HUMAN ANTIGEN BINDING PROTEINS THAT BIND TO PROPROTEIN CONVERTASE SUBTILISIN KEXIN TYPE 9

[0001] The present disclosure relates to nucleic acid molecules encoding antigen binding proteins (APBs) that bind to proprotein convertais subtilisin kexin type 9 (hereinafter “PCSK9”), as well as pharmaceutical compositions comprising antigen binding proteins that bind to PCSK9, including antigen binding proteins that inhibit the binding of PCSK9 to the LDL receptor, and methods for treating metabolic disorders using such nucleic acids, polypeptides, or pharmaceutical compositions. Diagnostic methods using the antigen binding proteins are also provided.

[0002] Proprotein convertase subtilisin kexin type 9 (PCSK9) is a serine protease involved in regulating the levels of the low density lipoprotein receptor (LDLR) protein (Horton et al., 2007; Seidah and Prat, 2007). In vitro experiments have shown that adding PCSK9 to HepG2 cells lowers the levels of cell surface LDLR (Benjannet et al., 2004; Lagace et al., 2006; Maxwell et al., 2005; Park et al., 2004). Experiments with mice have shown that increasing PCSK9 protein levels decreases levels of LDLR protein in the liver (Benjannet et al., 2004; Lagace et al., 2006; Maxwell et al., 2005; Park et al., 2004), while PCSK9 knockout mice have increased levels of LDLR in the liver (Rashid et al., 2005). Additionally, various human PCSK9 mutations that result in either increased or decreased levels of plasma LDL have been identified (Kotowski et al., 2006; Zhao et al., 2006). PCSK9 has been shown to reduce LDL-receptor levels in the liver, resulting in high levels of LDL-cholesterol in the plasma and increased susceptibility to coronary heart disease. (Peterson et al., J Lipid Res. 49(7):1595-9 (2008)). Therefore, it would be highly advantageous to produce a therapeutic antagonist of PCSK9 that inhibits the activity of PCSK9 and the corresponding role PCSK9 plays in various disease conditions.

[0003] The invention is in part based on a variety of antibodies to PCSK9. PCSK9 presents as an important and advantageous therapeutic target, and the invention provides antibodies as therapeutic and diagnostic agents for use in targeting pathological conditions associated with expression and/or activity of PCSK9. Accordingly, the invention provides methods, compositions, kits and articles of manufacture related to PCSK9.

[0004] In a further embodiment an isolated anti-PCSK9 antigen binding protein s comprising an immunoglobulin heavy chain variable domain polypeptide, or functional fragment thereof having at least 85%, 90%, 95% sequence identity with or comprises the amino acid sequence of any one of SEQ ID NO: 270 to 353 is provided. In a further embodiment an isolated anti-PCSK9 antigen binding protein of any of the preceding claims comprising an immunoglobulin light chain variable domain polypeptide, or functional fragment thereof having at least 85%, 90%, 95% sequence identity with or comprises the amino acid sequence of any one of SEQ ID NO: 186 to 269 is provided. In a further embodiment, an antigen binding protein of any of the previously described ABPs, wherein the antigen binding protein comprises one or more of: (a) a heavy chain and light chain comprised in any one of the antibodies in (d) and comprising an amino acid sequence according comprised in any one of the antibodies, (b) a heavy and light chain variable domain comprised in any one of the antibodies in (d) or (c) a CDRH1, CDRH2, and CDRH3 and a CDRL1, CDRL2 and CDRL3 comprised in any one of the antibodies listed in (d). is provided wherein (d) is antibodies SS-13406 (8A3HLE-51), SS-13407 (8A3HLE-112), SS-14888 (P2C6-HLE51), 13G9, 19A12, 20D12, 25B5, 30G7, SS-15057, SS-15058, SS-15059, SS-15065, SS-15079, SS-15080, SS-15087, SS-15101, SS-15103, SS-15104, SS-15105, SS-15106, SS-15108, SS-15112, SS-15113, SS-15114, SS-15117, SS-15121, SS-15123, SS-15124, SS-15126, SS-15132, SS-15133, SS-15136, SS-15139, SS-15140, SS-15141, SS-13983 (A01), SS-13991 (A02), SS-13993 (C02), SS-12685 (P1B1), SS-12686 (P2F5), SS-12687 (P2C6), SS-14892 (P2F5/P2C6), SS-15509, SS-15510, SS-15511, SS-15512, SS-15513, SS-15514, SS-15497, SS-15515, SS-15516, SS-15517, SS-15518, SS-15519, SS-15520, SS-15522, SS-15524, SS-14835, SS-15194, SS-15195, SS-15196, SS-14894, SS-15504, SS-15494, SS-14892, SS-15495, SS-15496, SS-15497, SS-115503, SS-15505, SS-15506, SS-15507, SS-15502, SS-15508, SS-1550, SS-15500, SS-15003, SS-15005, SS-15757 (P1F4), SS-15758 (P1B6), SS-15759 (P2F4), SS-15761 (P2G5), SS-15763 (P2H7) or SS-15764 (P2H8).

[0005] In a further embodiment, an anti-PCSK9 antigen binding protein of any of the above described ABPS, wherein the antigen binding protein is a monoclonal antibody is provided. In a further embodiment, an anti-PCSK9 antigen binding protein of any of the above described ABPS, wherein the antibody is humanized is provided. In a further embodiment, an anti-PCSK9 antibody of any of the above described antibodies, wherein the antibody is human is provided. In a further embodiment, an anti-PCSK9 antibody of any of the above described antibodies, wherein the antibody is an antibody fragment selected from a Fab, Fab′-SH, Fv, scFv or (Fab′).sub.2 fragment is provided. In a further embodiment, an anti-PCSK9 antibody of any of the above described antibodies, wherein at least a portion of the framework sequence is a human consensus framework sequence is provided.

[0006] In a further embodiment, an isolated nucleic acid encoding an anti-PCSK9 antigen binding protein of any of the above described ABPs is provided. In a further embodiment, a vector comprising the nucleic acid encoding an above described ABP is provided. In one embodiment, the vector of the invention is an expression vector. In another embodiment, a host cell comprising the vector of the invention is provided. In one embodiment host cell of the invention is a prokaryotic host cell. In another embodiment of the invention, the host cell is a eukaryotic host cell. In a further embodiment, a method for making an anti-PCSK9 antigen binding protein of the invention, said method comprising culturing a host cell comprising a vector comprising a nucleic acid encoding an above described anti-PCSK9 antigen binding protein 1 under conditions suitable for expression of the nucleic acid encoding the anti-PCSK9 antibody is provided. In a further embodiment the method of the invention, further comprising recovering the anti-PCSK9 antigen binding protein from the host cell is provided.

[0007] In another embodiment, a pharmaceutical composition comprising an above described anti-PCSK9 antigen binding protein and a pharmaceutically acceptable carrier is provided. In a further embodiment, a method of reducing LDL-cholesterol level in a subject, said method comprising administering to the subject an effective amount of any of the above described anti-PCSK9 antigen binding proteins is provided. In a further embodiment, a method of treating cholesterol related disorder in a subject, said method comprising administering to the subject an effective amount of any of the above-described anti-PCSK9 antigen binding proteins is provided. In a further embodiment, a method of treating hypercholesterolemia in a subject, said method comprising administering to the subject an effective amount of the any of the above-described anti-PCSK9 antigen binding proteins is provided. In another embodiment, the above described method of treatment further comprising administering to the subject an effective amount of a second medicament, wherein the anti-PCSK9 antigen binding protein is the first medicament is provided. In some embodiments a method wherein the second medicament elevates the level of LDLR is provided. In some embodiments a method wherein the second medicament reduces the level of LDL-cholesterol is provided. In some embodiments, a method wherein the second medicament comprises a statin is provided. In some embodiments, a method wherein the statin is selected from the group consisting of atorvastatin, fluvastatin, lovastatin, mevastatin, pitavastatin, pravastatin, rosuvastatin, simvastatin, and any combination thereof, is provided. In another embodiment, a method of inhibiting binding of PCSK9 to LDLR in a subject, said method comprising administering to the subject an effective amount of any of the above described anti-PCSK9 antigen binding proteins is provided.

[0008] In a further embodiment, a method of detecting PCSK9 protein in a sample, said method comprising (a) contacting the sample with any of the above described antigen binding proteins and (b) detecting formation of a complex between the anti-PCSK9 antigen binding protein and the PCSK9 protein is provided.

[0016] The section headings used herein are for organizational purposes only and are not to be construed as limiting the subject matter described.

[0017] Unless otherwise defined herein, scientific and technical terms used in connection with the present application shall have the meanings that are commonly understood by those of ordinary skill in the art. Further, unless otherwise required by context, singular terms shall include pluralities and plural terms shall include the singular.

[0018] Generally, nomenclatures used in connection with, and techniques of, cell and tissue culture, molecular biology, immunology, microbiology, genetics and protein and nucleic acid chemistry and hybridization described herein are those well known and commonly used in the art. The methods and techniques of the present application are generally performed according to conventional methods well known in the art and as described in various general and more specific references that are cited and discussed throughout the present specification unless otherwise indicated. See, e.g., Sambrook et al., Molecular Cloning: A Laboratory Manual, 3^rd ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y. (2001) and subsequent editions, Ausubel et al., Current Protocols in Molecular Biology, Greene Publishing Associates (1992), and Harlow & Lane, Antibodies: A Laboratory Manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y. (1988), which are incorporated herein by reference. Enzymatic reactions and purification techniques are performed according to manufacturer's specifications, as commonly accomplished in the art or as described herein. The terminology used in connection with, and the laboratory procedures and techniques of, analytical chemistry, synthetic organic chemistry, and medicinal and pharmaceutical chemistry described herein are those well known and commonly used in the art. Standard techniques can be used for chemical syntheses, chemical analyses, pharmaceutical preparation, formulation, and delivery, and treatment of patients.

[0019] It should be understood that the instant disclosure is not limited to the particular methodology, protocols, and reagents, etc., described herein and as such can vary. The terminology used herein is for the purpose of describing particular embodiments only, and is not intended to limit the scope of the present disclosure.

[0020] Other than in the operating examples, or where otherwise indicated, all numbers expressing quantities of ingredients or reaction conditions used herein should be understood as modified in all instances by the term “about.” The term “about” when used in connection with percentages can mean±5%, e.g., 1%, 2%, 3%, or 4%.

[0021] As used herein, the terms “a” and “an” mean “one or more” unless specifically stated otherwise.

[0022] As used herein, an “antigen binding protein” is a protein comprising a portion that binds to an antigen or target and, optionally, a scaffold or framework portion that allows the antigen binding portion to adopt a conformation that promotes binding of the antigen binding protein to the antigen. Examples of antigen binding proteins include a human antibody, a humanized antibody; a chimeric antibody; a recombinant antibody; a single chain antibody; a diabody; a triabody; a tetrabody; a Fab fragment; a F(ab′)₂ fragment; an IgD antibody; an IgE antibody; an IgM antibody; an IgG1 antibody; an IgG2 antibody; an IgG3 antibody; or an IgG4 antibody, and fragments thereof. The antigen binding protein can comprise, for example, an alternative protein scaffold or artificial scaffold with grafted CDRs or CDR derivatives. Such scaffolds include, but are not limited to, antibody-derived scaffolds comprising mutations introduced to, for example, stabilize the three-dimensional structure of the antigen binding protein as well as wholly synthetic scaffolds comprising, for example, a biocompatible polymer. See, e.g., Komdorfer et al., (2003) Proteins: Structure, Function, and Bioinformatics, 53(1):121-129; Roque et al., (2004) Biotechnol. Prog. 20:639-654. In addition, peptide antibody mimetics (“PAMs”) can be used, as well as scaffolds based on antibody mimetics utilizing fibronectin components as a scaffold.

[0023] An antigen binding protein can have, for example, the structure of a naturally occurring immunoglobulin. An “immunoglobulin” is a tetrameric molecule. In a naturally occurring immunoglobulin, each tetramer is composed of two identical pairs of polypeptide chains, each pair having one “light” (about 25 kDa) and one “heavy” chain (about 50-70 kDa). The amino-terminal portion of each chain includes a variable region of about 100 to 110 or more amino acids primarily responsible for antigen recognition. The carboxy-terminal portion of each chain defines a constant region primarily responsible for effector function. Human light chains are classified as kappa and lambda light chains. Heavy chains are classified as mu, delta, gamma, alpha, or epsilon, and define the antibody's isotype as IgM, IgD, IgG, IgA, and IgE, respectively. Within light and heavy chains, the variable and constant regions are joined by a “J” region of about 12 or more amino acids, with the heavy chain also including a “D” region of about 10 more amino acids. See generally, Fundamental Immunology 2^nd ed. Ch. 7 (Paul, W., ed., Raven Press, N.Y. (1989)), incorporated by reference in its entirety for all purposes. The variable regions of each light/heavy chain pair form the antibody binding site such that an intact immunoglobulin has two binding sites.

[0024] Naturally occurring immunoglobulin chains exhibit the same general structure of relatively conserved framework regions (FR) joined by three hypervariable regions, also called complementarity determining regions or CDRs. From N-terminus to C-terminus, both light and heavy chains comprise the domains FR1, CDR1, FR2, CDR2, FR3, CDR3 and FR4. The assignment of amino acids to each domain can be done in accordance with the definitions of Kabat et al., (1991) “Sequences of Proteins of Immunological Interest”, 5^th Ed., US Dept. of Health and Human Services, PHS, NIH, NIH Publication no. 91-3242. Although presented herein using the Kabat nomenclature system, as desired, the CDRs disclosed herein can also be redefined according an alternative nomenclature scheme, such as that of Chothia (see Chothia & Lesk, (1987) J. Mol. Biol. 196:901-917; Chothia et al., (1989) Nature 342:878-883 or Honegger & Pluckthun, (2001) J. Mol. Biol. 309:657-670).

[0025] In the context of the instant disclosure an antigen binding protein is said to “specifically bind” or “selectively bind” its target antigen when the dissociation constant (K_D) is ≦10⁻⁸ M. The antibody specifically binds antigen with “high affinity” when the K_D is ≦5×10⁻⁹ M, and with “very high affinity” when the K_D is ≦5×10⁻¹ M. In one embodiment, the antibodies will bind to PCSK9 with a K_D of between about 10⁻⁷ M and 10⁻¹² M, and in yet another embodiment the antibodies will bind with a K_D≦5×10⁻⁹.

[0026] An “antibody” refers to an intact immunoglobulin or to an antigen binding portion thereof that competes with the intact antibody for specific binding, unless otherwise specified. Antigen binding portions can be produced by recombinant DNA techniques or by enzymatic or chemical cleavage of intact antibodies. Antigen binding portions include, inter alia, Fab, Fab′, F(ab′)₂, Fv, domain antibodies (dAbs), fragments including complementarity determining regions (CDRs), single-chain antibodies (scFv), chimeric antibodies, diabodies, triabodies, tetrabodies, and polypeptides that contain at least a portion of an immunoglobulin that is sufficient to confer specific antigen binding to the polypeptide.

[0027] A Fab fragment is a monovalent fragment having the V_L, V_H, C_L and C_H1 domains; a F(ab′)₂ fragment is a bivalent fragment having two Fab fragments linked by a disulfide bridge at the hinge region; a Fd fragment has the V_H and C_H1 domains; an Fv fragment has the V_L and V_H domains of a single arm of an antibody; and a dAb fragment has a V_H domain, a V_L domain, or an antigen-binding fragment of a V_H or V_L domain (U.S. Pat. Nos. 6,846,634, and 6,696,245; and US App. Pub. Nos. 05/0202512, 04/0202995, 04/0038291, 04/0009507, 03/0039958, Ward et al., Nature 341:544-546 (1989)).

[0028] A single-chain antibody (scFv) is an antibody in which a V₁ and a V₁ region are joined via a linker (e.g., a synthetic sequence of amino acid residues) to form a continuous protein chain wherein the linker is long enough to allow the protein chain to fold back on itself and form a monovalent antigen binding site (see, e.g., Bird et al., (1988) Science 242:423-26 and Huston et al., (1988) Proc. Natl. Acad. Sci. USA 85:5879-83). Diabodies are bivalent antibodies comprising two polypeptide chains, wherein each polypeptide chain comprises V_H and V_L domains joined by a linker that is too short to allow for pairing between two domains on the same chain, thus allowing each domain to pair with a complementary domain on another polypeptide chain (see, e.g., Holliger et al., (1993) Proc. Natl. Acad. Sci. USA 90:6444-48, and Poljak et al., (1994) Structure 2:1121-23). If the two polypeptide chains of a diabody are identical, then a diabody resulting from their pairing will have two identical antigen binding sites. Polypeptide chains having different sequences can be used to make a diabody with two different antigen binding sites. Similarly, tribodies and tetrabodies are antibodies comprising three and four polypeptide chains, respectively, and forming three and four antigen binding sites, respectively, which can be the same or different.

[0029] Complementarity determining regions (CDRs) and framework regions (FR) of a given antibody can be identified using the system described by Kabat et al., (1991) “Sequences of Proteins of Immunological Interest”, 5^th Ed., US Dept. of Health and Human Services, PHS, NIH, NIH Publication no. 91-3242. Although presented using the Kabat nomenclature system, as desired, the CDRs disclosed herein can also be redefined according an alternative nomenclature scheme, such as that of Chothia (see Chothia & Lesk, (1987) J. Mol. Biol. 196:901-917; Chothia et al., (1989) Nature 342:878-883 or Honegger & Pluckthun, (2001) J. Mol. Biol. 309:657-670). One or more CDRs can be incorporated into a molecule either covalently or noncovalently to make it an antigen binding protein. An antigen binding protein can incorporate the CDR(s) as part of a larger polypeptide chain, can covalently link the CDR(s) to another polypeptide chain, or can incorporate the CDR(s) noncovalently. The CDRs permit the antigen binding protein to specifically bind to a particular antigen of interest.

[0030] An antigen binding protein can but need not have one or more binding sites. If there is more than one binding site, the binding sites can be identical to one another or can be different. For example, a naturally occurring human immunoglobulin typically has two identical binding sites, while a “bispecific” or “bifunctional” antibody has two different binding sites. Antigen binding proteins of this bispecific form (e.g., those comprising various heavy and light chain CDRs provided herein) comprise aspects of the instant disclosure.

[0031] The term “human antibody” includes all antibodies that have one or more variable and constant regions derived from human immunoglobulin sequences. In one embodiment, all of the variable and constant domains are derived from human immunoglobulin sequences (a fully human antibody). These antibodies can be prepared in a variety of ways, examples of which are described below, including through the immunization with an antigen of interest of a mouse that is genetically modified to express antibodies derived from human heavy and/or light chain-encoding genes, such as a mouse derived from a XENOMOUSE®, ULTIMAB™, HUMAB-MOUSE®, VELOCIMOUSE®, VELOCIMMUNE®, KYMOUSE, or ALIVAMAB system, or derived from human heavy chain transgenic mouse, transgenic rat human antibody repertoire, transgenic rabbit human antibody repertoire or cow human antibody repertoire or HUTARG™ technology. Phage-based approaches can also be employed.

[0032] A humanized antibody has a sequence that differs from the sequence of an antibody derived from a non-human species by one or more amino acid substitutions, deletions, and/or additions, such that the humanized antibody is less likely to induce an immune response, and/or induces a less severe immune response, as compared to the non-human species antibody, when it is administered to a human subject. In one embodiment, certain amino acids in the framework and constant domains of the heavy and/or light chains of the non-human species antibody are mutated to produce the humanized antibody. In another embodiment, the constant domain(s) from a human antibody are fused to the variable domain(s) of a non-human species. In another embodiment, one or more amino acid residues in one or more CDR sequences of a non-human antibody are changed to reduce the likely immunogenicity of the non-human antibody when it is administered to a human subject, wherein the changed amino acid residues either are not critical for immunospecific binding of the antibody to its antigen, or the changes to the amino acid sequence that are made are conservative changes, such that the binding of the humanized antibody to the antigen is not significantly worse than the binding of the non-human antibody to the antigen. Examples of how to make humanized antibodies can be found in U.S. Pat. Nos. 6,054,297, 5,886,152 and 5,877,293.

[0033] The term “chimeric antibody” refers to an antibody that contains one or more regions from one antibody and one or more regions from one or more other antibodies. In one embodiment, one or more of the CDRs are derived from a human antibody that binds to PCSK9. In another embodiment, all of the CDRs are derived from a human antibody that binds to PCSK9. In another embodiment, the CDRs from more than one human antibody that binds to PCSK9 are mixed and matched in a chimeric antibody. For instance, a chimeric antibody can comprise a CDR1 from the light chain of a first human antibody that binds to PCSK9, a CDR2 and a CDR3 from the light chain of a second human antibody that binds to PCSK9, and the CDRs from the heavy chain from a third antibody that binds to PCSK9. Further, the framework regions can be derived from one of the same antibodies that binds PCSK9, from one or more different antibodies, such as a human antibody, or from a humanized antibody. In one example of a chimeric antibody, a portion of the heavy and/or light chain is identical with, homologous to, or derived from an antibody from a particular species or belonging to a particular antibody class or subclass, while the remainder of the chain(s) is/are identical with, homologous to, or derived from an antibody or antibodies from another species or belonging to another antibody class or subclass. Also included are fragments of such antibodies that exhibit the desired biological activity (e.g., the ability to specifically bind to PCSK9).

[0034] The term “light chain” includes a full-length light chain and fragments thereof having sufficient variable region sequence to confer binding specificity. A full-length light chain includes a variable region domain, V_L, and a constant region domain, C_L. The variable region domain of the light chain is at the amino-terminus of the polypeptide. Light chains include kappa (“κ”) chains and lambda (“λ”) chains.

[0035] The term “heavy chain” includes a full-length heavy chain and fragments thereof having sufficient variable region sequence to confer binding specificity. A full-length heavy chain includes a variable region domain, V_H, and three constant region domains, C_H1, C_H2, and C_H3. The V_H domain is at the amino-terminus of the polypeptide, and the C_H domains are at the carboxyl-terminus, with the C_H3 being closest to the carboxy-terminus of the polypeptide. Heavy chains can be of any isotype, including IgG (including IgG1, IgG2, IgG3 and IgG4 subtypes), IgA (including IgA1 and IgA2 subtypes), IgM and IgE.

[0036] The term “immunologically functional fragment” (or simply “fragment”) of an antigen binding protein, e.g., an antibody or immunoglobulin chain (heavy or light chain), as used herein, is an antigen binding protein comprising a portion (regardless of how that portion is obtained or synthesized) of an antibody that lacks at least some of the amino acids present in a full-length chain but which is capable of specifically binding to an antigen. Such fragments are biologically active in that they bind specifically to the target antigen and can compete with other antigen binding proteins, including intact antibodies, for specific binding to a given epitope. In one aspect, such a fragment will retain at least one CDR present in the full-length light or heavy chain, and in some embodiments will comprise a single heavy chain and/or light chain or portion thereof. These biologically active fragments can be produced by recombinant DNA techniques, or can be produced by enzymatic or chemical cleavage of antigen binding proteins, including intact antibodies. Immunologically functional immunoglobulin fragments include, but are not limited to, Fab, Fab′, F(ab′)₂, Fv, domain antibodies and single-chain antibodies, and can be derived from any mammalian source, including but not limited to human, mouse, rat, camelid or rabbit. It is contemplated further that a functional portion of the antigen binding proteins disclosed herein, for example, one or more CDRs, could be covalently bound to a second protein or to a small molecule to create a therapeutic agent directed to a particular target in the body, possessing bifunctional therapeutic properties, or having a prolonged serum half-life.

[0037] An “Fc” region contains two heavy chain fragments comprising the C_H2 and C_H3 domains of an antibody. The two heavy chain fragments are held together by two or more disulfide bonds and by hydrophobic interactions of the C_H3 domains.

[0038] An “Fab′ fragment” contains one light chain and a portion of one heavy chain that contains the V_H domain and the C_H1 domain and also the region between the C_H1 and C_H2 domains, such that an interchain disulfide bond can be formed between the two heavy chains of two Fab′ fragments to form an F(ab′) molecule.

[0039] An “F(ab′)₂ fragment” contains two light chains and two heavy chains containing a portion of the constant region between the C_H1 and C_H2 domains, such that an interchain disulfide bond is formed between the two heavy chains. A F(ab′)₂ fragment thus is composed of two Fab′ fragments that are held together by a disulfide bond between the two heavy chains.

[0040] The “Fv region” comprises the variable regions from both the heavy and light chains, but lacks the constant regions.

[0041] A “domain antibody” is an immunologically functional immunoglobulin fragment containing only the variable region of a heavy chain or the variable region of a light chain. In some instances, two or more V_H regions are covalently joined with a peptide linker to create a bivalent domain antibody. The two V_H regions of a bivalent domain antibody can target the same or different antigens.

[0042] A “hemibody” is an immunologically-functional immunoglobulin construct comprising a complete heavy chain, a complete light chain and a second heavy chain Fc region paired with the Fe region of the complete heavy chain. A linker can, but need not, be employed to join the heavy chain Fc region and the second heavy chain Fc region. In particular embodiments a hemibody is a monovalent form of an antigen binding protein disclosed herein. In other embodiments, pairs of charged residues can be employed to associate one Fc region with the second Fc region.

[0043] A “bivalent antigen binding protein” or “bivalent antibody” comprises two antigen binding sites. In some instances, the two binding sites have the same antigen specificities. Bivalent antigen binding proteins and bivalent antibodies can be bispecific, as described herein, and form aspects of the instant disclosure.

[0044] A “multispecific antigen binding protein” or “multispecific antibody” is one that targets more than one antigen or epitope, and forms another aspect of the instant disclosure.

[0045] A “bispecific,” “dual-specific” or “bifunctional” antigen binding protein or antibody is a hybrid antigen binding protein or antibody, respectively, having two different antigen binding sites. Bispecific antigen binding proteins and antibodies are a species of multispecific antigen binding protein or multispecific antibody and can be produced by a variety of methods including, but not limited to, fusion of hybridomas or linking of Fab′ fragments. See, e.g., Songsivilai and Lachmann, (1990) Clin. Exp. Immunol. 79:315-321; Kostelny et al., (1992) J. Immunol. 148:1547-1553. The two binding sites of a bispecific antigen binding protein or antibody will bind to two different epitopes, which can reside on the same (e.g., PCSK9) or different protein targets, including (e.g.: lecithin cholesterol acyl transferase (LCAT), angiopoietin protein like-3 (ANGPTL3), ANGPTL4, Endothelial Lipase (EL), apolipoprotein CIII (ApoCIII), lipoprotein lipase (LPL), fibroblast growth factor 21 (FGF21)).

[0046] The term “polynucleotide” or “nucleic acid” includes both single-stranded and double-stranded nucleotide polymers. The nucleotides comprising the polynucleotide can be ribonucleotides or deoxyribonucleotides or a modified form of either type of nucleotide. Said modifications include base modifications such as bromouridine and inosine derivatives, ribose modifications such as 2′,3′-dideoxyribose, and internucleotide linkage modifications such as phosphorothioate, phosphorodithioate, phosphoroselenoate, phosphorodiselenoate, phosphoroanilothioate, phoshoraniladate and phosphoroamidate.

[0047] The term “oligonucleotide” means a polynucleotide comprising 200 or fewer nucleotides. In some embodiments, oligonucleotides are 10 to 60 bases in length. In other embodiments, oligonucleotides are 12, 13, 14, 15, 16, 17, 18, 19, or 20 to 40 nucleotides in length. Oligonucleotides can be single stranded or double stranded, e.g., for use in the construction of a mutant gene. Oligonucleotides can be sense or antisense oligonucleotides. An oligonucleotide can include a label, including a radiolabel, a fluorescent label, a hapten or an antigenic label, for detection assays. Oligonucleotides can be used, for example, as PCR primers, cloning primers or hybridization probes.

[0048] An “isolated nucleic acid molecule” means a DNA or RNA of genomic, mRNA, cDNA, or synthetic origin or some combination thereof which is not associated with all or a portion of a polynucleotide in which the isolated polynucleotide is found in nature, or is linked to a polynucleotide to which it is not linked in nature. For purposes of this disclosure, it is understood that “a nucleic acid molecule comprising” a particular nucleotide sequence does not encompass intact chromosomes. Isolated nucleic acid molecules “comprising” specified nucleic acid sequences can include, in addition to the specified sequences, coding sequences for up to ten or even up to twenty other proteins or portions thereof, or can include operably linked regulatory sequences that control expression of the coding region of the recited nucleic acid sequences, and/or can include vector sequences.

[0049] Unless specified otherwise, the left-hand end of any single-stranded polynucleotide sequence discussed herein is the 5′ end; the left-hand direction of double-stranded polynucleotide sequences is referred to as the 5′ direction. The direction of 5′ to 3′ addition of nascent RNA transcripts is referred to as the transcription direction; sequence regions on the DNA strand having the same sequence as the RNA transcript that are 5′ to the 5′ end of the RNA transcript are referred to as “upstream sequences;” sequence regions on the DNA strand having the same sequence as the RNA transcript that are 3′ to the 3′ end of the RNA transcript are referred to as “downstream sequences.”

[0050] The term “control sequence” refers to a polynucleotide sequence that can affect the expression and processing of coding sequences to which it is ligated. The nature of such control sequences can depend upon the host organism. In particular embodiments, control sequences for prokaryotes can include a promoter, a ribosomal binding site, and a transcription termination sequence. For example, control sequences for eukaryotes can include promoters comprising one or a plurality of recognition sites for transcription factors, transcription enhancer sequences, and transcription termination sequence. “Control sequences” can include leader sequences and/or fusion partner sequences.

[0051] The term “vector” means any molecule or entity (e.g., nucleic acid, plasmid, bacteriophage or virus) used to transfer protein coding information into a host cell.

[0052] The term “expression vector” or “expression construct” refers to a vector that is suitable for transformation of a host cell and contains nucleic acid sequences that direct and/or control (in conjunction with the host cell) expression of one or more heterologous coding regions operatively linked thereto. An expression construct can include, but is not limited to, sequences that affect or control transcription, translation, and, if introns are present, affect RNA splicing of a coding region operably linked thereto.

[0053] As used herein, “operably linked” means that the components to which the term is applied are in a relationship that allows them to carry out their inherent functions under suitable conditions. For example, a control sequence in a vector that is “operably linked” to a protein coding sequence is ligated thereto so that expression of the protein coding sequence is achieved under conditions compatible with the transcriptional activity of the control sequences.

[0054] The term “host cell” means a cell that has been transformed, or is capable of being transformed, with a nucleic acid sequence and thereby expresses a gene of interest. The term includes the progeny of the parent cell, whether or not the progeny is identical in morphology or in genetic make-up to the original parent cell, so long as the gene of interest is present.

[0055] The term “transduction” means the transfer of genes from one bacterium to another, usually by bacteriophage. “Transduction” also refers to the acquisition and transfer of eukaryotic cellular sequences by replication-defective retroviruses.

[0056] The term “transfection” means the uptake of foreign or exogenous DNA by a cell, and a cell has been “transfected” when the exogenous DNA has been introduced inside the cell membrane. A number of transfection techniques are well known in the art and are disclosed herein. See, e.g., Graham et al., (1973) Virology 52:456; Sambrook et al., (2001), supra; Davis et al., (1986) Basic Methods in Molecular Biology, Elsevier, Chu et al., (1981) Gene 13:197. Such techniques can be used to introduce one or more exogenous DNA moieties into suitable host cells.

[0057] The term “transformation” refers to a change in a cell's genetic characteristics, and a cell has been transformed when it has been modified to contain new DNA or RNA. For example, a cell is transformed where it is genetically modified from its native state by introducing new genetic material via transfection, transduction, or other techniques. Following transfection or transduction, the transforming DNA can recombine with that of the cell by physically integrating into a chromosome of the cell, or can be maintained transiently as an episomal element without being replicated, or can replicate independently as a plasmid. A cell is considered to have been “stably transformed” when the transforming DNA is replicated with the division of the cell.

[0058] The terms “polypeptide” or “protein” are used interchangeably herein to refer to a polymer of amino acid residues. The terms also apply to amino acid polymers in which one or more amino acid residues is an analog or mimetic of a corresponding naturally occurring amino acid, as well as to naturally occurring amino acid polymers. The terms can also encompass amino acid polymers that have been modified, e.g., by the addition of carbohydrate residues to form glycoproteins, or phosphorylated. Polypeptides and proteins can be produced by a naturally-occurring and non-recombinant cell, or polypeptides and proteins can be produced by a genetically-engineered or recombinant cell. Polypeptides and proteins can comprise molecules having the amino acid sequence of a native protein, or molecules having deletions from, additions to, and/or substitutions of one or more amino acids of the native sequence. The terms “polypeptide” and “protein” encompass antigen binding proteins that specifically or selectively bind to PCSK9, or sequences that have deletions from, additions to, and/or substitutions of one or more amino acids of an antigen binding protein that specifically or selectively binds to PCSK9. The term “polypeptide fragment” refers to a polypeptide that has an amino-terminal deletion, a carboxyl-terminal deletion, and/or an internal deletion as compared with the full-length protein. Such fragments can also contain modified amino acids as compared with the full-length protein. In certain embodiments, fragments are about five to 500 amino acids long. For example, fragments can be at least 5, 6, 8, 10, 14, 20, 50, 70, 100, 110, 150, 200, 250, 300, 350, 400, or 450 amino acids long. Useful polypeptide fragments include immunologically functional fragments of antibodies, including binding domains. In the case of an antigen binding protein that binds to PCSK9, useful fragments include but are not limited to a CDR region, a variable domain of a heavy or light chain, a portion of an antibody chain or just its variable region including two CDRs, and the like.

[0059] The term “isolated protein” referred means that a subject protein (1) is free of at least some other proteins with which it would normally be found, (2) is essentially free of other proteins from the same source, e.g., from the same species, (3) is expressed by a cell from a different species, (4) has been separated from at least about 50 percent of polynucleotides, lipids, carbohydrates, or other materials with which it is associated in nature, (5) is operably associated (by covalent or noncovalent interaction) with a polypeptide with which it is not associated in nature, or (6) does not occur in nature. Typically, an “isolated protein” constitutes at least about 5%, at least about 10%, at least about 25%, or at least about 50% of a given sample. Genomic DNA, cDNA, mRNA or other RNA, of synthetic origin, or any combination thereof can encode such an isolated protein. Preferably, the isolated protein is substantially free from proteins or polypeptides or other contaminants that are found in its natural environment that would interfere with its therapeutic, diagnostic, prophylactic, research or other use.

[0060] A “variant” of a polypeptide (e.g., an antigen binding protein, or an antibody) comprises an amino acid sequence wherein one or more amino acid residues are inserted into, deleted from and/or substituted into the amino acid sequence relative to another polypeptide sequence. Variants include fusion proteins.

[0061] A “derivative” of a polypeptide is a polypeptide (e.g., an antigen binding protein, or an antibody) that has been chemically modified in some manner distinct from insertion, deletion, or substitution variants, e.g., by conjugation to another chemical moiety.

[0062] The term “naturally occurring” as used throughout the specification in connection with biological materials such as polypeptides, nucleic acids, host cells, and the like, refers to materials which are found in nature.

[0063] “Antigen binding region” means a protein, or a portion of a protein, that specifically binds a specified antigen, e.g. PCSK9. For example, that portion of an antigen binding protein that contains the amino acid residues that interact with an antigen and confer on the antigen binding protein its specificity and affinity for the antigen is referred to as “antigen binding region.” An antigen binding region typically includes one or more “complementary binding regions” (“CDRs”). Certain antigen binding regions also include one or more “framework” regions. A “CDR” is an amino acid sequence that contributes to antigen binding specificity and affinity. “Framework” regions can aid in maintaining the proper conformation of the CDRs to promote binding between the antigen binding region and an antigen.

[0064] In certain aspects, recombinant antigen binding proteins that bind to PCSK9, are provided. In this context, a “recombinant protein” is a protein made using recombinant techniques, i.e., through the expression of a recombinant nucleic acid as described herein. Methods and techniques for the production of recombinant proteins are well known in the art.

[0065] The term “compete” when used in the context of antigen binding proteins (e.g., neutralizing antigen binding proteins, neutralizing antibodies, agonistic antigen binding proteins, agonistic antibodies and binding proteins that bind to PCSK9 that compete for the same epitope or binding site on a target means competition between antigen binding proteins as determined by an assay in which the antigen binding protein (e.g., antibody or immunologically functional fragment thereof) under study prevents or inhibits the specific binding of a reference molecule (e.g., a reference ligand, or reference antigen binding protein, such as a reference antibody) to a common antigen (e.g., PCSK9 or a fragment thereof). Numerous types of competitive binding assays can be used to determine if a test molecule competes with a reference molecule for binding. Examples of assays that can be employed include solid phase direct or indirect radioimmunoassay (RIA), solid phase direct or indirect enzyme immunoassay (EIA), sandwich competition assay (see, e.g., Stahli et al., (1983) Methods in Enzymology 9:242-253); solid phase direct biotin-avidin EIA (see, e.g., Kirkland et al., (1986) J. Immunol. 137:3614-3619) solid phase direct labeled assay, solid phase direct labeled sandwich assay (see, e.g., Harlow and Lane, (1988) supra); solid phase direct label RIA using 1-125 label (see, e.g., Morel et al., (1988) Molec. Immunol. 25:7-15); solid phase direct biotin-avidin EIA (see, e.g., Cheung, et al., (1990) Virology 176:546-552); and direct labeled RIA (Moldenhauer et al., (1990) Scand. J. Immunol. 32:77-82). Typically, such an assay involves the use of a purified antigen bound to a solid surface or cells bearing either of an unlabelled test antigen binding protein or a labeled reference antigen binding protein. Competitive inhibition is measured by determining the amount of label bound to the solid surface or cells in the presence of the test antigen binding protein. Usually the test antigen binding protein is present in excess. Antigen binding proteins identified by competition assay (competing antigen binding proteins) include antigen binding proteins binding to the same epitope as the reference antigen binding proteins and antigen binding proteins binding to an adjacent epitope sufficiently proximal to the epitope bound by the reference antigen binding protein for steric hindrance to occur. Additional details regarding methods for determining competitive binding are provided in the examples herein. Usually, when a competing antigen binding protein is present in excess, it will inhibit specific binding of a reference antigen binding protein to a common antigen by at least 40%, 45%, 50%, 55%, 60%, 65%, 70% or 75%. In some instance, binding is inhibited by at least 80%, 85%, 90%, 95%, or 97% or more.

[0066] The term “antigen” refers to a molecule or a portion of a molecule capable of being bound by a selective binding agent, such as an antigen binding protein (including, e.g., an antibody or immunological functional fragment thereof), and may also be capable of being used in an animal to produce antibodies capable of binding to that antigen. An antigen can possess one or more epitopes that are capable of interacting with different antigen binding proteins, e.g., antibodies.

[0067] The term “epitope” means the amino acids of a target molecule that are contacted by an antigen binding protein (for example, an antibody) when the antigen binding protein is bound to the target molecule. The term includes any subset of the complete list of amino acids of the target molecule that are contacted when an antigen binding protein, such as an antibody, is bound to the target molecule. An epitope can be contiguous or non-contiguous (e.g., (i) in a single-chain polypeptide, amino acid residues that are not contiguous to one another in the polypeptide sequence but that within in context of the target molecule are bound by the antigen binding protein, or (ii) in a multimeric receptor comprising two or more individual components, amino acid residues that are present on one or more of the individual components, but which are still bound by the antigen binding protein). In certain embodiments, epitopes can be mimetic in that they comprise a three dimensional structure that is similar to an antigenic epitope used to generate the antigen binding protein, yet comprise none or only some of the amino acid residues found in that epitope used to generate the antigen binding protein. Most often, epitopes reside on proteins, but in some instances can reside on other kinds of molecules, such as nucleic acids. Epitope determinants can include chemically active surface groupings of molecules such as amino acids, sugar side chains, phosphoryl or sulfonyl groups, and can have specific three dimensional structural characteristics, and/or specific charge characteristics. Generally, antigen binding proteins specific for a particular target molecule will preferentially recognize an epitope on the target molecule in a complex mixture of proteins and/or macromolecules.

[0068] The term “identity” refers to a relationship between the sequences of two or more polypeptide molecules or two or more nucleic acid molecules, as determined by aligning and comparing the sequences. “Percent identity” means the percent of identical residues between the amino acids or nucleotides in the compared molecules and is calculated based on the size of the smallest of the molecules being compared. For these calculations, gaps in alignments (if any) must be addressed by a particular mathematical model or computer program (i.e., an “algorithm”). Methods that can be used to calculate the identity of the aligned nucleic acids or polypeptides include those described in Computational Molecular Biology, (Lesk, A. M., ed.), (1988) New York: Oxford University Press; Biocomputing Informatics and Genome Projects, (Smith, D. W., ed.), 1993, New York: Academic Press; Computer Analysis of Sequence Data, Part I, (Griffin, A. M., and Griffin, H. G., eds.), 1994, New Jersey: Humana Press; von Heinje, G., (1987) Sequence Analysis in Molecular Biology, New York: Academic Press; Sequence Analysis Primer, (Gribskov, M. and Devereux, J., eds.), 1991, New York: M. Stockton Press; and Carillo et al., (1988) J. Applied Math. 48:1073.

[0069] In calculating percent identity, the sequences being compared are aligned in a way that gives the largest match between the sequences. The computer program used to determine percent identity is the GCG program package, which includes GAP (Devereux et al., (1984) Nucl. Acid Res. 12:387; Genetics Computer Group, University of Wisconsin, Madison, Wis.). The computer algorithm GAP is used to align the two polypeptides or polynucleotides for which the percent sequence identity is to be determined. The sequences are aligned for optimal matching of their respective amino acid or nucleotide (the “matched span”, as determined by the algorithm). A gap opening penalty (which is calculated as 3× the average diagonal, wherein the “average diagonal” is the average of the diagonal of the comparison matrix being used; the “diagonal” is the score or number assigned to each perfect amino acid match by the particular comparison matrix) and a gap extension penalty (which is usually 1/10 times the gap opening penalty), as well as a comparison matrix such as PAM 250 or BLOSUM 62 are used in conjunction with the algorithm. In certain embodiments, a standard comparison matrix (see, Dayhoff et al., (1978) Atlas of Protein Sequence and Structure 5:345-352 for the PAM 250 comparison matrix; Henikoff et al., (1992) Proc. Natl. Acad. Sci. U.S.A. 89:10915-10919 for the BLOSUM 62 comparison matrix) is also used by the algorithm.

[0070] Recommended parameters for determining percent identity for polypeptides or nucleotide sequences using the GAP program are the following:

[0071] Algorithm: Needleman et al., 1970, J. Mol. Biol. 48:443-453;

[0072] Comparison matrix: BLOSUM 62 from Henikoff et al., 1992. supra;

[0073] Gap Penalty: 12 (but with no penalty for end gaps)

[0074] Gap Length Penalty: 4

[0075] Threshold of Similarity: 0

[0076] Certain alignment schemes for aligning two amino acid sequences can result in matching of only a short region of the two sequences, and this small aligned region can have very high sequence identity even though there is no significant relationship between the two full-length sequences. Accordingly, the selected alignment method (e.g., the GAP program) can be adjusted if so desired to result in an alignment that spans at least 50 contiguous amino acids of the target polypeptide.

[0077] As used herein, “substantially pure” means that the described species of molecule is the predominant species present, that is, on a molar basis it is more abundant than any other individual species in the same mixture. In certain embodiments, a substantially pure molecule is a composition wherein the object species comprises at least 50% (on a molar basis) of all macromolecular species present. In other embodiments, a substantially pure composition will comprise at least 80%, 85%, 90%, 95%, or 99% of all macromolecular species present in the composition. In other embodiments, the object species is purified to essential homogeneity wherein contaminating species cannot be detected in the composition by conventional detection methods and thus the composition consists of a single detectable macromolecular species.

[0078] The terms “treat” and “treating” refer to any indicia of success in the treatment or amelioration of an injury, pathology or condition, including any objective or subjective parameter such as abatement; remission; diminishing of symptoms or making the injury, pathology or condition more tolerable to the patient; slowing in the rate of degeneration or decline; making the final point of degeneration less debilitating, improving a patient's physical or mental well-being. The treatment or amelioration of symptoms can be based on objective or subjective parameters; including the results of a physical examination, neuropsychiatric exams, and/or a psychiatric evaluation. For example, certain methods presented herein can be employed to treat dyslipidemia, either prophylactically or as an acute treatment, to decrease circulating cholesterol levels and/or ameliorate a symptom associated with primary hyperlipidemia (heterozygous familial and non-familial), mixed dyslipidemia, and homozygous familial hypercholesterolemia.

[0079] An “effective amount” is generally an amount sufficient to reduce the severity and/or frequency of symptoms, eliminate the symptoms and/or underlying cause, prevent the occurrence of symptoms and/or their underlying cause, and/or improve or remediate the damage that results from or is associated with diabetes, obesity and dyslipidemia. In some embodiments, the effective amount is a therapeutically effective amount or a prophylactically effective amount. A “therapeutically effective amount” is an amount sufficient to remedy a disease state (e.g., diabetes, obesity or dyslipidemia) or symptoms, particularly a state or symptoms associated with the disease state, or otherwise prevent, hinder, retard or reverse the progression of the disease state or any other undesirable symptom associated with the disease in any way whatsoever. A “prophylactically effective amount” is an amount of a pharmaceutical composition that, when administered to a subject, will have the intended prophylactic effect, e.g., preventing or delaying the onset (or reoccurrence) of diabetes, obesity or dyslipidemia, or reducing the likelihood of the onset (or reoccurrence) of diabetes, obesity or dyslipidemia or associated symptoms. The full therapeutic or prophylactic effect does not necessarily occur by administration of one dose, and may occur only after administration of a series of doses. Thus, a therapeutically or prophylactically effective amount can be administered in one or more administrations.

[0080] “Amino acid” takes its normal meaning in the art. The twenty naturally-occurring amino acids and their abbreviations follow conventional usage. See, Immunology-A Synthesis, 2^nd Edition, (E. S. Golub and D. R. Green, eds.), Sinauer Associates: Sunderland, Mass. (1991), incorporated herein by reference for any purpose. Stereoisomers (e.g., D-amino acids) of the twenty conventional amino acids, unnatural or non-naturally occurring or encoded amino acids such as α-,α-disubstituted amino acids, N-alkyl amino acids, and other unconventional amino acids can also be suitable components for polypeptides and are included in the phrase “amino acid.” Examples of non-natural and non-naturally encoded amino acids (which can be substituted for any naturally-occurring amino acid found in any sequence disclosed herein, as desired) include: 4-hydroxyproline, γ-carboxyglutamate, ε-N,N,N-trimethyllysine, ε-N-acetyllysine, O-phosphoserine, N-acetylserine, N-formylmethionine, 3-methylhistidine, 5-hydroxylysine, σ-N-methylarginine, and other similar amino acids and imino acids (e.g., 4-hydroxyproline). In the polypeptide notation used herein, the left-hand direction is the amino terminal direction and the right-hand direction is the carboxyl-terminal direction, in accordance with standard usage and convention. A non-limiting lists of examples of non-naturally occurring/encoded amino acids that can be inserted into an antigen binding protein sequence or substituted for a wild-type residue in an antigen binding sequence include β-amino acids, homoamino acids, cyclic amino acids and amino acids with derivatized side chains. Examples include (in the L-form or D-form; abbreviated as in parentheses): citrulline (Cit), homocitrulline (hCit), Nα-methylcitrulline (NMeCit), Nα-methylhomocitrulline (Nα-MeHoCit), ornithine (Orm), Nα-Methylornithine (Nα-MeOrn or NMeOrn), sarcosine (Sar), homolysine (hLys or hK), homoarginine (hArg or hR), homoglutamine (hQ), Nα-methylarginine (NMeR), Nα-methylleucine (Nα-MeL or NMeL), N-methylhomolysine (NMeHoK), Nα-methylglutamine (NMeQ), norleucine (Nle), norvaline (Nva), 1,2,3,4-tetrahydroisoquinoline (Tic), Octahydroindole-2-carboxylic acid (Oic), 3-(1-naphthyl)alanine (1-Nal), 3-(2-naphthyl)alanine (2-Nal), 1,2,3,4-tetrahydroisoquinoline (Tic), 2-indanylglycine (IgI), para-iodophenylalanine (pI-Phe), para-aminophenylalanine (4AmP or 4-Amino-Phe), 4-guanidino phenylalanine (Guf), glycyllysine (abbreviated “K(Nε-glycyl)” or “K(glycyl)” or “K(gly)”), nitrophenylalanine (nitrophe), aminophenylalanine (aminophe or Amino-Phe), benzylphenylalanine (benzylphe), γ-carboxyglutamic acid (γ-carboxyglu), hydroxyproline (hydroxypro), p-carboxyl-phenylalanine (Cpa), α-aminoadipic acid (Aad), Nα-methyl valine (NMeVal), N-α-methyl leucine (NMeLeu), Nα-methylnorleucine (NMeNle), cyclopentylglycine (Cpg), cyclohexylglycine (Chg), acetylarginine (acetylarg), α, β-diaminopropionoic acid (Dpr), α,γ-diaminobutyric acid (Dab), diaminopropionic acid (Dap), cyclohexylalanine (Cha), 4-methyl-phenylalanine (MePhe), β,β-diphenyl-alanine (BiPhA), aminobutyric acid (Abu), 4-phenyl-phenylalanine (or biphenylalanine; 4Bip), α-amino-isobutyric acid (Aib), beta-alanine, beta-aminopropionic acid, piperidinic acid, aminocaprioic acid, aminoheptanoic acid, aminopimelic acid, desmosine, diaminopimelic acid, N-ethylglycine, N-ethylaspargine, hydroxylysine, allo-hydroxylysine, isodesmosine, allo-isoleucine, N-methylglycine, N-methylisoleucine, N-methylvaline, 4-hydroxyproline (Hyp), γ-carboxyglutamate, ε-N,N,N-trimethyllysine, ε-N-acetyllysine, O-phosphoserine, N-acetylserine, N-formylmethionine, 3-methylhistidine, 5-hydroxylysine, ω-methylarginine, 4-Amino-O-Phthalic Acid (4APA), and other similar amino acids, and derivatized forms of any of those specifically listed.

[0081] Antigen-binding proteins that bind to PCSK9 with extended in vivo half livers are provided herein. In some embodiments, the antigen binding proteins of the invention having extended half lives are pH sensitive binders. In some embodiments the pH sensitive binders are engineered to be more pH sensitive than a starting antibody, for example, by mutating one or more residue to a histidian in one or more CDR in the heavy or light chain or both. In some embodiments, the antigen binding proteins of the invention having extended half lives comprise mutations in their constant domains. In some embodiments, the antigen binding proteins of the invention having extended half lives are pH sensitive binders and comprise mutations in their constant domains.

[0082] In some embodiments of the present disclosure the antigen binding proteins provided can comprise polypeptides into which one or more complementary determining regions (CDRs) can be embedded and/or joined. In such antigen binding proteins, the CDRs can be embedded into a “framework” region, which orients the CDR(s) such that the proper antigen binding properties of the CDR(s) is achieved. In general, such antigen binding proteins that are provided inhibit the binding of PCSK9 to the LDLR, Accordingly, the antigen binding proteins provided herein and offer potential therapeutic benefit for the range of conditions which hypercholesterolemia, primary hyperlipidemia (heterozygous familial and non-familial), mixed dyslipidemia, homozygous familial hypercholesterolemia, cardiovascular disease, and broadly any disease or condition in which it is desirable to inhibit in vivo the binding of PCSK9 to LDLR.

[0083] Certain antigen binding proteins described herein are antibodies or are derived from antibodies. In certain embodiments, the polypeptide structure of the antigen binding proteins is based on antibodies, including, but not limited to, monoclonal antibodies, bispecific antibodies, minibodies, domain antibodies, synthetic antibodies (sometimes referred to herein as “antibody mimetics”), chimeric antibodies, humanized antibodies, human antibodies, antibody fusions (sometimes referred to herein as “antibody conjugates”), hemibodies and fragments thereof. The various structures are further described herein below.

[0084] The antigen binding proteins provided herein have been demonstrated to bind PCSK9 (e.g., human PCSK9). The antigen binding proteins that specifically bind to PCSK9 that are disclosed herein have a variety of utilities. Some of the antigen binding proteins, for instance, are useful in specific binding assays, in the affinity purification of PCSK9, including the human PCSK9, and in screening assays to identify other inhibitors of PCSK9 binding to LDLR.

[0085] The antigen binding proteins that specifically bind to PCSK9 that are disclosed herein can be used in a variety of treatment applications, as explained herein. For example, certain antigen binding proteins are useful for treating conditions associated with elevated cholesterol levels in a patient, such as reducing, alleviating, or treating dyslipidemia and cardiovascular disease. Other uses for the antigen binding proteins include, for example, diagnosis of diseases or conditions associated with PCSK9 and screening assays to determine the presence or absence of PCSK9. Some of the antigen binding proteins described herein can be useful in treating conditions, symptoms and/or the pathology associated with increased cholesterol levels. Exemplary conditions include, but are not limited to, dyslipidemia and cardiovascular disease.

[0086] The antigen binding proteins disclosed herein inhibit the binding of PCSK9 to LDLR as defined herein. In vivo, the mature form of PCSK9 is the active form of the molecule. The nucleotide sequence encoding full length human PCSK9 is provided; the nucleotides encoding the pro-domain sequence are underlined.

Accession number NM_174936
(SEQ ID NO: 1)
ATGGGCACCG TCAGCTCCAG GCGGTCCTGG TGGCCGCTGC CACTGCTGCT GCTGCTGCTG	60
CTGCTCCTGG GTCCCGCGGG CGCCCGTGCG CAGGAGGACG AGGACGGCGA CTACGAGGAG	120
CTGGTGCTAG CCTTGCGCTC CGAGGAGGAC GGCCTGGCCG AAGCACCCGA GCACGGAACC	180
ACAGCCACCT TCCACCGCTG CGCCAAGGAT CCGTGGAGGT TGCCTGGCAC CTACGTGGTG	240
GTGCTGAAGG AGGAGACCCA CCTCTCGCAG TCAGAGCGCA CTGCCCGCCG CCTGCAGGCC	300
CAGGCTGCCC GCCGGGGATA CCTCACCAAG ATCCTGCATG TCTTCCATGG CCTTCTTCCT	360
GGCTTCCTGG TGAAGATGAG TGGCGACCTG CTGGAGCTGG CCTTGAAGTT GCCCCATGTC	420
GACTACATCG AGGAGGACTC CTCTGTCTTT GCCCAGAGCA TCCCGTGGAA CCTGGAGCGG	480
ATTACCCCTC CGCGGTACCG GGCGGATGAA TACCAGCCCC CCGACGGAGG CAGCCTGGTG	540
GAGGTGTATC TCCTAGACAC CAGCATACAG AGTGACCACC GGGAAATCGA GGGCAGGGTC	600
ATGGTCACCG ACTTCGAGAA TGTGCCCGAG GAGGACGGGA CCCGCTTCCA CAGACAGGCC	660
AGCAAGTGTG ACAGTCATGG CACCCACCTG GCAGGGGTGG TCAGCGGCCG GGATGCCGGC	720
GTGGCCAAGG GTGCCAGCAT GCGCAGCCTG CGCGTGCTCA ACTGCCAAGG GAAGGGCACG	780
GTTAGCGGCA CCCTCATAGG CCTGGAGTTT ATTCGGAAAA GCCAGCTGGT CCAGCCTGTG	840
GGGCCACTGG TGGTGCTGCT GCCCCTGGCG GGTGGGTACA GCCGCGTCCT CAACGCCGCC	900
TGCCAGCGCC TGGCGAGGGC TGGGGTCGTG CTGGTCACCG CTGCCGGCAA CTTCCGGGAC	960
GATGCCTGCC TCTACTCCCC AGCCTCAGCT CCCGAGGTCA TCACAGTTGG GGCCACCAAT	1020
GCCCAGGACC AGCCGGTGAC CCTGGGGACT TTGGGGACCA ACTTTGGCCG CTGTGTGGAC	1080
CTCTTTGCCC CAGGGGAGGA CATCATTGGT GCCTCCAGCG ACTGCAGCAC CTGCTTTGTG	1140
TCACAGAGTG GGACATCACA GGCTGCTGCC CACGTGGCTG GCATTGCAGC CATGATGCTG	1200
TCTGCCGAGC CGGAGCTCAC CCTGGCCGAG TTGAGGCAGA GACTGATCCA CTTCTCTGCC	1260
AAAGATGTCA TCAATGAGGC CTGGTTCCCT GAGGACCAGC GGGTACTGAC CCCCAACCTG	1320
GTGGCCGCCC TGCCCCCCAG CACCCATGGG GCAGGTTGGC AGCTGTTTTG CAGGACTGTG	1380
TGGTCAGCAC ACTCGGGGCC TACACGGATG GCCACAGCCA TCGCCCGCTG CGCCCCAGAT	1440
GAGGAGCTGC TGAGCTGCTC CAGTTTCTCC AGGAGTGGGA AGCGGCGGGG CGAGCGCATG	1500
GAGGCCCAAG GGGGCAAGCT GGTCTGCCGG GCCCACAACG CTTTTGGGGG TGAGGGTGTC	1560
TACGCCATTG CCAGGTGCTG CCTGCTACCC CAGGCCAACT GCAGCGTCCA CACAGCTCCA	1620
CCAGCTGAGG CCAGCATGGG GACCCGTGTC CACTGCCACC AACAGGGCCA CGTCCTCACA	1680
GGCTGCAGCT CCCACTGGGA GGTGGAGGAC CTTGGCACCC ACAAGCCGCC TGTGCTGAGG	1740
CCACGAGGTC AGCCCAACCA GTGCGTGGGC CACAGGGAGG CCAGCATCCA CGCTTCCTGC	1800
TGCCATGCCC CAGGTCTGGA ATGCAAAGTC AAGGAGCATG GAATCCCGGC CCCTCAGGGG	1860
CAGGTGACCG TGGCCTGCGA GGAGGGCTGG ACCCTGACTG GCTGCAGCGC CCTCCCTGGG	1920
ACCTCCCACG TCCTGGGGGC CTACGCCGTA GACAACACGT GTGTAGTCAG GAGCCGGGAC	1980
GTCAGCACTA CAGGCAGCAC CAGCGAAGAG GCCGTGACAG CCGTTGCCAT CTGCTGCCGG	2040
AGCCGGCACC TGGCGCAGGC CTCCCAGGAG CTCCAG	2076

[0087] The amino acid sequence of full length human PCSK9 is provided; the amino acids that make up the pro-domain sequence are underlined:

Accession number NM_777596

(SEQ ID NO: 2)

MGTVSSRRSWWPLPLLLLLLLLLGPAGARA

QEDEDGDYEELVLALRSEEDGLAEAPEHGTTATFHRCAKDPWRLPGTYV

VVLKEETHLSOSERTARRLQAQAARRGYLTKILHVFHGLLPGFLVKMSGD

LLELALKLPHVDYIEEDSSVFAQSIPWNLERITPPRYRADEYQPPDGGSL

VEVYLLDTSIQSDHREIEGRVMVTDFENVPEEDGTRFHRQASKCDSHGTH

LAGVVSGRDAGVAKGASMRSLRVLNCQGKGTVSGTLIGLEFIRKSQLVQ

PVGPLVVLLPLAGGYSRVLNAACQRLARAGVVLVTAAGNFRDDACLYS

PASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSD

CSTCFVSQSGTSQAAAHVAGIAAMMLSAEPELTLAELRQRLIHFSAKD

VINEAWFPEDQRVLTPNLVAALPPSTHGAGWQLFCRTVWSAHSGPTRM

ATAIARCAPDEELLSCSSFSRSGKRRGERMEAQGGKLVCRAHNAFGGE

GVYAIARCCLLPQANCSVHTAPPAEASMGTRVHCHQQGHVLTGCSSHW

EVEDLGTHKPPVLRPRGQPNQCNGHREASIHASCCHAPGLECKVKEH

GIPAPQGQVTVACEEGWTLTGCSALPGTSHVLGAYAVDNTCVVRSRDV

STTGSTSEEAVTAVAICCRSRHLAQASQELQ

The nucleotide sequence encoding full length cynomolgus PCSK9 is provided; the nucleotides encoding the pro-domain sequence are underlined.

(SEQ ID NO: 3)

ATGGGTACCGTCAGCTCCAGGCGGTCCTGGTGGCCTCTGCCGCTGCCACT

GCTGCTGCTCCTGCTCCTGGGTCCCGCTGGCGCCCGTGCGCAGGAGGACG

AGGACGGCGACTACGAGGAGCTGGTGCTAGCCTTGCGTTCCGAGGAGGAC

GGCCTGGCCGACGCACCCGAGCACGGAGCCACAGCCACCTTCCACCGCTG

CGCCAAGGATCCGTGGAGGTTGCCCGGCACCTACGTGGTGGTGCTGAAGG

AGGAGACCCACCGCTCGCAGTCAGAGCGCACTGCCCGCCGCCTGCAGGCC

CAAGCTGCCCGCCGGGGATACCTCACCAAGATCCTGCATGTCTTCCATCA

CCTTCTTCCTGGCTTCCTGGTGAAGATGAGTGGCGACCTGCTGGAGCTGG

CCCTGAAGTTGCCCCATGTCGACTACATCGAGGAGGACTCCTCTGTCTTC

GCCCAGAGCATCCCATGGAACCTGGAGCGAATTACTCCTGCACGGTACCG

GGCGGATGAATACCAGCCCCCCAAAGGAGGCAGCCTGGTGGAGGTGTATC

TCCTAGACACCAGCATACAGAGTGACCACCGGGAAATCGAGGGCAGGGTC

ATGGTCACCGACTTCGAGAGTGTGCCCGAGGAGGACGGGACCCGCTTCCA

CAGACAGGCCAGCAAGTGTGACAGCCATGGCACCCACCTGGCAGGGGTGG

TCAGCGGCCGGGATGCCGGCGTGGCCAAGGGCGCCGGCCTGCGTAGCCTG

CGCGTGCTCAACTGCCAAGGGAAGGGCACGGTCAGCGGCACCCTCATAGG

CCTGGAGTTTATTCGGAAAAGCCAGCTGGTCCAGCCCGTGGGGCCACTGG

TTGTGCTGCTGCCCGTGGCGGGTGGGTACAGCCGGGTCTTCAACGCCGCC

TGCCAGCGCCTGGCGAGGGCTGGGGTCGTGCTGGTCACCGCTGCCGGCAA

CTTCCGGGACGATGCCTGCCTCTACTCTCCAGCCTCGGCTCCCGAGGTCA

TCACAGTTGGGGCCACCAATGCCCAGGACCAGCCGGTGACCCTGGGGACT

TTGGGGACCAACTTTGGCCGCTGTGTGGACCTCTTTGCCCCAGGGGAGGA

CATCATTGGTGCCTCCAGCGACTGCAGCACCTGCTTTGTGTCACGGAGTG

GGACATCGCAGGCTGCTGCCCACGTGGCTGGCATTGCAGCCATGATGCTG

TCTGCCGAGCCGGAGCTCACTCTGGCCGAGTTGAGGCAGAGACTGATCCA

CTTCTCTGCCAAAGATGTCATCAATGAGGCCTGGTTCCCTGAGGACCAGC

GGGTACTGACCCCCAACCTGGTGGCCGCCCTGCCCCCCAGCACCCACAGG

GCAGGTTGGCAGCTGTTTTGCAGGACTGTGTGGTCAGCACACTCGGGTCC

TACACGGATGGCCACAGCCGTAGCCCGCTGCGCCCAGGATGAGGAGCTGC

TGAGCTGCTCCAGTTTCTCCAGGAGTGGGAAGCGGCGGGGCGAGCGCATC

GAGGCCCAAGGGGGCAAGCGGGTCTGCCGGGCCCACAACGCTTTTGGGGG

TGAGGGTGTCTACGCCATTGCCAGGTGCTGCCTGCTACCCCAGGTCAACT

GCAGCGTCCACACAGCTCCACCAGCTGGGGCCAGCATGGGGACCCGTGTC

CACTGCCATCAGCAGGGCCACGTCCTCACAGGCTGCAGCTCCCACTGGGA

GGTGGAGGACCTTGGCACCCACAAGCCGCCTGTGCTGAGGCCACGAGGTC

AGCCCAACCAGTGTGTGGGCCACAGGGAGGCCAGCATCCACGCTTCCTGC

TGCCATGCCCCAGGTCTGGAATGCAAAGTCAGGGAGCATGGAATCCCGGC

CCCTCAGGAGCAGGTTATCGTGGCCTGTGAGGACGGCTGGACCCTGACCG

GCTGCAGTGCCCTCCCTGGGACCTCCCATGTCCTGGGGGCCTACGCTGTA

GACAACACGTGTGTGGTCAGGAGCCGGGACGTCAGCACCACAGGCAGCAC

CAGCGAAGAAGCCGTGGCAGCCGTTGCCATCTGCTGCCGGAGCCGGCACC

TGGTGCAGGCCTCCCAGGAGCTCCAG

[0088] The amino acid sequence of full length cynomolgous PCSK9 is provided; the amino acids that make up the pro-domain sequence are underlined:

(SEQ ID NO: 4)

MGTVSSRRSWWPLPLPLLLLLLLGPAGARA

QEDEDGDYEELVLALRSEEDGLADAPEHGATATFHRCAKDPWRLPGTYV

VVLKEETHRSQSERTARRLQAQAARRGYLTKILHVFHHLLPGFLVKMSG

DLLELALKLPHVDYIEEDSSVFAQSIPWNLERITPARYRADEYQPPKGG

SLVEVYLLDTSIQSDHREIEGRVMVTDFESVPEEDGTRFHRQASKCDSH

GTHLAGVVSGRDAGVAKGAGLRSLRVLNCQGKGTVSGTLIGLEFIRKSQ

LVQPVGPLVVLLPLAGGYSRVFNAACQRLARAGVVLVTAAGNFRDDACL

YSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASS

DCSTCFVSRSGTSQAAAHVAGIAAMMLSAEPELTLAELRQRLIHFSAKD

VINEAWFPEDQRVLTPNLVAALPPSTHRAGWQLFCRTVWSAHSGPTRMA

TAVARCAQDEELLSCSSFSRSGKLRRGERIEAQGGKRVCRAHNAFGGEG

VYAIARCCLLPQVNCSVHTAPPAGASMGTRVHCHQQGHVLTGCSSHWEV

EDLGTHKPPVLRPRGQPNQCVGHREASIHASCCHAPGLECKVREHGIPA

PQEQVIVACEDGWTLTGCSALPGTSHVLGAYAVDNTCVVRSRDVSTTGS

TSEEAVAAVAICCRSRHLVQASQELQ

[0089] As described herein, PCSK9 proteins can also include fragments. The term PCSK9 also includes post-translational modifications of the PCSK9 amino acid sequence, for example, possible N-linked glycosylation sites. Thus, the antigen binding proteins can bind to or be generated from proteins glycosylated at one or more position.

Antigen Binding Proteins that Specifically Bind to PCSK9

[0090] A variety of selective binding agents useful for inhibiting PCSK9 binding to LDLR are provided. These agents include, for instance, antigen binding proteins that contain an antigen binding domain (e.g., single chain antibodies, domain antibodies, hemibodies, immunoadhesions, and polypeptides with an antigen binding region) and specifically bind to PCSK9, in particular a human PCSK9.

[0091] In general, the antigen binding proteins that are provided typically comprise one or more CDRs as described herein (e.g., 1, 2, 3, 4, 5 or 6 CDRs). In some embodiments the antigen binding proteins are naturally expressed by clones, while in other embodiments, the antigen binding protein can comprise (a) a polypeptide framework structure and (b) one or more CDRs that are inserted into and/or joined to the polypeptide framework structure. In some of these embodiments a CDR forms a component of a heavy or light chains expressed by the clones described herein; in other embodiments a CDR can be inserted into a framework in which the CDR is not naturally expressed. A polypeptide framework structure can take a variety of different forms. For example, a polypeptide framework structure can be, or comprise, the framework of a naturally occurring antibody, or fragment or variant thereof, or it can be completely synthetic in nature. Examples of various antigen binding protein structures are further described below.

[0092] In some embodiments in which the antigen binding protein comprises (a) a polypeptide framework structure and (b) one or more CDRs that are inserted into and/or joined to the polypeptide framework structure, the polypeptide framework structure of an antigen binding protein is an antibody or is derived from an antibody, including, but not limited to, monoclonal antibodies, bispecific antibodies, minibodies, domain antibodies, synthetic antibodies (sometimes referred to herein as “antibody mimetics”), chimeric antibodies, humanized antibodies, antibody fusions (sometimes referred to as “antibody conjugates”), and portions or fragments of each, respectively. In some instances, the antigen binding protein is an immunological fragment of an antibody (e.g., a Fab, a Fab′, a F(ab′)₂, or a scFv).

[0093] Certain of the antigen binding proteins as provided herein specifically bind to PCSK9, including the human form of this protein. In one embodiment, an antigen binding protein specifically binds human self-cleaved, mature, secreted PCSK9 comprising amino acids 31 to 692 of the amino acid sequence of SEQ ID NO: 2 and inhibits PCSK9 from binding to LDLR. FIG. 1 is a conceptual depiction of how in some embodiments, the antigen binding proteins of the invention bind to human self-cleaved, mature, secreted PCSK9.

[0094] Some of the antigen binding proteins that specifically bind PCSK9, including the human form provided herein have a structure typically associated with naturally occurring antibodies. The structural units of these antibodies typically comprise one or more tetramers, each composed of two identical couplets of polypeptide chains, though some species of mammals also produce antibodies having only a single heavy chain. In a typical antibody, each pair or couplet includes one full-length “light” chain (in certain embodiments, about 25 kDa) and one full-length “heavy” chain (in certain embodiments, about 50-70 kDa). Each individual immunoglobulin chain is composed of several “immunoglobulin domains,” each consisting of roughly 90 to 110 amino acids and expressing a characteristic folding pattern. These domains are the basic units of which antibody polypeptides are composed. The amino-terminal portion of each chain typically includes a variable domain that is responsible for antigen recognition. The carboxy-terminal portion is more conserved evolutionarily than the other end of the chain and is referred to as the “constant region” or “C region”. Human light chains generally are classified as kappa (“κ”) and lambda (“λ”) light chains, and each of these contains one variable domain and one constant domain. Heavy chains are typically classified as mu, delta, gamma, alpha, or epsilon chains, and these define the antibody's isotype as IgM, IgD, IgG, IgA, and IgE, respectively. IgG has several subtypes, including, but not limited to, IgG1, IgG2, IgG3, and IgG4. IgM subtypes include IgM, and IgM2. IgA subtypes include IgA1 and IgA2. In humans, the IgA and IgD isotypes contain four heavy chains and four light chains; the IgG and IgE isotypes contain two heavy chains and two light chains; and the IgM isotype contains five heavy chains and five light chains. The heavy chain C region typically comprises one or more domains that can be responsible for effector function. The number of heavy chain constant region domains will depend on the isotype. IgG heavy chains, for example, each contain three C region domains known as C_H1, C_H2 and C_H3. The antibodies that are provided can have any of these isotypes and subtypes. In certain embodiments, an antigen binding protein that specifically binds to PCSK9.

[0095] In full-length light and heavy chains, the variable and constant regions are joined by a “J” region of about twelve or more amino acids, with the heavy chain also including a “D” region of about ten more amino acids. See, e.g., Fundamental Immunology, 2nd ed., Ch. 7 (Paul, W., ed.) 1989, New York: Raven Press (hereby incorporated by reference in its entirety for all purposes). The variable regions of each light/heavy chain pair typically form the antigen binding site.

[0096] One example of an IgG2 heavy constant domain of an exemplary monoclonal antibody that specifically binds to PCSK9 has the amino acid sequence:

(SEQ ID NO: 5)

ASTKGPSVFPLAPCSRSTSESTAALGCLVKDYFPEPVTVSWNSGALTSGV

HTFPAVLQSSGLYSLSSVVTVPSSNFGTQTYTCNVDHKPSNTKVDKTVE

RKCCVECPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHE

DPEVQFNWYVDGVEVHNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKE

YKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTC

LVKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGSFFLYSKLTVDKSR

WQQGNVFSCSVMHEALHNHYTQKSLSLSPGK.

[0097] One example of a kappa light constant domain of an exemplary monoclonal antibody that binds to a PCSK9 has the amino acid sequence:

(SEQ ID NO: 6)

RTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQ

SGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSS

PVTKSFNRGEC.

[0098] One example of a lambda light constant domain of an exemplary monoclonal antibody that binds to PCSK9 has the amino acid sequence:

(SEQ ID NO: 7)

QPKANPTVTLFPPSSEELQANKATLVCLISDFYPGAVTV

AWKADGSPVKAGVETTKPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVT

HEGSTVEKTVAPTECS.

[0099] Variable regions of immunoglobulin chains generally exhibit the same overall structure, comprising relatively conserved framework regions (FR) joined by three hypervariable regions, more often called “complementarity determining regions” or CDRs. The CDRs from the two chains of each heavy chain/light chain pair mentioned above typically are aligned by the framework regions to form a structure that binds specifically with a specific epitope on the target protein (e.g., PCSK9). From N-terminal to C-terminal, naturally-occurring light and heavy chain variable regions both typically conform with the following order of these elements: FR1, CDR1, FR2, CDR2, FR3, CDR3 and FR4. A numbering system has been devised for assigning numbers to amino acids that occupy positions in each of these domains. This numbering system is defined in Kabat et al., (1991) “Sequences of Proteins of Immunological Interest”, 5^th Ed., US Dept. of Health and Human Services, PHS, NIH, NIH Publication no. 91-3242. Although presented using the Kabat nomenclature system, as desired, the CDRs disclosed herein can also be redefined according an alternative nomenclature scheme, such as that of Chothia (see Chothia & Lesk, (1987) J. Mol. Biol. 196:901-917; Chothia et al., (1989) Nature 342:878-883 or Honegger & Pluckthun, (2001) J. Mol. Biol. 309:657-670).

[0100] The various heavy chain and light chain variable regions of antigen binding proteins provided herein are depicted in Table 2. Each of these variable regions can be attached to the disclosed heavy and light chain constant regions to form a complete antibody heavy and light chain, respectively. Further, each of the so-generated heavy and light chain sequences can be combined to form a complete antibody structure. It should be understood that the heavy chain and light chain variable regions provided herein can also be attached to other constant domains having different sequences than the exemplary sequences listed above.

[0101] Specific examples of some of the full length light and heavy chains of the antibodies that are provided and their corresponding amino acid sequences are summarized in Tables 1A and 1B. Table 1A shows exemplary light chain sequences, and Table 1B shows exemplary heavy chain sequences.

TABLE 1A
Exemplary Antibody Light ChainSequences
	SEQ
	ID
Ab ID	NO:	Amino AcidSequence
SS-13406	8	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
(8A3HLE-51)		PVTPGEPASISCRSSQSLLHSNGYNYLDWYLQKP
		GQSPQLLIYLGSNRASGVPDRFSGSGSGTDFTLKI
		SRVEAEDVGVYYCMQALQTPLTFGGGTKVEIKR
		TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE
		AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
		STLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-13407	9	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
(8A3HLE-		PVTPGEPASISCRSSQSLLHSNGYNYLDWYLQKP
112)		GQSPQLLIYLGSNRASGVPDRFSGSGSGTDFTLKI
		SRVEAEDVGVYYCMQALQTPLTFGGGTKVEIKR
		TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE
		AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
		STLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-14888	10	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
(P2C6-		PVTPGEPASISCRSSQSLLHSNGYNYLDWYLQKP
HLE51)		GQSPQLLIYLGLNRASGVPDRFSGSGSGTDFTLKI
		SRVEAEDVGVYYCMQALQTPLTFGGGTKVEIKR
		TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE
		AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
		STLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
13G9	11	QSVLTQPPSVSGAPGQRVTISCTGSRSNIGAGYD
		VNWYQQLPGTAPKLLIYGNSNRPSGVPDRFSGS
		KSGTSASLVITGLQAEDEADYYCQSYDSNLSGSV
		FGGGTKLTVLGQPKANPTVTLFPPSSEELQANKA
		TLVCLISDFYPGAVTVAWKADGSPVKAGVETTK
		PSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVT
		HEGSTVEKTVAPTECS
19A12	12	DIVLTQSPDFLAVSLGERATINCKSSQNVLYSSSN
		KNYLVWYQHKPGQPPKLLIYWASTRESGVPDRF
		SGSGSGTDFTLTISSLQAEDVAVYYCHQYYSTPW
		TFGQGTKVEIKRRTVAAPSVFIFPPSDEQLKSGTA
		SVVCLLNNFYPREAKVQWKVDNALQSGNSQES
		VTEQDSKDSTYSLSSTLTLSKADYEKHKVYACE
		VTHQGLSSPVTKSFNRGEC
20D12	13	QSVLTQPPSASGTPGQRVTISCSGSNSNIGSNTVN
		WYQQVPGTAPKLLIYSNNQRPSGVPDRFSGSKSG
		TSASLAISGLQSEDEADYYCAAWDDSLNGWVFG
		GGTKLTVLGQPKANPTVTLFPPSSEELQANKATL
		VCLISDFYPGAVTVAWKADGSPVKAGVETTKPS
		KQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHE
		GSTVEKTVAPTECS
25B5	14	QSALTQPASVSGSPGQSITISCTGTSSDVGGYNSV
		SWYQQHPGKPPKLMIYEVSNRPSGISNRFSGSKS
		GNTASLTISGLQAEDEADYFCSSYTSTSMVFGGG
		TKLAVLRQPKANPTVTLFPPSSEELQANKATLVC
		LISDFYPGAVTVAWKADGSPVKAGVETTKPSKQ
		SNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGS
		TVEKTVAPTECS
30G7	15	QSALTQPASVSGSPGQSITISCTGTSSDVGGYNSV
		SWYQQHPGKPPKLMIYEVSNRPSGVSNRFSGSKS
		ANTASLTISGLQADDEADYFCSSYTSTSMVFGGG
		TKLTVLRQPKANPTVTLFPPSSEELQANKATLVC
		LISDFYPGAVTVAWKADGSPVKAGVETTKPSKQ
		SNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGS
		TVEKTVAPTECS
SS-15057	16	MDMRVPAQLLGLLLLWLRGARCESVLTQPPSVS
		GAPGQRVTISCTGSSSNIGAGHDVHWYQQLPGT
		APKLLISGNSNRPSGVPDRFSGSKSGTSASLAITG
		LQAEDEADYYCQSYDSSLSGSVFGGGTKLTVLG
		QPKAAPSVILFPPSSEELQANKATLVCLISDFYPG
		AVTVAWKADSSPVKAGVETTTPSKQSNNKYAA
		SSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAP
		TECS
15058	17	MDMRVPAQLLGLLLLWLRGARCESVLTQPPSVS
		GAPGQRVTISCTGSSSNIGAGHDVHWYQQLPGT
		APKLLISGNSNRPSGVPDRFSGSKSGTSASLAITG
		LQAEDEADYYCQSYDSSLSGSVFGGGTKLTVLG
		QPKAAPSVTLFPPSSEELQANKATLVCLISDFYPG
		AVTVAWKADSSPVKAGVETTTPSKQSNNKYAA
		SSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAP
		TECS
15059	18	MDMRVPAQLLGLLLLWLRGARCESVLTQPPSVS
		GAPGQRVTISCTGSSSNIGAGHDVHWYQQLPGT
		APKLLISGNSNRPSGVPDRFSGSKSGTSASLAITG
		LQAEDEADYYCQSYDSSLSGSVFGGGTKLTVLG
		QPKAAPSVTLFPPSSEELQANKATLVCLISDFYPG
		AVTVAWKADSSPVKAGVETTTPSKQSNNKYAA
		SSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAP
		TECS
15065	19	MDMRVPAQLLGLLLLWLRGARCESVLTQPPSVS
		GAPGQRVTISCTGSSSNIGAGHDVHWYQQLPGT
		APKLLISGNSNRPSGVPDRFSGSKSGTSASLAITG
		LQAEDEADYYCQSYDSSLSGSVFGGGTKLTVLG
		QPKAAPSVTLFPPSSEELQANKATLVCLISDFYPG
		AVTVAWKADSSPVKAGVETTTPSKQSNNKYAA
		SSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAP
		TECS
15079	20	MDMRVPAQLLGLLLLWLRGARCESVLTQPPSVS
		GAPGQRVTISCTGSSSNIGAGYDVHWYQQLPGT
		APKLLISGNSNRPSGVPDRFSGSKSGTSASLAITG
		LQAEDEADYYCQSYDSSLHGSVFGGGTKLTVLG
		QPKAAPSVTLFPPSSEELQANKATLVCLISDFYPG
		AVTVAWKADSSPVKAGVETTTPSKQSNNKYAA
		SSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAP
		TECS
15080	21	MDMRVPAQLLGLLLLWLRGARCESVLTQPPSVS
		GAPGQRVTISCTGSSSNIGAGYDVHWYQQLPGT
		APKLLISGNSNRPSGVPDRFSGSKSGTSASLAITG
		LQAEDEADYYCQSYDSSLHGSVFGGGTKLTVLG
		QPKAAPSVTLFPPSSEELQANKATLVCLISDFYPG
		AVTVAWKADSSPVKAGVETTTPSKQSNNKYAA
		SSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAP
		TECS
15087	22	MDMRVPAQLLGLLLLWLRGARCESVLTQPPSVS
		GAPGQRVTISCTGSSSNIGAGYDVHWYQQLPGT
		APKLLISGNSNRPSGVPDRFSGSKSGTSASLAITG
		LQAEDEADYYCQSYDSSLHGSVFGGGTKLTVLG
		QPKAAPSVTLFPPSSEELQANKATLVCLISDFYPG
		AVTVAWKADSSPVKAGVETTTPSKQSNNKYAA
		SSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAP
		TECS
15101	23	MDMRVPAQLLGLLLLWLRGARCESVLTQPPSVS
		GAPGQRVTISCTGSSSNIGAGYDVHWYQQLPGT
		APKLLISGNSNRPSGVPDRFSGSKSGTSASLAITG
		LQAEDEADYYCQSYDSSLSGSVFGGGTKLTVLG
		QPKAAPSVTLFPPSSEELQANKATLVCLISDFYPG
		AVTVAWKADSSPVKAGVETTTPSKQSNNKYAA
		SSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAP
		TECS
15103	24	MDMRVPAQLLGLLLLWLRGARCESVLTQPPSVS
		GAPGQRVTISCTGSSSNIGAGYDVHWYQQLPGT
		APKLLISGNSNRPSGVPDRFSGSKSGTSASLAITG
		LQAEDEADYYCQSYDSSLSGSVFGGGTKLTVLG
		QPKAAPSVTLFPPSSEELQANKATLVCLISDFYPG
		AVTVAWKADSSPVKAGVETTTPSKQSNNKYAA
		SSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAP
		TECS
15104	25	MDMRVPAQLLGLLLLWLRGARCESVLTQPPSVS
		GAPGQRVTISCTGSSSNIGAGYDVHWYQQLPGT
		APKLLISGNSNRPSGVPDRESGSKSGTSASLAITG
		LQAEDEADYYCQSYDSSLSGSVFGGGTKLTVLG
		QPKAAPSVTLFPPSSEELQANKATLVCLISDFYPG
		AVTVAWKADSSPVKAGVETTTPSKQSNNKYAA
		SSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAP
		TECS
15105	26	MDMRVPAQLLGLLLLWLRGARCESVLTQPPSVS
		GAPGQRVTISCTGSSSNIGAGYDVHWYQQLPGT
		APKLLISGNSNRPSGVPDRFSGSKSGTSASLAITG
		LQAEDEADYYCQSYDSSLSGSVFGGGTKLTVLG
		QPKAAPSVTLFPPSSEELQANKATLCLISDFYPG
		AVTVAWKADSSPVKAGVETTTPSKQSNNKYAA
		SSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAP
		TECS
15106	27	MDMRVPAQLLGLLLLWLRGARCESVLTQPPSVS
		GAPGQRVTISCTGSSSNIGAGYDVHWYQQLPGT
		APKLLISGNSNRPSGVPDRFSGSKSGTSASLAITG
		LQAEDEADYYCQSYDSSLSGSVFGGGTKLTVLG
		QPKAAPSVTLFPPSSEELQANKATLVCLISDFYPG
		AVTVAWKADSSPVKAGVETTTPSKQSNNKYAA
		SSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAP
		TECS
15108	28	MDMRVPAQLLGLLLLWLRGARCESVLTQPPSVS
		GAPGQRVTISCTGSSSNIGAGYDVHWYQQLPGT
		APKLLISGNSNRPSGVPDRFSGSKSGTSASLAITG
		LQAEDEADYYCQSYDSSLSGSVFGGGTKLTVLG
		QPKAAPSVTLFPPSSEELQANKATLVCLISDFYPG
		AVTVAWKADSSPVKAGVETTTPSKQSNNKYAA
		SSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAP
		TECS
15112	29	MDMRVPAQLLGLLLLWLRGARCESVLTQPPSVS
		GAPGQRVTISCTGSSSNIGAGYDVHWYQQLPGT
		APKLLISGNSNRPSGVPDRFSGSKSGTSASLAITG
		LQAEDEADYYCQSYDSSLSGSVFGGGTKLTVLG
		QPKAAPSVTLFPPSSEELQANKATLVCLISDFYPG
		AVTVAWKADSSPVKAGVETTTPSKQSNNKYAA
		SSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAP
		TECS
15113	30	MDMRVPAQLLGLLLLWLRGARCESVLTQPPSVS
		GAPGQRVTISCTGSSSNIGAGYDVHWYQQLPGT
		APKLLISGNSNRPSGVPDRFSGSKSGTSASLAITG
		LQAEDEADYYCQSYDSSLSGSVFGGGTKLTVLG
		QPKAAPSVTLFPPSSEELQANKATLVCLISDFYPG
		AVTVAWKADSSTVKAGVETTTPSKQSNNKYAA
		SSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAP
		TECS
15114	31	MDMRVPAQLLGLLLLWLRGARCESVLTQPPSVS
		GAPGQRVTISCTGSSSNIGAGYDVHWYQQLPGT
		APKLLISGNSNRPSGVPDRFSGSKSGTSASLAITG
		LQAEDEADYYCQSYDSSLSGSVFGGGTKLTVLG
		QPKAAPSVTLFPPSSEELQANKATLVCLISDFYPG
		AVTVAWKADSSPVKAGVETTTPSKQSNNKYAA
		SSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAP
		TECS
15117	32	MDMRVPAQLLGLLLLWLRGARCESVLTQPP
		SVSGAPGQRVTISCTGSSSNIGAGYDVHWYQ
		QLPGTAPKLLISGNSNRPSGVPDRFSGSKSGT
		SASLASITGLQAEDEADYYCQSYDSSLSGSVF
		GGGTKLTVLGQPKAAPSVTLFPPSSEELQAN
		KATLVCLISDFYPGAVTVAWKADSSPVKAG
		VETTTPSKQSNNKYAASSYLSLTPEQWKSHR
		SYSCQVTHEGSTVEKTVAPTECS
15121	33	MDMRVPAQLLGLLLLWLRGARCESVLTQPPSVS
		GAPGQRVTISCTGSSSNIGAGYDVHWYQQLPGT
		APKLLISGNSNRPSGVPDRFSGSKSGTSASLAITG
		LQAEDEADYYCQSYDSSLSGSVFGGGTKLTVLG
		QPKAAPSVTLFPPSSEELQANKATLVCLISDFYPG
		AVTVAWKADSSPVKAGVETTTPSKQSNNKYAA
		SSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAP
		TECS
15123	34	MDMRVPAQLLGLLLLWLRGARCESVLTQPPSVS
		GAPGQRVTISCTGSSSNIGAGYDVHWYQQLPGT
		APKLLISGNSNRPSGVPDRFSGSKSGTSASLAITG
		LQAEDEADYYCQSYDSSLSGSVFGGGTKLTVLG
		QPKAAPSVTLFPPSSEELQANKATLVCLISDFYPG
		AVWAWKADSSPVKAGVETTTPSKQSNNKYAA
		SSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAP
		TECS
15124	35	MDMRVPAQLLGLLLLWLRGARCESVLTQPPSVS
		GAPGQRVTISCTGSSSNIGAGYDVHWYQQLPGT
		APKLLISGNSNRPSGVPDRFSGSKSGTSASLAITG
		LQAEDEADYYCQSYDSSLSGSVFGGGTKLTVLG
		QPKAAPSVTLFPPSSEELQANKATLVCLISDFYPG
		AVTVAWKADSSPVKAGVETTTPSKQSNNKYAA
		SSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAP
		TECS
15126	36	MDMRVPAQLLGLLLLWLRGARCESVLTQPPSVS
		GAPGQRVTISCTGSSSNIGAGYDVHWYQQLPGT
		APKLLISGNSNRPSGVPDRFSGSKSGTSASLAITG
		LQAEDEADYYCQSYDSSLSGSVFGGGTKLTVLG
		QPKAAPSVTLFPPSSEELQANKATLVCLISDFYPG
		AVTVAWKADSSPVKAGVETTTPSKQSNNKYAA
		SSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAP
		TECS
15132	37	MDMRVPAQLLGLLLLWLRGARCESVLTQPPSVS
		GAPGQRVTISCTGSSSNIGAGYDVHWYQQLPGT
		APKLLISGNSNRPSGVPDRFSGSKSGTSASLAITG
		LQAEDEADYYCQSYDSSLSGSVFGGGTKLTVLG
		QPKAAPSVTLFPPSSEELQANKATLVCLISDFYPG
		AVTVAWKADSSPVKAGVETTTPSKQSNNKYAA
		SSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAP
		TECS
15133	38	MDMRVPAQLLGLLLLWLRGARCESVLTQPPSVS
		GAPGQRVTISCTGSSSNIGAGYDVHWYQQLPGT
		APKLLISGNSNRPSGVPDRFSGSKSGTSASLAITG
		LQAEDEADYYCQSYDSSLSGSVFGGGTKLTVLG
		QPKAAPSVTLFPPSSEELQANKATLVCLISDFYPG
		AVTVAWKADSSPVKAGVETTTPSKQSNNKYAA
		SSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAP
		TECS
15136	39	MDMRVPAQLLGLLLLWLRGARCESVLTQPPSVS
		GAPGQRVTISCTGSSSNIGAGYDVHWYQQLPGT
		APKLLISGNSNRPSGVPDRFSGSKSGTSASLAITG
		LQAEDEADYYCQSYDSSLSGSVFGGGTKLTVLG
		QPKAAPSVTLFPPSSEELQANKATLVCLISDFYPG
		AVTVAWKADSSPVKAGVETTTPSKQSNNKYAA
		SSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAP
		TECS
15139	40	MDMRVPAQLLGLLLLWLRGARCESVLTQPPSVS
		GAPGQRVTISCTGSSSNIGAGYDVHWYQQLPGT
		APKLLISGNSNRPSGVPDRFSGSKSGTSASLAITG
		LQAEDEADYYCQSYDSSLSGSVFGGGTKLTVLG
		QPKAAPSVTLFPPSSEELQANKATLVCLISDFYPG
		AVTVAWKADSSPVKAGVETTTPSKQSNNKYAA
		SSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAP
		TECS
15140	41	MDMRVPAQLLGLLLLWLRGARCESVLTQPPSVS
		GAPGQRVTISCTGSSSNIGAGYDVHWYQQLPGT
		APKLLISGNSNRPSGVPDRFSGSKSGTSASLAITG
		LQAEDEADYYCQSYDSSLSGSVFGGGTKLTVLG
		QPKAAPSVTLFPPSSEELQANKATLVCLISDFYPG
		AVTVAWKADSSPVKAGVETTTPSKQSNNKYAA
		SSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAP
		TECS
15141	42	MDMRVPAQLLGLLLLWLRGARCESVLTQPPSVS
		GAPGQRVTISCTGSSSNIGAGYDVHWYQQLPGT
		APKLLISGNSNRPSGVPDRFSGSKSGTSASLAITG
		LQAEDEADYYCQSYDSSLSGSVFGGGTKLTVLG
		QPKAAPSVTLFPPSSEELQANKATLVCLISDFYPG
		AVTVAWKADSSPVKAGVETTTPSKQSNNKYAA
		SSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAP
		TECS
SS-13983	43	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
A01		PVTPGEPASISCRSSQSLLHSNGHNYLDWYLQKP
		GQSPQLLIYLGLNRASGVPDRFSGSGSGTDFTLKI
		SRVEAEDVGVYYCMQALQTPLTFGGGTKVEIKR
		TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE
		AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
		STLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-13991	44	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
A02		PVTPGEPASISCRSSQSLLHSNGHNYLDWYLQKP
		GQSPQLLIYLGLNRAHGVPDRFSGSGSGTDFTLKI
		SRVEAEDVGVYYCMQALQTPLTFGGGTKVEIKR
		TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE
		AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
		STLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-13993	45	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
C02		PVTPGEPASISCRSSQSLLHSNGHNYLDWYLQKP
		GQSPQLLIYLGLNRASGVPDRFSGSGHGTDFTLKI
		SRVEAEDVGVYYCMQALQTPLTFGGGTKVEIKR
		TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE
		AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
		STLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-12685	46	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
P1B1		PVTPGEPASISCRSSQSLLHSYGYNYLDWYLQKP
		GQSPQLLIYLGSNRASGVPDRFSGSGSGTDFTLKI
		SRVEAEDVGVYYCMQALQTPLTFGGGTKVEIKR
		TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE
		AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
		STLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-12686	47	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
P2F5		PVTPGEPASISCRSSQSLLHSFGYNYLDWYLQKP
		GQSPQLLIYLGSNRASGVPDRFSGSGSGTDFTLKI
		SRVEAEDVGVYYCMQALQTPLTFGGGTKVEIKR
		TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE
		AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
		STLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-12687	48	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
P2C6		PVTPGEPASISCRSSQSLLHSNGYNYLDWYLQKP
		GQSPQLLIYLGLNRASGVPDRFSGSGSGTDFTLKI
		SRVEAEDVGVYYCMQALQTPLTFGGGTKVEIKR
		TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE
		AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
		STLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-14892	49	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
P2F5/P2C6		PVTPGEPASISCRSSQSLLHSFGYNYLDWYLQKP
		GQSPQLLIYLGLNRASGVPDRFSGSGSGTDFTLKI
		SRVEAEDVGVYYCMQALQTPLTFGGGTKVEIKR
		TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE
		AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
		STLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-15509	50	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
		PVTPGEPASISCRSSQSLLHSFGYNYLDWYLQKP
		GQSPQLLIYLGMNRASGVPDRFSGSGSGTDFTLK
		ISRVEAEDVGVYYCMQALQTPLTFGGGTKVEIK
		RTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPR
		EAKVQWKVDNALQSGNSQESVTEQDSKDSTYSL
		SSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-15510	51	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
		PVTPGEPASISCRSSQSLLHSFGYNYLDWYLQKP
		GQSPQLLIYLGFNRASGVPDRFSGSGSGTDFTLKI
		SRVEAEDVGVYYCMQALQTPLTFGGGTKVEIKR
		TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE
		AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
		STLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
SS-15511	52	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
		PVTPGEPASISCRSSQSLLHSFGYNYLDWTYLQKP
		GQSPQLLIYLGHNRASGVPDRFSGSGSGTDFTLKI
		SRVEAEDVGVYYCMQALQTPLTFGGGTKVEIKR
		TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE
		AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
		STLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-15512	53	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
		PVTPGEPASISCRSSQSLLHSFGYNYLDWYLQKP
		GQSPQLLIYLGNNRASGVPDRFSGSGSGTDFTLKI
		SRVEAEDVGVYYCMQALQTPLTFGGGTKVEIKR
		TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE
		AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
		STLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-15513	54	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
		PVTPGEPASISCRSSQSLLHSFGYNYLDWYLQKP
		GQSPQLLIYLGWNRASGVPDRFSGSGSGTDFTLK
		ISRVEAEDVGVYYCMQALQTPLTFGGGTKVEIK
		RTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPR
		EAKVQWKVDNALQSGNSQESVTEQDSKDSTYSL
		SSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-15514	55	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
		PVTPGEPASISCRSSQSLLHSFGYNYLDWYLQKP
		GQSPQLLIYLGQNRASGVPDRFSGSGSGTDFTLKI
		SRVEAEDVGVYYCMQALQTPLTFGGGTKVEIKR
		TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE
		AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
		STLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-15497	56	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
		PVTPGEPASISCRSSQSLLHSGNGYNYLDWYLQK
		PGQSPQLLIYLGLNRASGVPDRFSGSGSGTDFTL
		KISRVEAEDVGVYYCMQAIHTPLTFGGGTKVEIK
		RTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPR
		EAKVQWKVDNALQSGNSQESVTEQDSKDSTYSL
		SSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-15515	57	MGSTAILGLLLAVLQGGRADIVMTQSPLSLPVTP
		GEPASISCRSSQSLLHSGNGYNYLDWYLQKPGQS
		PQLLIYLGMNRASGVPDRFSGSGSGTDFTLKISR
		VEAEDVGVYYCMQAIHTPLTFGGGTKVEIKRTV
		AAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAK
		VQWKVDNALQSGNSQESVTEQDSKDSTYSLSST
		LTLSKADYEKHKVYACEVTHQGLSSPVTKSFNR
		GEC
SS-15516	58	MGSTAILGLLLAVLQGGRADIVMTQSPLSLPVTP
		GEPASISCRSSQSLLHSGNGYNYLDWYLQKPGQS
		PQLLIYLGFNRASGVPDRFSGSGSGTDFTLKISRV
		EAEDVGVYYCMQAIHTPLTFGGGTKVEIKRTVA
		APSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKV
		QWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL
		TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRG
		EC
SS-15517	59	MGSTAILGLLLAVLQGGRADIVMTQSPLSLPVTP
		GEPASISCRSSQSLLHSGNGYNYLDWYLQKPGQS
		PQLLIYLGHNRASGVPDRFSGSGSGTDFTLKISRV
		EAEDVGVYYCMQAIHTPLTFGGGTKVEIKRTVA
		APSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKV
		QWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL
		TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRG
		EC
SS-15518	60	MGSTAILGLLLAVLQGGRADIVMTQSPLSLPVTP
		GEPASISCRSSQSLLHSGNGYNYLDWYLQKPGQS
		PQLLIYLGNNRASGVPDRFSGSGSGTDFTLKISRV
		EAEDVGVYYCMQAIHTPLTFGGGTKVEIKRTVA
		APSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKV
		QWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL
		TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRG
		EC
SS-15519	61	MGSTAILGLLLAVLQGGRADIVMTQSPLSLPVTP
		GEPASISCRSSQSLLHSGNGYNYLDWYLQKPGQS
		PQLLIYLGWNRASGVPDRFSGSGSGTDFTLKISR
		VEAEDVGVYYCMQAIHTPLTFGGGTKVEIKRTV
		AAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAK
		VQWKVDNALQSGNSQESVTEQDSKDSTYSLSST
		LTLSKADYEKHKVYACEVTHQGLSSPVTKSFNR
		GEC
SS-15520	62	MGSTAILGLLLAVLQGGRADIVMTQSPLSLPVTP
		GEPASISCRSSQSLLHSGNGYNYLDWYLQKPGQS
		PQLLIYLGQNRASGVPDRFSGSGSGTDFTLKISRV
		EAEDVGVYYCMQAIHTPLTFGGGTKVEIKRTVA
		APSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKV
		QWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL
		TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRG
		EC
SS-15522	63	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
		PVTPGEPASISCRSSQSLLHSNGYNYLDWYLQKP
		GQSPQLLIYLGLARASGVPDRFSGSGSGTDFTLKI
		SRVEAEDVGVYYCMQALQTPLTFGGGTKVEIKR
		TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE
		AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
		STLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-15524	64	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
		PVTPGEPASISCRSSQSLLHSNGYNYLDWYLQKP
		GQSPQLLIYLGLARASGVPDRFSGSGSGTDFTLKI
		SRVEAEDVGVYYCMQALQTPLTFGGGTKVEIKR
		TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE
		AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
		STLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-14835	65	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
		PVTPGEPASISCRSSQSLLHSGNGYNYLDWYLQK
		PGQSPQLLIYLGLNRASGVPDRFSGSGSGTDFTL
		KISRVEAEDVGVYYCMQAIHTPLTFGGGTKVEIK
		RTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPR
		EAKVQWKVDNALQSGNSQESVTEQDSKDSTYSL
		SSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-15194	66	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
		PVTPGEPASISCRSSQSLLHSNGHNYLDWYLQKP
		GQSPQLLIYLGLNRASGVPDRFSGSGSGTDFTLKI
		SRVEAEDVGVYYCMQALQTPLTFGGGTKVEIKR
		TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE
		AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
		STLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-15195	67	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
		PVTPGEPASISCRSSQSLLHSNGHNYLDWYLQKP
		GQSPQLLIYLGLNRAHGVPDRFSGSGSGTDFTLKI
		SRVEAEDVGVYYCMQALQTPLTFGGGTKVEIKR
		TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE
		AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
		STLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-15196	68	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
		PVTPGEPASISCRSSQSLLHSGNGYNYLDWYLQK
		PGQSPQLLIYLGLNRASGVPDRFSGSGSGTDFTL
		KISRVEAEDVGVYYCMQAIHTPLTFGGGTKVEIK
		RTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPR
		EAKVQWKVDNALQSGNSQESVTEQDSKDSTYSL
		SSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-14894	69	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
		PVTPGEPASISCRSSQSLLHSGNGYNYLDWYLQK
		PGQSPQLLIYLGLNRASGVPDRFSGSGSGTDFTL
		KISRVEAEDVGVYYCMQALQTPLTFGGGTKVEI
		KRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYP
		REAKVQWKVDNALQSGNSQESVTEQDSKDSTY
		SLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTK
		SFNRGEC
SS-15504	70	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
		PVTPGEPASISCRSSQSLLHSNGHNYLDWYLQKP
		GQSPQLLIYLGLNRAHGVPDRFSGSGSGTDFTLKI
		SRVEAEDVGVYYCMQALQTPLTFGGGTKVEIKR
		TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE
		AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
		STLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-15494	71	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
		PVTPGEPASISCRSSQSLLHSFGYNYLDWYLQKP
		GQSPQLLIYLGLNRASGVPDRFSGSGSGTDFTLKI
		SRVEAEDVGVYYCMQALQTPLTFGGGTKVEIKR
		TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE
		AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
		STLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-14892	72	DIVMTQSPLSLPVTPGEPASISCRSSQSLLHSF
		GYNYLDWYLQKPGQSPQ
		LLIYLGLNRASGVPDRFSGSGSGTDFTLKISR
		VEAEDVGVYYCMQALQTP
		LTFGGGTKVEIKRTVAAPSVFIFPPSDEQLKS
		GTASVVCLLNNFYPREAK
		VQWKVDNALQSGNSQESVTEQDSKDSTYSL
		SSTLTLSKADYEKHKVYACE
		VTHQGLSSPVTKSFNRGEC
SS-15495	73	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
		PVTPGEPASISCRSSQSLLHSFGHNYLDWYLQKP
		GQSPQLLIYLGLNRAHGVPDRFSGSGSGTDFTLKI
		SRVEAEDVGVYYCMQALQTPLTFGGGTKVEIKR
		TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE
		AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
		STLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-15496	74	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
		PVTPGEPASISCRSSQSLLHSFGHNYLDWYLQKP
		GQSPQLLIYLGLNRAHGVPDRFSGSGSGTDFTLKI
		SRVEAEDVGVYYCMQALQTPLTFGGGTKVEIKR
		TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE
		AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
		STLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-15497	75	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
		PVTPGEPASISCRSSQSLLHSGNGYNYLDWYLQK
		PGQSPQLLIYLGLNRASGVPDRFSGSGSGTDFTL
		KISRVEAEDVGVYYCMQAIHTPLTFGGGTKVEIK
		RTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPR
		EAKVQWKVDNALQSGNSQESVTEQDSKDSTYSL
		SSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-15503	76	MDMRVPAQLLGLLLLWLRGARCDIVMTQSP
		LSLPVTPGEPASISCRSSQSLLHSFGYNYLDW
		YLQKPGQSPQLLIYLGLNRASGVPDRFSGSG
		SGTDFTLKISRVEAEDVGVYYCMQALQTPLT
		FGGGTKVEIKRTVAAPSVFIFPPSDEQLKSGT
		ASVVCLLNNFYPREAKVQWKVDNALQSGN
		SQESVTEQDSKDSTYSLSSTLTLSKADYEKH
		KVYACEVTHQGLSSPVTKSFNRGEC
SS-15505	77	MDMRVPAQLLGLLLLWLRGARCDIVMTQSP
		LSLPVTPGEPASISCRSSQSLLHSNGHNYLDW
		YLQKPGQSPQLLIYLGLNRAHGVPDRFSGSG
		SGTDFTLKISRVEAEDVGVYYCMQALQTPLT
		FGGGTKVEIKRTVAAPSVFIFPPSDEQLKSGT
		ASVVCLLNNFYPREAKVQWKVDNALQSGN
		SQESVTEQDSKDSTYSLSSTLTLSKADYEKH
		KVYACEVTHQGLSSPVTKSFNRGEC
SS-15506	78	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
		PVTPGEPASISCRSSQSLLHSNGHNYLDWYLQKP
		GQSPQLLIYLGLNRAHGVPDRFSGSGSGTDFTLKI
		SRVEAEDVGVYYCMQALQTPLTFGGGTKVEIKR
		TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE
		AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
		STLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-15507	79	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
		PVTPGEPASISCRSSQSLLHSFGYNYLDWYLQKP
		GQSPQLLIYLGLNRASGVPDRFSGSGSGTDFTLKI
		SRVEAEDVGVYYCMQALQTPLTFGGGTKVEIKR
		TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE
		AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
		STLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-15502	80	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
		PVTPGEPASISCRSSQSLLHSFGYNYLDWYLQKP
		GQSPQLLIYLGLNRASGVPDRFSGSGSGTDFTLKI
		SRVEAEDVGVYYCMQALQTPLTFGGGTKVEIKR
		TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE
		AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
		STLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-15508	81	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
		PVTPGEPASISCRSSQSLLHSFGHNYLDWYLQKP
		GQSPQLLIYLGLNRAHGVPDRFSGSGSGTDFTLKI
		SRVEAEDVGVYYCMQALQTPLTFGGGTKVEIKR
		TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE
		AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
		STLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-15501	82	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
		PVTPGEPASISCRSSQSLLHSYGHNYLDWYLQKP
		GQSPQLLIYLGLNRAHGVPDRFSGSGSGTDFTLKI
		SRVEAEDVGVYYCMQALQTPLTFGGGTKVEIKR
		TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE
		AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
		STLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-15500	83	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
		PVTPGEPASISCRSSQSLLHSYGHNYLDWYLQKP
		GQSPQLLIYLGLNRAHGVPDRFSGSGSGTDFTLKI
		SRVEAEDVGVYYCMQALQTPLTFGGGTKVEIKR
		TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE
		AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
		STLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-15003	84	MDMRVPAQLLGLLLLWLRGARCESVLTQPPSVS
		AAPGQKVTISCSGSSSNIGNNFVSWYQQLPGTAP
		KLLIYDYNKRPSGIPDRFSGSKSGTSATLGITGLQ
		TGDEADYYCGTWDSSLSAYVFGTGTRVTVLGQP
		KAAPSVTLFPPSSEELQANKATLVCLISDFYPGAV
		TVAWKADSSPVKAGVETTTPSKQSNNKYAASSY
		LSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS
SS-15005	85	MGSTAILGLLLAVLQGGRADIQMTQSPSSLSASV
		GDRVTITCRASQSISIYLNWYQQKPGKAPYLLIY
		AAASLQSGVPSRFSGSGSGTDFTLTISSLQPEDFA
		TYYCQQSYSAPITFGQGTRLEIKRTVAAPSVFIFP
		PSDEQLKSGTASVVCLLNNFYPREAKVQWKVDN
		ALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADY
		EKHKVYACEVTHQGLSSPVTKSFNRGEC
SS-15757	86	MDMRVPAQLLGLLLLWLRGARCDIVNITQSPLSL
(P1F4)		PVTPGEPASISCRSSQSLLHSNGYNYLDWYLQKP
		GQSPQLLIYLGSNRASGVPDRFSGSGSGTDFTLKI
		SRVEAEDVGVYYCMQAMQTPLTFGGGTKVEIK
		RTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPR
		EAKVQWKVDNALQSGNSQESVTEQDSKDSTYSL
		SSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-15758	87	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
(P1B6)		PVTPGEPASISCRSSQSLLHSNGYNYLDVYLQKP
		GQSPQLLIYLGSNRASGVPDRFSGSGSGTDFTLKI
		SRVEAEDVGVYYCMQALQTPLTFGGGTKVEIKR
		TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE
		AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
		STLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-15759	88	MDMRYPAQLLGLLLLWLRGARCDIVMTQSPLSL
(P2F4)		PVTPGEPASISCRSSQSLLHSNMYNYLDWYLQKP
		GQSPQLLIYLGSNRASGVPDRFSGSGSGTDFTLKI
		SRVEAEDVGVYYCMQALQTPLTFGGGTKVEIKR
		TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE
		AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
		STLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGECQ
SS-15761	89	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
(P2G5)		PVTPGEPASISCRSSQSLLHSNQYNYLDWYLQKP
		GQSPQLLIYLGSNRASGVPDRESGSGSGTDFTLKI
		SRVEAEDVGVYCMQALQTPLTFGGGTKVEIRR
		TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE
		AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
		STLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-15763	90	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
(P2H7)		PVTPGEPASISCRSSQSLMHSNGYNYLDWYLQKP
		GQSPQLLIYLGSNRASGVPDRFSGSGSGTDFTLKI
		SRVEAEDVGVYYCMQALQTPLTFGGGTKVEIKR
		TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE
		AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
		STLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC
SS-15764	91	MDMRVPAQLLGLLLLWLRGARCDIVMTQSPLSL
(P2H8)		PVTPGEPASISCRSSQSLLHSNGYNYLDWYLQKP
		GQSPQLLIYLGINRASGVPDRFSGSGSGTDFTLKI
		SRVEAEDVGVYYCMQALQTPLTFGGGTKVEIKR
		TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE
		AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
		STLTLSKADYEKHKVYACEVTHQGLSSPVTKSF
		NRGEC

TABLE 1B
Exemplary Antibody Heavy Chain Sequences
	SEQ
	ID
Ab ID	NO:	Amino Acid Sequence
SS-13406	92	MDMRVPAQLLGLLLLWLRGARCEVQLVESGGGLV
(8A3HLE-		QPGGSLRLSCAASGFTFSSYWMSWVRQAPGKGLE
51)		WVASIKQDGSEKYYVDSVKGRFTISRDNARNSLYL
		QMNSLRAEDTAVYYCARDLVLMVYDIDYYYYGM
		DVWGQGTTVTVSSASTKGPSVFPLAPCSRSTSESTA
		ALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQ
		SSGLYSLSSVVTVPSSNFGTQTYTCNVDHKPSNTKV
		DKTVERKCCVECPPCPAPPVAGPSVFLFPPKPKDTL
		MISRTPEVFCVVVDVSHEDPEVQFNWYVDGVEVH
		NAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKEY
		KCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPSRE
		EMTKNQVSLTCLVKGFYPSDIAVEWESNGGCHLPF
		AVCGGGQPENNYKTTPPMLDSDGSFFLYSKLTVDK
		SRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK
SS-13407	93	MDMRVPAQLLGLLLLWLRGARCEVQLVESGGGLV
(8A3HLE-		QPGGSLRLSCAASGFTFSSYWMSWVRQAPGKGLE
112)		WVASIKQDGSEKYYVDSVKGRFTISRDNARNSLYL
		QMNSLRAEDTAVYYCARDLVLMVYDIDYYYYGM
		DVWGQGTTVTVSSASTKGPSVFPLAPCSRSTSESTA
		ALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQ
		SSGLYSLSSVVTVPSSNFGTQTYTCNVDHKPSNTKV
		DKTVERKCCVECPPCPAPPVAGPSVFLFPPKPKDTL
		MISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEVH
		NAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKEY
		KCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPSRE
		EMTKNQVSLTCLVKGFYPSDIAVEWESNGGCALYP
		TNCGGGQPENNYKTIPPMLDSDGSFFLYSKLTVDK
		SRWQQGNVFSCSVMHEALHNHYTQKSLSESPGK
SS-14888	94	MDMRVPAQLLGLLLLWLRGARCEVQLVESGGGLV
(P2C6-		QPGGSLRLSCAASGFTFSSYWMSWVRQAPGKGLE
HLE51)		WVASIKQDGSEKYYVDSVKGRFTISRDNARNSLYL
		QMNSLRAEDTAVYYCARDLVLMVYDMDYYYYG
		MDVWGQGTTVTVSSASTKGPSVFPLAPCSRSTSEST
		AALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL
		QSSGLYSLSSVVTVPSSNFGTQTYTCNVDHKPSNTK
		VDKTVERKCCVECPPCPAPPVAGPSVFLFPPKPKDT
		LMISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEV
		HNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKE
		YKCKVSNKGLPAPIEKTISKTKGQPRETQVYTLPPS
		REEMTKNQVSLTCLVKGFYPSDIAVEWESNGGCHL
		PFAVCGGGQPENNYKTTPPMLDSDGSFFLYSKLTV
		DKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK
13G9	95	QVQLVQSGAEVTKPGASVKVSCKASGYTFTSYGIS
		WVRQAPGQGLEWMGWISVYKGNTNYAQKLQGRV
		TMTTDTSTSTAYMELRSLRSDDTAVYYCARNYQIF
		SFDYWGQGTLVTVSSASTKGPSVFPLAPCSRSTSES
		TAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAV
		LQSSGLYSLSSVVTVPSSNFGTQTYTCNVDHKPSNT
		KVDKTVERKCCVECPPCPAPPVAGPSVFLFPPKPKD
		TLMISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEV
		HNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKE
		YKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPS
		REEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPEN
		NYKTTPPMLDSDGSFFLYSKLTVDKSRWQQGNVFS
		CSVMHEALHNHYTQKSLSLSPGK
19A12	96	QVQLVESGGGVVQPGRSLRLSCAASGFTFSSYGMH
		WVRQAPGKGLEWVAVIWYDGSNKYYADSVKGRF
		TISRDNSKNTLYLQMNSLRAEDTAVYYCVRDRGLD
		WGQGTLVTVSSASTKGPSVFPLAPCSRSTSESTAAL
		GCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSS
		GLYSLSSVVTVPSSNFGTQTYTCNVDHKPSNTKVD
		KTVERKCCVECPPCPAPPVAGPSVFLFPPKPKDTLM
		ISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEVHN
		AKTKPREEQFNSTFRVVSVLTVVHQDWLNGKEYK
		CKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPSREE
		MTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYK
		TTPPMLDSDGSFFLYSKLTVDKSRWQQGNVFSCSV
		MHEALHNHYTQKSLSLSPGK
20D12	97	QVQLQQWGAGLLKPSETLSLTCAVSGGSFRAYYW
		NWIRQPPGKGLEWIGEINHSGRTDYNPSLKSRVTIS
		VDTSKNQFSLKLSSVTAADTAVYYCARGQLVPFDY
		WGQGTLVTVSSASTKGPSVFPLAPCSRSTSESTAAL
		GCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSS
		GLYSLSSVVTVPSSNFGTQTYTCNVDHKPSNTKVD
		KTVERKCCVECPPCPAPPVAGPSVFLFPPKPKDTLM
		ISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEVHN
		AKTKPREEQFNSTFRVVSVLTVVHQDWLNGKEYK
		CKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPSREE
		MTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYK
		TTPPMLDSDGSFFLYSKLTVDKSRWQQGNVFSCSV
		MHEALHNHYTQKSLSLSPGK
25B5	98	QIQLVQSGAEVKKPGASVKVSCKASGYTLTSYGIS
		WVRQAPGQGLEWMGWISFYNGNTNYAQKVQGRV
		TMTTDTSTSTVYMELRSLRSDDTAVYFCARGYGM
		DVWGQGTTVTVSSASTKGPSVFPLAPCSRSTSESTA
		ALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQ
		SSGLYSLSSVVTVPSSNFGTQTYTCNVDHKPSNTKV
		DKTVERKCCVECPPCPAPPVAGPSVFLFPPKPKDTL
		MISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEVH
		NAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKEY
		KCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPSRE
		EMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNY
		KTTPPMLDSDGSFFLYSKLTVDKSRWQQGNVFSCS
		VMHEALHNHYTQKSLSLSPGK
30G7	99	QVQLVQSGAEVKKSGASVKVSCKASGYTLTSYGIS
		WVRQAPGQGLEWMGWISVYNGNTNYAQKVQGR
		VTMTTDTSTSTVYMEVRSLRSDDTAVYYCARGYG
		MDVWGQGTTVTVSSASTKGPSVFPLAPCSRSTSEST
		AALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL
		QSSGLYSLSSVVTVPSSNFGTQTYTCNVDHKPSNTK
		VDKTVERKCCVECPPCPAPPVAGPSVFLFPPKPKDT
		LMISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEV
		HNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKE
		YKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPS
		REEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPEN
		NYKTTPPMLDSDGSFFLYSKLTVDKSRWQQGNVFS
		CSVMHEALHNHYTQKSLSLSPGK
SS-15057	100	MELGLRWVFLVAILEGVQCEVQLVESGGGLVKPG
		GSLRLSCAASGFTHSSYSMNWVRQAPGKGLEWVS
		SISSSSSYISYADSVKGRFTISRDNAKNSLYLQMNSL
		RAEDTAVYFCARDYDFHSAYYDAFDVWGQGTMV
		TVSSASTKGPSVFPLAPCSRSTSESTAALGCLVKDY
		FPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSV
		VTVPSSNFGTQTYTCNVDHKPSNTKVDKTVERKCC
		VECPPCPAPPVAGPSVFLFPPKEKDTLMISRTPEVTC
		VVVDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQ
		FNSTFRVVSVLTVVHQDWLNGKEYKCKVSNKGLP
		APIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLT
		CLVKGFYPSDIAVEWESNGQPENNYKTTPPMLDSD
		GSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNH
		YTQKSLSLSPGK
15058	101	MELGLRWVFLVAILEGVQCEVQLVESGGGLVKPG
		GSLRLSCAASGFTFSSHSMNWVRQAPGKGLEWVSS
		ISSSSSYISYADSVKGRFTISRDNAKNSLYLQMNSLR
		AEDTAVYFCARDYDFHSAYYDAFDVWGQGTMVT
		VSSASTKGPSVFPLAPCSRSTSESTAALGCLVKDYFP
		EPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVT
		VPSSNFGTQTYTCNVDHKPSNTKVDKTVERKCCVE
		CPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVV
		VDVSPIEDPEVQFNWYVDGVEVHNAKTKPREEQFN
		STFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPAPI
		EKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCL
		VKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGS
		FFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYT
		QKSLSLSPGK
15059	102	MELGLRWVFLVAILEGVQCEVQLVESGGGLVKPG
		GSLRLSCAASGFTFSSYSMNWVRQAPGKGLEWVSS
		ISSHSSYISYADSVKGRFTISRDNAKNSLYLQMNSLR
		AEDTAVYFCARDYDFHSAYYDAFDVWGQGTMVT
		VSSASTKGPSVFPLAPCSRSTSESTAALGCLVKDYFP
		EPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSWT
		VPSSNFGTQTYTCNVDHKPSNTKVDKTVERKCCVE
		CPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVV
		VDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQFN
		STFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPAPI
		EKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCL
		VKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGS
		FFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYT
		QKSLSLSPGK
15065	103	MELGLRWVFLVAILEGVQCEVQLVESGGGLVKPG
		GSLRLSCAASGFTFSSYSMNWVRQAPGKGLEWVSS
		ISSSSSYISYADSVKGRFTISRDNAKNSLYLQMNSLR
		AEDTAVYFCARDYDFHSAHYDAFDVWGQGTMVT
		VSSASTKGPSVFPLAPCSRSTSESTAALGCLVKDYFP
		EPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVT
		VPSSNFGTQTYTCNVDHKPSNTKVDKTVERKCCVE
		CPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVV
		VDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQFN
		STFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPAPI
		EKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCL
		VKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGS
		FFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYT
		QKSLSLSPGK
15079	104	MELGLRWVFLVAILEGVOCEVQLVESGGGLVKPG
		GSLRLSCAASGFTHSSYSMNWVRQAPGKGLEWVS
		SISSSSSYISYADSVKGRFTISRDNAKNSLYLQMNSL
		RAEDTAVYFCARDYDFHSAYYDAFDVWGQGTMV
		TVSSASTKGPSVFPLAPCSRSTSESTAALGCLVKDY
		FPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSV
		VTVPSSNFGTQTYTCNVDHKPSNTKVDKTVERKCC
		VECPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTC
		VVVDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQ
		FNSTFRVVSVLTVVHQDWLNGKEYKCKVSNKGLP
		APIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLT
		CLVKGFYPSDIAVEWESNGQPENNYKTTPPMLDSD
		GSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNH
		YTQKSLSLSPGK
15080	105	MELGLRWVFLVAILEGVQCEVQLVESGGGLVKPG
		GSLRLSCAASGFTFSSHSMNWVRQAPGKGLEWVSS
		ISSSSSYISYADSVKGRFTISRDNAKNSLYLQMNSLR
		AEDTAVYFCARDYDFHSAYYDAFDVWGQGTMVT
		VSSASTKGPSVFPLAPCSRSTSESTAALGCLVKDYFP
		EPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVT
		VPSSNFGTQTYTCNVDHKPSNTKVDKTVERKCCVE
		CPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVV
		VDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQFN
		STFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPAPI
		EKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCL
		VKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGS
		FFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYT
		QKSLSLSPGK
15087	106	MELGLRWVFLVAILEGVQCEVQLVESGGGLVKPG
		GSLRLSCAASGFTFSSYSMNWVRQAPGKGLEWVSS
		ISSSSSYISYADSVKGRFTISRDNAKNSLYLQMNSLR
		AEDTAVYFCARDYDFHSAHYDAFDVWGQGTMVT
		VSSASTKGPSVFPLAPCSRSTSESTAALGCLVKDYFP
		EPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVT
		VPSSNFGTQTYTCNVDHKPSNTKVDKTVERKCCVE
		CPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVV
		VDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQFN
		STFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPAPI
		EKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCL
		VKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGS
		FFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYT
		QKSLSLSPGK
15101	107	MELGLRWVFLVAILEGVQCEVQLVESGGGLVKPG
		GSLRLSCAASGFTHSSYSMNWVRQAPGKGLEWVS
		SISSSSHYISYADSVKGRFTISRDNAKNSLYLQMNSL
		RAEDTAVYFCARDYDFHSAYYDAFDVWGQGTMV
		TVSSASTKGPSVFPLAPCSRSTSESTAALGCLVKDY
		FPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSV
		VTVPSSNFGTQTYTCNVDHKPSNTKVDKTVERKCC
		VECPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTC
		VVVDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQ
		FNSTFRVVSVLTVVHQPWLNGKEYKCKVSNKGLP
		APIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLT
		CLVKGFYPSDIAVEWESNGQPENNYKTTPPMLDSD
		GSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNH
		YTQKSLSLSPGK
15103	108	MELGLRWVFLVAILEGVQCEVQLVESGGGLVKPG
		GSLRLSCAASGFTHSSYSMNWVRQAPGKGLEWVS
		SISSSSSYISHADSVKGRFTISRDNAKNSLYQMNSL
		RAEDTAVYFCARDYDFHSAYYDAEDVWGQGTMV
		TVSSASTKGPSVFPLAPCSRSTSESTAALGCLVKDY
		FPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSV
		VTVPSSNFGTQTYTCNVDHKPSNTKVDKTVERKCC
		VECPPCPAPPVAGPSVELFPPKPKDTLMISRTPEVTC
		VVVDVSHEDPEVQFNWYVDGEVHNAKTKPREEQ
		FNSTFRVVSVLTVVHQDWLNGKEYKCKVSNKGLP
		APIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLT
		CLVKGFYPSDIAVEWESNGQPENNYKTTPPMLDSD
		GSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNH
		YTQKSLSLSPGK
15104	109	MELGLRWVFLVAILEGVQCEVQLVESGGGLVKPG
		GSLRLSCAASGFTHSSYSMNWVRQAPGKGLEWVS
		SISSSSSYISYAHSVKGRFTISRDNAKNSLYLQMNSL
		RAEDTAVYFCARDYDFHSAYYDAFDVWGQGTMV
		TVSSASTKGPSVFPLAPCSRSTSESTAALGCLVKDY
		FPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSV
		VTVPSSNFGTQTYTCNVDHKPSNTKVDKTVERKCC
		VECPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTC
		VVVDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQ
		FNSTFRVVSVLTVVHQDWLNGKEYKCKVSNKGLP
		APIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLT
		CLVKGFYPSDIAVEWESNGQPENNYKTTPPMLDSD
		GSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNH
		YTQKSLSLSPGK
15105	110	MELGLRWVFLVAILEGVQCEVQLVESGGGLVKPG
		GSLRLSCAASGFTHSSYSMNWVRQAPGKGLEWVS
		SISSSSHYISYADSVKGRFTISRDNAKNSLYLQMNSL
		RAEDTAVYFCARDYDFHSAYYDAFDVWGQGTMV
		TVSSASTKGPSVFPLAPCSRSTSESTAALGCLVKDY
		FPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSV
		VTVPSSNFGTQTYTCNVDHKPSNTKVDKTVERKCC
		VECPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTC
		VVVDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQ
		FNSTFRVVSVLTVVHQPWLNGKEYKCKVSNKGLP
		APIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLT
		CLVKGFYPSDIAVEWESNGQPENNYKTTPPMLDSD
		GSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNH
		YTQKSLSLSPGK
15106	111	MELGLRWVFLVAILEGVQCEVQLVESGGGLVKPG
		GSLRLSCAASGFTHSSYSMNWVRQAPGKGLEWVS
		SISSSSSYISHADSVKGRFTISRDNAKNSLYQMNSL
		RAEDTAVYFCARDYDFHSAYYDAEDVWGQGTMV
		TVSSASTKGPSVFPLAPCSRSTSESTAALGCLVKDY
		FPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSV
		VTVPSSNFGTQTYTCNVDHKPSNTKVDKTVERKCC
		VECPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTC
		VVVDVSHEDPEVQFNWYVDGEVHNAKTKPREEQ
		FNSTFRVVSVLTVVHQDWLNGKEYKCKVSNKGLP
		APIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLT
		CLVKGFYPSDIAVEWESNGQPENNYKTTPPMLDSD
		GSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNH
		YTQKSLSLSPGK
15108	112	MELGLRWVFLVAILEGVQCEVQLVESGGGLVKPG
		GSLRLSCAASGFTFSSHSMNWVRQAPGKGLEWVSS
		ISSHSSYISYADSVKGRFTISRDNAKNSLYLQMNSLR
		AEDTAVYFCARDYDFHSAYYDAFDVWGQGTMVT
		VSSASTKGPSVFPLAPCSRSTSESTAALGCLVKDYFP
		EPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVT
		VPSSNFGTQTYTCNVDHKPSNTKVDKTVERKCCVE
		CPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVV
		VDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQFN
		STFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPAPI
		EKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCL
		VKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGS
		FFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYT
		QKSLSLSPGK
15112	113	MELGLRWVFLVAILEGVQCEVQLVESGGGLVKPG
		GSLRLSCAASGFTFSSHSMNWVRQAPGKGLEWVSS
		ISSSSSYISYAHSVKGRFTISRDNAKNSLYLQMNSLR
		AEDTAVYFCARDYDFHSAYYDAFDVWGQGTMVT
		VSSASTKGPSVFPLAPCSRSTSESTAALGCLVKDYFP
		EPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVT
		VPSSNFGTQTYTCNVDHKPSNTKVDKTVERKCCVE
		CPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVV
		VDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQFN
		STFRVVSVLTVVHQPWLNGKEYKCKVSNKGLPAPI
		EKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCL
		VKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGS
		FFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYT
		QKSLSLSPGK
15113	114	MELGLRWVFLVAILEGVQCEVQLVESGGGLVKPG
		GSLRLSCAASGFTFSSHSMNWVRQAPGKGLEWVSS
		ISSSSSYISYADSVKGRFTISRDNAKNSLYQMNSLR
		AEDTAVYFCARDYDFHSAYYDAFDVWGQGTMVT
		VSSASTKGPSVFPLAPCSRSTSESTAALGCLVKDYFP
		EPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVT
		VPSSNFGTQTYTCNVDHKPSNTKVDKTVERKCCVE
		CPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVV
		VDVSHEDPEVQFNWYVDGEVHNAKTKPREEQFN
		STFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPAPI
		EKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCL
		VKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGS
		FFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYT
		QKSLSLSPGK
15114	115	MELGLRWVFLVAILEGVQCEVQLVESGGGLVKPG
		GSLRLSCAASGFTFSSHSMNWVRQAPGKGLEWVSS
		ISSSSSYISYADSVKGRFTISRDNAKNSLYLQMNSLR
		AEDTAVYFCARDYDFHSAHYDAFDVWGQGTMVT
		VSSASTKGPSVFPLAPCSRSTSESTAALGCLVKDYFP
		EPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVT
		VPSSNFGTQTYTCNVDHKPSNTKVDKTVERKCCVE
		CPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVV
		VDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQFN
		STFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPAPI
		EKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCL
		VKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGS
		FFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYT
		QKSLSLSPGK
15117	116	MELGLRWVFLVAILEGVQCEVQLVESGGGLVKPG
		GSLRLSCAASGFTFSSYSMNWVRQAPGKGLEWVSS
		ISSHSSYHSYADSVKGRFTISRDNAKNSLYLQMNSL
		RAEDTAWFCARDYDFHSAYYDAFDVWGQGTMV
		TVSSASTKGPSVFPLAPCSRSTSESTAALGCLVKDY
		FPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSV
		VTVPSSNFGTQTYTCNVDHKPSNTKVDKTVERKCC
		VECPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTC
		VVVDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQ
		FNSTFRVVSVLTVVHQDWLNGKEYKCKVSNKGLP
		APIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLT
		CLVKGFYPSDIAVEWESNGQPENNYKTTPPMLDSD
		GSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNH
		YTQKSLSLSPGK
15121	117	MELGLRWVFLVAILEGVQCEVQLVESGGGLVKPG
		GSLRLSCAASGFTFSSYSMNWVRQAPGKGLEWVSS
		ISSHSSYISYADSVKGRFTISRDNAKNSLYLQMNSLR
		AEDTAVYFCARDYDFHSAHYDAFDVWGQGTMVT
		VSSASTKGPSVFPLAPCSRSTSESTAALGCLVKDYFP
		EPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVT
		VPSSNFGTQTYTCNVDHKPSNTKVDKTVERKCCVE
		CPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVV
		VDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQFN
		STFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPAPI
		EKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCL
		VKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGS
		FFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYT
		QKSLSLSPGK
15123	118	MELGLRWVFLVAILEGVQCEVQLVESGGGLVKPG
		GSLRLSCAASGFTFSSYSMNWVRQAPGKGLEWVSS
		ISSSSHYHSYADSVKGRFTISRDNAKNSLYLQMNSL
		RAEDTAVYFCARDYDFHSAYYDAFDVWGQGTMV
		TVSSASTKGPSVFPLAPCSRSTSESTAALGCLVKDY
		FPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSV
		VTVPSSNFGTQTYTCNVDHKPSNTKVDKTVERKCC
		VECPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTC
		VVVDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQ
		FNSTFRVVSVLTVVHQDWLNGKEYKCKVSNKGLP
		APIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLT
		CLVKGFYPSDIAVEWESNGQPENNYKTTPPMLDSD
		GSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNH
		YTQKSLSLSPGK
15124	119	MELGLRWVFLVAILEGVQCEVQLVESGGGLVKPG
		GSLRLSCAASGFTFSSYSMNWVRQAPGKGLEWVSS
		ISSSSHYISHADSVKGRFTISRDNAKNSLYLQMNSLR
		AEDTAVYFCARDYDFHSAYYDAFDVWGQGTMVT
		VSSASTKGPSVFPLAPCSRSTSESTAALGCLVKDYFP
		EPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVT
		VPSSNFGTQTYTCNVDHKPSNTKVDKTVERKCCVE
		CPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVV
		VDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQFN
		STFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPAPI
		EKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCL
		VKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGS
		FFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYT
		QKSLSLSPGK
15126	120	MELGLRWVFLVAILEGVQCEVQLVESGGGLVKPG
		GSLRLSCAASGFTFSSYSMNWVRQAPGKGLEWVSS
		ISSSSHYISYADHVKGRFTISRDNAKNSLYLQMNSL
		RAEDTAVYFCARDYDFHSAYYDAFDVWGQGTMV
		TVSSASTKGPSVFPLAPCSRSTSESTAALGCLVKDY
		FPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSV
		VTVPSSNFGTQTYTCNVDHKRSNTKVDKTVERKCC
		VECPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTC
		VVVDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQ
		FNSTFRVVSVLTVVHQDWLNGKEYKCKVSNKGLP
		APIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLT
		CLVKGFYPSDIAVEWESNGQPENNYKTTPPMLDSD
		GSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNH
		YTQKSLSLSPGK
15132	121	MELGLRWVFLVAILEGVQCEVQLVESGGGLVKPG
		GSLRLSCAASGFTFSSYSMNWVRQAPGKGLEWVSS
		ISSSSSYHSYADSVKGRFTISRDNAKNSLYLQMNSL
		RAEDTAVYFCARDYDFHSAHYDAFDVWGQGTMV
		TVSSASTKGPSVFPLAPCSRSTSESTAALGCLVKDY
		FPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSV
		VTVPSSNFGTQTYTCNVDHKPSNTKVDKTVERKCC
		VECPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTC
		VVVDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQ
		FNSTFRVVSVLTVVHQDWLNGKEYKCKVSNKGLP
		APIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLT
		CLVKGFYPSDIAVEWESNGQPENNYKTTPPMLDSD
		GSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNH
		YTQKSLSLSPGK
15133	122	MELGLRWVFLVAILEGVQCEVQLVESGGGLVKPG
		GSLRLSCAASGFTFSSYSMNWVRQAPGKGLEWVSS
		ISSSSSYHSYADSVKGRFTISRDNAKNSLYLQMNSL
		RAEDTAVYFCARDYDFHSAYHDAFDVWGQGTMV
		TVSSASTKGPSVFPLAPCSRSTSESTAALGCLVKDY
		FPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSV
		VTVPSSNFGTQTYTCNVDHKPSNTKVDKTVERKCC
		VECPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTC
		VVVDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQ
		FNSTFRVVSVLTVVHQDWLNGKEYKCKVSNKGLP
		APIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLT
		CLVKGFYPSDIAVEWESNGQPENNYKTTPPMLDSD
		GSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNH
		YTQKSLSLSPGK
15136	123	MELGLRWVFLVAILEGVQCEVQLVESGGGLVKPG
		GSLRLSCAASGFTFSSYSMNWVRQAPGKGLEWVSS
		ISSSSSYISHADSVKGRFTISRDNAKNSLYLQMNSLR
		AEDTAVYFCARDYDFHSAHYDAFDVWGQGTMVT
		VSSASTKGPSVFPLAPCSRSTSESTAALGCLVKDYFP
		EPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVT
		VPSSNFGTQTYTCNVDHKPSNTKVDKTVERKCCVE
		CPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVV
		VDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQFN
		STFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPAPI
		EKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCL
		VKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGS
		FFLYSKLTVDKSRWQQGWFSCSVMHEALHNHYT
		QKSLSLSPGK
15139	124	MELGLRWVFLVAILEGVQCEVQLVESGGGLVKPG
		GSLRLSCAASGFTFSSYSMNWVRQAPGKGLEWVSS
		ISSSSSYISYAHSVKGRFTISRDNAKNSLYLQMNSLR
		AEDTAVYFCARDYDFHSAHYDAFDVWGQGTMVT
		VSSASTKGPSVFPLAPCSRSTSESTAALGCLVKDYFP
		EPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVT
		VPSSNFGTQTYTCNVDHKPSNTKVDKTVERKGCVE
		CPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVV
		VDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQFN
		STFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPAPI
		EKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCL
		VKGFYPSDLWEWESNGQPENNYKTTPPMLDSDGS
		FFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYT
		QKSLSLSPGK
15140	125	MELGLRWVFLVAILEGVQCEVQLVESGGGLVKPG
		GSLRLSCAASGFTFSSYSMNWVRQAPGKGLEWVSS
		ISSSSSYISYAHSVKGRFTISRDNAKNSLYLQMNSLR
		AEDTAVYFCARDYDFHSAYHDAFDVWGQGTMVT
		VSSASTKGPSVFPLAPCSRSTSESTAALGCLVKDYFP
		EPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVT
		VPSSNFGTQTYTCNVDHKPSNTKVDKTVERKCCVE
		CPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVV
		VDVSHEDPEYQFNWYVDGVEVHNAKTKPREEQFN
		STFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPAPI
		EKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCL
		VKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGS
		FFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYT
		QKSLSLSPGK
15141	126	MELGLRWVFLVAILEGVQCEVQLVESGGGLVKPG
		GSLRLSCAASGFTFSSYSMNWVRQAPGKGLEWVSS
		ISSSSSYISYADHVKGRFTISRDNAKNSLYLQMNSLR
		AEDTAVYFCARDYDFHSAHYDAFDVWGQGTMVT
		VSSASTKGPSVFPLAPCSRSTSESTAALGCLVKDYFP
		EPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVT
		VPSSNFGTQTYTCNVDHKPSNTKVDKTVERKCCVE
		CPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVV
		VDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQFN
		STFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPAPI
		EKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCL
		VKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGS
		FFLYSKLTVDKSRWQQGNWSCSVMHEALHNHYT
		QKSLSLSPGK
SS-13983	127	MDMRVPAQLLGLLLLWLRGARCEVQLVESGGGLV
A01		QPGGSLRLSCAASGFTFSSYWMSWVRQAPGKGLE
		WVASIKQDGSEKYYVDSVKGRFTISRDNARNSLYL
		QMNSLRAEDTAVYYCARDLVLMVYDIDYYYYGM
		DVWGQGTTVTVSSASTKGPSVFPLAPCSRSTSESTA
		ALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQ
		SSGLYSLSSVVTVPSSNFGTQTYTCNVDHKPSNTKV
		DKTVERKCCVECPPCPAPPVAGPSVFLFPPKPKDTL
		MISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEVH
		NAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKEY
		KCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPSRE
		EMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNY
		KTTPPMLDSDGSFFLYSKLTVDKSRWQQGNVFSCS
		VMHEALHNHYTQKSLSLSPGK
SS-13991	128	MDMKYPAQLLGLLLLWLRGARCEVQLVESGGGLV
A02		QPGGSLRLSCAASGFTFSSYWMSWVRQAPGKGLE
		WVASIKQDGSEKYYVDSVKGRFTISRDNARNSLYL
		QMNSLRAEDTAVYYCARDLVLMVYDIDYYYYGM
		DVWGQGTTVTVSSASTKGPSVFPLAPCSRSTSESTA
		ALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQ
		SSGLYSLSSVVTVPSSNFGTQTYTCNVDHKPSNTKV
		DKTVERKCCVECPPCPAPPVAGPSVFLFPPKPKDTL
		MISRTPEVTCVVVDVSHEDPEVQFNWYDGVEVH
		NAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKEY
		KCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPSRE
		EMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNY
		KTTPPMLDSDGSFFLYSKLTVDKSRWQQGNVFSCS
		VMHEALHNHYTQKSLSLSPGK
SS-13993	129	MDMRVPAQLLGLLLLWLRGARCEVQLVESGGGLV
C02		QPGGSLRLSCAASGFTFSSYWMSWVRQAPGKGLE
		WVASIKQDGSEKYYVDSVKGRFTISRDNARNSLYL
		QMNSLRAEDTAVYYCARDLVLMVYDIDYYYYGM
		DVWGQGTTVTVSSASTKGPSVFPLAPCSRSTSESTA
		ALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQ
		SSGLYSLSSVVTVPSSNFGTQTYTCNVDHKPSNTKV
		DKTVERKCCVECPPCPAPPVAGPSVFLFPPKPKDTL
		MISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEVH
		NAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKEY
		KCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPSRE
		EMTKNQVSLTCLVTCGFYPSDIAVEWESNGQPENNY
		KTTPPMLDSDGSFFLYSKLTVDKSRWQQGNVFSCS
		VMHEALHNHYTQKSLSLSPGK
SS-12685	130	MDMRVPAQLLGLLLLWLRGARCEVQLVESGGGLV
P1B1		QPGGSLRLSCAASGFTFSSYWMSWVRQAPGKGLE
		WVASIKQDGSEKYYVDSVKGRFTISRDNARNSLYL
		QMNSLRAEDTAVYYCARDLVLMVYDMDYYYYG
		MDVWGQGTTVTVSSASTKGPSVFPLAPCSRSTSEST
		AALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL
		QSSGLYSLSSVVTVPSSMFGTQTYTCNVDHKPSNTK
		VDKTVERKCCVECPPCPAPPVAGPSVFLFPPKPKDT
		LMISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEV
		HNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKE
		YKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPS
		REEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPEN
		NYKTTPPMLDSDGSFFLYSKLTVDKSRWQQGNVFS
		CSVMHEALHNHYTQKSLSLSPGK
SS-12686	131	MDMRVPAQLLGLLLLWLRGARCEVQLVESGGGLV
P2F5		QPGGSLRLSCAASGFTFSSYWMSWVRQAPGKGLE
		WVASIKQDGSEKYYVDSVKGRFTISRDNARNSLYL
		QMNSLRAEDTAVYYCARDLVLMVYDMDYYYYG
		MDVWGQGTTVTVSSASTKGPSVFPLAPCSRSTSEST
		AALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL
		QSSGLYSLSSVVTVPSSNFGTQTYTCNVDHKPSNTK
		VDKTVERKCCVECPPCPAPPVAGPSVFLFPPKPKDT
		LMISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEV
		HNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKE
		YKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPS
		REEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPEN
		NYKTTPPMLDSDGSFFLYSKLTVDKSRWQQGNVFS
		CSVMHEALHNHYTQKSLSLSPGK
SS-12687	132	MDMRVPAQLLGLLLLWLRGARCEVQLVESGGGLV
P2C6		QPGGSLRLSCAASGFTFSSYWMSWVRQAPGKGLE
		WVASIKQDGSEKYYVDSVKGRFTISRDNARNSLYL
		QMNSLRAEDTAVYYCARDLVLMVYDMDYYYYG
		MDVWGQGTTVTVSSASTKGPSVFPLAPCSRSTSEST
		AALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL
		QSSGLYSLSSVVTVPSSNFGTQTYTCNVDHKPSNTK
		VDKTVERKCCVECPPCPAPPVAGPSVFLFPPKPKDT
		LMISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEV
		HNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKE
		YKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPS
		REEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPEN
		NYKTTPPMLDSDGSFFLYSKLTVDKSRWQQGNVFS
		CSVMHEALHNHYTQKSLSLSPGK
SS-14892	133	MDMRVPAQLLGLLLLWLRGARCEVQLVESGGGLV
P2F5/P2C6		QPGGSLRLSCAASGFTFSSYWMSWVRQAPGKGLE
		WVASIKQDGSEKYYVDSVKGRFTISRDNARNSLYL
		QMNSLRAEDTAVYYCARDLVLMVYDMDYYYYG
		MDVWGQGTTVTVSSASTKGPSVFPLAPCSRSTSEST
		AALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL
		QSSGLYSLSSVVTVPSSNFGTQTYTCNVDYHKPSNTK
		VDKTVERKCCVECPPCPAPPVAGPSVFLFPPKPKDT
		LMISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEV
		HNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKE
		YKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPS
		REEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPEN
		NYKTTPPMLDSDGSFFLYSKLTVDKSRWQQGNVFS
		CSVMHEALHNHYTQKSLSLSPGK
SS-15509	134	MGSTAILGLLLAVLQGGRAEVQLVESGGGLVQPGG
		SLRLSCAASGFTFSSYWMSWVRQAPGKGLEWVASI
		KQDGSEKYYVDSVKGRFTISRDNARNSLYLQMNSL
		RAEDTAVYYCARDLVLFVYDMDYYYYGMDVWG
		QGTTVTVSSASTKGPSVFPLAPCSRSTSESTAALGCL
		VKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY
		SLSSVVTVPSSNFGTQTYTCNVDHKPSNTKVDKTV
		ERKCCVECPPCPAPPVAGPSVFLFPPKPKDTLMISRT
		PEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTK
		PREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVS
		NKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTK
		NQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTP
		PMLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMH
		EALHNHYTQKSLSLSPGK
SS-15510	135	MGSTAILGLLLAVLQGGRAEVQLVESGGGLVQPGG
		SLRLSCAASGFTFSSYWMSWVRQAPGKGLEWVASI
		KQDGSEKYYVDSVKGRFTISRDNARNSLYLQMNSL
		RAEDTAVYYCARDLVLFVYDMDYYYYGMDVWG
		QGTTVTVSSASTKGPSVFPLAPCSRSTSESTAALGCL
		VKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY
		SLSSVVTVPSSNFGTQTYTCNVDHKPSNTKVDKTV
		ERKCCVECPPCPAPPVAGPSVFLFPPKPKDTLMISRT
		PEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTK
		PREEQFNSTFRVVSVLTVVHQDWLNGKEYKGKVS
		NKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTK
		NQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTP
		PMLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMH
		EALHNHYTQKSLSLSPGK
SS-15511	136	MGSTAILGLLLAVLQGGRAEVQLVESGGGLVQPGG
		SLRLSCAASGFTFSSYWMSWVRQAPGKGLEWVASI
		KQDGSEKYYVDSVKGRFTISRDNARNSLYLQMNSL
		RAEDTAVYYCARDLVLFVYDMDYYYYGMDVWG
		QGTTVTVSSASTKGPSVFPLAPCSRSTSESTAALGCL
		VKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY
		SLSSVVTVPSSNFGTQTYTCNVDHKPSNTKVDKTV
		ERKCCVECPPCPAPPVAGPSVFLFPPKPKDTLMISRT
		PEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTK
		PREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVS
		NKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTK
		NQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTP
		PMLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMH
		EALHNHYTQKSLSLSPGK
SS-15512	137	MGSTAILGLLLAVLQGGRAEVQLVESGGGLVQPGG
		SLRLSCAASGFTFSSYWMSWVRQAPGKGLEWVASI
		KQDGSEKYYVDSVKGRFTISRDNARNSLYLQMNSL
		RAEDTAVYYCARDLVLFVYDMDYYYYGMDVWG
		QGTTVTVSSASTKGPSVFPLAPCSRSTSESTAALGCL
		VKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY
		SLSSVVTVPSSNFGTQTYTCNVDHKPSNTKVDKTV
		ERKCCVECPPCPAPPVAGPSVFLFPPKPKDTLMISRT
		PEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTK
		PREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVS
		NKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTK
		NQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTP
		PMLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMH
		EALHNHYTQKSLSLSPGK
SS-15513	138	MGSTAILGLLLAVLQGGRAEVQLVESGGGLVQPGG
		SLRLSCAASGFTFSSYWMSWVRQAPGKGLEWVASI
		KQDGSEKYYVDSVKGRFTISRDNARNSLYLQMNSL
		RAEDTAVYYCARDLVLFVYDMDYYYYGMDVWG
		QGTTVTVSSASTKGPSVFPLAPCSRSTSESTAALGCL
		VKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY
		SLSSVVTVPSSNFGTQTYTCNVDHKPSNTKVDKTV
		ERKCCVECPPCPAPPVAGPSVFLFPPKPKDTLMISRT
		PEVTCVVVDVSHEDPEVQFNWYVDGVEVPFNAKTK
		PREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVS
		NKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTK
		NQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTP
		PMLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMH
		EALHNHYTQKSLSLSPGK
SS-15514	139	MGSTAILGLLLAVLQGGRAEVQLVESGGGLVQPGG
		SLRLSCAASGFTFSSYWMSWVRQAPGKGLEWVASI
		KQDGSEKYYVDSVKGRFTISRDNARNSLYLQMNSL
		RAEDTAVYYCARDLVLFVYDMDYYYYGMDVWG
		QGTTVTVSSASTKGPSVFPLAPCSRSTSESTAALGCL
		VKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY
		SLSSVVTVPSSNFGTQTYTCNVDHKPSNTKVDKTV
		ERKCCVECPPCPAPPVAGPSVFLFPPKPKDTLMISRT
		PEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTK
		PREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVS
		NKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTK
		NQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTP
		PMLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMH
		EALHNHYTQKSLSLSPGK
SS-15497	140	MGSTAILGLLLAVLQGGRAEVQLVESGGGLVQPGG
		SLRLSCAASGFTFSSYWMSWVRQAPGKGLEWVASI
		KQDGSEKYYVDSVKGRFTISRDNARNSLYLQMNSL
		RAEDTAVYYCARDLVLSVYDMDYYYYGMDVWG
		QGTTVTVSSASTKGPSVFPLAPCSRSTSESTAALGCL
		VKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY
		SLSSVVTVPSSNFGTQTYTCNVDHKPSNTKVDKTV
		ERKCCVECPPCPAPPVAGPSVFLFPPKPKDTLMISRT
		PEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTK
		PREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVS
		NKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTK
		NQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTP
		PMLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMH
		EALHNHYTQKSLSLSPGK
SS-15515	141	MGSTAILGLLLAVLQGGRAEVQLVESGGGLVQPGG
		SLRLSCAASGFTFSSYWMSWVRQAPGKGLEWVASI
		KQDGSEKYYVDSVKGRFTISRDNARNSLYLQMNSL
		RAEDTAVYYCARDLVLSVYDMDYYYYGMDVWG
		QGTTVTVSSASTKGPSVFPLAPCSRSTSESTAALGCL
		VKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY
		SLSSVVTVPSSNFGTQTYTCNVDHKPSNTKVDKTV
		ERKCCVECPPCPAPPVAGPSVFLFPPKPKDTLMISRT
		PEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTK
		PREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVS
		NKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTK
		NQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTP
		PMLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMH
		EALHNHYTQKSLSLSPGK
SS-15516	142	MGSTAILGLLLAVLQGGRAEVQLVESGGGLVQPGG
		SLRLSCAASGFTFSSYWMSWVRQAPGKGLEWVASI
		KQDGSEKYYVDSVKGRFTISRDNARNSLYLQMNSL
		RAEDTAVYYCARDLVLSVYDMDYYYYGMDVWG
		QGTTVTVSSASTKGPSVFPLAPCSRSTSESTAALGCL
		VKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY
		SLSSVVTVPSSNFGTQTYTCNVDHKPSNTKVDKTV
		ERKCCVECPPCPAPPVAGPSVFLFPPKPKDTLMISRT
		PEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTK
		PREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVS
		NKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTK
		NQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTP
		PMLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMH
		EALHNHYTQKSLSLSPGK
SS-15517	143	MGSTAILGLLLAVLQGGRAEVQLVESGGGLVQPGG
		SLRLSCAASGFTFSSYWMSWVRQAPGKGLEWVASI
		KQDGSEKYYVDSVKGRFTISRDNARNSLYLQMNSL
		RAEDTAVYYCARDLVLSVYDMDYYYYGMDVWG
		QGTTVTVSSASTKGPSVFPLAPCSRSTSESTAALGCL
		VKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY
		SLSSVVTVPSSNFGTQTYTCNVDHKPSNTKVDKTV
		ERKCCVECPPCPAPPVAGPSVFLFPPKPKDTLMISRT
		PEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTK
		PREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVS
		NKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTK
		NQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTP
		PMLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMH
		EALHNHYTQKSLSLSPGK
SS-15518	144	MGSTAILGLLLAVLQGGRAEVQLVESGGGLVQPGG
		SLRLSCAASGFTFSSYWMSWVRQAPGKGLEWVASI
		KQDGSEKYYVDSVKGRFTISRDNARNSLYLQMNSL
		RAEDTAVYYCARDLVLSVYDMDYYYYGMDVWG
		QGTTVTVSSASTKGPSVFPLAPCSRSTSESTAALGCL
		VKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY
		SLSSVVTVPSSNFGTQTYTCNVDHKPSNTKVDKTV
		ERKCCVECPPCPAPPVAGPSVFLFPPKPKDTLMISRT
		PEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTK
		PREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVS
		NKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTK
		NQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTP
		PMLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMH
		EALHNHYTQKSLSLSPGK
SS-15519	145	MGSTAILGLLLAVLQGGRAEVQLVESGGGLVQPGG
		SLRLSCAASGFTFSSYWMSWVRQAPGKGLEWVASI
		KQDGSEKYYVDSVKGRFTISRDNARNSLYLQMNSL
		RAEDTAVYYCARDLVLSVYDMDYYYYGMDVWG
		QGTTVTVSSASTKGPSVFPLAPCSRSTSESTAALGCL
		VKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY
		SLSSVVTVPSSNFGTQTYTCNVDHKPSNTKVDKTV
		ERKCCVECPPCPAPPVAGPSVFLFPPKPKDTLMISRT
		PEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTK
		PREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVS
		NKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTK
		NQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTP
		PMLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMH
		EALHNHYTQKSLSLSPGK
SS-15520	146	MGSTAILGLLLAVLQGGRAEVQLVESGGGLVQPGG
		SLRLSCAASGFTFSSYWMSWVRQAPGKGLEWVASI
		KQDGSEKYYVDSVKGRFTISRDNARNSLYLQMNSL
		RAEDTAVYYCARDLVLSVYDMDYYYYGMDVWG
		QGTTVTVSSASTKGPSVFPLAPCSRSTSESTAALGCL
		VKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY
		SLSSVVTVPSSNFGTQTYTCNVDHKPSNTKVDKTV
		ERKCCVECPPCPAPPVAGPSVFLFPPKPKDTLMISRT
		PEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTK
		PREEQFNSTFRAVVSVLTVVHQDWLNGKEYKCKVS
		NKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTK
		NQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTP
		PMLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMH
		EALHNHYTQKSLSLSPGK
SS-15522	147	MGSTAILGLLLAVLQGGRAEVQLVESGGGLVQPGG
		SLRLSCAASGFTFSSYWMSWVRQAPGKGLEWVASI
		KQDGSEKYYVDSVKGRFTISRDNARNSLYLQMNSL
		RAEDTAVYYCARDLVLSVYDMDYYYYGMDVWG
		QGTTVTVSSASTKGPSVFPLAPCSRSTSESTAALGCL
		VKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY
		SLSSVVTVPSSNFGTQTYTCNVDHKPSNTKVDKTV
		ERKCCVECPPCPAPPVAGPSVFLFPPKPKDTLMISRT
		PEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTK
		PREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVS
		NKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTK
		NQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTP
		PMLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMH
		EALHNHYTQKSLSLSPGK
SS-15524	148	MGSTAILGLLLAVLQGGRAEVQLVESGGGLVQPGG
		SLRLSCAASGFTFSSYWMSWVRQAPGKGLEWVASI
		KQDGSEKYYVDSVKGRFTISRDNARNSLYLQMNSL
		RAEDTAVYYCARDLVLFVYDMDYYYYGMDVWG
		QGTTVTVSSASTKGPSVFPLAPCSRSTSESTAALGCL
		VKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY
		SLSSVVTVPSSNFGTQTYTCNVDHKPSNTKVDKTV
		ERKCCVECPPCPAPPVAGPSVFLFPPKPKDTLMISRT
		PEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTK
		PREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVS
		NKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTK
		NQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTP
		PMLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMH
		EALHNHYTQKSLSLSPGK
SS-14835	149	MDMRVPAQLLGLLLLWLRGARCEVQLVESGGGLV
		QPGGSLRLSCAASGFTFSSYWMSWVRQAPGKGLE
		WVASIKQDGSEKYYVDSVKGRFTISRDNARNSLYL
		QMNSLRAEDTAVYYCARDLVLMVYDIDYYYYGM
		DVWGQGTTVTVSSASTKGPSVFPLAPCSRSTSESTA
		ALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQ
		SSGLYSLSSVVTVPSSNFGTQTYTCNVDHKPSNTKV
		DKTVERKCCVECPPCPAPPVAGPSVFLFPPKPKDTL
		MISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEVH
		NAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKEY
		KCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPSRE
		EMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNY
		KTTPPMLDSDGSFFLYSKLTVDKSRWQQGNVFSCS
		VMHEALHNHYTQKSLSLSPGK
SS-15194	150	TTMDMRVPAQLLGLLLLWLRGARCEVQLVESGGG
		LVQPGGSLRLSCAASGFTFSSYWMSWVRQAPGKG
		LEWVASIKQDGSEKYYVDSVKGRFTISRDNARNSL
		YLQMNSLRAEDTAVYYCARDLVLMVYDMDYYYY
		GMDVWGQGTTVTVSSASTKGPSVFPLAPCSRSTSE
		STAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPA
		VLQSSGLYSLSSVVTVPSSNFGTQTYTCNVDHKPSN
		TKVDKTVERKCCVECPPCPAPPVAGPSVFLFPPKPK
		DTLMISRTPEVTCVVVDVSHEDPEVQFNWYVDGVE
		VHNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGK
		EYKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPS
		REEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPEN
		NYKTTPPMLDSDGSFFLYSKLTVDKSRWQQGNVFS
		CSVMHEALHNHYTQKSLSLSPGK
SS-15195	151	MDMRVPAQLLGLLLLWLRGARCEVQLVESGGGLV
		QPGGSLRLSCAASGFTFSSYWMSWVRQAPGKGLE
		WVASIKQDGSEKYYVDSVKGRFTISRDNARNSLYL
		QMNSLRAEDTAVYYCARDLVLMVYDMDYYYYG
		MDVWGQGTTVTVSSASTKGPSVFPLAPCSRSTSEST
		AALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL
		QSSGLYSLSSVVTVPSSNFGTQTYTCNVDHKPSNTK
		VDKTVERKCCVECPPCPAPPVAGPSVFLFPPKPKDT
		LMISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEV
		HNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKE
		YKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPS
		REEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPEN
		NYKTTPPMLDSDGSFFLYSKLTVDKSRWQQGNVFS
		CSVMHEALHNHYTQKSLSLSPGK
SS-15196	152	MDMRVPAQLLGLLLLWLRGARCEVQLVESGGGLV
		QPGGSLRLSCAASGFTFSSYWMSWVRQAPGKGLE
		WVASIKQDGSEKYYVDSVKGRFTISRDNARNSLYL
		QMNSLRAEDTAVYYCARDLVLMVYDMDYYYYG
		MDVWGQGTTVTVSSASTKGPSVFPLAPCSRSTSEST
		AALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL
		QSSGLYSLSSVVTVPSSNFGTQTYTCNVDHKPSNTK
		VDKTVERKCCVECPPCPAPPVAGPSVFLFPPKPKDT
		LMISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEV
		HNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKE
		YKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPS
		REEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPEN
		NYKTTPPMLDSDGSFFLYSKLTVDKSRWQQGNVFS
		CSVMHEALHNHYTQKSLSLSPGK
SS-14894	153	TTMDMRVPAQLLGLLLLWLRGARCEVQLVESGGG
		LVQPGGSLRLSCAASGFTFSSYWMSWVRQAPGKG
		LEWVASIKQDGSEKYYVDSVKGRFTISRDNARNSL
		YLQMNSLRAEDTAVYYCARDLVLMVYDMDYYYY
		GMDVWGQGTTVTVSSASTKGPSVFPLAPCSRSTSE
		STAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPA
		VLQSSGLYSLSSVVTVPSSNFGTQTYTCNVDHKPSN
		TKVDKTVERKCCVECPPCPAPPVAGPSVFLFPPKPK
		DTLMISRTPEVTCVVVDVSHEDPEVQFNWYVDGVE
		VHNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGK
		EYKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPS
		REEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPEN
		NYKTTPPMLDSDGSFFLYSKLTVDKSRWQQGNVFS
		CSVMHEALHNHYTQKSLSLSPGK
SS-15504	154	MGSTAILGLLLAVLQGGRAEVQLVESGGGLVQPGG
		SLRLSCAASGFTFSSYWMSWVRQAPGKGLEWVASI
		KQDGSEKYYVDSVKGRFTISRDNARNSLYLQMNSL
		RAEDTAVYYCARDLVLSVYDMDYYYYGMDVWG
		QGTTVTVSSASTKGPSVFPLAPCSRSTSESTAALGCL
		VKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY
		SLSSVVTVPSSNFGTQTYTCNVDHKPSNTKVDKTV
		ERKCCVECPPCPAPPVAGPSVFLFPPKPKDTLMISRT
		PEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTK
		PREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVS
		NKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTK
		NQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTP
		PMLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMH
		EALHNHYTQKSLSLSPGK
SS-15494	155	MGSTAILGLLLAVLQGGRAEVQLVESGGGLVQPGG
		SLRLSCAASGFTFSSYWMSWVRQAPGKGLEWVASI
		KQDGSEKYYVDSVKGRFTISRDNARNSLYLQMNSL
		RAEDTAVYYCARDLVLFVYDMDYYYYGMDVWG
		QGTTVTVSSASTKGPSVFPLAPCSRSTSESTAALGCL
		VKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY
		SLSSVVTVPSSNFGTQTYTCNVDHKPSNTKVDKTV
		ERKCCVECPPCPAPPVAGPSVFLFPPKPKDTLMISRT
		PEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTK
		PREEQFNSTFRAVVSVLTVVHQDWLNGKEYKCKVS
		NKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTK
		NQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTP
		PMLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMH
		EALHNHYTQKSLSLSPGK
SS-14892	156	MDMRVPAQLLGLLLLWLRGARCEVQLVESGGGLN
		QPGGSLRLSCAASGFTFSSYWMSWVRQAPGKGLE
		WVASIKQDGSEKYYVDSVKGRFTISRDNARNSLYL
		QMNSLRAEDTAVYYCARDLVLMVYDMDYYYYG
		MDVWGQGTTVTVSSASTKGPSVFPLAPCSRSTSEST
		AALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL
		QSSGLYSLSSVVTVPSSNFGTQTYTCNVDHKPSNTK
		VDKTVERKCCVECPPCPAPPVAGPSVFLFPPKPKDT
		LMISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEV
		HNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKE
		YKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPS
		REEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPEN
		NYKTTPPMLDSDGSFFLYSKLTVDKSRWQQGNVFS
		CSVMHEALHNHYTQKSLSLSPGK
SS-15495	157	MGSTAILGLLLAVLQGGRAEVQLVESGGGLVQPGG
		SLRLSCAASGFTFSSYWMSWVRQAPGKGLEWVASI
		KQDGSEKYYVDSVKGRFTISRDNARNSLYLQMNSL
		RAEDTAVYYCARDLVLFVYDMDYYYYGMDVWG
		QGTTVTVSSASTKGPSVFPLAPCSRSTSESTAALGCL
		VKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY
		SLSSVVTVPSSNFGTQTYTCNVDHKPSNTKVDKTV
		ERKCCVECPPCPAPPVAGPSVFLFPPKPKDTLMISRT
		PEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTK
		PREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVS
		NKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTK
		NQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTP
		PMLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMH
		EALHNHYTQKSLSLSPGK
SS-15496	158	MDMRVPAQLLGLLLLWLRGARCEVQLVESGGGLV
		QPGGSLRLSCAASGFTFSSYWMSWVRQAPGKGLE
		WVASIKQDGSEKYYVDSVKGRFTISRDNARNSLYL
		QMNSLRAEDTAVYYCARDLYLMVYDMDYYYYG
		MDVWGQGTTVTSSASTKGPSVFPLAPCSRSTSEST
		AALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL
		QSSGLYSLSSVVTVPSSNFGTQTYTCNVDHKPSNTK
		VDKTVERKCCVECPPCPAPPVAGPSVFLFPPKPKDT
		LMISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEV
		HNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKE
		YKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPS
		REEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPEN
		NYKTTPPMLDSDGSFFLYSKLTVDKSRWQQGNVFS
		CSVMHEALHNHYTQKSLSLSPGK
SS-15497	159	MGSTAILGLLLAVLQGGRAEVQLVESGGGLVQPGG
		SLRLSCAASGFTFSSYWMSWVRQAPGKGLEWVASI
		KQDGSEKYYVDSVKGRFTISRDNARNSLYLQMNSL
		RAEDTAVYYCARDLVLSVYDMDYYYYGMDVWG
		QGTTVTVSSASTKGPSVFPLAPCSRSTSESTAALGCL
		VKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY
		SLSSVVTVPSSNFGTQTYTCNVDHKPSNTKVDKTV
		ERKCCVECPPCPAPPVAGPSVFLFPPKPKDTLMISRT
		PEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTK
		PREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVS
		NKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTK
		NQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTP
		PMLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMH
		EALHNHYTQKSLSLSPGK
SS-15503	160	MGSTAILGLLLAVLQGGRAEVQLVESGGGL
		VQPGGSLRLSCAASGFTFSSYWMSWVRQAP
		GKGLEWVASIKQDGSEKYYVDSVKGRFTISR
		DNARNSLYLQMNSLRAEDTAVYYCARDLVL
		SVYDMDYYYYGMDVWGQGTTVTVSSASTK
		GPSVFPLAPCSRSTSESTAALGCLVKDYFPEP
		VTVSWNSGALTSGVHTFPAVLQSSGLYSLSS
		VVTVPSSNFGTQTYTCNVDHKPSNTKVDKT
		VERKCCVECPPCPAPPVAGPSVFLFPPKPKD
		TLMISRTPEVTCVVVDVSHEDPEVQFNWYV
		DGVEVHNAKTKPREEQFNSTFRVVSVLYVV
		HQDWLNGKEYKCKVSNKGLPAPIEKTISKT
		KGQPREPQVYTLPPSREEMTKNQVSLTCLV
		KGFYPSDIAVEWESNGQPENNYKTTPPMLDS
		DGSFFLYSKLTVDKSRWQQGNVFSCSVMHE
		ALHNHYTQKSLSLSPGK
SS-15505	161	MGSTAILGLLLAVLQGGRAEVQLVESGGGL
		VQPGGSLRLSCSAAGFTFSSYWMSWVRQAP
		GKGLEWVASIKQDGSEKYYVDSVKGRFTISR
		DNARNSLYLQMNSLRAEDTAVYYCARDLVL
		FVYDMDYYYYGMDVWGQGTTVTVSSASTK
		GPSVFPLAPCSRSTSESTAALGCLVKDYFPEP
		VTVSWNSGALTSGVHTFPAVLQSSGLYSLSS
		VVTVPSSNFGTQTYTCNVDHKPSNTKVDKT
		VERKCCVECPPCPAPPVAGPSVFLFPPKPKD
		TLMISRTPEVTCVVVDVSHEDPEVQFNWYV
		DGVEVHNAKTKPREEQFNSTFRVVSVLTVV
		HQDWLNGKEYKCKVSNKGLPAPIEKTISKT
		KGQPREPQVYTLPPSREEMTKNQVSLTCLV
		KGFYPSDIAVEWESNGQPENNYKTTPPMLDS
		DGSFFLYSKLTVDKSRWQQGNVFSCSVMHE
		ALHNHYTQKSLSLSPGK
SS-15506	162	MGSTAILGLLLAVLQGGRAEVQLVESGGGLVQPGG
		SLRLSCAASGFTFSSYWMSWVRQAPGKGLEWVASI
		KQDGSEKYYVDSVKGRFTISRDNARNSLYLQMNSL
		RAEDTAVYYCARDLVLNVYDMDYYYYGMDVWG
		QGTTVTVSSASTKGPSVFPLAPCSRSTSESTAALGCL
		VKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY
		SLSSVVTVPSSNFGTQTYTCNVDHKPSNTKVDKTV
		ERKCCVECPPCPAPPVAGPSVFLFPPKPKDTLMISRT
		PEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTK
		PREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVS
		NKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTK
		NQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTP
		PMLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMH
		EALHNHYTQKSLSLSPGK
SS-15507	163	MDMRVPAQLLGLLLLWLRGARCEVQLVESGGGLV
		QPGGSLRLSCAASGFTFSSYWMSWVRQAPGKGLE
		WVASIKQDGSEKYYVDSVKGRFTISRDNARNSLYL
		QMNSLRAEDTAVYYCARDLVLMVYDIDYYYYGM
		DVWGQGTTVTVSSASTKGPSVFPLAPCSRSTSESTA
		ALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQ
		SSGLYSLSSVVTVPSSNFGTQTYTCNVDHKPSNTKV
		DKTVERKCCVECPPCPAPPVAGPSVFLFPPKPKDTL
		MISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEVH
		NAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKEY
		KCKVSNKGLPAPIEKTISKPKGQPREPQVYTLPPSRE
		EMTKNQVSLCLVKGFYPSDIAVEWESNGQPENNY
		KTTPPMLDSDGSFFLYSKLTVDKSRWQQGNVFSCS
		VMHEALHNHYTQKSLSLSPGK
SS-15502	164	MGSTAILGLLLAVLQGGRAEVQLVESGGGLVQPGG
		SLRLSCAASGFTFSSYWMSWVRQAPGKGLEWVASI
		KQDGSEKYYVDSVKGRFTISRDNARNSLYLQMNSL
		RAEDTAVYYCARDLVLNVYDMDYYYYGMDVWG
		QGTTVTVSSASTKGPSVFPLAPCSRSTSESTAALGCL
		VKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY
		SLSSVVTVPSSNFGTQTYTCNVDHKPSNTKVDKTV
		ERKCCVECPPCPAPPVAGPSVFLFPPKPKDTLMISRT
		PEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTK
		PREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVS
		NKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTK
		NQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTP
		PMLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMH
		EALHNHYTQKSLSLSPGK
SS-15508	165	MDMRVPAQLLGLLLLWLRGARCEVQLVESGGGLV
		QPGGSLRLSCAASGFTFSSYWMSWVRQAPGKGLE
		WVASIKQDGSEKYYVDSVKGRFTISRDNARNSLYL
		QMNSLRAEDTAVYYCARDLVLMVYDIDYYYYGM
		DVWGQGTTVTVSSASTKGPSVFPLAPCSRSTSESTA
		ALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQ
		SSGLYSLSSVVTVPSSNFGTQTYTCNVDHKPSNTKV
		DKTVERKCCVECPPCPAPPVAGPSVFLFPPKPKDTL
		MISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEVH
		NAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKEY
		KCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPSRE
		EMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNY
		KTTPPMLDSDGSFFLYSKLTVDKSRWQQGNVFSCS
		VMHEALHNHYTQKSLSLSPGK
SS-15501	166	MGSTAILGLLLAVLQGGRAEVQLVESGGGLVQPGG
		SLRLSCAASGFTFSSYWMSWVRQAPGKGLEWVASI
		KQDGSEKYYVDSVKGRFTISRDNARNSLYLQMNSL
		RAEDTAVYYCARDLVLSVYDMDYYYYGMDVWG
		QGTTVTVSSASTKGPSVFPLAPCSRSTSESTAALGCL
		VKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY
		SLSSVVTVPSSNFGTQTYTCNVDHKPSNTKVDKTV
		ERKCCVECPPCPAPPVAGPSVFLFPPKPKDTLMISRT
		PEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTK
		PREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVS
		NKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTK
		NQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTP
		PMLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMH
		EALHNHYTQKSLSLSPGK
SS-15500	167	MGSTAILGLLLAVLQGGRAEVQLVESGGGLVQPGG
		SLRLSCAASGFTFSSYWMSWVRQAPGKGLEWVASI
		KQDGSEKYYVDSVKGRFTISRDNARNSLYLQMNSL
		RAEDTAVYYCARDLVLNVYDMDYYYYGMDVWG
		QGTTVTVSSASTKGPSVFPLAPCSRSTSESTAALGCL
		VKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY
		SLSSVVTVPSSNFGTQTYTCNVDHKPSNTKVDKTV
		ERKCCVECPPCPAPPVAGPSVFLFPPKPKDTLMISRT
		PEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTK
		PREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVS
		NKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTK
		NQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTP
		PMLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMH
		EALHNHYTQKSLSLSPGK
SS-15003	168	MEFGLSWVFLVALLRGVQCEVHLVESGGGVVQPG
		RSLRLSCAASGFTFNSFGMHWVRQAPGKGLEWVA
		LIWSDGSDEYYADSVKGRFTISRDNSKNTLYLQMN
		SLRAEDTAVYYCARAIAALYYYYGMDVWGQGTT
		VTVSSASTKGPSVFPLAPCSRSTSESTAALGCLVKD
		YFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSS
		VVTVPSSNFGTQTYTCNVDHKPSNTKVDKTVERKC
		CVECPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVT
		CVVVDVSHEDPEVQFNWYVDGVEVHNAKTKPREE
		QFNSTFRVVSVLTVVHQDWLNGKEYKCKVSNKGL
		PAPIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSL
		TCLVKGFYPSDIAVEWESNGQPENNYKTTPPMLDS
		DGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHN
		HYTQKSLSLSPGK
SS-15005	169	MGSTAILGLLLAVLQGGRAEVQLLESGGGLVQPGG
		SLRLSCAASGFTFSSYAMNWVRQAPGKGLEWVSTI
		SGSGGNTYYADSVKGRFTISRDNSKNTLYLQMNSL
		RAEDTAVYYCAKKFVLMVYAMLDYWGQGTLVTV
		SSASTKGPSVFPLAPCSRSTSESTAALGCLVKDYFPE
		PVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVT
		VPSSNFGTQTYTCNVDHKPSNTKVDKTVERKCCVE
		CPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVV
		VDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQFN
		STFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPAPI
		EKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCL
		VKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGS
		FFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYT
		QKSLSLSPGK
SS-15757	170	MDMRVPAQLLGLLLLWLRGARCEVQLVESGGGLV
(P1F4)		QPGGSLRLSCAASGFTFSSYWMSWVRQAPGKGLE
		WVASIKQDGSEKYYVDSVKGRFTISRDNARNSLYL
		QMNSLRAEDTAVYYCARDLVLMVYDIDYYYYGM
		DVWGQGTTVTVSSASTKGPSVFPLAPCSRSTSESTA
		ALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQ
		SSGLYSLSSVVTVPSSNFGTQTYTCNVDHKPSNTKV
		DKTVERKCCVECPPCPAPPVAGPSVFLFPPKPKDTL
		MISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEVH
		NAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKEY
		KCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPSRE
		EMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNY
		KTTPPMLDSDGSFFLYSKLTVDKSRWQQGNVFSCS
		VMHEALHNHYTQKSLSLSPGK
SS-15758	171	MDMRVPAQLLGLLLLWLRGARCEVQLVESGGGLV
(P1B6)		QPGGSLRLSCAASGFTFSSYWMSWVRQAPGKGLE
		WVASIKQDGSEKYYVDSVKGRFTISRDNARNSLYL
		QMNSLRAEDTAVYYCARDLVLMVYDLDYYYYGM
		DVWGQGTTVTVSSASTKGPSVFPLAPCSRSTSESTA
		ALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQ
		SSGLYSLSSVVTVPSSNFGTQTYTCNVDHKPSNTKV
		DKTVERKCCVECPPCPAPPVAGPSVFLFPPKPKDTL
		MISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEVH
		NAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKEY
		KCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPSRE
		EMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNY
		KTTPPMLDSDGSFFLYSKLTVDKSRWQQGNVFSCS
		VMHEALHNHYTQKSLSLSPGK
SS-15759	172	MDMRVPAQLLGLLLLWLRGARCEVQLVESGGGLV
(P2F4)		QPGGSLRLSCAASGFTFSSYWMSWVRQAPGKGLE
		WVASIKQDGSEKYYVDSVKGRFTISRDNARNSLYL
		QMNSLRAEDTAVYYCARDLVLMVYDMDYYYYG
		MDVWGQGTTVTVSSASTKGPSVFPLAPCSRSTSEST
		AALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL
		QSSGLYSLSSVVTVPSSNFGTQTYTCNVDHKPSNTK
		VDKTVERKCCVECPPCPAPPVAGPSVFLFPPKPKDT
		LMISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEV
		HNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKE
		YKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPS
		REEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPEN
		NYKTTPPMLDSDGSFFLYSKLTVDKSRWQQGNVFS
		CSVMHEALHNHYTQKSLSLSPGK
SS-15761	173	MDMRVPAQLLGLLLLWLRGARCEVQLVESGGGLV
(P2G5)		QPGGSLRLSCAASGFTFSSYWMSWVRQAPGKGLE
		WVASIKQDGSEKYYVDSVKGRFTISRDNARNSLYL
		QMNSLRAEDTAVYYCARDLVLMVYDMDYYYYG
		MDVWGQGTTVTVSSASTKGPSVFPLAPCSRSTSEST
		AALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL
		QSSGLYSLSSVVTVPSSNFGTQTYTCNVDHKPSNTK
		VDKTVERKCCVECPPCPAPPVAGPSVFLFPPKPKDT
		LMISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEV
		HNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKE
		YKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPS
		REEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPEN
		NYKTTPPMLDSDGSFFLYSKLTVDKSRWQQGNVFS
		CSVMHEALHNHYTQKSLSLSPGK
SS-15763	174	MDMRVPAQLLGLLLLWLRGARCEVQLVESGGGLV
(P2H7)		QPGGSLRLSCAASGFTFSSYWMSWVRQAPGKGLE
		WVASIKQDGSEKYYVDSVKGRFFISRDNARNSLYL
		QMNSLRAEDTAVYYCARDLVLMVYDMDYYYYG
		MDVWGQGTTVTVSSASTKGPSVFPLAPCSRSTSEST
		AALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL
		QSSGLYSLSSVVTVPSSNFGTQTYTCNVDHKPSNTK
		VDKTVERKCCVECPPCPAPPVAGPSVFLFPPKPKDT
		LMISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEV
		HNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKE
		YKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPS
		REEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPEN
		NYKTTPPMLDSDGSFFLYSKLTVDKSRWQQGNVFS
		CSVMHEALHNHYTQKSLSLSPGK
SS-15764	175	MDMRVPAQLLGLLLLWLRGARCEVQLVESGGGLV
(P2H8)		QPGGSLRLSCAASGFTFSSYWMSWVRQAPGKGLE
		WVASIKQDGSEKYYVDSVKGRFTISRDNARNSLYL
		QMNSLRAEDTAVYYCARDLVLMVYDMDYYYYG
		MDVWGQGTTVTVSSASTKGPSVFPLAPCSRSTSEST
		AALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL
		QSSGLYSLSSVVTVPSSNFGTQTYTCNVDHKPSNTK
		VDKTVERKCCVECPPCPAPPVAGPSVFLFPPKPKDT
		LMISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEV
		HNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKE
		YKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPS
		REEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPEN
		NYKTTPPMLDSDGSFFLYSKLTVDKSRWQQGNVFS
		CSVMHEALHNHYTQKSLSLSPGK