp Glu Arg Lys Val Asp Phe Leu Glu Glu Asn Ile Thr Ala Leu Leu
 1 5 10 15
 Glu Glu Ala Gln Ile Gln Gln Glu Lys Asn Met Tyr Glu Leu Gln Lys
 20 25 30
 Leu Asn Ser
 35
 (2) INFORMATION FOR SEQ ID NO: 363:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:363
 Glu Arg Lys Val Asp Phe Leu Glu Glu Asn Ile Thr Ala Leu Leu Glu
 1 5 10 15
 Glu Ala Gln Ile Gln Gln Glu Lys Asn Met Tyr Glu Leu Gln Lys Leu
 20 25 30
 Asn Ser Trp
 35
 (2) INFORMATION FOR SEQ ID NO: 364:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:364
 Arg Lys Val Asp Phe Leu Glu Glu Asn Ile Thr Ala Leu Leu Glu Glu
 1 5 10 15
 Ala Gln Ile Gln Gln Glu Lys Asn Met Tyr Glu Leu Gln Lys Leu Asn
 20 25 30
 Ser Trp Asp
 35
 (2) INFORMATION FOR SEQ ID NO: 365:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:365
 Lys Val Asp Phe Leu Glu Glu Asn Ile Thr Ala Leu Leu Glu Glu Ala
 1 5 10 15
 Gln Ile Gln Gln Glu Lys Asn Met Tyr Glu Leu Gln Lys Leu Asn Ser
 20 25 30
 Trp Asp Val
 35
 (2) INFORMATION FOR SEQ ID NO: 366:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:366
 Val Asp Phe Leu Glu Glu Asn Ile Thr Ala Leu Leu Glu Glu Ala Gln
 1 5 10 15
 Ile Gln Gln Glu Lys Asn Met Tyr Glu Leu Gln Lys Leu Asn Ser Trp
 20 25 30
 Asp Val Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 367:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:367
 Asp Phe Leu Glu Glu Asn Ile Thr Ala Leu Leu Glu Glu Ala Gln Ile
 1 5 10 15
 Gln Gln Glu Lys Asn Met Tyr Glu Leu Gln Lys Leu Asn Ser Trp Asp
 20 25 30
 Val Phe Gly
 35
 (2) INFORMATION FOR SEQ ID NO: 368:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:368
 Phe Leu Glu Glu Asn Ile Thr Ala Leu Leu Glu Glu Ala Gln Ile Gln
 1 5 10 15
 Gln Glu Lys Asn Met Tyr Glu Leu Gln Lys Leu Asn Ser Trp Asp Val
 20 25 30
 Phe Gly Asn
 35
 (2) INFORMATION FOR SEQ ID NO: 369:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:369
 Asn Lys Ser Leu Glu Gln Ile Trp Asn Asn Met Thr Trp Met Glu Trp
 1 5 10 15
 Asp Arg Glu Ile Asn Asn Tyr Thr Ser Leu Ile His Ser Leu Ile Glu
 20 25 30
 Glu Gln Asn
 35
 (2) INFORMATION FOR SEQ ID NO: 370:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:370
 Lys Ser Leu Glu Gln Ile Trp Asn Asn Met Thr Trp Met Glu Trp Asp
 1 5 10 15
 Arg Glu Ile Asn Asn Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu
 20 25 30
 Gln Asn Gln
 35
 (2) INFORMATION FOR SEQ ID NO: 371:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:371
 Ser Leu Glu Gln Ile Trp Asn Asn Met Thr Trp Met Glu Trp Asp Arg
 1 5 10 15
 Glu Ile Asn Asn Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Gln
 20 25 30
 Asn Gln Gln
 35
 (2) INFORMATION FOR SEQ ID NO: 372:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:372
 Leu Glu Gln Ile Trp Asn Asn Met Thr Trp Met Glu Trp Asp Arg Glu
 1 5 10 15
 Ile Asn Asn Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Gln Asn
 20 25 30
 Gln Gln Glu
 35
 (2) INFORMATION FOR SEQ ID NO: 373:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:373
 Glu Gln Ile Trp Asn Asn Met Thr Trp Met Glu Trp Asp Arg Glu Ile
 1 5 10 15
 Asn Asn Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Gln Asn Gln
 20 25 30
 Gln Glu Lys
 35
 (2) INFORMATION FOR SEQ ID NO: 374:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:374
 Gln Ile Trp Asn Asn Met Thr Trp Met Glu Trp Asp Arg Glu Ile Asn
 1 5 10 15
 Asn Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Gln Asn Gln Gln
 20 25 30
 Glu Lys Asn
 35
 (2) INFORMATION FOR SEQ ID NO: 375:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:375
 Ile Trp Asn Asn Met Thr Trp Met Glu Trp Asp Arg Glu Ile Asn Asn
 1 5 10 15
 Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Gln Asn Gln Gln Glu
 20 25 30
 Lys Asn Glu
 35
 (2) INFORMATION FOR SEQ ID NO: 376:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:376
 Trp Asn Asn Met Thr Trp Met Glu Trp Asp Arg Glu Ile Asn Asn Tyr
 1 5 10 15
 Thr Ser Leu Ile His Ser Leu Ile Glu Glu Gln Asn Gln Gln Glu Lys
 20 25 30
 Asn Glu Gln
 35
 (2) INFORMATION FOR SEQ ID NO: 377:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:377
 Asn Asn Met Thr Trp Met Glu Trp Asp Arg Glu Ile Asn Asn Tyr Thr
 1 5 10 15
 Ser Leu Ile His Ser Leu Ile Glu Glu Gln Asn Gln Gln Glu Lys Asn
 20 25 30
 Glu Gln Glu
 35
 (2) INFORMATION FOR SEQ ID NO: 378:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:378
 Asn Met Thr Trp Met Glu Trp Asp Arg Glu Ile Asn Asn Tyr Thr Ser
 1 5 10 15
 Leu Ile His Ser Leu Ile Glu Glu Gln Asn Gln Gln Glu Lys Asn Glu
 20 25 30
 Gln Glu Leu
 35
 (2) INFORMATION FOR SEQ ID NO: 379:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:379
 Met Thr Trp Met Glu Trp Asp Arg Glu Ile Asn Asn Tyr Thr Ser Leu
 1 5 10 15
 Ile His Ser Leu Ile Glu Glu Gln Asn Gln Gln Glu Lys Asn Glu Gln
 20 25 30
 Glu Leu Leu
 35
 (2) INFORMATION FOR SEQ ID NO: 380:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 46 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:380
 Met Thr Trp Met Glu Trp Asp Arg Glu Ile Asn Asn Tyr Thr Ser Leu
 1 5 10 15
 Ile His Ser Leu Ile Glu Glu Gln Asn Gln Gln Glu Lys Asn Glu Gln
 20 25 30
 Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu Trp Asn Trp
 35 40 45
 (2) INFORMATION FOR SEQ ID NO: 381:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:381
 Thr Trp Met Glu Trp Asp Arg Glu Ile Asn Asn Tyr Thr Ser Leu Ile
 1 5 10 15
 His Ser Leu Ile Glu Glu Gln Asn Gln Gln Glu Lys Asn Glu Gln Glu
 20 25 30
 Leu Leu Glu
 35
 (2) INFORMATION FOR SEQ ID NO: 382:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:382
 Trp Met Glu Trp Asp Arg Glu Ile Asn Asn Tyr Thr Ser Leu Ile His
 1 5 10 15
 Ser Leu Ile Glu Glu Gln Asn Gln Gln Glu Lys Asn Glu Gln Glu Leu
 20 25 30
 Leu Glu Leu
 35
 (2) INFORMATION FOR SEQ ID NO: 383:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 34 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:383
 Trp Met Glu Trp Asp Arg Glu Ile Asn Asn Tyr Thr Ser Leu Ile His
 1 5 10 15
 Ser Leu Ile Glu Glu Gln Asn Gln Gln Glu Lys Asn Glu Gln Glu Leu
 20 25 30
 Leu Glu
 (2) INFORMATION FOR SEQ ID NO: 384:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:384
 Met Glu Trp Asp Arg Glu Ile Asn Asn Tyr Thr Ser Leu Ile His Ser
 1 5 10 15
 Leu Ile Glu Glu Gln Asn Gln Gln Glu Lys Asn Glu Gln Glu Leu Leu
 20 25 30
 Glu Leu Asp
 35
 (2) INFORMATION FOR SEQ ID NO: 385:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:385
 Glu Trp Asp Arg Glu Ile Asn Asn Tyr Thr Ser Leu Ile His Ser Leu
 1 5 10 15
 Ile Glu Glu Gln Asn Gln Gln Glu Lys Asn Glu Gln Glu Leu Leu Glu
 20 25 30
 Leu Asp Lys
 35
 (2) INFORMATION FOR SEQ ID NO: 386:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 29 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:386
 Glu Trp Asp Arg Glu Ile Asn Asn Tyr Thr Ser Leu Ile His Ser Leu
 1 5 10 15
 Ile Glu Glu Gln Asn Gln Gln Glu Lys Asn Glu Gln Glu
 20 25
 (2) INFORMATION FOR SEQ ID NO: 387:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 32 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:387
 Glu Trp Asp Arg Glu Ile Asn Asn Tyr Thr Ser Leu Ile His Ser Leu
 1 5 10 15
 Ile Glu Glu Gln Asn Gln Gln Glu Lys Asn Glu Gln Glu Gly Gly Cys
 20 25 30
 (2) INFORMATION FOR SEQ ID NO: 388:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:388
 Trp Asp Arg Glu Ile Asn Asn Tyr Thr Ser Leu Ile His Ser Leu Ile
 1 5 10 15
 Glu Glu Gln Asn Gln Gln Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu
 20 25 30
 Asp Lys Trp
 35
 (2) INFORMATION FOR SEQ ID NO: 389:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:389
 Asp Arg Glu Ile Asn Asn Tyr Thr Ser Leu Ile His Ser Leu Ile Glu
 1 5 10 15
 Glu Gln Asn Gln Gln Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp
 20 25 30
 Lys Trp Ala
 35
 (2) INFORMATION FOR SEQ ID NO: 390:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:390
 Arg Glu Ile Asn Asn Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu
 1 5 10 15
 Gln Asn Gln Gln Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys
 20 25 30
 Trp Ala Ser
 35
 (2) INFORMATION FOR SEQ ID NO: 391:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:391
 Glu Ile Asn Asn Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Gln
 1 5 10 15
 Asn Gln Gln Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp
 20 25 30
 Ala Ser Leu
 35
 (2) INFORMATION FOR SEQ ID NO: 392:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:392
 Ile Asn Asn Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Gln Asn
 1 5 10 15
 Gln Gln Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala
 20 25 30
 Ser Leu Trp
 35
 (2) INFORMATION FOR SEQ ID NO: 393:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 34 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:393
 Ile Asn Asn Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Gln Asn
 1 5 10 15
 Gln Gln Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala
 20 25 30
 Ser Leu
 (2) INFORMATION FOR SEQ ID NO: 394:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 27 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:394
 Ile Asn Asn Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Gln Asn
 1 5 10 15
 Gln Gln Glu Lys Asn Glu Gln Glu Leu Leu Glu
 20 25
 (2) INFORMATION FOR SEQ ID NO: 395:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 25 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:395
 Ile Asn Asn Tyr Thr Ser Leu Ile Gly Ser Leu Ile Glu Glu Gln Asn
 1 5 10 15
 Gln Gln Glu Lys Asn Glu Gln Glu Leu
 20 25
 (2) INFORMATION FOR SEQ ID NO: 396:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:396
 Asn Asn Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Gln Asn Gln
 1 5 10 15
 Gln Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser
 20 25 30
 Leu Trp Asn
 35
 (2) INFORMATION FOR SEQ ID NO: 397:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:397
 Asn Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Gln Asn Gln Gln
 1 5 10 15
 Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu
 20 25 30
 Trp Asn Trp
 35
 (2) INFORMATION FOR SEQ ID NO: 398:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 34 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:398
 Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Gln Asn Gln Gln Glu
 1 5 10 15
 Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu Trp
 20 25 30
 Asn Trp
 (2) INFORMATION FOR SEQ ID NO: 399:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:399
 Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Ser Gln Asn Gln Gln
 1 5 10 15
 Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu
 20 25 30
 Trp Asn Trp Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 400:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:400
 Thr Ser Leu Ile His Ser Leu Ile Glu Glu Ser Gln Asn Gln Gln Glu
 1 5 10 15
 Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu Trp
 20 25 30
 Asn Trp Phe Asn
 35
 (2) INFORMATION FOR SEQ ID NO: 401:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:401
 Ser Leu Ile His Ser Leu Ile Glu Glu Ser Gln Asn Gln Gln Glu Lys
 1 5 10 15
 Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu Trp Asn
 20 25 30
 Trp Phe Asn Ile
 35
 (2) INFORMATION FOR SEQ ID NO: 402:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:402
 Leu Ile His Ser Leu Ile Glu Glu Ser Gln Asn Gln Gln Glu Lys Asn
 1 5 10 15
 Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu Trp Asn Trp
 20 25 30
 Phe Asn Ile Thr
 35
 (2) INFORMATION FOR SEQ ID NO: 403:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:403
 Ile His Ser Leu Ile Glu Glu Ser Gln Asn Gln Gln Glu Lys Asn Glu
 1 5 10 15
 Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu Trp Asn Trp Phe
 20 25 30
 Asn Ile Thr Asn
 35
 (2) INFORMATION FOR SEQ ID NO: 404:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:404
 His Ser Leu Ile Glu Glu Ser Gln Asn Gln Gln Glu Lys Asn Glu Gln
 1 5 10 15
 Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu Trp Asn Trp Phe Asn
 20 25 30
 Ile Thr Asn Trp
 35
 (2) INFORMATION FOR SEQ ID NO: 405:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:405
 Ser Leu Ile Glu Glu Ser Gln Asn Gln Gln Glu Lys Asn Glu Gln Glu
 1 5 10 15
 Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu Trp Asn Trp Phe Asn Ile
 20 25 30
 Thr Asn Trp Leu
 35
 (2) INFORMATION FOR SEQ ID NO: 406:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:406
 Leu Ile Glu Glu Ser Gln Asn Gln Gln Glu Lys Asn Glu Gln Glu Leu
 1 5 10 15
 Leu Glu Leu Asp Lys Trp Ala Ser Leu Trp Asn Trp Phe Asn Ile Thr
 20 25 30
 Asn Trp Leu Trp
 35
 (2) INFORMATION FOR SEQ ID NO: 407:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:407
 Ile Glu Glu Ser Gln Asn Gln Gln Glu Lys Asn Glu Gln Glu Leu Leu
 1 5 10 15
 Glu Leu Asp Lys Trp Ala Ser Leu Trp Asn Trp Phe Asn Ile Thr Asn
 20 25 30
 Trp Leu Trp Leu
 35
 (2) INFORMATION FOR SEQ ID NO: 408:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:408
 Glu Glu Ser Gln Asn Gln Gln Glu Lys Asn Glu Gln Glu Leu Leu Glu
 1 5 10 15
 Leu Asp Lys Trp Ala Ser Leu Trp Asn Trp Phe Asn Ile Thr Asn Trp
 20 25 30
 Leu Trp Leu Ile
 35
 (2) INFORMATION FOR SEQ ID NO: 409:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:409
 Glu Ser Gln Asn Gln Gln Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu
 1 5 10 15
 Asp Lys Trp Ala Ser Leu Trp Asn Trp Phe Asn Ile Thr Asn Trp Leu
 20 25 30
 Trp Leu Ile Lys
 35
 (2) INFORMATION FOR SEQ ID NO: 410:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:410
 Ser Gln Asn Gln Gln Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp
 1 5 10 15
 Lys Trp Ala Ser Leu Trp Asn Trp Phe Asn Ile Thr Asn Trp Leu Trp
 20 25 30
 Leu Ile Lys Ile
 35
 (2) INFORMATION FOR SEQ ID NO: 411:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:411
 Gln Asn Gln Gln Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys
 1 5 10 15
 Trp Ala Ser Leu Trp Asn Trp Phe Asn Ile Thr Asn Trp Leu Trp Leu
 20 25 30
 Ile Lys Ile Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 412:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:412
 Asn Gln Gln Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp
 1 5 10 15
 Ala Ser Leu Trp Asn Trp Phe Asn Ile Thr Asn Trp Leu Trp Leu Ile
 20 25 30
 Lys Ile Phe Ile
 35
 (2) INFORMATION FOR SEQ ID NO: 413:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 36 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:413
 Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Ser Gln Asn Gln Gln
 1 5 10 15
 Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu
 20 25 30
 Trp Asn Trp Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 414:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 18 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:414
 Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Ser Gln Asn Gln Gln
 1 5 10 15
 Glu Lys
 (2) INFORMATION FOR SEQ ID NO: 415:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 23 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:415
 Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Ser Gln Asn Gln Gln
 1 5 10 15
 Glu Lys Asn Glu Gln Glu Leu
 20
 (2) INFORMATION FOR SEQ ID NO: 416:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:416
 Thr Ser Leu Ile His Ser Leu Ile Glu Glu Ser Gln Asn Gln Gln Glu
 1 5 10 15
 Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu Trp
 20 25 30
 Asn Trp Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 417:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 33 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:417
 Leu Ile His Ser Leu Ile Glu Glu Ser Gln Asn Gln Gln Glu Lys Asn
 1 5 10 15
 Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu Trp Asn Trp
 20 25 30
 Phe
 (2) INFORMATION FOR SEQ ID NO: 418:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 32 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:418
 Tyr Thr Ser Leu Ile His Ser Leu Ile Glu Glu Ser Gln Asn Gln Gln
 1 5 10 15
 Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu
 20 25 30
 (2) INFORMATION FOR SEQ ID NO: 419:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 29 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:419
 Leu Ile Glu Glu Ser Gln Asn Gln Gln Glu Lys Asn Glu Gln Glu Leu
 1 5 10 15
 Leu Glu Leu Asp Lys Trp Ala Ser Leu Trp Asn Trp Phe
 20 25
 (2) INFORMATION FOR SEQ ID NO: 420:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 26 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:420
 Glu Ser Gln Asn Gln Gln Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu
 1 5 10 15
 Asp Lys Trp Ala Ser Leu Trp Asn Trp Phe
 20 25
 (2) INFORMATION FOR SEQ ID NO: 421:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 23 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:421
 Asn Gln Gln Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp
 1 5 10 15
 Ala Ser Leu Trp Asn Trp Phe
 20
 (2) INFORMATION FOR SEQ ID NO: 422:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 20 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:422
 Glu Lys Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu
 1 5 10 15
 Trp Asn Trp Phe
 20
 (2) INFORMATION FOR SEQ ID NO: 423:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 18 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:423
 Asn Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu Trp Asn
 1 5 10 15
 Trp Phe
 (2) INFORMATION FOR SEQ ID NO: 424:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 17 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:424
 Glu Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu Trp Asn Trp
 1 5 10 15
 Phe
 (2) INFORMATION FOR SEQ ID NO: 425:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 16 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:425
 Gln Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu Trp Asn Trp Phe
 1 5 10 15
 (2) INFORMATION FOR SEQ ID NO: 426:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 15 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:426
 Glu Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu Trp Asn Trp Phe
 1 5 10 15
 (2) INFORMATION FOR SEQ ID NO: 427:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 14 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:427
 Leu Leu Glu Leu Asp Lys Trp Ala Ser Leu Trp Asn Trp Phe
 1 5 10
 (2) INFORMATION FOR SEQ ID NO: 428:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 13 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:428
 Leu Glu Leu Asp Lys Trp Ala Ser Leu Trp Asn Trp Phe
 1 5 10
 (2) INFORMATION FOR SEQ ID NO: 429:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 28 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:429
 Lys Val Glu Glu Leu Leu Ser Lys Asn Tyr His Leu Glu Asn Glu Leu
 1 5 10 15
 Glu Leu Asp Lys Trp Ala Ser Leu Trp Asn Trp Phe
 20 25
 (2) INFORMATION FOR SEQ ID NO: 430:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 15 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:430
 Cys Leu Glu Leu Asp Lys Trp Ala Ser Leu Trp Asn Trp Phe Cys
 1 5 10 15
 (2) INFORMATION FOR SEQ ID NO: 431:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 15 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:431
 Cys Leu Glu Leu Asp Lys Trp Ala Ser Leu Ala Asn Trp Phe Cys
 1 5 10 15
 (2) INFORMATION FOR SEQ ID NO: 432:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 15 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:432
 Cys Leu Glu Leu Asp Lys Trp Ala Ser Leu Trp Asn Phe Phe Cys
 1 5 10 15
 (2) INFORMATION FOR SEQ ID NO: 433:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 13 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:433
 Leu Glu Leu Asp Lys Trp Ala Ser Leu Ala Asn Trp Phe
 1 5 10
 (2) INFORMATION FOR SEQ ID NO: 434:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 12 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:434
 Glu Leu Asp Lys Trp Ala Ser Leu Trp Asn Trp Phe
 1 5 10
 (2) INFORMATION FOR SEQ ID NO: 435:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 11 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:435
 Leu Asp Lys Trp Ala Ser Leu Trp Asn Trp Phe
 1 5 10
 (2) INFORMATION FOR SEQ ID NO: 436:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 10 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:436
 Asp Lys Trp Ala Ser Leu Trp Asn Trp Phe
 1 5 10
 (2) INFORMATION FOR SEQ ID NO: 437:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 28 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:437
 Met Thr Leu Thr Val Gln Ala Arg Gln Leu Leu Ser Gln Ile Val Gln
 1 5 10 15
 Gln Gln Asn Asn Leu Leu Arg Ala Ile Glu Ala Gln
 20 25
 (2) INFORMATION FOR SEQ ID NO: 438:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 28 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:438
 Gln Ala Arg Gln Leu Leu Ser Gln Ile Val Gln Gln Gln Asn Asn Leu
 1 5 10 15
 Leu Arg Ala Ile Glu Ala Gln Gln Asn Leu Leu Gln
 20 25
 (2) INFORMATION FOR SEQ ID NO: 439:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 28 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:439
 Arg Gln Leu Leu Ser Gln Ile Val Gln Gln Gln Asn Asn Leu Leu Arg
 1 5 10 15
 Ala Ile Glu Ala Gln Gln Asn Leu Leu Gln Leu Thr
 20 25
 (2) INFORMATION FOR SEQ ID NO: 440:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 28 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:440
 Val Gln Gln Gln Asn Asn Leu Leu Arg Ala Ile Glu Ala Gln Gln Asn
 1 5 10 15
 Leu Leu Gln Leu Thr Val Trp Gln Ile Lys Gln Leu
 20 25
 (2) INFORMATION FOR SEQ ID NO: 441:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 38 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:441
 Asn Asn Leu Leu Arg Ala Ile Glu Ala Gln Gln Asn Leu Leu Gln Leu
 1 5 10 15
 Thr Val Trp Gln Ile Lys Gln Leu Gln Ala Arg Ile Leu Ala Val Glu
 20 25 30
 Arg Tyr Leu Lys Asp Gln
 35
 (2) INFORMATION FOR SEQ ID NO: 442:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 19 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:442
 Gln Ile Lys Gln Leu Gln Ala Arg Ile Leu Ala Val Glu Arg Tyr Leu
 1 5 10 15
 Lys Asp Gln
 (2) INFORMATION FOR SEQ ID NO: 443:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 28 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:443
 Leu Arg Ala Ile Glu Ala Gln Gln Asn Leu Leu Gln Leu Thr Val Trp
 1 5 10 15
 Gln Ile Lys Gln Leu Gln Ala Arg Ile Leu Ala Val
 20 25
 (2) INFORMATION FOR SEQ ID NO: 444:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 27 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:444
 Leu Arg Ala Ile Glu Ala Gln Gln Asn Leu Leu Gln Leu Thr Val Trp
 1 5 10 15
 Gln Ile Lys Gln Leu Ala Arg Ile Leu Ala Val
 20 25
 (2) INFORMATION FOR SEQ ID NO: 445:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 28 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:445
 Gln Asn Leu Leu Gln Leu Thr Val Trp Gln Ile Lys Gln Leu Gln Ala
 1 5 10 15
 Arg Ile Leu Ala Val Glu Arg Tyr Leu Lys Asp Gln
 20 25
 (2) INFORMATION FOR SEQ ID NO: 446:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 28 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:446
 Val Trp Gln Ile Lys Gln Leu Gln Ala Arg Ile Leu Ala Val Glu Arg
 1 5 10 15
 Tyr Leu Lys Asp Gln Gln Leu Leu Gln Ile Trp Gln
 20 25
 (2) INFORMATION FOR SEQ ID NO: 447:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:447
 Ser Glu Leu Glu Ile Lys Arg Tyr Lys Asn Arg Val Ala Ser Arg Lys
 1 5 10 15
 Cys Arg Ala Lys Phe Lys Gln Leu Leu Gln His Tyr Arg Glu Val Ala
 20 25 30
 Ala Ala Lys
 35
 (2) INFORMATION FOR SEQ ID NO: 448:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:448
 Glu Leu Glu Ile Lys Arg Tyr Lys Asn Arg Val Ala Ser Arg Lys Cys
 1 5 10 15
 Arg Ala Lys Phe Lys Gln Leu Leu Gln His Tyr Arg Glu Val Ala Ala
 20 25 30
 Ala Lys Ser
 35
 (2) INFORMATION FOR SEQ ID NO: 449:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:449
 Leu Glu Ile Lys Arg Tyr Lys Asn Arg Val Ala Ser Arg Lys Cys Arg
 1 5 10 15
 Ala Lys Phe Lys Gln Leu Leu Gln His Tyr Arg Glu Val Ala Ala Ala
 20 25 30
 Lys Ser Ser
 35
 (2) INFORMATION FOR SEQ ID NO: 450:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:450
 Glu Ile Lys Arg Tyr Lys Asn Arg Val Ala Ser Arg Lys Cys Arg Ala
 1 5 10 15
 Lys Phe Lys Gln Leu Leu Gln His Tyr Arg Glu Val Ala Ala Ala Lys
 20 25 30
 Ser Ser Glu
 35
 (2) INFORMATION FOR SEQ ID NO: 451:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:451
 Ile Lys Arg Tyr Lys Asn Arg Val Ala Ser Arg Lys Cys Arg Ala Lys
 1 5 10 15
 Phe Lys Gln Leu Leu Gln His Tyr Arg Glu Val Ala Ala Ala Lys Ser
 20 25 30
 Ser Glu Asn
 35
 (2) INFORMATION FOR SEQ ID NO: 452:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:452
 Lys Arg Tyr Lys Asn Arg Val Ala Ser Arg Lys Cys Arg Ala Lys Phe
 1 5 10 15
 Lys Gln Leu Leu Gln His Tyr Arg Glu Val Ala Ala Ala Lys Ser Ser
 20 25 30
 Glu Asn Asp
 35
 (2) INFORMATION FOR SEQ ID NO: 453:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:453
 Arg Tyr Lys Asn Arg Val Ala Ser Arg Lys Cys Arg Ala Lys Phe Lys
 1 5 10 15
 Gln Leu Leu Gln His Tyr Arg Glu Val Ala Ala Ala Lys Ser Ser Glu
 20 25 30
 Asn Asp Arg
 35
 (2) INFORMATION FOR SEQ ID NO: 454:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:454
 Tyr Lys Asn Arg Val Ala Ser Arg Lys Cys Arg Ala Lys Phe Lys Gln
 1 5 10 15
 Leu Leu Gln His Tyr Arg Glu Val Ala Ala Ala Lys Ser Ser Glu Asn
 20 25 30
 Asp Arg Leu
 35
 (2) INFORMATION FOR SEQ ID NO: 455:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:455
 Lys Asn Arg Val Ala Ser Arg Lys Cys Arg Ala Lys Phe Lys Gln Leu
 1 5 10 15
 Leu Gln His Tyr Arg Glu Val Ala Ala Ala Lys Ser Ser Glu Asn Asp
 20 25 30
 Arg Leu Arg
 35
 (2) INFORMATION FOR SEQ ID NO: 456:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:456
 Asn Arg Val Ala Ser Arg Lys Cys Arg Ala Lys Phe Lys Gln Leu Leu
 1 5 10 15
 Gln His Tyr Arg Glu Val Ala Ala Ala Lys Ser Ser Glu Asn Asp Arg
 20 25 30
 Leu Arg Leu
 35
 (2) INFORMATION FOR SEQ ID NO: 457:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:457
 Arg Val Ala Ser Arg Lys Cys Arg Ala Lys Phe Lys Gln Leu Leu Gln
 1 5 10 15
 His Tyr Arg Glu Val Ala Ala Ala Lys Ser Ser Glu Asn Asp Arg Leu
 20 25 30
 Arg Leu Leu
 35
 (2) INFORMATION FOR SEQ ID NO: 458:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:458
 Val Ala Ser Arg Lys Cys Arg Ala Lys Phe Lys Gln Leu Leu Gln His
 1 5 10 15
 Tyr Arg Glu Val Ala Ala Ala Lys Ser Ser Glu Asn Asp Arg Leu Arg
 20 25 30
 Leu Leu Leu
 35
 (2) INFORMATION FOR SEQ ID NO: 459:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:459
 Ala Ser Arg Lys Cys Arg Ala Lys Phe Lys Gln Leu Leu Gln His Tyr
 1 5 10 15
 Arg Glu Val Ala Ala Ala Lys Ser Ser Glu Asn Asp Arg Leu Arg Leu
 20 25 30
 Leu Leu Lys
 35
 (2) INFORMATION FOR SEQ ID NO: 460:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:460
 Ser Arg Lys Cys Arg Ala Lys Phe Lys Gln Leu Leu Gln His Tyr Arg
 1 5 10 15
 Glu Val Ala Ala Ala Lys Ser Ser Glu Asn Asp Arg Leu Arg Leu Leu
 20 25 30
 Leu Lys Gln
 35
 (2) INFORMATION FOR SEQ ID NO: 461:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:461
 Arg Lys Cys Arg Ala Lys Phe Lys Gln Leu Leu Gln His Tyr Arg Glu
 1 5 10 15
 Val Ala Ala Ala Lys Ser Ser Glu Asn Asp Arg Leu Arg Leu Leu Leu
 20 25 30
 Lys Gln Met
 35
 (2) INFORMATION FOR SEQ ID NO: 462:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:462
 Lys Cys Arg Ala Lys Phe Lys Gln Leu Leu Gln His Tyr Arg Glu Val
 1 5 10 15
 Ala Ala Ala Lys Ser Ser Glu Asn Asp Arg Leu Arg Leu Leu Leu Lys
 20 25 30
 Gln Met Cys
 35
 (2) INFORMATION FOR SEQ ID NO: 463:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:463
 Cys Arg Ala Lys Phe Lys Gln Leu Leu Gln His Tyr Arg Glu Val Ala
 1 5 10 15
 Ala Ala Lys Ser Ser Glu Asn Asp Arg Leu Arg Leu Leu Leu Lys Gln
 20 25 30
 Met Cys Pro
 35
 (2) INFORMATION FOR SEQ ID NO: 464:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:464
 Arg Ala Lys Phe Lys Gln Leu Leu Gln His Tyr Arg Glu Val Ala Ala
 1 5 10 15
 Ala Lys Ser Ser Glu Asn Asp Arg Leu Arg Leu Leu Leu Lys Gln Met
 20 25 30
 Cys Pro Ser
 35
 (2) INFORMATION FOR SEQ ID NO: 465:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:465
 Ala Lys Phe Lys Gln Leu Leu Gln His Tyr Arg Glu Val Ala Ala Ala
 1 5 10 15
 Lys Ser Ser Glu Asn Asp Arg Leu Arg Leu Leu Leu Lys Gln Met Cys
 20 25 30
 Pro Ser Leu
 35
 (2) INFORMATION FOR SEQ ID NO: 466:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:466
 Lys Phe Lys Gln Leu Leu Gln His Tyr Arg Glu Val Ala Ala Ala Lys
 1 5 10 15
 Ser Ser Glu Asn Asp Arg Leu Arg Leu Leu Leu Lys Gln Met Cys Pro
 20 25 30
 Ser Leu Asp
 35
 (2) INFORMATION FOR SEQ ID NO: 467:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:467
 Phe Lys Gln Leu Leu Gln His Tyr Arg Glu Val Ala Ala Ala Lys Ser
 1 5 10 15
 Ser Glu Asn Asp Arg Leu Arg Leu Leu Leu Lys Gln Met Cys Pro Ser
 20 25 30
 Leu Asp Val
 35
 (2) INFORMATION FOR SEQ ID NO: 468:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:468
 Lys Gln Leu Leu Gln His Tyr Arg Glu Val Ala Ala Ala Lys Ser Ser
 1 5 10 15
 Glu Asn Asp Arg Leu Arg Leu Leu Leu Lys Gln Met Cys Pro Ser Leu
 20 25 30
 Asp Val Asp
 35
 (2) INFORMATION FOR SEQ ID NO: 469:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:469
 Gln Leu Leu Gln His Tyr Arg Glu Val Ala Ala Ala Lys Ser Ser Glu
 1 5 10 15
 Asn Asp Arg Leu Arg Leu Leu Leu Lys Gln Met Cys Pro Ser Leu Asp
 20 25 30
 Val Asp Ser
 35
 (2) INFORMATION FOR SEQ ID NO: 470:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:470
 Leu Gln His Tyr Arg Glu Val Ala Ala Ala Lys Ser Ser Glu Asn Asp
 1 5 10 15
 Arg Leu Arg Leu Leu Leu Lys Gln Met Cys Pro Ser Leu Asp Val Asp
 20 25 30
 Ser Ile Ile
 35
 (2) INFORMATION FOR SEQ ID NO: 471:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:471
 Gln His Tyr Arg Glu Val Ala Ala Ala Lys Ser Ser Glu Asn Asp Arg
 1 5 10 15
 Leu Arg Leu Leu Leu Lys Gln Met Cys Pro Ser Leu Asp Val Asp Ser
 20 25 30
 Ile Ile Pro
 35
 (2) INFORMATION FOR SEQ ID NO: 472:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:472
 His Tyr Arg Glu Val Ala Ala Ala Lys Ser Ser Glu Asn Asp Arg Leu
 1 5 10 15
 Arg Leu Leu Leu Lys Gln Met Cys Pro Ser Leu Asp Val Asp Ser Ile
 20 25 30
 Ile Pro Arg
 35
 (2) INFORMATION FOR SEQ ID NO: 473:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:473
 Tyr Arg Glu Val Ala Ala Ala Lys Ser Ser Glu Asn Asp Arg Leu Arg
 1 5 10 15
 Leu Leu Leu Lys Gln Met Cys Pro Ser Leu Asp Val Asp Ser Ile Ile
 20 25 30
 Pro Arg Thr
 35
 (2) INFORMATION FOR SEQ ID NO: 474:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:474
 Arg Glu Val Ala Ala Ala Lys Ser Ser Glu Asn Asp Arg Leu Arg Leu
 1 5 10 15
 Leu Leu Lys Gln Met Cys Pro Ser Leu Asp Val Asp Ser Ile Ile Pro
 20 25 30
 Arg Thr Pro
 35
 (2) INFORMATION FOR SEQ ID NO: 475:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:475
 Glu Val Ala Ala Ala Lys Ser Ser Glu Asn Asp Arg Leu Arg Leu Leu
 1 5 10 15
 Leu Lys Gln Met Cys Pro Ser Leu Asp Val Asp Ser Ile Ile Pro Arg
 20 25 30
 Thr Pro Asp
 35
 (2) INFORMATION FOR SEQ ID NO: 476:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:476
 Val Ala Ala Ala Lys Ser Ser Glu Asn Asp Arg Leu Arg Leu Leu Leu
 1 5 10 15
 Lys Gln Met Cys Pro Ser Leu Asp Val Asp Ser Ile Ile Pro Arg Thr
 20 25 30
 Pro Asp Val
 35
 (2) INFORMATION FOR SEQ ID NO: 477:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:477
 Ala Ala Ala Lys Ser Ser Glu Asn Asp Arg Leu Arg Leu Leu Leu Lys
 1 5 10 15
 Gln Met Cys Pro Ser Leu Asp Val Asp Ser Ile Ile Pro Arg Thr Pro
 20 25 30
 Asp Val Leu
 35
 (2) INFORMATION FOR SEQ ID NO: 478:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:478
 Ala Ala Lys Ser Ser Glu Asn Asp Arg Leu Arg Leu Leu Leu Lys Gln
 1 5 10 15
 Met Cys Pro Ser Leu Asp Val Asp Ser Ile Ile Pro Arg Thr Pro Asp
 20 25 30
 Val Leu His
 35
 (2) INFORMATION FOR SEQ ID NO: 479:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:479
 Ala Lys Ser Ser Glu Asn Asp Arg Leu Arg Leu Leu Leu Lys Gln Met
 1 5 10 15
 Cys Pro Ser Leu Asp Val Asp Ser Ile Ile Pro Arg Thr Pro Asp Val
 20 25 30
 Leu His Glu
 35
 (2) INFORMATION FOR SEQ ID NO: 480:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:480
 Lys Ser Ser Glu Asn Asp Arg Leu Arg Leu Leu Leu Lys Gln Met Cys
 1 5 10 15
 Pro Ser Leu Asp Val Asp Ser Ile Ile Pro Arg Thr Pro Asp Val Leu
 20 25 30
 His Glu Asp
 35
 (2) INFORMATION FOR SEQ ID NO: 481:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:481
 Ser Glu Asn Asp Arg Leu Arg Leu Leu Leu Lys Gln Met Cys Pro Ser
 1 5 10 15
 Leu Asp Val Asp Ser Ile Ile Pro Arg Thr Pro Asp Val Leu His Glu
 20 25 30
 Asp Leu Leu
 35
 (2) INFORMATION FOR SEQ ID NO: 482:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:482
 Glu Asn Asp Arg Leu Arg Leu Leu Leu Lys Gln Met Cys Pro Ser Leu
 1 5 10 15
 Asp Val Asp Ser Ile Ile Pro Arg Thr Pro Asp Val Leu His Glu Asp
 20 25 30
 Leu Leu Asn
 35
 (2) INFORMATION FOR SEQ ID NO: 483:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:483
 Asn Asp Arg Leu Arg Leu Leu Leu Lys Gln Met Cys Pro Ser Leu Asp
 1 5 10 15
 Val Asp Ser Ile Ile Pro Arg Thr Pro Asp Val Leu His Glu Asp Leu
 20 25 30
 Leu Asn Phe
 35
 (2) INFORMATION FOR SEQ ID NO: 484:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:484
 Pro Leu Leu Val Leu Gln Ala Gly Phe Phe Leu Leu Thr Arg Ile Leu
 1 5 10 15
 Thr Ile Pro Gln Ser Leu Asp Ser Trp Trp Thr Ser Leu Asn Phe Leu
 20 25 30
 Gly Gly Thr
 35
 (2) INFORMATION FOR SEQ ID NO: 485:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:485
 Leu Leu Val Leu Gln Ala Gly Phe Phe Leu Leu Thr Arg Ile Leu Thr
 1 5 10 15
 Ile Pro Gln Ser Leu Asp Ser Trp Trp Thr Ser Leu Asn Phe Leu Gly
 20 25 30
 Gly Thr Thr
 35
 (2) INFORMATION FOR SEQ ID NO: 486:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:486
 Leu Val Leu Gln Ala Gly Phe Phe Leu Leu Thr Arg Ile Leu Thr Ile
 1 5 10 15
 Pro Gln Ser Leu Asp Ser Trp Trp Thr Ser Leu Asn Phe Leu Gly Gly
 20 25 30
 Thr Thr Val
 35
 (2) INFORMATION FOR SEQ ID NO: 487:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:487
 Val Leu Gln Ala Gly Phe Phe Leu Leu Thr Arg Ile Leu Thr Ile Pro
 1 5 10 15
 Gln Ser Leu Asp Ser Trp Trp Thr Ser Leu Asn Phe Leu Gly Gly Thr
 20 25 30
 Thr Val Cys
 35
 (2) INFORMATION FOR SEQ ID NO: 488:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:488
 Leu Gln Ala Gly Phe Phe Leu Leu Thr Arg Ile Leu Thr Ile Pro Gln
 1 5 10 15
 Ser Leu Asp Ser Trp Trp Thr Ser Leu Asn Phe Leu Gly Gly Thr Thr
 20 25 30
 Val Cys Leu
 35
 (2) INFORMATION FOR SEQ ID NO: 489:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:489
 Gln Ala Gly Phe Phe Leu Leu Thr Arg Ile Leu Thr Ile Pro Gln Ser
 1 5 10 15
 Leu Asp Ser Trp Trp Thr Ser Leu Asn Phe Leu Gly Gly Thr Thr Val
 20 25 30
 Cys Leu Gly
 35
 (2) INFORMATION FOR SEQ ID NO: 490:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:490
 Ala Gly Phe Phe Leu Leu Thr Arg Ile Leu Thr Ile Pro Gln Ser Leu
 1 5 10 15
 Asp Ser Trp Trp Thr Ser Leu Asn Phe Leu Gly Gly Thr Thr Val Cys
 20 25 30
 Leu Gly Gln
 35
 (2) INFORMATION FOR SEQ ID NO: 491:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:491
 Gly Phe Phe Leu Leu Thr Arg Ile Leu Thr Ile Pro Gln Ser Leu Asp
 1 5 10 15
 Ser Trp Trp Thr Ser Leu Asn Phe Leu Gly Gly Thr Thr Val Cys Leu
 20 25 30
 Gly Gln Asn
 35
 (2) INFORMATION FOR SEQ ID NO: 492:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:492
 Phe Phe Leu Leu Thr Arg Ile Leu Thr Ile Pro Gln Ser Leu Asp Ser
 1 5 10 15
 Trp Trp Thr Ser Leu Asn Phe Leu Gly Gly Thr Thr Val Cys Leu Gly
 20 25 30
 Gln Asn Ser
 35
 (2) INFORMATION FOR SEQ ID NO: 493:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:493
 Phe Leu Leu Thr Arg Ile Leu Thr Ile Pro Gln Ser Leu Asp Ser Trp
 1 5 10 15
 Trp Thr Ser Leu Asn Phe Leu Gly Gly Thr Thr Val Cys Leu Gly Gln
 20 25 30
 Asn Ser Gln
 35
 (2) INFORMATION FOR SEQ ID NO: 494:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:494
 Leu Leu Thr Arg Ile Leu Thr Ile Pro Gln Ser Leu Asp Ser Trp Trp
 1 5 10 15
 Thr Ser Leu Asn Phe Leu Gly Gly Thr Thr Val Cys Leu Gly Gln Asn
 20 25 30
 Ser Gln Ser
 35
 (2) INFORMATION FOR SEQ ID NO: 495:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:495
 Pro Gly Tyr Arg Trp Met Cys Leu Arg Arg Phe Ile Ile Phe Leu Phe
 1 5 10 15
 Ile Leu Leu Leu Cys Leu Ile Phe Leu Leu Val Leu Leu Asp Tyr Gln
 20 25 30
 Gly Met Leu
 35
 (2) INFORMATION FOR SEQ ID NO: 496:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:496
 Gly Tyr Arg Trp Met Cys Leu Arg Arg Phe Ile Ile Phe Leu Phe Ile
 1 5 10 15
 Leu Leu Leu Cys Leu Ile Phe Leu Leu Val Leu Leu Asp Tyr Gln Gly
 20 25 30
 Met Leu Pro
 35
 (2) INFORMATION FOR SEQ ID NO: 497:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:497
 Tyr Arg Trp Met Cys Leu Arg Arg Phe Ile Ile Phe Leu Phe Ile Leu
 1 5 10 15
 Leu Leu Cys Leu Ile Phe Leu Leu Val Leu Leu Asp Tyr Gln Gly Met
 20 25 30
 Leu Pro Val
 35
 (2) INFORMATION FOR SEQ ID NO: 498:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:498
 Arg Trp Met Cys Leu Arg Arg Phe Ile Ile Phe Leu Phe Ile Leu Leu
 1 5 10 15
 Leu Cys Leu Ile Phe Leu Leu Val Leu Leu Asp Tyr Gln Gly Met Leu
 20 25 30
 Pro Val Cys
 35
 (2) INFORMATION FOR SEQ ID NO: 499:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:499
 Trp Met Cys Leu Arg Arg Phe Ile Ile Phe Leu Phe Ile Leu Leu Leu
 1 5 10 15
 Cys Leu Ile Phe Leu Leu Val Leu Leu Asp Tyr Gln Gly Met Leu Pro
 20 25 30
 Val Cys Pro
 35
 (2) INFORMATION FOR SEQ ID NO: 500:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:500
 Met Cys Leu Arg Arg Phe Ile Ile Phe Leu Phe Ile Leu Leu Leu Cys
 1 5 10 15
 Leu Ile Phe Leu Leu Val Leu Leu Asp Tyr Gln Gly Met Leu Pro Val
 20 25 30
 Cys Pro Leu
 35
 (2) INFORMATION FOR SEQ ID NO: 501:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:501
 Cys Leu Arg Arg Phe Ile Ile Phe Leu Phe Ile Leu Leu Leu Cys Leu
 1 5 10 15
 Ile Phe Leu Leu Val Leu Leu Asp Tyr Gln Gly Met Leu Pro Val Cys
 20 25 30
 Pro Leu Ile
 35
 (2) INFORMATION FOR SEQ ID NO: 502:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:502
 Leu Arg Arg Phe Ile Ile Phe Leu Phe Ile Leu Leu Leu Cys Leu Ile
 1 5 10 15
 Phe Leu Leu Val Leu Leu Asp Tyr Gln Gly Met Leu Pro Val Cys Pro
 20 25 30
 Leu Ile Pro
 35
 (2) INFORMATION FOR SEQ ID NO: 503:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:503
 Arg Arg Phe Ile Ile Phe Leu Phe Ile Leu Leu Leu Cys Leu Ile Phe
 1 5 10 15
 Leu Leu Val Leu Leu Asp Tyr Gln Gly Met Leu Pro Val Cys Pro Leu
 20 25 30
 Ile Pro Gly
 35
 (2) INFORMATION FOR SEQ ID NO: 504:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:504
 Arg Phe Ile Ile Phe Leu Phe Ile Leu Leu Leu Cys Leu Ile Phe Leu
 1 5 10 15
 Leu Val Leu Leu Asp Tyr Gln Gly Met Leu Pro Val Cys Pro Leu Ile
 20 25 30
 Pro Gly Ser
 35
 (2) INFORMATION FOR SEQ ID NO: 505:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:505
 Phe Ile Ile Phe Leu Phe Ile Leu Leu Leu Cys Leu Ile Phe Leu Leu
 1 5 10 15
 Val Leu Leu Asp Tyr Gln Gly Met Leu Pro Val Cys Pro Leu Ile Pro
 20 25 30
 Gly Ser Ser
 35
 (2) INFORMATION FOR SEQ ID NO: 506:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:506
 Ile Ile Phe Leu Phe Ile Leu Leu Leu Cys Leu Ile Phe Leu Leu Val
 1 5 10 15
 Leu Leu Asp Tyr Gln Gly Met Leu Pro Val Cys Pro Leu Ile Pro Gly
 20 25 30
 Ser Ser Thr
 35
 (2) INFORMATION FOR SEQ ID NO: 507:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:507
 Ile Phe Leu Phe Ile Leu Leu Leu Cys Leu Ile Phe Leu Leu Val Leu
 1 5 10 15
 Leu Asp Tyr Gln Gly Met Leu Pro Val Cys Pro Leu Ile Pro Gly Ser
 20 25 30
 Ser Thr Ser
 35
 (2) INFORMATION FOR SEQ ID NO: 508:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:508
 Phe Leu Phe Ile Leu Leu Leu Cys Leu Ile Phe Leu Leu Val Leu Leu
 1 5 10 15
 Asp Tyr Gln Gly Met Leu Pro Val Cys Pro Leu Ile Pro Gly Ser Ser
 20 25 30
 Thr Ser Thr
 35
 (2) INFORMATION FOR SEQ ID NO: 509:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:509
 Leu Phe Ile Leu Leu Leu Cys Leu Ile Phe Leu Leu Val Leu Leu Asp
 1 5 10 15
 Tyr Gln Gly Met Leu Pro Val Cys Pro Leu Ile Pro Gly Ser Ser Thr
 20 25 30
 Ser Thr Gly
 35
 (2) INFORMATION FOR SEQ ID NO: 510:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:510
 Phe Ile Leu Leu Leu Cys Leu Ile Phe Leu Leu Val Leu Leu Asp Tyr
 1 5 10 15
 Gln Gly Met Leu Pro Val Cys Pro Leu Ile Pro Gly Ser Ser Thr Ser
 20 25 30
 Thr Gly Pro
 35
 (2) INFORMATION FOR SEQ ID NO: 511:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:511
 Ile Leu Leu Leu Cys Leu Ile Phe Leu Leu Val Leu Leu Asp Tyr Gln
 1 5 10 15
 Gly Met Leu Pro Val Cys Pro Leu Ile Pro Gly Ser Ser Thr Ser Thr
 20 25 30
 Gly Pro Cys
 35
 (2) INFORMATION FOR SEQ ID NO: 512:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:512
 Leu Leu Leu Cys Leu Ile Phe Leu Leu Val Leu Leu Asp Tyr Gln Gly
 1 5 10 15
 Met Leu Pro Val Cys Pro Leu Ile Pro Gly Ser Ser Thr Ser Thr Gly
 20 25 30
 Pro Cys Arg
 35
 (2) INFORMATION FOR SEQ ID NO: 513:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:513
 Leu Leu Cys Leu Ile Phe Leu Leu Val Leu Leu Asp Tyr Gln Gly Met
 1 5 10 15
 Leu Pro Val Cys Pro Leu Ile Pro Gly Ser Ser Thr Ser Thr Gly Pro
 20 25 30
 Cys Arg Thr
 35
 (2) INFORMATION FOR SEQ ID NO: 514:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:514
 Leu Cys Leu Ile Phe Leu Leu Val Leu Leu Asp Tyr Gln Gly Met Leu
 1 5 10 15
 Pro Val Cys Pro Leu Ile Pro Gly Ser Ser Thr Ser Thr Gly Pro Cys
 20 25 30
 Arg Thr Cys
 35
 (2) INFORMATION FOR SEQ ID NO: 515:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:515
 Cys Leu Ile Phe Leu Leu Val Leu Leu Asp Tyr Gln Gly Met Leu Pro
 1 5 10 15
 Val Cys Pro Leu Ile Pro Gly Ser Ser Thr Ser Thr Gly Pro Cys Arg
 20 25 30
 Thr Cys Met
 35
 (2) INFORMATION FOR SEQ ID NO: 516:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:516
 Leu Ile Phe Leu Leu Val Leu Leu Asp Tyr Gln Gly Met Leu Pro Val
 1 5 10 15
 Cys Pro Leu Ile Pro Gly Ser Ser Thr Ser Thr Gly Pro Cys Arg Thr
 20 25 30
 Cys Met Thr
 35
 (2) INFORMATION FOR SEQ ID NO: 517:
 (i) SEQUENCE CHARACTERISTICS:
 (A) LENGTH: 35 amino acids
 (B) TYPE: amino acid
 (C) STRANDEDNESS:
 (D) TOPOLOGY: unknown
 (ii) MOLECULE TYPE: peptide
 (vi) ORIGINAL SOURCE:
 (A) ORGANISM: not provided
 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:517
 Ile Phe Leu Leu Val Leu Leu Asp Tyr Gln Gly Met Leu Pro Val Cys
 1 5 10 15
 Pro Leu Ile Pro Gly Ser Ser Thr Ser Thr Gly Pro Cys Arg Thr Cys
 20 25 30
 Met Thr Thr
 35