Activatable cytokine polypeptides and methods of use thereof

ACTIVATABLE CYTOKINE POLYPEPTIDES AND METHODS OF USE THEREOF

[1] This present application claims the benefit of U.S. Provisional Application No. 62/935,605 filed on November 14,2019, the entire teachings of which are incorporated herein by reference.

SEQUENCE LISTING

[2] The instant application contains a Sequence Listing which has been submitted electronically in ASCII format and is hereby incorporated by reference in its entirety. Said ASCII copy, created on November 12,2020, is named 761146_000146_SL.txt and is 2,974,211 bytes in size.

BACKGROUND

[3] The development of mature immunocompetent lymphoid cells from less-committed precursors, their subsequent antigen-driven immune responses, and the suppression of these and unwanted autoreactive responses are highly dependent and regulated by cytokines (including interleukin-2 [IL-2], IL-4, IL-7, IL-9, IL-15, and IL-21) that utilize receptors in the common γ-chain (yc) family (Rochman et al., 2009) and family members including IL-12, 18 and 23. IL-2 is essential for thymic development of Treg cells and critically regulates several key aspects of mature peripheral Treg and antigen-activated conventional T cells. Because of its potent T cell growth factor activity in vitro, IL-2 has been extensively studied in part because this activity offered a potential means to directly boost immunity, e.g., in cancer and AIDS-HIV patients, or a target to antagonize unwanted responses, e.g., transplantation rejection and autoimmune diseases. Although in vitro studies with IL-2 provided a strong rationale for these studies, the function of IL-2 in vivo is clearly much more complex as first illustrated in IL deficient mice, where a rapid lethal autoimmune syndrome, not lack of immunity, was observed (Sadlack et al., 1993,1995). Similar observations were later made when the gene encoding IL-2Ra (I12ra) and IL-2Rp (I12rb) were individually ablated (Suzuki et al., 1995; Willerford et al., 1995).

[4] The present invention refers to conditionally active and/or targeted cytokines for use in the treatment of cancer and other diseases dependent on immune up or down regulation. For example, the antitumoral activity of some cytokines is well known and described and some cytokines have already been used therapeutically in humans. Cytokines such as interleukin-2 (IL-2) and interferon a (IFNa) have shown positive antitumoral activity in patients with different types of tumors, such as kidney metastatic carcinoma, hairy cell leukemia, Kaposi sarcoma, melanoma, multiple myeloma, and the like. Other cytokines like ΙΡΝβ, the Tumor Necrosis Factor (TNF) a, ΤΝΡβ, IL-1,4, 6, 12, 15 and the CSFs have shown a certain antitumoral activity on some types of tumors and therefore are the object of further studies.

SUMMARY

[5] Provided herein are therapeutic proteins, nucleic acids (e.g., DNA, RNA, mRNA) that encode the proteins, and compositions and methods of using the proteins and nucleic acids for the treatment of a disease or disorder, such as proliferative disease, a tumorous disease, an inflammatory disease, an immunological disorder, an autoimmune disease, an infectious disease, a viral disease, an allergic reaction, a parasitic reaction, graft-versus-host disease and the like. In certain embodiments, the fusion protein the amino acid sequence of any one of SEQ ID NOs.: 193-271. Certain fusion proteins disclosed herein are referred to as ACP200-208, ACP211, ACP213-ACP215, ACP240-ACP245, ACP247, ACP284-ACP292, ACP296-ACP300, ACP302-ACP306, ACP309-ACP314, ACP336ACP359, ACP371-ACP379, ACP383-ACP434, ACP439-ACP447, or ACP451-ACP471. This disclosure also relates to nucleic acids (e.g., DNA, RNA, mRNA) that encode the fusion proteins, methods of making fusion proteins, compositions comprising a fusion protein, as well as methods of using the fusion proteins to treat cancer including combination of two or more fusion proteins and one or more fusion protein in combination with another therapeutic agent.

[6] The invention features fusion proteins that are conditionally active variants of a cytokine of interest. Cytokines of particular interest include IL-2, IL-12, and IFN. In one aspect, the full-length polypeptides of the invention have reduced or minimal cytokine-receptor activating activity even though they contain a functional cytokine polypeptide. Upon activation, e.g., by cleavage of a linker that joins a blocking moiety, e.g. a steric blocking polypeptide, in sequence to the active cytokine, the cytokine, e.g., IL-2, IL-7, IL-12, IL-15, IL-18, IL-21, IL-23, IFNalpha, IFNbeta, IFNgamma, TNFalpha, lymphotoxin, TGF-betal, TGFbeta2, TGFbeta3, GM-CSF, CXCL10, CCL19, CCL20, CCL21 or functional fragment or mutein or functional variant or a subunit of any of the foregoing, can bind its receptor and effect signaling. If desired, the full-length polypeptides can include a blocking polypeptide moiety that also provides additional advantageous properties. For example, the full-length polypeptide can contain a blocking polypeptide moiety that also extends the serum half-life and/or targets the full-length polypeptide to a desired site of cytokine activity. Alternatively, the fulllength fusion polypeptides can contain a serum half-life extension element and/or targeting domain that are distinct from the blocking polypeptide moiety. Preferably, the fusion protein contains at least one element or domain capable of extending in vivo circulating half-life. Preferably, this element is removed enzymatically in the desired body location (e.g. protease cleavage in the tumor microenvironment), restoring pharmacokinetic properties to the payload molecule (e.g. IL2, IL-12, IFNb or IFNa) substantially similar to the naturally occurring payload molecule. The fusion proteins may be targeted to a desired cell or tissue.

[7] The fusion polypeptides typically comprise a cytokine polypeptide [A], a blocking moiety [D], optionally a half-life extension moiety [H], and a protease-cleavable polypeptide linker. The cytokine polypeptide and the blocking moiety and the optional half-life extension element when

present are operably linked by the protease-cleavable polypeptide linker and the fusion polypeptide has attenuated cytokine receptor activating activity, e.g., the cytokine-receptor activating activity of the fusion polypeptide is at least about 10X less than the cytokine receptor activating activity of the polypeptide that contains the cytokine polypeptide that is produced by cleavage of the protease cleavable linker. Some preferred fusion polypeptides are of one of formula (I) - (VI): [A]-[L1]-[H]-[L2]-[D] (I);

[D]-[L2]-[H]-[L1]-[A] (II);

[A]-[L1]-[D]-[L2]-[H] (III);

[H]-[L2]-[D]-[L1]-[A] (IV);

[H]-[L1]-[A]-[L2’]-[D] (V);

[D]-[L1]-[A]-[L2’]-[H] (VI);

wherein A is a cytokine polypeptide, D is a blocking moiety, H is a half-life extension moiety, LI is a protease-cleavable polypeptide linker, L2 is an polypeptide linker that is optionally proteasecleavable, and L2’ is a protease-cleavable polypeptide linker. LI and L2 or LI and L2’ can be have the same or different amino acid sequence and or protease-cleavage site (when L2 is proteasecleavable) as desired.

[8] In some aspects, the fusion proteins described herein are conditionally active variants of IL12, IL-2, or IFN. In embodiments, the fusion protein can contain an IL-2 polypeptide. The fusion protein containing an IL-2 polypeptide can comprise or consist of the amino acid sequence of SEQ ID NOs. 257-300, 302-317, 325-353, 355-365, 366,372-381, 383-385, 388-420, 579-608, and 636-646. The fusion proteins disclosed as SEQ ID NOs. 257-300, 302-317, 325-353,355-365, 366, 372-381, 383-385, 388-420, 579-608, 636-646 are referred to herein as ACP289-ACP292, ACP296-ACP302, WW0301, ACP304-ACP306, ACP309-ACP313, WW0353, ACP414, ACP336-ACP398, WW0472WW0477, ACP406-ACP426, ACP439-ACP447, ACP451-ACP471, WW0729, WW0734-WW0792, ACP101, ACP293-ACP295, ACP316-ACP335, ACP427-ACP438, and ACP448-ACP450. For example, the fusion protein can comprise the amino acid sequence of SEQ ID NO: 272. The fusion protein can comprise the amino acid sequence of SEQ ID NO: 286. The fusion protein can comprise the amino acid sequence of SEQ ID NO:362. The fusion protein can comprise the amino acid sequence of SEQ ID NO:336. The fusion protein can comprise the amino acid sequence of SEQ ID NO: 348. The fusion protein can comprise the amino acid sequence of SEQ ID NO: 363. The fusion protein can comprise the amino acid sequence of SEQ ID NO: 580.

[9] In embodiments, the fusion protein can contain IL-12. The fusion protein containing an IL-12 polypeptide can comprise or consist of the amino acid sequence of any one of SEQ ID NOs. 368-371, 434-440,453-519, or 523-538. The fusion proteins disclosed as SEQ ID NOs. 368-371,434-440,453519, or 523-538 are referred to herein as ACP240-ACP245, ACP247, ACP285-ACP288, WW0641, WW0649-WW0652, WW0662-WW0725, WW0765-WW0772, and WW0796-WW0803. For

example, the fusion protein can comprise the amino acid sequence of SEQ ID NO: 424. For example, the fusion protein can comprise the amino acid sequence of SEQ ID NO: 428. For example, the fusion protein can comprise the amino acid sequence of SEQ ID NO: 541. For example, the fusion protein can comprise the amino acid sequence of SEQ ID NO: 556. For example, the fusion protein can comprise the amino acid sequence of SEQ ID NO: 560. For example, the fusion protein can comprise the amino acid sequence of SEQ ID NO: 568. For example, the fusion protein can comprise the amino acid sequence of SEQ ID NO: 573.

[10] In embodiments, the fusion protein contains IFN. The fusion protein containing an IFN polypeptide can comprise or consist of the amino acid sequence of any one of SEQ ID NOs. 421-430, and 539-578. The fusion proteins disclosed as SEQ ID NOs. 421-430, and 539-578 can be referred to herein as ACP200-ACP209, WW0644-WW0648, WW0781-WW0786, WW0815-WW0822, WW0831-WW0834, WW0737-WW0748, and WW0787-WW0790.

[11] In some aspects, the fusion polypeptide disclosed herein can be covalently or non-covalently bonded to a second polypeptide chain. For example, a fusion polypeptide can dimerize (i.e. form a dimer) or a portion of a fusion polypeptide may associate with another polypeptide, for example, to form a functional binding site for a cytokine polypeptide or serum albumin. In certain embodiments, the second polypeptide chain and the blocking moiety on the fusion polypeptide are complementary and together form a functional binding site that has specificity for the cytokine polypeptide contained in the fusion polypeptide. Exemplary functional binding sites that can be formed by the blocking moiety of the fusion polypeptide and a complimentary second polypeptide include antigen binding sites of antibodies, such as a Fab fragment of an antibody or a portion thereof. For example, one chain of a Fab that binds the cytokine can be the blocking moiety of the fusion polypeptide, e.g., a VH-CH1, and the complementary VL-CL can be part of the second polypeptide. In such situations, the blocking moiety of the fusion protein i.e., VH-CH1 and the second polypeptide that comprises the complementary VL-CL, can associate to form a functional binding site with specificity for the cytokine polypeptide contained within the fusion protein (e.g., IL-2, IL-12, IFNalpha, IFNbeta) and attenuate cytokine polypeptide activity.

[12] In embodiments, the fusion protein containing an IL-2 cytokine polypeptide can be bonded covalently or noncovalently to a second polypeptide chain. The second polypeptide chain can contain an antibody light chain VL-CL that comprises or consists of the amino acid sequence of SEQ ID NO: 263,264, or 333. Such a second polypeptide can bond with a complimentary VH-CH1 polypeptide contained within the fusion protein, e.g., as contained within SEQ ID NOS: 362,363, 325,286, 579, 581, or 582. The second polypeptide chain disclosed as SEQ ID NOs. 263,264, and 333 can be referred herein as WW0523 (ACP381), WW0524 (ACP382), or WW0556 (ACP414).

[13] In embodiments, the fusion polypeptide can comprise or consist of the amino acid sequence of SEQ ID NOs. 362, 363, 325,286, 579, 581, or 582 and the second polypeptide chain can comprise

or consist of the amino acid sequence of SEQ ID NOs: 263,264, or 333. The fusion polypeptide disclosed as SEQ ID NOs. 362, 363, 325,286, 579, 581, or 582 can be referred to as WW0520 (ACP378), WW0521 (ACP379), WW0548 (ACP406), WW0621 (ACP457), WW0729, WW0735, or WW0736, and the second polypeptide chain disclosed as SEQ ID NOs. 263,264, and 333 can be referred herein as WW0523 (ACP381), WW0524 (ACP382), or WW0556 (ACP414). For example, the fusion protein can comprise or consist the amino acid sequence of SEQ ID NO: 362 and the second polypeptide chain can comprise or consist the amino acid sequence of SEQ ID NO: 263. For example, the fusion protein can comprise or consist the amino acid sequence of SEQ ID NO: 362 and the second polypeptide chain can comprise or consist the amino acid sequence of SEQ ID NO: 264. For example, the fusion protein can comprise or consist the amino acid sequence of SEQ ID NO: 362 and the second polypeptide chain can comprise or consist the amino acid sequence of SEQ ID NO: 333. For example, the fusion protein can comprise or consist of an amino acid sequence of SEQ ID NO: 363 and the second polypeptide chain can comprise or consist of an amino acid sequence of SEQ ID NO: 263. For example, the fusion protein can comprise or consist of an amino acid sequence of SEQ ID No. 363 and the second polypeptide chain can comprise or consist of an amino acid sequence of SEQ ID NO: 264. For example, the fusion protein can comprise or consist of an amino acid sequence of SEQ ID NO: 363 and the second polypeptide chain can comprise or consist of an amino acid sequence of SEQ ID NO: 333. For example, the fusion protein can comprise or consist of an amino acid sequence of SEQ ID NO: 325 and the second polypeptide chain can comprise or consist of an amino acid sequence of SEQ ID NO: 264. For example, the fusion protein can comprise or consist of an amino acid sequence of SEQ ID NO: 325 and the second polypeptide chain can comprise or consist of an amino acid sequence of SEQ ID NO: 333. For example, the fusion protein can comprise or consist of an amino acid sequence of SEQ ID NO: 325 and the second polypeptide chain can comprise or consist of an amino acid sequence of SEQ ID NO: 263. For example, the fusion protein can comprise or consist of an amino acid sequence of SEQ ID NO: 286 and the second polypeptide chain can comprise or consist of an amino acid sequence of SEQ ID NO: 263. For example, the fusion protein can comprise or consist of an amino acid sequence of SEQ ID NO: 286 and the second polypeptide chain can comprise or consist of an amino acid sequence of SEQ ID NO: 264. For example, the fusion protein can comprise or consist of an amino acid sequence of SEQ ID NO: 286, and the second polypeptide can comprise or consist of an amino acid sequence of SEW ID NO: 333. For example, the fusion protein can comprise or consist of an amino acid sequence of SEQ ID NO: 579 and the second polypeptide chain can comprise or consist of an amino acid sequence of SEQ ID NO: 263. For example, the fusion protein can comprise or consist of an amino acid sequence of SEQ ID NO: 579 and the second polypeptide chain can comprise or consist of an amino acid sequence of SEQ ID NO: 264. For example, the fusion protein can comprise or consist of an amino acid sequence of SEQ ID NO: 579 and the second polypeptide chain can comprise or consist of an amino acid

sequence of SEQ ID NO: 233. For example, the fusion protein can comprise or consist of SEQ ID NO: 581 and the second polypeptide chain can comprise or consist of SEQ ID NO.: 263. For example, the fusion protein can comprise or consist of SEQ ID NO: 581 and the second polypeptide chain can comprise or consist of SEQ ID NO.: 264. For example, the fusion protein can comprise or consist of SEQ ID NO: 581 and the second polypeptide chain can comprise or consist of SEQ ID NO.: 333. For example, the fusion protein can comprise or consist of SEQ ID NO: 582 and the second polypeptide chain can comprise or consist of SEQ ID NO: 263. For example, the fusion protein can comprise or consist of SEQ ID NO: 582 and the second polypeptide chain can comprise or consist of SEQ ID NO: 264. For example, the fusion protein can comprise or consist of SEQ ID NO: 582 and the second polypeptide chain can comprise or consist of SEQ ID NO: 333.

[14] As described herein targeting is accomplished through the action of a blocking polypeptide moiety that also binds to a desired target, or through a targeting domain. The domain that recognizes a target antigen on a preferred target (for example a tumor-specific antigen), may be attached to the cytokine via a cleavable or non-cleavable linker. If attached by a non-cleavable linker, the targeting domain may further aid in retaining the cytokine in the tumor, and it may be considered a retention domain. The targeting domain does not necessarily need to be directly linked to the payload molecule, and it may be linked directly to another element of the fusion protein. This is especially true if the targeting domain is attached via a cleavable linker.

[15] In one aspect is provided a fusion polypeptide comprising a cytokine polypeptide, or functional fragment, a mutein thereof, a functional variant thereof or a subunit thereof, and a blocking moiety, e.g. a steric blocking domain. The blocking moiety is fused to the cytokine polypeptide, directly or through a linker, and can be separated from the cytokine polypeptide by cleavage (e.g., protease mediated cleavage) of the fusion polypeptide at or near the fusion site or linker or in the blocking moiety. For example, when the cytokine polypeptide is fused to a blocking moiety through a linker that contains a protease cleavage site, the cytokine polypeptide is released from the blocking moiety and can bind its receptor, upon protease mediated cleavage of the linker. The linker is designed to be cleaved at the site of desired cytokine activity, for example in the tumor microenvironment, avoiding off-target cytokine activity and reducing overall toxicity of cytokine therapy.

[16] The blocking moiety can also function as a serum half-life extension element. In some embodiments, the fusion polypeptide further comprises a separate serum half-life extension element. In some embodiments, the fusion polypeptide further comprises a targeting domain. In various embodiments, the serum half-life extension element is a water-soluble polypeptide such as optionally branched or multi- armed polyethylene glycol (PEG), full length human serum albumin (HSA) or a fragment that preserves binding to FcRn, an Fc fragment, or a nanobody that binds to FcRn directly or to human serum albumin.

[17] In addition to serum half-life extension elements, the pharmaceutical compositions described herein preferably comprise at least one, or more targeting domains that bind to one or more target antigens or one or more regions on a single target antigen. It is contemplated herein that a polypeptide construct of the invention is cleaved, for example, in a disease-specific microenvironment or in the blood of a subject at the protease cleavage site and that the targeting domain(s) will bind to a target antigen on a target cell. At least one target antigen is involved in and/or associated with a disease, disorder or condition. Exemplary target antigens include those associated with a proliferative disease, a tumorous disease, an inflammatory disease, an immunological disorder, an autoimmune disease, an infectious disease, a viral disease, an allergic reaction, a parasitic reaction, a graft-versus-host disease or a host-versus-graft disease.

[18] In some embodiments, a target antigen is a cell surface molecule such as a protein, lipid or polysaccharide. In some embodiments, a target antigen is a on a tumor cell, virally infected cell, bacterially infected cell, damaged red blood cell, arterial plaque cell, or fibrotic tissue cell.

[19] Target antigens, in some cases, are expressed on the surface of a diseased cell or tissue, for example a tumor or a cancer cell. Target antigens for tumors include but are not limited to Fibroblast activation protein alpha (FAPa), Trophoblast glycoprotein (5T4), Tumor-associated calcium signal transducer 2 (Trop2), Fibronectin EDB (EDB-FN), fibronectin EIIIB domain, CGS-2, EpCAM, EGFR, HER-2, HER-3, c-Met, FOLRI, FAP, and CEA. Pharmaceutical compositions disclosed herein, also include proteins comprising two antigen binding domains that bind to two different target antigens known to be expressed on a diseased cell or tissue. Exemplary pairs of antigen binding domains include but are not limited to EGFR/CEA, EpCAM/CEA, and HER-2/HER-3.

[20] In some embodiments, the targeting polypeptides independently comprise a scFv, a VH domain, a VL domain, a non-Ig domain, or a ligand that specifically binds to the target antigen. In some embodiments, the targeting polypeptides specifically bind to a cell surface molecule. In some embodiments, the targeting polypeptides specifically bind to a tumor antigen. In some embodiments, the targeting polypeptides specifically and independently bind to a tumor antigen selected from at least one of EpCAM, EGFR, HER-2, HER-3, cMet, CEA, and FOLRI. In some embodiments, the targeting polypeptides specifically and independently bind to two different antigens, wherein at least one of the antigens is a tumor antigen selected from EpCAM, EGFR, HER-2, HER-3, cMet, CEA, and FOLRI. In some embodiments, the targeting polypeptide serves as a retention domain and is attached to the cytokine via a non-cleavable linker.

[21] As described herein, the cytokine blocking moiety can bind to the cytokine and thereby block activation of the cognate receptor of the cytokine.

[22] This disclosure also related to nucleic acids, e.g., DNA, RNA, mRNA, that encode the conditionally active proteins described herein, as well as vectors and host cells that contain such nucleic acids.

[23] This disclosure also relates to pharmaceutical compositions that contain a conditionally active protein, nucleic acid that encodes the conditionally active protein, and vectors and host cells that contain such nucleic acids. Typically, the pharmaceutical composition contains one or more physiologically acceptable carriers and/or excipients.

[24] The disclosure also relates to therapeutic methods that include administering to a subject in need thereof an effective amount of a conditionally active protein, nucleic acid that encodes the conditionally active protein, vector or host cells that contain such a nucleic acid, and pharmaceutical compositions of any of the foregoing. Typically, the subject has, or is at risk of developing, a proliferative disease, a tumorous disease, an inflammatory disease, an immunological disorder, an autoimmune disease, an infectious disease, a viral disease, an allergic reaction, a parasitic reaction, a graft-versus-host disease or a host-versus-graft disease.

[25] The disclosure also relates to the use of a conditionally active protein, nucleic acid that encodes the conditionally active protein, vector or host cells that contain such a nucleic acid, and pharmaceutical compositions of any of the foregoing, for treating a subject in need thereof. Typically, the subject has, or is at risk of developing, a proliferative disease, a tumorous disease, an inflammatory disease, an immunological disorder, an autoimmune disease, an infectious disease, a viral disease, an allergic reaction, a parasitic reaction, a graft-versus-host disease or a host-versusgraft disease.

[26] The disclosure also relates to the use of a conditionally active protein, nucleic acid that encodes the conditionally active protein, vector or host cells that contain such a nucleic acid for the manufacture of a medicament for treating a disease, such as a proliferative disease, a tumorous disease, an inflammatory disease, an immunological disorder, an autoimmune disease, an infectious disease, a viral disease, an allergic reaction, a parasitic reaction, a graft-versus-host disease or a hostversus-graft disease.

BRIEF DESCRIPTION OF THE DRAWINGS

[27] FIGs. 1A-1E are a series of graphs showing activity of IL-2 fusion proteins in a HEKBlue IL2 reporter assay in the presence of HSA. Squares depict activity of the uncut IL-2 polypeptide (intact) and triangles depict the activity of the cut polypeptide (cleaved). Circles depict activity of control IL2. EC50 for each IL-12. EC50 values for each are shown in the table. FIGs. 1A-1E also depict results of the protein cleavage assay for each IL-2 polypeptide. Constructs tested and depicted include WW0475 (FIG. 1A), WW0517 (FIG. IB), WW0548/556 (FIG. IC), WW0735/523 (FIG. ID), and WW0621/523 (FIG. IE). FIG. IF is a graph showing activity of a non-cleavable control, WW0729/523. FIG. IF also depicts results of a protein cleavage assay for the non-cleavable control.

[28] FIGs. 2A-2L are a series of graphs showing activity of fusion proteins in an IL-2 luciferase reporter assay. Closed squares depict activity of the uncut IL-2 polypeptide (intact) and open squares depict the activity of the cut IL-2 polypeptide (cleaved). Circles depict activity of the control (human

IL-2). EC50 values for each are shown in the table (human IL-2). EC50 values for each are shown in the table. Constructs tested and depicted include WW0521/WW0556 (FIG. 2A), WW0521/WW0524 (FIG. 2B), WW0521/WW0523 (FIG. 2C), WW0520/WW0524 (FIG. 2D), WW0517 (FIG. 2E),

WW0516 (FIG. 2F), WW0417 (FIG. 2G), WW0317 (FIG. 2H), WW0317 (FIG. 21), and

WW0520/WW0523 (FIG. 2J), WW0621/WW0523 (FIG. 2K), WW0048 (FIG. 2L).

[29] FIGs. 3A-3J are a series of graphs showing activity of fusion proteins in an IL-2 T-Blast assay. Squares depict activity of the uncut IL-2 polypeptide (intact) and triangles depict the activity of the cut polypeptide (cleaved). Circles depict activity of the control human IL-2. EC50 values for each are shown in the table. Constructs tests and depicted include WW0317 (FIG. 3A), WW0516 (FIG. 3B), WW0354 (FIG. 3C), WW0517 (FIG. 3D), WW0621/0523 (FIG. 3E), WW0521/524 (FIG. 3F), WW0520/0523 (FIG. 3G), WW0729/523 (FIG. 3H), and WW0735/523 (FIG. 31), WW0520/524 (FIG. 3J).

[30] FIGs. 4A-4G are graphs that show results of analyzing WW0475, WW0520/0523, WW0548/0524, WW0548/0556, WW0517, WW0621/0523, and WW0619 IL-2 fusion proteins in a syngeneic MC38 mouse tumor model. Each graph shows average tumor volume (Mean+/- SEM) over time in mice treated with different doses of each of the fusion proteins as indicated. The data show tumor volume decreasing over time in a dose-dependent manner.

[31] FIGs. 5A-5C are a series of spider plots showing activity of fusion proteins in the MC38 mouse syngeneic model corresponding to the data shown in FIG. 4A-4G. Each line in the plots is the tumor volume over time for a single mouse. FIG. 5A contains the data corresponding to vehicle treatment and fusion proteins WW0517 and WW0520/523. FIG. 5B contains the data corresponding to treatment with fusion proteins WW0548/0524, WW0548/0556, and WW0475. FIG. 5C contains the data corresponding to treatment with fusion proteins WW0619 and WW0621/0523.

[32] FIGs. 6A-6C are a series of spider plots showing the impact of fusion proteins on body weight in an MC38 mouse syngeneic model corresponding to the data shown in FIGs. 5A-5C. Each line in the plots is the body weight over time for a single mouse. FIG. 6A contains the data corresponding to vehicle treatment and fusion proteins WW0517 and WW0520/523. FIG. 6B contains the data corresponding to treatment with fusion proteins WW0548/0524, WW0548/0556, and WW0475. FIG. 6C contains the data corresponding to treatment with fusion proteins WW0619 and WW0621/0523.

[33] FIGs. 7A-7Q are a series of graphs showing activity of fusion proteins in an HEKBlue IL-12 reporter assay. FIGs. 7A-7Q depict IL-12/STAT4 activation in a comparison of human p40/murine p35 IL-12 or human IL-12 fusion proteins to chimeric IL-12 (mouse p35/human p40) or recombinant human IL-12 (control). Squares depict activity of the uncut IL-12 polypeptide (intact) and triangles depict the activity of the cut IL-12 polypeptide (cleaved). Circles depict activity of the control. EC50 values for each are shown in the table.

[34] FIGs. 8A-8D are a series of graphs showing activity of fusion proteins in an IL 12 T-Blast assay. FIGs. 8A-8D depicts activation of IL-12 signaling in a comparison of a human p40/murine p35 IL 12 or human IL 12 fusion protein to control, chimeric IL-12 (human p40/murine p3 5 IL 12) or recombinant human IL12. Squares depict activity of the uncut IL-12 polypeptide (intact) and triangles depict the activity of the cut IL-12 polypeptide (cleaved). Circles depict activity of the control chimeric IL-12 or recombinant human IL-12. EC50 values for each are shown in the table.

[35] FIGs. 9A-9C are a series of graphs showing activity of fusion proteins in an IL-12 luciferase reporter assay. FIGs. 9A-9B depict activation of IL-12 signaling in a comparison of a human p40/murine p35 IL-12 fusion protein to recombinant human IL-12 (control). FIG. 9C depicts activation of IL-12 signaling in comparison of a human IL-12 (human p40/human p35 IL-12) fusion protein to recombinant human IL12. Closed squares depict activity of the uncut IL-12 polypeptide (intact) and open squares depict the activity of the cut polypeptide (cleaved). Circles depict activity of the control. EC50 values for each are shown in the table.

[36] FIGs. 10A-10J are a series of graphs showing activity of fusion proteins in the B16-Blue IFN-α/β reporter assay. FIGs. 10A-10J depict activation of the IFN-α/β pathway in a comparison of mouse INFa fusion protein to mouse INFa (control). Squares depict activity of the uncut INFa polypeptide (intact) and triangles depict the activity of the cut INFa polypeptide (cleaved). Circles depict activity of the control (mouse IFNa). EC50 values for each are shown in the table. FIGs. 10A10J also depict results of the protein cleavage assay for each INFa fusion protein. Each INFa fusion protein was run on an SDS-PAGE gel in both cleaved and uncleaved form. As can be seen in the gel, cleavage was complete.

[37] FIGs. 11A-11B are graphs depicting results from a HEK-Blue IL-12 reporter assay performed on human p40/murine p35 IL12 fusion proteins before and after protease cleavage. Constructs ACP35 (FIG. 11 A) and ACP34 (FIG. 1 IB) were tested. Analysis was performed based on quantification of Secreted Alkaline Phosphatase (SEAP) activity using the reagent QUANTI-Blue® (InvivoGen). Results confirm that IL 12 protein fusion proteins are active.

[38] FIGs. 12A-12F show a series of graphs depicting the results of HEK-blue assay of four IL-12 fusion proteins, before and after cleavage by MMP9. Analysis was performed based on quantification of Secreted Alkaline Phosphatase (SEAP) activity using the reagent QUANTI-Blue (InvivoGen). The data show greater activity in the cleaved IL 12 than in the full fusion protein. Constructs tested were ACP06 (FIG. 12A), ACP07 (FIG. 12C), ACP08 (FIG. 12B), ACP09 (FIG. 12D), ACP10 (FIG. 12E), ACP11 (FIG. 12F).

[39] FIG. 13 shows results of protein cleavage assay. Fusion protein ACPI 1 was run on an SDSPAGE gel in both cleaved and uncleaved form. As can be seen in the gel, cleavage was complete.

[40] FIG. 14 is a schematic which depicts a non-limiting example of an inducible cytokine

protein, wherein the construct is activated upon protease cleavage of a linker attached between two subunits of the cytokine.

[41] FIGs. 15A-15D are graphs depicting results from a HEK-Blue assay performed on human p40/murine p35 IL12 fusion proteins before and after protease cleavage. Results confirm that IL 12 protein fusion proteins are active. Each proliferation assay was performed with HSA or without HSA.

[42] FIGs. 16A-16F are a series of graphs showing activity of exemplary ΙΕΝγ fusion proteins compared to activity of mouse ΙΕΝγ control using WEHI279 cell survival assay. Each assay was performed with medium containing HSA (+HSA) or not containing HSA (-HSA). Each fusion protein comprises an anti-HSA binder, and both uncleaved and MMP9 protease cleaved versions of the fusion protein were used in each assay.

[43] FIGs. 17A-17F are a series of graphs showing activity of exemplary IFNy fusion proteins compared to activity of mouse ΙΕΝγ control using B16 reporter assay. Each assay was performed with medium containing HSA (+HSA) or not containing HSA (-HSA). Each fusion protein comprises an anti-HSA binder, and both uncleaved and MMP9 protease cleaved versions of the fusion protein were used in each assay.

[44] FIGs. 18A-18B show results of protein cleavage assay, as described in Example 2. Two constructs, ACP31 (IFN-a fusion protein; FIG. 18A) and ACP55 (IFN-γ fusion protein; 18B), were run on an SDS-PAGE gel in both cleaved and uncleaved form. As can be seen in the gel, cleavage was complete.

[45] FIGs. 19A-19B are a series of graphs (FIGS. 19A and 19B) showing activity of exemplary ΙΕΝγ fusion proteins before and after protease cleavage using B16 reporter assay. Each assay was performed with culture medium containing HSA, and each fusion protein comprises an anti-HSA binder. Both uncleaved and MMP9 protease cleaved versions of the fusion protein were used in each assay.

[46] FIGs. 20A-20B are a series of graphs (FIG. 20A and FIG. 20B) showing activity of exemplary IFNa fusion proteins before and after cleavage using a B16 reporter assay. Each assay was performed with medium containing HSA, and each fusion protein comprises an anti-HSA binder. Both uncleaved and MMP9 protease cleaved versions of the fusion protein were used in each assay.

[47] FIGs. 21A-21D are a series of graphs depicting the results of tumor growth studies using the MC38 cell line. FIG. 21A-C show the effect of ΙΕΝγ and IFNy fusion proteins on tumor growth when injected intraperitoneally (IP) using different dosing levels and schedules (ug=micrograms, BID=twice daily, BIW= twice weekly, QW= weekly). FIG. 2ID shows the effect of intratumoral (IT) injection of IFNy and IL-2 on tumor growth.

[48] FIGs. 22A-22B are a series of graphs showing activity of exemplary ΙΡΝγ fusion proteins (ACP51 (FIG. 22A), and ACP52 (FIG. 22B)) cleaved by MMP9 protease compared to activity of uncleaved fusion proteins using B16 reporter assay. Each fusion protein comprises an anti-HSA

binder and a tumor targeting domain.

[49] FIGs. 23A-23B are a series of graphs showing activity of exemplary IFNy fusion proteins (ACP53 and ACP54) cleaved by MMP9 protease compared to activity of uncleaved fusion proteins using B16 reporter assay. Each fusion protein comprises IFNy directly fused to albumin.

[50] FIGs. 24A-24D are graphs depicting results from a HEK-Blue IL-2 reporter assay performed on IL-2 fusion proteins and recombinant human IL2 (Rec hIL-2). Analysis was performed based on quantification of Secreted Alkaline Phosphatase (SEAP) activity using the reagent QUANTI-Blue (InvivoGen). FIG. 24A shows results of IL-2 constructs ACP132 and ACP 133 with and without albumin. FIG. 24B shows results of IL-2 construct ACP 16 cleaved and uncleaved. Results of a protein cleavage assay of ACP 16 in cleaved and uncleaved forms is also depicted. FIG. 24C shows results of IL-2 construct ACP 153 in cleaved and uncleaved forms. Results of a protein cleavage assay are also depicted. FIG. 24D illustrates the results from a HEK-Blue IL-2 assay using wild-type cytokine, intact fusion protein, and protease-cleaved fusion protein.

[51] FIGs. 25A and 25B are two graphs showing analysis of ACP16 (FIG. 25A) and ACP124 (FIG. 25B) in a HEKBlue IL-2 reporter assay in the presence of HSA. Circles depict the activity of the uncut polypeptide; squares depict activity of the cut polypeptide. FIG. 25C is a graph showing results of a CTLL-2 proliferation assay. CTLL2 cells (ATCC) were plated in suspension at a concentration of 500,000 cells/well in culture media with or without 40mg/ml human serum albumin (HSA) and stimulated with a dilution series of activatable hIL2 for 72 hours at 37°C and 5% CO2. Activity of uncleaved and cleaved activatable ACP 16 was tested. Cleaved activatable hIL2 was generated by incubation with active MMP9. Cell activity was assessed using a CellTiter-Glo (Promega) luminescence-based cell viability assay. Circles depict intact fusion protein, and squares depict protease-cleaved fusion protein.

[52] FIGs. 26A-26C are a series of graphs showing activity of fusion proteins in an HEKBlue IL12 reporter assay. FIG. 26A depicts IL-12/STAT4 activation in a comparison of ACPI 1 (a human p40/murine p35 IL12 fusion protein) to ACP04 (negative control). FIG. 26B is a graph showing analysis of ACP91 (a chimeric IL-12 fusion protein). Squares depict activity of the uncut ACP91 polypeptide, and triangles depict the activity of the cut polypeptide (ACP91 + MMP9). EC50 values for each are shown in the table. FIG. 26C is a graph showing analysis of ACP136 (a chimeric IL-12 fusion protein). Squares depict activity of the uncut ACP 136 polypeptide, and triangles depict the activity of the cut polypeptide (ACP136 + MMP9). EC50 values for each are shown in the table insert.

[53] FIGs. 27A-27F Fare a series of graphs showing that cleaved mouse IFNal polypeptides ACP31 (FIG. 27A), ACP125 (FIG. 27B), ACP126 (FIG. 27C) are active in an B16-Blue IFN-α/β reporter assay.

[54] FIGs. 28A-28N are a series of graphs depicting the activity of ACP56 (FIG. 28A), ACP57

(FIG. 28B) ACP58 (FIG. 28C), ACP59 (FIG. 28D), ACP60 (FIG. 28E), ACP61 + HSA (FIG. 28F),

ACP30 + HSA (FIG. 28G), ACP73 (FIG. 28H), ACP70 + HSA (FIG. 281), ACP71 (FIG. 28J),

ACP72 (FIG. 28K), ACP 73 (FIG. 28L), ACP74 (FIG. 28M), and ACP75 (FIG. 28N) in a B16 ΙΕΝγ reporter assay. Each fusion was tested for its activity when cut (squares) and uncut (circles).

[55] FIGs. 29A-29B are two graphs showing results of analyzing ACP31 (mouse IFNal fusion protein) and ACPI 1 (a human p40/murine p35 IL12 fusion protein) in a tumor xenograft model. FIG. 29A shows tumor volume over time in mice treated with 33pg ACP31 (circles), 11 Opg ACP31 (triangles), 330μg ACP31 (diamonds), and as controls Ipg murine wild type IFNal (dashed line, squares) and 10 pg mIFNal (dashed line, small circles). Vehicle alone is indicated by large open circles. The data show tumor volume decreasing over time in a dose-dependent manner in mice treated with ACP31. FIG. 29B shows tumor volume over time in mice treated with 17.5pg ACPI 1 (squares), 175pg ACP31 (triangles), 525pg ACP31 (circles), and as controls 2pg ACP04 (dashed line, triangles) and 10 pg ACP04 (dashed line, diamonds). Vehicle alone is indicated by large open circles. The data show tumor volume decreasing over time in a dose-dependent manner in mice treated with both ACPI 1 and ACP04 (a human p40/murine p35 IL12 fusion protein).

[56] FIGs. 30A-30F are a series of spaghetti plots showing tumor volume over time in a mouse xenograft tumor model in mice each treated with vehicle alone (FIG. 30A), 2pg ACP04 (FIG. 30B), lOpg ACP04 (FIG. 30C), 17.5pg ACPI 1 (FIG. 30D), 175pg ACPI 1 (FIG. 30E), and 525pg ACPI 1 (FIG. 30F). Each line represents a single mouse.

[57] FIG. 31A-31C are three graphs showing results of analyzing ACP16 andACP124 in a tumor xenograft model. FIG. 31A shows tumor volume over time in mice treated with 4.4pg ACP16 (squares), 17pg ACP16 (triangles), 70pg ACP16 (downward triangles), 232pg ACP16 (dark circles), and as a comparator 12pg wild type IL-2 (dashed line, triangles) and 36pg wild type IL-2 (dashed line, diamonds. Vehicle alone is indicated by large open circles. The data show tumor volume decreasing over time in a dose-dependent manner in mice treated with ACP 16 at higher concentrations. FIG. 3 IB shows tumor volume over time in mice treated with 17pg ACP 124 (squares), 70pg ACP 124 (triangles), 230pg ACP 124 (downward triangles), and 700pg ACP 124. Vehicle alone is indicated by large open circles. FIG. 31C shows tumor volume over time in mice treated with 17pg ACP16 (triangles), 70pg ACP16 (circles), 232pg ACP16 (dark circles), and as a comparator 17pg ACP124 (dashed line, triangles) 70pg ACP124 (dashed line, diamonds), 230pg ACP 124 (dashed line, diamonds). Vehicle alone is indicated by dark downward triangles. The data show tumor volume decreasing over time in a dose-dependent manner in mice treated with ACP 16, but not ACP124.

[58] FIG. 32A-32B are a series of spaghetti plots showing activity of fusion proteins in an MC38 mouse xenograft model corresponding to the data shown in FIG. 31. Each line in the plots is a single mouse.

[59] FIG. 33 is a graph showing tumor volume over time in a mouse xenograft model showing tumor growth in control mice (open circles) and AP16-treated mice (squares).

[60] FIGs. 34A-34D are a series of survival plots showing survival of mice over time after treatment with cleavable fusion proteins. FIG. 34A shows data for mice treated with vehicle alone (gray line), 17pg ACP16 (dark line), and 17 pg ACP124 (dashed line). FIG. 34B shows data for mice treated with vehicle alone (gray line), 70pg ACP16 (dark line), and 70pg ACP124 (dashed line). FIG. 34C shows data for mice treated with vehicle alone (gray line), 232pg ACPI6 (dark line), and 230pg ACP124 (dashed line). FIG. 34D shows data for mice treated with vehicle alone (gray line), 232pg ACP16 (dark line), and 700pg ACP124 (dashed line).

[61] FIG. 35 a series of spaghetti plots showing activity of fusion proteins in an MC38 mouse xenograft model. All mouse groups were given four doses total except for the highest three doses of APC 132, wherein fatal toxicity was detected after 1 week/2 doses. Shown are vehicle alone (top), 17, 55, 70, and 230 pg ACP16 (top full row), 9,28, 36, and 119 pg ACP132 (middle full row), and 13, 42, 54, and 177 pg ACP21 (bottom full row). Each line in the plots represents an individual animal. [62] FIGs. 36A-36H are a series of graphs showing activity of fusion proteins in the HEK-Blue IFN-α/β reporter assay. FIGs. 36A-36H depict activation of the IFN-α/β pathway in a comparison of human IFNa fusion protein) to control (human IFNa). Squares depict activity of the uncut IFNa polypeptide (intact) and triangles depict the activity of the cut IFNa polypeptide (cleaved). Circles depict activity of the control (human IFNa). EC50 values for each are shown in the table. Results confirm that the IFNa fusion proteins are active and inducible. FIGs. 36A-36H also depict results of the protein cleavage assay for each INFa fusion protein. Each INFa fusion protein was run on an SDS-PAGE gel in both cleaved and uncleaved form. As can be seen in the gel, cleavage was complete.

[63] FIGs. 37A-37D are a series of graphs showing activity of fusion proteins in the HEK-Blue IFN-α/β reporter assay. FIGs. 37A-37B depict activation of the IFN-α/β pathway in a comparison of a mouse ΙΝΡβ fusion protein to control (mouse ΙΡΝβ). FIGs. 37C-37D depict activation of the IFNα/β pathway in a comparison of a human ΙΝΡβ fusion protein to control (human ΙΡΝβ). Squares depict activity of the uncut ΙΝΡβ polypeptide (intact) and triangles depict the activity of the cut ΙΝΡβ polypeptide (cleaved). Circles depict activity of the control. EC50 values for each are shown in the table. Results confirm that the ΙΡΝβ fusion proteins are active and inducible.

[64] FIGs. 38A-38C are a series of graphs showing activity of fusion proteins in the human PBMCs assay. FIGs. 38A-38C depict activation of the IFNa pathway in a comparison of human IFNa fusion protein to control (human IFNa). Squares depict activity of the uncut IFNa polypeptide (intact) and triangles depict the activity of the cut IFNa polypeptide (cleaved). Circles depict activity of the control human IFNa. EC50 values for each are shown in the table. Analysis was performed

based on quantification of CXCL-10 (IP-10). Results confirm that the IFNa fusion proteins are active and inducible.

[65] FIGs. 39A-39G show are results of analyzing INF fusion proteins in syngeneic MC38 mouse tumor model. FIG. 39A shows average tumor volume over time in mice treated with 369pg WW0610 (square), 553pg WW0610 (down triangle), 830pg WW0610 (up triangle), and 1,245pg WW0610 (circle). Vehicle alone is indicated by a black circle. FIG. 39B shows average tumor volume over time in mice treated with 1,231 pg WW0815 (square), l,845pg WW0815 (down triangle), 2,770pg WW0815 (up triangle), and 4,154pg WW0815 (circle). Vehicle alone is indicated by a black circle. FIG. 39C shows average tumor volume over time in mice treated with 4.6pg WW0644 (square), 9.3pg WW0644 (down triangle), 19pg WW0644 (up triangle), and 37pg WW0644 (circle). Vehicle alone is indicated by a black circle. FIG. 39D shows average tumor volume over time in mice treated with 31pg WW0816 (square), 62pg WW0816 (down triangle), 123pg WW0816 (up triangle), and 247pg WW0816 (circle). Vehicle alone is indicated by a black circle. FIG. 39E shows average tumor volume over time in mice treated with 1 lOpg WW0609 (square), 830pg WW0609 (down triangle), and l,320pg WW0609 (up triangle). FIG. 39F shows average tumor volume over time in mice treated with 1 lOpg WW0610 (square), 830pg WW0610 (down triangle), and l,320pg WW0610 (up triangle). FIG. 39G shows average tumor volume over time in mice treated with 0.3pg WW0643 (square), 1.5pg WW0643 (down triangle), 7.5pg WW0643 (up triangle), and 37.5pg WW0643 (diamond).

Vehicle alone is indicated by a black circle.

[66] FIG. 40A-40G shows a series of spider plots showing activity of fusion proteins in an MC38 xenograft model corresponding to data in FIGs. 39A-39G. Each line in the plots is the tumor volume over time for a single mouse.

[67] FIG. 41A-41G show average percent body weight over time in mice treated with the INF fusion proteins in FIGs. 39A-39G.

[68] FIGs. 42A-42E shows the results of B16IFN reporter assays. Inducible interferon constructs of interest were tested before and after cleavage. The relevant wildtype IFN was tested as a control.

[69] FIG. 43 shows binding data of ACP16, ACP10, ACP11

[70] FIGs. 44A-44D depict the activity of cytokine fusion proteins constructs ACP243, ACP244, ACP243, ACP244, and ACP247.

[71] FIG. 45 shows a series of spider plots showing tumor volume over time during treatment with vehicle, IL-12, ACPI 1 or ACP10.

[72] FIGs. 46A-46D, 47A-47D, 48A, A8B, A9A-49I, 50A, 50B, and 51A-51C shows data (tumor volume and/or body weight) for mice treated with cytokine fusion proteins constructs.

[73] FIGs. 52A-52N, 53A, and 53B depict the activity of cytokine fusion proteins constructs.

[74] FIG. 54A-54N shows the results of proliferation assays comparing cut protein, uncut protein, and IL2 as a control.

[75] FIGs. 55A-55N shows the results of HekBlue IL2 reporter assays comparing activity of constructs with and without protease cleavage; IL-2 is included as a control.

[76] FIGs. 56, 57A-57D, 58, 59A-59Z depict the activity of cytokine fusion proteins constructs.

[77] FIGs. 60A-60G shows a series of spider plots showing the impact of INF fusion proteins on body weight in an MC38 mouse xenograft model corresponding to the data shown in FIGs. 41A-41G. Each line in the plots is the body weight over time for a single mouse.

[78] FIGs. 61A-61B are a series of graphs showing activity of fusion proteins in the B16-Blue

IFN-α/β reporter assay. FIG. 61A depicts activation of the IFN-α/β pathway for construct WW0609 in the presence and absence of albumin. FIG. 6 IB depicts activation of the IFN-α/β pathway for construct WW0643 in the presence and absence of albumin. Squares depict activity of the uncut INFa polypeptide (intact) and triangles depict the activity of the cut INFa polypeptide (cleaved). Circles depict activity of the control (mouse IFNa). EC50 values for each are shown in the table.

DETAILED DESCRIPTION

[79] Disclosed herein are methods and compositions to engineer and use constructs comprising inducible cytokines. Cytokines are potent immune agonists, which lead to them being considered promising therapeutic agents for oncology. However, cytokines proved to have a very narrow therapeutic window. Cytokines have short serum half-lives and are also considered to be highly potent. Consequently, therapeutic administration of cytokines produced undesirable systemic effects and toxicities. These were exacerbated by the need to administer large quantities of cytokine in order to achieve the desired levels of cytokine at the intended site of cytokine action (e.g., a tumor). Unfortunately, due to the biology of cytokines and inability to effectively target and control their activity, cytokines did not achieve the hoped-for clinical advantages in the treatment of tumors.

[80] Disclosed herein are fusion proteins that overcome the toxicity and short half-life problems that have severely limited the clinical use of cytokines in oncology. The fusion proteins contain cytokine polypeptides that have receptor agonist activity. But in the context of the fusion protein, the cytokine receptor agonist activity is attenuated, and the circulating half-life is extended. The fusion proteins include protease cleave sites, which are cleaved by proteases that are associated with a desired site of cytokine activity (e.g., a tumor), and are typically enriched or selectively present at the site of desired activity. Thus, the fusion proteins are preferentially (or selectively) and efficiently cleaved at the desired site of activity to limit cytokine activity substantially to the desired site of activity, such as the tumor microenvironment. Protease cleavage at the desired site of activity, such as in a tumor microenvironment, releases a form of the cytokine from the fusion protein that is much more active as a cytokine receptor agonist than the fusion protein (typically at least about 100X more active than the fusion protein). The form of the cytokine that is released upon cleavage of the fusion protein typically has a short half-life, which is often substantially similar to the half-life of the

naturally occurring cytokine, further restricting cytokine activity to the tumor microenvironment. Even though the half-life of the fusion protein is extended, toxicity is dramatically reduced or eliminated because the circulating fusion protein is attenuated, and active cytokine is targeted to the tumor microenvironment. The fusion proteins described herein, for the first time, enable the administration of an effective therapeutic dose of a cytokine to treat tumors with the activity of the cytokine substantially limited to the tumor microenvironment, and dramatically reduces or eliminates unwanted systemic effects and toxicity of the cytokine.

[81] The fusion proteins disclosed herein typically comprise a cytokine polypeptide [A], a blocking moiety [D], optionally a half-life extension moiety [H], and a protease-cleavable polypeptide linker. The cytokine polypeptide and the blocking moiety and the optional half-life extension element when present are operably linked by the protease-cleavable polypeptide linker and the fusion polypeptide has attenuated cytokine receptor activating activity, e.g., the cytokine-receptor activating activity of the fusion polypeptide is at least about 10X less than the cytokine receptor activating activity of the polypeptide that contains the cytokine polypeptide that is produced by cleavage of the protease cleavable linker. Some preferred fusion polypeptides are of one of formula (I) - (VI):

[A]-[L1]-[H]-[L2]-[D] (I);

[D]-[L2]-[H]-[L1]-[A] (II);

[A]-[L1]-[D]-[L2]-[H] (III);

[H]-[L2]-[D]-[L1]-[A] (IV);

[H]-[L1]-[A]-[L2’]-[D] (V);

[D]-[L1]-[A]-[L2’]-[H] (VI);

wherein [A] is a cytokine polypeptide, [D] is a blocking moiety, [H] is a half-life extension moiety, [LI] is a protease-cleavable polypeptide linker, [L2] is an polypeptide linker that is optionally protease-cleavable, and [L2’] is a protease-cleavable polypeptide linker. [LI] and [L2] or [LI] and [L2’] can be have the same or different amino acid sequence and or protease-cleavage site (when L2 is protease-cleavable) as desired.

[82] This disclosure further relates to pharmaceutical compositions that contain the inducible fusion protein and an additional therapeutic agent, as well as nucleic acids that encode the polypeptides, and recombinant expression vectors and host sells for making such fusion proteins. Also provided herein are methods of using the disclosed fusion proteins in the treatment of diseases, conditions, and disorders.

[83] Unless otherwise defined, all terms of art, notations and other scientific terminology used herein are intended to have the meanings commonly understood by those of skill in the art to which this invention pertains. In some cases, terms with commonly understood meanings are defined herein for clarity and/or for ready reference, and the inclusion of such definitions herein should not necessarily be construed to represent a difference over what is generally understood in the art. The

techniques and procedures described or referenced herein are generally well understood and commonly employed using conventional methodologies by those skilled in the art, such as, for example, the widely utilized molecular cloning methodologies described in Sambrook et al., Molecular Cloning: A Laboratory Manual 4th ed. (2012) Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. As appropriate, procedures involving the use of commercially available kits and reagents are generally carried out in accordance with manufacturer-defined protocols and conditions unless otherwise noted.

[84] “Cytokine” is a well-known term of art that refers to any of a class of immunoregulatory proteins (such as interleukin or interferon) that are secreted by cells especially of the immune system and that are modulators of the immune system. Cytokine polypeptides that can be used in the fusion proteins disclosed herein include, but are not limited to transforming growth factors, such as TGF-a and TGF-β (e.g., TGFbetal, TGFbeta2, TGFbeta3); interferons, such as interferon-a, interferon-β, interferon-γ, interferon-kappa and interferon-omega; interleukins, such as IL-1, IL-la, IL-2, IL-3, IL4, IL-5, IL-6, IL-7, IL-8, IL-9, IL-10, IL-11, IL-12, IL-13, IL-14, IL-15, IL-16, IL-17, IL-18, IL-21 and IL-25; tumor necrosis factors, such as tumor necrosis factor alpha and lymphotoxin; chemokines (e.g., C-X-C motif chemokine 10 (CXCL10), CCL19, CCL20, CCL21), and granulocyte macrophage-colony stimulating factor (GM-CS), as well as fragments of such polypeptides that active the cognate receptors for the cytokine (i.e., functional fragments of the foregoing). “Chemokine” is a term of art that refers to any of a family of small cytokines with the ability to induce directed chemotaxis in nearby responsive cells.

[85] Cytokines are well-known to have short serum half-lives that frequently are only a few minutes or hours. Even forms of cytokines that have altered amino acid sequences intended to extend the serum half-life yet retain receptor agonist activity typically also have short serum half-lives. As used herein, a “short-half-life cytokine” refers to a cytokine that has a substantially brief half-life circulating in the serum of a subject, such as a serum half-life that is less than 10, less than 15, less than 30, less than 60, less than 90, less than 120, less than 240, or less than 480 minutes. As used herein, a short half-life cytokine includes cytokines which have not been modified in their sequence to achieve a longer than usual half-life in the body of a subject and polypeptides that have altered amino acid sequences intended to extend the serum half-life yet retain receptor agonist activity. This latter case is not meant to include the addition of heterologous protein domains, such as a bona fide half-life extension element, such as serum albumin.

[86] “Sortases” are transpeptidases that modify proteins by recognizing and cleaving a carboxylterminal sorting signal embedded in or terminally attached to a target protein or peptide. Sortase A catalyzes the cleavage of the LPXTG motif (SEQ ID NO.: 442) (where X is any standard amino acid) between the Thr and Gly residue on the target protein, with transient attachment of the Thr residue to the active site Cys residue on the enzyme, forming an enzyme-thioacyl intermediate. To complete

transpeptidation and create the peptide-monomer conjugate, a biomolecule with an N-terminal nucleophilic group, typically an oligoglycine motif, attacks the intermediate, displacing Sortase A and joining the two molecules.

[87] As used herein, the term “steric blocker” refers to a polypeptide or polypeptide moiety that can be covalently bonded to a cytokine polypeptide directly or indirectly through other moieties such as linkers, for example in the form of a chimeric polypeptide (fusion protein), but otherwise does not covalently bond to the cytokine polypeptide. A steric blocker can non-covalently bond to the cytokine polypeptide, for example though electrostatic, hydrophobic, ionic or hydrogen bonding. A steric blocker typically inhibits or blocks the activity of the cytokine moiety due to its proximity to the cytokine moiety and comparative size. A steric blocker may also block by virtue of recruitment of a large protein binding partner. An example of this is an antibody which binds to serum albumin; while the antibody itself may or may not be large enough to block activation or binding on its own, recruitment of albumin allows for sufficient steric blocking.

[88] As used and described herein, a “half-life extension element” is a part of the chimeric polypeptide that increases the serum half-life and improve pK, for example, by altering its size (e.g., to be above the kidney filtration cutoff), shape, hydrodynamic radius, charge, or parameters of absorption, biodistribution, metabolism, and elimination.

[89] As used herein, the terms “activatable,” “activate,” “induce,” and “inducible” refer to the ability of a protein, i.e. a cytokine, that is part of a fusion protein, to bind its receptor and effectuate activity upon cleavage of additional elements from the fusion protein.

[90] As used herein, “plasmids” or “viral vectors” are agents that transport the disclosed nucleic acids into the cell without degradation and include a promoter yielding expression of the nucleic acid molecule and/or polypeptide in the cells into which it is delivered.

[91] As used herein, the terms “peptide”, “polypeptide”, or “protein” are used broadly to mean two or more amino acids linked by a peptide bond. Protein, peptide, and polypeptide are also used herein interchangeably to refer to amino acid sequences. It should be recognized that the term polypeptide is not used herein to suggest a particular size or number of amino acids comprising the molecule and that a peptide of the invention can contain up to several amino acid residues or more.

[92] As used throughout, “subject” can be a vertebrate, more specifically a mammal (e.g. a human, horse, cat, dog, cow, pig, sheep, goat, mouse, rabbit, rat, and guinea pig), birds, reptiles, amphibians, fish, and any other animal. The term does not denote a particular age or sex. Thus, adult and newborn subjects, whether male or female, are intended to be covered.

[93] As used herein, “patient” or “subject” may be used interchangeably and can refer to a subject with a disease or disorder (e.g. cancer). The term patient or subject includes human and veterinary subjects.

[94] As used herein the terms “treatment”, “treat”, or “treating” refers to a method of reducing the

effects of a disease or condition or symptom of the disease or condition. Thus, in the disclosed method, treatment can refer to at least about 10%, at least about 20%, at least about 30%, at least about 40%, at least about 50%, at least about 60%, at least about 70%, at least about 80%, at least about 90%, or substantially complete reduction in the severity of an established disease or condition or symptom of the disease or condition. For example, a method for treating a disease is considered to be a treatment if there is a 10% reduction in one or more symptoms of the disease in a subject as compared to a control. Thus, the reduction can be a 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 100%, or any percent reduction in between 10% and 100% as compared to native or control levels. It is understood that treatment does not necessarily refer to a cure or complete ablation of the disease, condition, or symptoms of the disease or condition.

[95] As used herein, the terms “prevent”, “preventing”, and “prevention” of a disease or disorder refers to an action, for example, administration of the chimeric polypeptide or nucleic acid sequence encoding the chimeric polypeptide, that occurs before or at about the same time a subject begins to show one or more symptoms of the disease or disorder, which inhibits or delays onset or exacerbation of one or more symptoms of the disease or disorder.

[96] As used herein, references to “decreasing”, “reducing”, or “inhibiting” include a change of at least about 10%, of at least about 20%, of at least about 30%, of at least about 40%, of at least about 50%, of at least about 60%, of at least about 70%, of at least about 80%, of at least about 90% or greater as compared to a suitable control level. Such terms can include but do not necessarily include complete elimination of a function or property, such as agonist activity.

[97] An “attenuated cytokine receptor agonist” is a cytokine receptor agonist that has decreased receptor agonist activity as compared to the cytokine receptor’s naturally occurring agonist. An attenuated cytokine agonist may have at least about 10X, at least about 50X, at least about 100X, at least about 250X, at least about 500X, at least about 1000X or less agonist activity as compared to the receptor’s naturally occurring agonist. When a fusion protein that contains a cytokine polypeptide as described herein is described as “attenuated” or having “attenuated activity”, it is meant that the fusion protein is an attenuated cytokine receptor agonist.

[98] An “intact fusion protein” is a fusion protein in which no domain has been removed, for example by protease cleavage. A domain may be removable by protease cleavage or other enzymatic activity, but when the fusion protein is “intact”, this has not occurred.

[99] As used herein “moiety” refers to a portion of a molecule that has a distinct function within that molecule, and that function may be performed by that moiety in the context of another molecule. A moiety may be a chemical entity with a particular function, or a portion of a biological molecule with a particular function. For example, a “blocking moiety” within a fusion protein is a portion of the fusion protein which is capable of blocking the activity of some or all of the fusion polypeptide. This may be a protein domain, such as serum albumin. Blocking may be accomplished by a steric blocker

or a specific blocker. A steric blocker blocks by virtue of size and position and not based upon specific binding; an examples is serum albumin. A specific blocker blocks by virtue of specific interactions with the moiety to be blocked. A specific blocker must be tailored to the particular cytokine or active domain; a steric blocker can be used regardless of the payload, as long as it is large enough. If desired a blocking moiety that is incorporated into a fusion proteins described herein can associate with another polypeptide to create a specific binding domain. For example, if a cytokine binding fragment of an antibody is used as the blocking moiety, the fusion polypeptide can include an scFv that is specific for the cytokine as the blocking moiety or the fusion polypeptide can comprise half of a Fab, for example VH-CH1 or VL-CL as the blocking moity, which can associate with a complementary chain VL-CL or VH-CH1, respectively, to form an Fab fragment that specifically binds the cytokine. As further described herein, the blocking moiety may block activity of the fusion protein directly or when the blocking moiety associates with another polypeptide. For example, when an anti-HSA scFv binds HSA or when a VH-CH1 polypeptide associates with a complementary VLCL polypeptide and then binds the cytokine polypeptide.

[100] In general, the therapeutic use of cytokines is strongly limited by their systemic toxicity. TNF, for example, was originally discovered for its capacity of inducing the hemorrhagic necrosis of some tumors, and for its in vitro cytotoxic effect on different tumoral lines, but it subsequently proved to have strong pro-inflammatory activity, which can, in case of overproduction conditions, dangerously affect the human body. As the systemic toxicity is a fundamental problem with the use of pharmacologically active amounts of cytokines in humans, novel derivatives and therapeutic strategies are now under evaluation, aimed at reducing the toxic effects of this class of biological effectors while keeping their therapeutic efficacy.

[101] IL-2 exerts both stimulatory and regulatory functions in the immune system and is, along with other members of the common γ chain (yc) cytokine family, central to immune homeostasis. IL-2 mediates its action by binding to IL-2 receptors (IL-2R), consisting of either trimeric receptors made of IL-2Ra (CD25), IL-2Rp (CD122), and IL-2Ry (yc, CD132) chains or dimeric βγ IL-2Rs (1, 3). Both IL-2R variants are able to transmit signal upon IL-2 binding. However, trimeric αβγ IL-2Rs have a roughly 10-100 times higher affinity for IL-2 than dimeric βγ IL-2Rs (3), implicating that CD25 confers high-affinity binding of IL-2 to its receptor but is not crucial for signal transduction. Trimeric IL-2Rs are found on activated T cells and CD4+ forkhead box P3 (FoxP3)+ T regulatory cells (Treg), which are sensitive to IL-2 in vitro and in vivo. Conversely, antigen-experienced (memory) CD8+, CD44 high memory-phenotype (MP) CD8+, and natural killer (NK) cells are endowed with high levels of dimeric βγ IL-2Rs, and these cells also respond vigorously to IL-2 in vitro and in vivo.

[102] Expression of the high-affinity IL-2R is critical for endowing T cells to respond to low concentrations of IL-2 that is transiently available in vivo. IL-2Ra expression is absent on naive and

memory T cells but is induced after antigen activation. IL-2Rp is constitutively expressed by NK, NKT, and memory CD8+ T cells but is also induced on naive T cells after antigen activation, yc is much less stringently regulated and is constitutively expressed by all lymphoid cells. Once the highaffinity IL-2R is induced by antigen, IL-2R signaling upregulates the expression of IL-2Ra in part through Stat5-dependent regulation of I12ra transcription (Kim et al., 2001). This process represents a mechanism to maintain expression of the high-affinity IL-2R and sustain IL-2 signaling while there remains a source of IL-2.

[103] IL-2 is captured by IL-2Ra through a large hydrophobic binding surface surrounded by a polar periphery that results in a relatively weak interaction (Kd 10-8 M) with rapid on-off binding kinetics. However, the IL-2Ra-IL-2 binary complex leads to a very small conformational change in IL-2 that promotes association with IL-2Rp through a distinct polar interaction between IL-2 and IL2Κβ. The pseudo-high affinity of the ΙΚ2/α/β trimeric complex (i.e. Kd ~300 pM) clearly indicates that the trimeric complex is more stable than either IL2 bound to the a chain alone (Kd = 10 nM) or to the β chain alone (Kd = 450 nM) as shown by Ciardelli's data. In any event, the 1Κ2/α/β trimer then recruits the y chain into the quaternary complex capable of signaling, which is facilitated by the large composite binding site on the IL2-bound β chain for the γ chain.

[104] In other words, the ternary ΙΚ-2Κα-ΙΚ-2Κβ-ΙΚ-2 complex then recruits yc through a weak interaction with IL-2 and a stronger interaction with ΙΚ-2Κβ to produce a stable quaternary highaffinity IL-2R (Kd 10-11 M which is 10 pM). The formation of the high-affinity quaternary IL IL2R complex leads to signal transduction through the tyrosine kinases Jaki and Jak3, which are associated with ΙΚ-2Κβ and yc, respectively (Nelson and Willerford, 1998). The quaternary IL IL2R complex is rapidly internalized, where IL-2,1Κ-2Κβ, and yc are rapidly degraded, but IL-2Ra is recycled to the cell surface (Hemar et al., 1995; Yu and Malek, 2001). Thus, those functional activities that require sustained IL-2R signaling require a continued source of IL-2 to engage IL-2Ra and form additional IL IL-2R signaling complexes.

[105] Interleukin-15 (IL-15), another member of the 4-alpha-helix bundle family of cytokines, has also emerged as an immunomodulator for the treatment of cancer. IL-15 is initially captured via IL15Ra, which is expressed on antigen-presenting dendritic cells, monocytes and macrophages. IL-15 exhibits broad activity and induces the differentiation and proliferation of T, B and natural killer (NK) cells via signaling through the IL-15/ΙΚ Κ-β (CD 122) and the common y chain (CD 132). It also enhances cytolytic activity of CD8+ T cells and induces long-lasting antigen-experienced CD8+CD44 memory T cells. IL-15 stimulates differentiation and immunoglobulin synthesis by B cells and induces maturation of dendritic cells. It does not stimulate immunosuppressive T regulatory cells (Tregs). Thus, boosting IL-15 activity selectively in the tumor micro-environment could enhance innate and specific immunity and fight tumors (Waldmann et al., 2012). IL-15 was initially identified for its ability to stimulate T cell proliferation in an IL like manner through common receptor

components (IL-2R/15R3־yc) and signaling through JAK1/JAK3 and STAT3/STAT5. Like IL-2, IL15 has been shown to stimulate proliferation of activated CD4-CD8-, CD4+CD8+, CD4+ and CD8+ T cells as well as facilitate the induction of cytotoxic T-lymphocytes, and the generation, proliferation and activation of NK cells (Waldmann et al., 1999). However, unlike IL-2 which is required to maintain forkhead box P3 (FOXP3)-expressing CD4+CD25+ Treg cells and for the retention of these cells in the periphery, IL-15 has little effect on Tregs (Berger et al., 2009). This is important as FOXP3-expressing CD4+CD25+ Tregs inhibit effector T cells, thereby inhibiting immune responses including those directed against the tumor. IL-2 also has a crucial role in initiating activation induced cell death (AICD), a process that leads to the elimination of self-reactive T cells, whereas IL-15 is an anti-apoptotic factor for T cells (Marks-Konczalik et al., 2000). IL-15 co-delivered with HIV peptide vaccines has been shown to overcome CD4+ T cell deficiency by promoting longevity of antigenspecific CD8+ T cells and blocking TRAIL- mediated apoptosis (Oh et al., 2008). Furthermore, IL-15 promotes the long-term maintenance of CD8+CD44hi memory T cells (Kanegane et al., 1996).

[106] The importance of IL-15 and IL-15Ra to T and NK cell development is further highlighted by the phenotype of IL-15Ra_/_ and IL-15_/_ mice. Knockout mice demonstrate decreased numbers of total CD8+ T cells, and are deficient in memory-phenotype CD8+ T cells, NK cells, NK/T cells and some subsets of intestinal intraepithelial lymphocytes, indicating that IL-15 provides essential positive homeostatic functions for these subsets of cells (Lodolce et al., 1996; Kennedy et al., 1998). The similarities in the phenotypes of these two strains of knockout mice suggest the importance of IL15Ra in maintaining physiologically relevant IL-15 signals.

[107] IL-15 is presented in trans by the IL-15 receptor alpha-chain to the IL-15RPyc complex displayed on the surface of T cells and natural killer (NK) cells (Han et al., 2011). The IL-15Ra-chain plays a role of chaperone protein, stabilizes, and increases IL-15 activity (Desbois et al., 2016). It has been shown that exogenous IL-15 may have a limited impact on patients with cancer due to its dependency on IL-15Ra frequently downregulated in cancer patients. Therefore, the fusion protein RLI, composed of the sushi+ domain of IL15Ra coupled via a linker to IL-15, has been suggested as an alternative approach to IL15 therapy (Bessard et al., 2009). It was found that administration of soluble IL-15/IL-15Ra complexes greatly enhanced IL-15 serum half-life and bioavailability in vivo (Stoklasek et al., 2010).

[108] In addition to the effects on T and NK cells, IL-15 also has several effects on other components of the immune system. IL-15 protects neutrophils from apoptosis, modulates phagocytosis and stimulates the secretion of IL-8 and IL-1R antagonist. It functions through the activation of JAK2, p38 and ERK1/2 MAPK, Syk kinase and the NF-kB transcriptional factor (Pelletier et al., 2002). In mast cells, IL-15 can act as a growth factor and an inhibitor of apoptosis. In these cells IL-15 activates the JAK2/STAT5 pathway without the requirement of yc binding (Tagaya et al., 1996). IL-15 also induces B lymphocyte proliferation and differentiation, and increases

immunoglobulin secretion (Armitage et al., 1995). It also prevents Fas-mediated apoptosis and allows induction of antibody responses partially independent of CD4-help (Demerci et al., 2004; Steel et al., 2010). Monocytes, macrophages and dendritic cells effectively transcribe and translate IL-15. They also respond to IL-15 stimulation. Macrophages respond by increasing phagocytosis, inducing IL-8, IL-12 and MCP-1 expression, and secreting IL-6, IL-8 and TNF a (Budagian et al., 2006). Dendritic cells incubated with IL-15 demonstrate maturation with increased CD83, CD86, CD40, and MHC class II expression, are also resistant to apoptosis, and show enhanced interferon-γ secretion (Anguille et al., 2009).

[109] IL-15 has also been shown to have effects on non-hematological cells including myocytes, adipocytes, endothelial and neural cells. IL-15 has an anabolic effect on muscle and may support muscle cell differentiation (Quinn et al., 1995). It stimulates myocytes and muscle fibers to accumulate contractile protein and is able to slow muscle wasting in rats with cancer-related cachexia (Figueras et al., 2004). IL-15 has also been shown to stimulate angiogenesis (Angiolillo et al., 1997) and induce microglial growth and survival (Hanisch et al., 1997).

[110] Interleukin-7 (IL-7), also of the IL-2/IL-15 family, is a well-characterized pleiotropic cytokine, and is expressed by stromal cells, epithelial cells, endothelial cells, fibroblasts, smooth muscle cells and keratinocytes, and following activation, by dendritic cells (Alpdogan et al., 2005). Although it was originally described as a growth and differentiation factor for precursor B lymphocytes, subsequent studies have shown that IL-7 is critically involved in T-lymphocyte development and differentiation. Interleukin-7 signaling is essential for optimal CD8 T-cell function, homeostasis and establishment of memory (Schluns et al., 2000); it is required for the survival of most T-cell subsets, and its expression has been proposed to be important for regulating T-cell numbers.

[Ill] IL-7 binds to a dimeric receptor, including IL-7Ra and yc to form a ternary complex that plays fundamental roles in extracellular matrix remodeling, development, and homeostasis of T and B cells (Mazzucchelli and Durum, 2007). IL-7Ra also cross-reacts to form a ternary complex with thymic stromal lymphopoietin (TSLP) and its receptor (TSLPR), and activates the TSLP pathway, resulting in T and dendritic cell proliferation in humans and further B cell development in mice (Leonard, 2002). Tight regulation of the signaling cascades activated by the complexes are therefore crucial to normal cellular function. Under-stimulation of the IL-7 pathway caused by mutations in the IL-7Ra ectodomain inhibits T and B cell development, resulting in patients with a form of severe combined immunodeficiency (SCID) (Giliani et al., 2005; Puel et al., 1998).

[112] IL-7 has a potential role in enhancing immune reconstitution in cancer patients following cytotoxic chemotherapy. IL-7 therapy enhances immune reconstitution and can augment even limited thymic function by facilitating peripheral expansion of even small numbers of recent thymic emigrants. Therefore, IL-7 therapy could potentially repair the immune system of patients who have been depleted by cytotoxic chemotherapy (Capitini et al., 2010).

[113] Interleukin-12 (IL-12) is a disulfide-linked heterodimer of two separately encoded subunits (p35 and p40), which are linked covalently to give rise to the so-called bioactive heterodimeric (p70) molecule (Lieschke et al., 1997; Jana et al., 2014). Apart from forming heterodimers (IL-12 and IL23), the p40 subunit is also secreted as a monomer (p40) and a homodimer (p402). It is known in the art that synthesis of the heterodimer as a single chain with a linker connecting the p35 to the p40 subunit preserves the full biological activity of the heterodimer. IL-12 plays a critical role in the early inflammatory response to infection and in the generation of Thl cells, which favor cell-mediated immunity. It has been found that overproduction of IL-12 can be dangerous to the host because it is involved in the pathogenesis of a number of autoimmune inflammatory diseases (e.g. MS, arthritis, type 1 diabetes).

[114] The IL-12 receptor (IL-12R) is a heterodimeric complex consisting of IL-12Rp1 and IL12Rp2 chains expressed on the surface of activated T-cells and natural killer cells (Trinchieri et al., 2003). The IL-12Rp1 chain binds to the IL-12p40 subunit, whereas IL-12p35 in association with IL12Κβ2 confers an intracellular signaling ability (Benson et al., 2011). Signal transduction through IL12R induces phosphorylation of Janus kinase (Jak2) and tyrosine kinase (Tyk2), that phosphorylate and activate signal transducer and activator of transcription (STAT)l, STAT3, STAT4, and STAT5. The specific cellular effects of IL-12 are due mainly to activation of STAT4. IL-12 induces natural killer and T-cells to produce cytokines, in particular interferon (IFN)y, that mediate many of the proinflammatory activities of IL-12, including CD4+ T-cell differentiation toward the Thl phenotype (Montepaone et al., 2014).

[115] Regulatory T cells actively suppress activation of the immune system and prevent pathological self-reactivity and consequent autoimmune disease. Developing drugs and methods to selectively activate regulatory T cells for the treatment of autoimmune disease is the subject of intense research and, until the development of the present invention, which can selectively deliver active interleukins at the site of inflammation, has been largely unsuccessful. Regulatory T cells (Treg) are a class of CD4+CD25+ T cells that suppress the activity of other immune cells. Treg are central to immune system homeostasis, and play a major role in maintaining tolerance to self-antigens and in modulating the immune response to foreign antigens. Multiple autoimmune and inflammatory diseases, including Type 1 Diabetes (T1D), Systemic Lupus Erythematosus (SLE), and Graft-versusHost Disease (GVHD) have been shown to have a deficiency of Treg cell numbers or Treg function. [116] Consequently, there is great interest in the development of therapies that boost the numbers and/or function of Treg cells. One treatment approach for autoimmune diseases being investigated is the transplantation of autologous, ex vivo-expanded Treg cells (Tang, Q., et al, 2013, Cold Spring Harb. Perspect. Med., 3:1-15). While this approach has shown promise in treating animal models of disease and in several early stage human clinical trials, it requires personalized treatment with the patient’s own T cells, is invasive, and is technically complex. Another approach is treatment with low

dose Interleukin-2 (IL-2). Treg cells characteristically express high constitutive levels of the high affinity IL-2 receptor, ΓΕ2Καβγ, which is composed of the subunits IL2Ra (CD25), IL2Rβ (CD122), and IL2Ry (CD132), and Treg cell growth has been shown to be dependent on IL-2 (Malek, T. R., et al., 2010, Immunity, 33:153-65).

[117] Conversely, immune activation has also been achieved using IL-2, and recombinant IL-2 (Proleukin®) has been approved to treat certain cancers. High-dose IL-2 is used for the treatment of patients with metastatic melanoma and metastatic renal cell carcinoma with a long-term impact on overall survival.

[118] Clinical trials of low-dose IL-2 treatment of chronic GVHD (Koreth, J., et al., 2011, N Engl J Med., 365:2055-66) and HCV-associated autoimmune vasculitis patients (Saadoun, D., et al., 2011, N Engl J Med., 365:2067-77) have demonstrated increased Treg levels and signs of clinical efficacy. New clinical trials investigating the efficacy of IL-2 in multiple other autoimmune and inflammatory diseases have been initiated. The rationale for using so-called low dose IL-2 was to exploit the high IL-2 affinity of the trimeric IL-2 receptor which is constitutively expressed on Tregs while leaving other T cells which do not express the high affinity receptor in the inactivated state. Aldesleukin (marketed as Proleukin® by Prometheus Laboratories, San Diego, CA), the recombinant form of IL-2 used in these trials, is associated with high toxicity. Aldesleukin, at high doses, is approved for the treatment of metastatic melanoma and metastatic renal cancer, but its side effects are so severe that its use is only recommended in a hospital setting with access to intensive care (Web address: www.proleukin.com/assets/pdf/proleukin.pdf).

[119] The clinical trials of IL-2 in autoimmune diseases have employed lower doses of IL-2 in order to target Treg cells, because Treg cells respond to lower concentrations of IL-2 than many other immune cell types due to their expression of IL2R alpha (Klatzmann D, 2015 Nat Rev Immunol. 15:283-94). However, even these lower doses resulted in safety and tolerability issues, and the treatments used have employed daily subcutaneous injections, either chronically or in intermittent 5day treatment courses. Therefore, there is a need for an autoimmune disease therapy that potentiates Treg cell numbers and function, that targets Treg cells more specifically than IL- 2, that is safer and more tolerable, and that is administered less frequently.

[120] One approach that has been suggested for improving the therapeutic index of IL based therapy for autoimmune diseases is to use variants of IL-2 that are selective for Treg cells relative to other immune cells. IL-2 receptors are expressed on a variety of different immune cell types, including T cells, NK cells, eosinophils, and monocytes, and this broad expression pattern likely contributes to its pleiotropic effect on the immune system and high systemic toxicity. In particular, activated T effector cells express IL2Raβγ, as do pulmonary epithelial cells. But, activating T effector cells runs directly counter to the goal of down-modulating and controlling an immune response, and activating pulmonary epithelial cells leads to known dose-limiting side effects of IL-2

including pulmonary edema. In fact, the major side effect of high-dose IL-2 immunotherapy is vascular leak syndrome (VLS), which leads to accumulation of intravascular fluid in organs such as lungs and liver with subsequent pulmonary edema and liver cell damage. There is no treatment of

VLS other than withdrawal of IL-2. Low-dose IL-2 regimens have been tested in patients to avoid

VLS, however, at the expense of suboptimal therapeutic results.

[121] According to the literature, VLS is believed to be caused by the release of proinflammatory cytokines from IL activated NK cells. However, there is some evidence that pulmonary edema results from direct binding of IL-2 to lung endothelial cells, which expressed low to intermediate levels of functional αβγ IL-2Rs. And, the pulmonary edema associated with interaction of IL-2 with lung endothelial cells was abrogated by blocking binding to CD25 with an anti-CD25 monoclonal antibody (mAb), in CD25-deficient host mice, or by the use of CD122-specific IL-2/anti-IL-2 mAb (IL-2/mAb) complexes, thus preventing VLS.

[122] Treatment with interleukin cytokines other than IL-2 has been more limited. IL-15 displays immune cell stimulatory activity similar to that of IL-2 but without the same inhibitory effects, thus making it a promising immunotherapeutic candidate. Clinical trials of recombinant human IL-15 for the treatment of metastatic malignant melanoma or renal cell cancer demonstrated appreciable changes in immune cell distribution, proliferation, and activation and suggested potential antitumor activity (Conlon et. al., 2014). IL-15 is currently in clinical trials to treat various forms of cancer. However, IL-15 therapy is known to be associated with undesired and toxic effects, such as exacerbating certain leukemias, graft-versus-host disease, hypotension, thrombocytopenia, and liver injury. (Mishra A., et al., Cancer Cell, 2012,22(5):645-55; Alpdogan O. et al., Blood, 2005, 105(2):866-73; Conlon KC et al., J Clin Oncol, 2015, 33(1):74-82.)

[123] IL-7 promotes lymphocyte development in the thymus and maintains survival of naive and memory T cell homeostasis in the periphery. Moreover, it is important for the organogenesis of lymph nodes (LN) and for the maintenance of activated T cells recruited into the secondary lymphoid organs (SLOs) (Gao et. al., 2015). In clinical trials of IL-7, patients receiving IL-7 showed increases in both CD4+ and CD8+ T cells, with no significant increase in regulatory T cell numbers as monitored by FoxP3 expression (Sportes et al., 2008). In clinical trials reported in 2006,2008 and 2010, patients with different kinds of cancers such as metastatic melanoma or sarcoma were injected subcutaneously with different doses of IL-7. Little toxicity was seen except for transient fevers and mild erythema. Circulating levels of both CD4+ and CD8+ T cells increased significantly and the number of Treg reduced. TCR repertoire diversity increased after IL-7 therapy. However, the anti-tumor activity of IL-7 was not well evaluated (Gao et. al., 2015). Results suggest that IL-7 therapy could enhance and broaden immune responses.

[124] IL-12 is a pleiotropic cytokine, the actions of which create an interconnection between the innate and adaptive immunity. IL-12 was first described as a factor secreted from PMA-induced EBV

transformed B-cell lines. Based on its actions, IL-12 has been designated as cytotoxic lymphocyte maturation factor and natural killer cell stimulatory factor. Due to bridging the innate and adaptive immunity and potently stimulating the production of IFNy, a cytokine coordinating natural mechanisms of anticancer defense, IL-12 seemed ideal candidate for tumor immunotherapy in humans. However, severe side effects associated with systemic administration of IL-12 in clinical investigations and the very narrow therapeutic index of this cytokine markedly tempered enthusiasm for the use of this cytokine in cancer patients (Lasek et. al., 2014). Approaches to IL-12 therapy in which delivery of the cytokine is tumor-targeted, which may diminish some of the previous issues with IL-12 therapy, are currently in clinical trials for cancers.

[125] The direct use of IL-2 as an agonist to bind the IL-2R and modulate immune responses therapeutically has been problematic due its well-documented therapeutic risks, e.g., its short serum half-life and high toxicity. These risks have also limited the therapeutic development and use of other cytokines. New forms of cytokines that reduce these risks are needed. Disclosed herein are compositions and methods comprising IL-2 and IL-15 and other cytokines, functional fragments and muteins of cytokines, variants, and subunits of cytokines as well as conditionally active cytokines designed to address these risks and provide needed immunomodulatory therapeutics.

[126] The present invention is designed to address the shortcomings of direct IL-2 therapy and therapy using other cytokines, for example using cytokine blocking moieties, e.g. steric blocking polypeptides, serum half-life extending polypeptides, targeting polypeptides, linking polypeptides, including protease cleavable linkers, and combinations thereof. Cytokines, including interleukins (e.g., IL-2, IL-7, IL-12, IL-15, IL-18, IL-21 IL-23), interferons (IFNs, including IFNalpha, IFNbeta and IFNgamma), tumor necrosis factors (e.g., TNFalpha, lymphotoxin), transforming growth factors (e.g., TGFbetal, TGFbeta2, TGFbeta3), chemokines (C-X-C motif chemokine 10 (CXCL10), CCL19, CCL20, CCL21), and granulocyte macrophage-colony stimulating factor (GM-CS) are highly potent when administered to patients. As used herein, “chemokine” means a family of small cytokines with the ability to induce directed chemotaxis in nearby responsive cells Cytokines can provide powerful therapy, but are accompanied by undesired effects that are difficult to control clinically and which have limited the clinical use of cytokines. This disclosure relates to new forms of cytokines that can be used in patients with reduced or eliminated undesired effects. In particular, this disclosure relates to pharmaceutical compositions including chimeric polypeptides (fusion proteins), nucleic acids encoding fusion proteins and pharmaceutical formulations of the foregoing that contain cytokines or active fragments or muteins of cytokines that have decreased cytokine receptor activating activity in comparison to the corresponding cytokine. However, under selected conditions or in a selected biological environment the chimeric polypeptides activate their cognate receptors, often with the same or higher potency as the corresponding naturally occurring cytokine. As described herein, this is typically achieved using a cytokine blocking moiety that blocks or inhibits the receptor activating

function of the cytokine, active fragment or mutein thereof under general conditions but not under selected conditions, such as those present at the desired site of cytokine activity (e.g., an inflammatory site or a tumor).

[127] The chimeric polypeptides and nucleic acids encoding the chimeric polypeptides can be made using any suitable method. For example, nucleic acids encoding a chimeric polypeptide can be made using recombinant DNA techniques, synthetic chemistry or combinations of these techniques, and expressed in a suitable expression system, such as in CHO cells. Chimeric polypeptides can similarly be made, for example by expression of a suitable nucleic acid, using synthetic or semi-synthetic chemical techniques, and the Idee. In some embodiments, the blocking moiety can be attached to the cytokine polypeptide via sortase-mediated conjugation. “Sortases” are transpeptidases that modify proteins by recognizing and cleaving a carboxyl-terminal sorting signal embedded in or terminally attached to a target protein or peptide. Sortase A catalyzes the cleavage of the LPXTG motif (SEQ ID No.: 442) (where X is any standard amino acid) between the Thr and Gly residue on the target protein, with transient attachment of the Thr residue to the active site Cys residue on the enzyme, forming an enzyme-thioacyl intermediate. To complete transpeptidation and create the peptide-monomer conjugate, a biomolecule with an N-terminal nucleophilic group, typically an oligoglycine motif, attacks the intermediate, displacing Sortase A and joining the two molecules.

[128] To form the cytokine-blocking moiety fusion protein, the cytokine polypeptide is first tagged at the N-terminus with a polyglycine sequence, or alternatively, with at the C-terminus with a LPXTG motif (SEQ ID NO.: 442). The blocking moiety or other element has respective peptides attached that serve as acceptor sites for the tagged polypeptides. For conjugation to domains carrying a LPXTG (SEQ ID NO.: 442) acceptor peptide attached via its N-terminus, the polypeptide will be tagged with an N-terminal poly-glycine stretch. For conjugation to domain carrying a poly-glycine peptide attached via its C-terminus, the polypeptide will be tagged at its C-terminus with a LPXTG (SEQ ID NO.: 442) sortase recognition sequence. Recognizing poly-glycine and LPXTG (SEQ ID NO.: 442) sequences, sortase will form a peptide bond between polymer-peptide and tagged polypeptides. The sortase reaction cleaves off glycine residues as intermediates and occurs at room temperature.

[129] A variety of mechanisms can be exploited to remove or reduce the inhibition caused by the blocking moiety. For example, the pharmaceutical compositions can include a cytokine moiety and a blocking moiety, e.g. a steric blocking moiety, with a protease cleavable linker comprising a protease cleavage site located between the cytokine and cytokine blocking moiety or within the cytokine blocking moiety. When the protease cleavage site is cleaved, the blocking moiety can dissociate from cytokine, and the cytokine can then activate cytokine receptor. A cytokine moiety can also be blocked by a specific blocking moiety, such as an antibody, which binds an epitope found on the relevant cytokine.

[130] Any suitable linker can be used. For example, the linker can comprise glycine-glycine, a

sortase-recognition motif, or a sortase-recognition motif and a peptide sequence (Gly4Ser)n (SEQ ID NO.: 443) or (Gly3Ser)n, (SEQ ID NO.: 444) wherein n is 1,2, 3,4 or 5. Typically, the sortaserecognition motif comprises a peptide sequence LPXTG (SEQ ID NO.: 442), where X is any amino acid. In some embodiments, the covalent linkage is between a reactive lysine residue attached to the C-terminal of the cytokine polypeptide and a reactive aspartic acid attached to the N-terminal of the blocker or other domain. In other embodiments, the covalent linkage is between a reactive aspartic acid residue attached to the N-terminal of the cytokine polypeptide and a reactive lysine residue attached to the C-terminal of said blocker or other domain.

[131] Accordingly, as described in detail herein, the cytokine blocking moieties used can be steric blockers. As used herein, a “steric blocker” refers to a polypeptide or polypeptide moiety that can be covalently bonded to a cytokine polypeptide directly or indirectly through other moieties such as linkers, for example in the form of a chimeric polypeptide (fusion protein), but otherwise does not covalently bond to the cytokine polypeptide. A steric blocker can non-covalently bond to the cytokine polypeptide, for example though electrostatic, hydrophobic, ionic or hydrogen bonding. A steric blocker typically inhibits or blocks the activity of the cytokine moiety due to its proximity to the cytokine moiety and comparative size. The steric inhibition of the cytokine moiety can be removed by spatially separating the cytokine moiety from the steric blocker, such as by enzymatically cleaving a fusion protein that contains a steric blocker and a cytokine polypeptide at a site between the steric blocker and the cytokine polypeptide.

[132] As described in greater detail herein, the blocking function can be combined with or due to the presence of additional functional components in the pharmaceutical composition, such as a targeting domain, a serum half-life extension element, and protease-cleavable linking polypeptides. For example, a serum half-life extending polypeptide can also be a steric blocker.

[133] In the interest of presenting a concise disclosure of the full scope of the invention, aspects of the invention are described in detail using the cytokine IL-2 as an exemplary cytokine. However, the invention and this disclosure are not limited to IL-2. It will be clear to a person of skill in the art that this disclosure, including the disclosed methods, polypeptides and nucleic acids, adequately describes and enables the use of other cytokines, fragments, variants, cytokine subunits, and muteins, such as IL-2, IL-7, IL-12, IL-15, IL-18, IL-21 IL-23, IFNalpha, IFNbeta, IFNgamma, TNFalpha, lymphotoxin, TGF-betal, TGFbeta2, TGFbeta3, GM-CSF, CXCL10, CCL19, CCL20, CCL21 and functional fragments or muteins of any of the foregoing. Preferred cytokines for use in the fusion proteins disclosed herein are IL-2, IL-12, IFNalpha, IFNbeta, IFNgamma, muteins, functional variants, and functional fragments, or subunits of any of the foregoing. For example, the cytokine a IL-12 cytokine may be a p35 subunit, a p40 subunit, a heterodimer.

[134] Various elements ensure the delivery and activity of IL-2 preferentially at the site of desired IL-2 activity and to severely limit systemic exposure to the interleukin via a blocking and/or a

targeting strategy preferentially linked to a serum half-life extension strategy. In this serum half-life extension strategy, the blocked version of interleukin circulates for extended times (preferentially 1-2 or more weeks) but the activated version has the typical serum half-life of the interleukin.

[135] By comparison to a serum half-life extended version, the serum half-life of IL-2 administered intravenously is only ~10 minutes due to distribution into the total body extracellular space, which is large, ~15 L in an average sized adult. Subsequently, IL-2 is metabolized by the kidneys with a halflife of ~2.5 hours. (Smith, K. Interleukin 2 immunotherapy. Therapeutic Immunology 240 (2001)). By other measurements, IL-2 has a very short plasma half-life of 85 minutes for intravenous administration and 3.3 hours subcutaneous administration (Kirchner, G. 1., et al., 1998, Br J Clin Pharmacol. 46:5-10). In some embodiments of this invention, the half-life extension element is linked to the interleukin via a linker which is cleaved at the site of action (e.g. by inflammation-specific or tumor-specific proteases) releasing the interleukin’s full activity at the desired site and also separating it from the half-life extension of the uncleaved version. In such embodiments, the fully active and free interleukin would have very different pharmacokinetic (pK) properties - a half-life of hours instead of weeks. In addition, exposure to active cytokine is limited to the site of desired cytokine activity (e.g., an inflammatory site or tumor) and systemic exposure to active cytokine, and associated toxicity and side effects, are reduced.

[136] Other cytokines envisioned in this invention have similar pharmacology (e.g. IL-15 as reported by Blood 2011 117:4787-4795; doi: doi.org/10.1182/blood 10-311456) as IL-2 and accordingly, the designs of this invention address the shortcomings of using these agents directly, and provide chimeric polypeptides that can have extended half-life and/or be targeted to a site of desired activity (e.g., a site of inflammation or a tumor).

[137] If desired, IL-2 can be engineered to bind the IL-2R complex generally or one of the three IL2R subunits specifically with an affinity that differs from that of the corresponding wild-type IL-2, for example toto selectively activate Tregs or Teff. For example, IL-2 polypeptides that are said to have higher affinity for the trimeric form of the IL-2 receptor relative to the dimeric beta/gamma form of the 11-2 receptor in comparison to wild type IL-2 can have an amino acid sequence that includes one of the following sets of mutations with respect to SEQ ID NO: 1 (a mature IL-2 protein comprising amino acids 21-153 of human IL-2 having the Uniprot Accession No. P60568-1): (a) K64R, V69A, and Q74P; (b) V69A, Q74P, and T101A; (c) V69A, Q74P, and I128T; (d) N30D, V69A, Q74P, and F103S; (e) K49E, V69A, A73V, and K76E; (f) V69A, Q74P, T101A, and T133N; (g) N30S, V69A, Q74P, and I128A; (h) V69A, Q74P, N88D, and S99P; (i) N30S, V69A, Q74P, and I128T; (j) K9T, QI IR, K35R, V69A, and Q74P; (k) AIT, M46L, K49R, E61D, V69A, and H79R; (1) K48E, E68D, N71T, N90H, F103S, and II 14V; (m) S4P, T10A, QI IR, V69A, Q74P, N88D, and T133A; (η) E15K, N30S Y31H, K35R, K48E, V69A, Q74P, and I92T; (o) N30S, E68D, V69A, N71A, Q74P, S75P, K76R, andN90H; (p) N30S, Y31C, T37A, V69A, A73V, Q74P, H79R, and I128T; (q) N26D, N29S,

N30S, K54R, E67G, V69A, Q74P, and I92T; (r) K8R, Q13R, N26D, N30T, K35R, T37R, V69A, Q74P, and I92T; and (s) N29S, Y31H, K35R, T37A, K48E, V69A, N71R, Q74P, N88D, and I89V. This approach can also be applied to prepare muteins of other cytokines including interleukins (e.g., IL-2, IL-7, IL-12, IL-15, IL-18, IL-23), interferons (IFNs, including IFNalpha, IFNbeta and IFNgamma), tumor necrosis factors (e.g., TNFalpha, lymphotoxin), transforming growth factors (e.g., TGFbetal, TGFbeta2, TGFbeta3) and granulocyte macrophage-colony stimulating factor (GM-CS). For example, muteins can be prepared that have desired binding affinity for a cognate receptor.

[138] As noted above, any of the mutant IL-2 polypeptides disclosed herein can include the sequences described; they can also be limited to the sequences described and otherwise identical to SEQ ID NO: 1. Moreover, any of the mutant IL-2 polypeptides disclosed herein can optionally include a substitution of the cysteine residue at position 125 with another residue (e.g., serine) and/or can optionally include a deletion of the alanine residue at position 1 of SEQ ID NO: 1.

[139] Another approach to improving the therapeutic index of an IL-2 based therapy is to optimize the pharmacokinetics of the molecule to maximally activate Treg cells. Early studies of IL-2 action demonstrated that IL-2 stimulation of human T cell proliferation in vitro required a minimum of 5-6 hours exposure to effective concentrations of IL-2 (Cantrell, D. A., et. al., 1984, Science, 224: 13121316). When administered to human patients, IL-2 has a very short plasma half-life of 85 minutes for intravenous administration and 3.3 hours subcutaneous administration (Kirchner, G. 1., et al., 1998, Br J Clin Pharmacol. 46:5-10). Because of its short half-life, maintaining circulating IL-2 at or above the level necessary to stimulate T cell proliferation for the necessary duration necessitates high doses that result in peak IL-2 levels significantly above the EC50 for Treg cells or will require frequent administration. These high IL-2 peak levels can activate IL2RPy receptors and have other unintended or adverse effects, for example VLS as noted above. An IL-2 analog, or a multifunctional protein with IL-2 attached to a domain that enables binding to the FcRn receptor, with a longer circulating half-life than IL-2 can achieve a target drug concentration for a specified period of time at a lower dose than IL-2, and with lower peak levels. Such an IL-2 analog will therefore require either lower doses or less frequent administration than IL-2 to effectively stimulate Treg cells. Less frequent subcutaneous administration of an IL-2 drug will also be more tolerable for patients. A therapeutic with these characteristics will translate clinically into improved pharmacological efficacy, reduced toxicity, and improved patient compliance with therapy. Alternatively, IL-2 or muteins of IL-2 (herein, “IL-2*”) can be selectively targeted to the intended site of action (e.g. sites of inflammation or a tumor). This targeting can be achieved by one of several strategies, including the addition of domains to the administered agent that comprise blockers of the IL-2 (or muteins) that are cleaved away or by targeting domains or a combination of the two.

[140] In some embodiments, IL-2* partial agonists can be tailored to bind with higher or lower affinity depending on the desired target; for example, an IL-2* can be engineered to bind with

enhanced affinity to one of the receptor subunits and not the others. These types of partial agonists, unlike full agonists or complete antagonists, offer the ability to tune the signaling properties to an amplitude that elicits desired functional properties while not meeting thresholds for undesired properties. Given the differential activities of the partial agonists, a repertoire of IL-2 variants could be engineered to exhibit an even finer degree of distinctive signaling activities, ranging from almost full to partial agonism to complete antagonism.

[141] In some embodiments, the IL-2* has altered affinity for IL-2Ra. In some embodiments, the IL-2* has a higher affinity for IL-2Ra than wild-type IL-2. In other embodiments, the IL-2* has altered affinity for IL-2Rp. In one embodiment, IL-2* has enhanced binding affinity for IL-2Rp, e.g., the N-terminus of IL-2Rp, that eliminates the functional requirement for IL-2Ra. In another embodiment, an IL-2* is generated that has increased binding affinity for IL-2Rp but that exhibited decreased binding to IL-2Ry, and thereby is defective ΙΕ-2Κβγ heterodimerization and signaling.

[142] Blocking moieties, described in further detail below, can also be used to favor binding to or activation of one or more receptors. In one embodiment, blocking moieties are added such that IL2Κβγ binding or activation is blocked but IL-2Ra binding or activation is not changed. In another embodiment, blocking moieties are added such that IL-2Ra binding or activation is diminished. In another embodiment, blocking moieties are added such that binding to and or activation of all three receptors is inhibited. This blocking may be relievable by removal of the blocking moieties in a particular environment, for example by proteolytic cleavage of a linker linking one or more blocking moieties to the cytokine.

[143] A similar approach can be applied to improve other cytokines, particularly for use as immunostimulatory agents, for example for treating cancer. For example, in this aspect, the pharmacokinetics and/or pharmacodynamics of the cytokine (e.g., IL-2, IL-7, IL-12, IL-15, IL-18, IL21 IL-23, IFNalpha, IFNbeta and IFNgamma, TNFalpha, lymphotoxin, TGFbetal, TGFbeta2, TGFbeta3 GM-CSF, CXCL10, CCL19, CCL20, and CCL21 can be tailored to maximally activate effector cells (e.g., effect T cells, NK cells) and/or cytotoxic immune response promoting cells (e.g., induce dendritic cell maturation) at a site of desired activity, such as in a tumor, but preferably not systemically.

[144] Thus, provided herein are pharmaceutical compositions comprising at least one cytokine polypeptide, such as interleukins (e.g., IL-2, IL-7, IL-12, IL-15, IL-18, IL-21, IL-23), interferons (IFNs, including IFNalpha, IFNbeta and IFNgamma), tumor necrosis factors (e.g., TNFalpha, lymphotoxin), transforming growth factors (e.g., TGFbetal, TGFbeta2, TGFbeta3), chemokines (e.g. CXCL10, CCL19, CCL20, CCL21) and granulocyte macrophage-colony stimulating factor (GM-CS) or a functional fragment or mutein of any of the foregoing. The polypeptide typically also includes at least one linker amino acid sequence, wherein the amino acid sequence is in certain embodiments capable of being cleaved by an endogenous protease. In one embodiment, the linker comprises an

amino acid sequence comprising HSSKLQ (SEQ ID NO.: 25), GPLGVRG (SEQ ID NO.: 445), IPVSLRSG (SEQ ID NO.: 446), VPLSLYSG (SEQ ID NO. 447), or SGESPAYYTA (SEQ ID NO. 448). In other embodiments, the chimeric polypeptide further contains a blocking moiety, e.g. a steric blocking polypeptide moiety, capable of blocking the activity of the interleukin polypeptide. The blocking moiety, for example, can comprise a human serum albumin (HSA) binding domain or an optionally branched or multi-armed polyethylene glycol (PEG). Alternatively, the pharmaceutical composition comprises a first cytokine polypeptide or a fragment thereof, and blocking moiety, e.g. a steric blocking polypeptide moiety, wherein the blocking moiety blocks the activity of the cytokine polypeptide on the cytokine receptor, and wherein the blocking moiety in certain embodiments comprises a protease cleavable domain. In some embodiments, blockade and reduction of cytokine activity is achieved simply by attaching additional domains with very short linkers to the N or C terminus of the interleukin domain. In such embodiments, it is anticipated the blockade is relieved by protease digestion of the blocking moiety or of the short linker that tethers the blocker to the interleukin. Once the domain is clipped or is released, it will no longer be able to achieve blockade of cytokine activity.

[145] The pharmaceutical composition e.g., chimeric polypeptide can comprise two or more cytokines, which can be the same cytokine polypeptide or different cytokine polypeptides. For example, the two or more different types of cytokines have complementary functions. In some examples, a first cytokine is IL-2 and a second cytokine is IL-12. In some embodiments, each of the two or more different types of cytokine polypeptides have activities that modulate the activity of the other cytokine polypeptides. In some examples of chimeric polypeptides that contain two cytokine polypeptides, a first cytokine polypeptide is T-cell activating, and a second cytokine polypeptide is non-T-cell-activating. In some examples of chimeric polypeptides that contain two cytokine polypeptides, a first cytokine is a chemoattractant, e.g. CXCL10, and a second cytokine is an immune cell activator.

[146] Preferably, the cytokine polypeptides (including functional fragments) that are included in the fusion proteins disclosed herein are not mutated or engineered to alter the properties of the naturally occurring cytokine, including receptor binding affinity and specificity or serum half-life. However, changes in amino acid sequence from naturally occurring (including wild type) cytokine are acceptable to facilitate cloning and to achieve desired expression levels, for example. Blocking Moiety

[147] The blocking moiety can be any moiety that inhibits the ability of the cytokine to bind and/or activate its receptor. The blocking moiety can inhibit the ability of the cytokine to bind and/or activate its receptor sterically blocking and/or by noncovalently binding to the cytokine. Examples of suitable blocking moieties include the full length or a cytokine-binding fragment or mutein of the cognate receptor of the cytokine. Antibodies and fragments thereof including, a polyclonal antibody,

a recombinant antibody, a human antibody, a humanized antibody a single chain variable fragment (scFv), single-domain antibody such as a heavy chain variable domain (VH), a light chain variable domain (VL) and a variable domain of camelid-type nanobody (VHH), a dAb and the like that bind the cytokine can also be used. Other suitable antigen-binding domain that bind the cytokine can also be used, include non-immunoglobulin proteins that mimic antibody binding and/or structure such as, anticalins, affilins, affibody molecules, affimers, affitins, alphabodies, avimers, DARPins, fynomers, kunitz domain peptides, monobodies, and binding domains based on other engineered scaffolds such as SpA, GroEL, fibronectin, lipocallin and CTLA4 scaffolds. Further examples of suitable blocking polypeptides include polypeptides that sterically inhibit or block binding of the cytokine to its cognate receptor. Advantageously, such moieties can also function as half-life extending elements. For example, a peptide that is modified by conjugation to a water-soluble polymer, such as PEG, can sterically inhibit or prevent binding of the cytokine to its receptor. Polypeptides, or fragments thereof, that have long serum half-lives can also be used, such as serum albumin (human serum albumin), immunoglobulin Fc, transferrin and the like, as well as fragments and muteins of such polypeptides. Antibodies and antigen-binding domains that bind to, for example, a protein with a long serum halflife such as HSA, immunoglobulin or transferrin, or to a receptor that is recycled to the plasma membrane, such as FcRn or transferrin receptor, can also inhibit the cytokine, particularly when bound to their antigen. Examples of such antigen-binding polypeptides include a single chain variable fragment (scFv), single-domain antibody such as a heavy chain variable domain (VH), a light chain variable domain (VL) and a variable domain of camelid-type nanobody (VHH), a dAb and the like. Other suitable antigen-binding domain that bind the cytokine can also be used, include nonimmunoglobulin proteins that mimic antibody binding and/or structure such as, anticalins, affilins, affibody molecules, affimers, affitins, alphabodies, avimers, DARPins, fynomers, kunitz domain peptides, monobodies, and binding domains based on other engineered scaffolds such as SpA, GroEL, fibronectin, lipocallin and CTLA4 scaffolds.

[148] In illustrative examples, when IL-2 is the cytokine in the chimeric polypeptide, the blocking moiety can be the full length or fragment or mutein of the alpha chain of IL-2 receptor (IL-2Ra) or beta (IL-2RP) or gamma chain of IL-2 receptor (IL-2Ry), an anti-IL-2 single-domain antibody (dAb) or scFv, a Fab, an anti-CD25 antibody or fragment thereof, and anti-HSA dAb or scFv, and the like. As described further herein, when an antibody fragement is used to attenuate the activity of the cytokine polypeptide, the blocking moiety in the fusion protein can be a single chain antibody binding fragment, such as an scFv. The blocking moiety can also be half of a two chain antigen binding fragment such as a VH-CH1, which associates with a complementary VL-CL on a second polypeptide for form an antibody binding site the binds the cytokine polypeptide.

In vivo Half-life Extension Elements

[149] Preferably, the chimeric polypeptides comprise an in vivo half-life extension element.

Increasing the in vivo half-life of therapeutic molecules with naturally short half-lives allows for a more acceptable and manageable dosing regimen without sacrificing effectiveness. As used herein, a “half-life extension element” is a part of the chimeric polypeptide that increases the in vivo half-life and improve pK, for example, by altering its size (e.g., to be above the kidney filtration cutoff), shape, hydrodynamic radius, charge, or parameters of absorption, biodistribution, metabolism, and elimination. An exemplary way to improve the pK of a polypeptide is by expression of an element in the polypeptide chain that binds to receptors that are recycled to the plasma membrane of cells rather than degraded in the lysosomes, such as the FcRn receptor on endothelial cells and transferrin receptor. Three types of proteins, e.g., human IgGs, HSA (or fragments), and transferrin, persist for much longer in human serum than would be predicted just by their size, which is a function of their ability to bind to receptors that are recycled rather than degraded in the lysosome. These proteins, or fragments of them that retain the FcRn binding are routinely linked to other polypeptides to extend their serum half-life. In one embodiment, the half-life extension element is a human serum albumin (HSA) binding domain. HSA (SEQ ID NO: 2) may also be directly bound to the pharmaceutical compositions or bound via a short linker. Fragments of HSA may also be used. HSA and fragments thereof can function as both a blocking moiety and a half-life extension element. Human IgGs and Fc fragments can also carry out a similar function.

[150] The serum half-life extension element can also be antigen-binding polypeptide that binds to a protein with a long serum half-life such as serum albumin, transferrin and the like. Examples of such polypeptides include antibodies and fragments thereof including, a polyclonal antibody, a recombinant antibody, a human antibody, a humanized antibody a single chain variable fragment (scFv), single-domain antibody such as a heavy chain variable domain (VH), a light chain variable domain (VL) and a variable domain of camelid-type nanobody (VHH), a dAb and the like. Other suitable antigen-binding domain include non-immunoglobulin proteins that mimic antibody binding and/or structure such as, anticalins, affilins, affibody molecules, affimers, affitins, alphabodies, avimers, DARPins, fynomers, kunitz domain peptides, monobodies, and binding domains based on other engineered scaffolds such as SpA, GroEL, fibronectin, lipocallin and CTLA4 scaffolds. Further examples of antigen-binding polypeptides include a ligand for a desired receptor, a ligand-binding portion of a receptor, a lectin, and peptides that binds to or associates with one or more target antigens.

[151] Some preferred serum half-life extension elements are polypeptides that comprise complementarity determining regions (CDRs), and optionally non-CDR loops. Advantageously, such serum half-life extension elements can extend the serum half-life of the cytokine, and also function as inhibitors of the cytokine (e.g., via steric blocking, non-covalent interaction or combination thereof) and/or as targeting domains. In some instances, the serum half-life extension elements are domains derived from an immunoglobulin molecule (Ig molecule) or engineered protein scaffolds that mimic antibody structure and/or

binding activity. The Ig may be of any class or subclass (IgGl, IgG2, IgG3, IgG4, IgA, IgE, IgM etc). A polypeptide chain of an Ig molecule folds into a series of parallel beta strands linked by loops. In the variable region, three of the loops constitute the complementarity determining regions (CDRs) which determine the antigen binding specificity of the molecule. An IgG molecule comprises at least two heavy (H) chains and two light (L) chains inter-connected by disulfide bonds, or an antigen binding fragment thereof. Each heavy chain is comprised of a heavy chain variable region (abbreviated herein as VH) and a heavy chain constant region. The heavy chain constant region is comprised of three domains, CHI, CH2 and CH3. Each light chain is comprised of a light chain variable region (abbreviated herein as VL) and a light chain constant region. The light chain constant region is comprised of one domain, CL. The VH and VL regions can be further subdivided into regions of hypervariability, termed complementarity determining regions (CDRs) with are hypervariable in sequence and/or involved in antigen recognition and/or usually form structurally defined loops, interspersed with regions that are more conserved, termed framework regions (FR). Each VH and VL is composed of three CDRs and four FRs, arranged from amino-terminus to carboxy-terminus in the following order: FR1, CDR1, FR2, CDR2, FR3, CDR3, FR4. In some embodiments of this disclosure, at least some or all of the amino acid sequences of FR1, FR2, FR3, and FR4 are part of the non-CDR loop” of the binding moieties described herein. A variable domain of an immunoglobulin molecule has several beta strands that are arranged in two sheets. The variable domains of both light and heavy immunoglobulin chains contain three hypervariable loops, or complementarity-determining regions (CDRs). The three CDRs of a V domain (CDR1, CDR2, CDR3) cluster at one end of the beta barrel. The CDRs are the loops that connect beta strands B-C, C'-C, and F-G of the immunoglobulin fold, whereas the bottom loops that connect beta strands AB, CO, C -D and E-F of the immunoglobulin fold, and the top loop that connects the D-E strands of the immunoglobulin fold are the non-CDR loops. In some embodiments of this disclosure, at least some amino acid residues of a constant domain, CHI, CH2, or CH3, are part of the “non-CDR loop” of the binding moieties described herein. Non-CDR loops comprise, in some embodiments, one or more of AB, CD, EF, and DE loops of a Cl-set domain of an Ig or an Ig-like molecule; AB, CC’, EF, FG, BC, and EC’ loops of a C2-set domain of an Ig or an Ig-like molecule; DE, BD, GF, A(A1A2)B, and EF loops of I(Intermediate)-set domain of an Ig or Ig-like molecule.

[152] Within the variable domain, the CDRs are believed to be responsible for antigen recognition and binding, while the FR residues are considered a scaffold for the CDRs. However, in certain cases, some of the FR residues play an important role in antigen recognition and binding. Framework region residues that affect Ag binding are divided into two categories. The first are FR residues that contact the antigen, thus are part of the binding-site, and some of these residues are close in sequence to the CDRs. Other residues are those that are far from the CDRs in sequence, but are in close proximity to it in the 3-D structure of the molecule, e.g., a loop in heavy chain.

[153] The binding moieties are any kinds of polypeptides. For example, in certain instances the binding moieties are natural peptides, synthetic peptides, or fibronectin scaffolds, or engineered bulk serum proteins.

The bulk serum protein comprises, for example, albumin, fibrinogen, or a globulin. In some embodiments, the binding moieties are engineered scaffolds. Engineered scaffolds comprise, for example, sdAb, a scFv, a

Fab, a VHH, a fibronectin type III domain, immunoglobulin-like scaffold (as suggested in Halaby et al.,

1999. Prot Eng 12(7):563-571), DARPin, cystine knot peptide, lipocalin, three-helix bundle scaffold, protein

G-related albumin-binding module, or a DNA or RNA aptamer scaffold.

[154] In some cases, the serum half-life extending element comprises a binding site for a bulk serum protein. In some embodiments, the CDRs provide the binding site for the bulk serum protein. The bulk serum protein is, in some examples, a globulin, albumin, transferrin, IgGl, IgG2, IgG4, IgG3, IgA monomer, Factor XIII, Fibrinogen, IgE, or pentameric IgM. In some embodiments, the CDR form a binding site for an immunoglobulin light chain, such as an IgK free light chain or an IgX free light chain.

[155] The serum half-life extension element can be any type of binding domain, including but not limited to, domains from a monoclonal antibody, a polyclonal antibody, a recombinant antibody, a human antibody, a humanized antibody. In some embodiments, the binding moiety is a single chain variable fragment (scFv), single-domain antibody such as a heavy chain variable domain (VH), a light chain variable domain (VL) and a variable domain (VHH) of camelid derived nanobody. In other embodiments, the binding moieties are non-Ig binding domains, i.e., antibody mimetic, such as anticalins, affilins, affibody molecules, affimers, affitins, alphabodies, avimers, DARPins, fynomers, kunitz domain peptides, and monobodies.

[156] In other embodiments, the serum half-life extension element can be a water-soluble polymer or a peptide that is conjugated to a water-soluble polymer, such as PEG. “PEG,” “polyethylene glycol” and “poly(ethylene glycol)” as used herein, are interchangeable and encompass any nonpeptidic water-soluble poly(ethylene oxide). The term “PEG” also means a polymer that contains a majority, that is to say, greater than 50%, of —OCH2CH2— repeating subunits. With respect to specific forms, the PEG can take any number of a variety of molecular weights, as well as structures or geometries such as “branched,” “linear,” “forked,” “multifunctional,” and the Idee, to be described in greater detail below. The PEG is not limited to a particular structure and can be linear (e.g., an end capped, e.g., alkoxy PEG or a bifunctional PEG), branched or multi-armed (e.g., forked PEG or PEG attached to a polyol core), a dendritic (or star) architecture, each with or without one or more degradable linkages. Moreover, the internal structure of the PEG can be organized in any number of different repeat patterns and can be selected from the group consisting of homopolymer, alternating copolymer, random copolymer, block copolymer, alternating tripolymer, random tripolymer, and block tripolymer. PEGs can be conjugated to polypeptide and peptides through any suitable method. Typically, a reactive PEG derivative, such as N-hydroxysuccinamidyl ester PEG, is reacted with a peptide or polypeptide that includes amino acids with a side chain that contains an amine, sulfhydryl, carboxylic acid or hydroxyl functional group, such as cysteine, lysine, asparagine, glutamine, theonine, tyrosine, serine, aspartic acid, and glutamic acid.

Targeting and Retention Domains

[157] For certain applications, it may be desirable to maximize the amount of time the construct is present in its desired location in the body. This can be achieved by including one further domain in the chimeric polypeptide (fusion protein) to influence its movements within the body. For example, the chimeric nucleic acids can encode a domain that directs the polypeptide to a location in the body, e.g., tumor cells or a site of inflammation; this domain is termed a “targeting domain” and/or encode a domain that retains the polypeptide in a location in the body, e.g., tumor cells or a site of inflammation; this domain is termed a “retention domain”. In some embodiments a domain can function as both a targeting and a retention domain. In some embodiments, the targeting domain and/or retention domain are specific to a protease-rich environment. In some embodiments, the encoded targeting domain and/or retention domain are specific for regulatory T cells (Tregs), for example targeting the CCR4 or CD39 receptors. Other suitable targeting and/or retention domains comprise those that have a cognate ligand that is overexpressed in inflamed tissues, e.g., the IL-1 receptor, or the IL-6 receptor. In other embodiments, the suitable targeting and/or retention domains comprise those who have a cognate ligand that is overexpressed in tumor tissue, e.g., Epcam, CEA or mesothelin. In some embodiments, the targeting domain is linked to the interleukin via a linker which is cleaved at the site of action (e.g. by inflammation or cancer specific proteases) releasing the interleukin full activity at the desired site. In some embodiments, the targeting and/or retention domain is linked to the interleukin via a linker which is not cleaved at the site of action (e.g. by inflammation or cancer specific proteases), causing the cytokine to remain at the desired site.

[158] Antigens of choice, in some cases, are expressed on the surface of a diseased cell or tissue, for example a tumor or a cancer cell. Antigens useful for tumor targeting and retention include but are not limited to EpCAM, EGFR, HER-2, HER-3, c-Met, FOLRI, and CEA. Pharmaceutical compositions disclosed herein, also include proteins comprising two targeting and/or retention domains that bind to two different target antigens known to be expressed on a diseased cell or tissue. Exemplary pairs of antigen binding domains include but are not limited to EGFR/CEA, EpCAM/CEA, and HER-2/HER3.

[159] Suitable targeting and/or retention domains include antigen-binding domains, such as antibodies and fragments thereof including, a polyclonal antibody, a recombinant antibody, a human antibody, a humanized antibody a single chain variable fragment (scFv), single-domain antibody such as a heavy chain variable domain (VH), a light chain variable domain (VL) and a variable domain of camelid-type nanobody (VHH), a dAb and the like. Other suitable antigen-binding domain include non-immunoglobulin proteins that mimic antibody binding and/or structure such as, anticalins, affilins, affibody molecules, affimers, affitins, alphabodies, avimers, DARPins, fynomers, kunitz domain peptides, monobodies, and binding domains based on other engineered scaffolds such as SpA, GroEL, fibronectin, lipocallin and CTLA4 scaffolds. Further examples of antigen-binding polypeptides include a ligand for a desired receptor, a ligand-binding portion of a receptor, a lectin,

and peptides that binds to or associates with one or more target antigens.

[160] In some embodiments, the targeting and/or retention domains specifically bind to a cell surface molecule. In some embodiments, the targeting and/or retention domains specifically bind to a tumor antigen. In some embodiments, the targeting polypeptides specifically and independently bind to a tumor antigen selected from at least one of Fibroblast activation protein alpha (FAPa), Trophoblast glycoprotein (5T4), Tumor-associated calcium signal transducer 2 (Trop2), Fibronectin EDB (EDB-FN), fibronectin EIIIB domain, CGS-2, EpCAM, EGFR, HER-2, HER-3, cMet, CEA, and FOLRI. In some embodiments, the targeting polypeptides specifically and independently bind to two different antigens, wherein at least one of the antigens is a tumor antigen selected from EpCAM, EGFR, HER-2, HER-3, cMet, CEA, and FOLRL

[161] The targeting and/or retention antigen can be a tumor antigen expressed on a tumor cell. Tumor antigens are well known in the art and include, for example, EpCAM, EGFR, HER-2, HER-3, c-Met, FOLRI, PSMA, CD38, BCMA, and CEA. 5T4, AFP, B7-H3, Cadherin-6, CAIX, CD117, CD123, CD138, CD166, CD19, CD20, CD205, CD22, CD30, CD33, CD352, CD37, CD44, CD52, CD56, CD70, CD71, CD74, CD79b, DLL3, EphA2, FAP, FGFR2, FGFR3, GPC3, gpA33, FLT-3, gpNMB, HPV-16 E6, HPV-16 E7, ITGA2, ITGA3, SLC39A6, MAGE, mesothelin, Mucl, Mucl6, NaPi2b, Nectin-4, P-cadherin, NY-ESO1, PRLR, PSCA, PTK7, ROR1, SLC44A4, SLTRK5, SLTRK6, STEAP1, TIM1, Trop2, WTL

[162] The targeting and/or retention antigen can be an immune checkpoint protein. Examples of immune checkpoint proteins include but are not limited to CD27, CD137,2B4, TIGIT, CD155, ICOS, HVEM, CD40L, LIGHT, TIM-1, 0X40, DNAM-1, PD-L1, PD1, PD-L2, CTLA-4, CD8, CD40, CEACAM1, CD48, CD70, A2AR, CD39, CD73, B7-H3, B7-H4, BTLA, IDO1, IDO2, TDO, KIR, LAG-3, TIM-3, or VISTA.

[163] The targeting and/or retention antigen can be a cell surface molecule such as a protein, lipid or polysaccharide. In some embodiments, a targeting and/or retention antigen is a on a tumor cell, virally infected cell, bacterially infected cell, damaged red blood cell, arterial plaque cell, inflamed or fibrotic tissue cell. The targeting and/or retention antigen can comprise an immune response modulator. Examples of immune response modulator include but are not limited to granulocyte-macrophage colony stimulating factor (GM-CSF), macrophage colony stimulating factor (M-CSF), granulocyte colony stimulating factor (G-CSF), interleukin 2 (IL-2), interleukin 3 (IL-3), interleukin 12 (IL-12), interleukin 15 (IL-15), B7-1 (CD80), B7-2 (CD86), GITRL, CD3, or GITR.

[164] The targeting and/or retention antigen can be a cytokine receptor. Examples, of cytokine receptors include but are not limited to Type I cytokine receptors, such as GM-CSF receptor, G-CSF receptor, Type I IL receptors, Epo receptor, LIF receptor, CNTF receptor, TPO receptor; Type II Cytokine receptors, such as IFN-alpha receptor (IFNAR1, IFNAR2), IFB-beta receptor, IFN-gamma receptor (IFNGR1, IFNGR2), Type II IL receptors; chemokine receptors, such as CC chemokine receptors, CXC chemokine receptors, CX3C chemokine receptors, XC chemokine receptors; tumor necrosis receptor superfamily receptors, such as TNFRSF5/CD40, TNFRSF8/CD30, TNFRSF7/CD27, TNFRSFlA/TNFRl/CD120a, TNFRSF1B / TNFR2 /

CD120b; TGF-beta receptors, such as TGF-beta receptor 1, TGF-beta receptor 2; Ig super family receptors, such as IL-1 receptors, CSF-1R, PDGFR (PDGFRA, PDGFRB), SCFR.

Linkers

[165] As stated above, the pharmaceutical compositions comprise one or more linker sequences. A linker sequence serves to provide flexibility between polypeptides, such that, for example, the blocking moiety is capable of inhibiting the activity of the cytokine polypeptide. The linker sequence can be located between any or all of the cytokine polypeptide, the serum half-life extension element, and/or the blocking moiety. As described herein at least one of the linkers is protease cleavable, and contains a (one or more) cleavage site for a (one or more) desired protease. Preferably, the desired protease is enriched or selectively expressed at the desired site of cytokine activity (e.g., the tumor microenvironment). Thus, the fusion protein is preferentially or selectively cleaved at the site of desired cytokine activity.

[166] Suitable linkers can be of different lengths, such as from 1 amino acid (e.g., Gly) to 20 amino acids, from 2 amino acids to 15 amino acids, from 3 amino acids to 12 amino acids, including 4 amino acids to 10 amino acids, amino acids to 9 amino acids, 6 amino acids to 8 amino acids, or 7 amino acids to 8 amino acids, and may be 1,2, 3,4, 5,6, 7, 8, 9,10,11,12,13,14, 15,16,17,18,19,20,21, 22,23,24,25,26,27,28,29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39,40,41,42,43,44,45,46,47,48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, or 60 amino acids.

[167] The orientation of the components of the pharmaceutical composition, are largely a matter of design choice and it is recognized that multiple orientations are possible and all are intended to be encompassed by this disclosure. For example, a blocking moiety can be located C-terminally or Nterminally to a cytokine polypeptide.

[168] Proteases known to be associated with diseased cells or tissues include but are not limited to serine proteases, cysteine proteases, aspartate proteases, threonine proteases, glutamic acid proteases, metalloproteases, asparagine peptide lyases, serum proteases, cathepsins, Cathepsin B, Cathepsin C, Cathepsin D, Cathepsin E, Cathepsin K, Cathepsin L, kallikreins, hKl, hK10, hK15, plasmin, collagenase, Type IV collagenase, stromelysin, Factor Xa, chymotrypsin-like protease, trypsin-like protease, elastase-like protease, subtilisin-like protease, actinidain, bromelain, calpain, caspases, caspase-3, Mirl-CP, papain, HIV-1 protease, HSV protease, CMV protease, chymosin, renin, pepsin, matriptase, legumain, plasmepsin, nepenthesin, metalloexopeptidases, metalloendopeptidases, matrix metalloproteases (MMP), MMP1, MMP2, MMP3, MMP8, MMP9, MMP13, MMP11, MMP14, urokinase plasminogen activator (uPA), enterokinase, prostate-specific antigen (PSA, hK3), interleukin-1β converting enzyme, thrombin, FAP (FAP-a), dipeptidyl peptidase, meprins, granzymes and dipeptidyl peptidase IV (DPPIV/CD26). Proteases capable of cleaving amino acid sequences encoded by the chimeric nucleic acid sequences provided herein can, for example, be selected from the group consisting of a prostate specific antigen (PSA), a matrix metalloproteinase (MMP), an A

Disintigrin and a Metalloproteinase (ADAM), a plasminogen activator, a cathepsin, a caspase, a tumor cell surface protease, and an elastase. The MMP can, for example, be matrix metalloproteinase 2 (MMP2) or matrix metalloproteinase 9 (MMP9).

[169] Proteases useful in the methods disclosed herein are presented in Table 1, and exemplary proteases and their cleavage site are presented in Table la:

Table 1. Proteases relevant to inflammation and cancer

<td> Protease</td><td> Specificity</td><td> Other aspects</td>

<td colspan="3"> Secreted by killer T cells:</td>

<td> Granzyme B (grB)</td><td> Cleaves after Asp residues (asp-ase)</td><td> Type of serine protease; strongly implicated in inducing perforin-dependent target cell apoptosis</td>

<td> Granzyme A (grA)</td><td> trypsin-like, cleaves after basic residues</td><td> Type of serine protease;</td>

<td> Granzyme H (grH)</td><td> Unknown substrate specificity</td><td> Type of serine protease; Other granzymes are also secreted by killer T cells, but not all are present in humans</td>

<td> Caspase-8</td><td> Cleaves after Asp residues</td><td> Type of cysteine protease; plays essential role in TCR-induced cellular expansionexact molecular role unclear</td>

<td> Mucosa-associated lymphoid tissue (MALT1)</td><td> Cleaves after arginine residues</td><td> Type of cysteine protease; likely acts both as a scaffold and proteolytically active enzyme in the CBM-dependent signaling pathway</td>

<td> Tryptase</td><td> Targets: angiotensin I, fibrinogen, prourokinase, TGFp; preferentially cleaves proteins after lysine or arginine residues</td><td> Type of mast cell-specific serine protease; trypsin-like; resistant to inhibition by macromolecular protease inhibitors expressed in mammals due to their tetrameric structure, with all sites facing narrow central pore; also associated with inflammation</td>

<td colspan="3"> Associated with inflammation:</td>

<td> Thrombin</td><td> Targets: FGF-2, HB-EGF, Osteo-pontin, PDGF, VEGF</td><td> Type of serine protease; modulates activity of vascular growth factors, chemokines and extracellular proteins; strengthens VEGF-induced proliferation; induces cell migration; angiogenic factor; regulates hemostasis</td>

<td> Chymase</td><td> Exhibit chymotrypsinlike specificity, cleaving proteins after aromatic amino acid residues</td><td> Type of mast cell-specific serine protease</td>

<td> Carboxypeptidase A (MC-CPA)</td><td> Cleaves amino acid residues from C-terminal</td><td> Type of zinc-dependent metalloproteinase</td>

<td></td><td> end of peptides and proteins</td><td></td>

<td> Kallikreins</td><td> Targets: high molecular weight kininogen, pro-urokinase</td><td> Type of serine protease; modulate relaxation response; contribute to inflammatory response; fibrin degradation</td>

<td> Elastase</td><td> Targets: E-cadherin, GMCSF, IL-1, IL-2, IL-6, IL8, _?38^^ TNFa, VEcadherin</td><td> Type of neutrophil serine protease; degrades ECM components; regulates inflammatory response; activates proapoptotic signaling</td>

<td> Cathepsin G</td><td> Targets: EGF, ENA-78, IL-8, MCP-1, MMP-2, MT1-MMP, PAI-1, RANTES, TGFp, TNFa</td><td> Type of serine protease; degrades ECM components; chemo-attractant of leukocytes; regulates inflammatory response; promotes apoptosis</td>

<td> PR-3</td><td> Targets: ENA-78, IL-8, IL-18, JNK, _?38^^ TNFa</td><td> Type of serine protease; promotes inflammatory response; activates proapoptotic signaling</td>

<td> Granzyme M (grM)</td><td> Cleaves after Met and other long, unbranched hydrophobic residues</td><td> Type of serine protease; only expressed in NK cells</td>

<td> Calpains</td><td> Cleave between Arg and Gly</td><td> Family of cysteine proteases; calciumdependent; activation is involved in the process of numerous inflammationassociated diseases</td>

Table la: Exemplary Proteases and Protease Recognition Sequences

<td> Protease</td><td> Cleavage Domain Sequence</td><td> SEQ ID NO:</td>

<td> MMP7</td><td> KRALGLPG</td><td> 3</td>

<td> MMP7</td><td> (DE)8RPLALWRS(DR)₈</td><td> 4</td>

<td> MMP9</td><td> PR(S/T)(L/I)(S/T)</td><td> 5</td>

<td> MMP9</td><td> LEATA</td><td> 6</td>

<td> MMP11</td><td> GGAANLVRGG</td><td> ר</td>

<td> MMP14</td><td> SGRIGFLRTA</td><td> 8</td>

<td> MMP</td><td> PLGLAG</td><td> 9</td>

<td> MMP</td><td> PLGLAX</td><td> 10</td>

<td> MMP</td><td> PLGC(me)AG</td><td> 11</td>

<td> MMP</td><td> ESPAYYTA</td><td> 12</td>

<td> MMP</td><td> RLQLKL</td><td> 13</td>

<td> MMP</td><td> RLQLKAC</td><td> 14</td>

<td> MMP2, MMP9, MMP14</td><td> EP(Cit)G(Hof)YL</td><td> 15</td>

<td> Urokinase plasminogen activator (uPA)</td><td> SGRSA</td><td> 16</td>

<td> Urokinase plasminogen activator (uPA)</td><td> DAFK</td><td> 17</td>

<td> Urokinase plasminogen activator (uPA)</td><td> GGGRR</td><td> 18</td>

<td> Lysosomal Enzyme</td><td> GFLG</td><td> 19</td>

<td> Lysosomal Enzyme</td><td> ALAL</td><td> 20</td>

<td> Lysosomal Enzyme</td><td> FK</td><td> 21</td>

<td> Cathepsin B</td><td> NLL</td><td> 22</td>

<td> Cathepsin D</td><td> PIC(Et)FF</td><td> 23</td>

<td> Cathepsin K</td><td> GGPRGLPG</td><td> 24</td>

<td> Prostate Specific Antigen</td><td> HSSKLQ</td><td> 25</td>

<td> Prostate Specific Antigen</td><td> HSSKLQL</td><td> 26</td>

<td> Prostate Specific Antigen</td><td> HSSKLQEDA</td><td> 27</td>

<td> Herpes Simplex Virus Protease</td><td> LVLASSSFGY</td><td> 28</td>

<td> HIV Protease</td><td> GVSQNYPIVG</td><td> 29</td>

<td> CMV Protease</td><td> GWQASCRLA</td><td> 30</td>

<td> Thrombin</td><td> F(Pip)RS</td><td> 31</td>

<td> Thrombin</td><td> DPRSFL</td><td> 32</td>

<td> Thrombin</td><td> PPRSFL</td><td> 33</td>

<td> Caspase-3</td><td> DEVD</td><td> 34</td>

<td> Caspase-3</td><td> DEVDP</td><td> 35</td>

<td> Caspase-3</td><td> KGSGDVEG</td><td> 36</td>

<td> Interleukin 1β converting enzyme</td><td> GWEHDG</td><td> 37</td>

<td> Enterokinase</td><td> EDDDDKA</td><td> 38</td>

<td> FAP</td><td> KQEQNPGST</td><td> 39</td>

<td> Kallikrein 2</td><td> GKAFRR</td><td> 40</td>

<td> Plasmin</td><td> DAFK</td><td> 41</td>

<td> Plasmin</td><td> DVLK</td><td> 42</td>

<td> Plasmin</td><td> DAFK</td><td> 43</td>

<td> TOP</td><td> ALLLALL</td><td> 44</td>

[170] Provided herein are pharmaceutical compositions comprising polypeptide sequences. As with all peptides, polypeptides, and proteins, including fragments thereof, it is understood that additional modifications in the amino acid sequence of the chimeric polypeptides (amino acid sequence variants) can occur that do not alter the nature or function of the peptides, polypeptides, or proteins. Such modifications include conservative amino acid substitutions and are discussed in greater detail below. [171] The compositions provided herein have a desired function. The compositions are comprised of at least a cytokine polypeptide, such as IL-2, IL-7, IL-12, IL-15, IL-18, IL-21, IFNa, or ΙΡΝγ, or a chemokine, such as CXCL10, CCL19, CCL20, CCL21, a blocking moiety, e.g. a steric blocking polypeptide, and an optional serum half-life extension element, and an optional targeting polypeptide, with one or more linkers connecting each polypeptide in the composition. The first polypeptide, e.g., an IL-2 mutein, is provided to be an active agent. The blocking moiety is provided to block the activity of the interleukin. The linker polypeptide, e.g., a protease cleavable polypeptide, is provided to be cleaved by a protease that is specifically expressed at the intended target of the active agent. Optionally, the blocking moiety blocks the activity of the first polypeptide by binding the interleukin polypeptide. In some embodiments, the blocking moiety, e.g. a steric blocking peptide, is linked to the interleukin via a protease-cleavable linker which is cleaved at the site of action (e.g. by inflammation-specific or tumor-specific proteases) releasing the cytokine full activity at the desired site.

[172] The protease cleavage site may be a naturally occurring protease cleavage site or an

artificially engineered protease cleavage site. The artificially engineered protease cleavage site can be cleaved by more than one protease specific to the desired environment in which cleavage will occur,

e.g. a tumor. The protease cleavage site may be cleavable by at least one protease, at least two proteases, at least three proteases, or at least four proteases.

[173] In some embodiments, the linker comprises glycine-glycine, a sortase-recognition motif, or a sortase-recognition motif and a peptide sequence (Gly4Ser)n (SEQ ID NO.: 443) or (Gly3Ser)n, (SEQ ID NO.: 444), wherein n is 1,2, 3,4 or 5. In one embodiment, the sortase-recognition motif comprises a peptide sequence LPXTG (SEQ ID NO.: 442), where X is any amino acid. In one embodiment, the covalent linkage is between a reactive lysine residue attached to the C-terminal of the cytokine polypeptide and a reactive aspartic acid attached to the N-terminal of the blocking or other moiety. In one embodiment, the covalent linkage is between a reactive aspartic acid residue attached to the N-terminal of the cytokine polypeptide and a reactive lysine residue attached to the Cterminal of the blocking or other moiety.

Cleavage and Inducibilitv

[174] As described herein, the activity of the cytokine polypeptide the context of the fusion protein is attenuated, and protease cleavage at the desired site of activity, such as in a tumor microenvironment, releases a form of the cytokine from the fusion protein that is much more active as a cytokine receptor agonist than the fusion protein. For example, the cytokine-receptor activating (agonist) activity of the fusion polypeptide can be at least about 10X, at least about 50X, at least about 100X, at least about 250X, at least about 500X, or at least about lOOOx less than the cytokine receptor activating activity of the cytokine polypeptide as a separate molecular entity. The cytokine polypeptide that is part of the fusion protein exists as a separate molecular entity when it contains an amino acid that is substantially identical to the cytokine polypeptide and does not substantially include additional amino acids and is not associated (by covalent or non-covalent bonds) with other molecules. If necessary, a cytokine polypeptide as a separate molecular entity may include some additional amino acid sequences, such as a tag or short sequence to aid in expression and/or purification.

[175] In other examples, the cytokine-receptor activating (agonist) activity of the fusion polypeptide is at least about 10X, at least about 50X, at least about 100X, at least about 250X, at least about 500X, or about lOOOx less than the cytokine receptor activating activity of the polypeptide that contains the cytokine polypeptide that is produced by cleavage of the protease cleavable linker in the fusion protein. In other words, the cytokine receptor activating (agonist) activity of the polypeptide that contains the cytokine polypeptide that is produced by cleavage of the protease cleavable linker in the fusion protein is at least about 10X, at least about 50X, at least about 100X, at least about 250X, at least about 500X, or at least about lOOOx greater than the cytokine receptor activating activity of the

fusion protein.

Polypeptide variants and amino acid substitutions

[176] The polypeptides described herein can include components (e.g., the cytokine, the blocking moiety) that have the same amino acid sequence of the corresponding naturally occurring protein (e.g., IL-2, IL-15, HSA) or can have an amino acid sequence that differs from the naturally occurring protein so long as the desired function is maintained. It is understood that one way to define any known modifications and derivatives or those that might arise, of the disclosed proteins and nucleic acids that encode them is through defining the sequence variants in terms of identity to specific known reference sequences. Specifically disclosed are polypeptides and nucleic acids which have at least, 70, 71, 72, 73, 74, 75,76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97,98, 99 percent identity to the chimeric polypeptides provided herein. For example, provided are polypeptides or nucleic acids that have at least, 70, 71, 72, 73, 74, 75,76, 77, 78,79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99 percent identity to the sequence of any of the nucleic acids or polypeptides described herein. Those of skill in the art readily understand how to determine the identity of two polypeptides or two nucleic acids. For example, the identity can be calculated after aligning the two sequences so that the identity is at its highest level.

[177] Another way of calculating identity can be performed by published algorithms. Optimal alignment of sequences for comparison may be conducted by the local identity algorithm of Smith and Waterman Adv. Appl. Math. 2:482 (1981), by the identity alignment algorithm of Needleman and Wunsch, J. Mol. Biol. 48:443 (1970), by the search for similarity method of Pearson and Lipman, Proc. Natl. Acad. Sci. USA 85:2444 (1988), by computerized implementations of these algorithms (GAP, BESTFIT, FASTA, and TFASTA in the Wisconsin Genetics Software Package, Genetics Computer Group, 575 Science Dr., Madison, Wis.), or by inspection.

[178] The same types of identity can be obtained for nucleic acids by, for example, the algorithms disclosed in Zuker, Science 244:48-52 (1989); Jaeger et al., Proc. Natl. Acad. Sci. USA 86:7706-7710 (1989); Jaeger et al., Methods Enzymol. 183:281-306 (1989), which are herein incorporated by reference for at least material related to nucleic acid alignment. It is understood that any of the methods typically can be used and that in certain instances the results of these various methods may differ, but the skilled artisan understands if identity is found with at least one of these methods, the sequences would be said to have the stated identity, and be disclosed herein.

[179] Protein modifications include amino acid sequence modifications. Modifications in amino acid sequence may arise naturally as allelic variations (e.g., due to genetic polymorphism), may arise due to environmental influence (e.g., by exposure to ultraviolet light), or may be produced by human intervention (e.g., by mutagenesis of cloned DNA sequences), such as induced point, deletion, insertion and substitution mutants. These modifications can result in changes in the amino acid sequence, provide silent mutations, modify a restriction site, or provide other specific mutations.

Amino acid sequence modifications typically fall into one or more of three classes: substitutional, insertional or deletional modifications. Insertions include amino and/or carboxyl terminal fusions as well as intrasequence insertions of single or multiple amino acid residues. Insertions ordinarily will be smaller insertions than those of amino or carboxyl terminal fusions, for example, on the order of one to four residues. Deletions are characterized by the removal of one or more amino acid residues from the protein sequence. Typically, no more than about from 2 to 6 residues are deleted at any one site within the protein molecule. Amino acid substitutions are typically of single residues, but can occur at a number of different locations at once; insertions usually will be on the order of about from 1 to 10 amino acid residues; and deletions will range about from 1 to 30 residues. Deletions or insertions preferably are made in adjacent pairs, i.e. a deletion of 2 residues or insertion of 2 residues. Substitutions, deletions, insertions or any combination thereof may be combined to arrive at a final construct. The mutations must not place the sequence out of reading frame and preferably will not create complementary regions that could produce secondary mRNA structure. Substitutional modifications are those in which at least one residue has been removed and a different residue inserted in its place. Such substitutions generally are made in accordance with the following Table 2 and are referred to as conservative substitutions.

Table 2. Exemplary amino acid substitutions

<td rowspan="2"> Amino Acid</td><td> Exemplary Substitutions</td>

<td></td>

<td> Ala</td><td> Ser, Gly, Cys</td>

<td> Arg</td><td> Lys, Gin, Met, He</td>

<td> Asn</td><td> Gin, His, Glu, Asp</td>

<td> Asp</td><td> Glu, Asn, Gin</td>

<td> Cys</td><td> Ser, Met, Thr</td>

<td> Gin</td><td> Asn, Lys, Glu, Asp</td>

<td> Glu</td><td> Asp, Asn, Gin</td>

<td> Gly</td><td> Pro, Ala</td>

<td> His</td><td> Asn, Gin</td>

<td> He</td><td> Leu, Vai, Met</td>

<td> Leu</td><td> He, Vai, Met</td>

<td> Lys</td><td> Arg, Gin, Met, He</td>

<td> Met</td><td> Leu, He, Vai</td>

<td> Phe</td><td> Met, Leu, Tyr, Trp, His</td>

<td> Ser</td><td> Thr, Met, Cys</td>

<td> Thr</td><td> Ser, Met, Vai</td>

<td> Trp</td><td> Tyr, Phe</td>

<td> Tyr</td><td> Trp, Phe, His</td>

<td> Vai</td><td> He, Leu, Met</td>

[180] Modifications, including the specific amino acid substitutions, are made by known methods. For example, modifications are made by site specific mutagenesis of nucleotides in the DNA encoding the polypeptide, thereby producing DNA encoding the modification, and thereafter expressing the DNA in recombinant cell culture. Techniques for making substitution mutations at predetermined sites in DNA having a known sequence are well known, for example M13 primer mutagenesis and PCR mutagenesis.

[181] Modifications can be selected to optimize binding. For example, affinity maturation techniques can be used to alter binding of the scFv by introducing random mutations inside the complementarity determining regions (CDRs). Such random mutations can be introduced using a variety of techniques, including radiation, chemical mutagens or error-prone PCR. Multiple rounds of mutation and selection can be performed using, for example, phage display.

[182] The disclosure also relates to nucleic acids that encode the chimeric polypeptides described herein, and to the use of such nucleic acids to produce the chimeric polypeptides and for therapeutic purposes. For example, the invention includes DNA and RNA molecules (e.g., mRNA, selfreplicating RNA) that encode a chimeric polypeptide and to the therapeutic use of such DNA and RNA molecules.

Exemplary Compositions

[183] Exemplary fusion proteins of the invention combine the above described elements in a variety of orientations. The orientations described in this section are meant as examples and are not to be

considered limiting.

[184] In some embodiments, the fusion protein comprises a cytokine, a blocking moiety and a halflife extension element. In some embodiments, the cytokine is positioned between the half-life extension element and the blocking moiety. In some embodiments, the cytokine is N-terminal to the blocking moiety and the half-life extension element. In some such embodiments, the cytokine is proximal to the blocking moiety; in some such embodiments, the cytokine is proximal to the half-life extension element. At least one protease-cleavable linker must be included in all embodiments, such that the cytokine may be active upon cleavage. In some embodiments, the cytokine is C-terminal to the blocking moiety and the half-life extension element. Additional elements may be attached to one another by a cleavable linker, a non-cleavable linker, or by direct fusion.

[185] In some embodiments, the blocking domains used are capable of extending half-life, and the cytokine is positioned between two such blocking domains. In some embodiments, the cytokine is positioned between two blocking domains, one of which is capable of extending half-life.

[186] In some embodiments, two cytokines are included in the same construct. In some embodiments, the cytokines are connected to two blocking domains each (three in total in one molecule), with a blocking domain between the two cytokine domains. In some embodiments, one or more additional half-life extension domains may be included to optimize pharmacokinetic properties. In some cases, it is beneficial to include two of the same cytokine to facilitate dimerization. An example of a cytokine that works as a dimer is IFN.

[187] In some embodiments, three cytokines are included in the same construct. In some embodiments, the third cytokine may function to block the other two in place of a blocking domain between the two cytokines.

[188] Preferred half-life extension elements for use in the fusion proteins are human serum albumin (HSA), an antibody or antibody fragment (e.g., scFV, dAb) which binds serum albumin, a human or humanized IgG, or a fragment of any of the foregoing. In some preferred embodiments, the blocking moiety is human serum albumin (HSA), or an antibody or antibody fragment which binds serum albumin, an antibody which binds the cytokine and prevents activation of binding or activation of the cytokine receptor, another cytokine, or a fragment of any of the foregoing. In preferred embodiments comprising an additional targeting domain, the targeting domain is an antibody which binds a cell surface protein which is enriched on the surface of cancer cells, such as EpCAM, FOLRI, and Fibronectin.

[189] In embodiments, the fusion protein can contain an IL-2 polypeptide. The fusion protein containing an IL-2 polypeptide can comprise or consist of the amino acid sequence of any one of SEQ ID NOs. 257-300, 302-317, 325-353, 355-365, 366, 372-381, 383-385, 388-420, 579-608 and 636646. The fusion proteins disclosed as SEQ ID NOs. 257-300, 302-317, 325-353,355-365, 366, 372381, 383-385, 388-420, 579-608, and 636-646 are also referred to herein as ACP289-ACP292,

ACP296-ACP302, WW0301, ACP304-ACP306, ACP309-ACP313, WW0353, ACP414, ACP336ACP398, WW0472-WW0477, ACP406-ACP426, ACP439-ACP447, ACP451-ACP471, WW0729, WW0734-WW0792, ACP101, ACP293-ACP295, ACP316-ACP335, ACP427-ACP438, and ACP448-ACP450. For example, the fusion protein can comprise the amino acid sequence of SEQ ID NO: 272. The fusion protien can comprise the amino acid sequence of SEQ ID NO: 286. The fusion protien can comprise the amino acid sequence of SEQ ID NO:362. The fusion protien can comprise the amino acid sequence of SEQ ID NO:336. The fusion protien can comprise the amino acid sequence of SEQ ID NO: 348. The fusion protien can comprise the amino acid sequence of SEQ ID NO: 363. The fusion protien can comprise the amino acid sequence of SEQ ID NO: 580.

[190] In embodiments, the fusion protein can contain an IL-12 polypeptide. The fusion protein containing an IL-12 polypeptide can comprise or consist of the amino acid sequence of any one of SEQ ID NOs. 368-371,434-440,453-519, or 523-538. The fusion proteins disclosed as SEQ ID NOs. 368-371,434-440,453-519, or 523-538 are referred to herein as ACP240-ACP245, ACP247, ACP285-ACP288, WW0641, WW0649-WW0652, WW0662-WW0725, WW0765-WW0772, and WW0796-WW0803. For example, the fusion protein can comprise the amino acid sequence of SEQ ID NO:459. The fusion protein can comprise the amino acid sequence of SEQ ID NO: 466. The fusion protein can comprise the amino acid sequence of SEQ ID NO: 484. The fusion protein can comprise the amino acid sequence of SEQ ID NO: 506.

[191] In embodiments, the fusion protein contains an IFN (e.g., IFNgamma, IFNalpha, IFNbeta) polypeptide. In some examples the IFN polypeptide is an IFNalpha or an IFNbeta. The fusion protein containing an IFN polypeptide can comprise or consist of the amino acid sequence of SEQ ID NOs. 421-430, and 539-578. The fusion proteins disclosed as SEQ ID NOs. 421-430, and 539-578 can be referred to herein as ACP200-ACP209, WW0644-WW0648, WW0781-WW0786, WW0815WW0822, WW0831-WW0834, WW0737-WW0748, and WW0787-WW0790. For example, the fusion protein can comprise the amino acid sequence of SEQ ID NO: 421. The fusion protein can comprise the amino acid sequence of SEQ ID NO: 428. The fusion protein can comprise the amino acid sequence of 541. The fusion protein can comprise the amino acid sequence of SEQ IND NO: 558. The fusion protein can comprise the amino acid sequence of SEQ ID NO: 577.

[192] In some aspects, the fusion polypeptide disclosed herein can be covalently or non-covalently bonded to a second polypeptide chain. For example, a fusion polypeptide can dimerize (i.e. form a dimer) or a portion of a fusion polypeptide may associate with another polypeptide, for example, to form a functional binding site for a cytokine polypeptide or serum albumin. In certain embodiments, the second polypeptide chain and the blocking moiety on the fusion polypeptide are complementary and together form a functional binding site that has specificity for the cytokine polypeptide contained in the fusion polypeptide. Exemplary functional binding sites that can be formed by the blocking moiety of the fusion polypeptide and a complimentary second polypeptide include antigen binding

sites of antibodies, such as a Fab fragment of an antibody or a portion thereof. For example, one chain of a Fab that binds the cytokine can be the blocking moiety of the fusion polypeptide, e.g., a VH-CH1, and the complementary VL-CL can be part of the second polypeptide. In such situations, the blocking moiety of the fusion protein i.e., VH-CH1 and the second polypeptide that comprises the complementary VL-CL, can associate to form a functional binding site with specificity for the cytokine polypeptide contained within the fusion protein (e.g., IL-2, IL-12, IFNalpha, IFNbeta) and attenuates cytokine polypeptide activity. At least a portion of the blocking moiety can be on the second polypeptide chain can comprise at least a portion of the blocking moiety that associates with the blocking moiety on the fusion polypeptide.

[193] In embodiments, the fusion protein containing an IL-2 cytokine polypeptide can be bonded covalently or noncovalently to a second polypeptide chain. The second polypeptide chain can contain an antibody light chain VL-CL that comprises or consist of the amino acid sequence of SEQ ID NO: 263,264, or 333. Such a second polypeptide can bond with a complimentary VH-CH1 polypeptide contained within the fusion protein, e.g., as contained within SEQ ID NOS: 362,363, 325,286, 579, 581, or 582 . The second polypeptide chain disclosed as SEQ ID NOs. 263,264, and 333 can be referred herein as WW0523 (ACP381), WW0524 (ACP382), or WW0556 (ACP414).

[194] In embodiments, the fusion polypeptide can comprise or consist of the amino acid sequence of SEQ ID NOs. 362, 363, 325,286, 579, 581, or 582 and the second polypeptide chain can comprise or consist of the amino acid sequence of SEQ ID NOs: 263,264, or 333. The fusion polypeptide disclosed as SEQ ID NOs. 362, 363, 325,286, 579, 581, or 582 can be referred to as WW0520 (ACP378), WW0521 (ACP379), WW0548 (ACP406), WW0621 (ACP457), WW0729, WW0735, or WW0736, and the second polypeptide chain disclosed as SEQ ID NOs. 263,264, and 333 can be referred herein as WW0523 (ACP381), WW0524 (ACP382), or WW0556 (ACP414).

[195] For example, the fusion protein can comprise or consist the amino acid sequence of SEQ ID NO: 362 and the second polypeptide chain can comprise or consist the amino acid sequence of SEQ ID NO: 263. For example, the fusion protein can comprise or consist the amino acid sequence of SEQ ID NO: 362 and the second polypeptide chain can comprise or consist the amino acid sequence of SEQ ID NO: 264. For example, the fusion protein can comprise or consist the amino acid sequence of SEQ ID NO: 362 and the second polypeptide chain can comprise or consist the amino acid sequence of SEQ ID NO: 333. For example, the fusion protein can comprise or consist of an amino acid sequence of SEQ ID NO: 363 and the second polypeptide chain can comprise or consist of an amino acid sequence of SEQ ID NO: 263. For example, the fusion protein can comprise or consist of an amino acid sequence of SEQ ID No. 363 and the second polypeptide chain can comprise or consist of an amino acid sequence of SEQ ID NO: 264. For example, the fusion protein can comprise or consist of an amino acid sequence of SEQ ID NO: 363 and the second polypeptide chain can comprise or consist of an amino acid sequence of SEQ ID NO: 333. For example, the fusion protein can comprise

or consist of an amino acid sequence of SEQ ID NO: 325 and the second polypeptide chain can comprise or consist of an amino acid sequence of SEQ ID NO: 264. For example, the fusion protein can comprise or consist of an amino acid sequence of SEQ ID NO: 325 and the second polypeptide chain can comprise or consist of an amino acid sequence of SEQ ID NO: 333. For example, the fusion protein can comprise or consist of an amino acid sequence of SEQ ID NO: 325 and the second polypeptide chain can comprise or consist of an amino acid sequence of SEQ ID NO: 263. For example, the fusion protein can comprise or consist of an amino acid sequence of SEQ ID NO: 286 and the second polypeptide chain can comprise or consist of an amino acid sequence of SEQ ID NO: 263. For example, the fusion protein can comprise or consist of an amino acid sequence of SEQ ID NO: 286 and the second polypeptide chain can comprise or consist of an amino acid sequence of SEQ ID NO: 264. For example, the fusion protein can comprise or consist of an amino acid sequence of SEQ ID NO: 286, and the second polypeptide can comprise or consist of an amino acid sequence of SEW ID NO: 333. For example, the fusion protein can comprise or consist of an amino acid sequence of SEQ ID NO: 579 and the second polypeptide chain can comprise or consist of an amino acid sequence of SEQ ID NO: 263. For example, the fusion protein can comprise or consist of an amino acid sequence of SEQ ID NO: 579 and the second polypeptide chain can comprise or consist of an amino acid sequence of SEQ ID NO: 264. For example, the fusion protein can comprise or consist of an amino acid sequence of SEQ ID NO: 579 and the second polypeptide chain can comprise or consist of an amino acid sequence of SEQ ID NO: 233. For example, the fusion protein can comprise or consist of SEQ ID NO: 581 and the second polypeptide chain can comprise or consist of SEQ ID NO.: 263. For example, the fusion protein can comprise or consist of SEQ ID NO: 581 and the second polypeptide chain can comprise or consist of SEQ ID NO.: 264. For example, the fusion protein can comprise or consist of SEQ ID NO: 581 and the second polypeptide chain can comprise or consist of SEQ ID NO.: 333. For example, the fusion protein can comprise or consist of SEQ ID NO: 582 and the second polypeptide chain can comprise or consist of SEQ ID NO: 263. For example, the fusion protein can comprise or consist of SEQ ID NO: 582 and the second polypeptide chain can comprise or consist of SEQ ID NO: 264. For example, the fusion protein can comprise or consist of SEQ ID NO: 582 and the second polypeptide chain can comprise or consist of SEQ ID NO: 333.

Methods of treatment and Pharmaceutical Compositions

[196] This disclosure also relates to pharmaceutical compositions that comprise one or more fusion proteins as disclosed herein, optionally in combination with another therapeutic agent, which are preferably immunomodulators or anti-cancer agents. The disclosure also relates to the use of such pharmaceutical compositions, and one or more fusion proteins, optionally in combination with another therapeutic agent in treatment of cancers.

[197] The therapeutic combinations disclosed herein can comprise, for example, a fusion protein containing an IL-2 polypeptide, a fusion protein containing an IL-12 polypeptide, or a fusion protein

containing an IFN polypeptide. Therapy can be provided using two or more fusion proteins. For example, the therapeutic combination can comprise a fusion protein containing an IL-2 polypeptide and a fusion protein containing an IL-12 polypeptide, a fusion protein containing an IL-2 polypeptide and a fusion protein containing an IFN polypeptide, a fusion protein containing an IL-12 polypeptide and a fusion protein containing an IFN polypeptide.

[198] The therapeutic combinations disclosed herein can comprise a fusion polypeptide cytokine polypeptide [A], a blocking moiety [D], optionally a half-life extension moiety [H], and a proteasecleavable polypeptide linker; wherein the cytokine polypeptide and the blocking moiety and the optional half-life extension element when present are operably linked by the protease-cleavable polypeptide linker and the fusion polypeptide has attenuated cytokine receptor activating activity, wherein the cytokine-receptor activating activity of the fusion polypeptide is at least about 10X less than the cytokine receptor activating activity of the polypeptide that contains the cytokine polypeptide that is produced by cleavage of the protease cleavable linker, the fusion polypeptide has the formula:

[A]-[L1]-[H]-[L2]-[D] (I);

[D]-[L2]-[H]-[L1]-[A] (II);

[A]-[L1]-[D]-[L2]-[H] (III);

[H]-[L2]-[D]-[L1]-[A] (IV);

[H]-[L1]-[A]-[L2’]-[D] (V);

[D]-[L1]-[A]-[L2’]-[H] (VI);

wherein [A] is a cytokine polypeptide, [D] is a blocking moiety, [H] is a half-life extension moiety, [LI] is a protease-cleavable polypeptide linker, [L2] is an polypeptide linker that is optionally protease-cleavable, and [L2’] is a protease-cleavable polypeptide linker.

The therapeutic compositions can comprise a second fusion polypeptide comprising at least one of each of: a second cytokine polypeptide [A], a blocking moiety [D]optionally a half-life extension element [H]; and a protease-cleavable polypeptide linker [L]; wherein the cytokine polypeptide and the cytokine blocking moiety and the optional half-life extension element when present are operably linked by the protease-cleavable polypeptide linker and the fusion polypeptide has attenuated cytokine receptor activating activity, wherein the cytokine-receptor activating activity of the fusion polypeptide is at least about 10X less than the cytokine receptor activating activity of the polypeptide that contains the cytokine polypeptide that is produced by cleavage of the protease cleavable linker. The second fusion polypeptide can have the formula:

[A]-[L1]-[H]-[L2]-[D] (I);

[D]-[L2]-[H]-[L1]-[A] (II);

[A]-[L1]-[D]-[L2]-[H] (III);

[H]-[L2]-[D]-[L1]-[A] (IV);

[H]-[L1]-[A]-[L2’]-[D] (V);

[D]-[L1]-[A]-[L2’]-[H] (VI);

wherein [A] is a cytokine polypeptide, [D] is a blocking moiety, [H] is a half-life extension moiety,

[LI] is a protease-cleavable polypeptide linker, [L2] is an polypeptide linker that is optionally protease-cleavable, and [L2’] is a protease-cleavable polypeptide linker.

[199] The therapeutic combinations disclosed herein can comprise a first fusion protein comprising an amino acid selected from the group consisting of SEQ ID NOs. 257-300, 302-317, 325-353, 355365, 366, 372-381, 383-385, 388-420, 579-608,636-646, 368-371,434-440,453-519, 523-538,421430, and 539-578 and a second fusion protein comprising an amino acid sequence selected from the group consisting of selected from the group consisting of SEQ ID NOs. 257-300,302-317, 325-353, 355-365, 366, 372-381, 383-385, 388-420, 579-608,636-646, 368-371,434-440,453-519, 523-538, 421-430, and 539-578. It is preferred that the first fusion protein and the second fusion protein are different. In some preferred embodiments, the therapeutic combination comprises a first fusion protein comprising an amino acid sequence selected from SEQ ID NO: 257-300, 302-317, 325-353, 355-365, 366, 372-381, 383-385, 388-420, 579-608,636-646 and a second fusion protein comprising an amino acid sequence selected from SEQ ID NO: 368-371,434-440,453-519, 523-538,421-430, and 539-578. In some preferred embodiments, the therapeutic combination comprises a first fusion proteins comprising an amino acid sequence selected from SEQ ID NO: 368-371,434-440,453-519, or 523-538 and a second fusion protein comprising an amino acid sequence selected from SEQ ID NO: 257-300, 302-317, 325-353, 355-365, 366, 372-381, 383-385, 388-420, 636-646, 579-608,421430, and 539-578. In some preferred embodiments, the therapeutic combination comprises a first fusion protein comprising an amino acid sequence selected from SEQ ID NO: 421-430, and 539-578 and a second fusion protein comprising an amino acid sequence selected from SEQ ID NOs. 257-300, 302-317, 325-353, 355-365, 366, 372-381,383-385, 388-420, 579-608, 636-646, 368-371,434-440, 453-519, 523-538, or combinations thereof.

[200] The therapeutic combination disclosed herein can comprise a first fusion protein that is covalently or non-covalently bonded to a second polypeptide chain and a therapeutic agent. The therapeutic combination can comprise (i) a fusion polypeptide comprising an amino acid sequence selected from SEQ ID NOs. 362, 363, 325,286, 579, 581, or 582 and a second polypeptide chain comprising the amino acid sequence of SEQ ID NOs: 263, 264, or 333, and (ii) a second therapeutic agent, wherein the second therapeutic agent is a second fusion polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NOs. 257-300, 302-317, 325-353, 355-365, 366, 372-381, 383-385, 388-420, 579-608, 636-646,368-371,434-440,453-519, 523-538,421-430, 539-578, or combinations thereof. It is preferred that the first fusion protein and the second fusion protein are not the same.

[201] In embodiments, the therapeutic combination can comprise an additional therapeutic agent (e.g., one, two, three, four, five, or more therapeutic agents). In embodiments, the therapeutic

combination can comprise 2 or more fusion proteins and one or more therapeutic agents, preferably agents for treating cancer.

[202] Other exemplary therapeutic agents include, but are not limited to chemotherapeutic agents (e.g., Adriamycin, Cerubidine, Bleomycin, Alkeran, Velban, Oncovin, Fluorouracil, Thiotepa, Methotrexate, Bisantrene, Noantrone, Thiguanine, Cytaribine, Procarabizine), immuno-oncology agents (e.g., anti-PD-Ll, anti-CTLA4, anti-PD-1, anti-CD47, anti-GD2, VEGF inhibitor), antibodydrug conjugates, cellular therapies (e.g, CAR-T, T-cell therapy), oncolytic viruses, radiation therapy and/or small molecules.

[203] Non-limiting examples of anti-cancer agents that can be used include acivicin; aclarubicin; acodazole hydrochloride; acronine; adozelesin; aldesleukin; altretamine; ambomycin; ametantrone acetate; aminoglutethimide; amsacrine; anastrozole; anthramycin; asparaginase; asperlin; azacitidine; azetepa; azotomycin; batimastat; benzodepa; bicalutamide; bisantrene hydrochloride; bisnafide dimesylate; bizelesin; bleomycin sulfate; brequinar sodium; bropirimine; busulfan; cactinomycin; calusterone; caracemide; carbetimer; carboplatin; carmustine; carubicin hydrochloride; carzelesin; cedefingol; chlorambucil; cirolemycin; cisplatin; cladribine; crisnatol mesylate; cyclophosphamide; cytarabine; dacarbazine; dactinomycin; daunorubicin hydrochloride; decitabine; dexormaplatin; dezaguanine; dezaguanine mesylate; diaziquone; docetaxel; doxorubicin; doxorubicin hydrochloride; droloxifene; droloxifene citrate; dromostanolone propionate; duazomycin; edatrexate; eflomithine hydrochloride; elsamitrucin; enloplatin; enpromate; epipropidine; epirubicin hydrochloride; erbulozole; esorubicin hydrochloride; estramustine; estramustine phosphate sodium; etanidazole; etoposide; etoposide phosphate; etoprine; fadrozole hydrochloride; fazarabine; fenretinide; floxuridine; fludarabine phosphate; fluorouracil; flurocitabine; fosquidone; fostriecin sodium; gemcitabine; gemcitabine hydrochloride; hydroxyurea; idarubicin hydrochloride; ifosfamide; ilmofosine; interleukin II (including recombinant interleukin II, or rIL2), interferon alpha-2a; interferon alpha-2b; interferon alpha-nl interferon alpha-n3; interferon beta-I a; interferon gamma-I b; iproplatin; irinotecan hydrochloride; lanreotide acetate; letrozole; leuprolide acetate; liarozole hydrochloride; lometrexol sodium; lomustine; losoxantrone hydrochloride; masoprocol; maytansine; mechlorethamine hydrochloride; megestrol acetate; melengestrol acetate; melphalan; menogaril; mercaptopurine; methotrexate; methotrexate sodium; metoprine; meturedepa; mitindomide; mitocarcin; mitocromin; mitogillin; mitomalcin; mitomycin; mitosper; mitotane; mitoxantrone hydrochloride; mycophenolic acid; nocodazole; nogalamycin; ormaplatin; oxisuran; paclitaxel; pegaspargase; peliomycin; pentamustine; peplomycin sulfate; perfosfamide; pipobroman; piposulfan; piroxantrone hydrochloride; plicamycin; plomestane; porfimer sodium; porfiromycin; prednimustine; procarbazine hydrochloride; puromycin; puromycin hydrochloride; pyrazofurin; riboprine; rogletimide; safingol; safingol hydrochloride; semustine; simtrazene; sparfosate sodium; sparsomycin; spirogermanium hydrochloride; spiromustine; spiroplatin; streptonigrin; streptozocin; sulofenur;

talisomycin; tecogalan sodium; tegafur; teloxantrone hydrochloride; temoporfin; teniposide; teroxirone; testolactone; thiamiprine; thioguanine; thiotepa; tiazofurin; tirapazamine; toremifene citrate; trestolone acetate; triciribine phosphate; trimetrexate; trimetrexate glucuronate; triptorelin; tubulozole hydrochloride; uracil mustard; uredepa; vapreotide; verteporfin; vinblastine sulfate; vincristine sulfate; vindesine; vindesine sulfate; vinepidine sulfate; vinglycinate sulfate; vinleurosine sulfate; vinorelbine tartrate; vinzolidine sulfate; vinzolidine sulfate; vorozole; zeniplatin; zinostatin; zorubicin hydrochloride.

[204] Accordingly, this disclosure relates to a therapeutic combination of any of the fusions proteins disclosed herein (e.g., fusion proteins that comprise an IL-2 polypeptide, and IL-12 polypeptide or an IFN polypeptide) in combination with a chemotherapeutic agent, such as Adriamycin, Cerubidine, Bleomycin, Alkeran, Velban, Oncovin, Fluorouracil, Thiotepa, Methotrexate, Bisantrene, Noantrone, Thiguanine, Cytaribine, Procarabizine. This disclosure relates to a therapeutic combination of any of the fusions proteins disclosed herein (e.g., fusion proteins that comprise an IL-2 polypeptide, and IL12 polypeptide or an IFN polypeptide) in combination with an antibody-drug conjugate. A variety of antibody drug conjugates that are suitable for use in cancer therapy are well known and typically include an antibody that binds to a cellular antigen that is preferentially express or expressed at high levels on tumor cells, and a cytotoxic drug. This disclosure relates to a therapeutic combination of any of the fusion proteins disclosed herein (e.g., fusion proteins that comprise an IL-2 polypeptide, and IL-12 polypeptide, or an IFN polypeptide) in combination with a cellular therapy, such as CAR-T or T-cell therapy. The disclosure relates to a therapeutic combination of the fusion proteins disclosed herein (e.g., fusion proteins that comprise an IL-2 polypeptide, and IL-12 polypeptide, or an IFN polypeptide) in combination with an oncolytic virus. Exemplary oncolytic viruses include, oncolytic adenoviruses, type 1 herpes simplex virus (HSV), polioviruses, measles virus (MV), Newcastle disease virus (NDV), reoviruses, vesicular stomatitis virus (VSV), and Zika virus. This disclosure relates to a therapeutic combination of any of the fusion proteins disclosed herein (e.g., fusion proteins that comprise an IL-2 polypeptide, and IL-12 polypeptide, or an IFN polypeptide) in combination with radiation therapy, such an external beam radiation or internal therapy radiation therapy.

[205] This disclosure relates to a therapeutic combination of any of the fusion proteins disclosed herein (e.g., fusion proteins that comprise an IL-2 polypeptide, and IL-12 polypeptide, or an IFN polypeptide) in combination with cytokines (e.g., IL-2, IL-15), signal induction inhibitors (e.g., BRAF inhibitors or MEK inhibitors), checkpoint inhibitors (e.g., PDL-1, PD-1, CTLA-4), c-met inhibitors, kinase inhibitors (e.g., VGEF inhibitors), a proteasome inhibitor, mTOR inhibitor, angiogenesis inhibitor. In embodiments, any one of the fusion proteins disclosed herein (e.g., fusion proteins that comprise an IL-2 polypeptide, and IL-12 polypeptide, or an IFN polypeptide) can be combined with an anti-PD-Ll agent or an anti-PD-1 agent. Exemplary PD-1 and/or PD-L1 inhibitors include, but are

not limited to Spartalizumab, Camrelizumab, Sintilimab, Tislelizumab, Toripalimab, Dostarlimab,

INCMGA00012, AMP-224, and AMP-514). In embodiments, a fusion protein comprising the amino acid sequence selected from SEQ ID NO: 257-300, 302-317, 325-353, 355-365, 366, 372-381, 383385, 388-420, 579-608, 636-646, 368-371,434-440,453-519, 523-538,421-430, and 539-578 can be combined with a check-point inhibitor, such as PDL-1, PD-1, or CTL-4.

[206] Further provided are methods of treating a subject with or at risk of developing an of a disease or disorder, such as proliferative disease, a tumorous disease, an inflammatory disease, an immunological disorder, an autoimmune disease, an infectious disease, a viral disease, an allergic reaction, a parasitic reaction, or graft-versus-host disease. The methods disclosed herein are preferably used to treat a subject having cancer. The methods administering to a subject in need thereof an effective amount of a fusion protein as disclosed herein that is typically administered as a pharmaceutical composition. In some embodiments, the method further comprises selecting a subject with or at risk of developing such a disease or disorder. The pharmaceutical composition preferably comprises a blocked cytokine, fragment, variant, subunit, or mutein thereof that is activated at a site of inflammation or a tumor. In one embodiment, the chimeric polypeptide comprises a cytokine polypeptide, fragment or mutein thereof and a serum half-life extension element. In another embodiment, the chimeric polypeptide comprises a cytokine polypeptide, variant, subunit, fragment or mutein thereof and a blocking moiety, e.g. a steric blocking polypeptide, wherein the steric blocking polypeptide is capable of sterically blocking the activity of the cytokine polypeptide, fragment or mutein thereof. In another embodiment, the chimeric polypeptide comprises a cytokine polypeptide, fragment or mutein thereof, a blocking moiety, and a serum half-life extension element.

[207] Inflammation is part of the complex biological response of body tissues to harmful stimuli, such as pathogens, damaged cells, or irritants, and is a protective response involving immune cells, blood vessels, and molecular mediators. The function of inflammation is to eliminate the initial cause of cell injury, clear out necrotic cells and tissues damaged from the original insult and the inflammatory process, and to initiate tissue repair. Inflammation can occur from infection, as a symptom or a disease, e.g., cancer, atherosclerosis, allergies, myopathies, HIV, obesity, or an autoimmune disease. An autoimmune disease is a chronic condition arising from an abnormal immune response to a self-antigen. Autoimmune diseases that may be treated with the polypeptides disclosed herein include but are not limited to lupus, celiac disease, diabetes mellitus type 1, Graves disease, inflammatory bowel disease, multiple sclerosis, psoriasis, rheumatoid arthritis, and systemic lupus erythematosus.

[208] The pharmaceutical composition can comprise one or more protease-cleavable linker sequences. The linker sequence serves to provide flexibility between polypeptides, such that each polypeptide is capable of inhibiting the activity of the first polypeptide. The linker sequence can be located between any or all of the cytokine polypeptide, fragment or mutein thereof, the blocking

moiety, and serum half-life extension element. Optionally, the composition comprises, two, three, four, or five linker sequences. The linker sequence, two, three, or four linker sequences can be the same or different linker sequences. In one embodiment, the linker sequence comprises GGGGS (SEQ ID NO.: 449), GSGSGS (SEQ ID NO.: 450), or G(SGGG)2SGGT (SEQ ID NO.: 451). In another embodiment, the linker comprises a protease-cleavable sequence selected from group consisting of HSSKLQ (SEQ ID NO.: 25), GPLGVRG (SEQ ID NO.: 445), IPVSLRSG (SEQ ID NO.: 446), VPLSLYSG (SEQ ID NO.: 447), and SGESPAYYTA (SEQ ID NO.: 448).

[209] In some embodiments, the linker is cleaved by a protease selected from the group consisting of a kallikrein, thrombin, chymase, carboxypeptidase A, cathepsin G, an elastase, PR-3, granzyme M, a calpain, a matrix metalloproteinase (MMP), a plasminogen activator, a cathepsin, a caspase, a tryptase, or a tumor cell surface protease.

[210] Suitable linkers can be of different lengths, such as from 1 amino acid (e.g., Gly) to 20 amino acids, from 2 amino acids to 15 amino acids, from 3 amino acids to 12 amino acids, including 4 amino acids to 10 amino acids, amino acids to 9 amino acids, 6 amino acids to 8 amino acids, or 7 amino acids to 8 amino acids, and may be 1,2, 3,4, 5,6, 7, 8, 9,10,11,12,13,14, 15,16,17,18,19,20,21, 22,23,24,25,26,27,28,29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39,40,41,42,43,44,45,46,47,48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, or 60 amino acids.

[211] Further provided are methods of treating a subject with or at risk of developing cancer. The methods comprise administering to the subject in need thereof an effective amount of a chimeric polypeptide (a fusion protein) as disclosed herein that is typically administered as a pharmaceutical composition. In some embodiments, the method further comprises selecting a subject with or at risk of developing cancer. The pharmaceutical composition preferably comprises a blocked cytokine, fragment or mutein thereof that is activated at a tumor site.

[212] The methods disclosed herein can be used for any suitable cancer including, hematological malignancy, solid tumors, sarcomas, carcinomas, and other solid and non-solid tumors. Illustrative suitable cancers include, for example, acute lymphoblastic leukemia (ALL), acute myeloid leukemia (AML), adrenocortical carcinoma, anal cancer, appendix cancer, astrocytoma, basal cell carcinoma, brain tumor, bile duct cancer, bladder cancer, bone cancer, breast cancer, bronchial tumor, carcinoma of unknown primary origin, cardiac tumor, cervical cancer, chordoma, colon cancer, colorectal cancer, craniopharyngioma, ductal carcinoma, embryonal tumor, endometrial cancer, ependymoma, esophageal cancer, esthesioneuroblastoma, fibrous histiocytoma, Ewing sarcoma, eye cancer, germ cell tumor, gallbladder cancer, gastric cancer, gastrointestinal carcinoid tumor, gastrointestinal stromal tumor, gestational trophoblastic disease, glioma, head and neck cancer, hepatocellular cancer, histiocytosis, Hodgkin lymphoma, hypopharyngeal cancer, intraocular melanoma, islet cell tumor, Kaposi sarcoma, kidney cancer, Langerhans cell histiocytosis, laryngeal cancer, lip and oral cavity cancer, liver cancer, lobular carcinoma in situ, lung cancer, macroglobulinemia, malignant fibrous

histiocytoma, melanoma, Merkel cell carcinoma, mesothelioma, metastatic squamous neck cancer with occult primary, midline tract carcinoma involving NUT gene, mouth cancer, multiple endocrine neoplasia syndrome, multiple myeloma, mycosis fungoides, myelodysplastic syndrome, myelodysplastic/myeloproliferative neoplasm, nasal cavity and par nasal sinus cancer, nasopharyngeal cancer, neuroblastoma, non-small cell lung cancer, oropharyngeal cancer, osteosarcoma, ovarian cancer, pancreatic cancer, papillomatosis, paraganglioma, parathyroid cancer, penile cancer, pharyngeal cancer, pheochromocytomas, pituitary tumor, pleuropulmonary blastoma, primary central nervous system lymphoma, prostate cancer, rectal cancer, renal cell cancer, renal pelvis and ureter cancer, retinoblastoma, rhabdoid tumor, salivary gland cancer, Sezary syndrome, skin cancer, small cell lung cancer, small intestine cancer, soft tissue sarcoma, spinal cord tumor, stomach cancer, T-cell lymphoma, teratoid tumor, testicular cancer, throat cancer, thymoma and thymic carcinoma, thyroid cancer, urethral cancer, uterine cancer, vaginal cancer, vulvar cancer, and Wilms tumor.

[213] Preferably, the tumor is a solid tumor. Colon cancer, lung cancer, melanoma, sarcoma, renal cell carcinoma, and breast cancer are of particular interest.

[214] The method can further involve the administration of one or more additional agents to treat cancer, such as one or more cytokine fusion proteins described herein, chemotherapeutic agents (e.g., Adriamycin, Cerubidine, Bleomycin, Alkeran, Velban, Oncovin, Fluorouracil, Thiotepa, Methotrexate, Bisantrene, Noantrone, Thiguanine, Cytaribine, Procarabizine), immuno-oncology agents (e.g., anti-PD-Ll, anti-CTLA4, anti-PD-1, anti-CD47, anti-GD2, VEGF inhibitor), cellular therapies (e.g, CAR-T, T-cell therapy), oncolytic viruses, radiation therapy and the like.

[215] In embodiments, the fusion proteins described herein, can be administered with one or more additional cytokine fusion proteins that are inducible. For example, a fusion protein containing an IL2 polypeptide, as described herein, may be administered with fusion protein containing an IL-12 polypeptide, an IFN polypeptide, a different IL-2 polypeptide or a combinations thereof. A fusion protein containing an IL-12 polypeptide, as described herein, may be administered with a fusion protein containing an IL-2 polypeptide, an IFN polypeptide, a different IL-12 polypeptide or a combinations thereof. A fusion protein containing an IFN polypeptide, as described herein, may be administered with a fusion protein containing anIL-2 polypeptide, an IL-12 polypeptide, an different IFN polypeptide, or a combinations thereof.

[216] In some preferred embodiments, a first fusion protein comprising the amino acid sequence of any one of SEQ ID NOS: 257-300, 302-317, 325-353,355-365, 366, 372-381, 383-385, 388-420, 579-608, and 636-646 can be administered with a second different fusion protein comprising an amino acid sequence of any one of SEQ ID NOs. 368-371,434-440,453-519, 523-538,421-430, and 539-578. In some preferred embodiments, a first fusion proteins comprising the amino acid sequence of any one of 368-371,434-440,453-519, or 523-538 can be administered with a second different fusion protein comprising an amino acid sequence of any one of SEQ ID NOs. 257-300, 302-317,

325-353, 355-365, 366, 372-381, 383-385, 388-420, 579-608, 636-646,421-430, and 539-578. In some preferred embodiments, a first fusion protein comprising the amino acid sequence of any one of SEQ ID NOs. 421-430, and 539-578 can be administered with a second different fusion protein comprising the amino acid sequence of any one of SEQ ID NOs. 257-300, 302-317, 325-353, 355365, 366, 372-381, 383-385, 388-420, 579-608,636-646, 368-371,434-440,453-519, 523-538, or combinations thereof.

[217] Further exemplary agents that can be administered in combination with one or more inducible cytokine fusion proteins described herein include, but are not limited to cytokines (e.g., IL-2, IL-15), signal induction inhibitors (e.g., BRAF inhibitors or MEK inhibitors), checkpoint inhibitors (e.g., PDL-1, PD-1, CTLA-4), c-met inhibitors, kinase inhibitors (e.g., VGEF inhibitors), a proteasome inhibitor, mTOR inhibitor, angiogenesis inhibitor.

[218] A preferred immuno-oncology agent is an anti-PD-Ll agent or an anti-PD-1. Exemplary PD-1 and/or PD-L1 inhibitors include, but are not limited to Spartalizumab, Camrelizumab, Sintilimab, Tislelizumab, Toripalimab, Dostarlimab, INCMGA00012, AMP-224, and AMP-514). In embodiments, a fusion protein disclosed as 257-300, 302-317, 325-353, 355-365,366, 372-381, 383385, 388-420, 579-608, 636-646, 368-371,434-440,453-519, 523-538,421-430, and 539-578 can be administered in combination with a check-point inhibitor, such as PDL-1, PD-1, or CTL-4.

[219] Provided herein are pharmaceutical formulations or compositions containing the chimeric polypeptides and a pharmaceutically acceptable carrier. The herein provided compositions are suitable for administration in vitro or in vivo. By pharmaceutically acceptable carrier is meant a material that is not biologically or otherwise undesirable, i.e., the material is administered to a subject without causing undesirable biological effects or interacting in a deleterious manner with the other components of the pharmaceutical formulation or composition in which it is contained. The carrier is selected to minimize degradation of the active ingredient and to minimize adverse side effects in the subject.

[220] Suitable carriers and their formulations are described in Remington: The Science and Practice of Pharmacy, 21stEdition, David B. Troy, ed., Lippicott Williams &amp; Wilkins (2005). Typically, an appropriate amount of a pharmaceutically-acceptable salt is used in the formulation to render the formulation isotonic, although the formulate can be hypertonic or hypotonic if desired. Examples of the pharmaceutically-acceptable carriers include, but are not limited to, sterile water, saline, buffered solutions like Ringer's solution, and dextrose solution. The pH of the solution is generally about 5 to about 8 or from about 7 to 7.5. Other carriers include sustained release preparations such as semipermeable matrices of solid hydrophobic polymers containing the immunogenic polypeptides. Matrices are in the form of shaped articles, e.g., films, liposomes, or microparticles. Certain carriers may be more preferable depending upon, for instance, the route of administration and concentration of composition being administered. Carriers are those suitable for administration of the chimeric

polypeptides or nucleic acid sequences encoding the chimeric polypeptides to humans or other subjects.

[221] The pharmaceutical formulations or compositions are administered in a number of ways depending on whether local or systemic treatment is desired and on the area to be treated. The compositions are administered via any of several routes of administration, including topically, orally, parenterally, intravenously, intra-articularly, intraperitoneally, intramuscularly, subcutaneously, intracavity, transdermally, intrahepatically, intracranially, nebulization/inhalation, or by installation via bronchoscopy. In some embodiments, the compositions are administered locally (nonsystemically), including intratumorally, intra-articularly, intrathecally, etc.

[222] Preparations for parenteral administration include sterile aqueous or non-aqueous solutions, suspensions, and emulsions. Examples of non-aqueous solvents are propylene glycol, polyethylene glycol, vegetable oils such as olive oil, and injectable organic esters such as ethyl oleate. Aqueous carriers include water, alcoholic/aqueous solutions, emulsions or suspensions, including saline and buffered media. Parenteral vehicles include sodium chloride solution, Ringer's dextrose, dextrose and sodium chloride, lactated Ringer's, or fixed oils. Intravenous vehicles include fluid and nutrient replenishers, electrolyte replenishers (such as those based on Ringer's dextrose), and the like. Preservatives and other additives are optionally present such as, for example, antimicrobials, antioxidants, chelating agents, and inert gases and the like.

[223] Formulations for topical administration include ointments, lotions, creams, gels, drops, suppositories, sprays, liquids, and powders. Conventional pharmaceutical carriers, aqueous, powder, or oily bases, thickeners and the like are optionally necessary or desirable.

[224] Compositions for oral administration include powders or granules, suspension or solutions in water or non-aqueous media, capsules, sachets, or tables. Thickeners, flavorings, diluents, emulsifiers, dispersing aids or binders are optionally desirable.

[225] Optionally, the chimeric polypeptides or nucleic acid sequences encoding the chimeric polypeptides are administered by a vector. There are a number of compositions and methods which can be used to deliver the nucleic acid molecules and/or polypeptides to cells, either in vitro or in vivo via, for example, expression vectors. These methods and compositions can largely be broken down into two classes: viral based delivery systems and non-viral based delivery systems. Such methods are well known in the art and readily adaptable for use with the compositions and methods described herein. Such compositions and methods can be used to transfect or transduce cells in vitro or in vivo, for example, to produce cell lines that express and preferably secrete the encoded chimeric polypeptide or to therapeutically deliver nucleic acids to a subject. The components of the chimeric nucleic acids disclosed herein typically are operably linked in frame to encode a fusion protein.

[226] As used herein, plasmid or viral vectors are agents that transport the disclosed nucleic acids into the cell without degradation and include a promoter yielding expression of the nucleic acid

molecule and/or polypeptide in the cells into which it is delivered. Viral vectors are, for example, Adenovirus, Adeno-associated virus, herpes virus, Vaccinia virus, Polio virus, Sindbis, and other RNA viruses, including these viruses with the HIV backbone. Also preferred are any viral families which share the properties of these viruses which make them suitable for use as vectors. Retroviral vectors, in general are described by Coffin et al., Retroviruses, Cold Spring Harbor Laboratory Press (1997), which is incorporated by reference herein for the vectors and methods of making them. The construction of replication-defective adenoviruses has been described (Berkner et al., J. Virol. 61:1213-20 (1987); Massie et al., Mol. Cell. Biol. 6:2872-83 (1986); Haj-Ahmad et al., J. Virol. 57:267-74 (1986); Davidson et al., J. Virol. 61:1226-39 (1987); Zhang et al., BioTechniques 15:86872 (1993)). The benefit and the use of these viruses as vectors is that they are limited in the extent to which they can spread to other cell types, since they can replicate within an initial infected cell, but are unable to form new infectious viral particles. Recombinant adenoviruses have been shown to achieve high efficiency after direct, in vivo delivery to airway epithelium, hepatocytes, vascular endothelium, CNS parenchyma, and a number of other tissue sites. Other useful systems include, for example, replicating and host-restricted non-replicating vaccinia virus vectors.

[227] The provided polypeptides and/or nucleic acid molecules can be delivered via virus like particles. Virus like particles (VLPs) consist of viral protein(s) derived from the structural proteins of a virus. Methods for making and using virus like particles are described in, for example, Garcea and Gissmann, Current Opinion in Biotechnology 15:513-7 (2004).

[228] The provided polypeptides can be delivered by subviral dense bodies (DBs). DBs transport proteins into target cells by membrane fusion. Methods for making and using DBs are described in, for example, Pepperl-Klindworth et al., Gene Therapy 10:278-84 (2003).

[229] The provided polypeptides can be delivered by tegument aggregates. Methods for making and using tegument aggregates are described in International Publication No. WO 2006/110728.

[230] Non-viral based delivery methods, can include expression vectors comprising nucleic acid molecules and nucleic acid sequences encoding polypeptides, wherein the nucleic acids are operably linked to an expression control sequence. Suitable vector backbones include, for example, those routinely used in the art such as plasmids, artificial chromosomes, BACs, YACs, or PACs. Numerous vectors and expression systems are commercially available from such corporations as Novagen (Madison, Wis.), Clonetech (Pal Alto, Calif.), Stratagene (La Jolla, Calif.), and Invitrogen/Life Technologies (Carlsbad, Calif.). Vectors typically contain one or more regulatory regions. Regulatory regions include, without limitation, promoter sequences, enhancer sequences, response elements, protein recognition sites, inducible elements, protein binding sequences, 5&amp;#1523; and 3&amp;#1523; untranslated regions (UTRs), transcriptional start sites, termination sequences, polyadenylation sequences, and introns. Such vectors can also be used to make the chimeric polypeptides by expression is a suitable host cell, such as CHO cells.

[231] Preferred promoters controlling transcription from vectors in mammalian host cells may be obtained from various sources, for example, the genomes of viruses such as polyoma, Simian Virus 40 (SV40), adenovirus, retroviruses, hepatitis B virus, and most preferably cytomegalovirus (CMV), or from heterologous mammalian promoters, e.g. β-actin promoter or EFla promoter, or from hybrid or chimeric promoters (e.g., CMV promoter fused to the β-actin promoter). Of course, promoters from the host cell or related species are also useful herein.

[232] Enhancer generally refers to a sequence of DNA that functions at no fixed distance from the transcription start site and can be either 5&amp;#1523; or 3&amp;#1523; to the transcription unit. Furthermore, enhancers can be within an intron as well as within the coding sequence itself. They are usually between 10 and 300 base pairs (bp) in length, and they function in cis. Enhancers usually function to increase transcription from nearby promoters. Enhancers can also contain response elements that mediate the regulation of transcription. While many enhancer sequences are known from mammalian genes (globin, elastase, albumin, fetoprotein, and insulin), typically one will use an enhancer from a eukaryotic cell virus for general expression. Preferred examples are the SV40 enhancer on the late side of the replication origin, the cytomegalovirus early promoter enhancer, the polyoma enhancer on the late side of the replication origin, and adenovirus enhancers.

[233] The promoter and/or the enhancer can be inducible (e.g. chemically or physically regulated). A chemically regulated promoter and/or enhancer can, for example, be regulated by the presence of alcohol, tetracycline, a steroid, or a metal. A physically regulated promoter and/or enhancer can, for example, be regulated by environmental factors, such as temperature and light. Optionally, the promoter and/or enhancer region can act as a constitutive promoter and/or enhancer to maximize the expression of the region of the transcription unit to be transcribed. In certain vectors, the promoter and/or enhancer region can be active in a cell type specific manner. Optionally, in certain vectors, the promoter and/or enhancer region can be active in all eukaryotic cells, independent of cell type. Preferred promoters of this type are the CMV promoter, the SV40 promoter, the β-actin promoter, the EFla promoter, and the retroviral long terminal repeat (LTR).

[234] The vectors also can include, for example, origins of replication and/or markers. A marker gene can confer a selectable phenotype, e.g., antibiotic resistance, on a cell. The marker product is used to determine if the vector has been delivered to the cell and once delivered is being expressed. Examples of selectable markers for mammalian cells are dihydrofolate reductase (DHFR), thymidine kinase, neomycin, neomycin analog G418, hygromycin, puromycin, and blasticidin. When such selectable markers are successfully transferred into a mammalian host cell, the transformed mammalian host cell can survive if placed under selective pressure. Examples of other markers include, for example, the E. coli lacZ gene, green fluorescent protein (GFP), and luciferase. In addition, an expression vector can include a tag sequence designed to facilitate manipulation or detection (e.g., purification or localization) of the expressed polypeptide. Tag sequences, such as GFP,

glutathione S-transferase (GST), polyhistidine, c-myc, hemagglutinin, or FLAG™ tag (Kodak; New Haven, Conn.) sequences typically are expressed as a fusion with the encoded polypeptide. Such tags can be inserted anywhere within the polypeptide including at either the carboxyl or amino terminus. [235] As used herein, the terms peptide, polypeptide, or protein are used broadly to mean two or more amino acids linked by a peptide bond. Protein, peptide, and polypeptide are also used herein interchangeably to refer to amino acid sequences. It should be recognized that the term polypeptide is not used herein to suggest a particular size or number of amino acids comprising the molecule and that a peptide of the invention can contain up to several amino acid residues or more. As used throughout, subject can be a vertebrate, more specifically a mammal (e.g. a human, horse, cat, dog, cow, pig, sheep, goat, mouse, rabbit, rat, and guinea pig), birds, reptiles, amphibians, fish, and any other animal. The term does not denote a particular age or sex. Thus, adult and newborn subjects, whether male or female, are intended to be covered. As used herein, patient or subject may be used interchangeably and can refer to a subject with a disease or disorder (e.g. cancer). The term patient or subject includes human and veterinary subjects.

[236] A subject at risk of developing a disease or disorder can be genetically predisposed to the disease or disorder, e.g., have a family history or have a mutation in a gene that causes the disease or disorder, or show early signs or symptoms of the disease or disorder. A subject currently with a disease or disorder has one or more than one symptom of the disease or disorder and may have been diagnosed with the disease or disorder.

[237] The methods and agents as described herein are useful for both prophylactic and therapeutic treatment. For prophylactic use, a therapeutically effective amount of the chimeric polypeptides or chimeric nucleic acid sequences encoding the chimeric polypeptides described herein are administered to a subject prior to onset (e.g., before obvious signs of cancer or inflammation) or during early onset (e.g., upon initial signs and symptoms of cancer or inflammation). Prophylactic administration can occur for several days to years prior to the manifestation of symptoms of cancer or inflammation. Prophylactic administration can be used, for example, in the preventative treatment of subjects diagnosed with a genetic predisposition to cancer. Therapeutic treatment involves administering to a subject a therapeutically effective amount of the chimeric polypeptides or nucleic acid sequences encoding the chimeric polypeptides described herein after diagnosis or development of cancer or inflammation (e.g., an autoimmune disease). Prophylactic use may also apply when a patient is undergoing a treatment, e.g., a chemotherapy, in which inflammation is expected.

[238] According to the methods taught herein, the subject is administered an effective amount of the agent (e.g., a chimeric polypeptide). The terms effective amount and effective dosage are used interchangeably. The term effective amount is defined as any amount necessary to produce a desired physiologic response. Effective amounts and schedules for administering the agent may be determined empirically, and making such determinations is within the skill in the art. The dosage ranges for

administration are those large enough to produce the desired effect in which one or more symptoms of the disease or disorder are affected (e.g., reduced or delayed). The dosage should not be so large as to cause substantial adverse side effects, such as unwanted cross-reactions, anaphylactic reactions, and the like. Generally, the dosage will vary with the age, condition, sex, type of disease, the extent of the disease or disorder, route of administration, or whether other drugs are included in the regimen, and can be determined by one of skill in the art. The dosage can be adjusted by the individual physician in the event of any contraindications. Dosages can vary and can be administered in one or more dose administrations daily, for one or several days. Guidance can be found in the literature for appropriate dosages for given classes of pharmaceutical products.

[239] As used herein the terms treatment, treat, or treating refers to a method of reducing the effects of a disease or condition or symptom of the disease or condition. Thus, in the disclosed method, treatment can refer to a 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, or 100% reduction in the severity of an established disease or condition or symptom of the disease or condition. For example, a method for treating a disease is considered to be a treatment if there is a 10% reduction in one or more symptoms of the disease in a subject as compared to a control. Thus, the reduction can be a 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 100%, or any percent reduction in between 10% and 100% as compared to native or control levels. It is understood that treatment does not necessarily refer to a cure or complete ablation of the disease, condition, or symptoms of the disease or condition.

[240] As used herein, the terms prevent, preventing, and prevention of a disease or disorder refers to an action, for example, administration of the chimeric polypeptide or nucleic acid sequence encoding the chimeric polypeptide, that occurs before or at about the same time a subject begins to show one or more symptoms of the disease or disorder, which inhibits or delays onset or exacerbation of one or more symptoms of the disease or disorder. As used herein, references to decreasing, reducing, or inhibiting include a change of 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or greater as compared to a control level. Such terms can include but do not necessarily include complete elimination.

[241] IL-2 variants have been developed that are selective for ΓΕ2Καβγ relative to ΙΕ2Κβγ (Shanafelt, A. B., et al., 2000, Nat Biotechnol. 18:1197-202; Cassell, D. J., et. al., 2002, Curr Pharm Des., 8:2171-83). These variants have amino acid substitutions which reduce their affinity for IL2RB. Because IL-2 has undetectable affinity for IL2RG, these variants consequently have reduced affinity for the IL2RPy receptor complex and reduced ability to activate IL2Rβγ-expressing cells, but retain the ability to bind IL2RA and the ability to bind and activate the ΓΕ2Καβγ receptor complex.

[242] One of these variants, IL2/N88R (Bay 50-4798), was clinically tested as a low- toxicity version of IL-2 as an immune system stimulator, based on the hypothesis that IL2Rβγ-expressing NK cells are a major contributor to toxicity. Bay 50-4798 was shown to selectively stimulate the proliferation of activated T cells relative to NK cells, and was evaluated in phase I/II clinical trials in

cancer patients (Margolin, K., et. al., 2007, Clin Cancer Res., 13:3312-9) and HIV patients (Davey, R. T., et. al., 2008, J Interferon Cytokine Res., 28:89-100). These clinical trials showed that Bay 50-4798 was considerably safer and more tolerable than aldesleukin, and also showed that it increased the levels of CD4+CD25+ T cells, a cell population enriched in Treg cells. Subsequent to these trials, research in the field more fully established the identity of Treg cells and demonstrated that Treg cells selectively express ΙΕ2Καβγ (reviewed in Malek, T. R., et al., 2010, Immunity, 33:153-65).

[243] In addition, mutants can be made that selectively alter the affinity for the CD25 chain relative to native 11-2.

[244] IL-2 can be engineered to produce mutants that bind the IL-2R complex generally or the IL2Ra subunit specifically with an affinity that differs from that of the corresponding wild-type IL-2 or of a presently available mutant (referred to as C125S, as the cysteine residue at position 125 is replaced with a serine residue).

[245] Accordingly, the present invention features mutant interleukin-2 (IL-2*) polypeptides that include an amino acid sequence that is at least 80% identical to wild-type IL-2 (e.g., 85, 87, 90, 95, 97, 98, or 99% identical) and that bind, as compared to WT IL-2, with higher to the IL-2 trimeric receptor relative to the dimeric IL-2 receptor. Typically, the muteins will also bind an IL-2 receptor a subunit (IL-2Ra) with an affinity that is greater than the affinity with which wild type IL-2 binds the IL-2Ra. The amino acid sequence within mutant IL-2 polypeptides can vary from SEQ ID NO: 1 (UniProtKB accession number P60568) by virtue of containing (or only containing) one or more amino acid substitutions, which may be considered conservative or non-conservative substitutions. Non-naturally occurring amino acids can also be incorporated. Alternatively, or in addition, the amino acid sequence can vary from SEQ ID NO: 1 (which may be considered the “reference” sequence) by virtue of containing and addition and/or deletion of one or more amino acid residues. More specifically, the amino acid sequence can differ from that of SEQ ID NO: 1 by virtue of a mutation at least one of the following positions of SEQ ID NO:1: 1,4, 8, 9, 10, 11, 13, 15,26,29, 30, 31,35, 37, 46,48,49, 54, 61, 64, 67,68, 69, 71, 73, 74, 75, 76, 79, 88, 89, 90, 92, 99, 101, 103, 114, 125, 128, or 133 (or combinations thereof). As noted, as few as one of these positions may be altered, as may two, three, four, five, six, seven, eight, nine, ten, or 11 or more (including up to all) of the positions. For example, the amino acid sequence can differ from SEQ ID NO: 1 at positions 69 and 74 and further at one or more of positions 30, 35, and 128. The amino acid sequence can also differ from SEQ ID NO:2 (as disclosed in US 7569215, incorporated herein by reference) at one of the following sets of positions: (a) positions 64, 69, and 74; (b) positions 69,74, and 101; (c) positions 69, 74, and 128; (d) positions 30, 69, 74, and 103; (e) positions 49,69, 73, and 76; (f) positions 69, 74,101, and 133; (g) positions 30, 69, 74, and 128; (h) positions 69, 74, 88, and 99; (i) positions 30, 69,74, and 128; (j) positions 9, 11, 35, 69, and 74; (k) positions 1,46,49,61, 69, and 79; (1) positions 48, 68, 71, 90, 103, and 114; (m) positions 4, 10, 11,69, 74, 88, and 133; (n) positions 15,30 31,35, 48,69, 74, and

92; (Ο) positions 30, 68, 69, 71, 74, 75, 76, and 90; (p) positions 30, 31, 37,69, 73, 74, 79, and 128; (q) positions 26,29, 30, 54, 67, 69, 74, and 92; (r) positions 8, 13,26, 30, 35, 37,69, 74, and 92; and (s) positions 29, 31, 35, 37,48, 69, 71,74, 88, and 89. Aside from mutations at these positions, the amino acid sequence of the mutant IL-2 polypeptide can otherwise be identical to SEQ ID NO: 1. With respect to specific substitutions, the amino acid sequence can differ from SEQ ID NO: 1 by virtue of having one or more of the following mutations: AIT, S4P, K8R, K9T, T10A, QI IR, Q13R, E15K, N26D, N29S, N30S, N30D, N30T, Y31H, Y31C, K35R, T37A, T37R, M46L, K48E, K49R, K49E, K54R, E61D, K64R, E67G, E68D, V69A, N71T, N71A, N71R, A73V, Q74P, S75P, K76E, K76R, H79R, N88D, I89V, N90H, I92T, S99P, T101A, F103S, Il 14V, I128T, I128A, T133A, or T133N. Our nomenclature is consistent with that of the scientific literature, where the single letter code of the amino acid in the wild-type or reference sequence is followed by its position within the sequence and then by the single letter code of the amino acid with which it is replaced. Thus, AIT designates a substitution of the alanine residue a position 1 with threonine. Other mutant polypeptides within the scope of the invention include those that include a mutant of SEQ ID NO:2 having substitutions at V69 (e.g. A) and Q74 (e.g., P). For example, the amino acid sequence can include one of the following sets of mutations with respect to SEQ ID NO:2: (a) K64R, V69A, and Q74P; (b) V69A, Q74P, and T101A; (c) V69A, Q74P, and I128T; (d) N30D, V69A, Q74P, and F103S; (e) K49E, V69A, A73V, and K76E; (f) V69A, Q74P, T101A, and T133N; (g) N30S, V69A, Q74P, and I128A; (h) V69A, Q74P, N88D, and S99P; (i) N30S, V69A, Q74P, and I128T; (j) K9T, QI IR, K35R, V69A, and Q74P; (k) AIT, M46L, K49R, E61D, V69A, and H79R; (1) K48E, E68D, N71T, N90H, F103S, and II 14V; (m) S4P, T10A, QI IR, V69A, Q74P, N88D, and T133A; (η) E15K, N30S Y31H, K35R, K48E, V69A, Q74P, and I92T; (0) N30S, E68D, V69A, N71A, Q74P, S75P, K76R, and N90H; (p) N30S, Y31C, T37A, V69A, A73V, Q74P, H79R, and I128T; (q) N26D, N29S, N30S, K54R, E67G, V69A, Q74P, and I92T; (r) K8R, Q13R, N26D, N30T, K35R, T37R, V69A, Q74P, and I92T; and (s) N29S, Y31H, K35R, T37A, K48E, V69A, N71R, Q74P, N88D, and I89V. SEQ ID NO:2 is disclosed in US 7569215, which is incorporated herein by reference as an exemplary IL-2 polypeptide sequence that can be used in the invention.

[246] As noted above, any of the mutant IL-2 polypeptides disclosed herein can include the sequences described; they can also be limited to the sequences described and otherwise identical to SEQ ID NO: 1. Moreover, any of the mutant IL-2 polypeptides described herein can optionally include a substitution of the cysteine residue at position 125 with another residue (e.g., serine) and/or can optionally include a deletion of the alanine residue at position 1 of SEQ ID NO: 1.

[247] The mutant IL-2 polypeptides disclosed herein can bind to the IL-2Ra subunit with a Kd of less than about 28 nM (e.g., less than about 25 nM; less than about 5 nM; about 1 nM; less than about 500 pM; or less than about 100 pM). More specifically, a mutant IL-2 polypeptide can have an affinity equilibrium constant less than 1.0 nM (e.g., about 0.8, 0.6, 0.4, or 0.2 nM). Affinity can also

be expressed as a relative rate of dissociation from an IL-2Ra subunit or from an IL-2 receptor complex (e.g., a complex expressed on the surface of a cell or otherwise membrane bound). For example, the mutant IL-2 polypeptides can dissociate from, e.g., IL-2Ra, at a decreased rate relative to a wild-type polypeptide or to an IL-2 based therapeutic, e.g., IL-2*. Alternatively, affinity can be characterized as the time, or average time, an IL-2* polypeptide persists on, for example, the surface of a cell expressing an IL-2R. For example, an IL-2*polypeptide can persist on the receptor for at least about 2, 5, 10, 50, 100, or 250 times (or more).

[248] Disclosed are materials, compositions, and components that can be used for, can be used in conjunction with, can be used in preparation for, or are products of the disclosed methods and compositions. These and other materials are disclosed herein, and it is understood that when combinations, subsets, interactions, groups, etc. of these materials are disclosed that while specific reference of each various individual and collective combinations and permutations of these compounds may not be explicitly disclosed, each is specifically contemplated and described herein. For example, if a method is disclosed and discussed and a number of modifications that can be made to a number of molecules including the method are discussed, each and every combination and permutation of the method, and the modifications that are possible are specifically contemplated unless specifically indicated to the contrary. Likewise, any subset or combination of these is also specifically contemplated and disclosed. This concept applies to all aspects of this disclosure including, but not limited to, steps in methods using the disclosed compositions. Thus, if there are a variety of additional steps that can be performed, it is understood that each of these additional steps can be performed with any specific method steps or combination of method steps of the disclosed methods, and that each such combination or subset of combinations is specifically contemplated and should be considered disclosed.

[249] Publications cited herein and the material for which they are cited are hereby specifically incorporated by reference in their entireties.

EXAMPLES

[250] The following are examples of methods and compositions of the invention. It is understood that various other embodiments may be practiced, given the general description provided herein.

Example 1: Detection of IL-2, IL-2 mutein, IL-2Ra and IL-2Ry in Fusion Proteins by ELISA [251] IL-2 mutein is detected with a commercially available antibody, e.g., the anti-IL-2 monoclonal (JES6-1A12) (BD Pharmingen; San Jose, Calif.). A positive control is used to show whether the monoclonal antibody recognizes the cytokine or mutein. Antibodies against IL-2Ra and IL-2Ry chain are also used. Wells of a 96-well plate are coated with an antibody (2.5 gg/ml) in PBS. Wells are blocked with 5% non-fat milk in PBS with 0.2% Tween®20 (PBS-M-Tw) and fusion

proteins are added for 1-2 hours at 37° C. After washing, an anti-IL-2 biotin-labeled antibody, e.g.,

JES5H4 (BD Pharmingen) is added and binding is detected using Strepavidin HRP (Southern

Biotechnology Associates; Birmingham, Ala.). The ELISA plate is developed by adding 50 μ&amp;#912; Ophenylenediamine (OPD) (Sigma-Aldrich) in 0.1M Citrate pH 4.5 and 0.04% H2O2, stopped by adding 50 μ&amp;#912;/well 2N H2SO4 and the absorbance was read at 490 nm.

Example 2: Protease cleavage of fusion protein by MMP9 protease

[252] One of skill in the art would be familiar with methods of setting up protein cleavage assay. lOOug of protein in IxPBS pH 7.4 were cleaved with 1 pg active MMP9 (Sigma catalog # SAE007850 or Enzo catalog BML-SE360) and incubated at room temperature for up to 16 hours. Digested protein is subsequently used in functional assays or stored at -80°C prior to testing. Extent of cleavage was monitored by SDS PAGE using methods well known in the art. As shown in FIGs. 10,13,18A, 18B, 24B, 24C, and 27A full cleavage of the fusion proteins by MMP9 protease is seen.

Example 3: CTLL-2 assay

[253] CTLL2 cells (ATCC) were plated in suspension at a concentration of 500,000 cells/well in culture media with or without 40mg/ml human serum albumin (HSA) and stimulated with a dilution series of recombinant hIL2 or activatable hIL2 for 72 hours at 37°C and 5% CO2. Activity of uncleaved and cleaved activatable hIL2 was tested. Cleaved activatable hIL2 was generated by incubation with active MMP9. Cell activity was assessed using a CellTiter-Glo (Promega) luminescence-based cell viability assay.

Example 4: Protease Cleavage of the IL-2/IL-2Ra/IL-2Ry Chimeric Polypeptide Results in Increased Accessibility to Antibodies and Biologically Active IL-2 mutein

[254] The IL-2 mutein fusion proteins are biochemically characterized before and after cleavage with a protease, e.g., PSA. hnmunoblot analyses will show that the fusion proteins can be cleaved by PSA and that there is an increase in intensity of the predicted low molecular weight cleavage product of approximately 20 kDa reactive with an anti-IL-2 antibody after treatment of the samples with PSA. The degree of cleavage is dependent upon the amount of PSA as well as the time of incubation. Interestingly, when the fusion protein is analyzed before and after PSA treatment by ELISA, it was found that the apparent amount of IL-2 is increased after PSA cleavage. In this experiment, there is an approximately 2 or 4-fold increase in the apparent amount of IL-2 detected using this sandwich ELISA depending on the construct, suggesting that the antibody binding is partially hindered in the intact fusion protein. Aliquots of the same samples are also analyzed after PSA treatment using the CTLL-2 cell line that requires IL-2 for growth and survival and the viability of cells can be ascertained using the colorimetric MTT assay. In this assay, the more a supernatant can be diluted, the

more biologically active IL-2 it contains, and there is an increase in the amount of biologically active

IL-2 after PSA cleavage. The amount of IL-2 mutein increase will suggest that after PSA cleavage there is an increase in the predicted low molecular weight cleavage fragment of approximately 20 kDa reactive with an anti-IL-2 antibody, an increase in antibody accessibility, and most importantly, an increase in the amount of biologically active IL-2 mutein.

Example 5. In Vivo Delivery of a Protease Activated Fusion Protein Results in Decreased Tumor Growth

[255] The chimeric polypeptide is examined to determine if it could have biological effects in vivo. For these experiments a system is used in which tumor cells injected intraperitoneally rapidly and preferentially attach and grow initially on the milky spots, a series of organized immune aggregates found on the omentum (Gerber et al., Am. J. Pathol. 169:1739-52 (2006)). This system offers a convenient way to examine the effects of fusion protein treatment on tumor growth since fusion proteins can be delivered intraperitoneally multiple times and tumor growth can be analyzed by examining the dissociated omental cells. For these experiments, the Colon 38 cell line, a rapidly growing tumor cell line that expresses both MMP2 and MMP9 in vitro, may be used. The omental tissue normally expresses a relatively small amount of MMP2 and MMP9, but, when Colon 38 tumor is present on the omentum, MMP levels increase. Using this tumor model, the ability of IL-2 mutein fusion proteins to affect tumor growth is examined. Colon 38 cells are injected intraperitoneally, allowed to attach and grow for 1 day, and then treated daily with fusion protein interaperitoneally. At day I, the animals are sacrificed and the omenta examined for tumor growth using flow cytometry and by a colony-forming assay.

Example 6: Construction of an Exemplary Activatable IL2 Protein Targeting CD20

Generation of an activatable IL2 domain

[256] An IL-2 polypeptide capable of binding to CD20 polypeptide present in a tumor or on a tumor cell is produced as follows. A nucleic acid is produced that contains nucleic acid sequences: (1) encoding an ΙΕΝγ polypeptide sequence and (2) one or more polypeptide linkers. Activatable interleukin plasmid constructs can have optional Flag, His or other affinity tags, and are electroporated into HEK293 or other suitable human or mammalian cell lines and purified. Validation assays include T cell activation assays using T cells responsive to IFNy stimulation in the presence of a protease.

Generation of a scFv CD20 binding domain

[257] CD20 is one of the cell surface proteins present on B-lymphocytes. CD20 antigen is found in normal and malignant pre-B and mature B lymphocytes, including those in over 90% of B-cell non-

Hodgkin's lymphomas (NHL). The antigen is absent in hematopoietic stem cells, activated B lymphocytes (plasma cells) and normal tissue. As such, several antibodies mostly of murine origin have been described: 1F5,2B8/C2B8,2H7, and 1H4.

[258] Human or humanized anti-CD20 antibodies are therefore used to generate scFv sequences for CD20 binding domains of an activatable interleukin protein. DNA sequences coding for human or humanized VL and VH domains are obtained, and the codons for the constructs are, optionally, optimized for expression in cells from Homo sapiens. The order in which the VL and VH domains appear in the scFv is varied (i.e., VL-VH, or VH-VL orientation), and three copies of the G4S (SEQ ID NO.: 449) or “G4S” (SEQ ID NO.: 449) subunit (G4S)3 (SEQ ID NO.: 452) connect the variable domains to create the scFv domain. Anti-CD20 scFv plasmid constructs can have optional Flag, His or other affinity tags, and are electroporated into HEK293 or other suitable human or mammalian cell lines and purified. Validation assays include binding analysis by FACS, kinetic analysis using Proteon, and staining of CD20-expressing cells.

Cloning of DNA expression constructs encoding the activatable IL2 protein

[259] The activatable IL2 construct with protease cleavage site domains are used to construct an activatable interleukin protein in combination with an anti-CD20 scFv domain and a serum half-life extension element (e.g., a HSA binding peptide or VH domain). For expression of an activatable interleukin protein in CHO cells, coding sequences of all protein domains are cloned into a mammalian expression vector system. In brief, gene sequences encoding the activatable interleukin domain, serum half-life extension element, and CD20 binding domain along with peptide linkers LI and L2 are separately synthesized and subcloned. The resulting constructs are then ligated together in the order of CD20 binding domain - LI - IL2 subunit 1- L2 - protease cleavage domain - L3 - IL2 subunit 2 - L4 - anti-CD20 scFv - L5 - serum half-life extension element to yield a final construct. All expression constructs are designed to contain coding sequences for an N-terminal signal peptide and a C-terminal hexahistidine (6xHis)-tag (SEQ ID NO. 354) to facilitate protein secretion and purification, respectively.

Expression of activatable IL2 proteins in stably transfected CHO cells

[260] A CHO cell expression system (Flp-In®, Life Technologies), a derivative of CHO-K1 Chinese Hamster ovary cells (ATCC, CCL-61) (Kao and Puck, Proc. Natl. Acad Sci USA 1968;60(4): 1275-81), is used. Adherent cells are subcultured according to standard cell culture protocols provided by Life Technologies.

[261] For adaption to growth in suspension, cells are detached from tissue culture flasks and placed in serum-free medium. Suspension-adapted cells are cryopreserved in medium with 10% DMSO.

[262] Recombinant CHO cell lines stably expressing secreted activatable interleukin proteins are generated by transfection of suspension-adapted cells. During selection with the antibiotic Hygromycin B viable cell densities are measured twice a week, and cells are centrifuged and resuspended in fresh selection medium at a maximal density of O.lxlO6 viable cells/mL. Cell pools stably expressing activatable interleukin proteins are recovered after 2-3 weeks of selection at which point cells are transferred to standard culture medium in shake flasks. Expression of recombinant secreted proteins is confirmed by performing protein gel electrophoresis or flow cytometry. Stable cell pools are cryopreserved in DMSO containing medium.

[263] Activatable IL2 proteins are produced in 10-day fed-batch cultures of stably transfected CHO cell lines by secretion into the cell culture supernatant. Cell culture supernatants are harvested after 10 days at culture viabilities of typically >75%. Samples are collected from the production cultures every other day and cell density and viability are assessed. On day of harvest, cell culture supernatants are cleared by centrifugation and vacuum filtration before further use.

[264] Protein expression titers and product integrity in cell culture supernatants are analyzed by SDS-PAGE.

Purification of activatable IL2 proteins

[265] Activatable IL2 proteins are purified from CHO cell culture supernatants in a two-step procedure. The constructs are subjected to affinity chromatography in a first step followed by preparative size exclusion chromatography (SEC) on Superdex 200 in a second step. Samples are buffer-exchanged and concentrated by ultrafiltration to a typical concentration of >1 mg/mL. Purity and homogeneity (typically >90%) of final samples are assessed by SDS PAGE under reducing and non-reducing conditions, followed by immunoblotting using an anti-HSA or anti idiotype antibody as well as by analytical SEC, respectively. Purified proteins are stored at aliquots at -80°C until use.

Example 7: Determination of antigen affinity by flow cytometry

[266] The activatable interleukin proteins of Example 6 are tested for their binding affinities to human CD20+ cells and cynomolgus CD20+ cells.

[267] CD20+ cells are incubated with 100 pL of serial dilutions of the activatable interleukin proteins of Example 1 and at least one protease. After washing three times with FACS buffer the cells are incubated with 0.1 mL of 10 pg/mL mouse monoclonal anti-idiotype antibody in the same buffer for 45 min on ice. After a second washing cycle, the cells are incubated with 0.1 mL of 15 pg/mL FITC-conjugated goat anti-mouse IgG antibodies under the same conditions as before. As a control, cells are incubated with the anti-His IgG followed by the FITC-conjugated goat anti-mouse IgG antibodies without the activatable IL2 proteins. The cells were then washed again and resuspended in 0.2 mL of FACS buffer containing 2 pg/mL propidium iodide (PI) in order to exclude dead cells. The

fluorescence of IxlO4 living cells is measured using a Beckman-Coulter FC500 MPL flow cytometer using the MXP software (Beckman-Coulter, Krefeld, Germany) or a Millipore Guava EasyCyte flow cytometer using the Incyte software (Merck Millipore, Schwalbach, Germany). Mean fluorescence intensities of the cell samples are calculated using CXP software (Beckman-Coulter, Krefeld, Germany) or Incyte software (Merck Millipore, Schwalbach, Germany). After subtracting the fluorescence intensity values of the cells stained with the secondary and tertiary reagents alone the values are then used for calculation of the Kd values with the equation for one-site binding (hyperbola) of the GraphPad Prism (version 6.00 for Windows, GraphPad Software, La Jolla California USA).

[268] CD20 binding and crossreactivity are assessed on the human CD20+ tumor cell lines. The Kd ratio of crossreactivity is calculated using the Kd values determined on the CHO cell lines expressing either recombinant human or recombinant cynomolgus antigens.

Example 8: Cytotoxicity Assay

[269] The activatable interleukin protein of Example 6 is evaluated in vitro on its mediation of immune response to CD20+ target cells.

[270] Fluorescence labeled CD20+ REC-1 cells (a Mantle cell lymphoma cell line, ATCC CRL3004) are incubated with isolated PBMC of random donors or CB15 T-cells (standardized T-cell line) as effector cells in the presence of the activatable IL2 protein of Example 5 and at least one protease. After incubation for 4 h at 37°C in a humidified incubator, the release of the fluorescent dye from the target cells into the supernatant is determined in a spectrofluorimeter. Target cells incubated without the activatable IL2 protein of Example land target cells totally lysed by the addition of saponin at the end of the incubation serve as negative and positive controls, respectively.

[271] Based on the measured remaining living target cells, the percentage of specific cell lysis is calculated according to the following formula: [!-(number of living targetS(samp1e)/number of living targetS(spontaneous))] x 100%. Sigmoidal dose response curves and EC50 values are calculated by nonlinear regression/4-parameter logistic fit using the GraphPad Software. The lysis values obtained for a given antibody concentration are used to calculate sigmoidal dose-response curves by 4 parameter logistic fit analysis using the Prism software.

Example 9: Pharmacokinetics of activatable interleukin proteins

[272] The activatable interleukin protein of Example 6 is evaluated for half-time elimination in animal studies.

[273] The activatable IL2 protein is administered to cynomolgus monkeys as a 0.5 mg/kg bolus injection into the saphenous vein. Another cynomolgus monkey group receives a comparable IL2 construct in size, but lacking a serum half-life extension element. A third and fourth group receive an

IL2 construct with serum half-life extension element and a cytokine with CD20 and serum half-life extension elements respectively, and both comparable in size to the activatable interleukin protein.

Each test group consists of 5 monkeys. Serum samples are taken at indicated time points, serially diluted, and the concentration of the proteins is determined using a binding ELISA to CD20.

[274] Pharmacokinetic analysis is performed using the test article plasma concentrations. Group mean plasma data for each test article conforms to a multi-exponential profile when plotted against the time post-dosing. The data are fit by a standard two-compartment model with bolus input and first-order rate constants for distribution and elimination phases. The general equation for the best fit of the data for i.v. administration is: c(t)=Ae-at+Be_(5t, where c(t) is the plasma concentration at time t, A and B are intercepts on the Y-axis, and a and β are the apparent first-order rate constants for the distribution and elimination phases, respectively. The a-phase is the initial phase of the clearance and reflects distribution of the protein into all extracellular fluid of the animal, whereas the second or βphase portion of the decay curve represents true plasma clearance. Methods for fitting such equations are well known in the art. For example, Α=&#911;/ν(α-Ε21)/(α-β), Β=&#911;/ν(β-Ε21)/(α-β), and a and β (for α>β) are roots of the quadratic equation: r2+(kl2+k21+kl0)r-i-k21kl0=0 using estimated parameters of V=volume of distribution, klO=elimination rate, kl2=transfer rate from compartment 1 to compartment 2 and k21=transfer rate from compartment 2 to compartment 1, and D=the administered dose.

[275] Data analysis: Graphs of concentration versus time profiles are made using KaleidaGraph (KaleidaGraph™ V. 3.09 Copyright 1986-1997. Synergy Software. Reading, Pa.). Values reported as less than reportable (LTR) are not included in the PK analysis and are not represented graphically. Pharmacokinetic parameters are determined by compartmental analysis using WinNonlin software (WinNonlin® Professional V. 3.1 WinNonlin™ Copyright 1998-1999. Pharsight Corporation. Mountain View, Calif.). Pharmacokinetic parameters are computed as described in Ritschel W A and Kearns G L, 1999, IN: Handbook Of Basic Pharmacokinetics Including Clinical Applications, 5 th edition, American Pharmaceutical Assoc., Washington, D.C.

[276] It is expected that the activatable interleukin protein of Example 5 has improved pharmacokinetic parameters such as an increase in elimination half-time as compared to proteins lacking a serum half-life extension element.

Example 10: Xenograft Tumor Model

[277] The activatable IL2 protein of Example 6 is evaluated in a xenograft model.

[278] Female immune-deficient NOD/scid mice are sub-lethally irradiated (2 Gy) and subcutaneously inoculated with 4x106 Ramos RAI cells into the right dorsal flank. When tumors reach 100 to 200 mm3, animals are allocated into 3 treatment groups. Groups 2 and 3 (8 animals each) are intraperitoneally injected with 1.5xl07 activated human T-cells. Three days later, animals

from Group 3 are subsequently treated with a total of 9 intravenous doses of 50 pg activatable interleukin protein of Example 1 (qdx9d). Groups 1 and 2 are only treated with vehicle. Body weight and tumor volume are determined for 30 days.

[279] It is expected that animals treated with the activatable interleukin protein of Example 5 have a statistically significant delay in tumor growth in comparison to the respective vehicle-treated control group.

[280] While preferred embodiments of the present invention have been shown and described herein, it will be obvious to those skilled in the art that such embodiments are provided by way of example only. Numerous variations, changes, and substitutions will now occur to those skilled in the art without departing from the invention. It should be understood that various alternatives to the embodiments of the invention described herein may be employed in practicing the invention. It is intended that the following claims define the scope of the invention and that methods and structures within the scope of these claims and their equivalents be covered thereby.

Example 11: Mouse IFNy WEHI cell survival assay

[281] WEHI279 cells (ATCC) were plated in suspension at a concentration of 25,000 cells/well in culture media with or without 1.5% human serum albumin (HSA) and stimulated with a dilution series of recombinant mIFNy or inducible mIFNy for 72 hours at 37°C and 5% CO2. Activity of uncleaved and cleaved inducible mIFNy was tested. Cleaved inducible mIFNg was generated by incubation with active MMP9. Cell survival was assessed using a CellTiter-Glo (Promega) luminescence-based cell viability assay. The EC50 values for cleaved inducible mIFNg molecules were at least lOOx more potent than un-cleaved inducible mIFNg molecules. As shown in FIGs. 16A16F, greater inducibility was seen in assays wherein the culture media contained human serum albumin.

Example 12: Mouse IFNy B16 reporter and Mouse IFNa/β B16 reporter cell assays

[282] B16-Blue IFNy cells (InvivoGen) were plated at a concentration of 75,000 cells/well in culture media with or without 1.5% human serum albumin (HSA) and stimulated with a dilution series of recombinant mIFNy or inducible mIFNy for 24 hours at 37°C and 5% CO2. Activity of uncleaved and cleaved inducible mIFNy was tested. Cleaved inducible mIFNy was generated by incubation with active MMP9. Supernatants were harvested, and SEAP activation was assessed by adding QUANTI-Blue Reagent (InvivoGen), incubating at 37°C for 2 hours, and measuring absorbance at 620nm. Results are shown in FIGs. 17A-17F, 19A, 19B, 22A, 22B, 23A, 23B, and 28A-28N. This experiment was repeated with for IFNa fusion proteins using B16-Blue IFNa/β cells. The EC50 values for cleaved inducible mIFNa molecules were at least lOOx more potent than uncleaved inducible mIFNa molecules.

[283] B16-Blue IFN-α/β cells (InvivoGen) were plated in suspension at a density of 75,000 cells/well in culture media with or without 15 mg/ml mouse serum albumin (HSA) and stimulated with a dilution series of recombinant mouse IFNa (or ΙΡΝβ) and activatable mouse IFNa (or ΙΡΝβ) for 20-24 hours at 37°C and 5% CO2. Activity of uncleaved and cleaved activatable IFNa (or ΙΡΝβ) was tested. Cleaved inducible IFNa (or ΙΡΝβ) was generated by incubation with active recombinant protease. Stimulation of B16-Blue IFN-α/β cells with IFNa (or ΙΡΝβ) induces expression of Secreted Alkaline Phosphatase (SEAP) from an ISRE-ISG54-SEAP reporter. IFNa (or ΙΡΝβ) activity was assessed by quantification of SEAP activity using the reagent QUANTI-Blue (InvivoGen), a colorimetric based assay. Results are shown in FIGs. 10A-10J.

Example 13. In Vivo Delivery of a Protease Activated Fusion Protein Results in Decreased Tumor Growth

[284] The chimeric polypeptide is examined to determine if it could have biological effects in vivo. For these experiments a system is used in which tumor cells injected intraperitoneally rapidly and preferentially attach and grow initially on the milky spots, a series of organized immune aggregates found on the omentum (Gerber et al., Am. J. Pathol. 169:1739-52 (2006)). This system offers a convenient way to examine the effects of fusion protein treatment on tumor growth since fusion proteins can be delivered intraperitoneally multiple times and tumor growth can be analyzed by examining the dissociated omental cells. For these experiments, the Colon 38 cell line, a rapidly growing tumor cell line that expresses both MMP2 and MMP9 in vitro, may be used. The omental tissue normally expresses a relatively small amount of MMP2 and MMP9, but, when Colon 38 tumor is present on the omentum, MMP levels increase. Using this tumor model, the ability of IFN fusion proteins to affect tumor growth is examined. Colon 38 cells are injected intraperitoneally, allowed to attach and grow for 1 day, and then treated daily with fusion protein interaperitoneally. At day 7, the animals are sacrificed and the omenta examined for tumor growth using flow cytometry and by a colony-forming assay.

Example 13b: The chimeric polypeptide was examined to determine its biological effects in vivo. [285] The MC38 cell line, a rapidly growing colon adenocarcinoma cell line that expresses MMP9 in vitro, was used. Using this tumor model, the ability of ΙΤΝγ fusion proteins to affect tumor growth was examined. MC38 cells were injected subcutaneously, allowed to grow for 10-14 days, and then treated with fusion protein twice weekly intraperitoneally for a total of four doses, at the levels shown in FIG. 21A-21C. As a comparator, wild-type πιΙΤΝγ was administered at the dose levels indicated, twice daily for 2 weeks on a 5 day on/2 day off schedule (10 total doses). Tumor growth and body weight were monitored approximately twice per week for two weeks.

Example 14: Construction of an Exemplary IFNy Protein Targeting CD20

Generation of an activatable cytokine domain

[286] An ΙΡΝγ polypeptide capable of binding to CD20 polypeptide present in a tumor or on a tumor cell is produced as follows. A nucleic acid is produced that contains nucleic acid sequences: (1) encoding an ΙΡΝγ polypeptide sequence and (2) one or more polypeptide linkers. Activatable ΙΡΝγ plasmid constructs can have optional Flag, His or other affinity tags, and are electroporated into HEK293 or other suitable human or mammalian cell lines and purified. Validation assays include T cell activation assays using T cells responsive to IFNy stimulation in the presence of a protease.

Generation of a scFv CD20 binding domain

[287] CD20 is one of the cell surface proteins present on B-lymphocytes. CD20 antigen is found in normal and malignant pre-B and mature B lymphocytes, including those in over 90% of Β-cell nonHodgkin's lymphomas (NHL). The antigen is absent in hematopoietic stem cells, activated B lymphocytes (plasma cells) and normal tissue. As such, several antibodies mostly of murine origin have been described: 1F5,2B8/C2B8,2H7, and 1H4.

[288] Human or humanized anti-CD20 antibodies are therefore used to generate scFv sequences for CD20 binding domains of an activatable ΙΡΝγ protein. DNA sequences coding for human or humanized VL and VH domains are obtained, and the codons for the constructs are, optionally, optimized for expression in cells from Homo sapiens. The order in which the VL and VH domains appear in the scFv is varied (i.e., VL-VH, or VH-VL orientation), and three copies of the G4S (SEQ ID NO.: 449) or “G4S” (SEQ ID NO.: 449) subunit (G4S)3 (SEQ ID NO.: 452) connect the variable domains to create the scFv domain. Anti-CD20 scFv plasmid constructs can have optional Flag, His or other affinity tags, and are electroporated into HEK293 or other suitable human or mammalian cell lines and purified. Validation assays include binding analysis by FACS, kinetic analysis using Proteon, and staining of CD20-expressing cells.

Cloning of DNA expression constructs encoding the activatable IFNy protein

[289] The activatable ΙΡΝγ construct with protease cleavage site domains are used to construct an activatable ΙΡΝγ protein in combination with an anti-CD20 scFv domain and a serum half-life extension element (e.g., a HSA binding peptide or VH domain), with the domains organized. For expression of an activatable ΙΡΝγ protein in CHO cells, coding sequences of all protein domains are cloned into a mammalian expression vector system. In brief, gene sequences encoding the activatable ΙΡΝγ domain, serum half-life extension element, and CD20 binding domain along with peptide linkers LI and L2 are separately synthesized and subcloned. The resulting constructs are then ligated together in the order of CD20 binding domain - LI - ΙΡΝγ subunit 1- L2 - protease cleavage domain

- L3 - IFNy subunit2 - L4 - anti-CD20 scFv - L5 - serum half-life extension element to yield a final construct. All expression constructs are designed to contain coding sequences for an N-terminal signal peptide and a C-terminal hexahistidine (6xHis)-tag (SEQ ID NO.: 354) to facilitate protein secretion and purification, respectively.

Expression of activatable IFNy proteins in stably transfected CHO cells

[290] A CHO cell expression system (Flp-In®, Life Technologies), a derivative of CHO-K1 Chinese Hamster ovary cells (ATCC, CCL-61) (Kao and Puck, Proc. Natl. Acad Sci USA 1968;60(4): 1275-81), is used. Adherent cells are subcultured according to standard cell culture protocols provided by Life Technologies.

[291] For adaption to growth in suspension, cells are detached from tissue culture flasks and placed in serum-free medium. Suspension-adapted cells are cryopreserved in medium with 10% DMSO.

[292] Recombinant CHO cell lines stably expressing secreted activatable IFNy proteins are generated by transfection of suspension-adapted cells. During selection with the antibiotic Hygromycin B viable cell densities are measured twice a week, and cells are centrifuged and resuspended in fresh selection medium at a maximal density of O.lxlO6 viable cells/mL. Cell pools stably expressing activatable ΙΡΝγ proteins are recovered after 2-3 weeks of selection at which point cells are transferred to standard culture medium in shake flasks. Expression of recombinant secreted proteins is confirmed by performing protein gel electrophoresis or flow cytometry. Stable cell pools are cryopreserved in DMSO containing medium.

[293] Activatable IFNy proteins are produced in 10-day fed-batch cultures of stably transfected CHO cell lines by secretion into the cell culture supernatant. Cell culture supernatants are harvested after 10 days at culture viabilities of typically >75%. Samples are collected from the production cultures every other day and cell density and viability are assessed. On day of harvest, cell culture supernatants are cleared by centrifugation and vacuum filtration before further use.

[294] Protein expression titers and product integrity in cell culture supernatants are analyzed by SDS-PAGE.

Purification of activatable IFNy proteins

[295] Activatable IFNy proteins are purified from CHO cell culture supernatants in a two-step procedure. The constructs are subjected to affinity chromatography in a first step followed by preparative size exclusion chromatography (SEC) on Superdex 200 in a second step. Samples are buffer-exchanged and concentrated by ultrafiltration to a typical concentration of >1 mg/mL. Purity and homogeneity (typically >90%) of final samples are assessed by SDS PAGE under reducing and non-reducing conditions, followed by immunoblotting using an anti-HSA or anti idiotype antibody as well as by analytical SEC, respectively. Purified proteins are stored at aliquots at -80°C until use.

Example 15: Determination of antigen affinity by flow cytometry

[296] The activatable IFNy proteins of Example 1 are tested for their binding affinities to human

CD20+ cells and cynomolgus CD20+ cells.

[297] CD20+ cells are incubated with 100 pL of serial dilutions of the activatable IFNy proteins of Example 1 and at least one protease. After washing three times with FACS buffer the cells are incubated with 0.1 mL of 10 pg/mL mouse monoclonal anti-idiotype antibody in the same buffer for 45 min on ice. After a second washing cycle, the cells are incubated with 0.1 mL of 15 pg/mL FITCconjugated goat anti-mouse IgG antibodies under the same conditions as before. As a control, cells are incubated with the anti-His IgG followed by the FITC-conjugated goat anti-mouse IgG antibodies without the activatable lENyproteins. The cells were then washed again and resuspended in 0.2 mL of FACS buffer containing 2 pg/mL propidium iodide (PI) in order to exclude dead cells. The fluorescence of IxlO4 living cells is measured using a Beckman-Coulter FC500 MPL flow cytometer using the MXP software (Beckman-Coulter, Krefeld, Germany) or a Millipore Guava EasyCyte flow cytometer using the Incyte software (Merck Millipore, Schwalbach, Germany). Mean fluorescence intensities of the cell samples are calculated using CXP software (Beckman-Coulter, Krefeld, Germany) or Incyte software (Merck Millipore, Schwalbach, Germany). After subtracting the fluorescence intensity values of the cells stained with the secondary and tertiary reagents alone the values are then used for calculation of the Kd values with the equation for one-site binding (hyperbola) of the GraphPad Prism (version 6.00 for Windows, GraphPad Software, La Jolla California USA).

[298] CD20 binding and crossreactivity are assessed on the human CD20+ tumor cell lines. The Kd ratio of crossreactivity is calculated using the Kd values determined on the CHO cell lines expressing either recombinant human or recombinant cynomolgus antigens.

Example 16: Cytotoxicity Assay

[299] The activatable IFNy protein of Example 5 is evaluated in vitro on its mediation of immune response to CD20+ target cells.

[300] Fluorescence labeled CD20+ REC-1 cells (a Mantle cell lymphoma cell line, ATCC CRL3004) are incubated with isolated PBMC of random donors or CB15 T-cells (standardized T-cell line) as effector cells in the presence of the activatable ΙΡΝγ protein of Example 5 and at least one protease. After incubation for 4 h at 37°C in a humidified incubator, the release of the fluorescent dye from the target cells into the supernatant is determined in a spectrofluorimeter. Target cells incubated without the activatable ΙΡΝγ protein of Example 5 and target cells totally lysed by the addition of saponin at the end of the incubation serve as negative and positive controls, respectively.

[301] Based on the measured remaining living target cells, the percentage of specific cell lysis is

calculated according to the following formula: [!-(number of living targetS(samp1e)/number of living targetS(spontaneous))] x 100%. Sigmoidal dose response curves and EC50 values are calculated by nonlinear regression/4-parameter logistic fit using the GraphPad Software. The lysis values obtained for a given antibody concentration are used to calculate sigmoidal dose-response curves by 4 parameter logistic fit analysis using the Prism software.

Example 17: Pharmacokinetics of activatable IFNy Proteins

[302] The activatable ΙΕΝγ protein of Example 5 is evaluated for half-time elimination in animal studies.

[303] The activatable ΙΕΝγ protein is administered to cynomolgus monkeys as a 0.5 mg/kg bolus injection into the saphenous vein. Another cynomolgus monkey group receives a comparable cytokine in size, but lacking a serum half-life extension element. A third and fourth group receive a cytokine with serum half-life extension elements and a cytokine with CD20 and serum half-life extension elements respectively, and both comparable in size to the activatable ΙΕΝγ protein. Each test group consists of 5 monkeys. Serum samples are taken at indicated time points, serially diluted, and the concentration of the proteins is determined using a binding ELISA to CD20.

[304] Pharmacokinetic analysis is performed using the test article plasma concentrations. Group mean plasma data for each test article conforms to a multi-exponential profile when plotted against the time post-dosing. The data are fit by a standard two-compartment model with bolus input and first-order rate constants for distribution and elimination phases. The general equation for the best fit of the data for i.v. administration is: c(t)=Ae-aL1-Be_pt, where c(t) is the plasma concentration at time t, A and B are intercepts on the Y-axis, and a and β are the apparent first-order rate constants for the distribution and elimination phases, respectively. The a-phase is the initial phase of the clearance and reflects distribution of the protein into all extracellular fluid of the animal, whereas the second or βphase portion of the decay curve represents true plasma clearance. Methods for fitting such equations are well known in the art. For example, Α=&#911;/ν(α^21)/(α-β), Β=&#911;/ν(β^21)/(α-β), and a and β (for α>β) are roots of the quadratic equation: r2+(kl2+k21+kl0)r+k21kl 0=0 using estimated parameters of V=volume of distribution, kl0=elimination rate, kl2=transfer rate from compartment 1 to compartment 2 and k21=transfer rate from compartment 2 to compartment 1, and D=the administered dose.

[305] Data analysis: Graphs of concentration versus time profiles are made using KaleidaGraph (KaleidaGraph™ V. 3.09 Copyright 1986-1997. Synergy Software. Reading, Pa.). Values reported as less than reportable (LTR) are not included in the PK analysis and are not represented graphically. Pharmacokinetic parameters are determined by compartmental analysis using WinNonlin software (WinNonlin® Professional V. 3.1 WinNonlin™ Copyright 1998-1999. Pharsight Corporation. Mountain View, Calif.). Pharmacokinetic parameters are computed as described in Ritschel W A and

Kearns G L, 1999, IN: Handbook Of Basic Pharmacokinetics Including Clinical Applications, 5 th edition, American Pharmaceutical Assoc., Washington, D.C.

[306] It is expected that the activatable ΙΡΝγ protein of Example 5 has improved pharmacokinetic parameters such as an increase in elimination half-time as compared to proteins lacking a serum halflife extension element.

Example 18: Xenograft Tumor Model

[307] The activatable IFNy protein of Example 5 is evaluated in a xenograft model.

[308] Female immune-deficient NOD/scid mice are sub-lethally irradiated (2 Gy) and subcutaneously inoculated with 4x106 Ramos RAI cells into the right dorsal flank. When tumors reach 100 to 200 mm3, animals are allocated into 3 treatment groups. Groups 2 and 3 (8 animals each) are intraperitoneally injected with 1.5xl07 activated human T-cells. Three days later, animals from Group 3 are subsequently treated with a total of 9 intravenous doses of 50 pg activatable IFNy protein of Example 5 (qdx9d). Groups 1 and 2 are only treated with vehicle. Body weight and tumor volume are determined for 30 days.

[309] It is expected that animals treated with the activatable IFNy protein of Example 5 have a statistically significant delay in tumor growth in comparison to the respective vehicle-treated control group.

[310] While preferred embodiments of the present invention have been shown and described herein, it will be obvious to those skilled in the art that such embodiments are provided by way of example only. Numerous variations, changes, and substitutions will now occur to those skilled in the art without departing from the invention. It should be understood that various alternatives to the embodiments of the invention described herein may be employed in practicing the invention. It is intended that the following claims define the scope of the invention and that methods and structures within the scope of these claims and their equivalents be covered thereby.

Example 19: HEK-Blue assay

[311] HEK-Blue IL12 cells (InvivoGen) were plated in suspension at a concentration of 50,000 cells/well in culture media with or without 15 or 40mg/ml human serum albumin (HSA) and stimulated with a dilution series of recombinant hIL12, chimeric IL 12 (mouse p35/human p40) or activatable hIL12 for 20-24 hours at 37°C and 5% CO2. Activity of uncleaved and cleaved activatable hIL12 was tested. Cleaved inducible hIL12 was generated by incubation with active MMP9. IL12 activity was assessed by quantification of Secreted Alkaline Phosphatase (SEAP) activity using the reagent QUANTI-Blue (InvivoGen), a colorimetric based assay. Results are shown in FIGs. 7A-7Q, 11 A-l IB, 12A-12F, 15A-15D, and 26A-26D.

[312] HEK-Blue IL2 cells (InvivoGen) were plated in suspension at a concentration of 50,000 cells/well in culture media with or without 15-40 mg/ml human serum albumin (HSA) and stimulated with a dilution series of recombinant hIL2 or activatable hIL2 for 24 hours at 37°C and 5% CO2.

Activity of uncleaved and cleaved activatable hIL2 was tested. Cleaved inducible hIL2 was generated by incubation with active MMP9. IL12 activity was assessed by quantification of Secreted Alkaline Phosphatase (SEAP) activity using the reagent QUANTI-Blue (InvivoGen), a colorimetric based assay. Exemplary results are shown in FIGs. 1A-1F and FIGs. 24A-24D.

[313] HEK-Blue IFN-a/b cells (InvivoGen) were plated in suspension at a density of 50,000 cells/well in culture media with or without 15 mg/ml human serum albumin (HSA) and stimulated with a dilution series of recombinant human IFNa (or IFNb) and activatable human IFNa (or IFNb) for 20-24 hours at 370C and 5% CO2. Activity of uncleaved and cleaved activatable IFNa (or IFNb) was tested. Cleaved inducible IFNa (or IFNb) was generated by incubation with active recombinant protease. Stimulation of HEK-Blue IFN-ot/β cells with IFNa (or ΙΡΝβ) induces expression of Secreted Alkaline Phosphatase (SEAP) from an ISG54-SEAP reporter. IFNa (or ΙΡΝβ) activity was assessed by quantification of SEAP activity using the reagent QUANTI-Blue (InvivoGen), a colorimetric based assay. Results are shown in FIGs. 36A-36H.

Example 20: Splenocyte T-Blast assay

[314] T-Blasts were induced from murine splenocytes with a 6-day incubation with PHA and a 24hr incubation with recombinant hIL12. Tbiasts were then plated in suspension at a concentration of 200,000 cells/well in culture media with or without 40mg/ml human serum albumin (HSA) and stimulated with a dilution series of recombinant hIL12 or chimeric IL 12 (mouse p35/human p40) or mouse IL12 for 72 hours at 37°C and 5% CO2. Activity of uncleaved and cleaved IL12 fusion proteins was tested. Cleaved inducible hIL12 was generated by incubation with active MMP9. IL12 activity was assessed by downstream quantification of ΙΡΝγ production using a πιΙΡΝγ alpha ELISA.

Example 21: In Vivo Delivery of a Protease Activated Fusion Protein Results in Decreased Tumor Growth

[315] The chimeric polypeptide is examined to determine if it could have biological effects in vivo. For these experiments a system is used in which tumor cells injected intraperitoneally rapidly and preferentially attach and grow initially on the milky spots, a series of organized immune aggregates found on the omentum (Gerber et al., Am. J. Pathol. 169:1739-52 (2006)). This system offers a convenient way to examine the effects of fusion protein treatment on tumor growth since fusion proteins can be delivered intraperitoneally multiple times and tumor growth can be analyzed by examining the dissociated omental cells. For these experiments, the Colon 38 cell line, a rapidly growing tumor cell line that expresses both MMP2 and MMP9 in vitro, may be used. The omental

tissue normally expresses a relatively small amount of MMP2 and MMP9, but, when Colon 38 tumor is present on the omentum, MMP levels increase. Using this tumor model, the ability of IL-2 mutein fusion proteins to affect tumor growth is examined. Colon 38 cells are injected intraperitoneally, allowed to attach and grow for 1 day, and then treated daily with fusion protein interaperitoneally. At day 7, the animals are sacrificed and the omenta examined for tumor growth using flow cytometry and by a colony-forming assay.

Example 22: Construction of an Exemplary Activatable Interleukin Protein Targeting CD20 Generation of an activatable interleukin domain

[316] The human IL-12p35 chain canonical sequence is Uniprot Accession No. P29459. The human IL-12p40 chain canonical sequence is Uniprot Accession No. P29460. IL-12p35 and IL-12p40 are cloned into an expression construct. A protease cleavage site is included between the IL-12p35 and IL-12p40 domains. An IL-12 polypeptide capable of binding to CD20 polypeptide present in a tumor or on a tumor cell is produced as follows. A nucleic acid is produced that contains nucleic acid sequences: (1) encoding an IFNy polypeptide sequence and (2) one or more polypeptide linkers. Activatable interleukin plasmid constructs can have optional Flag, His or other affinity tags, and are electroporated into HEK293 or other suitable human or mammalian cell lines and purified. Validation assays include T cell activation assays using T cells responsive to IL-12 stimulation in the presence of a protease.

Generation of a scFv CD20 binding domain

[317] CD20 is one of the cell surface proteins present on B-lymphocytes. CD20 antigen is found in normal and malignant pre-B and mature B lymphocytes, including those in over 90% of B-cell nonHodgkin's lymphomas (NHL). The antigen is absent in hematopoietic stem cells, activated B lymphocytes (plasma cells) and normal tissue. As such, several antibodies mostly of murine origin have been described: 1F5,2B8/C2B8,2H7, and 1H4.

[318] Human or humanized anti-CD20 antibodies are therefore used to generate scFv sequences for CD20 binding domains of an activatable interleukin protein. DNA sequences coding for human or humanized VL and VH domains are obtained, and the codons for the constructs are, optionally, optimized for expression in cells from Homo sapiens. The order in which the VL and VH domains appear in the scFv is varied (i.e., VL-VH, or VH-VL orientation), and three copies of the G4S (SEQ ID NO.: 449) or “G4S” (SEQ ID NO.: 449) subunit (G4S)3 (SEQ ID NO.: 452) connect the variable domains to create the scFv domain. Anti-CD20 scFv plasmid constructs can have optional Flag, His or other affinity tags, and are electroporated into HEK293 or other suitable human or mammalian cell lines and purified. Validation assays include binding analysis by FACS, kinetic analysis using Proteon, and staining of CD20-expressing cells.

Cloning of DNA expression constructs encoding the activatable interleukin protein

[319] The activatable interleukin construct with protease cleavage site domains are used to construct an activatable interleukin protein in combination with an anti-CD20 scFv domain and a serum half-life extension element (e.g., a HSA binding peptide or VH domain). For expression of an activatable interleukin protein in CHO cells, coding sequences of all protein domains are cloned into a mammalian expression vector system. In brief, gene sequences encoding the activatable interleukin domain, serum half-life extension element, and CD20 binding domain along with peptide linkers LI and L2 are separately synthesized and subcloned. The resulting constructs are then ligated together in the order of CD20 binding domain - LI - IL-12p35- L2 - protease cleavage domain - L3 - IL-12p40 - L4 - anti-CD20 scFv - L5 - serum half-life extension element to yield a final construct. All expression constructs are designed to contain coding sequences for an N-terminal signal peptide and a C-terminal hexahistidine (6xHis)-tag (SEQ ID NO.: 354) to facilitate protein secretion and purification, respectively.

Expression of activatable interleukin proteins in stably transfected CHO cells

[320] A CHO cell expression system (Flp-In®, Life Technologies), a derivative of CHO-K1 Chinese Hamster ovary cells (ATCC, CCL-61) (Kao and Puck, Proc. Natl. Acad Sci USA 1968;60(4): 1275-81), is used. Adherent cells are subcultured according to standard cell culture protocols provided by Life Technologies.

[321] For adaption to growth in suspension, cells are detached from tissue culture flasks and placed in serum-free medium. Suspension-adapted cells are cryopreserved in medium with 10% DMSO.

[322] Recombinant CHO cell lines stably expressing secreted activatable interleukin proteins are generated by transfection of suspension-adapted cells. During selection with the antibiotic Hygromycin B viable cell densities are measured twice a week, and cells are centrifuged and resuspended in fresh selection medium at a maximal density of O.lxlO6 viable cells/mL. Cell pools stably expressing activatable interleukin proteins are recovered after 2-3 weeks of selection at which point cells are transferred to standard culture medium in shake flasks. Expression of recombinant secreted proteins is confirmed by performing protein gel electrophoresis or flow cytometry. Stable cell pools are cryopreserved in DMSO containing medium.

[323] Activatable interleukin proteins are produced in 10-day fed-batch cultures of stably transfected CHO cell lines by secretion into the cell culture supernatant. Cell culture supernatants are harvested after 10 days at culture viabilities of typically >75%. Samples are collected from the production cultures every other day and cell density and viability are assessed. On day of harvest, cell culture supernatants are cleared by centrifugation and vacuum filtration before further use.

[324] Protein expression titers and product integrity in cell culture supernatants are analyzed by SDS-PAGE.

Purification of activatable interleukin proteins

[325] Activatable interleukin proteins are purified from CHO cell culture supernatants in a two-step procedure. The constructs are subjected to affinity chromatography in a first step followed by preparative size exclusion chromatography (SEC) on Superdex 200 in a second step. Samples are buffer-exchanged and concentrated by ultrafiltration to a typical concentration of >1 mg/mL. Purity and homogeneity (typically >90%) of final samples are assessed by SDS PAGE under reducing and non-reducing conditions, followed by immunoblotting using an anti-HSA or anti idiotype antibody as well as by analytical SEC, respectively. Purified proteins are stored at aliquots at -80°C until use.

Example 23: Determination of antigen affinity by flow cytometry

[326] The activatable interleukin proteins of Example 5 are tested for their binding affinities to human CD20+ cells and cynomolgus CD20+ cells.

[327] CD20+ cells are incubated with 100 pL of serial dilutions of the activatable interleukin proteins of Example 5 and at least one protease. After washing three times with FACS buffer the cells are incubated with 0.1 mL of 10 pg/mL mouse monoclonal anti-idiotype antibody in the same buffer for 45 min on ice. After a second washing cycle, the cells are incubated with 0.1 mL of 15 pg/mL FITC-conjugated goat anti-mouse IgG antibodies under the same conditions as before. As a control, cells are incubated with the anti-His IgG followed by the FITC-conjugated goat anti-mouse IgG antibodies without the activatable interleukin proteins. The cells were then washed again and resuspended in 0.2 mL of FACS buffer containing 2 pg/mL propidium iodide (PI) in order to exclude dead cells. The fluorescence of IxlO4 living cells is measured using a Beckman-Coulter FC500 MPL flow cytometer using the MXP software (Beckman-Coulter, Krefeld, Germany) or a Millipore Guava EasyCyte flow cytometer using the Incyte software (Merck Millipore, Schwalbach, Germany). Mean fluorescence intensities of the cell samples are calculated using CXP software (Beckman-Coulter, Krefeld, Germany) or Incyte software (Merck Millipore, Schwalbach, Germany). After subtracting the fluorescence intensity values of the cells stained with the secondary and tertiary reagents alone the values are then used for calculation of the Kd values with the equation for one-site binding (hyperbola) of the GraphPad Prism (version 6.00 for Windows, GraphPad Software, La Jolla California USA).

[328] CD20 binding and crossreactivity are assessed on the human CD20+ tumor cell lines. The Kd ratio of crossreactivity is calculated using the Kd values determined on the CHO cell lines expressing either recombinant human or recombinant cynomolgus antigens.

Example 24: Cytotoxicity Assay

[329] The activatable interleukin protein of Example 5 is evaluated in vitro on its mediation of immune response to CD20+ target cells.

[330] Fluorescence labeled CD20+ REC-1 cells (a Mantle cell lymphoma cell line, ATCC CRL3004) are incubated with isolated PBMC of random donors or CB15 T-cells (standardized T-cell line) as effector cells in the presence of the activatable interleukin protein of Example 5 and at least one protease. After incubation for 4 h at 37°C in a humidified incubator, the release of the fluorescent dye from the target cells into the supernatant is determined in a spectrofluorimeter. Target cells incubated without the activatable interleukin protein of Example 5and target cells totally lysed by the addition of saponin at the end of the incubation serve as negative and positive controls, respectively.

[331] Based on the measured remaining living target cells, the percentage of specific cell lysis is calculated according to the following formula: [!-(number of living targetS(samp1e)/number of living targetS(spontaneous))] x 100%. Sigmoidal dose response curves and EC50 values are calculated by nonlinear regression/4-parameter logistic fit using the GraphPad Software. The lysis values obtained for a given antibody concentration are used to calculate sigmoidal dose-response curves by 4 parameter logistic fit analysis using the Prism software.

Example 25: Pharmacokinetics of activatable interleukin Proteins

[332] The activatable interleukin protein of Example 5 is evaluated for half-time elimination in animal studies.

[333] The activatable interleukin protein is administered to cynomolgus monkeys as a 0.5 mg/kg bolus injection into the saphenous vein. Another cynomolgus monkey group receives a comparable cytokine in size, but lacking a serum half-life extension element. A third and fourth group receive a cytokine with serum half-life extension elements and a cytokine with CD20 and serum half-life extension elements respectively, and both comparable in size to the activatable interleukin protein. Each test group consists of 5 monkeys. Serum samples are taken at indicated time points, serially diluted, and the concentration of the proteins is determined using a binding ELISA to CD20.

[334] Pharmacokinetic analysis is performed using the test article plasma concentrations. Group mean plasma data for each test article conforms to a multi-exponential profile when plotted against the time post-dosing. The data are fit by a standard two-compartment model with bolus input and first-order rate constants for distribution and elimination phases. The general equation for the best fit of the data for i.v. administration is: c(t)=Ae-a,TBe_pt, where c(t) is the plasma concentration at time t, A and B are intercepts on the Y-axis, and a and β are the apparent first-order rate constants for the distribution and elimination phases, respectively. The a-phase is the initial phase of the clearance and reflects distribution of the protein into all extracellular fluid of the animal, whereas the second or βphase portion of the decay curve represents true plasma clearance. Methods for fitting such equations

are well known in the art. For example, A=D/V(a-k21)/(a-p), Β=&#971;/ν(βΑ21)/(α-β), and a and β (for α>β) are roots of the quadratic equation: r2+(kl2+k21+kl0)r+k21kl 0=0 using estimated parameters of V=volume of distribution, klO=elimination rate, kl2=transfer rate from compartment 1 to compartment 2 and k21=transfer rate from compartment 2 to compartment 1, and D=the administered dose.

[335] Data analysis: Graphs of concentration versus time profiles are made using KaleidaGraph (KaleidaGraph™ V. 3.09 Copyright 1986-1997. Synergy Software. Reading, Pa.). Values reported as less than reportable (LTR) are not included in the PK analysis and are not represented graphically. Pharmacokinetic parameters are determined by compartmental analysis using WinNonlin software (WinNonlin® Professional V. 3.1 WinNonlin™ Copyright 1998-1999. Pharsight Corporation. Mountain View, Calif.). Pharmacokinetic parameters are computed as described in Ritschel W A and Kearns G L, 1999, IN: Handbook Of Basic Pharmacokinetics Including Clinical Applications, 5 th edition, American Pharmaceutical Assoc., Washington, D.C.

[336] It is expected that the activatable interleukin protein of Example 5 has improved pharmacokinetic parameters such as an increase in elimination half-time as compared to proteins lacking a serum half-life extension element.

Example 26: Xenograft Tumor Model

[337] The activatable interleukin protein of Example 5 is evaluated in a xenograft model.

[338] Female immune-deficient NOD/scid mice are sub-lethally irradiated (2 Gy) and subcutaneously inoculated with 4x106 Ramos RAI cells into the right dorsal flank. When tumors reach 100 to 200 mm3, animals are allocated into 3 treatment groups. Groups 2 and 3 (8 animals each) are intraperitoneally injected with 1.5xl07 activated human T-cells. Three days later, animals from Group 3 are subsequently treated with a total of 9 intravenous doses of 50 pg activatable interleukin protein of Example 5 (qdx9d). Groups 1 and 2 are only treated with vehicle. Body weight and tumor volume are determined for 30 days.

[339] It is expected that animals treated with the activatable interleukin protein of Example 5 have a statistically significant delay in tumor growth in comparison to the respective vehicle-treated control group.

[340] While preferred embodiments of the present invention have been shown and described herein, it will be obvious to those skilled in the art that such embodiments are provided by way of example only. Numerous variations, changes, and substitutions will now occur to those skilled in the art without departing from the invention. It should be understood that various alternatives to the embodiments of the invention described herein may be employed in practicing the invention. It is intended that the following claims define the scope of the invention and that methods and structures within the scope of these claims and their equivalents be covered thereby.

Example 27: MC38 experiments

[341] The MC38 cell line, a rapidly growing colon adenocarcinoma cell line that expresses MMP9 in vitro, was used. Using this tumor model, the ability of fusion proteins to affect tumor growth was examined.

Example 27a: MC38IL-2POC

Agents and Treatment:

<td> Gr.</td><td> N</td><td> Agent</td><td> Formulation dose</td><td> Route</td><td> Schedule</td>

<td> 1^#</td><td> 10</td><td> Vehicle</td><td> -</td><td> ip</td><td> biwk x 3</td>

<td> 2</td><td> 7</td><td> ACPI 6</td><td> 700pg/animal</td><td> ip</td><td> biwk x 3</td>

<td> 3</td><td> 7</td><td> ACPI 6</td><td> 230pg/animal</td><td> ip</td><td> biwk x 3</td>

<td> 4</td><td> 7</td><td> ACPI 6</td><td> 70pg/animal</td><td> ip</td><td> biwk x 3</td>

<td> 5</td><td> 7</td><td> ACPI 6</td><td> 55ug/animal</td><td> ip</td><td> biwk x 3</td>

<td> 6</td><td> 7</td><td> ACPI 6</td><td> 17pg/animal</td><td> ip</td><td> biwk x 3</td>

<td> 7</td><td> 7</td><td> ACPI 32</td><td> 361 pg/animal</td><td> ip</td><td> biwk x 3</td>

<td> 8</td><td> 7</td><td> ACPI 32</td><td> 119pg/animal</td><td> ip</td><td> biwk x 3</td>

<td> 9</td><td> 7</td><td> ACPI 32</td><td> 36 pg/animal</td><td> ip</td><td> biwk x 3</td>

<td> 10</td><td> 7</td><td> ACPI 32</td><td> 28pg/animal</td><td> ip</td><td> biwk x 3</td>

<td> 11</td><td> 7</td><td> ACPI 32</td><td> 9 pg/animal</td><td> ip</td><td> biwk x 3</td>

<td> 12</td><td> 7</td><td> ACP21</td><td> 540pg/animal</td><td> ip</td><td> biwk x 3</td>

<td> 13</td><td> 7</td><td> ACP21</td><td> 177pg/animal</td><td> ip</td><td> biwk x 3</td>

<td> 14</td><td> 7</td><td> ACP21</td><td> 54pg/animal</td><td> ip</td><td> biwk x 3</td>

<td> 15</td><td> 7</td><td> ACP21</td><td> 42pg/animal</td><td> ip</td><td> biwk x 3</td>

<td> 16</td><td> 7</td><td> ACP21</td><td> 13pg/animal</td><td> ip</td><td> biwk x 3</td>

<td> #</td><td> ControlGrou P</td><td></td><td></td><td></td><td></td>

Procedures:

[342] Mice were anaesthetized with isoflurane for implant of cells to reduce the ulcerations. 308 CR female C57BL/6 mice were set up with 5xl05 MC38 tumor cells in 0% Matrigel sc in flank. Cell Injection Volume was 0.1 mL/mouse. Mouse age at start date was 8 to 12 weeks. Pair matches were

performed when tumors reach an average size of 100 - 150 mm3 and begin treatment. Body weights were taken at initiation and then biweekly to the end. Caliper measurements were taken biweekly to the end. Any adverse reactions were to be reported immediately. Any individual animal with a single observation of > than 30% body weight loss or three consecutive measurements of >25% body weight loss was euthanized. Any group with a mean body weight loss of >20 % or >10% mortality stopped dosing; the group was not euthanized and recovery is allowed. Within a group with >20% weight loss, individuals hitting the individual body weight loss endpoint were euthanized. If the group treatment related body weight loss is recovered to within 10% of the original weights, dosing resumed at a lower dose or less frequent dosing schedule. Exceptions to non-treatment body weight % recovery were allowed on a case-by-case basis. Endpoint was tumor growth delay (TGD). Animals were monitored individually. The endpoint of the experiment was a tumor volume of 1500 mm3 or 45 days, whichever comes first. Responders were followed longer. When the endpoint was reached, the animals are to be euthanized.

[343] Results are shown in FIG. 35.

Example 27b: MC38 IL-2 POC. Treatment with ACP16, ACP124 and ACP130

Agents and Treatment:

<td> Gr.</td><td> N</td><td> Agent</td><td> Formulation dose</td><td> Route</td><td> Schedule</td>

<td> 1^#</td><td> 12</td><td> Vehicle</td><td> -</td><td> ip</td><td> biwk x 2</td>

<td> 2</td><td> 8</td><td> ACPI 6</td><td> 4.4 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 3</td><td> 8</td><td> ACPI 6</td><td> 17 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 4</td><td> 8</td><td> ACPI 6</td><td> 70 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 5</td><td> 8</td><td> ACPI 6</td><td> 232 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 6</td><td> 8</td><td> ACPI 30</td><td> 19 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 7</td><td> 8</td><td> ACPI 30</td><td> 45 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 8</td><td> 8</td><td> ACPI 30</td><td> 180 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 9</td><td> 8</td><td> ACPI 30</td><td> 600 pg/animal</td><td> ip</td><td> biwk x 1</td>

<td> 12</td><td> 8</td><td> ACP124</td><td> 17 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 13</td><td> 8</td><td> ACP124</td><td> 70 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 14</td><td> 8</td><td> ACP124</td><td> 230 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 15</td><td> 8</td><td> ACP124</td><td> 700 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 16</td><td> 8</td><td> IL-2WTI</td><td> 12 pg/animal</td><td> ip</td><td> bid x 5 then 2-day pause then bid x 5 then 2day pause</td>

<td> 17</td><td> 8</td><td colspan="2"> IL-2- WTI</td><td> 36 pg/animal</td><td> ip</td><td> bid x 5 then 2-day pause then bid x 5 then 2day pause</td>

<td></td><td colspan="2"> - Control Group</td><td colspan="4"></td>

Procedures:

[344] Mice were anaesthetized with isoflurane for implant of cells to reduce the ulcerations. 308 CR female C57BL/6 mice were set up with 5xl05 MC38 tumor cells in 0% Matrigel sc in flank. Cell Injection Volume was 0.1 mL/mouse. Mouse age at start date was 8 to 12 weeks.Pair matches were performed when tumors reach an average size of 100 - 150 mm3 and begin treatment. Body weights were taken at initiation and then biweekly to the end. Caliper measurements were taken biweekly to the end. Any adverse reactions were to be reported immediately. Any individual animal with a single observation of > than 30% body weight loss or three consecutive measurements of >25% body weight loss was euthanized. Any group with a mean body weight loss of >20 % or >10% mortality stopped dosing; the group was not euthanized and recovery is allowed. Within a group with >20% weight loss, individuals hitting the individual body weight loss endpoint were euthanized. If the group treatment related body weight loss is recovered to within 10% of the original weights, dosing resumed at a lower dose or less frequent dosing schedule. Exceptions to non-treatment body weight % recovery were allowed on a case-by-case basis. Endpoint was tumor growth delay (TGD). Animals were monitored individually. The endpoint of the experiment was a tumor volume of 1500 mm3 or 45 days, whichever comes first. Responders were followed longer. When the endpoint was reached, the animals are to be euthanized.

Results are shown in FIG. 31A-31C and FIG. 32B-32C. Survival curves are shown in FIGs. 34A-34D.

Example 27c: MC38 IFNa and IL-12 Agents and Treatment:

<td> Gr.</td><td> N</td><td> Agent</td><td> Formulation dose</td><td> Route</td><td> Schedule</td>

<td> 1^#</td><td> 12</td><td> Vehicle</td><td> -</td><td> ip</td><td> biwk x 3</td>

<td> 2</td><td> 8</td><td> ACP11</td><td> 17.5 pg/animal</td><td> ip</td><td> biwk x 3</td>

<td> 3</td><td> 8</td><td> ACP11</td><td> 175 pg/animal</td><td> ip</td><td> biwk x 3</td>

<td> 4</td><td> 8</td><td> ACP11</td><td> 525 pg/animal</td><td> ip</td><td> biwk x 3</td>

<td> 5</td><td> 8</td><td> ACP31</td><td> 33 pg/animal</td><td> ip</td><td> biwk x 3</td>

<td> 6</td><td> 8</td><td> ACP31</td><td> 110 pg/animal</td><td> ip</td><td> biwk x 3</td>

<td> 7</td><td> 8</td><td> ACP31</td><td> 330 pg/animal</td><td> ip</td><td> biwk x 3</td>

<td> 8</td><td> 8</td><td colspan="2"> ACP131</td><td> 1 pg/animal</td><td> ip</td><td> bid x 5 then 2-day pause then bid x 5 then 2day pause</td>

<td> 9</td><td> 8</td><td colspan="2"> ACP131</td><td> 10 pg/animal</td><td> ip</td><td> bid x 5 then 2-day pause then bid x 5 then 2day pause</td>

<td> 10</td><td> 8</td><td colspan="2"> ACP131</td><td> 30 pg/animal</td><td> ip</td><td> bid x 5 then 2-day pause then bid x 5 then 2day pause</td>

<td> 11</td><td> 8</td><td colspan="2"> mIFNal- WTI</td><td> 1 pg/animal</td><td> ip</td><td> bid x 5 then 2-day pause then bid x 5 then 2day pause</td>

<td> 12</td><td> 8</td><td colspan="2"> mIFNal- WTI</td><td> 10 pg/animal</td><td> ip</td><td> bid x 5 then 2-day pause then bid x 5 then 2day pause</td>

<td> 13</td><td> 8</td><td colspan="2"> IL-12- HM- WTI</td><td> 2 pg/animal</td><td> ip</td><td> bid x 5 then 2-day pause then bid x 5 then 2day pause</td>

<td> 14</td><td> 8</td><td colspan="2"> IL-12- HM- WTI</td><td> 10 pg/animal</td><td> ip</td><td> bid x 5 then 2-day pause then bid x 5 then 2day pause</td>

<td> 15</td><td> 8</td><td colspan="2"> ACP131</td><td> 5 pg/animal</td><td> itu</td><td> bid x 5 then 2-day pause then bid x 5 then 2day pause</td>

<td></td><td colspan="2"> - Control Group</td><td colspan="4"></td>

Procedures:

[345] Mice were anaesthetized with isoflurane for implant of cells to reduce the ulcerations. 308 CR female C57BL/6 mice were set up with 5xl05 MC38 tumor cells in 0% Matrigel sc in flank. Cell Injection Volume was 0.1 mL/mouse. Mouse age at start date was 8 to 12 weeks.Pair matches were performed when tumors reach an average size of 100 - 150 mm3 and begin treatment. Body weights were taken at initiation and then biweekly to the end. Caliper measurements were taken biweekly to the end. Any adverse reactions were to be reported immediately. Any individual animal with a single observation of > than 30% body weight loss or three consecutive measurements of >25% body weight loss was euthanized. Any group with a mean body weight loss of >20 % or >10% mortality stopped dosing; the group was not euthanized and recovery is allowed. Within a group with >20% weight loss, individuals hitting the individual body weight loss endpoint were euthanized. If the group treatment related body weight loss is recovered to within 10% of the original weights, dosing resumed at a lower dose or less frequent dosing schedule. Exceptions to non-treatment body weight % recovery

were allowed on a case-by-case basis. Endpoint was tumor growth delay (TGD). Animals were monitored individually. The endpoint of the experiment was a tumor volume of 1500 mm3 or 45 days, whichever comes first. Responders were followed longer. When the endpoint was reached, the animals are to be euthanized. Results are show in in FIGs. 29A-29B, and 30.

Example 27d: Treatment with ACP16, ACP132, and ACP21

Agents and Treatment:

<td> Gr.</td><td> N</td><td> Agent</td><td> Formulation dose</td><td> Route</td><td> Schedule</td>

<td> 1^#</td><td> 10</td><td> Vehicle</td><td> -</td><td> ip</td><td> biwk x 2</td>

<td> 2</td><td> 7</td><td> ACPI 6</td><td> 17 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 3</td><td> 7</td><td> ACPI 6</td><td> 55 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 4</td><td> 7</td><td> ACPI 6</td><td> 70 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 5</td><td> 7</td><td> ACPI 6</td><td> 230 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 6</td><td> 7</td><td> ACPI 32</td><td> 9 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 7</td><td> 7</td><td> ACPI 32</td><td> 28 pg/animal</td><td> ip</td><td> biwk x 1</td>

<td> 8</td><td> 7</td><td> ACPI 32</td><td> 36 pg/animal</td><td> ip</td><td> biwk x 1</td>

<td> 9</td><td> 7</td><td> ACPI 32</td><td> 119 pg/animal</td><td> ip</td><td> biwk x 1</td>

<td> 10</td><td> 7</td><td> ACP21</td><td> 13 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 11</td><td> 7</td><td> ACP21</td><td> 42 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 12</td><td> 7</td><td> ACP21</td><td> 54 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 13</td><td> 7</td><td> ACP21</td><td> 177 pg/animal</td><td> ip</td><td> biwk x 2</td>

Procedures:

[346] Mice were anaesthetized with isoflurane for implant of cells to reduce the ulcerations. CR female C57BL/6 mice were set up with 5xl05 MC38 tumor cells in 0% Matrigel sc in flank. Cell Injection Volume was 0.1 mL/mouse. Mouse age at start date was 8 to 12 weeks.Pair matches were performed when tumors reach an average size of 100 - 150 mm3 and begin treatment.ACP16 was dosed at 17, 55, 70, or 230 pg/animal; ACP132 was dosed at 9,28, 36, or 119ug/animal; ACP21 was dosed at 13,42, 54, or 177pg/animal. Body weights were taken at initiation and then biweekly to the end. Caliper measurements were taken biweekly to the end. Any adverse reactions were to be reported immediately. Any individual animal with a single observation of > than 30% body weight loss or three consecutive measurements of >25% body weight loss was euthanized. Any group with a mean body weight loss of >20 % or >10% mortality stopped dosing; the group was not euthanized and

recovery is allowed. Within a group with >20% weight loss, individuals hitting the individual body weight loss endpoint were euthanized. If the group treatment related body weight loss is recovered to within 10% of the original weights, dosing resumed at a lower dose or less frequent dosing schedule. Exceptions to non-treatment body weight % recovery were allowed on a case-by-case basis. Endpoint was tumor growth delay (TGD). Animals were monitored individually. The endpoint of the experiment was a tumor volume of 1500 mm3 or 45 days, whichever comes first. Responders were followed longer. When the endpoint was reached, the animals are to be euthanized. Results are shown in FIG. 35.

Example 27e: MC38 rechallenge

[347] Cured mice (ACP16-treated) from Example 27b were rechallenged with tumor implantation to determine whether anti-tumor memory had been established from the initial treatments.

Agents and Treatment:

<td> Gr.</td><td> N</td><td colspan="2"> Agent</td><td> Formulation dose</td><td> Route</td><td> Schedule</td>

<td> 1^#</td><td> 33</td><td colspan="2"> No Treatment</td><td></td><td> -</td><td> -</td>

<td> 2</td><td> 7</td><td colspan="2"> ACP 16</td><td> 70 pg/animal</td><td> ip</td><td> (ACP16biwkx2)</td>

<td> 3</td><td> 8</td><td colspan="2"> ACP 16</td><td> 232 pg/animal</td><td> ip</td><td> (ACP16biwkx2)</td>

<td> 5</td><td> 5</td><td colspan="2"> IL-2-WTI</td><td> 12 pg/animal</td><td> ip</td><td> (IL-2-WTI bid x 5 then 2-day pause then bid x 5 then 2-day pause)</td>

<td> 6</td><td> 7</td><td colspan="2"> IL-2-WTI</td><td> 36 pg/animal</td><td> ip</td><td> (IL-2-WTI bid x 5 then 2-day pause then bid x 5 then 2-day pause)</td>

<td></td><td colspan="2"> - Control Group</td><td colspan="4"></td>

Procedures:

[348] Mice were anaesthetized with isoflurane for implant of cells to reduce the ulcerations. This portion of the study began on the day of implant (Day 1). Group 1 consisted of 33 CR female C57BL/6 mice set up with 5xl05 MC38 tumor cells in 0% Matrigel subcutaneously in the flank. Groups 2-6 consisted of 33 CR female C57BL/6 mice set up with 5xl05 MC38 tumor cells in 0% Matrigel sc in the left flank. The tumors from the previous MC38 experiment (Example 27b) were implanted in the right flank of each animal. Cell Injection Volume was 0.1 mL/mouse. Age of control

mice at initiation wasl4 to 17 weeks. These mice were age matched to mice from the previous MC38 experiment (Example 27b). No dosing of active agent occurred during rechallenge. Body Weights were take biweekly until end, as were caliper measurements. Any adverse reactions or death were reported immediately. Any individual animal with a single observation of > than 30% body weight loss or three consecutive measurements of >25% body weight loss was euthanized. Endpoint was tumor growth delay (TGD). Animals were monitored individually. The endpoint of the experiment was a tumor volume of 1000 mm3 or 45 days, whichever comes first. Responders were followed longer when possible. When the endpoint is reached, the animals were euthanized. Results are shown in FIG. 33.

Example 27f: Treatment with ACP10, ACP11

Agents and Treatment:

<td> Gr.</td><td> N</td><td> Agent</td><td> Formulation dose</td><td> Route</td><td> Schedule</td>

<td> 1^#</td><td> 12</td><td> Vehicle</td><td> -</td><td> ip</td><td> biwk x 2</td>

<td> 2</td><td> 8</td><td> ACP11</td><td> 175 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 3</td><td> 8</td><td> ACP11</td><td> 300 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 4</td><td> 8</td><td> ACP10</td><td> 5 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 5</td><td> 8</td><td> ACP10</td><td> 10 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 6</td><td> 8</td><td> ACP10</td><td> 43 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 7</td><td> 8</td><td> ACP10</td><td> 43 pg/animal</td><td> ip</td><td> qwkx2</td>

<td> 8</td><td> 8</td><td> ACP10</td><td> 172 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 9</td><td> 8</td><td> IL-12-HM-WTI</td><td> 5 pg/animal</td><td> ip</td><td> bid for 5 days first day 1 dose then 2-day pause then bid for 5 days first day 1 dose then 2-day pause</td>

<td> 10</td><td> 8</td><td> IL-12-HM-WTI</td><td> 20 pg/animal</td><td> ip</td><td> bid for 5 days first day 1 dose then 2-day pause then bid for 5 days first day 1 dose then 2-day pause</td>

Procedures:

[349] Mice were anaesthetized with isoflurane for implant of cells to reduce the ulcerations. CR female C57BL/6 mice were set up with 5xl05 MC38 tumor cells in 0% Matrigel sc in flank. Cell Injection Volume was 0.1 mL/mouse. Mouse age at start date was 8 to 12 weeks. Pair matches were performed when tumors reach an average size of 100 - 150 mm3 and begin treatment.ACPI 1 was dosed at 175 or 300 pg/animal; ACP10 was dosed at 5, 10,43, or 172 ug/animal; IL HM-WTI was dosed at 5 or 20 ug/animal. Body weights were taken at initiation and then biweekly to the end.

Caliper measurements were taken biweekly to the end. Any adverse reactions were to be reported immediately. Any individual animal with a single observation of > than 30% body weight loss or three consecutive measurements of >25% body weight loss was euthanized. Any group with a mean body weight loss of >20 % or >10% mortality stopped dosing; the group was not euthanized and recovery is allowed. Within a group with >20% weight loss, individuals hitting the individual body weight loss endpoint were euthanized. If the group treatment related body weight loss is recovered to within 10% of the original weights, dosing resumed at a lower dose or less frequent dosing schedule. Exceptions to non-treatment body weight % recovery were allowed on a case-by-case basis. Endpoint was tumor growth delay (TGD). Animals were monitored individually. The endpoint of the experiment was a tumor volume of 1500 mm3 or 45 days, whichever comes first. Responders were followed longer. When the endpoint was reached, the animals are to be euthanized. Results are shown in FIG. 45 and FIGs. 46A-46D.

Example 27g: Treatment with ACP16, APC153, ACP155, ACP156 and ACP292

Agents and Treatment:

<td> Gr.</td><td> N</td><td> Agent</td><td> Formulation dose</td><td> Route</td><td> Schedule</td>

<td> 1^#</td><td> 12</td><td> Vehicle</td><td> -</td><td> ip</td><td> biwk x 2</td>

<td> 2</td><td> 8</td><td> ACPI 6</td><td> 17 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 3</td><td> 8</td><td> ACPI 6</td><td> 55 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 4</td><td> 8</td><td> ACPI 6</td><td> 230 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 5</td><td> 8</td><td> ACPI 55</td><td> 55 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 6</td><td> 8</td><td> ACPI 55</td><td> 230 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 7</td><td> 8</td><td> ACPI 53</td><td> 55 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 8</td><td> 8</td><td> ACPI 53</td><td> 230 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 9</td><td> 8</td><td> ACPI 56</td><td> 55 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 10</td><td> 8</td><td> ACPI 56</td><td> 230 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 11</td><td> 8</td><td> ACP292</td><td> 45 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 12</td><td> 8</td><td> ACP292</td><td> 186 pg/animal</td><td> ip</td><td> biwk x 2</td>

Procedures:

[350] Mice were anaesthetized with isoflurane for implant of cells to reduce the ulcerations. CR female C57BL/6 mice were set up with 5xl05 MC38 tumor cells in 0% Matrigel sc in flank. Cell Injection Volume was 0.1 mL/mouse. Mouse age at start date was 8 to 12 weeks. Pair matches were performed when tumors reach an average size of 100 - 150 mm3 and begin treatment. ACPI6 was

dosed at 17, 55 or 230 pg/animal; ACP153, ACP155 and ACP156 were dosed at 55 or 230 pg/animal; ACP292 was dosed at 45 or 186 pg/animal. Body weights were taken at initiation and then biweekly to the end. Caliper measurements were taken biweekly to the end. Any adverse reactions were to be reported immediately. Any individual animal with a single observation of > than 30% body weight loss or three consecutive measurements of >25% body weight loss was euthanized. Any group with a mean body weight loss of >20 % or >10% mortality stopped dosing; the group was not euthanized and recovery is allowed. Within a group with >20% weight loss, individuals hitting the individual body weight loss endpoint were euthanized. If the group treatment related body weight loss is recovered to within 10% of the original weights, dosing resumed at a lower dose or less frequent dosing schedule. Exceptions to non-treatment body weight % recovery were allowed on a case-bycase basis. Endpoint was tumor growth delay (TGD). Animals were monitored individually. The endpoint of the experiment was a tumor volume of 1500 mm3 or 45 days, whichever comes first. Responders were followed longer. When the endpoint was reached, the animals are to be euthanized. Results are shown in FIGs. 49A-49I.

Example 27h: Treatment with ACP16, APC302 and ACP314

<td colspan="6"> Agents and Treatment:</td>

<td> Gr.</td><td> N</td><td> Agent</td><td> Formulation dose</td><td> Route</td><td> Schedule</td>

<td> 1^#</td><td> 12</td><td> Vehicle</td><td> -</td><td> ip</td><td> biwk x 2</td>

<td> 2</td><td> 9</td><td> ACPI 6</td><td> 55 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 3</td><td> 9</td><td> ACPI 6</td><td> 230 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 4</td><td> 9</td><td> ACP302</td><td> 33 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 5</td><td> 9</td><td> ACP302</td><td> 106 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 6</td><td> 9</td><td> ACP302</td><td> 442 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 7</td><td> 9</td><td> ACP302</td><td> 1,344 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 8</td><td> 9</td><td> ACP314</td><td> 21 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 9</td><td> 9</td><td> ACP314</td><td> 68 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 10</td><td> 9</td><td> ACP314</td><td> 283 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 11</td><td> 9</td><td> ACP314</td><td> 861 pg/animal</td><td> ip</td><td> biwk x 2</td>

Procedures:

[351] Mice were anaesthetized with isoflurane for implant of cells to reduce the ulcerations. CR female C57BL/6 mice were set up with 5xl05 MC38 tumor cells in 0% Matrigel sc in flank. Cell Injection Volume was 0.1 mL/mouse. Mouse age at start date was 8 to 12 weeks. Pair matches were performed when tumors reach an average size of 100 - 150 mm3 and begin treatment. ACPI6 was

dosed at 55 or 230 pg/animal; ACP302 was dosed at 33,106,442 or 1344 ug/animal; ACP314 was dosed at 21,68,283 or 861 pg/animal. Body weights were taken at initiation and then biweekly to the end. Caliper measurements were taken biweekly to the end. Any adverse reactions were to be reported immediately. Any individual animal with a single observation of > than 30% body weight loss or three consecutive measurements of >25% body weight loss was euthanized. Any group with a mean body weight loss of >20 % or >10% mortality stopped dosing; the group was not euthanized and recovery is allowed. Within a group with >20% weight loss, individuals hitting the individual body weight loss endpoint were euthanized. If the group treatment related body weight loss is recovered to within 10% of the original weights, dosing resumed at a lower dose or less frequent dosing schedule. Exceptions to non-treatment body weight % recovery were allowed on a case-by-case basis. Endpoint was tumor growth delay (TGD). Animals were monitored individually. The endpoint of the experiment was a tumor volume of 1500 mm3 or 45 days, whichever comes first. Responders were followed longer. When the endpoint was reached, the animals are to be euthanized. Results are shown in FIG. 50A-50B.

Example 27i: Treatment with ACP339

<td colspan="6"> Agents and Treatment:</td>

<td> Gr.</td><td> N</td><td> Agent</td><td> Formulation dose</td><td> Route</td><td> Schedule</td>

<td> 1^#</td><td> 12</td><td> Vehicle</td><td> -</td><td> ip</td><td> biwk x 2</td>

<td> 2</td><td> 9</td><td> ACP339</td><td> 55 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 3</td><td> 9</td><td> ACP339</td><td> 230 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 4</td><td> 9</td><td> ACP339</td><td> 700 pg/animal</td><td> ip</td><td> biwk x 2</td>

Procedures:

[352] Mice were anaesthetized with isoflurane for implant of cells to reduce the ulcerations. CR female C57BL/6 mice were set up with 5xl05 MC38 tumor cells in 0% Matrigel sc in flank. Cell Injection Volume was 0.1 mL/mouse. Mouse age at start date was 8 to 12 weeks. Pair matches were performed when tumors reach an average size of 100 - 150 mm3 and begin treatment. ACP339 was dosed at 55,230 or 700 pg/animal. Body weights were taken at initiation and then biweekly to the end. Caliper measurements were taken biweekly to the end. Any adverse reactions were to be reported immediately. Any individual animal with a single observation of > than 30% body weight loss or three consecutive measurements of >25% body weight loss was euthanized. Any group with a mean

PCTZUS2020Z060624

100 body weight loss of >20 % or >10% mortality stopped dosing; the group was not euthanized and recovery is allowed. Within a group with >20% weight loss, individuals hitting the individual body weight loss endpoint were euthanized. If the group treatment related body weight loss is recovered to within 10% of the original weights, dosing resumed at a lower dose or less frequent dosing schedule. Exceptions to non-treatment body weight % recovery were allowed on a case-by-case basis. Endpoint was tumor growth delay (TGD). Animals were monitored individually. The endpoint of the experiment was a tumor volume of 1500 mm3 or 45 days, whichever comes first. Responders were followed longer. When the endpoint was reached, the animals are to be euthanized. Results are shown in FIGs. 51 A-5IC.

Example 28: CT26 experiments

[353] The CT26 cell line, a rapidly growing colon adenocarcinoma cell line that expresses MMP9 in vitro, was used. Using this tumor model, the ability of fusion proteins to affect tumor growth was examined.

Example 28a: Treatment with ACP16 alone or in combination with anti-PDl antibody

Agents and Treatment:

<td> Gr.</td><td> N</td><td> Agent</td><td> Formulation dose</td><td> Route</td><td> Schedule</td>

<td> 1^#</td><td> 12</td><td> vehicle 1 // vehicle 2</td><td> naZZ na</td><td> ipZZ ip</td><td> days 1,4,8,11 ZZ days 3,6,10,13</td>

<td> 2</td><td> 10</td><td> vehicle 1 // ACP 16</td><td> naZZ 70 ggZanimal</td><td> ipZZ ip</td><td> days 1,4,8,11 ZZ days 3,6,10,13</td>

<td> 3</td><td> 10</td><td> vehicle 1 // ACP 16</td><td> naZZ 232 pgZanimal</td><td> ipZZ ip</td><td> days 1,4,8,11 ZZ days 3,6,10,13</td>

<td> 4</td><td> 10</td><td> vehicle 1 // ACP 16</td><td> naZZ 500 pgZanimal</td><td> ipZZ ip</td><td> days 1,4,8,11 ZZ days 3,6,10,13</td>

<td> 5</td><td> 10</td><td> anti-PD-1 RMP1-14II vehicle 2</td><td> 200 pgZanimal ZZ na</td><td> ipZZ ip</td><td> days 1,4,8,11 ZZ days 3,6,10,13</td>

<td> 6</td><td> 10</td><td> anti-PD-1 RMP1-14II ACP 16</td><td> 200 pgZanimal ZZ 70 ggZanimal</td><td> ipZZ ip</td><td> days 1,4,8,11 ZZ days 3,6,10,13</td>

<td> 7</td><td> 10</td><td> anti-PD-1 RMP1-14II ACP 16</td><td> 200 pgZanimal ZZ 232 ggZanimal</td><td> ipZZ ip</td><td> days 1,4,8,11 ZZ days 3,6,10,13</td>

<td> 8</td><td> 10</td><td> anti-PD-1 RMP1-14 H ACP 16</td><td> 200 pgZanimal ZZ 500 pgZanimal</td><td> ipZZ ip</td><td> days 1,4,8,11 ZZ days 3,6,10,13</td>

<td> 9</td><td> 10</td><td> vehicle 1II IL-2</td><td> naZZ 12 pgZanimal</td><td> ipZZ ip</td><td> days 1,4,8,11 ZZ bid x 5 first day 1 dose per week x 2</td>

<td> 10</td><td> 10</td><td> anti-PD-1 RMP1-14II IL-2</td><td> 200 pgZanimal ZZ 12 pgZanimal</td><td> ipZZ ip</td><td> days 1,4,8,11 ZZ bid x 5 first day 1 dose per week x 2</td>

Procedures:

[354] Mice were anaesthetized with isoflurane for implant of cells to reduce the ulcerations. CR female BALB/c mice were set up with 3xl05 CT26 tumor cells in 0% Matrigel sc in flank. Cell Injection Volume was 0.1 mL/mouse. Mouse age at start date was 8 to 12 weeks. Pair matches were performed when tumors reach an average size of 100 - 150 mm3 and begin treatment. ACPI6 was dosed at 70,230 or 500 pg/animal with or without anti-PD-1 antibody (RMP1-14) at 200 pg/animal. Body weights were taken at initiation and then biweekly to the end. Caliper measurements were taken biweekly to the end. Any adverse reactions were to be reported immediately. Any individual animal with a single observation of > than 30% body weight loss or three consecutive measurements of >25% body weight loss was euthanized. Any group with a mean body weight loss of >20 % or >10% mortality stopped dosing; the group was not euthanized and recovery is allowed. Within a group with >20% weight loss, individuals hitting the individual body weight loss endpoint were euthanized. If the group treatment related body weight loss is recovered to within 10% of the original weights, dosing resumed at a lower dose or less frequent dosing schedule. Exceptions to non-treatment body weight % recovery were allowed on a case-by-case basis. Endpoint was tumor growth delay (TGD). Animals were monitored individually. The endpoint of the experiment was a tumor volume of 1500 mm3 or 45 days, whichever comes first. Responders were followed longer. When the endpoint was reached, the animals are to be euthanized. Results are shown in FIGs. 47A-47D and FIGs. 48A-48B.

Example 29. Human Tblast Assay

[355] IL-2 T-Blast Assay. Pre-stimulated T cells (T-blasts) were used to assess the activity of inducible IL-2 fusion proteins. T-Blasts were induced from human PBMCs with a 3-day incubation with PHA. Tbiasts were then plated in suspension at a concentration of 50,000 or 75,000 cells/well in X-VIVO culture media (containing human serum albumin) and stimulated with a dilution series of recombinant IL-2 fusion proteins or human IL-2 for 72 hours at 37°C and 5% CO2. Activity of uncleaved and cleaved IL-2 fusion proteins was tested. Cleaved inducible IL-2 was generated by incubation with active MMP9. IL-2 activity was assessed measuring proliferation with CellTiter-Glo. Exemplary results are shown in FIG. 3A-3I.

[356] IL-12 T-Blast Assay. T-Blasts were induced from human PBMCs through PHA stimulation for 72 hours. T-blasts were then washed and frozen prior use. For the assay, T-Blasts were thaw and plated in suspension at 100,000 cells/well in culture media containing human albumin and stimulated with a dilution series of recombinant hIL12 or chimeric IL 12 (mouse p35/human p40) indukines or hIL12 indukines for 72 hours at 37°C and 5% CO2. Activity of uncleaved and cleaved IL12 fusion proteins was tested. Cleaved inducible hIL12 was generated by incubation with active MMP9

102 enzyme. IL12 activity was assessed by quantification of IFNy production in supernatants using a hlFNy Alpha-LISA kit. Exemplary results are shown in FIGs. 8A-8D.

Example 30. Luciferase Reporter Assay

[357] IL-2 luciferase reporter cells (Promega), purchased from the manufacturer in a “Thaw and Use” format, were plated according to the manufacturer’s directions and stimulated with a dilution series of recombinant hIL-2 or activatable hIL-2 for 6 hours at 370C and 5% CO2. Activity of uncleaved and cleaved activatable IL-2 was tested. Cleaved inducible IL-2 was generated by incubation with active MMP9. IL-2 activity was assessed by quantification of luciferase activity using Bio-Gio™ Reagent (Promega), which allows for the measurement of luciferase activity by luminescence readout. Results are shown in FIGS. 2A-2J.

[358] IL 12 luciferase reporter cells (Promega), purchased from the manufacturer in a “Thaw and Use” format, were plated according to the manufacturer’s directions and stimulated with a dilution series of recombinant hIL12 or activatable hIL12 for 6 hours at 37°C and 5% CO2. Activity of uncleaved and cleaved activatable IL12 was tested. Cleaved inducible IL12 was generated by incubation with active MMP9. IL12 activity was assessed by quantification of luciferase activity using Bio-Gio™ Reagent (Promega), which allows for the measurement of luciferase activity by luminescence readout. Results are shown in FIGs. 9A-9C.

Example 31. MC38 Experiments

[359] Agents and Treatment

<td> Group</td><td> N</td><td> Agent</td><td> Dose</td><td> Route</td><td> Schedule</td>

<td> 1</td><td> 12</td><td> vehicle</td><td> -</td><td> ip</td><td> biwk x 2</td>

<td> 2</td><td> 8</td><td> WW0417</td><td> 55 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 3</td><td> 8</td><td> WW0517</td><td> 55 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 4</td><td> 8</td><td> WW0517</td><td> 230 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 5</td><td> 8</td><td> WW0517</td><td> 700 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 6</td><td> 8</td><td> WWW0520/0523</td><td> 76 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 7</td><td> 8</td><td> WWW0520/0523</td><td> 315 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 8</td><td> 8</td><td> WWW0520/0523</td><td> 959 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 9</td><td> 8</td><td> WWW0548/0524</td><td> 88 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 10</td><td> 8</td><td> WWW0548/0524</td><td> 368 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 11</td><td> 8</td><td> WWW0548/0524</td><td> 1,120 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 12</td><td> 8</td><td> WWW0548/0556</td><td> 113 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 13</td><td> 8</td><td> WWW0548/0556</td><td> 474 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 14</td><td> 8</td><td> WWW0548/0556</td><td> 1,442 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 15</td><td> 8</td><td> WW0475</td><td> 68 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 16</td><td> 8</td><td> WW0475</td><td> 283 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 17</td><td> 8</td><td> WW0475</td><td> 861 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 10</td><td> 8</td><td> WW0619</td><td> 17 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 11</td><td> 8</td><td> WW0619</td><td> 35 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 12</td><td> 8</td><td> WW0619</td><td> 70 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 13</td><td> 8</td><td> WW0619</td><td> 700 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 14</td><td> 8</td><td> WW0621/0523</td><td> 24 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 15</td><td> 8</td><td> WW0621/0523</td><td> 48 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 16</td><td> 8</td><td> WW0621/0523</td><td> 96 pg/animal</td><td> ip</td><td> biwk x 2</td>

<td> 17</td><td> 8</td><td> WW0621/0523</td><td> 960 pg/animal</td><td> ip</td><td> biwk x 2</td>

Procedures:

[360] Mice were anaesthetized with isoflurane for implant of cells to reduce the ulcerations. 308 CR female C57BL/6 mice were set up with 5xl05 MC38 tumor cells in 0% Matrigel sc in flank. Cell Injection Volume was 0.1 mL/mouse. Mouse age at start date was 8 to 12 weeks. Pair matches were performed when tumors reach an average size of 100 - 150 mm3 and begin treatment. Body weights were taken at initiation and then biweekly to the end. Caliper measurements were taken biweekly to the end. Any adverse reactions were to be reported immediately. Any individual animal with a single observation of > than 30% body weight loss or three consecutive measurements of >25% body weight loss was euthanized. Any group with a mean body weight loss of >20 % or >10% mortality stopped dosing; the group was not euthanized, and recovery is allowed. Within a group with >20% weight loss, individuals hitting the individual body weight loss endpoint were euthanized. If the group treatment related body weight loss is recovered to within 10% of the original weights, dosing resumed at a lower dose or less frequent dosing schedule. Exceptions to non-treatment body weight % recovery were allowed on a case-by-case basis. Endpoint was tumor growth delay (TGD). Animals were monitored individually. The endpoint of the experiment was a tumor volume of 1500 mm3 or 45 days, whichever comes first. Responders were followed longer. When the endpoint was reached, the animals are to be euthanized. Results are shown in FIGs. 4-6.

[361] Sample fusion protein constructs are detailed in Table 3. In table 3, “L” is an abbreviation of “linker”, and “cleav. link.” is an abbreviation of “cleavable linker”. Other abbreviations “mIFNg” indicates mouse interferon gamma (IFNg); “hAlbumin” indicates human serum albumin (HSA); “mAlbumin” indicates mouse serum albumin.

Example 32. Human Interferon PBMC Assay

[362] Human PBMCs were isolated form blood obtained from healthy donors. After isolation, PBMCs were cryopreserved until the assay was performed. For the assay, PBMCs were thawed and plated in suspension at 100,000 cells/well in X-Vivo media supplemented with 1.5% of human serum albumin. 96 well round bottom plates were used for the assay. Cells were stimulated with a dilution series of recombinant human IFNa and activatable human IFNa for 48 hours at 37°C and 5% CO2. Activity of uncleaved and cleaved activatable IFNa was tested. Cleaved inducible IFNa was generated by incubation with active recombinant protease. PBMC supernatants were collected and amounts of CXCL-10 (IP-10) produced were quantified using AlphaLISA as a measure of response. Results are shown in FIGs. 38A-38C.

Table 3: CONSTRUCT PERMUTATION TABLE (6xHis disclosed as SEQ ID NO: 354)

<td> Construct Name</td><td> Construct Description</td>

<td> ACP01</td><td> (anti-HSA)-(cleav. link.)-mouse IFNg-(cleav. link.)-(anti-HSA)-6xHis</td>

<td> ACP02</td><td> (anti-HSA)-(cleav. link.)-mouse IFNg-(cleav. lmk.)-mouse IFNg-(cleav. link.)-(anti-HSA)6xHis</td>

<td> ACP03</td><td> (anti-HSA)-(cleav. link.)-mouse IFNg-mouse IFNg-(cleav. link.)-(anti-HSA)-6xHis</td>

<td> ACP50</td><td> (anti-EpCAM)-(anti-HSA)-(cleav. lmk.)-mouse IFNg-mouse IFNg-(cleav. lmk.)-(anti-HSA)6xHis</td>

<td> ACP51</td><td> (anti-EpCAM)-Linker-(anti-HSA)-(cleav. link.)-mIFNg-(cleav. link.)-(anti-HSA)-6xHis</td>

<td> ACP52</td><td> (anti-HSA)-(cleav. link.)-mIFNg-(cleav. lmk.)-(anti-HSA)-Lmker-(anti-EpCAM)-6xHis</td>

<td> ACP53</td><td> mAlbumin-(cleav. link.)-mIFNg-(cleav. lmk.)-mAlbumin-6xHis</td>

<td> ACP54</td><td> mAlbumin-(cleav. link.)-mIFNg-Lmker-mIFNg-(cleav. lmk.)-mAlbumm-6xHis</td>

<td> ACP30</td><td> (anti-HSA)-(cleav. link.)-mouse IFNg-(cleav. lmk.)-(anti-HSA)-(cleav. lmk.)-mouse IFNg(cleav. link.)-(anti-HSA)-6xHis</td>

<td> ACP55</td><td> (anti-HSA)-(cleav. link.)-mouse IFNg-(cleav. lmk.)-(anti-HSA)-(cleav. lmk.)-mouse IFNg(cleav. lmk.)-(anti-HSA)-6xHis-C-tag</td>

<td> ACP56</td><td> (anti-FOLRl )-Lmker-(anti-HSA)-(cleav. lmk.)-mIFNg-(cleav. link.)-(anti-HSA)-6xHis</td>

<td> ACP57</td><td> (anti-HSA)-(cleav. link.)-mIFNg-(cleav. lmk.)-(anti-HSA)-Lmker-(anti-FOLRl )-6xHis</td>

<td> ACP58</td><td> (anti-HSA)-(cleav. link.)-mIFNg-(cleav. lmk.)-mIFNg-(cleav. link.)-(anti-HSA)-Lmker-(antiEpCAM)-6xHis</td>

<td> ACP59</td><td> (anti-FOLRl )-Lmker-(anti-HSA)-(cleav. lmk.)-mIFNg-(cleav. lmk.)-mIFNg-(cleav. link.)(anti-HSA)-6xHis</td>

<td> ACP60</td><td> (anti-HSA)-(cleav. link.)-mIFNg-(cleav. lmk.)-mIFNg-(cleav. lmk.)-(anti-HSA)-Lmker-(antiFOLRI )-6xHis</td>

<td> ACP61</td><td> (anti-HSA)-(cleav. link.)-mIFNg-(cleav. lmk.)-mIFNg-(cleav. link.)-(anti-HSA)-LmkerFN(CGS-2)-6xHis</td>

<td> ACP63</td><td> anti-FN CGS-2 scFv (Vh/Vl)-6xHis</td>

<td> ACP69</td><td> (anti-HSA)-(cleav. link.)-mouse IFNg-(cleav. lmk.)-(anti-HSA)-(cleav. lmk.)-mouse IFNg</td>

<td> ACP70</td><td> mouse IFNg-(cleav. lmk.)-(anti-HSA)-(cleav. lmk.)-mouse IFNg-(cleav. link.)-(anti-HSA)</td>

<td> ACP71</td><td> mouse IFNg-(cleav. lmk.)-mAlbumm-(cleav. lmk.)-mouse IFNg-(cleav. lmk.)-mAlbumin</td>

<td> ACP72</td><td> mAlbumin-(cleav. lmk.)-mouse IFNg-(cleav. link.)-mAlbumin-(cleav. link.)-mouse IFNg</td>

<td> ACP73</td><td> mAlbumin-(cleav. lmk.)-mouse IFNg-(cleav. lmk.)-mAlbumin-(cleav. link.)-mouse IFNg(cleav. lmk.)-mAlbumin</td>

<td> ACP74</td><td> mAlbumin-(cleav. lmk.)-mouse IFNg-(cleav. lmk.)-5mer linker-mAlbumin-5mer linker-(cleav. link.)-mouse IFNg-(cleav. link.)-mAlbumin</td>

<td> ACP75</td><td> mAlbumin-(cleav. lmk.)-mouse IFNg-(cleav. lmk.)-10mer linker-mAlbumin-lOmer linker(cleav. link.)-mouse IFNg-(cleav. lmk.)-mAlbumin</td>

<td> ACP78</td><td> (anti-HSA)-Lmker-mouse_IFNg-Lmker-(anti-HSA)-Lmker-mouse_IFNg-Lmker-(antiHSA)_(non-cleavable_control)</td>

<td> ACP134</td><td> Anti-HSA-(cleav. lmk.)-mouse_IFNg-(cleav. lmk.)-anti-HSA-(cleav. lmk.)-mouse_IFNg(cleav. link.)-anti-HSA-L-anti-FOLRl</td>

<td> ACP135</td><td> Anti-FOLRl-L-HSA-(cleav. lmk.)-mouse_IFNg-(cleav. link.)-HSA-(cleav. lmk.)-mouse_IFNg(cleav. link.)-HSA</td>

<td> ACP04</td><td> human p40-murine p35-6xHis</td>

<td> ACP05</td><td> human p40-human p35-6xHis</td>

<td> ACP34</td><td> mouse p35-(cleav. lmk.)-mouse p40-6xHis</td>

<td> ACP35</td><td> mouse p35-GS-(cleav. lmk.)-GS-mouse p40-6xHis</td>

<td> ACP36</td><td> (anti-HSA)-(Cleav. Linker)-mouse p40-mouse p35-(Cleav. Linker)-(anti-HSA)-6xHis</td>

<td> ACP37</td><td> (anti-EpCAM)-(anti-HSA)-(Cleav. Linker)-mouse p40-mouse p35-(Cleav. Linker)-(anti-HSA)6xHis</td>

<td> ACP79</td><td> (anti-EpCAM)-Linker-(anti-HSA)-(cleav. link.)-mIL12-(cleav. lmk.)-(Anti-HSA)-6xHis</td>

<td> ACP80</td><td> (anti-HSA)-(cleav. link.)-mIL12-(cleav. link.)-(anti-HSA)-Linker-(anti-EpCAM)-6xHis</td>

<td> ACP06</td><td> Blocker 12-Linker-(cleav. link.)-human p40-Linker-mouse p35-(cleav. link.)-(anti-HSA)-6xHis</td>

<td> ACP07</td><td> Blocker 12-Linker-(cleav. link.)-human p40-Linker-mouse p35-(cleav. link.)-(anti-HSA)Linker-(anti-FOLRl )-6xHis</td>

<td> ACP08</td><td> (anti-FOLRl)-Lmker-Blockerl2-Linker-(cleav. link.)-human p40-Lmker-mouse p35-(cleav. link.)-(anti-HSA)-6xHis</td>

<td> ACP09</td><td> (anti-HSA)-Lmker-B10ckerl2-Lmker-(cleav. link.)-human p40-Linker-mouse p35-6xHis</td>

<td> ACP10</td><td> (anti-HSA)-(cleav. link.)-human p40-L-mouse p35-(cleav. lmk.)-Lmker-Blocker 12-6xHis</td>

<td> ACP11</td><td> Human_p40-Linker-mouse_p35-(cleav. lmk.)-Lmker-B10ckerl2-Lmker-(anti-HSA)-6xHis</td>

<td> ACP91</td><td> human_p40-Lmker-mouse_p35-Linker-Linker-Blocker-Linker-(anti-HSA)_(noncleavablecontrol)</td>

<td> ACP136</td><td> human p40-L-mouse p35-(cleav. link.)-B10cker</td>

<td> ACP138</td><td> human_p40-L-mouse_p35-(cleav. lmk.)-Blocker-L-(anti-HSA)-L-FOLRl</td>

<td> ACP139</td><td> Anti-FOLRl-L-human_p40-L-mouse_p35-(cleav. link.)-Blocker 12-L-(anti-HSA)</td>

<td> ACP140</td><td> Anti-FOLRl-(cleav. lmk.)-human_p40-L-mouse_p35-(cleav. link. )-B locker 12-L-(anti-HSA)</td>

<td> ACP12</td><td> (anti-EpCAM)-IL2-(cleav. link.)-(anti-HSA)-blocker2-6xHis</td>

<td> ACP13</td><td> (anti-EpCAM)-B10cker2-(anti-HSA)-(cleav. lmk.)-IL2-6xHis</td>

<td> ACP14 (WW0045)</td><td> B10cker2-Linker-(cleav. link.)-IL2- (cleav. link.)-(anti-HSA)-6xHis</td>

<td> ACP15 (WW0047)</td><td> B10cker2-Lmker-(anti-HSA)-Lmker-(cleav. link.)- IL2 -6xHis</td>

<td> ACP16 (WW0048)</td><td> IL2-(cleav. link.)-(anti-HSA)-Lmker-(cleav. lmk.)-B10cker2-6xHis</td>

<td> ACP17</td><td> (anti-EpCAM)-Lmker-IL2-(cleav. lmk.)-(anti-HSA)-Lmker-(cleav. lmk.)-B10cker2-6xHis</td>

<td> ACPI 8</td><td> (anti-EpCAM)-Lmker-IL2-(cleav. lmk.)-(anti-HSA)-Lmker-vh(cleav. link.)vl-6xHis</td>

<td> ACP19</td><td> IL2-(cleav. lmk.)-Lmker-B10cker2-Linker-(anti-HSA)-Lmker-(anti-EpCAM) -6xHis</td>

<td> ACP20 (WW0056)</td><td> IL2-(cleav. link.)-B10cker2-6xHis</td>

<td> ACP21 (WW0057)</td><td> IL2-(cleav. lmk.)-Lmker-B10cker2-6xHis</td>

<td> ACP22</td><td> IL2-(cleav. lmk.)-Lmker-blocker-(cleav. link.)-(anti-HSA)-Lmker-(anti-EpCAM)-6xHis</td>

<td> ACP23</td><td> (anti-FOLRl )-(cleav. link.)-B10cker2-Linker-(cleav. link.)-(anti-HSA)-(cleav. link.)- IL2-6xHis</td>

<td> ACP24 (WW0074)</td><td> (B10cker2)-(cleav. link.)-(IL2)-6xHis</td>

<td> ACP25 (WW0075)</td><td> B10cker2-Linker-(cleav. link.)-IL2-6xHis</td>

<td> ACP26</td><td> (anti-EpCAM)-Linker-IL2-(cleav. link.)-(anti-HSA)-Linker-blocker(NARA 1 Vh/Vl)</td>

<td> ACP27</td><td> (anti-EpCAM)-Linker-IL2-(cleav. link.)-(anti-HSA)-Linker-blocker(NARA 1 Vl/Vh)</td>

<td> ACP28</td><td> IL2-(cleav. Imk.)-Lmker-Blocker2-(NARA1 Vh/Vl)-Linker-(anti-HSA)-Linker-(anti-EpCAM)</td>

<td> ACP29</td><td> IL2-(cleav. Imk.)-Lmker-Blocker2-(NARA1 Vl/Vh)-Linker-(anti-HSA)-Linker-(anti-EpCAM)</td>

<td> ACP38</td><td> IL2-(cleav. lmk.)-blocker-(anti-HSA)-(anti-EpCAM)-6xHis</td>

<td> ACP39</td><td> (anti-EpCAM)-(cleav. link.)-(anti-HSA)-(cleav. lmk.)-B10cker2-(cleav. lmk.)-IL-2-6xHis</td>

<td> ACP40 (WW0076)</td><td> CD25ecd-Lmker-(cleav. link.)-IL2-6xHis</td>

<td> ACP41 (WW0077)</td><td> IL2-(cleav. lmk.)-Lmker-CD25ecd-6xHis</td>

<td> ACP42</td><td> (anti-HSA)-Lmker-CD25 ecd-Linker-(cleav. link.)-IL2-6xHis</td>

<td> (WW0078)</td><td></td>

<td> ACP43 (WW0079)</td><td> IL2-(cleav. lmk.)-Lmker-CD25ecd-Lmker-(anti-HSA)-6xHis</td>

<td> ACP44 (WW0080)</td><td> IL2-(cleav. lmk.)-Lmker-CD25ecd-(cleav. lmk.)-(anti-HSA)-6xHis</td>

<td> ACP45 (WW0046)</td><td> (anti-HSA)-(cleav. lmk.)-B10cker2-Lmker-(cleav. lmk.)-IL2-6xHis</td>

<td> ACP46</td><td> IL2-(cleav. lmk.)-lmkerL-vh(cleav. link.)vl-Linker-(anti-HSA)-L-(anti-EpCAM)-6xHis</td>

<td> ACP47</td><td> (anti-EpCAM)-Lmker-IL2-(Cleavable Linker)-(anti-HSA)-Lmker-B10cker2-6xHis</td>

<td> ACP48 (WW0054)</td><td> IL2-(cleav. link.)-B10cker2-Linker-(anti-HSA)-6xHis</td>

<td> ACP49 (WW0055)</td><td> IL2-(cleav. link.)-Lmker-B10cker2-Linker-(anti-HSA)-6xHis</td>

<td> ACP92</td><td> (anti-HSA)-(16mer Cleav. Link.)-IL2-(16mer Cleav. Lmk.)-(anti-HSA)-6XHis</td>

<td> ACP93</td><td> (anti-EpCAM)-(anti-HSA)-(anti-EpCAM)-B10cker2-(cleav. link.)-IL2-6xHis</td>

<td> ACP94</td><td> (anti-EpCAM)-(anti-HSA)-B10cker2-(cleav. lmk.)-IL2-6xHis</td>

<td> ACP95</td><td> (anti-EpCAM)-(anti-HSA)-(cleav. lmk.)-IL2-6xHis</td>

<td> ACP96</td><td> (anti-EpCAM)-(16mer cleav. lmk.)-IL2-(16mer cleav. link.)-(anti-HSA)</td>

<td> ACP97</td><td> (anti-EpCAM)-(anti-HSA)-(cleav. lmk.)-IL2-(cleav. lmk.)-(anti-HSA)-6xHis</td>

<td> ACP99</td><td> (anti-EpCAM)-Lmker-IL2-(cleav. link.)-(anti-HSA)-6xHis</td>

<td> ACP100</td><td> (anti-EpCAM)-Linker-IL2-6xHis</td>

<td> ACP101 (WW0061)</td><td> IL2-(cleav. lmk.)-(anti-HSA)-6xHis</td>

<td> ACP102</td><td> (anti-EpCAM)-(cleav. link.)-IL2-(cleav. link.)-(anti-HSA)-Lmker-blocker-6xHis</td>

<td> ACP103</td><td> IL2-(cleav. lmk.)-Lmker-Blocker2-Linker-(anti-HSA)-Linker-(antiI-FOLRl)-6xHis</td>

<td> ACP104</td><td> (anti-FOLRl )-IL2-(cleav. link.)-(anti-HSA)-Linker-B10cker2-6xHis</td>

<td> ACP105</td><td> B10cker2-Lmker-(cleav. link.)-IL2-(cleav. lmk.)-(anti-HSA)-Lmker-(anti-FOLRl )-6xHis</td>

<td> ACP106</td><td> (anti-FOLRl )-Lmker-(anti-HSA)-(cleav. link.)-blocker-Lmker-(cleav. lmk.)-IL2 -6xHis</td>

<td> ACP107</td><td> B10cker2-Lmker-(anti-HSA)-(cleav. link.)-IL2-Linker-(anti-FOLRl)-6xHis</td>

<td> ACP108</td><td> (anti-EpCAM)-IL2-(Dually cleav. link.)-(anti-HSA)-Linker-blocker-6xHis</td>

<td> ACPI 17</td><td> anti-FN CGS-2 scFv (Vh/Vl)-6xHis</td>

<td> ACPI 18</td><td> NARA1 Vh/Vl non-cleavable</td>

<td> ACPI 19</td><td> NARA1 Vh/Vl cleavable</td>

<td> ACP120</td><td> NARA1 Vl/Vh non-cleavable</td>

<td> ACP121</td><td> NARA1 Vl/Vh cleavable</td>

<td> ACP124 (WW0159)</td><td> IL2-Linker-(anti-HSA)-Lmker-Linker-blocker_(non-cleavable_control)</td>

<td> ACP132</td><td> IL2-L-HSA</td>

<td> (WW0177)</td><td></td>

<td> ACP141 (WW0178)</td><td> IL2-L-human_Albumin</td>

<td> ACP142 (WW0179)</td><td> IL2-(cleav. lmk.)-human_Albumin</td>

<td> ACP144</td><td> IL2-(cleav. lmk.)-HSA-(cleav.-lmk.)blocker-L-(anti-FOLRl)</td>

<td> ACP145</td><td> Anti-FOLRl-L-IL2-(cleav. link.)-HSA-Lmker-(cleav. Ii11k.)-blocker2</td>

<td> ACP146</td><td> Anti-FOLRl-(cleav. lmk)-IL2-(cleav. lmk.)-HSA-Lmker-(cleav. Iink.)-blocker2</td>

<td> ACP133 (WW0196)</td><td> IL2-6x His</td>

<td> ACP147</td><td> IL2-(cleav. Li11ker)-(anti-HSA)-Linker-(cleav. link.)-blocker2-L-(anti-EpCAM)</td>

<td> ACP148</td><td> (anti-EpCAM)-L-IL2-(cleav. link.)-(anti-HSA)-L-(cleav. Lmker)-blocker2</td>

<td> ACP149</td><td> (anti-EpCAM)-(cleav. lmk.)-IL2-(cleav. Lmker)-(anti-HSA)-L-(cleav. Lmker)-blocker2</td>

<td> ACP31</td><td> (anti-HSA)-(cleav. link.)-mIFNal-(cleav. link.)-(anti-HSA)</td>

<td> ACP32</td><td> (anti-HSA)-(cleav. link.)-mIFNal(N+C trunc)-(cleav. lmk.)-(anti-HSA)</td>

<td> ACP33</td><td> (anti-HSA)-(cleav. link.)-mIFNal(C trunc)-(cleav. link.)-(anti-HSA)</td>

<td> ACP131</td><td> mIFNal</td>

<td> ACP125</td><td> Anti-HSA-(cleav. lmk.)-mIFNal</td>

<td> ACP126</td><td> mIFNal-(cleav. lmk.)-(anti-HSA)</td>

<td> ACP127</td><td> Mouse_Albumin-(cleav. Link.)-mIFNal-(cleav lmk)-mouse_Albumm</td>

<td> ACP128</td><td> Mouse_Albumin-(cleav. link.)-mIFNal</td>

<td> ACP129</td><td> mIFNal-(cleav. lmk.)-mAlb</td>

<td> ACP150</td><td> (Anti-FOLRl )-L-(anti-HS A)-(cleav. Lmk.)-mIFNal -(cleav. Lmk.)-(anti-HS A)</td>

<td> ACP151</td><td> Anti-FOLRl -L-(anti-HSA)-(cleav. Lmk.)-mIFNal -(cleav. Lmk.)-(anti-HSA)-L-(anti-FOLRl)</td>

<td> ACP152</td><td> (anti-HSA)-L-mIFNal-L-(anti-HSA)_(non-cleavable_control)</td>

<td> ACP153 (WW0201)</td><td> IL2-(cleav. lmk.)-(anti-HSA)-lmker(cleav. Ii11k.)-blocker2</td>

<td> ACP154 (WW0202)</td><td> IL2-(cleav. lmk.)-(anti-HSA)-lmker(cleav. Ii11k.)-blocker2</td>

<td> ACP155 (WW0203)</td><td> IL2-(cleav. lmk.)-(anti-HSA)-lmker(cleav. Ii11k.)-blocker2</td>

<td> ACP156 (WW0204)</td><td> IL2-X-anti-HSA-LX-blocker_(X=Linker4_Blocker=Vh-Vl)</td>

<td> ACP157 (WW0205)</td><td> IL2-X-anti-HSA-LX-blocker_(X=Linker5_Blocker=Vh-Vl)</td>

<td> ACP200</td><td> m Alb(D3)-X-mouse-IFNa-X-m Alb(D3)(X=Linker 1)</td>

<td> ACP201</td><td> mAlb(Dl-L-D3)-X-mouse-IFNa-X-mAlb(Dl-L-D3)(X=Linker 1)</td>

<td> ACP202</td><td> HSA-X-mIFNal -X-HS A_(X=Linker 1+17aa)</td>

<td> ACP203</td><td> HSA-X-mIFNal-X-HSA _(X= Linker 2)</td>

<td> ACP204</td><td> HSA-X-mIFNal-X-HSA _(X=Linker 3)</td>

<td> ACP205</td><td> HSA-X-mIFNal-X-HSA _(X=Linker 4)</td>

<td> ACP206</td><td> HSA-X-Human_IFNA2b-X-HSA _(X= Linker 2)</td>

<td> ACP207</td><td> HSA-X-Human_IFNA2b-X-HSA _(X=Linker 3)</td>

<td> ACP208</td><td> HSA-X-Human_IFNA2b-X-HSA _(X=Linker 4)</td>

<td> ACP211</td><td> HSA-X-mouse-IFNg-X-IFNa-X-mouse-IFNg-X-HSA_(X=Linker 1)</td>

<td> ACP213</td><td> m Alb(D3)-X-mouse-IFNg-X-m Alb(D3)-X-mouse-IFNg-X-m Alb(D3)(X=Linker 1)</td>

<td> ACP214</td><td> mAlb(Dl-L-D3)-X-mouse-IFNg-X-mAlb(Dl-L-D3)-X-mouse-IFNg-X-mAlb(Dl-L- D3) (X=Linker 1)</td>

<td> ACP215</td><td> HSA-X-mouse-IFNg-X-HSA-X-mouse-IFNg-X-HSA_(X=Linker l+17aa)</td>

<td> ACP240</td><td> HSA-L-human_p40-L-mouse_p35-LL-Blocker_(non-cleavable;Blocker=Vl/Vh)</td>

<td> ACP241</td><td> mAlb-X-human_p40-L-mouse_p35-XL-Blocker_(X=Linker 1 ;B10cker=Vl/Vh)</td>

<td> ACP242</td><td> human_p40-L-mouse_p35-XL-Blocker-X-mAlb_(X=Linker 1 ;B10cker=Vl/Vh)</td>

<td> ACP243</td><td> mIgGl_Fc-X-human_p40-L-mouse_p35-XL-Blocker_(X=Linker l;B10cker= Vl/Vh)</td>

<td> ACP244</td><td> human_p40-L-mouse_p35-XL-Blocker-X-mIgGl_Fc_(X=Linker l;B10cker= Vl/Vh)</td>

<td> ACP245</td><td> HSA-X-human_p40-L-mouse_p35-XL-Blocker(cleavable)_(X=Linker 1 ;B10cker= Vl-X-Vh)</td>

<td> ACP247</td><td> HSA-X-human_p40-L-mouse_p35-XL-Blocker_(Blocker=3CYT5;X=Linker 1)</td>

<td> ACP284</td><td> HSA-X-mouse_p35-XL-Blocker_(Blocker=Vl/Vh;X=Linker 1)</td>

<td> ACP285</td><td> HSA-X-human_p40_C199S-L-mouse_p35_C92S-XL-Blocker_(Blocker=_Vl/Vh;X=Linker 1)</td>

<td> ACP286</td><td> HSA-X-human p40-L(4xG4S (SEQ ID NO: 453))-mouse p35-XL-B10cker_(B10cker= Vl/Vh;X=Linker 1)</td>

<td> ACP287</td><td> HSA-X-human_p40_mouse_p35-XL-Blocker_(Blocker=Vl/Vh_VH44- VL100 disulfide;X=Linker 1)</td>

<td> ACP288</td><td> HS A-X-human_p40_mouse_p3 5 -XL-B10cker(B10cker=Vl/VhVH 105- VL43 disulfide;X=Linker 1)</td>

<td> ACP289 (WW0233)</td><td> Geneart_WW0048_IL2-X-HSA-LX-blocker_Fusion_protem-6xHis</td>

<td> ACP290 (WW0234)</td><td> IL2-X-HS A-LX-blocker(X=Linker 1 ;Blocker=3TOW69)</td>

<td> ACP291 (WW0235)</td><td> IL2-X-HS A-LX-blocker(X=Linker 1 ;Blocker=3TOW85)</td>

<td> ACP292 (WW0236)</td><td> IL2-X-HSA-LX-blocker (X=Linker l;Blocker=2TOW91)</td>

<td> ACP296 (WW0250)</td><td> IL2-X-HS A-LX-blocker(cleavable)(X=Linker 1 ;B10cker=Vh-X-Vl)</td>

<td> ACP297 (WW0251)</td><td> IL2-X-HS A-LX-blocker(A46L)(X=Linker 1 ;B10cker=Vh/Vl)</td>

<td> ACP298 (WW0252)</td><td> IL2-X-HSA-LX-blocker(A46G)(X=Linker 1 ;Blocked Vh/Vl)</td>

<td> ACP299</td><td> IL2(Cysl 45Ser)-X-HSA-LX-blocker(X=Linker 1 ;Blocked Vh/Vl)</td>

<td> (WW0253)</td><td></td>

<td> ACP300 (WW0255)</td><td> IL2-X-hAlb-LX-blocker_(X=Linker 1 ;Blocked Vh/Vl)</td>

<td> ACP302 (WW0296)</td><td> IL2-X-mAlb-LX-blocker_(X=Linker 1 ;B10cker=Vh/Vl)</td>

<td> ACP303</td><td> mAlb-X-IL2(Nterm-41)-X-mALB(X=Linker 1)</td>

<td> ACP304 (WW0302)</td><td> IL2-X-HSA-LX-blocker-XL-CD25ecd_(X=Linker 1 ;Blocked Vh/Vl)</td>

<td> ACP305 (WW0303)</td><td> CD25ecd-LX-IL2-X-HSA-LX-blocker_(X=Linker 1 ;Blocked Vh/Vl)</td>

<td> ACP306 (WW0304)</td><td> IL2-XL-CD25ecd-X-HSA-LX-blocker_(X=Linker 1 ;Blocked Vh/Vl)</td>

<td> ACP309 (WW0307)</td><td> IL2-X-HSA-LX-blocker(A46S)_(X=Linker 1 ;Blocked Vh/Vl)</td>

<td> ACP310 (WW0308)</td><td> IL2-X-HS A-LX-blocker(QAPRLFR2)(X=Linker 1 ;B10cker=Vh/Vl)</td>

<td> ACP311 (WW0316)</td><td> IL2-X-IgG4_Fc(S228P)-LX-B10cker_(X=Linker 1 ;Blocked Vh/Vl)</td>

<td> ACP312 (WW0317)</td><td> IgG4Fc(S228P)-X-IL2-LX-B10cker(X=Linker 1 ;Blocked Vh/Vl)</td>

<td> ACP313 (WW0318)</td><td> IL2-XL-B10cker-X-IgG4_Fc(S228P)_(X=Linker 1 ;Blocked Vh/Vl)</td>

<td> ACP314 (WW0354)</td><td> mIgGlFc-X-IL2-LX-B10cker(X=Linker 1 ;B10cker=Vh/Vl)</td>

<td> ACP336 (WW0414)</td><td> IL2-X-anti-HSA-LX-blocker(Blocker=VHVL.F2.high.A02Vh-X-VlA46S;X= Linker 2)</td>

<td> ACP337 (WW0415)</td><td> IL2-X-anti-HSA-LX-blocker_(Blocker=VHVL.F2.high.A02_Vh/Vl_A46S;X= Linker 2)</td>

<td> ACP338 (WW0416)</td><td> IL2-X-anti-HSA-LX-blocker(Blocker=VHVL.F2.high.F03Vh-X-Vl;X= Linker 2)</td>

<td> ACP339 (WW0417)</td><td> IL2-X-anti-HSA-LX-blocker(Blocker=VHVL.F2.high.F03Vh/Vl;X= Linker 2)</td>

<td> ACP340 (WW0418)</td><td> IL2-X-anti-HSA-LX-blocker(Blocker=Hu2TOW91B;X= Linker 2)</td>

<td> ACP341 (WW0419)</td><td> IL2-X-anti-HSA-LX-blocker(Blocker=Hu3TOW85A;X= Linker 2)</td>

<td> ACP342 (WW0420)</td><td> CD25ecdC213S-LX-IL2-X-anti-HSA-LX-blocker(Blocker=VHVL.F2.high.A02Vh-X- V1_A46S;X= Linker 2)</td>

<td> ACP343 (WW0421)</td><td> CD25ecd_C213S-LX-IL2-X-anti-HSA-LX- blocker_(Blocker=VHVL.F2.high.A02_Vh/Vl_A46S;X= Linker 2)</td>

<td> ACP344 (WW0422)</td><td> CD25ecdC213S-LX-IL2-X-anti-HSA-LX-blocker(Blocker=VHVL.F2.high.F03Vh-X- V1;X= Linker 2)</td>

<td> ACP345 (WW0423)</td><td> CD25ecdC213S-LX-IL2-X-anti-HSA-LX-blocker(Blocker=VHVL.F2.high.F03Vh/Vl;X= Linker 2)</td>

<td> ACP346 (WW0424)</td><td> CD25ecdC213S-LX-IL2-X-anti-HSA-LX-blocker(Blocker=Hu2TOW91B;X= Linker 2)</td>

<td> ACP347 (WW0425)</td><td> CD25ecdC213S-LX-IL2-X-anti-HSA-LX-blocker(Blocker=Hu3TOW85A;X= Linker 2)</td>

<td> ACP348 (WW0426)</td><td> IgG4Fc(S228P)-X-IL2-LX-Blocker(Blocker=VHVL.F2.high.A02Vh-X-VlA46S;X= Linker 2)</td>

<td> ACP349 (WW0427)</td><td> IgG4 Fc(S228P)-X-IL2-LX-B10cker (Blocker=VHVL.F2.high.A02 VhWl A46S;X= Linker 2)</td>

<td> ACP350 (WW0428)</td><td> IgG4Fc(S228P)-X-IL2-LX-Blocker(Blocker=VHVL.F2.high.F03Vh-X-Vl;X= Linker 2)</td>

<td> ACP351 (WW0429)</td><td> IgG4Fc(S228P)-X-IL2-LX-Blocker(Blocker=VHVL.F2.high.F03Vh\Vl;X= Linker 2)</td>

<td> ACP352 (WW0430)</td><td> IgG4Fc(S228P)-X-IL2-LX-Blocker(Blocker=Hu2TOW91B;X= Linker 2)</td>

<td> ACP353 (WW0431)</td><td> IgG4Fc(S228P)-X-IL2-LX-Blocker(Blocker=Hu3TOW85A;X= Linker 2)</td>

<td> ACP354 (WW0432)</td><td> IgG4Fc(S228P)-X-CD25ecdC213S-LX-IL2-LX-Blocker(Blocker=VHVL.F2.high.A02Vh- X-V1_A46S;X= Linker 2)</td>

<td> ACP355 (WW0433)</td><td> IgG4_Fc(S228P)-X-CD25ecd_C213S-LX-IL2-LX- Blocker_(Blocker=VHVL.F2.high.A02_Vh\Vl_A46S;X= Linker 2)</td>

<td> ACP356 (WW0434)</td><td> IgG4Fc(S228P)-X-CD25ecdC213S-LX-IL2-LX-Blocker(Blocker=VHVL.F2.high.F03Vh- X-V1;X= Linker 2)</td>

<td> ACP357 (WW0435)</td><td> IgG4_Fc(S228P)-X-CD25ecd_C213S-LX-IL2-LX- Blocker(Blocker=VHVL.F2.high.F03Vh\Vl;X= Linker 2)</td>

<td> ACP358 (WW0436)</td><td> IgG4Fc(S228P)-X-CD25ecdC213S-LX-IL2-LX-Blocker(Blocker=Hu2TOW91B;X= Linker 2)</td>

<td> ACP359 (WW0437)</td><td> IgG4Fc(S228P)-X-CD25ecdC213S-LX-IL2-LX-Blocker(Blocker=Hu3TOW85A;X= Linker 2)</td>

<td> ACP371 (WW0513)</td><td> IL2-X-anti-HSA-LX-blocker(Blocker= Vh/V1VH44-VL1 OO_disulfide;X= Linker 2)</td>

<td> ACP372 (WW0514)</td><td> IL2-X-anti-HSA-LX-blocker(Blocker= Vh/V1_VH105-VL43_disulfide;X=Linker 2)</td>

<td> ACP373 (WW0515)</td><td> IL2-X-anti-HSA-LX-blocker(Blocker=VHVL.F2.high.A02Vh/VlVH44- VL100_disulfide;X= Linker 2)</td>

<td> ACP374 (WW0516)</td><td> IL2-X-anti-HS A-LX-blocker(Blocker=VHVL.F2.high. A02Vh/VlVH 105- VL43_disulfide;X= Linker 2)</td>

<td> ACP375 (WW0517)</td><td> IL2-X-anti-HSA-LX-blocker(Blocker=VHVL.F2.high.F03Vh/VlVH44- VL100_disulfide;X= Linker 2)</td>

<td> ACP376 (WW0521)</td><td> IL2-X-anti-HSA-LX-blocker(Blocker=VHVL.F2.high.F03Vh/VlVH105-VL43disulfideX= Linker 2)</td>

<td> ACP377 (WW0519)</td><td> IL2-X-anti-HSA-LX-blocker(Blocker=Hu2TOW91A;X= Linker 2)</td>

<td> ACP378 (WW0520)</td><td> IL2-X-anti-HS A-LX-HeavyblockerFab(Blocker=VH-CHl ;X=Linker 2)</td>

<td> ACP379 (WW0521)</td><td> IgG4Fc(S228P)-X-IL2-LX-HeavyblockerFab(Blocke1=VH-CHl ;X= Linker 2)</td>

<td> ACP383 (WW0525)</td><td> IgG4Fc(S228P)-X-IL2-LX-blocker(Blocker=Vh/VlVH44-VL100disulfide;X=LINKER2)</td>

<td> ACP38 (WW05264)</td><td> IgG4Fc(S228P)-X-IL2-LX-blocker(Blocker=Vh/VlVH105-VL43disulfide;X=MMP14-l)</td>

<td> ACP385 (WW0527)</td><td> IgG4Fc(S228P)-X-IL2-LX-blocker(Blocker=VHVL.F2.high.A02Vh/VlVH44- VL100_disulfide;X=LINKER 2)</td>

<td> ACP386 (WW0528)</td><td> IgG4Fc(S228P)-X-IL2-LX-blocker(Blocker=VHVL.F2.high.A02Vh/VlVH105- VL43_disulfide;X=Linker 2)</td>

<td> ACP387 (WW0529)</td><td> IgG4Fc(S228P)-X-IL2-LX-blocker(Blocker=VHVL.F2.high.F03Vh/VlVH44- VL 1 OOdi sulfide;X=Linker 2)</td>

<td> ACP388 (WW0530)</td><td> IgG4Fc(S228P)-X-IL2-LX-blocker(Blocker=VHVL.F2.high.F03Vh/VlVH105- VL43_disulfide;X=Linker 2)</td>

<td> ACP389 (WW0531)</td><td> IgG4Fc(S228P)-X-IL2-LX-blocker(Blocker=Hu2TOW9 l_A;X=Linker 2)</td>

<td> ACP390 (WW0532)</td><td> IL2-X-anti-HSA-LX-blocker(Blocker=VHVL.F2.high.A02Vh/VlA46SVH44- VL 1 OOdi sulfide;X=Linker 2)</td>

<td> ACP391 (WW0533)</td><td> IgG4Fc(S228P)-X-IL2-LX-blocker(Blocker=VHVL.F2.high.A02Vh/VlA46SVH44- VL 1 OOdi sulfide;X=Linker 2)</td>

<td> ACP392 (WW0534)</td><td> IL2-XL-CD25ecd_C213S-X-HSA-LX- blocker(Blocker=VHVL.F2.high. A02VhG44CVlA46SGl 00C;X=Linker 2)</td>

<td> ACP393 (WW0535)</td><td> IL2-XL-CD25ecd_C213S-X-HSA-LX- blocker_(Blocker=VHVL.F2.high.A02_Vh_Q105C_Vl_A43C;X=Linker 2)</td>

<td> ACP394 (WW0536)</td><td> IL2-XL-CD25ecd_C213S-X-HSA-LX- blocker(Blocker=VHVL.F2.high.F03VhG44CVlGl 00C;X=Linker 2)</td>

<td> ACP395 (WW0537)</td><td> IL2-XL-CD25ecd_C213S-X-HSA-LX- blocker(Blocker=VHVL.F2.high.F03VhQ105CVlA43C;X=Linker2)</td>

<td> ACP396 (WW0538)</td><td> IL2-XL-CD25ecdC213S-X-HSA-LX-blocker(Blocker=Hu2TOW91A;X=Linker2)</td>

<td> ACP397 (WW0539)</td><td> IL2-XL-CD25ecdC213S-X-HSA-LX-blocker(Blocker=Hu2TOW91B;X=Linker2)</td>

<td> ACP398 (WW0540)</td><td> IL2-XL-CD25ecdC213S-X-HSA-LX-HeavyblockerFab(Blocker=VH-CHl;X=Linker2)</td>

<td> ACP399</td><td> B10cker-XL-HSA-X-IL2(Nterm-41)-X- HSA (Blocker=VHVL.F2.high.A02 Vh G44C Vl A46S G100C;X=Linker 2)</td>

<td> ACP400</td><td> B10cker-XL-HSA-X-IL2(Nterm-41)-X- HSA (Blocker=VHVL.F2.high.A02 Vh Q105C Vl A43C;X=Linker 2)</td>

<td> ACP401</td><td> B10cker-XL-HSA-X-IL2(Nterm-41)-X- HSA (Blocker=VHVL.F2.high.F03 Vh G44C Vl G100C;X=Linker 2)</td>

<td> ACP402</td><td> B10cker-XL-HSA-X-IL2(Nterm-41)-X- HSA (Blocker=VHVL.F2.high.F03 Vh Q105C Vl A43C;X=Linker 2)</td>

<td> ACP403</td><td> Blocker-XL-HSA-X-IL2(Nterm-41)-X-HSA(Blocker=Hu2TOW91A;X=Linker2)</td>

<td> ACP404</td><td> Blocker-XL-HSA-X-IL2(Nterm-41)-X-HSA(Blocker=Hu2TOW91B;X=Linker2)</td>

<td> ACP405</td><td> HeavyB10ckerFab-XL-HSA-X-IL2(Nterm-41)-X-HSA(B10cker=VH-CHl;X=Linker2)</td>

<td> ACP406 (WW0548)</td><td> mIgGlFc(S228P)-X-IL2-LX-HeavyblockerFab(Blocker=VH-CHl;X=Linker2)</td>

<td> ACP407 (WW0549)</td><td> mIgGlFc(S228P)-X-IL2-LX-blocker(Blocker=VHVL.F2.high.A02Vh/VlVH44- VL 1 OOdi sulfide;X=Linker 2)</td>

<td> ACP408 (WW0550)</td><td> mIgGlFc(S228P)-X-IL2-LX-blocker(Blocker=VHVL.F2.high.A02Vh/VlA46SVH44VL 1 OOdi sulfide;X=Linker 2)</td>

<td> ACP409 (WW0551)</td><td> mIgGlFc(S228P)-X-IL2-LX-blocker(Blocker=VHVL.F2.high.A02Vh/VlVH105- VL43_disulfidel;X=Linker 2)</td>

<td> ACP410 (WW0552)</td><td> mIgGlFc(S228P)-X-IL2-LX-blocker(Blocker=VHVL.F2.high.F03Vh/VlVH44- VL100_disulfidel;X=Linker 2)</td>

<td> ACP411 (WW0553)</td><td> mIgGlFc(S228P)-X-IL2-LX-blocker(Blocker=VHVL.F2.high.F03Vh/VlVH105- VL43_disulfidel;X=Linker 2)</td>

<td> ACP412 (WW0554)</td><td> mIgGlFc(S228P)-X-IL2-LX-blocker(Blocker=Hu2TOW9 lA;X=Linker 2)</td>

<td> ACP413 (WW0555)</td><td> CD25 213S-L-KappablockerFab(Blocker=VHVL.F2.high.A02A46SKappa)</td>

<td> ACP414 (WW0556)</td><td> CD25 213S-L-KappablockerFab(Blocker=VHVL.F2.high.F03Kappa)</td>

<td> ACP415 (WW0557)</td><td> IL2-XL-blocker-L-CD25_213S-X- HS AB10cker=VHVL.F2.high. A02VHG44CV1A46SG100C;X=Linker 2)</td>

<td> ACP416 (WW0558)</td><td> IL2-XL-blocker-L-CD25_213S-X- HS A(B10cker=VHVL.F2.high. A02VhQl 05C_Vl_A43C;X=Linker 2)</td>

<td> ACP417 (WW0559)</td><td> IL2-XL-blocker-L-CD25_213S-X- HS A(Blocker=VHVL.F2.high.F03VhG44CVlGl OOC;X=Linker 2)</td>

<td> ACP418 (WW0560)</td><td> IL2-XL-blocker-L-CD25_213S-X- HSA(Blocker=VHVL.F2.high.F03VhQ105CVlA43C;X=Linker2)</td>

<td> ACP419 (WW0561)</td><td> IL2-XL-blocker-L-CD25 213S-X-HSA(Blocker=Hu2TOW91A;X=Linker2)</td>

<td> ACP420 (WW0562)</td><td> IL2-XL-blocker-L-CD25 213S-X-HSA(Blocker=Hu2TOW91B;X=Linker2)</td>

<td> ACP421 (WW0563)</td><td> HSA-X-blocker-L-CD25_213S-LX- IL2(B10cker=VHVL.F2.high. A02VhG44CVlA46SGl OOC;X=Linker 2)</td>

<td> ACP422 (WW0564)</td><td> HSA-X-blocker-L-CD25_213S-LX- IL2(Blocker=VHVL.F2.high.A02VhQ105CVlA43C;X=Linker2)</td>

<td> ACP423 (WW0565)</td><td> HSA-X-blocker-L-CD25_213S-LX- IL2(Blocker=VHVL.F2.high.F03VhG44CVlGl OOC;X=Linker 2)</td>

<td> ACP424 (WW0566)</td><td> HSA-X-blocker-L-CD25_213S-LX- IL2(Blocker=VHVL.F2.high.F03VhQ105CVlA43C;X=Linker2)</td>

<td> ACP425 (WW0567)</td><td> HSA-X-blocker-L-CD25 213S-LX-IL2(Blocker=Hu2TOW91A;X=Linker2)</td>

<td> ACP426 (WW0568)</td><td> HSA-X-blocker-L-CD25 213S-LX-IL2(Blocker=Hu2TOW91B;X=Linker2)</td>

<td> ACP427 (WW0569)</td><td> IL2-X-anti-HS A-LX-Blockerl -L- Blocker2(Blockerl=VHVL.F2.high.A02VhG44CVlA46SG100C, Blocker2=Hu2TOW91 A;X=Linker2)</td>

<td> ACP428 (WW0570)</td><td> IL2-X-anti-HS A-LX-Blockerl -L- Blocker2(Blockerl=VHVL.F2.high.A02VhQ105CVlA43C, Blocker2=Hu2TOW91 A;X=Linker2)</td>

<td> ACP429 (WW0571)</td><td> IL2-X-anti-HS A-LX-Blockerl -L- Blocker2(Blockerl=VHVL.F2.high.F03VhG44CVlG100C, Blocker2=Hu2TOW91 A;X=Linker2)</td>

<td> ACP430 (WW0572)</td><td> IL2-X-anti-HS A-LX-Blockerl -L- Blocker2(Blockerl=VHVL.F2.high.F03VhQ105CVlA43C, Blocker2=Hu2TOW91 A;X=Linker2)</td>

<td> ACP431 (WW0573)</td><td> IL2-X-anti-HS A-LX-Blockerl -L- Blocker2(Blockerl=VHVL.F2.high.A02VhG44CVlA46SG100C, Blocker2=Hu2TOW91 B;X=Linker2)</td>

<td> ACP432 (WW0574)</td><td> IL2-X-anti-HS A-LX-Blockerl -L- Blocker2(Blockerl=VHVL.F2.high.A02VhQ105CVlA43C, Blocker2=Hu2TOW91 B;X=Linker2)</td>

<td> ACP433 (WW0575)</td><td> IL2-X-anti-HS A-LX-Blockerl -L- Blocker2(Blockerl=VHVL.F2.high.F03VhG44CVlG100C, Blocker2=Hu2TOW91 B;X=Linker2)</td>

<td> ACP434 (WW0576)</td><td> IL2-X-anti-HS A-LX-Blockerl -L- Blocker2(Blockerl=VHVL.F2.high.F03VhQ105CVlA43C, Blocker2=Hu2TOW91 B;X=Linker2)</td>

<td> ACP439 (WW0581)</td><td> IL2-X-anti-HSA-LX-blocker_(Blocker=VHVL.F2.high.C07_Vh/Vl;X=Linker2)</td>

<td> ACP440 (WW0582)</td><td> IL2-X-at1ti-HSA-LX-blocker_(Blocker=VHVL.F2.high.C07_Vh/Vl_A46S;X=Linker 2)</td>

<td> ACP441 (WW0583)</td><td> IL2-X-anti-HSA-LX-blocker(Blocker=VHVL.F2.high.C07Vh/VlA46L;X=Linker 2)</td>

<td> ACP442 (WW0584)</td><td> IL2-X-anti-HSA-LX-blocker(Blocker=VHVL.F2.high.C07Vh/VlA46SVH44- VL1OOdi sulfide;X=Linker 2)</td>

<td> ACP443 (WW0585)</td><td> IL2-X-anti-HSA-LX-blocker(Blocker=VHVL.F2.high.C07Vh/VlA46LVH44- VL 1 OOdi sulfide;X=Linker 2)</td>

<td> ACP444 (WW0586)</td><td> IL2-X-anti-HS A-LX-blocker(Blocker=VHVL.F2.high. C07Vh/VlVH 105- VL43_disulfide;X=Linker 2)</td>

<td> ACP445 (WW0587)</td><td> IL2-X-anti-HSA-LX-blocker(Blocker=VHVL.F2.high. A02Vh-X-VlA46L;X=Linker 2)</td>

<td> ACP446 (WW0588)</td><td> IL2-X-anti-HSA-LX-blocker(Blocker=VHVL.F2.high. A02Vh/VlA46L;X=Linker 2)</td>

<td> ACP447 (WW0589)</td><td> IL2-X-anti-HSA-LX-blocker(Blocker=VHVL.F2.high.A02Vh/VlA46LVH44- VL 1 OOdi sulfide;X=Linker 2)</td>

<td> ACP451 (WW0615)</td><td> IL2-X-at1ti-HSA-LX-blocker_(Blocker=VHVL.F2.high.A02_Vh/Vl_A46S;X=Linker 3)</td>

<td> ACP452 (WW0616)</td><td> IL2-X-anti-HSA-LX-blocker(Blocker=VHVL.F2.high.F03Vh/Vl;X=Linker 3)</td>

<td> ACP453 (WW0617)</td><td> IL2-X-anti-HSA-LX-blocker(Blocker=VHVL.F2.high.A02Vh/VlA46SVH44- VL100_disulfide;X=Linker 3)</td>

<td> ACP454 (WW0618)</td><td> IL2-X-anti-HS A-LX-blocker(Blocker=VHVL.F2.high. A02Vh/VlVH 105- VL43_disulfidel;X=Linker 3)</td>

<td> ACP455 (WW0619)</td><td> IL2-X-anti-HSA-LX-blocker(Blocker=VHVL.F2.high.F03Vh/VlVH44- VL100_disulfide;X=Linker 3)</td>

<td> ACP456 (WW0620)</td><td> IL2-X-anti-HS A-LX-blocker(Blocker=VHVL.F2.high.F03Vh/VlVH 105- VL43_disulfideX=Linker 3)</td>

<td> ACP457 (WW0621)</td><td> IL2-X-anti-HSA-LX-HeavyblockerFab(Blocker= VH-CHl;X=Linker 3)</td>

<td> ACP458 (WW0622)</td><td> IgG4Fc(S228P)-X-IL2-LX-HeavyblockerFab(Blocke1= VH-CH1 ;X=Linker 3)</td>

<td> ACP459 (WW0623)</td><td> IgG4 Fc(S228P)-X-IL2-LX-B10cker (Blocker=VHVL.F2.high.A02 VhWl A46S;X=Linker 3)</td>

<td> ACP460 (WW0624)</td><td> IgG4Fc(S228P)-X-IL2-LX-Blocker(Blocker=VHVL.F2.high.F03Vh\Vl;X=Linker 3)</td>

<td> ACP461 (WW0625)</td><td> IgG4Fc(S228P)-X-IL2-LX-blocker(Blocker=VHVL.F2.high.A02Vh/VlA46SVH44- VL1 OO_disulfide;X=Linker 3)</td>

<td> ACP462 (WW0626)</td><td> IgG4Fc(S228P)-X-IL2-LX-blocker(Blocker=VHVL.F2.high.A02Vh/VlVH105- VL43_disulfidel;X=Linker 3)</td>

<td> ACP463 (WW0627)</td><td> IgG4Fc(S228P)-X-IL2-LX-blocker(Blocker=VHVL.F2.high.F03Vh/VlVH44- VL100_disulfidel;X=Linker 3)</td>

<td> ACP464 (WW0628)</td><td> IgG4Fc(S228P)-X-IL2-LX-blocker(Blocker=VHVL.F2.high.F03Vh/VlVH105- VL43_disulfidel;X=Linker 3)</td>

<td> ACP465 (WW0629)</td><td> mIgGlFc-X-IL2-LX-Blocker(Blocker=VHVL.F2.high.A02Vh\VlA46S;X=Linker3)</td>

<td> ACP466 (WW0630)</td><td> mIgGlFc-X-IL2-LX-Blocker(Blocker=VHVL.F2.high.F03Vh\Vl;X=Linker 3)</td>

<td> ACP467 (WW0631)</td><td> mIgGlFc-X-IL2-LX-blocker(Blocker=VHVL.F2.high.A02Vh/VlA46SVH44- VL100_disulfide;X=Linker 3)</td>

<td> ACP468 (WW0632)</td><td> mIgGlFc-X-IL2-LX-blocker(Blocker=VHVL.F2.high.A02Vh/VlVH105- VL43_disulfidel;X=Linker 3)</td>

<td> ACP469 (WW0633)</td><td> mIgGlFc-X-IL2-LX-blocker(Blocker=VHVL.F2.high.F03Vh/VlVH44- VL100_disulfidel;X=Linker 3)</td>

<td> ACP470 (WW0634)</td><td> mIgGlFc-X-IL2-LX-blocker(Blocker=VHVL.F2.high.F03Vh/VlVH105- VL43_disulfidel;X=Linker 3)</td>

<td> ACP471 (WW0642)</td><td> mIgGlFc-X-IL2-LX-HeavyblockerFab(Blocker=VH-CHl ;X=Linker 3)</td>

<td> WW0301</td><td> IL2-X-anti-HSA-LL-blocker(X=LinkerlBlocker=Vh-Vl)</td>

<td> WW0353</td><td> IL2-X-mIgGlFc-LX-B10cker(X=LinkerlB10cker=Vh-Vl)</td>

<td> WW0355</td><td> IL2-XL-B10cker-X-mIgGlFc(X=LinkerlB10cker=Vh-Vl)</td>

<td> WW0365</td><td> IL-2-L-anti-HSA-LX-Blocker_(instead_of_WW0048_IL2-X-anti-HSA-LXblocker) (X=Linkerl)</td>

<td> WW0366</td><td> IL-2-X-anti-HS A_(GeneArt_version_of_WW0061)_(X=Linker 1)</td>

<td> WW0472</td><td> mIgGlFc-X-IL2-LX-Blocker(Blocker=VHVL.F2.high.A02Vh-X-VlA46SX=Linker2)</td>

<td> WW0473</td><td> mIgGlFc-X-IL2-LX-Blocker(Blocker=VHVL.F2.high.A02Vh-VlA46SX=Linker2)</td>

<td> WW0474</td><td> mIgGlFc-X-IL2-LX-Blocker(Blocker=VHVL.F2.high.F03Vh-X-VlX=Linker2)</td>

<td> WW0475</td><td> mIgGlFc-X-IL2-LX-Blocker(Blocker=VHVL.F2.high.F03Vh-VlX=Linker2)</td>

<td> WW0476</td><td> mIgGlFc-X-IL2-LX-Blocker(Blocker=Hu2TOW91BX=Linker2)</td>

<td> WW0477</td><td> mIgGlFc-X-IL2-LX-Blocker(Blocker=Hu3TOW85AX=Linker2)</td>

<td> WW0641</td><td> anti-HSA-X-human_p40mouse_p35-XL-Blocker(Blocker=Vl/VhVH 105- VL43 disulfide;X=Linkerl)</td>

<td> WW0649</td><td> anti-HSA-X-human_p40-L-mouse_p35-XL-Blocker_(Blocker=Vl/Vh_X=Linker2)</td>

<td> WW0650</td><td> anti-HS A-X-human_p40-L-Human_p3 5 -XL-B1 ocker(Bl ocker=Vl/Vh_X=Linker2)</td>

<td> WW0651</td><td> anti-HSA-X-human_p40-L-mouse_p35-XL-B10cker_(B10cker=Vl/Vh_X=Linker3)</td>

<td> WW0652</td><td> anti-HSA-X-human_p40-L-Human_p35-XL-Blocker_(Blocker=Vl/Vh_X=Linker3)</td>

<td> WW0662</td><td> anti-HSA-X-human_p40-L-mouse_p35-XL- Blocker (Blocker=Optl Hv D53E D61E Vl/Vh X=Linker2)</td>

<td> WW0663</td><td> anti-HSA-X-human_p40-L-human_p35-XL- Blocker (Blocker=Optl Hv D53E D61E Vl/Vh X=Linker2)</td>

<td> WW0664</td><td> anti-HSA-X-human_p40-L-mouse_p35-XL-Blocker(Blocker=Opt2LvN31EHv D53E D61E Vl/Vh X=Linker2)</td>

<td> WW0665</td><td> anti-HSA-X-human_p40-L-human_p35-XL-Blocker(Blocker=Opt2LvN31E- Hv D53E D61E Vl/Vh X=Linker2)</td>

<td> WW0666</td><td> anti-HSA-X-human_p40-L-mouse_p35-XL-Blocker(Blocker=Opt3LVS30D- Hv D53E D61E Vl/Vh X=Linker2)</td>

<td> WW0667</td><td> anti-HSA-X-human_p40-L-human_p35-XL-Blocker(Blocker=Opt3LVS30DHv D53E D61E Vl/Vh X=Linker2)</td>

<td> WW0668</td><td> anti-HSA-X-human_p40-L-mouse_p35-XL- Blocker (Blocker=Opt4 LV S30D N31E Vl/Vh X=Linker2)</td>

<td> WW0669</td><td> anti-HSA-X-human_p40-L-human_p35-XL- Blocker (Blocker=Opt4 LV S30D N31E Vl/Vh X=Linker2)</td>

<td> WW0670</td><td> anti-HSA-X-human_p40-L-mouse_p35-XL-Blocker(Blocker=Opt5LvS30DN31E- Hv D53E D61E Vl/Vh X=Linker2)</td>

<td> WW0672</td><td> anti-HSA-X-human_p40-L-mouse_p35-XL- Blocker (Blocker=Opt6 Lv R27E T32D(LCharge 16(combo2)) Vl/Vh X=Linker2)</td>

<td> WW0673</td><td> anti-HSA-X-human_p40-L-human_p35-XL- Blocker (Blocker=Opt6 Lv R27E T32D(LCharge 16(combo2)) Vl/Vh X=Linker2)</td>

<td> WW0674</td><td> anti-HSA-X-human_p40-L-mouse_p35-XL-Blocker(Blocker=Opt7LvS30E- Hv D53E D61E Vl/Vh X=Linker2)</td>

<td> WW0675</td><td> anti-HSA-X-human_p40-L-human_p35-XL-Blocker(Blocker=Opt7LvS30E- Hv D53E D61E Vl/Vh X=Linker2)</td>

<td> WW0676</td><td> anti-HSA-X-human_p40-L-mouse_p35-XL-Blocker(Blocker=Opt8LvS30E N31E Vl/Vh X=Linker2)</td>

<td> WW0677</td><td> anti-HSA-X-human_p40-L-human_p35-XL-Blocker(Blocker=Opt8LvS30E N31E Vl/Vh X=Linker2)</td>

<td> WW0678</td><td> anti-HSA-X-human_p40-L-mouse_p35-XL-Blocker(Blocker=Opt9LvN31EHv D53E Vl/Vh X=Linker2)</td>

<td> WW0679</td><td> anti-HSA-X-human_p40-L-human_p35-XL-Blocker(Blocker=Opt9LvN31E- Hv D53E Vl/Vh X=Linker2)</td>

<td> WW0680</td><td> anti-HSA-X-human_p40-L-mouse_p35-XL- Blocker (Blocker=Optl Hv D53E D61E Vl/Vh X=Linker3</td>

<td> WW0681</td><td> anti-HSA-X-human_p40-L-human_p35-XL- Blocker (Blocker=Optl Hv D53E D61E Vl/Vh X=Linker3)</td>

<td> WW0682</td><td> anti-HSA-X-human_p40-L-mouse_p35-XL-Blocker(Blocker=Opt2LvN31EHv D53E D61E Vl/Vh X=Linker3</td>

<td> WW0683</td><td> anti-HSA-X-human_p40-L-human_p35-XL-Blocker(Blocker=Opt2LvN31E- Hv D53E D61E Vl/Vh X=Linker3)</td>

<td> WW0684</td><td> anti-HSA-X-human_p40-L-mouse_p35-XL-Blocker(Blocker=Opt3LVS30D- Hv D53E D61E Vl/Vh X=Linker3</td>

<td> WW0685</td><td> anti-HSA-X-human_p40-L-human_p35-XL-Blocker(Blocker=Opt3LVS30D- Hv D53E D61E Vl/Vh X=Linker3)</td>

<td> WW0686</td><td> anti-HSA-X-human_p40-L-mouse_p35-XL- Blocker (Blocker=Opt4 LV S30D N31E Vl/Vh X=Linker3</td>

<td> WW0687</td><td> anti-HSA-X-human_p40-L-human_p35-XL- Blocker (Blocker=Opt4 LV S30D N31E Vl/Vh X=Linker3)</td>

<td> WW0688</td><td> anti-HSA-X-human_p40-L-mouse_p35-XL-Blocker(Blocker=Opt5LvS30DN31EHv D53E D61E Vl/Vh X=Linker3</td>

<td> WW0689</td><td> anti-HSA-X-human_p40-L-human_p35-XL-Blocker(Blocker=Opt5LvS30DN31E- Hv D53E D61E Vl/Vh X=Linker3)</td>

<td> WW0690</td><td> anti-HSA-X-human_p40-L-mouse_p35-XL- Blocker (Blocker=Opt6 Lv R27E T32D(LCharge 16(combo2)) Vl/Vh X=Linker3</td>

<td> WW0691</td><td> anti-HSA-X-human_p40-L-human_p35-XL- Blocker (Blocker=Opt6 Lv R27E T32D(LCharge 16(combo2)) Vl/Vh X=Linker3)</td>

<td> WW0692</td><td> anti-HSA-X-human_p40-L-mouse_p35-XL-Blocker(Blocker=Opt7LvS30E- Hv D53E D61E Vl/Vh X=Linker3</td>

<td> WW0693</td><td> anti-HSA-X-human_p40-L-human_p35-XL-Blocker(Blocker=Opt7LvS30E- Hv D53E D61E Vl/Vh X=Linker3)</td>

<td> WW0694</td><td> anti-HSA-X-human_p40-L-mouse_p35-XL- Blocker (Blocker=Opt8 Lv S30E N31E Vl/Vh X=Linker3</td>

<td> WW0695</td><td> anti-HSA-X-human_p40-L-human_p35-XL- Blocker (Blocker=Opt8 Lv S30E N31E Vl/Vh X=Linker3)</td>

<td> WW0698</td><td> anti-HSA-X-human_p40-L-mouse_p35-XL- Fab Lambda Blocker (B10cker=Lambda Fab IGLC2-01 X=Linker2)</td>

<td> WW0699</td><td> anti-HSA-X-human_p40-L-human_p35-XL- Fab Lambda Blocker (B10cker=Lambda Fab IGLC2-01 X=Linker2)</td>

<td> WW0700</td><td> anti-HSA-X-human_p40-L-mouse_p35-XL- Fab Lambda Blocker (B10cker=Lambda Fab N31E IGLC2-01 X=Linker2)</td>

<td> WW0701</td><td> anti-HSA-X-human_p40-L-human_p35-XL- Fab Lambda Blocker (B10cker=Lambda Fab N31E IGLC2-01 X=Linker2)</td>

<td> WW0702</td><td> anti-HSA-X-human_p40-L-mouse_p35-XL- Fab Lambda Blocker (B10cker=Lambda Fab S30D IGLC2-01 X=Linker2)</td>

<td> WW0703</td><td> anti-HSA-X-human_p40-L-human_p35-XL- Fab Lambda Blocker (B10cker=Lambda Fab S30D IGLC2-01 X=Linker2)</td>

<td> WW0704</td><td> anti-HSA-X-human_p40-L-mouse_p35-XL- Fab Lambda Blocker (B10cker=Lambda Fab S30D N31E IGLC2-01 X=Linker2)</td>

<td> WW0705</td><td> anti-HSA-X-human_p40-L-human_p35-XL- Fab Lambda Blocker (B10cker=Lambda Fab S30D N31E IGLC2-01 X=Linker2)</td>

<td> WW0706</td><td> anti-HSA-X-human_p40-L-mouse_p35-XL- Fab Lambda Blocker (B10cker=Lambda Fab R27E T32D IGLC2-01 X=Linker2)</td>

<td> WW0707</td><td> anti-HSA-X-human_p40-L-human_p35-XL- Fab Lambda Blocker (B10cker=Lambda Fab R27E T32D IGLC2-01 X=Linker2)</td>

<td> WW0708</td><td> anti-HSA-X-human_p40-L-mouse_p35-XL- Fab Lambda Blocker (B10cker=Lambda Fab S30E IGLC2-01 X=Linker2)</td>

<td> WW0709</td><td> anti-HSA-X-human_p40-L-human_p35-XL- Fab Lambda Blocker (B10cker=Lambda Fab S30E IGLC2-01 X=Linker2)</td>

<td> WW0710</td><td> anti-HSA-X-human_p40-L-mouse_p35-XL- Fab Lambda Blocker (B10cker=Lambda Fab S30E N31E IGLC2-01 X=Linker2)</td>

<td> WW0711</td><td> anti-HSA-X-human_p40-L-human_p35-XL- Fab Lambda Blocker (B10cker=Lambda Fab S30E N31E IGLC2-01 X=Linker2)</td>

<td> WW0712</td><td> anti-HSA-X-human_p40-L-mouse_p35-XL- Fab Lambda Blocker (B10cker=Lambda Fab IGLC2-01 X=Linker3)</td>

<td> WW0713</td><td> anti-HSA-X-human_p40-L-human_p35-XL- Fab Lambda Blocker (B10cker=Lambda Fab IGLC2-01 X=Linker3)</td>

<td> WW0714</td><td> anti-HSA-X-human_p40-L-mouse_p35-XL- Fab Lambda Blocker (B10cker=Lambda Fab N31E IGLC2-01 X=Linker3)</td>

<td> WW0715</td><td> anti-HSA-X-human_p40-L-human_p35-XL- Fab Lambda Blocker (B10cker=Lambda Fab N31E IGLC2-01 X=Linker3)</td>

<td> WW0716</td><td> anti-HSA-X-human_p40-L-mouse_p35-XL- Fab Lambda Blocker (B10cker=Lambda Fab S30D IGLC2-01 X=Linker3)</td>

<td> WW0717</td><td> anti-HSA-X-human_p40-L-human_p35-XL- Fab Lambda Blocker (B10cker=Lambda Fab S30D IGLC2-01 X=Linker3)</td>

<td> WW0718</td><td> anti-HSA-X-human_p40-L-mouse_p35-XL- Fab Lambda Blocker (B10cker=Lambda Fab S30D N31E IGLC2-01 X=Linker3)</td>

<td> WW0719</td><td> anti-HSA-X-human_p40-L-human_p35-XL- Fab Lambda Blocker (B10cker=Lambda Fab S30D N31E IGLC2-01 X=Linker3)</td>

<td> WW0720</td><td> anti-HSA-X-human_p40-L-mouse_p35-XL- Fab Lambda Blocker (B10cker=Lambda Fab R27E T32D IGLC2-01 X=Linker3)</td>

<td> WW0721</td><td> anti-HSA-X-human_p40-L-human_p35-XL- Fab Lambda Blocker (B10cker=Lambda Fab R27E T32D IGLC2-01 X=Linker3)</td>

<td> WW0722</td><td> anti-HSA-X-human_p40-L-mouse_p35-XL- Fab Lambda Blocker (B10cker=Lambda Fab S30E IGLC2-01 X=Linker3)</td>

<td> WW0723</td><td> anti-HSA-X-human_p40-L-human_p35-XL- Fab Lambda Blocker (B10cker=Lambda Fab S30E IGLC2-01 X=Linker3)</td>

<td> WW0724</td><td> anti-HSA-X-human_p40-L-mouse_p35-XL- Fab Lambda Blocker (B10cker=Lambda Fab S30E N31E IGLC2-01 X=Linker3)</td>

<td> WW0725</td><td> anti-HSA-X-human_p40-L-human_p35-XL- Fab Lambda Blocker (B10cker=Lambda Fab S30E N31E IGLC2-01 X=Linker3)</td>

<td> WW0726</td><td> FabHeavyB10cker(B10cker=IL-12HeavyFabIgGlFab)</td>

<td> WW0727</td><td> FabHeavyB10cker(B10cker=IL-12HeavyFabD53ED61EIgGlFab)</td>

<td> WW0728</td><td> Fab_Heavy_B10cker_(B10cker=IL-12_Heavy_Fab_D53E_IgGl_Fab)</td>

<td> WW0765</td><td> human_p40-L-mouse_p35-X-anti-HSA-L- Blocker (Blocker=Optl Hv D53E D61E Vl/Vh X=Linker2)</td>

<td> WW0766</td><td> human_p40-L-human_p35-X-anti-HSA-L- Blocker (Blocker=Optl Hv D53E D61E Vl/Vh X=Linker2)</td>

<td> WW0767</td><td> human_p40-L-mouse_p35-X-anti-HSA-L-Blocker(Blocke1=Opt5LvS30DN31E- Hv D53E D61E Vl/Vh X=Linker2)</td>

<td> WW0768</td><td> human_p40-L-human_p35-X-anti-HSA-L-Blocker(Blocker=Opt5LvS30DN31E- Hv D53E D61E Vl/Vh X=Linker2)</td>

<td> WW0769</td><td> human_p40-L-mouse_p35-X-anti-HSA-L- Fab Lambda Blocker (B10cker=Lambda Fab IGLC2-01 X=Linker2)</td>

<td> WW0770</td><td> human_p40-L-human_p35-X-anti-HSA-L- Fab Lambda Blocker (B10cker=Lambda Fab IGLC2-01 X=Linker2)</td>

<td> WW0771</td><td> human_p40-L-mouse_p35-X-anti-HSA-L- Fab Lambda Blocker (B10cker=Lambda Fab S30D N31E IGLC2-01 X=Linker2)</td>

<td> WW0772</td><td> human_p40-L-human_p35-X-anti-HSA-L- Fab Lambda Blocker (B10cker=Lambda Fab S30D N31E IGLC2-01 X=Linker2)</td>

<td> WW0796</td><td> human_p40-L-mouse_p35-X-anti-HSA-L-Blocker(Blocke1=OptlHvD53ED61EVl- Vh X=Linker3)</td>

<td> WW0797</td><td> human_p40-L-human_p35-X-anti-HSA-L-Blocker(Blocker=OptlHvD53ED61EVl- Vh X=Linker3)</td>

<td> WW0798</td><td> human_p40-L-mouse_p35-X-anti-HSA-L-Blocker(Blocke1=Opt5LvS30DN31E- Hv D53E D61E Vl-Vh X=Linker3)</td>

<td> WW0799</td><td> human_p40-L-human_p35-X-anti-HSA-L-Blocker(Blocker=Opt5LvS30DN31E- Hv D53E D61E Vl-Vh X=Linker3)</td>

<td> WW0800</td><td> human_p40-L-mouse_p35-X-anti-HSA-L- Fab Lambda Blocker (B10cker=Lambda Fab IGLC2-01 X=Linker3)</td>

<td> WW0801</td><td> human_p40-L-human_p35-X-anti-HSA-L- Fab Lambda Blocker (B10cker=Lambda Fab IGLC2-01 X=Linker3)</td>

<td> WW0802</td><td> human_p40-L-mouse_p35-X-anti-HSA-L- Fab Lambda Blocker (B10cker=Lambda Fab S30D N31E IGLC2-01 X=Linker3)</td>

<td> WW0803</td><td> human_p40-L-human_p35-X-anti-HSA-L- Fab Lambda Blocker (B10cker=Lambda Fab S30D N31E IGLC2-01 X=Linker3)</td>

<td> WW0643</td><td> HS A-X-mIFNal 1 -X-HS A(X=Linker2)</td>

<td> WW0644</td><td> HS A-X-mIFNal 1 -X-HS A(X=Linker3)</td>

<td> WW0645</td><td> HSA-X-HumanIFNA14-X-HSA(X=Linker2)</td>

<td> WW0646</td><td> HSA-X-HumanIFNA14-X-HSA(X=Linker3)</td>

<td> WW0647</td><td> MouselFNAl 1</td>

<td> WW0648</td><td> HumanIFNA14</td>

<td> WW0781</td><td> HSA-X-HumanIFNA2bT129E-X-HSA(X=Linker2)</td>

<td> WW0782</td><td> HSA-X-HumanIFNA14N95D-X-HSA(X=Linker2)</td>

<td> WW0783</td><td> HSA-X-HumanIFNA14N25DS27PN95D-X-HSA(X=Linker2)</td>

<td> WW0784</td><td> Human_IFNA2b_T129E</td>

<td> WW0785</td><td> Human_IFNA14_N95D</td>

<td> WW0786</td><td> Human_IFNA14_N25D_S27P_N95D</td>

<td> WW0815</td><td> mAlb-X-mIFNal -X-mAlb_(X=Linker3)</td>

<td> WW0816</td><td> m Alb-X-mIFNal 1 -X-m Alb(X=Linker3)</td>

<td> WW0817</td><td> anti-HS A-X-mIFNal -X-mAlb(X=Linker3)</td>

<td> WW0818</td><td> anti-HSA-X-mIFNal l-mAlb_(X=Linker3)</td>

<td> WW0819</td><td> mAlb-X-mIFNal -X-anti-HS A_(X=Linker3)</td>

<td> WW0820</td><td> m Alb-X-m IFNal 1 -anti-HS A(X=Linker3)</td>

<td> WW0821</td><td> Alb-X-Human_IFNA2b-X-Alb_(X=Linker3)</td>

<td> WW0822</td><td> Alb-X-Human_IFNA14-X-Alb_(X=Linker3)</td>

<td> WW0831</td><td> Alb-X-IFNa8-X-Alb_(X=Linker3)</td>

<td> WW0832</td><td> Alb-X-IFNal 6-Alb_(X=Linker3)</td>

<td> WW0833</td><td> Anti-HSA-X-IFNa8-X-anti-HSA(X=Linker3)</td>

<td> WW0834</td><td> Anti-HS A-X-IFNal6-X-anti-HSA(X=Linker3)</td>

<td> WW0737</td><td> HSA-X-mIFNb-X-HSA(X=Linker2)</td>

<td> WW0738</td><td> HSA-X-mIFNb-X-HSA(X=Linker3)</td>

<td> WW0739</td><td> HSA-X-mIFNbC38S-X-HSA(X=Linker2)</td>

<td> WW0740</td><td> HSA-X-mIFNbC38S-X-HSA(X=Linker3)</td>

<td> WW0741</td><td> HSA-X-HumanIFNB-X-HSA(X=Linker2)</td>

<td> WW0742</td><td> HSA-X-HumanIFNB-X-HSA(X=Linker3)</td>

<td> WW0743</td><td> HSA-X-HumanIFNBC38S-X-HSA(X=Linker2)</td>

<td> WW0744</td><td> HSA-X-HumanIFNBC38S-X-HSA(X=Linker3)</td>

<td> WW0745</td><td> MouselFNb</td>

<td> WW0746</td><td> Mouse_IFNb_C38S</td>

<td> WW0747</td><td> HumanIFNB</td>

<td> WW0748</td><td> HumanIFNABC38S</td>

<td> WW0787</td><td> HSA-X-HumanIFNBN101Q-X-HSA(X=Linker2)</td>

<td> WW0788</td><td> HSA-X-HumanIFNBN101QC38S-X-HSA(X=Linker2)</td>

<td> WW0789</td><td> HumanIFNBNIOlQ</td>

<td> WW0790</td><td> Human_IFNB_C38S_N101Q</td>

<td> WW0729</td><td> IL2-L-anti-HS A-LL-Heavy_blocker_F ab_(B10cker=VH-CH1 non-cleavable)</td>

<td> WW0734</td><td> IL2-X-anti-HSA-LL-HeavyblockerFab(Blocker=VH-CHlX=Linkerl)</td>

<td> WW0735</td><td> IL2-X-anti-HSA-LL-HeavyblockerFab(Blocker=VH-CHlX=Linker2)</td>

<td> WW0736</td><td> IL2-X-anti-HSA-LL-HeavyblockerFab(Blocker=VH-CHlX=Linker3)</td>

<td> WW0792</td><td> Anti-IL-2_F abHeavylgG 1 BlockerHistag</td>

<td> WW0061</td><td> IL2-X-anti-HS AFusion(X=Linker 1)</td>

<td></td><td> 121</td>

<td> ACP293 (WW0237)</td><td> 3TOW69sdAb</td>

<td> ACP294 (WW0238)</td><td> 3TOW85sdAb</td>

<td> ACP295 (WW0239)</td><td> 2TOW91sdAb</td>

<td> ACP315 (WW0368)</td><td> Hu2TOW91_A</td>

<td> ACP316 (WW0369)</td><td> Hu2TOW91 B</td>

<td> ACP317 (WW0370)</td><td> Hu2TOW91 C</td>

<td> ACP318 (WW0371)</td><td> Hu2TOW91 D</td>

<td> ACP319 (WW0372)</td><td> HELM2TOW91</td>

<td> ACP320 (WW0373)</td><td> HE L 2TOW91</td>

<td> ACP321 (WW0374)</td><td> Hu3TOW85_A</td>

<td> ACP322 (WW0375)</td><td> Hu3TOW85_B</td>

<td> ACP323 (WW0376)</td><td> Hu3TOW85_C</td>

<td> ACP324 (WW0377)</td><td> Hu3TOW85_D</td>

<td> ACP325 (WW0378)</td><td> HELM3TOW85</td>

<td> ACP326 (WW0379)</td><td> HEL3TOW85</td>

<td> ACP327 (WW0380)</td><td> HELMR45L3TOW85</td>

<td> ACP328 (WW0381)</td><td> Hu3TOW69_A</td>

<td> ACP329 (WW0382)</td><td> Hu3TOW69 B</td>

<td> ACP330 (WW0383)</td><td> Hu3TOW69 C</td>

<td> ACP331 (WW0384)</td><td> Hu3TOW69 D</td>

<td> ACP332 (WW0385)</td><td> Hu3TOW69_E</td>

<td> ACP333 (WW0386)</td><td> HELM3TOW69</td>

<td> ACP334 (WW0387)</td><td> HE L 3TOW69</td>

<td> ACP335 (WW0388_</td><td> HELMR45L3TOW69</td>

<td> ACP360 (WW0438)</td><td> Vh-Vl_3xG4S_A46S (3xG4S is disclosed as SEQ ID NO: 452)</td>

<td> ACP361(WW 0439)</td><td> Vh-Vl_3xG4S_A46S (3xG4S is disclosed as SEQ ID NO: 452)</td>

<td> ACP362 (WW0440)</td><td> Vh-X-Vl_X=Linker2</td>

<td> ACP363 (WW0441)</td><td> Vh-X-Vl_X=Linker2_A46S</td>

<td> ACP364 (WW0442)</td><td> VHVL.F2.high.A02_Vh-Vl_3xG4S (3xG4S is disclosed as SEQ ID NO: 452)</td>

<td> ACP365 (WW0443)</td><td> VHVL.F2.high.A02_Vh-Vl_3xG4S_A46S (3xG4S is disclosed as SEQ ID NO: 452)</td>

<td> ACP366(WW 0444)</td><td> VHVL·F2.high.A02_Vh-X-Vl_X=Li1זker2</td>

<td> ACP367 (WW0445)</td><td> VHVL·F2.high.A02_Vh-X-Vl_X=Li1זker2_A46S</td>

<td> ACP368 (WW0446)</td><td> VHVL.F2.high.F03_Vh-Vl_3xG4S (3xG4S is disclosed as SEQ ID NO: 452)</td>

<td> ACP369 (WW0449)</td><td> VHVL.F2.high.F03_Vh-X-Vl_X=Linker2</td>

<td> ACP370 (WW0450)</td><td> VHVL.F2.high.C07_Vh-Vl_3xG4S (3xG4S is disclosed as SEQ ID NO: 452)</td>

<td> ACP380 (WW0522)</td><td> KappablockerFab(Blocker=Kappa)</td>

<td> ACP381 (WW0523)</td><td> Kappa_blocker_Fab_(Blocker=VHVL.F2.high.A02_A46S_Kappa)</td>

<td> ACP382 (WW0524)</td><td> KappablockerFab(Blocker=VHVL.F2.high.F03Kappa)</td>

<td> ACP434 (WW0576)</td><td> IL2-X-anti-HS A-LX-Blockerl -L- Blocker2(Blockerl=VHVL.F2.high.F03VhQ105CVlA43CBlocker2=Hu2TOW91BX =Linker2)</td>

<td> ACP435 (WW0577)</td><td> Kappa_blockerl_Fab-L- blocker2(Blockerl=VHVL.F2.high.A02A46SKappaBlocker2=Hu2TOW91A)</td>

<td> ACP436 (WW0578)</td><td> Kappa_blockerl_Fab-L- blocker2(Blockerl=VHVL.F2.high.A02A46SKappaBlocker2=Hu2TOW91B)</td>

<td> ACP437 (WW0579)</td><td> Kappa_blockerl_Fab-L- blocker2(Blockerl=VHVL.F2.high.F03KappaBlocker2=Hu2TOW91A)</td>

<td> ACP438 (WW0580)</td><td> Kappa_blockerl_Fab-L- blocker2(Blockerl=VHVL.F2.high.F03KappaBlocker2=Hu2TOW91B)</td>

<td> ACP448 (WW0590)</td><td> KappablockerFab(Blocker=VHVL.F2.high.C07A46SKappa)</td>

<td> ACP449 (WW0591)</td><td> KappablockerFab(Blocker=VHVL.F2.high.C07A46LKappa)</td>

<td> ACP450 (WW0592)</td><td> KappablockerFab(Blocker=VHVL.F2.high.A02A46LKappa)</td>

Sequence Table

<td> SEQ ID NO.</td><td> Name</td><td> Sequence</td>

<td> 1</td><td> Human IL- 2</td><td> MYRMQLLSCIALSLALVTNS APTSSSTKKT QLQLEHLLLD LQMILNGINN YKNPKLTRML TFKFYMPKKA TELKHLQCLE EELKPLEEVL NLAQSKNFHL RPRDLISNIN VIVLELKGSE TTFMCEYADE TATIVEFLNR WITFCQSIISTLT</td>

<td> 2</td><td> Human serum albumin</td><td> MKWVTFISLL FLFSSAYSRG VFRRDAHKSE VAHRFKDLGE ENFKALVLIA FAQYLQQCPF EDHVKLVNEV TEFAKTCVAD ESAENCDKSL HTLFGDKLCT VATLRETYGE MADCCAKQEP ERNECFLQHK DDNPNLPRLV RPEVDVMCTA FHDNEETFLK KYLYEIARRH PYFYAPELLF F AKRYKAAFT ECCQAADKAA CLLPKLDELR DEGKASSAKQ GLKCASLQKF GERAFKAWAV ARLSQRFPKA EFAEVSKLVT DLTKVHTECC HGDLLECADD RADLAKYICE NQDSISSKLK ECCEKPLLEK SHCIAEVEND EMPADLPSLA ADFVGSKDVC KNYAEAKDVF LGMFLYEYAR RHPDYSWLL LRLAKTYETT LEKCCAAADP HECYAKVFDE FKPLVEEPQN LIKQNCELFE QLGEYKFQNA LLVRYTKKVP QVSTPTLVEV SRNLGKVGSK CCKHPEAKRM PCAEDCLSVF LNQLCVLHEK TPVSDRVTKC CTESLVNGRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALV ELVKHK PKATKEQLKAVMDDFAAFVEKCCKADDKET CFAEEGKKLVAASQAALGL</td>

<td> 45</td><td> ACP12 (IL2 fusion protein)</td><td> QVQLQESGGGLVQAGGSLRLSCAASGRIFSIDIMSWYRQAPGKQRELVARITR GGTISYDDSVKGRFTISRDNAKNTVYLQMNSLKPEDTGVYYCNALYGTDYW GKGTQVTVSSggggsggggsggggsaptssstkktqlqlehllldlqmilnginnyknpkltrmltfkfympkk atelkhlqcleeelkpleevlnlaqsknfhlrprdlisninvivlelkgsettfinceyadetativeflnrwitfcqsiistltSG GPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQ APGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTA VYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggsEVQLVESGGGLVQPGGSLR LSCAASGFIESSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRD NAKNSLYLQMNSLRAEDTAVYYCARDSbTWDALDYWGQGTTVTVSSGGGGS GGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKASQNVGTNVGWYQQKPGK APKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYT FGGGTKVEIKHHHHHH</td>

<td> 46</td><td> ACP13 (IL2 fusion protein)</td><td> QVQLQESGGGLVQAGGSLRLSCAASGRIFSIDIMSWYRQAPGKQRELVARITR GGTISYDDSVKGRFTISRDNAKNTVYLQMNSLKPEDTGVYYCNALYGTDYW GKGTQVTVSSggggsggggsggggsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSY TLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNS LRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDI QMTQSPSSLSASVGDRVTITCKASQNVGTNVGWYQQKPGKAPKALIYSASFR YSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIKgg ggsggggsggggsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGK GLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYC TIGGSLSVSSQGTLVTVSSSGGPGPAGMKGLPGSaptssstkktqlqlehllldlqmilnginny knpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrprdlisnmvivlelkgsettfinceyadetati veflnrwitfcqsiistltHHHHHH</td>

<td> 47</td><td> ACP14 (IL2 fusion protein) WW0045</td><td> EVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAID SSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDAL DYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCK ASQNVGTNVGWYQQKPGKAPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSL QPEDFATYYCQQYYTYPYTFGGGTKVEIKggggsggggsggggsggggsggggsggggsSG GPGPAGMKGLPGSaptssstkktqlqlehllldlqmilngmnyknpkltrmltfldympkkatelkhlqcleee IkpleevlnlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltSGGPGPAGM KGLPGSEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLE WVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIG GSLSVSSQGTLVTVSSHHHHHH</td>

<td> 48</td><td> ACP15 (IL2 fusion protein) (WW0047)</td><td> EVQLVESGGGLVQPGGSLRLSCAASGFIESSYTLAWVRQAPGKGLEWVAAID SSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDAL DYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCK ASQNVGTNVGWYQQKPGKAPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSL QPEDFATYYCQQYYTYPYTFGGGTKVEIKggggsggggsggggsggggsggggsggggsEV</td>

<td></td><td></td><td> QLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGS GRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQ GTLVTVSSggggsggggsggggsSGGPGPAGMKGLPGSaptssstkktqlqlehllldlqmilnginn yknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrprdlisninvivlelkgsettfinceyadetat iveflnrwitfcqsiistltHHHHHH</td>

<td> 49</td><td> ACP16 (IL2 fusion protein) (WW0048)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltSGGPGPAGMKGLPGSEVQLVES GGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTL YAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVT VSSggggsggggsggggsggggsggggsggggsSGGPGPAGMKGLPGSEVQLVESGGGLV QPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRG RFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVS SGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKASQNVGTNVGWY QQKPGKAPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQ YYTYPYTFGGGTKVEIKHHHHHH</td>

<td> 50</td><td> ACP17 (IL2 fusion protein)</td><td> QVQLQESGGGLVQAGGSLRLSCAASGRIFSIDIMSWYRQAPGKQRELVARITR GGTISYDDSVKGRFTISRDNAKNTVYLQMNSLKPEDTGVYYCNALYGTDYW GKGTQVTVSSggggsggggsggggsaptssstkktqlqlehllldlqmilnginnyknpkltrmltfkfympkk atelkhlqcleeelkpleevlnlaqsknfhlrprdlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltSG GPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQ APGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTA VYY CTIGGSLS VS SQGTLVTV SSggggsggggsggggsggggsggggsggggsSGGPGPAG MKGLPGSEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGL EWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCAR DSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVG DRVTITCKASQNVGTNVGWYQQKPGKAPKALIYSASFRYSGVPSRFSGSGSGT DFTLTISSLQPEDFAIYYCQQ YYTYPYTFGGGTKVEIKHHHHHH</td>

<td> 51</td><td> ACPI 8 (IL2 fusion protein)</td><td> QVQLQESGGGLVQAGGSLRLSCAASGRIFSIDIMSWYRQAPGKQRELVARITR GGTISYDDSVKGRFTISRDNAKNTVYLQMNSLKPEDTGVYYCNALYGTDYW GKGTQVTVSSggggsggggsggggsaptssstkktqlqlehllldlqmilnginnyknpkltrmltfkfympkk atelkhlqcleeelkpleevlnlaqsknfhlrprdlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltSG GPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQ APGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTA VYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggsggggsggggsggggsEVQLVESG GGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPD TVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTT VTVSSsggpgpagmkglpgsDIQMTQSPSSLSASVGDRVTITCKASQNVGTNVGWY QQKPGKAPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQ YYTYPYTFGGGTKVEIKHHHHHH</td>

<td> 52</td><td> ACP19 (IL2 fusion protein)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltSGGPGPAGMKGLPGSggggsggggs ggggsggggsggggsggggsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVR QAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTA VYYCARDSbTWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSS LSASVGDRVTITCKASQNVGTNVGWYQQKPGKAPKALIYSASFRYSGVPSRFS GSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIKggggsggggsggg gsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSI SGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSV SSQGTLVTVSSggggsggggsggggsQVQLQESGGGLVQAGGSLRLSCAASGRIFSID IMSWYRQAPGKQRELVARITRGGTISYDDSVKGRFTISRDNAKNTVYLQMNSL KPEDTGVYYCNALYGTDYWGKGTQVTVSSHHHHHH**</td>

<td> 53</td><td> ACP20 (IL2 fusion protein) (WW0056)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltSGGPGPAGMKGLPGSEVQLVES GGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSP DTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGT TVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKASQNVGTN VGWYQQKPGKAPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATY YCQQYYTYPYTFGGGTKVEIKHHHHHH</td>

<td> 54</td><td> ACP21 (IL2 fusion protein) (WW0057)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltSGGPGPAGMKGLPGSggggsggggs ggggsggggsggggsggggsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVR QAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTA VYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSS LSASVGDRVTITCKASQNVGTNVGWYQQKPGKAPKALIYSASFRYSGVPSRFS GSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIKHHHHHH</td>

<td> 55</td><td> ACP22 (IL2 fusion protein)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltSGGPGPAGMKGLPGSggggsggggs ggggsggggsggggsggggsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVR QAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTA VYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSS LSASVGDRVTITCKASQNVGTNVGWYQQKPGKAPKALIYSASFRYSGVPSRFS GSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIKSGGPGPAGM KGLPGSEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLE WVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIG GSLSVSSQGTLVTVSSggggsggggsggggsQVQLQESGGGLVQAGGSLRLSCAASG RIFSIDIMSWYRQAPGKQRELVARITRGGTISYDDSVKGRFTISRDNAKNTVYL QMNSLKPEDTGVYYCNALYGTDYWGKGTQVTVSSHHHHHH</td>

<td> 56</td><td> ACP23 (IL2 fusion protein)</td><td> QVQLQESGGGLAQAGGSLSLSCAASGFTVSNSVMAWYRQIPGKQREFVAIIN SVGSTNYADSVKGRFTISRDNAKNTVYLQMNNLKPEDTAVYVCNRNFDRIY WGQGTQVTVSSSGGPGPAGMKGLPGSEVQLVESGGGLVQPGGSLRLSCAASG FTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLY LQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGG GGSDIQMTQSPSSLSASVGDRVTITCKASQNVGTNVGWYQQKPGKAPKALIYS ASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKV EIKggggsggggsggggsggggsggggsggggsSGGPGPAGMKGLPGSEVQLVESGGGLVQ PGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKG RFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSSGGPG PAGMKGLPGSaptssstkktqlqlehllldlqmilnginnyknpkltrmltfkfympkkatelkhlqcleeelkple evlnlaqsknfhlrprdlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltHHHHHH</td>

<td> 57</td><td> ACP24 (IL2 fusion protein) (WW0074)</td><td> EVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAID SSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDAL DYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCK ASQNVGTNVGWYQQKPGKAPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSL QPEDFATYYCQQYYTYPYTFGGGTKVEIKSGGPGPAGMKGLPGSaptssstkktqlql ehllldlqmilnginnyknpkltrmltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrprdlisnmvivlelk gsettfinceyadetativeflnrwitfcqsiistltHHHHHH</td>

<td> 58</td><td> ACP25 (IL2 fusion protein) (WW0075)</td><td> EVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAID SSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDAL DYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCK ASQNVGTNVGWYQQKPGKAPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSL QPEDFATYYCQQYYTYPYTFGGGTKVEIKggggsggggsggggsggggsggggsggggsSG GPGPAGMKGLPGSaptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleee IkpleevlnlaqsknfhlrprdlisninvivlelkgsettfinceyadetativeflnrwitfcqsiistltHHHHHH</td>

<td> 59</td><td> ACP26 (IL2 fusion protein)</td><td> QVQLQESGGGLVQAGGSLRLSCAASGRIFSIDIMSWYRQAPGKQRELVARITR GGTISYDDSVKGRFTISRDNAKNTVYLQMNSLKPEDTGVYYCNALYGTDYW GKGTQVTVSSggggsggggsggggsaptssstkktqlqlehllldlqmilnginnyknpkltrmltfkfympkk atelkhlqcleeelkpleevlnlaqsknfhlrprdlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltSG GPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQ APGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTA VYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggsggggsQVQLQQSGAELVRPGT SVKVSCKASGYAFTNYLIEWVKQRPGQGLEWIGVINPGSGGTNYNEKFKGKA TLTADKSSSTAYMQLSSLTSDDSAVYFCARWRGDGYYAYFDVWGAGTTVTV SSggggsggggsggggsDIVLTQSPASLAVSLGQRATISCKASQSVDYDGDSYMNWY QQKPGQPPKLLIYAASNLESGIPARFSGSGSGTDFTLNIHPVEEEDAATYYCQQ SNEDPYTFGGGTKLEIKHHHHHHEPEA</td>

<td> 60</td><td> ACP27 (IL2 fusion protein)</td><td> QVQLQESGGGLVQAGGSLRLSCAASGRIFSIDIMSWYRQAPGKQRELVARITR GGTISYDDSVKGRFTISRDNAKNTVYLQMNSLKPEDTGVYYCNALYGTDYW GKGTQVTVSSggggsggggsggggsaptssstkktqlqlehllldlqmilnginnyknpkltrmltfkfympkk atelkhlqcleeelkpleevlnlaqsknfhlrprdlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltSG GPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQ APGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTA VYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggsggggsDIVLTQSPASLAVSLG QRATISCKASQSVDYDGDSYMNWYQQKPGQPPKLLIYAASNLESGIPARFSGS GSGTDFTLNIHPVEEEDAAIYYCQQSNEDPYTFGGGTKLEIKggggsggggsggggs QVQLQQSGAELVRPGTSVKVSCKASGYAFTNYLIEWVKQRPGQGLEWIGVIN PGSGGTNYNEKFKGKATLTADKSSSTAYMQLSSLTSDDSAVYFCARWRGDG YYAYFDVWGAGTTVTVSSHHHHHHEPEA</td>

<td> 61</td><td> ACP28 (IL2 fusion protein)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltSGGPGPAGMKGLPGSggggsggggs ggggsggggsggggsQVQLQQSGAELVRPGTSVKVSCKASGYAFTNYLIEWVKQRP GQGLEWIGVINPGSGGTNYNEKFKGKATLTADKSSSTAYMQLSSLTSDDSAV YFCARWRGDGYYAYFDVWGAGTTVTVSSggggsggggsggggsDIVLTQSPASLAV SLGQRATISCKASQSVDYDGDSYMNWYQQKPGQPPKLLIYAASNLESGIPARF SGSGSGTDFTLNIHPVEEEDAATYYCQQSNEDPYTFGGGTKLEIKggggsggggsgg ggsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSS ISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSV SSQGTLVTVSSggggsggggsggggsQVQLQESGGGLVQAGGSLRLSCAASGRIFSID IMSWYRQAPGKQRELVARITRGGTISYDDSVKGRFTISRDNAKNTVYLQMNSL KPEDTGVYYCNALYGTDYWGKGTQVTVSSHHHHHHEPEA</td>

<td> 62</td><td> ACP29 (IL2 fusion protein)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltSGGPGPAGMKGLPGSggggsggggs ggggsggggsggggsDIVLTQSPASLAVSLGQRATISCKASQSVDYDGDSYMNWYQ QKPGQPPKLLIYAASNLESGIPARFSGSGSGTDFTLNIHPVEEEDAATYYCQQS NEDPYTFGGGTKLEIKggggsggggsggggsQVQLQQSGAELVRPGTSVKVSCKASG YAFTNYLIEWVKQRPGQGLEWIGVINPGSGGTNYNEKFKGKATLTADKSSST AYMQLSSLTSDDSAVYFCARWRGDGYYAYFDVWGAGTTVTVSSggggsggggsg gggsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVS SISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLS VSSQGTLVTVSSggggsggggsggggsQVQLQESGGGLVQAGGSLRLSCAASGRIFSI DIMSWYRQAPGKQRELVARITRGGTISYDDSVKGRFTISRDNAKNTVYLQMN SLKPEDTGVYYCNALYGTDYWGKGTQVTVSSHHHHHHEPEA</td>

<td> 63</td><td> IL2Ra</td><td> 10 20 30 40 50 MDSYLLMWGL LTFIMVPGCQ AELCDDDPPE IPHATFKAMA YKEGTMLNCE 60 70 80 90 100</td>

<td></td><td></td><td> CKRGFRRIKS GSLYMLCTGN SSHSSWDNQC QCTSSATRNT TKQVTPQPEE 110 120 130 140 150 QKERKTTEMQ SPMQPVDQAS LPGHCREPPP WENEATERIY HFWGQMVYY 160 170 180 190 200 QCVQGYRALH RGPAESVCKM THGKTRWTQP QLICTGEMET SQFPGEEKPQ 210 220 230 240 250 ASPEGRPESE TSCLVTTTDF QIQTEMAATM ETSIFTTEYQ VAVAGCVFLL 260 270 ISVLLLSGLT WQRRQRKSRR Tl</td>

<td rowspan="2"> 64</td><td rowspan="2"> IL2Rb</td><td> 10 20 30 40 50 MAAPALSWRL PLLILLLPLA TSWASAAVNG TSQFTCFYNS RANISCVWSQ 60 70 80 90 100 DGALQDTSCQ VHAWPDRRRW NQTCELLPVS QASWACNLIL GAPDSQKLTT 110 120 130 140 150 VDIVTLRVLC REGVRWRVMA IQDFKPFENL RLMAPISLQV VHVETHRCNI 160 170 180 190 200 SWEISQASHY FERHLEFEAR TLSPGHTWEE APLLTLKQKQ EWICLETLTP 210 220 230 240 250 DTQYEFQVRV KPLQGEFTTW SPWSQPLAFR TKPAALGKDTIPWLGHLLVG 260 270 280 290 300 LSGAFGFIIL VYLLINCRNT GPWLKKVLKC NTPDPSKFFS QLSSEHGGDV 310 320 330 340 350 QKWLSSPFPS SSFSPGGLAP EISPLEVLER DKVTQLLLQQ DKVPEPASLS 360 370 380 390 400 SNHSLTSCFT NQGYFFFHLP DALEIEACQV YFTYDPYSEE DPDEGVAGAP 410 420 430 440 450 TGSSPQPLQP LSGEDDAYCT FPSRDDLLLF SPSLLGGPSP PSTAPGGSGA 460 470 480 490 500 GEERMPPSLQ ERVPRDWDPQ PLGPPTPGVP DLVDFQPPPE LVLREAGEEV 510 520 530 540 550 PDAGPREGVS FPWSRPPGQG EFRALNARLP LNTDAYLSLQ ELQGQDPTHL V</td>

<td></td>

<td rowspan="2"> 65</td><td rowspan="2"> IL2Rg</td><td> 10 20 30 40 50 MLKPSLPFTS LLFLQLPLLG VGLNTTILTP NGNEDTTADF FLTTMPTDSL 60 70 80 90 100 SVSTLPLPEV QCFVFNVEYM NCTWNSSSEP QPTNLTLHYW YKNSDNDKVQ 110 120 130 140 150 KCSHYLFSEE ITSGCQLQKK EIHLYQTFW QLQDPREPRR QATQMLKLQN 160 170 180 190 200 LVIPWAPENL TLHKLSESQL ELNWNNRFLN HCLEHLVQYR TDWDHSWTEQ 210 220 230 240 250 SVDYRHKFSL PSVDGQKRYT FRVRSRFNPL CGSAQHWSEW SHPIHWGSNT 260 270 280 290 300 SKENPFLFAL EAWISVGSM GLIISLLCVY FWLERTMPRI PTLKNLEDLV 310 320 330 340 350 TEYHGNFSAW SGVSKGLAES LQPDYSERLC LVSEIPPKGG ALGEGPGASP 360 CNQHSPYWAP PCYTLKPET</td>

<td></td>

<td> 66</td><td> ACP04 (human p40/murine p35 IL12 fusion protein)</td><td> iwelkkdvyweldwypdapgemwltcdtpeedgitwtldqssevlgsgktltiqvkefgdagqytchkggevlshs llllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwlttistdltfsvkssrgssdpqgvtcgaatlsaervrgd nkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssffirdiikpdppknlqlkplknsrqvevsweypdt wstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvraqdryyssswsewasvpcsggggsggggsgg ggsrvipvsgparclsqsmllkttddmvktareklkhysctaedidheditrdqtstlktclplelhknesclatretssttrgs clppqktslmmtlclgsiyedlkmyqtefqainaalqnhnhqqiildkgmlvaidelmqslnhngetlrqkppvgead pyrvkmklcillhafstrvvtmrvmgylssaHHHHHH</td>

<td> 67</td><td> ACP05 (human p40/murine p35 IL12 fusion protein)</td><td> iwelkkdvyweldwypdapgemwltcdtpeedgitwtldqssevlgsgktltiqvkefgdagqytchkggevlshs llllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwlttistdltfsvkssrgssdpqgvtcgaatlsaervrgd nkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssffirdiikpdppknlqlkplknsrqvevsweypdt wstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvraqdryyssswsewasvpcsggggsggggsgg ggsmlpvatpdpgmfpclhhsqnllravsnmlqkarqtleiypctseeidheditkdktstveaclpleltknesclnsre tsfitngsclasrktsfinmalclssiyedlkmyqvefktmnakllmdpkrqifldqnmlavidelmqalnfiisetvpqk ssleepdfyktkiklcillhafriravtidrvmsylnasHHHHHH</td>

<td> 68</td><td> ACP06 (human p40/murine p35 IL12 fusion protein)</td><td> QSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQQLPGTAPKLLIYYNDQ RPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLFGTGTK VTVLggggsggggsggggsQVQLVESGGGVVQPGRSLRLSCAASGFTFSSYGMHWV RQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAE DTAVYYCKTHGSHDNWGQGTMVTVSSggggsggggsggggsggggsggggsggggsSGG PGPAGMKGLPGSiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqssevlgsgktltiqvkef gdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwlttistdltfsvkssrgssd pqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssffirdiikpdppknlql kplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvraqdryyssswsew asvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedidheditrdqtstlktcl plelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiildkgmlvaidelm qslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssaSGGPGPAGMKGLPGSEVQ LVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGR DTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGT LVTVSSHHHHHHEPEA</td>

<td> 69</td><td> ACP07 (human p40/murine p35 IL12 fusion protein)</td><td> QSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQQLPGTAPKLLIYYNDQ RPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLFGTGTK VTVLggggsggggsggggsQVQLVESGGGVVQPGRSLRLSCAASGFTFSSYGMHWV RQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAE DTAVYYCKTHGSHDNWGQGTMVTVSSggggsggggsggggsggggsggggsggggsSGG PGPAGMKGLPGSiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqssevlgsgktltiqvkef gdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwlttistdltfsvkssrgssd pqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssffirdiikpdppknlql kplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvraqdryyssswsew asvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedidheditrdqtstlktcl</td>

<td></td><td></td><td> plelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiildkgmlvaidelm qslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssaSGGPGPAGMKGLPGSEVQ LVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGR DTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGT LVTVSSggggsggggsggggsQVQLQESGGGLAQAGGSLSLSCAASGFTVSNSVMA WYRQTPGKQREFVAIINSVGSTNYADSVKGRFTISRDNAKNTVYLQMNNLKP EDTAVYVCNRNFDRIYWGQGTQVTVSSHHHHHHEPEA</td>

<td> 70</td><td> ACP08 (human p40/murine p35 IL12 fusion protein)</td><td> QVQLQESGGGLAQAGGSLSLSCAASGFTVSNSVMAWYRQTPGKQREFVAIIN SVGSTNYADSVKGRFTISRDNAKNTVYLQMNNLKPEDTAVYVCNRNFDRIY WGQGTQVTVSSggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNIGSN TVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAEDEA DYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGWQPG RSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYDGSNKYYADSVKG RFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVSSggg gsggggsggggsggggsggggsggggsSGGPGPAGMKGLPGSiwelkkdvyweldwypdapgemv vltcdtpeedgitwtldqssevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktf Irceaknysgrftcwwlttistdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpiev mvdavhklkyenytssffirdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdr vftdktsatvicrknasisvraqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttdd mvktareklkhysctaedidheditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkm yqtefqamaalqnhnhqqiildkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtinrv mgylssaSGGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFG MSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNS LRPEDTAVYYCTIGGSLSVSSQGTLVTVSSHHHHHHEPEA</td>

<td> 71</td><td> ACP09 (human p40/murine p35 IL12 fusion protein)</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTV KWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAEDEADY YCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGVVQPGRS LRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYDGSNKYYADSVKGRF TISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVSSggggsg gggsggggsggggsggggsggggsSGGPGPAGMKGLPGSiwelkkdvyweldwypdapgemwltc dtpeedgitwtldqssevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrce aknysgrftcwwlttistdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmv davhklkyenytssffirdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftd ktsatvicrknasisvraqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvkt areklkhysctaedidheditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtef qamaalqnhnhqqiildkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgyls saHHHHHHEPEA</td>

<td> 72</td><td> ACP10 (human p40/murine p35 IL12 fusion protein)</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPGPAGMKGLPGSiwelkkdvyweldwypdapgemwltcdtpeedgitwtl dqssevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcw wlttistdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyeny tssffirdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrkna sisvraqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhyscta edidheditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnh qqiildkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssaSGGPGPA GMKGLPGSggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCS GSRSNIGSNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAIT GLQAEDEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVES GGGVVQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYDGSNK YYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGT MVTVSSHHHHHHEPEA</td>

<td> 73</td><td> ACP11 (human p40/murine p35 IL12 fusion protein)</td><td> iwelkkdvyweldwypdapgemwltcdtpeedgitwtldqssevlgsgktltiqvkefgdagqytchkggevlshs llllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwlttistdltfsvkssrgssdpqgvtcgaatlsaervrgd nkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssffirdiikpdppknlqlkplknsrqvevsweypdt wstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvraqdryyssswsewasvpcsggggsggggsgg ggsrvipvsgparclsqsmllkttddmvktareklkhysctaedidheditrdqtstlktclplelhknesclatretssttrgs clppqktslmmtlclgsiyedlkmyqtefqainaalqnhnhqqiildkgmlvaidelmqslnhngetlrqkppvgead pyrvkmklcillhafstrwtmrvmgylssaSGGPGPAGMKGLPGSggggsggggsggggsggggsggg gsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQQLPGTAPKLLI YYNDQRPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLF GTGTKVTVLggggsggggsggggsQVQLVESGGGVVQPGRSLRLSCAASGFTFSSYG MHWVRQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMN SLRAEDTAVYYCKTHGSHDNWGQGTMVTVSSggggsggggsggggsEVQLVESGG GLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS HHHHHHEPEA</td>

<td> 74</td><td> IL12 p40 human (Uniprot Accession No. P29460)</td><td> IS 23 30 40 58 FSLVFLASPL ¥ΑΠ&amp;£Κ0¥ YWELDWPE! APGEHWLTC 60 70 8© 9© 188 DTPEEDGIT-4 TL^SSEVLG SGO1.TIQW EEGDAGQYTC H^GGEYiSHS lie 120 130 140 158 LLLLHITEDG IGSTSILKOQ CEAK^YSGRF TCi^UTIST 168 178 188 19© 288 DLTFSVKSSR GS5DPQGVTC GAATLSAERV RGD*E¥E¥S VECQE8SACP 22© 220 230 248 238 AAEESLPIEV ©WAWKLKY ENYTSSEEIS SIIKPKWl LQLKPL.K8SR 268 278 28© 290 3W QVEVSGEvPD TkSIPHWFS LTECVQW6Y 5KREKK9RVF TDKTSATVIC 310 32© ?MASIWA &lt;W¥S5SW5 EHA5VPCS</td>

<td> 75</td><td> IL12p35 mouse (Uniprot Accession No. P43431)</td><td> 10 20 3© 40 5© «QSRYL1.E1. ATLALLMHLS LARVIPVSGP ARCLS^Sm LKTT^IVKT 60 78 88 I© 100 AREKLKHYSC TAEDWHE&amp;I TRDQTSTLKT £LPLEU«E SCLATRETSS 110 120 13© 148 IS© 7TRGS0LPFQ CTSL0MTLCL GSIYEDLKHY QTEFQAIHAA LQfWTOII 168 178 188 198 20© LD8G0LVAI8 EL0QSL8H06 ETLRQKPPVG EADPYRVK« LCILLHAFST 218 RVVT180YHG Y1SSA</td>

<td> 76</td><td> IL12Rb-2</td><td> 50. 40 20־ ·1-G 5w» ®sm 80 7S 95 90 ISO 110. 125 :.&lt; 140 155 J®®® SW+^SioX 1.85 17S 193 195 2 35· 215 &lt;7 233 243 253 »asm »»1 κκ» 2, 54:- 27G- 20 G 23G . 3:0 5 .300 .. 3:20 :.330. 343. 303: XS^XSf 31 £»83־^ 353: S7S 333 :393 4 95 SUlSS+Sx &lt;Β7Ϊ® XXSSXglX 41.» 42 3 433 443 433 xa^41kX?£1 4€+ 473 433 493 £93 ®38־S^Xg VS^X^XX JSSSK 913 SIC SSC E49 ΕΪ9 3:00 . . 393. 530 ׳370. .3:50 . . . . ·ss^aw^· WW$. W&amp;W £U· 52g •^5 545 05c XZV0^7^ 54;5· x&gt;:u ׳:*״: TOO ’^ca* 7 V5·. 2?־G 72 g 7 40 7 50 -,&lt;&lt;&lt;15 &lt;&lt;?&lt; CT-f X I⁵’7 30מ ^ע : ;on· ^,: &gt; '· :,·מ·. ־QJR7A' 553 43« 33«; 433 3^5 ·^1χΚ5״11·H TSSlltyPl Τξ״:»,1:29 V &lt;-:· ·-</td>

<td> 77</td><td> IL12Rb-l</td><td> 19 23 39 49 SO SSPWTTT^^ LL^LmSES GX&amp;CS.TSZCC fS^PP^DAS ESSASEESSL €9 S3 go go 100 RCY&amp;ISSSEy ECSWiESPI AGVSHFLRCC LSSGRCCTFS. ESS.ET&amp;LSFS 11.9 129 ISO 140 ISO DiiaGVSVLYT ETLW£Ss?ER SSTKXSPSVT LSLESSVJOIE EELSOlKvSK 135 170 !go ISO 2s&amp; LSESLiSlSSE TEOfiaV'gXEY SERSS3ESSE WLSDCGP2© DSTE5CLCPL 213 225 233 245 2S5 5WSS.QXFQL EKESLGS&amp;SS SXSK&amp;’SSWC WSXNPPQPS V^FSW^LGG 235 270 ;go 290 300 SSSERITLEE QElSLELS'ES CQGLXP5T£V TYElQLHKLg CECEftSSTEl 313 325 333 345 350 LHLGEWYLS SE+IKESVIS S&amp;QFS^SK^ TWIX^DTHS EEmi.tJISVS 3S-5 375 388 388 450 ISiElTESSSs. RAQSliTSiSlE XaWG^DSGl A1CSLTS»QD EESASE&amp;TIS 41-3 42 3 433 4 43 450 itSEE-gSyiGS SXCTYITIEX SAHPSKLTL^ STVLXTYHFG GS&amp;S&amp;S.GTPH 433 475 485 495 350 HYSl'SKH'SsO gYSVSSAFSl LSTCFGVLKE 297־:aCR3ESS KQV5XHWGP· SIS E25 535 S43 £50 TXTSVTLSGL .SAGVMTWV SADXASLXSV S'£CP^:2P.?SIE ·toVSSlVIFF w»3 37 5 533 S 9 0 05 0 ASLGSXLSIL 1&gt;5¥15&gt;931 SEAaEKLCED LPTSC&amp;S2XI ESTGGXESW 919 923 835 645 SSO ®1WV8F0EE .^IQ'EALWE ΚΕΚΏΕΰΕΕΤΕ ?LEKTELSEG EPEIALSTEL 8 89 SSX&amp;SDaCXS. 231</td>

<td> 78</td><td> IL-12 p35 human (Uniprot accession no. P29459)</td><td> .1® 20 38 40 58 E.irt־[ *,A; 7® 8® -C 100 ΟΙΡΕ&amp;δόΠΚ TLQQSSEVLG EGOLJIQW EFGDAGQYTC HKGGEVLSHS 118 128 138 14® 15® ELLLAKEEEG Ub5T®IL6DQ K ΕΡΑΠΤΕ LR CEAK87S8RF Τ»1ΐΠ5Τ 18® 178 188 190 288 D1TFSWSSR 8SSDPQWTC SAATLSAERY RW^KEY.EYS YECQEESACP 21® 228 238 240 258 AAEESLPIEY WDAYMLEY MWFIR DIIK88PP^ LQtKPLKRSR 26® 270 290 28® 388 WVSUEW® T^STPHSYFS L1FCVQYW 5OERKDRW TBKTSATVXC 31® 328 8OASISVRA .QDRYYSS5HS EUASV8CS</td>

<td> 79</td><td> IL-12 p40 mouse (Uniprot accession no. P43432)</td><td> 19 28 38 48 5® HCRQKLTISls FAIVLLVSPL WWEIEK0V YWEVWTPD APSETWLTC δ® 70 88 99 18® DTPEE80GTR TSDQRHWIG SGKTLTITVK EFLDAGQYTC 8KGGETLSHS 118 128 13g 14® IE® H. j־ _t »’־: ftה ״ c ״ _x j; !״ . 18® 170 188 198 288 R^IKSSSSSP DWVTCmA 5LSAEKVTLD QSDYEKYSV5 GQEDVTCPTA 218 228 238 24® 25® EETLPIELAL EA8QQ®K¥E® VSTSFFIR8I IKPDFPKflLO RKPLKflSQVE 26® 278 288 290 38® :,1 - Η H. + 1 ״^- t r.' '-^,tr״ ς s. 31® 320 338 FEVQCEGGW EVQAOSRVVN SEC EKkACVP CRVR5</td>

<td> 80</td><td> ACP01 (mouse IFNg fusion protein)</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPGPAGMKGLPGShgtviesleslnnyfiissgidveekslfldiwmwqkdgdm kilqsqiisfylrlfevlkdnqaisnnisvieshlittffsnskakkdafmsiakfevnnpqvqrqafiielirwhqllpesslr krkrsrcSGGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFG MSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNS LRPEDTAVYYCTIGGSLSVSSQGTLVTVSSHHHHHH</td>

<td> 81</td><td> ACP02 (mouse IFNg</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPGPAGMKGLPGShgtviesleslnnyfiissgidveekslfldiwmwqkdgdm kilqsqiisfylrlfevlkdnqaisnnisvieshlittffsnskakkdafmsiakfevnnpqvqrqafiielirwhqllpesslr</td>

<td></td><td> fusion protein)</td><td> krkrsrcSGGPGPAGMKGLPGShgtviesleslnnyfiissgidveekslfldiwmwqkdgdmkilqsqiisf ylrlfevlkdnqaisnnisvieshlittfFsnskakkdafinsiakfevnnpqvqrqafiielirwhqllpesslrkrkrsrcS GGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVR QAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDT AVYYCTIGGSLSVSSQGTLVTVSSHHHHHH</td>

<td> 82</td><td> ACP03 (mouse IFNg fusion protein)</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPGPAGMKGLPGShgtviesleslnnyfiissgidveekslfldiwmwqkdgdm kilqsqiistylrlfevlkdnqaisnnisvieshlittffsnskakkdafmsiakfevnnpqvqrqafiielirwhqllpesslr krkrsrcggggsggggsggggshgtviesleslnnyfiissgidveekslfldiwmwqkdgdmkilqsqiisfylrlfevl kdnqaisnnisvieshlittffsnskakkdafmsiakfevnnpqvqrqafiielirwhqllpesslrkrkrsrcSGGPGP AGMKGLPGSEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGK GLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYC TIGGSLSVSSQGTLVTVSSHHHHHH</td>

<td> 83</td><td> Human IFN-g (Uniprot Accession No. P01579)</td><td> 10 2.0 30 40 SO 60 70 00 100 LFLGILMJUK QXVSFYUTF HIF1ODQSIQ ΓΞ\·ΈΤΙΓΞ0'4 11g 120 130 148' 458 WKFF8SFO KR&amp;DFFXLTO YSVWtiW KAIHELIQW AELSPMOG 160 KRRR LRR GRRASQ</td>

<td> 84</td><td> Mouse IFN-g (Uniprot Accession No. P01580)</td><td> IS is 30 48 58 mATHCILAL. QLFimVSGC YCHSTVIESL E5L1WFKS5 GIWEEK5LF 60 70 S® 90 100 GEOLKCSvI ISFYLRLFEV ISVIESHLIT HO 1:6 130 148 1S0 TFFSHSKMK DAFmiAKFE WHPQWQA F0ELI8WHQ LLPESSLRKR kRSRC</td>

<td> 85</td><td> ACP30 (mouse IFNg fusion protein)</td><td> mdmrvpaqllgllllwlrgarcEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVR QAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDT AVYYCTIGGSLSVSSQGTLVTVSSSGGPGPAGMKGLPGShgtviesleslnnyfiissgidv eekslfldiwmwqkdgdmkilqsqiisfylrlfevlkdnqaisnnisvieshlittfFsnskakkdafinsiakfevnnpq vqrqafiielirwhqllpesslrkrkrsrcSGGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLR LSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISR DNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSSGGPGPAGM KGLPGShgtviesleslnnyfiissgidveekslfldiwmwqkdgdmkilqsqiistylrlfevlkdnqaisnnisvie</td>

<td></td><td></td><td> shlittffsnskakkdafmsiakfevnnpqvqrqafiielirwhqllpesslrkrkrsrcSGGPGPAGMKGLPG SEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSHHHHHH</td>

<td> 86</td><td> ACP31 (mouse IFNal fusion protein)</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPGPAGMKGLPGScdlpqthnlmkraltllvqmrrlsplsclkdrkdfgipqekvd aqqikkaqaipvlseltqqilniftskdssaawnttlldsfcndlhqqlndlqgclmqqvgvqeipltqedallavrkyfhri tvylrekkhspcawewraevwralsssanvlgrlreekSGGPGPAGMKGLPGSEVQLVESGGGL VQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESV KGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSHH HHHHEPEA</td>

<td> 87</td><td> ACP32 (mouse IFNal fusion protein)</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPGPAGMKGLPGScdlpqthnlmkraltllvqmrrlsplsclkdrkdfgipqekvd aqqikkaqaipvlseltqqilniftskdssaawnttlldsfcndlhqqlndlqgclmqqvgvqeipltqedallavrkyfhri tvylrekkhspcawewraevwralsssanvSGGPGPAGMKGLPGSEVQLVESGGGLVQPGN SLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFT ISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSHHHHHHE PEA</td>

<td> 88</td><td> IFNgRl</td><td> 7$ £0 SO 170 SAYAKSEEFA IKIBTF&amp;PSV 315 225 235 245 295 S’a 1334. ^.1 2 93־ Ji' 1YLVTICEVT VP.5ATLETKP 31¢ 328 338 348| 358 ESKr/SLITS GOESTEELS 355 375 335 390 £90 י ^rV X’ S &lt;»' Ά .^,β* A *« to. Ah X. J Pvx te^ Arte A te. Ah te^.*C*.Xh tete hr. 'rw* .¢ Ah te ל 'ref te.' t te^ Ah A ^terArtete '־ל Srs Jte A te hX X&gt; £.15 42 9 433 445 430 1־3^··׳ϋ ϊίΈίϊ'Li2 ΏΤ532τ_'.Σ:,ίί. H X T s Σ 31</td>

IFNgR2

<td> 15</td><td> 3 5</td><td> 35</td><td> 45</td><td> SO</td>

<td></td><td colspan="2"></td><td></td><td> SSAEQVISS«:</td>

<td> «5</td><td> 75</td><td> 80</td><td> 35</td><td> ISO</td>

<td> SV&amp;LSSSTRS</td><td> WYQV-QFKYT</td><td> S' S KS' EX AS ΣΉ</td><td> SISs’SCTQIT</td><td></td>

<td> 115</td><td> 135</td><td> 135</td><td> 145</td><td> ΐϋ</td>

<td> g SA S^: EXli SFK</td><td> VILP.LKSSLG</td><td></td><td></td><td> SP2SSIEVTE</td>

<td> 110</td><td> 175</td><td> 188</td><td> :135</td><td></td>

<td> S ESS LX Σ STS</td><td> SPFDIADTST</td><td></td><td> Ξ υ.· E vQX XQ</td><td> PFRS&amp;’SISLS</td>

<td> 215</td><td> 225</td><td> 235</td><td> 240</td><td> 230</td>

<td> NLKSSSVYCL</td><td></td><td></td><td></td><td></td>

<td></td><td> 375</td><td> 288</td><td> 235</td><td> 500</td>

<td> ISVSTFELLS</td><td></td><td> LSYPSLlKy®</td><td></td><td></td>

<td> 315</td><td> 325</td><td> 335</td><td></td><td></td>

<td></td><td> SPKWWSSV</td><td> S11SFPS££3</td><td></td><td></td>

ACP51

Mouse IFG fusion protein

ACP52

Mouse IFG fusion protein

ACP53

Mouse IFG fusion protein

QVQLQESGGGLVQAGGSLRLSCAASGRIFSIDIMSWYRQAPGKQRELVARITR GGTISYDDSVKGRFTISRDNAKNTVYLQMNSLKPEDTGVYYCNALYGTDYW GKGTQVTVSSggggsggggsggggsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKF GMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMN SLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSSGGPGPAGMKGLPGShgtvieslesln nyfiissgidveekslfldiwmwqkdgdmkilqsqiisfylrlfevlkdnqaisnnisvieshlittffsnskakkdafmsi akfevnnpqvqrqafiielirwhqllpesslrkrkrsrcSGGPGPAGMKGLPGSEVQLVESGGGLV QPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVK GRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSHHH HHH

EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPGPAGMKGLPGShgtviesleslnnyfiissgidveekslfldiwmwqkdgdm kilqsqiisfylrlfevlkdnqaisnnisvieshlittffsnskakkdafmsiakfevnnpqvqrqafiielirwhqllpesslr krkrsrcSGGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFG MSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNS LRPEDTAVYYCTIGGSLSVSSQGTLVTVSSSGGPGPAGMKGLPGSEVQLVESG GGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLY AESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTV SSggggsggggsggggsQVQLQESGGGLVQAGGSLRLSCAASGRIFSIDIMSWYRQA PGKQRELVARITRGGTISYDDSVKGRFTISRDNAKNTVYLQMNSLKPEDTGVY YCNALYGTDYWGKGTQVTVSSHHHHHH eahkseiahryndlgeqhfkglvliafsqylqkcsydehaklvqevtdfaktcvadesaancdkslhtlfgdklcaipnlr enygeladcctkqepemecflqhkddnpslppferpeaeamctsfkenpttfinghylhevarrhpyiyapellyyaeq yneiltqccaeadkescltpkldgvkekalvssvrqrmkcssmqkfgerafkawavarlsqtipnadfaeitklatdltkv nkecchgdllecaddraelakymcenqatissklqtccdkpllkkahclsevehdtmpadlpaiaadfvedqevckny aeakdvflgtflyeysrrhpdysvslllrlakkyeatlekccaeanppacygtvlaefqplveepknlvktncdlyeklgey gfqnailvrytqkapqvstptlveaamlgrvgtkcctlpedqrlpcvedylsailnrvcllhektpvsehvtkccsgslver rpcfsaltvdetyvpkefkaetftfhsdictlpekekqikkqtalaelvkhkpkataeqlktvmddfaqfldtcckaadkdt cfstegpnlvtrckdalaSGGPGPAGMKGLPGShgtviesleslnnyfiissgidveekslfldiwmwqkdgd

<td></td><td></td><td> mkilqsqiisfylrlfevlkdnqaisnnisvieshlittffsnskakkdafmsiakfevnnpqvqrqafiielirwhqllpes slrkrkrsrcSGGPGPAGMKGLPGSeahkseiahryndlgeqhfkglvliafsqylqkcsydehaklvqevtd faktcvadesaancdkslhtlfgdklcaipnlrenygeladcctkqepemecflqhkddnpslppferpeaeamctsfk enpttfmghylhevarrhpyfyapellyyaeqyneiltqccaeadkescltpkldgvkekalvssvrqrmkcssmqkf gerafkawavarlsqtlpnadfaeitklatdltkvnkecchgdllecaddraelakymcenqatissklqtccdkpllkka hclsevehdtmpadlpaiaadfvedqevcknyaeakdvflgtflyeysrrhpdysvslllrlakkyeatlekccaeanpp acygtvlaefqplveepknlvktncdlyeklgeygfqnailvrytqkapqvstptlveaamlgrvgtkcctlpedqrlpcv edylsailnrvcllhektpvsehvtkccsgslverrpcfsaltvdetyvpkefkaetftfhsdictlpekekqikkqtalaelv khkpkataeqlktvmddfaqfldtcckaadkdtcfstegpnlvtrckdalaHHHHHH</td>

<td> 93</td><td> ACP54 Mouse IFG fusion protein</td><td> eahkseiahryndlgeqhfkglvliafsqylqkcsydehaklvqevtdfaktcvadesaancdkslhtlfgdklcaipnlr enygeladcctkqepemecflqhkddnpslppferpeaeamctsfkenpttfinghylhevarrhpyiyapellyyaeq yneiltqccaeadkescltpkldgvkekalvssvrqrmkcssmqkfgerafkawavarlsqtipnadfaeitklatdltkv nkecchgdllecaddraelakymcenqatissklqtccdkpllkkahclsevehdtmpadlpaiaadfvedqevckny aeakdvflgtflyeysrrhpdysvslllrlakkyeatlekccaeanppacygtvlaefqplveepknlvktncdlyeklgey gfqnailvrytqkapqvstptlveaamlgrvgtkcctlpedqrlpcvedylsailnrvcllhektpvsehvtkccsgslver rpcfsaltvdetyvpkefkaetftfhsdictlpekekqikkqtalaelvkhkpkataeqlktvmddfaqfldtcckaadkdt cfstegpnlvtrckdalaSGGPGPAGMKGLPGShgtviesleslnnyfiissgidveekslfldiwmwqkdgd mkilqsqiisfylrlfevlkdnqaisnnisvieshlittfFsnskakkdafinsiakfevnnpqvqrqafiielirwhqllpes slrkrkrsrcggggsggggsggggshgtviesleslnnyfiissgidveekslfldiwmwqkdgdmkilqsqiisiylrlf evlkdnqaisnnisvieshlittffsnskakkdafmsiakfevnnpqvqrqafiielirwhqllpesslrkrkrsrcSGGP GPAGMKGLPGSeahkseiahryndlgeqhfkglvliafsqylqkcsydehaklvqevtdfaktcvadesaanc dkslhtlfgdklcaipnlrenygeladcctkqepemecflqhkddnpslppferpeaeamctsfkenpttfmghylhev arrhpyfyapellyyaeqyneiltqccaeadkescltpkldgvkekalvssvrqrmkcssmqkfgerafkawavarlsq tipnadfaeitklatdltkvnkecchgdllecaddraelakymcenqatissklqtccdkpllkkahclsevehdtmpadl paiaadfvedqevcknyaeakdvflgtflyeysrrhpdysvslllrlakkyeatlekccaeanppacygtvlaefqplvee pknlvktncdlyeklgeygfqnailvrytqkapqvstptlveaamlgrvgtkcctlpedqrlpcvedylsailnrvcllhe ktpvsehvtkccsgslverrpcfsaltvdetyvpkefkaetftfhsdictlpekekqikkqtalaelvkhkpkataeqlktv mddfaqfldtcckaadkdtcfstegpnlvtrckdalaHHHHHH</td>

<td> 94</td><td> ACP50 Mouse IFG fusion protein</td><td> mdmrvpaqllgllllwlrgarcQVQLQESGGGLVQAGGSLRLSCAASGRIFSIDIMSWYR QAPGKQRELVARITRGGTISYDDSVKGRFTISRDNAKNTVYLQMNSLKPEDTG VYYCNALYGTDYWGKGTQVTVSSggggsggggsggggsEVQLVESGGGLVQPGNS LRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTI SRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSSGGPGPAG MKGLPGShgtviesleslnnyfiissgidveekslfldiwmwqkdgdmkilqsqiisiylrlfevlkdnqaisnnisv ieshlittffsnskakkdafmsiakfevnnpqvqrqafiielirwhqllpesslrkrkrsrcggggsggggsggggshgtv iesleslnnyfiissgidveekslfldiwmwqkdgdmkilqsqiisfylrlfevlkdnqaisnnisvieshlittfFsnskak kdafmsiakfevnnpqvqrqafiielirwhqllpesslrkrkrsrcSGGPGPAGMKGLPGSEVQLVES GGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTL YAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVT VSSHHHHHH</td>

<td> 95</td><td> ACP55</td><td> mdmrvpaqllgllllwlrgarcEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVR QAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDT AVYYCTIGGSLSVSSQGTLVTVSSSGGPGPAGMKGLPGShgtviesleslnnyfiissgidv eekslfldiwmwqkdgdmkilqsqiisiylrlfevlkdnqaisnnisvieshlittfFsnskakkdafinsiakfevnnpq vqrqafiielirwhqllpesslrkrkrsrcSGGPGPAGMKGLPGSEVOLVESGGGLVOPGNSLR</td>

<td></td><td> Mouse IFG fusion protein</td><td> LSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISR DNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSSGGPGPAGM KGLPGShgtviesleslnnyfiissgidveekslfldiwmwqkdgdmkilqsqiisfylrlfevlkdnqaisnnisvie shlittffsnskakkdafmsiakfevnnpqvqrqafhelirwhqllpesslrkrkrsrcSGGPGPAGMKGLPG SEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSHHHHHH</td>

<td> 96</td><td> ACP56 Mouse IFG fusion protein</td><td> mdmrvpaqllgllllwlrgarcQVQLQESGGGLAQAGGSLSLSCAASGFTVSNSVMAWY RQIPGKQREFVAIINSVGSTNYADSVKGRFTISRDNAKNTVYLQMNNLKPEDT AVYVCNRNFDRIYWGQGTQVTVSSggggsggggsggggsEVQLVESGGGLVQPGNS LRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTI SRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSSGGPGPAG MKGLPGShgtviesleslnnyfiissgidveekslfldiwmwqkdgdmkilqsqiisfylrlfevlkdnqaisnnisv ieshlittffsnskakkdafmsiakfevnnpqvqrqafiielirwhqllpesslrkrkrsrcSGGPGPAGMKGLP GSEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSS ISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSV SSQGTLVTVSSHHHHHHEPEA</td>

<td> 97</td><td> ACP57 Mouse IFG fusion protein</td><td> mdmrvpaqllgllllwlrgarcEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVR QAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDT AVYYCTIGGSLSVSSQGTLVTVSSSGGPGPAGMKGLPGShgtviesleslnnyfnssgidv eekslfldiwmwqkdgdmkilqsqiisfylrlfevlkdnqaisnnisvieshlittffsnskakkdafinsiakfevnnpq vqrqafiielirwhqllpesslrkrkrsrcSGGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLR LSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISR DNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsgggg sQVQLQESGGGLAQAGGSLSLSCAASGFTVSNSVMAWYRQTPGKQREFVAIIN SVGSTNYADSVKGRFTISRDNAKNTVYLQMNNLKPEDTAVYVCNRNFDRIY WGQGTQVTVSSHHHHHHEPEA</td>

<td> 98</td><td> ACP58 Mouse IFG fusion protein</td><td> mdmrvpaqllgllllwlrgarcEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVR QAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDT AVYYCTIGGSLSVSSQGTLVTVSSSGGPGPAGMKGLPGShgtviesleslnnyfnssgidv eekslfldiwmwqkdgdmkilqsqiisfylrlfevlkdnqaisnnisvieshlittffsnskakkdafinsiakfevnnpq vqrqafiielirwhqllpesslrkrkrsrcSGGPGPAGMKGLPGShgtviesleslnnyfiissgidveekslfldi wmwqkdgdmkilqsqiisfylrlfevlkdnqaisnnisvieshlittffsnskakkdafinsiakfevnnpqvqrqafiiel irwhqllpesslrkrkrsrcSGGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRLSCAAS GFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTT LYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggsQVQLQ ESGGGLVQAGGSLRLSCAASGRIFSIDIMSWYRQAPGKQRELVARITRGGTISY DDSVKGRFTISRDNAKNTVYLQMNSLKPEDTGVYYCNALYGTDYWGKGTQV TVSSHHHHHHEPEA</td>

<td> 99</td><td> ACP59 Mouse IFG fusion protein</td><td> mdmrvpaqllgllllwlrgarcQVQLQESGGGLAQAGGSLSLSCAASGFTVSNSVMAWY RQIPGKQREFVAIINSVGSTNYADSVKGRFTISRDNAKNTVYLQMNNLKPEDT AVYVCNRNFDRIYWGQGTQVTVSSggggsggggsggggsEVQLVESGGGLVQPGNS LRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTI SRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSSGGPGPAG MKGLPGShgtviesleslnnyfiissgidveekslfldiwmwqkdgdmkilqsqiisfylrlfevlkdnqaisnnisv ieshlittffsnskakkdafmsiakfevnnpqvqrqafiielirwhqllpesslrkrkrsrcSGGPGPAGMKGLP GShgtviesleslnnyfiissgidveekslfldiwmwqkdgdmkilqsqiisfylrlfevlkdnqaisnnisvieshlittff snskakkdafmsiakfevnnpqvqrqafnelirwhqllpesslrkrkrsrcSGGPGPAGMKGLPGSEVQ LVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGR DTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGT LVTVSSHHHHHHEPEA</td>

<td> 100</td><td> ACP60 Mouse IFG fusion protein</td><td> mdmrvpaqllgllllwlrgarcEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVR QAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDT AVYYCTIGGSLSVSSQGTLVTVSSSGGPGPAGMKGLPGShgtviesleslnnyfnssgidv eekslfldiwmwqkdgdmkilqsqiisfylrlfevlkdnqaisnnisvieshlittffsnskakkdafinsiakfevnnpq vqrqafiielirwhqllpesslrkrkrsrcSGGPGPAGMKGLPGShgtviesleslnnyfiissgidveekslfldi wmwqkdgdmkilqsqiisfylrlfevlkdnqaisnnisvieshlittffsnskakkdafinsiakfevnnpqvqrqafiiel irwhqllpesslrkrkrsrcSGGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRLSCAAS</td>

<td></td><td></td><td> GFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTT LYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggsQVQLQ ESGGGLAQAGGSLSLSCAASGFTVSNSVMAWYRQTPGKQREFVAIINSVGSTN YADSVKGRFTISRDNAKNTVYLQMNNLKPEDTAVYVCNRNFDRIYWGQGTQ VTVSSHHHHHHEPEA</td>

<td> 101</td><td> ACP61 Mouse IFG fusion protein</td><td> mdmrvpaqllgllllwlrgarcEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVR QAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDT AVYYCTIGGSLSVSSQGTLVTVSSSGGPGPAGMKGLPGShgtviesleslnnyfiissgidv eekslfldiwmwqkdgdmkilqsqiisfylrlfevlkdnqaisnnisvieshlittffsnskakkdafinsiakfevnnpq vqrqafiielirwhqllpesslrkrkrsrcSGGPGPAGMKGLPGShgtviesleslnnyfiissgidveekslfldi wmwqkdgdmkilqsqiisfylrlfevlkdnqaisnnisvieshlittffsnskakkdafinsiakfevnnpqvqrqafiiel irwhqllpesslrkrkrsrcSGGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRLSCAAS GFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTT LYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggsEVQLV ESGGGLVQPGGSLRLSCAASGFTFSSYAMSWVRQAPGKGLEWVSAISGSGGS TYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARGVGAFRPYRKH EWGQGTLVTVSRggggsggggsggggsSSELTQDPAVSVALGQTVRITCQGDSLRSY YASWYQQKPGQAPVLVIYGKNNRPSGIPDRFSGSSSGNTASLTTTGAQAEDEA DYYCNSSPFEHNLWFGGGTKLTVLHHHHHHEPEA</td>

<td> 102</td><td> ACP63 Anti-FN CGS-2 scFv</td><td> mdmrvpaqllgllllwlrgarcEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYAMSWVR QAPGKGLEWVSAISGSGGSTYYADSVKGRFTISRDNSKNTLYLQMNSLRAED TAVYYCARGVGAFRPYRKHEWGQGTLVTVSRggggsggggsggggsSSELTQDPAV SVALGQTVRITCQGDSLRSYYASWYQQKPGQAPVLVIYGKNNRPSGIPDRFSG SSSGNTASLTTTGAQAEDEADYYCNSSPFEHNLWFGGGTKLTVLHHHHHHE PEA</td>

<td> 103</td><td> ACP69 Mouse IFG fusion protein</td><td> mdmrvpaqllgllllwlrgarcEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVR QAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDT AVYYCTIGGSLSVSSQGTLVTVSSSGGPGPAGMKGLPGShgtviesleslnnyfiissgidv eekslfldiwmwqkdgdmkilqsqiisfylrlfevlkdnqaisnnisvieshlittffsnskakkdafinsiakfevnnpq vqrqafiielirwhqllpesslrkrkrsrcSGGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLR LSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISR DNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSSGGPGPAGM KGLPGShgtviesleslnnyfiissgidveekslfldiwmwqkdgdmkilqsqiisfylrlfevlkdnqaisnnisvie shlittffsnskakkdafinsiakfevnnpqvqrqafiielirwhqllpesslrkrkrsrcHHHHHHEPEA</td>

<td> 104</td><td> ACP70 Mouse IFG fusion protein</td><td> mdmrvpaqllgllllwlrgarchgtviesleslnnyfiissgidveekslfldiwmwqkdgdmkilqsqiisiylrlfevlk dnqaisnnisvieshlittffsnskakkdafmsiakfevnnpqvqrqafiielirwhqllpesslrkrkrsrcSGGPGP AGMKGLPGSEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGK GLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYC TIGGSLSVSSQGTLVTVSSSGGPGPAGMKGLPGShgtviesleslnnyfiissgidveekslfldi wmwqkdgdmkilqsqiisfylrlfevlkdnqaisnnisvieshlittffsnskakkdafinsiakfevnnpqvqrqafiiel irwhqllpesslrkrkrsrcSGGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRLSCAAS GFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTT LYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSHHHHHHEPEA</td>

<td> 105</td><td> ACP71 Mouse IFG fusion protein</td><td> mdmrvpaqllgllllwlrgarchgtviesleslnnyfiissgidveekslfldiwmwqkdgdmkilqsqiisiylrlfevlk dnqaisnnisvieshlittffsnskakkdafmsiakfevnnpqvqrqafiielirwhqllpesslrkrkrsrcSGGPGP AGMKGLPGSEAHKSEIAHRYNDLGEQHFKGLVLIAFSQYLQKCSYDEHAKLV QEVTDFAKTCVADESAANCDKSLHTLFGDKLCAIPNLRENYGELADCCTKQE PERNECFLQHKDDNPSLPPFERPEAEAMCTSFKENPTTFMGHYLHEVARRHPY FYAPELLYYAEQYNEILTQCCAEADKESCLTPKLDGVKEKALVSSVRQRMKC SSMQKFGERAFKAWAVARLSQTFPNADFAEITKLATDLTKVNKECCHGDLLE CADDRAELAKYMCENQATISSKLQTCCDKPLLKKAHCLSEVEHDTMPADLPA IAADFVEDQEVCKNYAEAKDVFLGTFLYEYSRRHPDYSVSLLLRLAKKYEAT LEKCCAEANPPACYGTVLAEFQPLVEEPKNLVKTNCDLYEKLGEYGFQNAILV RYTQKAPQVSTPTLVEAARNLGRVGTKCCTLPEDQRLPCVEDYLSAILNRVCL LHEKTPVSEHVTKCCSGSLVERRPCFSALTVDETYVPKEFKAETFTFHSDICTL PEKEKQIKKQTALAELVKHKPKATAEQLKTVMDDFAQFLDTCCKAADKDTCF STEGPNLVTRCKDALASGGPGPAGMKGLPGShgtviesleslnnyfiissgidveekslfldiwm wqkdgdmkilqsqiislylrlfevlkdnqaismiisvieshlittffsnskakkdafmsiakfevmipqvqrqafiielirv</td>

<td></td><td></td><td> vhqllpesslrkrkrsrcSGGPGPAGMKGLPGSEAHKSEIAHRYNDLGEQHFKGLVLIAF SQYLQKCSYDEHAKLVQEVTDFAKTCVADESAANCDKSLHTLFGDKLCAIPN LRENYGELADCCTKQEPERNECFLQHKDDNPSLPPFERPEAEAMCTSFKENPT TFMGHYLHEVARRHPYFYAPELLYYAEQYNEILTQCCAEADKESCLTPKLDG VKEKALVSSVRQRMKCSSMQKFGERAFKAWAVARLSQTFPNADFAEITKLAT DLTKVNKECCHGDLLECADDRAELAKYMCENQATISSKLQTCCDKPLLKKAH CLSEVEHDTMPADLPAIAADFVEDQEVCKNYAEAKDVFLGTFLYEYSRRHPD YSVSLLLRLAKKYEATLEKCCAEANPPACYGTVLAEFQPLVEEPKNLVKTNC DLYEKLGEYGFQNAILVRYTQKAPQVSIPTLVEAARNLGRVGTKCCTLPEDQ RLPCVEDYLSAILNRVCLLHEKIPVSEHVTKCCSGSLVERRPCFSALTVDEIYV PKEFKAETFTFHSDICTLPEKEKQIKKQTALAELVKHKPKATAEQLKTVMDDF AQFLDTCCKAADKDTCFSTEGPNLVTRCKDALAHHHHHHEPEA</td>

<td> 106</td><td> ACP72 Mouse IFG fusion protein</td><td> mdmrvpaqllgllllwlrgarcEAHKSEIAHRYNDLGEQHFKGLVLIAFSQYLQKCSYDE HAKLVQEVTDFAKTCVADESAANCDKSLHTLFGDKLCAIPNLRENYGELADC CTKQEPERNECFLQHKDDNPSLPPFERPEAEAMCTSFKENPTTFMGHYLHEVA RRHPYFYAPELLYYAEQYNEILTQCCAEADKESCLTPKLDGVKEKALVSSVRQ RMKCSSMQKFGERAFKAWAVARLSQTFPNADFAEITKLATDLTKVNKECCH GDLLECADDRAELAKYMCENQATISSKLQTCCDKPLLKKAHCLSEVEHDTMP ADLPAIAADFVEDQEVCKNYAEAKDVFLGTFLYEYSRRHPDYSVSLLLRLAK KYEATLEKCCAEANPPACYGTVLAEFQPLVEEPKNLVKTNCDLYEKLGEYGF QNAILVRYTQKAPQVSIPTLVEAARNLGRVGTKCCTLPEDQRLPCVEDYLSAI LNRVCLLHEKIPVSEHVTKCCSGSLVERRPCFSALTVDETYVPKEFKAETFTFH SDICTLPEKEKQIKKQTALAELVKHKPKATAEQLKTVMDDFAQFLDTCCKAA DKDTCFSTEGPNLVTRCKDALASGGPGPAGMKGLPGShgtviesleslnnyfhssgidvee kslfldiwmwqkdgdmkilqsqiisfylrlfevlkdnqaisiinisvieshlittffsnskakkdafinsiakfevnnpqvq rqafiielirwhqllpesslrkrkrsrcSGGPGPAGMKGLPGSEAHKSEIAHRYNDLGEQHFK GLVLIAFSQYLQKCSYDEHAKLVQEVTDFAKTCVADESAANCDKSLHTLFGD KLCAIPNLRENYGELADCCTKQEPERNECFLQHKDDNPSLPPFERPEAEAMCT SFKENPTTFMGHYLHEVARRHPYFYAPELLYYAEQYNEILTQCCAEADKESCL TPKLDGVKEKALVSSVRQRMKCSSMQKFGERAFKAWAVARLSQTFPNADFA EITKLATDLTKVNKECCHGDLLECADDRAELAKYMCENQATISSKLQTCCDK PLLKKAHCLSEVEHDTMPADLPAIAADFVEDQEVCKNYAEAKDVFLGTFLYE YSRRHPDYSVSLLLRLAKKYEATLEKCCAEANPPACYGTVLAEFQPLVEEPKN LVKTNCDLYEKLGEYGFQNAILVRYTQKAPQVSIPTLVEAARNLGRVGTKCC TLPEDQRLPCVEDYLSAILNRVCLLHEKTPVSEHVTKCCSGSLVERRPCFSALT VDETYVPKEFKAETFTFHSDICTLPEKEKQIKKQTALAELVKHKPKATAEQLK TVMDDFAQFLDTCCKAADKDTCFSTEGPNLVTRCKDALASGGPGPAGMKGL PGShgtviesleslnnyfiissgidveekslfldiwmwqkdgdmkilqsqiisfylrlfevlkdnqaisnnisvieshlitt fFsnskakkdafinsiakfevnnpqvqrqafiielirwhqllpesslrkrkrsrcHHHHHHEPEA</td>

<td> 107</td><td> ACP73 Mouse IFG fusion protein</td><td> mdmrvpaqllgllllwlrgarcEAHKSEIAHRYNDLGEQHFKGLVLIAFSQYLQKCSYDE HAKLVQEVTDFAKTCVADESAANCDKSLHTLFGDKLCAIPNLRENYGELADC CTKQEPERNECFLQHKDDNPSLPPFERPEAEAMCTSFKENPTTFMGHYLHEVA RRHPYFYAPELLYYAEQYNEILTQCCAEADKESCLTPKLDGVKEKALVSSVRQ RMKCSSMQKFGERAFKAWAVARLSQTFPNADFAEITKLATDLTKVNKECCH GDLLECADDRAELAKYMCENQATISSKLQTCCDKPLLKKAHCLSEVEHDTMP ADLPAIAADFVEDQEVCKNYAEAKDVFLGTFLYEYSRRHPDYSVSLLLRLAK KYEATLEKCCAEANPPACYGTVLAEFQPLVEEPKNLVKTNCDLYEKLGEYGF QNAILVRYTQKAPQVSIPTLVEAARNLGRVGTKCCTLPEDQRLPCVEDYLSAI LNRVCLLHEKIPVSEHVTKCCSGSLVERRPCFSALTVDETYVPKEFKAETFTFH SDICTLPEKEKQIKKQTALAELVKHKPKATAEQLKTVMDDFAQFLDTCCKAA DKDTCFSTEGPNLVTRCKDALASGGPGPAGMKGLPGShgtviesleslnnyfhssgidvee kslfldiwmwqkdgdmkilqsqiisfylrlfevlkdnqaisnnisvieshlittfFsnskakkdafinsiakfevnnpqvq rqafiielirwhqllpesslrkrkrsrcSGGPGPAGMKGLPGSEAHKSEIAHRYNDLGEQHFK GLVLIAFSQYLQKCSYDEHAKLVQEVTDFAKTCVADESAANCDKSLHTLFGD KLCAIPNLRENYGELADCCTKQEPERNECFLQHKDDNPSLPPFERPEAEAMCT SFKENPTTFMGHYLHEVARRHPYFYAPELLYYAEQYNEILTQCCAEADKESCL TPKLDGVKEKALVSSVRQRMKCSSMQKFGERAFKAWAVARLSQTFPNADFA EITKLATDLTKVNKECCHGDLLECADDRAELAKYMCENQATISSKLQTCCDK PLLKKAHCLSEVEHDTMPADLPAIAADFVEDQEVCKNYAEAKDVFLGTFLYE</td>

<td></td><td></td><td> YSRRHPDYSVSLLLRLAKKYEATLEKCCAEANPPACYGTVLAEFQPLVEEPKN LVKTNCDLYEKLGEYGFQNAILVRYTQKAPQVSIPTLVEAARNLGRVGTKCC TLPEDQRLPCVEDYLSAILNRVCLLHEKTPVSEHVTKCCSGSLVERRPCFSALT VDETYVPKEFKAETFTFHSDICTLPEKEKQIKKQTALAELVKHKPKATAEQLK TVMDDFAQFLDTCCKAADKDTCFSTEGPNLVTRCKDALASGGPGPAGMKGL PGShgtviesleslnnyfiissgidveekslfldiwmwqkdgdmkilqsqiisfylrlfevlkdnqaisnnisvieshlitt ffsnskakkdafmsiakfevnnpqvqrqafiielirwhqllpesslrkrkrsrcSGGPGPAGMKGLPGSEA HKSEIAHRYNDLGEQHFKGLVLIAFSQYLQKCSYDEHAKLVQEVTDFAKTCV ADESAANCDKSLHTLFGDKLCAIPNLRENYGELADCCTKQEPERNECFLQHK DDNPSLPPFERPEAEAMCTSFKENPTTFMGHYLHEVARRHPYFYAPELLYYAE QYNEILTQCCAEADKESCLTPKLDGVKEKALVSSVRQRMKCSSMQKFGERAF KAWAVARLSQTFPNADFAEITKLATDLTKVNKECCHGDLLECADDRAELAKY MCENQATISSKLQTCCDKPLLKKAHCLSEVEHDTMPADLPAIAADFVEDQEV CKNYAEAKDVFLGTFLYEYSRRHPDYSVSLLLRLAKKYEATLEKCCAEANPP ACYGTVLAEFQPLVEEPKNLVKTNCDLYEKLGEYGFQNAILVRYTQKAPQVS TPTLVEAARNLGRVGTKCCTLPEDQRLPCVEDYLSAILNRVCLLHEKTPVSEH VTKCCSGSLVERRPCFSALTVDETYVPKEFKAETFTFHSDICTLPEKEKQIKKQ TALAELVKHKPKATAEQLKTVMDDFAQFLDTCCKAADKDTCFSTEGPNLVTR CKDALAHHHHHHEPEA</td>

<td> 108</td><td> ACP74 Mouse IFG fusion protein</td><td> mdmrvpaqllgllllwlrgarcEAHKSEIAHRYNDLGEQHFKGLVLIAFSQYLQKCSYDE HAKLVQEVTDFAKTCVADESAANCDKSLHTLFGDKLCAIPNLRENYGELADC CTKQEPERNECFLQHKDDNPSLPPFERPEAEAMCTSFKENPTTFMGHYLHEVA RRHPYFYAPELLYYAEQYNEILTQCCAEADKESCLTPKLDGVKEKALVSSVRQ RMKCSSMQKFGERAFKAWAVARLSQTFPNADFAEITKLATDLTKVNKECCH GDLLECADDRAELAKYMCENQATISSKLQTCCDKPLLKKAHCLSEVEHDTMP ADLPAIAADFVEDQEVCKNYAEAKDVFLGTFLYEYSRRHPDYSVSLLLRLAK KYEATLEKCCAEANPPACYGTVLAEFQPLVEEPKNLVKTNCDLYEKLGEYGF QNAILVRYTQKAPQVSIPTLVEAARNLGRVGTKCCTLPEDQRLPCVEDYLSAI LNRVCLLHEKIPVSEHVTKCCSGSLVERRPCFSALTVDETYVPKEFKAETFTFH SDICTLPEKEKQIKKQTALAELVKHKPKATAEQLKTVMDDFAQFLDTCCKAA DKDTCFSTEGPNLVTRCKDALASGGPGPAGMKGLPGShgtviesleslnnyfiissgidvee kslfldiwmwqkdgdmkilqsqiisfylrlfevlkdnqaisnnisvieshlittfFsnskakkdafinsiakfevnnpqvq rqafiielirwhqllpesslrkrkrsrcSGGPGPAGMKGLPGSggggsEAHKSEIAHRYNDLGEQ HFKGLVLIAFSQYLQKCSYDEHAKLVQEVTDFAKTCVADESAANCDKSLHTL FGDKLCAIPNLRENYGELADCCTKQEPERNECFLQHKDDNPSLPPFERPEAEA MCTSFKENPTTFMGHYLHEVARRHPYFYAPELLYYAEQYNEILTQCCAEADK ESCLTPKLDGVKEKALVSSVRQRMKCSSMQKFGERAFKAWAVARLSQTFPN ADFAEITKLATDLTKVNKECCHGDLLECADDRAELAKYMCENQATISSKLQT CCDKPLLKKAHCLSEVEHDTMPADLPAIAADFVEDQEVCKNYAEAKDVFLGT FLYEYSRRHPDYSVSLLLRLAKKYEATLEKCCAEANPPACYGTVLAEFQPLVE EPKNLVKTNCDLYEKLGEYGFQNAILVRYTQKAPQVSTPTLVEAARNLGRVG TKCCTLPEDQRLPCVEDYLSAILNRVCLLHEKIPVSEHVTKCCSGSLVERRPCF SALTVDETYVPKEFKAETFTFHSDICTLPEKEKQIKKQTALAELVKHKPKATAE QLKTVMDDFAQFLDTCCKAADKDTCFSTEGPNLVIRCKDALAggggsSGGPGP AGMKGLPGShgtviesleslnnyfiissgidveekslfldiwmwqkdgdmkilqsqiisfylrlfevlkdnqaisn msvieshlittffsnskakkdafmsiakfevnnpqvqrqafhelirwhqllpesslrkrkrsrcSGGPGPAGMK GLPGSEAHKSEIAHRYNDLGEQHFKGLVLIAFSQYLQKCSYDEHAKLVQEVTD FAKTCVADESAANCDKSLHTLFGDKLCAIPNLRENYGELADCCTKQEPERNEC FLQHKDDNPSLPPFERPEAEAMCTSFKENPTTFMGHYLHEVARRHPYFYAPEL LYYAEQYNEILTQCCAEADKESCLTPKLDGVKEKALVSSVRQRMKCSSMQKF GERAFKAWAVARLSQTFPNADFAEITKLATDLTKVNKECCHGDLLECADDRA ELAKYMCENQATISSKLQTCCDKPLLKKAHCLSEVEHDIMPADLPAIAADFVE DQEVCKNYAEAKDVFLGTFLYEYSRRHPDYSVSLLLRLAKKYEATLEKCCAE ANPPACYGTVLAEFQPLVEEPKNLVKTNCDLYEKLGEYGFQNAILVRYTQKA PQVSTPTLVEAARNLGRVGTKCCTLPEDQRLPCVEDYLSAILNRVCLLHEKIP VSEHVTKCCSGSLVERRPCFSALTVDETYVPKEFKAETFTFHSDICTLPEKEKQI KKQTALAELVKHKPKATAEQLKTVMDDFAQFLDTCCKAADKDTCFSTEGPN LVTRCKDALAHHHHHHEPEA</td>

<td> 109</td><td> ACP75 Mouse IFG fusion protein</td><td> mdmrvpaqllgllllwlrgarcEAHKSEIAHRYNDLGEQHFKGLVLIAFSQYLQKCSYDE HAKLVQEVTDFAKTCVADESAANCDKSLHTLFGDKLCAIPNLRENYGELADC CTKQEPERNECFLQHKDDNPSLPPFERPEAEAMCTSFKENPTTFMGHYLHEVA RRHPYFYAPELLYYAEQYNEILTQCCAEADKESCLTPKLDGVKEKALVSSVRQ RMKCSSMQKFGERAFKAWAVARLSQTFPNADFAEITKLATDLTKVNKECCH GDLLECADDRAELAKYMCENQATISSKLQTCCDKPLLKKAHCLSEVEHDIMP ADLPAIAADFVEDQEVCKNYAEAKDVFLGTFLYEYSRRHPDYSVSLLLRLAK KYEATLEKCCAEANPPACYGTVLAEFQPLVEEPKNLVKTNCDLYEKLGEYGF QNAILVRYTQKAPQVSTPTLVEAARNLGRVGTKCCTLPEDQRLPCVEDYLSAI LNRVCLLHEKTPVSEHVTKCCSGSLVERRPCFSALTVDETYVPKEFKAETFTFH SDICTLPEKEKQIKKQTALAELVKHKPKATAEQLKTVMDDFAQFLDTCCKAA DKDTCFSTEGPNLVTRCKDALASGGPGPAGMKGLPGShgtviesleslnnyfiissgidvee kslfldiwmwqkdgdmkilqsqiisfylrlfevlkdnqaisnnisvieshlittffsnskakkdafinsiakfevnnpqvq rqafiielirwhqllpesslrkrkrsrcSGGPGPAGMKGLPGSggggsggggsEAHKSEIAHRYND LGEQHFKGLVLIAFSQYLQKCSYDEHAKLVQEVTDFAKTCVADESAANCDKS LHTLFGDKLCAIPNLRENYGELADCCTKQEPERNECFLQHKDDNPSLPPFERPE AEAMCTSFKENPTTFMGHYLHEVARRHPYFYAPELLYYAEQYNEILTQCCAE ADKESCLTPKLDGVKEKALVSSVRQRMKCSSMQKFGERAFKAWAVARLSQT FPNADFAEITKLATDLTKVNKECCHGDLLECADDRAELAKYMCENQATISSKL QTCCDKPLLKKAHCLSEVEHDTMPADLPAIAADFVEDQEVCKNYAEAKDVFL GTFLYEYSRRHPDYSVSLLLRLAKKYEATLEKCCAEANPPACYGTVLAEFQPL VEEPKNLVKTNCDLYEKLGEYGFQNAILVRYTQKAPQVSTPTLVEAARNLGR VGTKCCTLPEDQRLPCVEDYLSAILNRVCLLHEKTPVSEHVTKCCSGSLVERR PCFSALTVDETYVPKEFKAETFTFHSDICTLPEKEKQIKKQTALAELVKHKPKA TAEQLKTVMDDFAQFLDTCCKAADKDTCFSTEGPNLVTRCKDALAggggsgggg sSGGPGPAGMKGLPGShgtviesleslnnyfiissgidveekslfldiwmwqkdgdmkilqsqiisfylrlfe vlkdnqaisnnisvieshlittffsnskakkdafinsiakfevnnpqvqrqafhelirwhqllpesslrkrkrsrcSGGP GPAGMKGLPGSEAHKSEIAHRYNDLGEQHFKGLVLIAFSQYLQKCSYDEHAK LVQEVTDFAKTCVADESAANCDKSLHTLFGDKLCAIPNLRENYGELADCCTK QEPERNECFLQHKDDNPSLPPFERPEAEAMCTSFKENPTTFMGHYLHEVARRH PYFYAPELLYYAEQYNEILTQCCAEADKESCLTPKLDGVKEKALVSSVRQRM KCSSMQKFGERAFKAWAVARLSQTFPNADFAEITKLATDLTKVNKECCHGDL LECADDRAELAKYMCENQATISSKLQTCCDKPLLKKAHCLSEVEHDIMPADL PAIAADFVEDQEVCKNYAEAKDVFLGTFLYEYSRRHPDYSVSLLLRLAKKYE ATLEKCCAEANPPACYGTVLAEFQPLVEEPKNLVKTNCDLYEKLGEYGFQNAI LVRYTQKAPQVSTPTLVEAARNLGRVGTKCCTLPEDQRLPCVEDYLSAILNRV CLLHEKTPVSEHVTKCCSGSLVERRPCFSALTVDETYVPKEFKAETFTFHSDIC TLPEKEKQIKKQTALAELVKHKPKATAEQLKTVMDDFAQFLDTCCKAADKDT CFSTEGPNLVTRCKDALAHHHHHHEPEA</td>

<td> 110</td><td> ACP78 Mouse IFG fusion protein</td><td> mdmrvpaqllgllllwlrgarcEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVR QAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDT AVYY CTIGGSLS VSSQGTLVTVS Sggggsggggsggggshgtviesleslnnyfiissgidveekslfld iwmwqkdgdmkilqsqiisfylrlfevlkdnqaisnnisvieshlittffsnskakkdafinsiakfevnnpqvqrqafiie lirwhqllpesslrkrkrsrcggggsggggsggggsEVQLVESGGGLVQPGNSLRLSCAASGFTF SKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYL QMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggshgtviesleslnn yfhssgidveekslfldiwmwqkdgdmkilqsqiisfylrlfevlkdnqaismiisvieshlittffsnskakkdafmsia kfevnnpqvqrqafiielirwhqllpesslrkrkrsrcggggsggggsggggsEVQLVESGGGLVQPGNS LRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTI SRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSHHHHHHEP EA</td>

<td> 111</td><td> ACP134 Mouse IFG fusion protein</td><td> mdmrvpaqllgllllwlrgarcEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVR QAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDT AVYYCTIGGSLSVSSQGTLVTVSSSGGPGPAGMKGLPGShgtviesleslnnyfhssgidv eekslfldiwmwqkdgdmkilqsqiisfylrlfevlkdnqaisnnisvieshlittffsnskakkdafinsiakfevnnpq vqrqafiielirwhqllpesslrkrkrsrcSGGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLR LSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISR DNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSSGGPGPAGM KGLPGShgtviesleslnnyfiissgidveekslfldiwmwqkdgdmkilqsqiislylrlfevlkdnqaisnnisvie</td>

<td></td><td></td><td> shlittffsnskakkdafmsiakfevnnpqvqrqafiielirwhqllpesslrkrkrsrcSGGPGPAGMKGLPG SEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSggggsggggsggggsQVQLQESGGGLAQAGGSLSLSCAASGFTVSNS VMAWYRQTPGKQREFVAIINSVGSTNYADSVKGRFTISRDNAKNTVYLQMNN LKPEDTAVYVCNRNFDRIYWGQGTQVTVSSHHHHHHEPEA</td>

<td> 112</td><td> ACP135 Mouse IFG fusion protein</td><td> mdmrvpaqllgllllwlrgarcQVQLQESGGGLAQAGGSLSLSCAASGFTVSNSVMAWY RQIPGKQREFVAIINSVGSTNYADSVKGRFTISRDNAKNTVYLQMNNLKPEDT AVYVCNRNFDRIYWGQGTQVTVSSggggsggggsggggsEVQLVESGGGLVQPGNS LRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTI SRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSSGGPGPAG MKGLPGShgtviesleslnnyfiissgidveekslfldiwmwqkdgdmkilqsqiisiylrlfevlkdnqaisnnisv ieshlittffsnskakkdafmsiakfevnnpqvqrqafiielirwhqllpesslrkrkrsrcSGGPGPAGMKGLP GSEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSS ISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSV SSQGTLVTVSSSGGPGPAGMKGLPGShgtviesleslnnyfiissgidveekslfldiwmwqkdgd mkilqsqiisfylrlfevlkdnqaisnnisvieshlittffsnskakkdafmsiakfevnnpqvqrqafiielirvvhqllpes slrkrkrsrcSGGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRLSCAASGFTFSKF GMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMN SLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSHHHHHHEPEA</td>

<td> 113</td><td> ACP34 Mouse IL12 fusion protein</td><td> mdmrvpaqllgllllwlrgarcrvipvsgparclsqsmllkttddmvktareklkhysctaedidheditrdqtstlktclp lelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiildkgmlvaidelmq slnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssaSGGPGPAGMKGLPGSmwele kdvywevdwtpdapgetvnltcdtpeedditwtsdqrhgvigsgktltitvkefldagqytchkggetlshshlllhkke ngiwsteilknfknktflkceapnysgrftcswlvqrnmdlkfiiikssssspdsravtcgmaslsaekvtldqrdyekys vscqedvtcptaeetlpielalearqqnkyenystsffirdiikpdppknlqmkplknsqvevsweypdswstphsyfsl kfivriqrkkekmketeegcnqkgaflvektstevqckggnvcvqaqdryynsscskwacvpcrvrsHHHHHH</td>

<td> 114</td><td> ACP35 Mouse IL12 fusion protein</td><td> mdmrvpaqllgllllwlrgarcrvipvsgparclsqsmllkttddmvktareklkhysctaedidheditrdqtstlktclp lelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiildkgmlvaidelmq slnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssaggggsggggsggggsSGGPGPAG MKGLPGSggggsggggsggggsmwelekdvywevdwtpdapgetvnltcdtpeedditwtsdqrhgvigsg ktltitvkefldagqytchkggetlshshlllhkkengiwsteilknfknktflkceapnysgrftcswlvqmmdlkfiiik ssssspdsravtcgmaslsaekvtldqrdyekysvscqedvtcptaeetlpielalearqqnkyenystsffirdiikpdpp knlqmkplknsqvevsweypdswstphsyfslkfivriqrkkekmketeegcnqkgaflvektstevqckggnvcv qaqdryynsscskwacvpcrvrsHHHHHH</td>

<td> 115</td><td> ACP36 Mouse IL12 fusion protein</td><td> mdmrvpaqllgllllwlrgarcEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVR QAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDT AVYYCTIGGSLSVSSQGTLVTVSSSGGPGPAGMKGLPGSmwelekdvywevdwtpd apgetvnltcdtpeedditwtsdqrhgvigsgktltitvkefldagqytchkggetlshshlllhkkengiwsteilknfkn ktflkceapnysgrftcswlvqmmdlkfiiikssssspdsravtcgmaslsaekvtldqrdyekysvscqedvtcptaee tlpielalearqqnkyenystsffirdiikpdppknlqmkplknsqvevsweypdswstphsyfslkfivriqrkkekm keteegcnqkgaflvektstevqckggnvcvqaqdryynsscskwacvpcrvrsggggsggggsggggsrvipvsg parclsqsmllkttddmvktareklkhysctaedidheditrdqtstlktclplelhknesclatretssttrgsclppqktsl mmtlclgsiyedlkmyqtefqamaalqnhnhqqiildkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmkl cillhafstrwtinrvmgylssaSGGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRLSC AASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNA KTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSHHHHHH</td>

<td> 116</td><td> ACP37 Mouse IL12 fusion protein</td><td> mdmrvpaqllgllllwlrgarcQVQLQESGGGLVQAGGSLRLSCAASGRIFSIDIMSWYR QAPGKQRELVARITRGGTISYDDSVKGRFTISRDNAKNTVYLQMNSLKPEDTG VYYCNALYGTDYWGKGTQVTVSSggggsggggsggggsEVQLVESGGGLVQPGNS LRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTI SRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSSGGPGPAG MKGLPGSmwelekdvywevdwtpdapgetvnltcdtpeedditwtsdqrhgvigsgktltitvkefldagqytc hkggetlshshlllhkkengiwsteilknfknktflkceapnysgrftcswlvqmmdlkfiiikssssspdsravtcgmas Isaekvtldqrdyekysvscqedvtcptaeetlpielalearqqnkyenystsffirdiikpdppknlqmkplknsqvevs weypdswstphsyfslkffvriqrkkekmketeegcnqkgaflvektstevqckggnvcvqaqdryynsscskwac vpcrvrsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedidheditrdqtstlktcl plelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiildkgmlvaidelm</td>

<td></td><td></td><td> qslnhngetlrqkppvgeadpyrvkmklcillhafstrvvtmrvmgylssaSGGPGPAGMKGLPGSEVQ LVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGR DTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGT LVTVSSHHHHHH</td>

<td> 117</td><td> ACP79 Mouse IL12 fusion protein</td><td> mdmrvpaqllgllllwlrgarcQVQLQESGGGLVQAGGSLRLSCAASGRIFSIDIMSWYR QAPGKQRELVARITRGGTISYDDSVKGRFTISRDNAKNTVYLQMNSLKPEDTG VYYCNALYGTDYWGKGTQVTVSSggggsggggsggggsEVQLVESGGGLVQPGNS LRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTI SRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSSGGPGPAG MKGLPGSmwelekdvywevdwtpdapgetvnltcdtpeedditwtsdqrhgvigsgktltitvkefldagqytc hkggetlshshlllhkkengiwsteilknfknktflkceapnysgrftcswlvqmmdlkfiiikssssspdsravtcgmas Isaekvtldqrdyekysvscqedvtcptaeetlpielalearqqnkyenystsffirdiikpdppknlqmkplknsqvevs weypdswstphsyfslkffvriqrkkekmketeegcnqkgaflvektstevqckggnvcvqaqdryynsscskwac vpcrvrsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedidheditrdqtstlktcl plelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiildkgmlvaidelm qslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssaSGGPGPAGMKGLPGSEVQ LVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGR DTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGT LVTVSSHHHHHH</td>

<td> 118</td><td> ACP80 Mouse IL12 fusion protein</td><td> mdmrvpaqllgllllwlrgarcEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVR QAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDT AVYYCTIGGSLSVSSQGTLVTVSSSGGPGPAGMKGLPGSmwelekdvywevdwtpd apgetvnltcdtpeedditwtsdqrhgvigsgktltitvkefldagqytchkggetlshshlllhkkengiwsteilknfkn ktflkceapnysgrftcswlvqmmdlkfiiikssssspdsravtcgmaslsaekvtldqrdyekysvscqedvtcptaee tlpielalearqqnkyenystsffirdiikpdppknlqmkplknsqvevsweypdswstphsyfslkfivriqrkkekm keteegcnqkgaflvektstevqckggnvcvqaqdryynsscskwacvpcrvrsggggsggggsggggsrvipvsg parclsqsmllkttddmvktareklkhysctaedidheditrdqtstlktclplelhknesclatretssttrgsclppqktsl mmtlclgsiyedlkmyqtefqainaalqnhnhqqiildkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmkl cillhafstrwtinrvmgylssaSGGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRLSC AASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNA KTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggsQV QLQESGGGLVQAGGSLRLSCAASGRIFSIDIMSWYRQAPGKQRELVARITRGG TISYDDSVKGRFTISRDNAKNTVYLQMNSLKPEDTGVYYCNALYGTDYWGK GTQVTVSSHHHHHH</td>

<td> 119</td><td> ACP91 Chimeric IL-12 fusion protein</td><td> mdmrvpaqllgllllwlrgarciwelkkdvyweldwypdapgemwltcdtpeedgitwtldqssevlgsgktltiqv kefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwlttistdltfsvkssrg ssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssffirdiikpdppkn Iqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvraqdryysssws ewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedidheditrdqtstlkt clplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiildkgmlvaidel mqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtinrvmgylssaggggsggggsggggsggggsgggg sggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQ QLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQS YDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLS CAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRD NSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVSSggggsggggsgg ggsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSS ISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSV SSQGTLVTVSSHHHHHHEPEA</td>

<td> 120</td><td> ACP136 Chimeric IL-12 fusion protein</td><td> mdmrvpaqllgllllwlrgarciwelkkdvyweldwypdapgemwltcdtpeedgitwtldqssevlgsgktltiqv kefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwlttistdltfsvkssrg ssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssffirdiikpdppkn Iqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvraqdryysssws ewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedidheditrdqtstlkt clplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiildkgmlvaidel mqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssaSGGPGPAGMKGLPGSggg gsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVK WYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAEDEADYY CQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGWQPGRSL</td>

<td></td><td></td><td> RLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTI SRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVSSHHHHH HEPEA</td>

<td> 121</td><td> ACP138 Chimeric IL-12 fusion protein</td><td> mdmrvpaqllgllllwlrgarciwelkkdvyweldwypdapgemwltcdtpeedgitwtldqssevlgsgktltiqv kefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwlttistdltfsvkssrg ssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssffirdiikpdppkn Iqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvraqdryysssws ewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedidheditrdqtstlkt clplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqainaalqnhnhqqiildkgmlvaidel mqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssaSGGPGPAGMKGLPGSggg gsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVK WYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAEDEADYY CQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGWQPGRSL RLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTI SRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVSSggggsggg gsggggsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEW VSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGS LSVSSQGTLVTVSSggggsggggsggggsQVQLQESGGGLAQAGGSLSLSCAASGFT VSNSVMAWYRQTPGKQREFVAIINSVGSTNYADSVKGRFTISRDNAKNTVYL QMNNLKPEDTAVYVCNRNFDRIYWGQGTQVTVSSHHHHHHEPEA</td>

<td> 122</td><td> ACP139 Chimeric IL-12 fusion protein</td><td> mdmrvpaqllgllllwlrgarcQVQLQESGGGLAQAGGSLSLSCAASGFTVSNSVMAWY RQTPGKQREFVAIINSVGSTNYADSVKGRFTISRDNAKNTVYLQMNNLKPEDT AVYVCNRNFDRIYWGQGTQVTVSSggggsggggsggggsiwelkkdvyweldwypdapgem wltcdtpeedgitwtldqssevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknk tflrceaknysgrftcwwlttistdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpie vmvdavhklkyenytssffirdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkd rvftdktsatvicrknasisvraqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttdd mvktareklkhysctaedidheditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkm yqtefqamaalqnhnhqqiildkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtinrv mgylssaSGGPGPAGMKGLPGSggggsggggsggggsggggsggggsggggsQSVLTQPPSVS GAPGQRVTISCSGSRSNIGSNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFS GSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggg gsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLE WVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKT HGSHDNWGQGTMVTVSSggggsggggsggggsEVQLVESGGGLVQPGNSLRLSCA ASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAK TTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSHHHHHHEPEA</td>

<td> 123</td><td> ACP140 Chimeric IL-12 fusion protein</td><td> mdmrvpaqllgllllwlrgarcQVQLQESGGGLAQAGGSLSLSCAASGFTVSNSVMAWY RQTPGKQREFVAIINSVGSTNYADSVKGRFTISRDNAKNTVYLQMNNLKPEDT AVYVCNRNFDRIYWGQGTQVTVSSSGGPGPAGMKGLPGSiwelkkdvyweldwyp dapgemwltcdtpeedgitwtldqssevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdq kepknktflrceaknysgrftcwwlttistdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpa aeeslpievmvdavhklkyenytssffirdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgk skrekkdrvftdktsatvicrknasisvraqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsr nllkttddmvktareklkhysctaedidheditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsi yedlkmyqtefqamaalqnhnhqqiildkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrv vtinrvmgylssaSGGPGPAGMKGLPGSggggsggggsggggsggggsggggsggggsQSVLTQP PSVSGAPGQRVTISCSGSRSNIGSNTVKWYQQLPGTAPKLLIYYNDQRPSGVPD RFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLFGTGTKVTVLgggg sggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKG LEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYC KTHGSHDNWGQGTMVTVSSggggsggggsggggsEVQLVESGGGLVQPGNSLRLSC AASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNA KTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSHHHHHHEPEA</td>

<td> 124</td><td> ACP38 IL-2 fusion protein</td><td> mdmrvpaqllgllllwlrgarcaptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcle eelkpleevlnlaqsknfhlrprdlisninvivlelkgsettfinceyadetativeflnrwitfcqsiistltSGGPGPAG MKGLPGSEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGL EWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCAR DSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVG</td>

<td></td><td></td><td> DRVTITCKASQNVGTNVGWYQQKPGKAPKALIYSASFRYSGVPSRFSGSGSGT DFTLTISSLQPEDFAIYYCQQYYTYPYTFGGGTKVEIKggggsggggsggggsEVQLV ESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDT LYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLV TVSSggggsggggsggggsQVQLQESGGGLVQAGGSLRLSCAASGRIFSIDIMSWYR QAPGKQRELVARITRGGTISYDDSVKGRFTISRDNAKNTVYLQMNSLKPEDTG VYYCNALYGTDYWGKGTQVTVSSHHHHHH</td>

<td> 125</td><td> ACP39 IL-2 fusion protein</td><td> mdmrvpaqllgllllwlrgarcQVQLQESGGGLVQAGGSLRLSCAASGRIFSIDIMSWYR QAPGKQRELVARITRGGTISYDDSVKGRFTISRDNAKNTVYLQMNSLKPEDTG VYYCNALYGTDYWGKGTQVTVSSSGGPGPAGMKGLPGSEVQLVESGGGLVQ PGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKG RFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSSGGPG PAGMKGLPGSEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPG KGLEWVAAIDSSSYIYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYY CARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSA SVGDRVTITCKASQNVGTNVGWYQQKPGKAPKALIYSASFRYSGVPSRFSGSG SGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIKSGGPGPAGMKGL PGSaptssstkktqlqlehllldlqmilnginnyknpkltrmltfklympkkatelkhlqcleeelkpleevlnlaqsknf hlrprdlisnmvivlelkgsettfmceyadetativeflnrwitfcq siistltHHHHHH* *</td>

<td> 126</td><td> ACP40 IL-2 fusion protein</td><td> mdmrvpaqllgllllwlrgarcelcdddppeiphatfkamaykegtmlnceckrgfrriksgslymlctgnsshsswd nqcqctssatmttkqvtpqpeeqkerkttemqspmqpvdqaslpghcrepppweneateriyhfwgqmvyyqcv qgyralhrgpaesvckmthgktrwtqpqlictgemetsqipgeekpqaspegrpesetsclvtttdfqiqtemaatmets iftteyqggggsggggsggggsggggsggggsggggsSGGPGPAGMKGLPGSaptssstkktqlqlehllld Iqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrprdlisnmvivlelkgsettf mceyadetativeflnrwitfcq siistltHHHHHH</td>

<td> 127</td><td> ACP41 IL-2 fusion protein (WW0076)</td><td> mdmrvpaqllgllllwlrgarcaptssstkktqlqlehllldlqmilngmnyknpkltrmltfklympkkatelkhlqcle eelkpleevlnlaqsknfhlrprdlisninvivlelkgsettfinceyadetativeflnrwitfcqsiistltSGGPGPAG MKGLPGSggggsggggsggggsggggsggggsggggselcdddppeiphatfkamaykegtmlnceckrgfr riksgslymlctgnsshsswdnqcqctssatmttkqvtpqpeeqkerkttemqspmqpvdqaslpghcrepppwen eateriyhfwgqmvyyqcvqgyralhrgpaesvckmthgktrwtqpqlictgemetsqipgeekpqaspegrpese tsclvtttdfqiqtemaatmetsiftteyqHHHHHH</td>

<td> 128</td><td> ACP42 IL-2 fusion protein (WW0078)</td><td> mdmrvpaqllgllllwlrgarcEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVR QAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDT AVYY CTIGGSLS VSSQGTLVTVS Sggggsggggsggggselcdddppeiphatfkamaykegtmln ceckrgfrriksgslymlctgnsshsswdnqcqctssatmttkqvtpqpeeqkerkttemqspmqpvdqaslpghcre pppweneateriyhfwgqmvyyqcvqgyralhrgpaesvckmthgktrwtqpqlictgemetsqipgeekpqasp egrpesetsclvtttdfqiqtemaatmetsiftteyqggggsggggsggggsggggsggggsggggsSGGPGPAG MKGLPGSaptssstkktqlqlehllldlqmilnginnyknpkltrmltfklympkkatelkhlqcleeelkpleevlnl aq sknfhlrprdlisnmvivlelkgsettfmceyadetativeflnrwitfcq siistltHHHHHH</td>

<td> 129</td><td> ACP43 IL-2 fusion protein (WW0079)</td><td> mdmrvpaqllgllllwlrgarcaptssstkktqlqlehllldlqmilngmnyknpkltrmltfklympkkatelkhlqcle eelkpleevlnlaqsknfhlrprdlisninvivlelkgsettfinceyadetativeflnrwitfcqsiistltSGGPGPAG MKGLPGSggggsggggsggggsggggsggggsggggselcdddppeiphatfkamaykegtmlnceckrgfr riksgslymlctgnsshsswdnqcqctssatmttkqvtpqpeeqkerkttemqspmqpvdqaslpghcrepppwen eateriyhfwgqmvyyqcvqgyralhrgpaesvckmthgktrwtqpqlictgemetsqipgeekpqaspegrpese tsclvtttdfqiqtemaatmetsiftteyqggggsggggsggggsEVQLVESGGGLVQPGNSLRLSCA ASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAK TTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSHHHHHH</td>

<td> 130</td><td> ACP44 IL-2 fusion protein (WW0080)</td><td> mdmrvpaqllgllllwlrgarcaptssstkktqlqlehllldlqmilngmnyknpkltrmltfklympkkatelkhlqcle eelkpleevlnlaqsknfhlrprdlisninvivlelkgsettfinceyadetativeflnrwitfcqsiistltSGGPGPAG MKGLPGSggggsggggsggggsggggsggggsggggselcdddppeiphatfkamaykegtmlnceckrgfr riksgslymlctgnsshsswdnqcqctssatmttkqvtpqpeeqkerkttemqspmqpvdqaslpghcrepppwen eateriyhfwgqmvyyqcvqgyralhrgpaesvckmthgktrwtqpqlictgemetsqipgeekpqaspegrpese tsclvtttdfqiqtemaatmetsiftteyqSGGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLR LSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISR DNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSHHHHHH</td>

<td> 131</td><td> ACP45</td><td> mdmrvpaqllgllllwlrgarcEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVR QAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDT AVYYCTIGGSLSVSSQGTLVTVSSSGGPGPAGMKGLPGSEVQLVESGGGLVQP</td>

<td></td><td> IL-2 fusion protein WW0046</td><td> GGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRF TISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSG GGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKASQNVGTNVGWYQQ KPGKAPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYY TYPYTFGGGTKVEIKggggsggggsggggsggggsggggsggggsSGGPGPAGMKGLPGSa ptssstkktqlqlehllldlqmilnginnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrprd lisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltHHHHHH</td>

<td> 132</td><td> ACP46 IL-2 fusion protein</td><td> mdmrvpaqllgllllwlrgarcaptssstkktqlqlehllldlqmilngmnyknpkltrmltfldympkkatelkhlqcle eelkpleevlnlaqsknfhlrprdlisninvivlelkgsettfinceyadetativeflnrwitfcqsiistltSGGPGPAG MKGLPGSggggsggggsggggsggggsggggsggggsEVQLVESGGGLVQPGGSLRLSCA ASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKN SLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSsggpgpagmkglp gsDIQMTQSPSSLSASVGDRVTITCKASQNVGTNVGWYQQKPGKAPKALIYSA SFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEI KggggsggggsggggsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQA PGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAV YYCTIGGSLSVSSQGTLVTVSSggggsggggsggggsQVQLQESGGGLVQAGGSLRL SCAASGRIFSIDIMSWYRQAPGKQRELVARITRGGTISYDDSVKGRFTISRDNA KNTVYLQMNSLKPEDTGVYYCNALYGTDYWGKGTQVTVSSHHHHHH</td>

<td> 133</td><td> ACP47 IL-2 fusion protein</td><td> mdmrvpaqllgllllwlrgarcQVQLQESGGGLVQAGGSLRLSCAASGRIFSIDIMSWYR QAPGKQRELVARITRGGTISYDDSVKGRFTISRDNAKNTVYLQMNSLKPEDTG VYYCNALYGTDYWGKGTQVTVSSggggsggggsggggsaptssstkktqlqlehllldlqmilngin nyknpkltrmltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrprdlismnvivlelkgsettfinceyadet ativeflnrwitfcqsiistltSGGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRLSCAAS GFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTT LYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggsggggsgg ggsggggsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLE WVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARD SNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGD RVTITCKASQNVGTNVGWYQQKPGKAPKALIYSASFRYSGVPSRFSGSGSGTD FTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIKHHHHHH</td>

<td> 134</td><td> ACP48 IL-2 fusion protein (WW0054)</td><td> mdmrvpaqllgllllwlrgarcaptssstkktqlqlehllldlqmilngmnyknpkltrmltfldympkkatelkhlqcle eelkpleevlnlaqsknfhlrprdlisninvivlelkgsettfinceyadetativeflnrwitfcqsiistltSGGPGPAG MKGLPGSEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGL EWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCAR DSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVG DRVTITCKASQNVGTNVGWYQQKPGKAPKALIYSASFRYSGVPSRFSGSGSGT DFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIKggggsggggsggggsEVQLV ESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDT LYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLV TVSSHHHHHH</td>

<td> 135</td><td> ACP49 IL-2 fusion protein (WW0055)</td><td> mdmrvpaqllgllllwlrgarcaptssstkktqlqlehllldlqmilngmnyknpkltrmltfldympkkatelkhlqcle eelkpleevlnlaqsknfhlrprdlisninvivlelkgsettfinceyadetativeflnrwitfcqsiistltSGGPGPAG MKGLPGSggggsggggsggggsggggsggggsggggsEVQLVESGGGLVQPGGSLRLSCA ASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKN SLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGG SGGGGSDIQMTQSPSSLSASVGDRVTITCKASQNVGTNVGWYQQKPGKAPKA LIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGG TKVEIKggggsggggsggggsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSW VRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPE DTAVYYCTIGGSLSVSSQGTLVTVSSHHHHHH</td>

<td> 136</td><td> ACP92 IL-2 fusion protein</td><td> mdmrvpaqllgllllwlrgarcEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVR QAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDT AVYYCTIGGSLSVSSQGTLVTVSSSGGPGPAGMKGLPGSaptssstkktqlqlehllldlqm ilnginnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrprdlisnmvivlelkgsettfince yadetativeflnrwitfcqsiistltSGGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRLSC AASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNA KTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSHHHHHH</td>

<td> 137</td><td> ACP93 IL-2 fusion protein</td><td> mdmrvpaqllgllllwlrgarcQVQLQESGGGLVQAGGSLRLSCAASGRIFSIDIMSWYR QAPGKQRELVARITRGGTISYDDSVKGRFTISRDNAKNTVYLQMNSLKPEDTG VYYCNALYGTDYWGKGTQVTVSSgsgsgsgsgsgsgsgsEVQLVESGGGLVQPGNS LRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTI SRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSgsgsgsgsgsgs gsgsQVQLQESGGGLVQAGGSLRLSCAASGRIFSIDIMSWYRQAPGKQRELVAR ITRGGTISYDDSVKGRFTISRDNAKNTVYLQMNSLKPEDTGVYYCNALYGTD YWGKGTQVTVSSgsgsgsgsgsgsgsgsEVQLVESGGGLVQPGGSLRLSCAASGFTFS SYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQM NSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGS DIQMTQSPSSLSASVGDRVTITCKASQNVGTNVGWYQQKPGKAPKALIYSASF RYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYIYPYTFGGGTKVEIK SGGPGPAGMKGLPGSaptssstkktqlqlehllldlqmilnginnyknpkltrmltfldympkkatelkhlqcl eeelkpleevlnlaqsknfhlrprdlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltHHHHHH</td>

<td> 138</td><td> ACP94 IL-2 fusion protein</td><td> mdmrvpaqllgllllwlrgarcQVQLQESGGGLVQAGGSLRLSCAASGRIFSIDIMSWYR QAPGKQRELVARITRGGTISYDDSVKGRFTISRDNAKNTVYLQMNSLKPEDTG VYYCNALYGTDYWGKGTQVTVSSgsgsgsgsgsgsgsgsEVQLVESGGGLVQPGNS LRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTI SRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSgsgsgsgsgsgs gsgsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVA AIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNW DALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTI TCKASQNVGTNVGWYQQKPGKAPKALIYSASFRYSGVPSRFSGSGSGTDFTLT ISSLQPEDFAIYYCQQYYTYPYTFGGGTKVEIKSGGPGPAGMKGLPGSaptssstk ktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrprdlisnmv ivlelkgsettfmceyadetativeflnrwitfcqsiistltHHHHHH</td>

<td> 139</td><td> ACP95 IL-2 fusion protein</td><td> mdmrvpaqllgllllwlrgarcQVQLQESGGGLVQAGGSLRLSCAASGRIFSIDIMSWYR QAPGKQRELVARITRGGTISYDDSVKGRFTISRDNAKNTVYLQMNSLKPEDTG VYYCNALYGTDYWGKGTQVTVSSgsgsgsgsgsgsgsgsEVQLVESGGGLVQPGNS LRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTI SRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSSGGPGPAG MKGLPGSaptssstkktqlqlehllldlqmilnginnyknpkltrmltfkiympkkatelkhlqcleeelkpleevlnl aq sknfhlrprdlisnmvivlelkgsettfmceyadetativeflnrwitfcq siistltHHHHHH</td>

<td> 140</td><td> ACP96 IL-2 fusion protein</td><td> mdmrvpaqllgllllwlrgarcQVQLQESGGGLVQAGGSLRLSCAASGRIFSIDIMSWYR QAPGKQRELVARITRGGTISYDDSVKGRFTISRDNAKNTVYLQMNSLKPEDTG VYYCNALYGTDYWGKGTQVTVSSSGGPGPAGMKGLPGSaptssstkktqlqlehllldlq milnginnyknpkltrmltfkiympkkatelkhlqcleeelkpleevlnlaqsknfhlrprdlismnvivlelkgsettfin ceyadetativeflnrwitfcqsiistltSGGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRL SCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRD nakttlylomnslrpedtavyyctiggslsvssogtlvtvsshhhhhh</td>

<td> 141</td><td> ACP97 IL-2 fusion protein</td><td> mdmrvpaqllgllllwlrgarcQVQLQESGGGLVQAGGSLRLSCAASGRIFSIDIMSWYR QAPGKQRELVARITRGGTISYDDSVKGRFTISRDNAKNTVYLQMNSLKPEDTG VYYCNALYGTDYWGKGTQVTVSSggggsggggsggggsEVQLVESGGGLVQPGNS LRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTI SRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSSGGPGPAG MKGLPGSaptssstkktqlqlehllldlqmilnginnyknpkltrmltfkiympkkatelkhlqcleeelkpleevlnl aqsknfhlrprdlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltSGGPGPAGMKGLPGS EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS sqgtlvtvsshhhhhh</td>

<td> 142</td><td> ACP99 IL-2 fusion protein</td><td> mdmrvpaqllgllllwlrgarcQVQLQESGGGLVQAGGSLRLSCAASGRIFSIDIMSWYR QAPGKQRELVARITRGGTISYDDSVKGRFTISRDNAKNTVYLQMNSLKPEDTG VYYCNALYGTDYWGKGTQVTVSSggggsggggsggggsaptssstkktqlqlehllldlqmilngm nyknpkltrmltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrprdlismnvivlelkgsettfinceyadet ativeflnrwitfcqsiistltSGGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRLSCAAS GFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTT lylomnslrpedtavyyctiggslsvssogtlvtvsshhhhhh</td>

<td> 143</td><td> ACP100 IL-2 fusion protein</td><td> mdmrvpaqllgllllwlrgarcQVQLQESGGGLVQAGGSLRLSCAASGRIFSIDIMSWYR QAPGKQRELVARITRGGTISYDDSVKGRFTISRDNAKNTVYLQMNSLKPEDTG VYYCNALYGTDYWGKGTQVTVSSggggsggggsggggsaptssstkktqlqlehllldlqmilngm nyknpkltrmltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrprdlismnvivlelkgsettfmceyadet ativeflnrwitfcq siistltHHHHHH</td>

<td> 144</td><td> ACP101 (WW0061) IL-2 fusion protein</td><td> mdmrvpaqllgllllwlrgarcaptssstkktqlqlehllldlqmilngmnyknpkltrmltfkiympkkatelkhlqcle eelkpleevlnlaqsknfhlrprdlisninvivlelkgsettfinceyadetativeflnrwitfcqsiistltSGGPGPAG MKGLPGSEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGL EWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTI GGSLSVSSQGTLVTVSSHHHHHH</td>

<td> 145</td><td> ACP102 IL-2 fusion protein</td><td> mdmrvpaqllgllllwlrgarcQVQLQESGGGLVQAGGSLRLSCAASGRIFSIDIMSWYR QAPGKQRELVARITRGGTISYDDSVKGRFTISRDNAKNTVYLQMNSLKPEDTG VYYCNALYGTDYWGKGTQVTVSSSGGPGPAGMKGLPGSaptssstkktqlqlehllldlq milngmnyknpkltrmltfkiympkkatelkhlqcleeelkpleevlnlaqsknfhlrprdlismnvivlelkgsettfin ceyadetativeflnrwitfcqsiistltSGGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRL SCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRD NAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggs ggggsggggsggggsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPG KGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYY CARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSA SVGDRVTITCKASQNVGTNVGWYQQKPGKAPKALIYSASFRYSGVPSRFSGSG SGTDFTLTISSLQPEDFATYYCQQYYTYPYIEGGGTKVEIKHHHHHH</td>

<td> 146</td><td> ACP103 IL-2 fusion protein</td><td> mdmrvpaqllgllllwlrgarcaptssstkktqlqlehllldlqmilngmnyknpkltrmltfkiympkkatelkhlqcle eelkpleevlnlaqsknfhlrprdlisninvivlelkgsettfinceyadetativeflnrwitfcqsiistltSGGPGPAG MKGLPGSggggsggggsggggsggggsggggsggggsEVQLVESGGGLVQPGGSLRLSCA ASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKN SLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGG SGGGGSDIQMTQSPSSLSASVGDRVTITCKASQNVGTNVGWYQQKPGKAPKA LIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGG TKVEIKggggsggggsggggsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSW VRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPE DTAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggsQVQLQESGGGLAQAGG SLSLSCAASGFTVSNSVMAWYRQIPGKQREFVAIINSVGSTNYADSVKGRFTIS RDNAKNTVYLQMNNLKPEDTAVYVCNRNFDRIYWGQGTQVTVSSHHHHHH</td>

<td> 147</td><td> ACP104 IL-2 fusion protein</td><td> mdmrvpaqllgllllwlrgarcQVQLQESGGGLAQAGGSLSLSCAASGFTVSNSVMAWY RQIPGKQREFVAIINSVGSTNYADSVKGRFTISRDNAKNTVYLQMNNLKPEDT AVYVCNRNFDRIYWGQGTQVTVSSaptssstkktqlqlehllldlqmilnginnyknpkltrmltfkiy mpkkatelkhlqcleeelkpleevlnlaqsknfhlrprdlisninvivlelkgsettfinceyadetativeflnrwitfcqsii stltSGGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMS WVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLR PEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggsggggsggggsggggsEVQL VESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYT YSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWG QGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKASQNV GTNVGWYQQKPGKAPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDF ATYYCQQYYTYPYTFGGGTKVEIKHHHHHH</td>

<td> 148</td><td> ACP105 IL-2 fusion protein</td><td> mdmrvpaqllgllllwlrgarcEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVR QAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTA VYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSS LSASVGDRVTITCKASQNVGTNVGWYQQKPGKAPKALIYSASFRYSGVPSRFS GSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIKggggsggggsggg gsggggsggggsggggsSGGPGPAGMKGLPGSaptssstkktqlqlehllldlqmilngmnyknpkltrml tfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitf cqsiistltSGGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFG MSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNS LRPEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggsQVQLQESGGGLA QAGGSLSLSCAASGFTVSNSVMAWYRQTPGKQREFVAIINSVGSTNYADSVK</td>

<td></td><td></td><td> GRFTISRDNAKNTVYLQMNNLKPEDTAVYVCNRNFDRIYWGQGTQVTVSSH HHHHH</td>

<td> 149</td><td> ACP106 IL-2 fusion protein</td><td> mdmrvpaqllgllllwlrgarcQVQLQESGGGLAQAGGSLSLSCAASGFTVSNSVMAWY RQIPGKQREFVAIINSVGSTNYADSVKGRFTISRDNAKNTVYLQMNNLKPEDT AVYVCNRNFDRIYWGQGTQVTVSSggggsggggsggggsEVQLVESGGGLVQPGNS LRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTI SRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSSGGPGPAG MKGLPGSEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGL EWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCAR DSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVG DRVTITCKASQNVGTNVGWYQQKPGKAPKALIYSASFRYSGVPSRFSGSGSGT DFTLTISSLQPEDFAIYYCQQYYTYPYTFGGGTKVEIKggggsggggsggggsggggsgg ggsggggsSGGPGPAGMKGLPGSaptssstkktqlqlehllldlqmilnginnyknpkltrmltfkfyrnpkk atelkhlqcleeelkpleevlnlaqsknfhlrprdlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltH HHHHH</td>

<td> 150</td><td> ACP107 IL-2 fusion protein</td><td> mdmrvpaqllgllllwlrgarcEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVR QAPGKGLEWVAAIDSSSYIYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTA VYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSS LSASVGDRVTITCKASQNVGTNVGWYQQKPGKAPKALIYSASFRYSGVPSRFS GSGSGTDFTLTISSLQPEDFATYYCQQYYIYPYTFGGGTKVEIKggggsggggsggg gsggggsggggsggggsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQA PGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAV YYCTIGGSLSVSSQGTLVTVSSSGGPGPAGMKGLPGSaptssstkktqlqlehllldlqmilng innyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrprdlisnmvivlelkgsettfinceyad etativeflnrwitfcqsiistltggggsggggsggggsQVQLQESGGGLAQAGGSLSLSCAASGFT VSNSVMAWYRQTPGKQREFVAIINSVGSTNYADSVKGRFTISRDNAKNTVYL QMNNLKPEDTAVYVCNRNFDRIYWGQGTQVTVSSHHHHHH</td>

<td> 151</td><td> ACP108 IL-2 fusion protein</td><td> mdmrvpaqllgllllwlrgarcQVQLQESGGGLVQAGGSLRLSCAASGRIFSIDIMSWYR QAPGKQRELVARITRGGTISYDDSVKGRFTISRDNAKNTVYLQMNSLKPEDTG VYYCNALYGTDYWGKGTQVTVSSggggsggggsggggsaptssstkktqlqlehllldlqmilngm nyknpkltrmltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrprdlismnvivlelkgsettfinceyadet ativeflnrwitfcqsiistltSGGPGPAGMKGLPGSrgetgpaaPGSEVQLVESGGGLVQPGNS LRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTI SRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsg gggsggggsggggsggggsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQ APGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAV YYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSL SASVGDRVTITCKASQNVGTNVGWYQQKPGKAPKALIYSASFRYSGVPSRFSG SGSGTDFTLTISSLQPEDFATYYCQQYYIYPYTFGGGTKVEIKHHHHHH</td>

<td> 152</td><td> ACPI 17 Anti-FN CGS-2 scFv</td><td> mdmrvpaqllgllllwlrgarcEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYAMSWVR QAPGKGLEWVSAISGSGGSTYYADSVKGRFTISRDNSKNTLYLQMNSLRAED TAVYYCARGVGAFRPYRKHEWGQGTLVTVSRggggsggggsggggsSSELTQDPAV SVALGQTVRITCQGDSLRSYYASWYQQKPGQAPVLVIYGKNNRPSGIPDRFSG SSSGNTASLTTTGAQAEDEADYYCNSSPFEHNLWFGGGTKLTVLHHHHHHE PEA</td>

<td> 153</td><td> ACPI 18 NARA1 Vh/Vl noncleavable</td><td> mdmrvpaqllgllllwlrgarcQVQLQQSGAELVRPGTSVKVSCKASGYAFTNYLIEWV KQRPGQGLEWIGVINPGSGGTNYNEKFKGKATLTADKSSSTAYMQLSSLTSD DSAVYFCARWRGDGYYAYFDVWGAGTTVTVSSggggsggggsggggsDIVLTQSP ASLAVSLGQRATISCKASQSVDYDGDSYMNWYQQKPGQPPKLLIYAASNLES GIPARFSGSGSGTDFTLNIHPVEEEDAAIYYCQQSNEDPYTFGGGTKLEIKHHH HHHEPEA</td>

<td> 154</td><td> ACPI 19 NARA1 Vh/Vl cleavable</td><td> mdmrvpaqllgllllwlrgarcQVQLQQSGAELVRPGTSVKVSCKASGYAFTNYLIEWV KQRPGQGLEWIGVINPGSGGTNYNEKFKGKATLTADKSSSTAYMQLSSLTSD DSAVYFCARWRGDGYYAYFDVWGAGTTVTVSSSGGPGPAGMKGLPGSDIVL TQSPASLAVSLGQRATISCKASQSVDYDGDSYMNWYQQKPGQPPKLLIYAAS NLESGIPARFSGSGSGTDFTLNIHPVEEEDAATYYCQQSNEDPYTFGGGTKLEI KHHHHHHEPEA</td>

<td> 155</td><td> ACP120 NARA1 Vl/Vh noncleavable</td><td> mdmrvpaqllgllllwlrgarcDIVLTQSPASLAVSLGQRATISCKASQSVDYDGDSYMN WYQQKPGQPPKLLIYAASNLESGIPARFSGSGSGTDFTLNIHPVEEEDAATYYC QQSNEDPYTFGGGTKLEIKggggsggggsggggsQVQLQQSGAELVRPGTSVKVSCK ASGYAFTNYLIEWVKQRPGQGLEWIGVINPGSGGTNYNEKFKGKATLTADKS SSTAYMQLSSLTSDDSAVYFCARWRGDGYYAYFDVWGAGTTVTVSSHHHHH HEPEA</td>

<td> 156</td><td> ACP121 NARA1 Vl/Vh cleavable</td><td> mdmrvpaqllgllllwlrgarcDIVLTQSPASLAVSLGQRATISCKASQSVDYDGDSYMN WYQQKPGQPPKLLIYAASNLESGIPARFSGSGSGTDFTLNIHPVEEEDAATYYC QQSNEDPYTFGGGTKLEIKSGGPGPAGMKGLPGSQVQLQQSGAELVRPGTSV KVSCKASGYAFTNYLIEWVKQRPGQGLEWIGVINPGSGGTNYNEKFKGKATL TADKSSSTAYMQLSSLTSDDSAVYFCARWRGDGYYAYFDVWGAGTTVTVSS HHHHHHEPEA</td>

<td> 157</td><td> ACP124 IL-2 fusion protein (WW0159)</td><td> mdmrvpaqllgllllwlrgarcaptssstkktqlqlehllldlqmilngmnyknpkltrmltfldympkkatelkhlqcle eelkpleevlnlaqsknfhlrprdlisninvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsg gggsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVS SISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLS VSSQGTLVTVSSHHHHHHEPEA</td>

<td> 158</td><td> ACP132 IL-2 fusion protein (WW0177)</td><td> mdmrvpaqllgllllwlrgarcaptssstkktqlqlehllldlqmilngmnyknpkltrmltfldympkkatelkhlqcle eelkpleevlnlaqsknfhlrprdlisninvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsg gggsdahksevahrfkdlgeenfkalvliafaqylqqcpfedhvklvnevtefaktcvadesaencdkslhtlfgdklctv atlretygemadccakqepemecflqhkddnpnlprlvrpevdvmctafhdneetflkkylyeiarrhpyiyapellff akrykaafteccqaadkaacllpkldelrdegkassakqrlkcaslqkfgerafkawavarlsqripkaefaevsklvtdlt kvhtecchgdllecaddradlakyicenqdsissklkeccekpllekshciaevendempadlpslaadfveskdvckn yaeakdvflgmflyeyarrhpdyswlllrlaktyettlekccaaadphecyakvfdefkplveepqnlikqncelfeqlg eykfqnallvrytkkvpqvstptlvevsmlgkvgskcckhpeakrmpcaedylswlnqlcvlhektpvsdrvtkcct eslvnrrpcfsalevdetyvpkefnaetftfhadictlsekerqikkqtalvelvkhkpkatkeqlkavmddfaafvekcc kaddketcfaeegkklvaasqaalglHHHHHHEPEA</td>

<td> 159</td><td> ACP141 IL-2 fusion protein (WW0178)</td><td> mdmrvpaqllgllllwlrgarcaptssstkktqlqlehllldlqmilngmnyknpkltrmltfldympkkatelkhlqcle eelkpleevlnlaqsknfhlrprdlisninvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsg gggsdahksevahrfkdlgeenfkalvliafaqylqqcpfedhvklvnevtefaktcvadesaencdkslhtlfgdklctv atlretygemadccakqepemecflqhkddnpnlprlvrpevdvmctafhdneetflkkylyeiarrhpyiyapellff akrykaafteccqaadkaacllpkldelrdegkassakqrlkcaslqkfgerafkawavarlsqripkaefaevsklvtdlt kvhtecchgdllecaddradlakyicenqdsissklkeccekpllekshciaevendempadlpslaadfveskdvckn yaeakdvflgmflyeyarrhpdyswlllrlaktyettlekccaaadphecyakvfdefkplveepqnlikqncelfeqlg eykfqnallvrytkkvpqvstptlvevsmlgkvgskcckhpeakrmpcaedylswlnqlcvlhektpvsdrvtkcct eslvnrrpcfsalevdetyvpkefnaetftfhadictlsekerqikkqtalvelvkhkpkatkeqlkavmddfaafvekcc kaddketcfaeegkklvaasqaalglHHHHHHEPEA</td>

<td> 160</td><td> ACP142 IL-2 fusion protein (WW0179)</td><td> mdmrvpaqllgllllwlrgarcaptssstkktqlqlehllldlqmilngmnyknpkltrmltfldympkkatelkhlqcle eelkpleevlnlaqsknfhlrprdlisninvivlelkgsettfinceyadetativeflnrwitfcqsiistltSGGPGPAG MKGLPGSdahksevahrfkdlgeenfkalvliafaqylqqcpfedhvklvnevtefaktcvadesaencdkslhtlf gdklctvatlretygemadccakqepemecflqhkddnpnlprlvrpevdvmctafhdneetflkkylyeiarrhpyf yapellffakrykaafteccqaadkaacllpkldelrdegkassakqrlkcaslqkfgerafkawavarlsqrlpkaefaev sklvtdltkvhtecchgdllecaddradlakyicenqdsissklkeccekpllekshciaevendempadlpslaadfves kdvcknyaeakdvflgmflyeyarrhpdyswlllrlaktyettlekccaaadphecyakvfdefkplveepqnlikqn celfeqlgeykfqnallvrytkkvpqvstptlvevsmlgkvgskcckhpeakrmpcaedylswlnqlcvlhektpvs drvtkccteslvnrrpcfsalevdetyvpkefiiaetftfhadictlsekerqikkqtalvelvkhkpkatkeqlkavmddfa afvekcckaddketcfaeegkklvaasqaalglHHHHHHEPEA</td>

<td> 161</td><td> ACP144 IL-2 fusion protein</td><td> mdmrvpaqllgllllwlrgarcaptssstkktqlqlehllldlqmilngmnyknpkltrmltfldympkkatelkhlqcle eelkpleevlnlaqsknfhlrprdlisninvivlelkgsettfinceyadetativeflnrwitfcqsiistltSGGPGPAG MKGLPGSEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGL EWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTI GGSLSVSSQGTLVTVSSggggsggggsggggsggggsggggsggggsSGGPGPAGMKGLPG SEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAI DSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDA LDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITC KASQNVGTNVGWYQQKPGKAPKALIYSASFRYSGVPSRFSGSGSGTDFTLTIS</td>

<td></td><td></td><td> SLQPEDFATYYCQQYYTYPYTFGGGTKVEIKggggsggggsggggsQVQLQESGGG LAQAGGSLSLSCAASGFTVSNSVMAWYRQTPGKQREFVAIINSVGSTNYADS VKGRFTISRDNAKNTVYLQMNNLKPEDTAVYVCNRNFDRIYWGQGTQVTVS SHHHHHHEPEA</td>

<td> 162</td><td> ACP145 IL-2 fusion protein</td><td> mdmrvpaqllgllllwlrgarcQVQLQESGGGLAQAGGSLSLSCAASGFTVSNSVMAWY RQTPGKQREFVAIINSVGSTNYADSVKGRFTISRDNAKNTVYLQMNNLKPEDT AVYVCNRNFDRIYWGQGTQVTVSSggggsggggsggggsaptssstkktqlqlehllldlqmilngi nnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrprdlisninvivlelkgsettfinceyade tativeflnrwitfcqsiistltSGGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRLSCAAS GFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTT LYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggsggggsgg ggsggggsSGGPGPAGMKGLPGSEVQLVESGGGLVQPGGSLRLSCAASGFTFSSY TLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNS LRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDI QMTQSPSSLSASVGDRVTITCKASQNVGTNVGWYQQKPGKAPKALIYSASFR YSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYIYPYTFGGGTKVEIKH HHHHHEPEA</td>

<td> 163</td><td> ACP146 IL-2 fusion protein</td><td> mdmrvpaqllgllllwlrgarcQVQLQESGGGLAQAGGSLSLSCAASGFTVSNSVMAWY RQTPGKQREFVAIINSVGSTNYADSVKGRFTISRDNAKNTVYLQMNNLKPEDT AVYVCNRNFDRIYWGQGTQVTVSSSGGPGPAGMKGLPGSaptssstkktqlqlehllldlq milnginnyknpkltrmltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrprdlismnvivlelkgsettfin ceyadetativeflnrwitfcqsiistltSGGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRL SCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRD NAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggs ggggsggggsggggsSGGPGPAGMKGLPGSEVQLVESGGGLVQPGGSLRLSCAASG FTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLY LQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGG GGSDIQMTQSPSSLSASVGDRVTITCKASQNVGTNVGWYQQKPGKAPKALIYS ASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKV EIKHHHHHHEPEA</td>

<td> 164</td><td> ACP133 (WW0196) IL-2-6xHis (“6xHis” disclosed as SEQ ID NO.: 354)</td><td> mdmrvpaqllgllllwlrgarcaptssstkktqlqlehllldlqmilngmnyknpkltrmltfldympkkatelkhlqcle eelkpleevlnlaqsknfhlrprdlisninvivlelkgsettfinceyadetativeflnrwitfcqsiistltHHHHHH</td>

<td> 165</td><td> ACP147 IL-2 fusion protein</td><td> mdmrvpaqllgllllwlrgarcaptssstkktqlqlehllldlqmilngmnyknpkltrmltfldympkkatelkhlqcle eelkpleevlnlaqsknfhlrprdlisninvivlelkgsettfinceyadetativeflnrwitfcqsiistltSGGPGPAG MKGLPGSEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGL EWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTI GGSLSVSSQGTLVTVSSggggsggggsggggsggggsggggsggggsSGGPGPAGMKGLPG SEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAI DSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDA LDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITC KASQNVGTNVGWYQQKPGKAPKALIYSASFRYSGVPSRFSGSGSGTDFTLTIS SLQPEDFATYYCQQYYTYPYTFGGGTKVEIKggggsggggsggggsQVQLQESGGG LVQAGGSLRLSCAASGRIFSIDIMSWYRQAPGKQRELVARITRGGTISYDDSVK GRFTISRDNAKNTVYLQMNSLKPEDTGVYYCNALYGTDYWGKGTQVTVSSH HHHHHEPEA</td>

<td> 166</td><td> ACP148 IL-2 fusion protein</td><td> mdmrvpaqllgllllwlrgarcQVQLQESGGGLVQAGGSLRLSCAASGRIFSIDIMSWYR QAPGKQRELVARITRGGTISYDDSVKGRFTISRDNAKNTVYLQMNSLKPEDTG VYYCNALYGTDYWGKGTQVTVSSggggsggggsggggsaptssstkktqlqlehllldlqmilngm nyknpkltrmltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrprdlismnvivlelkgsettfmceyadet ativeflnrwitfcqsiistltSGGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRLSCAAS</td>

<td></td><td></td><td> GFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTT LYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggsggggsgg ggsggggsSGGPGPAGMKGLPGSEVQLVESGGGLVQPGGSLRLSCAASGFTFSSY TLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNS LRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDI QMTQSPSSLSASVGDRVTITCKASQNVGTNVGWYQQKPGKAPKALIYSASFR YSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIKH HHHHHEPEA</td>

<td> 167</td><td> ACP149 IL-2 fusion protein</td><td> mdmrvpaqllgllllwlrgarcQVQLQESGGGLVQAGGSLRLSCAASGRIFSIDIMSWYR QAPGKQRELVARITRGGTISYDDSVKGRFTISRDNAKNTVYLQMNSLKPEDTG VYYCNALYGTDYWGKGTQVTVSSSGGPGPAGMKGLPGSaptssstkktqlqlehllldlq milnginnyknpkltrmltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrprdlismnvivlelkgsettfin ceyadetativeflnrwitfcqsiistltSGGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRL SCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRD NAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggs ggggsggggsggggsSGGPGPAGMKGLPGSEVQLVESGGGLVQPGGSLRLSCAASG FTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLY LQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGG GGSDIQMTQSPSSLSASVGDRVTITCKASQNVGTNVGWYQQKPGKAPKALIYS ASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKV EIKHHHHHHEPEA</td>

<td> 168</td><td> ACP33 Mouse IFNafusion protein</td><td> mdmrvpaqllgllllwlrgarcEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVR QAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDT AVYYCTIGGSLSVSSQGTLVTVSSSGGPGPAGMKGLPGScdlpqthnlmkraltllvqmrr Isplscikdrkdfgipqekvdaqqikkaqaipviseltqqilmftskdssaawnttlldsfcndihqqindiqgclmqqvg vqeipltqedallavrkyfhritvylrekkhspcawewraevwralsssanvSGGPGPAGMKGLPGSEV QLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGS GRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQ GTLVTVSSHHHHHHEPEA</td>

<td> 169</td><td> ACP131 Mouse IFNa</td><td> mdmrvpaqllgllllwlrgarccdlpqthnlmkraltllvqmrrlsplsclkdrkdfgipqekvdaqqikkaqaipvlsel tqqilmftskdssaawnttlldsfcndlhqqlndlqgclmqqvgvqeipltqedallavrkyfhritvylrekkhspcawe wraevwralsssanvlgrlreekHHHHHHEPEA</td>

<td> 170</td><td> ACP125 Mouse IFNafusion protein</td><td> mdmrvpaqllgllllwlrgarcEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVR QAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDT AVYYCTIGGSLSVSSQGTLVTVSSSGGPGPAGMKGLPGScdlpqthnlmkraltllvqmrr Isplsclkdrkdfglpqekvdaqqikkaqaipvlseltqqilmftskdssaawnttlldsfcndlliqqlndlqgclmqqvg vqeipltqedallavrkyfhritvylrekkhspcawewraevwralsssanvlgrlreekHHHHHHEPEA</td>

<td> 171</td><td> ACP126 Mouse IFNafusion protein</td><td> mdmrvpaqllgllllwlrgarccdlpqthnlmkraltllvqmrrlsplsclkdrkdfgipqekvdaqqikkaqaipvlsel tqqilniftskdssaawnttlldsfcndlhqqlndlqgclmqqvgvqeipltqedallavrkyfhritvylrekkhspcawe wraevwralsssanvlgrlreekSGGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRLSC AASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNA KTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSHHHHHHEPEA</td>

<td> 172</td><td> ACP127 Mouse IFNafusion protein</td><td> mdmrvpaqllgllllwlrgarcEAHKSEIAHRYNDLGEQHFKGLVLIAFSQYLQKCSYDE HAKLVQEVTDFAKTCVADESAANCDKSLHTLFGDKLCAIPNLRENYGELADC CTKQEPERNECFLQHKDDNPSLPPFERPEAEAMCTSFKENPTTFMGHYLHEVA RRHPYFYAPELLYYAEQYNEILTQCCAEADKESCLTPKLDGVKEKALVSSVRQ RMKCSSMQKFGERAFKAWAVARLSQTFPNADFAEITKLATDLTKVNKECCH GDLLECADDRAELAKYMCENQATISSKLQTCCDKPLLKKAHCLSEVEHDIMP ADLPAIAADFVEDQEVCKNYAEAKDVFLGTFLYEYSRRHPDYSVSLLLRLAK KYEATLEKCCAEANPPACYGTVLAEFQPLVEEPKNLVKTNCDLYEKLGEYGF QNAILVRYTQKAPQVSTPTLVEAARNLGRVGTKCCTLPEDQRLPCVEDYLSAI LNRVCLLHEKTPVSEHVTKCCSGSLVERRPCFSALTVDETYVPKEFKAETFTFH</td>

<td></td><td></td><td> SDICTLPEKEKQIKKQTALAELVKHKPKATAEQLKTVMDDFAQFLDTCCKAA DKDTCFSTEGPNLVTRCKDALASGGPGPAGMKGLPGScdlpqthnlmkraltllvqmrrls plsclkdrkdfgtpqekvdaqqikkaqaipvlseltqqilmftskdssaawnttlldsfcndlhqqlndlqgclmqqvgv qetpltqedallavrkyfhritvylrekkhspcawewraevwralsssanvlgrlreekSGGPGPAGMKGLP GSEAHKSEIAHRYNDLGEQHFKGLVLIAFSQYLQKCSYDEHAKLVQEVTDFA KTCVADESAANCDKSLHTLFGDKLCAIPNLRENYGELADCCTKQEPERNECFL QHKDDNPSLPPFERPEAEAMCTSFKENPTTFMGHYLHEVARRHPYFYAPELLY YAEQYNEILTQCCAEADKESCLTPKLDGVKEKALVSSVRQRMKCSSMQKFGE RAFKAWAVARLSQTFPNADFAEITKLATDLTKVNKECCHGDLLECADDRAEL AKYMCENQATISSKLQTCCDKPLLKKAHCLSEVEHDTMPADLPAIAADFVED QEVCKNYAEAKDVFLGTFLYEYSRRHPDYSVSLLLRLAKKYEATLEKCCAEA NPPACYGTVLAEFQPLVEEPKNLVKTNCDLYEKLGEYGFQNAILVRYTQKAP QVSTPTLVEAARNLGRVGTKCCTLPEDQRLPCVEDYLSAILNRVCLLHEKIPV SEHVTKCCSGSLVERRPCFSALTVDETYVPKEFKAETFTFHSDICTLPEKEKQIK KQTALAELVKHKPKATAEQLKTVMDDFAQFLDTCCKAADKDTCFSTEGPNL VTRCKDALAHHHHHHEPEA</td>

<td> 173</td><td> ACP128 Mouse IFNafusion protein</td><td> mdmrvpaqllgllllwlrgarcEAHKSEIAHRYNDLGEQHFKGLVLIAFSQYLQKCSYDE HAKLVQEVTDFAKTCVADESAANCDKSLHTLFGDKLCAIPNLRENYGELADC CTKQEPERNECFLQHKDDNPSLPPFERPEAEAMCTSFKENPTTFMGHYLHEVA RRHPYFYAPELLYYAEQYNEILTQCCAEADKESCLTPKLDGVKEKALVSSVRQ RMKCSSMQKFGERAFKAWAVARLSQTFPNADFAEITKLATDLTKVNKECCH GDLLECADDRAELAKYMCENQATISSKLQTCCDKPLLKKAHCLSEVEHDTMP ADLPAIAADFVEDQEVCKNYAEAKDVFLGTFLYEYSRRHPDYSVSLLLRLAK KYEATLEKCCAEANPPACYGTVLAEFQPLVEEPKNLVKTNCDLYEKLGEYGF QNAILVRYTQKAPQVSIPTLVEAARNLGRVGTKCCTLPEDQRLPCVEDYLSAI LNRVCLLHEKIPVSEHVTKCCSGSLVERRPCFSALTVDETYVPKEFKAETFTFH SDICTLPEKEKQIKKQTALAELVKHKPKATAEQLKTVMDDFAQFLDTCCKAA DKDTCFSTEGPNLVTRCKDALASGGPGPAGMKGLPGScdlpqthnlmkraltllvqmrrls plsclkdrkdfgtpqekvdaqqikkaqaipvlseltqqilmftskdssaawnttlldsfcndlhqqlndlqgclmqqvgv qefpltqedallavrkyfhritvylrekkhspcawewraevwralsssanvlgrlreekHHHHHHEPEA</td>

<td> 174</td><td> ACP129 Mouse IFNafusion protein</td><td> mdmrvpaqllgllllwlrgarccdlpqthnlmkraltllvqmrrlsplsclkdrkdfgtpqekvdaqqikkaqaipvlsel tqqilmftskdssaawnttlldsfcndlhqqlndlqgclmqqvgvqetpltqedallavrkyfhritvylrekkhspcawe wraevwralsssanvlgrlreekSGGPGPAGMKGLPGSEAHKSEIAHRYNDLGEQHFKGL VLIAFSQYLQKCSYDEHAKLVQEVTDFAKTCVADESAANCDKSLHTLFGDKL CAIPNLRENYGELADCCTKQEPERNECFLQHKDDNPSLPPFERPEAEAMCTSF KENPTTFMGHYLHEVARRHPYFYAPELLYYAEQYNEILTQCCAEADKESCLTP KLDGVKEKALVSSVRQRMKCSSMQKFGERAFKAWAVARLSQTFPNADFAEIT KLATDLTKVNKECCHGDLLECADDRAELAKYMCENQATISSKLQTCCDKPLL KKAHCLSEVEHDTMPADLPAIAADFVEDQEVCKNYAEAKDVFLGTFLYEYSR RHPDYSVSLLLRLAKKYEATLEKCCAEANPPACYGTVLAEFQPLVEEPKNLVK TNCDLYEKLGEYGFQNAILVRYTQKAPQVSTPTLVEAARNLGRVGTKCCTLP EDQRLPCVEDYLSAILNRVCLLHEKTPVSEHVTKCCSGSLVERRPCFSALTVDE TYVPKEFKAETFTFHSDICTLPEKEKQIKKQTALAELVKHKPKATAEQLKTVM DDFAQFLDTCCKAADKDTCFSTEGPNLVIRCKDALAHHHHHHEPEA</td>

<td> 175</td><td> ACP150 Mouse IFNafusion protein</td><td> mdmrvpaqllgllllwlrgarcQVQLQESGGGLAQAGGSLSLSCAASGFTVSNSVMAWY RQIPGKQREFVAIINSVGSTNYADSVKGRFTISRDNAKNTVYLQMNNLKPEDT AVYVCNRNFDRIYWGQGTQVTVSSggggsggggsggggsEVQLVESGGGLVQPGNS LRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTI SRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSSGGPGPAG MKGLPGScdlpqthnlrnkraltllvqmrrlsplsclkdrkdfgtpqekvdaqqikkaqaipvlseltqqilniftskd ssaawnttlldsfcndlhqqlndlqgclmqqvgvqetpltqedallavrkyfhritvylrekkhspcawewraevwral sssanvlgrlreekSGGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRLSCAASGFTF SKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYL QMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSHHHHHHEPEA</td>

<td> 176</td><td> ACP151 Mouse IFNa-</td><td> mdmrvpaqllgllllwlrgarcEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVR QAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDT AVYYCTIGGSLSVSSQGTLVTVSSSGGPGPAGMKGLPGScdlpqthnlrnkraltllvqmrr Isplsclkdrkdfgtpqekvdaqqikkaqaipvlseltqqilmftskdssaawnttlldsfcndlhqqlndlqgclmqqvg vqefpltqedallavrkyfhritvylrekkhspcawewraevwralsssanvlgrlreekSGGPGPAGMKGLP</td>

<td></td><td> fusion protein</td><td> GSEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSS ISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSV SSQGTLVTVSSggggsggggsggggsQVQLQESGGGLAQAGGSLSLSCAASGFTVSN SVMAWYRQTPGKQREFVAIINSVGSTNYADSVKGRFTISRDNAKNTVYLQMN NLKPEDTAVYVCNRNFDRIYWGQGTQVTVSSHHHHHHEPEA</td>

<td> 177</td><td> ACP152 Mouse IFNafusion protein</td><td> mdmrvpaqllgllllwlrgarcEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVR QAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDT AVYY CTIGGSLS VSSQGTLVTVS Sggggsggggsggggscdlpqthnlmkraltllvqmrrlsplscl kdrkdfgipqekvdaqqikkaqaipvlseltqqilniftskdssaawnttlldsfcndlhqqlndlqgclmqqvgvqeipl tqedallavrkyfhritvylrekkhspcawewraevwralsssanvlgrlreekggggsggggsggggsEVQLVE SGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTL YAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVT VSSHHHHHHEPEA</td>

<td> 178</td><td> ACP153 (WW0201) (IL-2 Conjugate)</td><td> mdmrvpaqllgllllwlrgarcaptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcle eelkpleevlnlaqsknfhlrprdlisninvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpGPAGL YAQpgsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLE WVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIG GSLSVSSQGTLVTVSSggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEV QLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSS YTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDY WGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKAS QNVGTNVGWYQQKPGKAPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQP EDFAIYYCQQYYTYPYTFGGGTKVEIKHHHHHHEPEA</td>

<td> 179</td><td> ACP154 (WW0202) (IL-2 Conjugate)</td><td> mdmrvpaqllgllllwlrgarcaptssstkktqlqlehllldlqmilngmnyknpkltrmltfldympkkatelkhlqcle eelkpleevlnlaqsknfhlrprdlisninvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpPGGPA GIGpgsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEW VSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGS LSVSSQGTLVTVSSggggsggggsggggsggggsggggsggggssggpPGGPAGIGpgsEVQLV ESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTY SPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQ GTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKASQNVG TNVGWYQQKPGKAPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFA TYYCQQYYIYPYTFGGGTKVEIKHHHHHHEPEA</td>

<td> 180</td><td> ACP155 (WW0203) (IL-2 Conjugate)</td><td> mdmrvpaqllgllllwlrgarcaptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcle eelkpleevlnlaqsknfhlrprdlisninvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpALFKSS FPpgsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWV SSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSL SVSSQGTLVTVSSggggsggggsggggsggggsggggsggggssggpALFKSSFPpgsEVQLVE SGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYS PDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQG TTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKASQNVGT NVGWYQQKPGKAPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFAT YYCQQYYTYPYTFGGGTKVEIKHHHHHHEPEA</td>

<td> 181</td><td> ACP156 (WW0204) (IL-2 Conjugate)</td><td> mdmrvpaqllgllllwlrgarcaptssstkktqlqlehllldlqmilngmnyknpkltrmltfldympkkatelkhlqcle eelkpleevlnlaqsknfhlrprdlisninvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpPLAQK LKSSpgsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLE WVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIG GSLSVSSQGTLVTVSSggggsggggsggggsggggsggggsggggssggpPLAQKLKSSpgsEV QLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSS YTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDY WGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKAS QNVGTNVGWYQQKPGKAPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQP EDFAIYYCQQYYTYPYTFGGGTKVEIKHHHHHHEPEA</td>

<td> 182</td><td> ACP157 (WW0205) (IL-2 Conjugate)</td><td> mdmrvpaqllgllllwlrgarcaptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcle eelkpleevlnlaqsknfhlrprdlisninvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpPGGPA GIGalfkssfpPLAQKLKSSpgsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGM SWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSL RPEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggsggggsggggsggggssggp PGGPAGIGalfkssfpPLAQKLKSSpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFS SYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQM NSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGS DIQMTQSPSSLSASVGDRVTITCKASQNVGTNVGWYQQKPGKAPKALIYSASF RYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIK HHHHHHEPEA</td>

<td> 183</td><td></td><td> Not assigned</td>

<td> 184</td><td></td><td> Not assigned</td>

<td> 185</td><td></td><td> Not assigned</td>

<td> 186</td><td></td><td> Not assigned</td>

<td> 187</td><td></td><td> Not assigned</td>

<td> 188</td><td></td><td> Not assigned</td>

<td> 189</td><td></td><td> Not assigned</td>

<td> 190</td><td></td><td> Not assigned</td>

<td> 191</td><td> Blocker 2 (IL2 blocker)</td><td> mdmrvpaqllgllllwlrgarcEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVR QAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTA VYYCARDSNWDALDYWGQGTTVTVSSggggsggggsggggsDIQMTQSPSSLSASV GDRVTITCKASQNVGTNVGWYQQKPGKAPKALIYSASFRYSGVPSRFSGSGSG TDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIKHHHHHH</td>

<td> 192</td><td> Blocker 12 (IL-12 blocker)</td><td> mdmrvpaqllgllllwlrgarcQSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQQ LPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSY DRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSC AASGFTFSSYGMHWVRQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDN SKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 193</td><td> HumanIF NA2b</td><td> cdlpqthslgsrrtlmllaqmrrislfsclkdrhdfgtpqeefgnqfqkaetipvlhemiqqifiilfstkdssaawdetlldk iytelyqqlndleacviqgvgvtetplmkedsilavrkyfqritlylkekkyspcawewraeimrsfslstnlqeslrske HHHHHH**</td>

<td> 194</td><td> ACP239geneart</td><td> iwelkkdvyweldwypdapgemwltcdtpeedgitwtldqssevlgsgktltiqvkefgdagqytchkggevlshs llllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwlttistdltfsvkssrgssdpqgvtcgaatlsaervrgd nkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssffirdiikpdppknlqlkplknsrqvevsweypdt wstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvraqdryyssswsewasvpcsggggsggggsgg ggsrvipvsgparclsqsmllkttddmvktareklkhysctaedidheditrdqtstlktclplelhknesclatretssttrgs clppqktslmmtlclgsiyedlkmyqtefqainaalqnhnhqqiildkgmlvaidelmqslnhngetlrqkppvgead pyrvkmklcillhafstrvvtmrvmgylssahhhhhh</td>

<td> 195</td><td> 3CYT5_sd Ab</td><td> QVQLQESGGGLVQAGGSLRLSCAASGRTFSSVYDMGWFRQAPGKDREFVARI TESARNTRYADSVRGRFTISRDNAKNTVYLQMNNLELEDAAVYYCAADPQT VWGTPDYWGQGTQVTVSSAAAYPYDVPDYGSHHHHHH</td>

<td> 196</td><td> ACP248</td><td> QSVLTQPPSVSGAPGQRVTISCtGSsSNIGSNTVKWYQQLPGTAPKLLIYgNDQR PSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPAyvFGTGTKVT VLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWVRQ APGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDT AVYYCKTHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 197</td><td> ACP249</td><td> QSVLTQPPSVSGAPGQRVTISCtGSsSNIGSNTVKWYQQLPGTAPKLLIYYNDQ RPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPAyvFGTGTK VTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWV RQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAE DTAVYYCKTHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 198</td><td> ACP250</td><td> QSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQQLPGTAPKLLIYYNDQ RPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLFGTGTK</td>

<td></td><td></td><td> VTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYaMHWV RQAPGKGLEWVAvIsYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAE DTAVYYCarHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 199</td><td> ACP251</td><td> QSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQQLPGTAPKLLIYYNDQ RPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLFGTGTK VTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWV RQAPGKGLEWVAFIRYeGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAE DTAVYYCKTHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 200</td><td> ACP252</td><td> QSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQQLPGTAPKLLIYYNDQ RPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLFGTGTK VTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWV RQAPGKGLEWVAFIRYDGSNKYYAeSVKGRFTISRDNSKNTLYLQMNSLRAE DTAVYYCKTHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 201</td><td> ACP253</td><td> QSVLTQPPSVSGAPGQRVTISCSGSRSNIGSqTVKWYQQLPGTAPKLLIYYNDQ RPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYeRYTHPALLFGTGTKV TVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWVR QAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAED TAVYYCKTHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 202</td><td> ACP254</td><td> QSVLTQPPSVSGAPGQRVTISCSGSRSNIGSqTVKWYQQLPGTAPKLLIYYNDQ RPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYsRYTHPALLFGTGTKV TVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWVR QAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAED TAVYYCKTHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 203</td><td> ACP255</td><td> QSVLTQPPSVSGAPGQRVTISCSGSeSNIGSNTVKWYQQLPGTAPKLLIYYNDQ RPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLFGTGTK VTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWV RQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAE DTAVYYCKTHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 204</td><td> ACP256</td><td> QSVLTQPPSVSGAPGQRVTISCSGSsSNIGSNTVKWYQQLPGTAPKLLIYYNDQ RPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLFGTGTK VTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWV RQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAE DTAVYYCKTHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 205</td><td> ACP257</td><td> QSVLTQPPSVSGAPGQRVTISCSGSRSNIGdNTVKWYQQLPGTAPKLLIYYNDQ RPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLFGTGTK VTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWV RQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAE DTAVYYCKTHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 206</td><td> ACP258</td><td> QSVLTQPPSVSGAPGQRVTISCSGSRSNIGeNTVKWYQQLPGTAPKLLIYYNDQ RPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLFGTGTK VTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWV RQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAE DTAVYYCKTHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 207</td><td> ACP259</td><td> QSVLTQPPSVSGAPGQRVTISCSGSRSNIGSdTVKWYQQLPGTAPKLLIYYNDQ RPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLFGTGTK VTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWV RQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAE DTAVYYCKTHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 208</td><td> ACP260</td><td> QSVLTQPPSVSGAPGQRVTISCSGSRSNIGSeTVKWYQQLPGTAPKLLIYYNDQ RPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLFGTGTK VTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWV RQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAE DTAVYYCKTHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 209</td><td> ACP261</td><td> QSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNdVKWYQQLPGTAPKLLIYYNDQ RPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLFGTGTK VTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWV RQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAE DTAVYYCKTHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 210</td><td> ACP262</td><td> QSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVdWYQQLPGTAPKLLIYYNDQ RPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLFGTGTK VTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWV RQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAE DTAVYYCKTHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 211</td><td> ACP263</td><td> QSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVeWYQQLPGTAPKLLIYYNDQ RPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLFGTGTK VTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWV RQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAE DTAVYYCKTHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 212</td><td> ACP264</td><td> QSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQQLPGTAPKLLIYYNDQ dPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLFGTGTK VTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWV RQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAE DTAVYYCKTHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 213</td><td> ACP265</td><td> QSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQQLPGTAPKLLIYYNDQ ePSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLFGTGTK VTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWV RQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAE DTAVYYCKTHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 214</td><td> ACP266</td><td> QSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQQLPGTAPKLLIYYNDQ RPdGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLFGTGTK VTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWV RQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAE DTAVYYCKTHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 215</td><td> ACP267</td><td> QSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQQLPGTAPKLLIYYNDQ RPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDeYTHPALLFGTGTK VTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWV RQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAE DTAVYYCKTHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 216</td><td> ACP268</td><td> QSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQQLPGTAPKLLIYYNDQ RPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTdPALLFGTGTK VTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWV RQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAE DTAVYYCKTHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 217</td><td> ACP269</td><td> QSVLTQPPSVSGAPGQRVTISCSGSeSNIGSNTVKWYQQLPGTAPKLLIYYNDQ ePSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDeYTHPALLFGTGTKV TVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWVR QAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAED TAVYYCKTHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 218</td><td> ACP270</td><td> QSVLTQPPSVSGAPGQRVTISCSGSeSNIGSNdVKWYQQLPGTAPKLLIYYNDQ RPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLFGTGTK VTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWV RQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAE DTAVYYCKTHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 219</td><td> ACP271</td><td> QSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQQLPGTAPKLLIYYNDQ RPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLFGTGTK VTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFeSYGMHWV RQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAE DTAVYYCKTHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 220</td><td> ACP272</td><td> QSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQQLPGTAPKLLIYYNDQ RPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLFGTGTK VTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSeYGMHWV RQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAE DTAVYYCKTHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 221</td><td> ACP273</td><td> QSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQQLPGTAPKLLIYYNDQ RPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLFGTGTK VTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSdYGMHWV</td>

<td></td><td></td><td> RQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAE DTAVYYCKTHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 222</td><td> ACP274</td><td> QSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQQLPGTAPKLLIYYNDQ RPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLFGTGTK VTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWV RQAPGKGLEWVAFIeYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAE DTAVYYCKTHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 223</td><td> ACP275</td><td> QSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQQLPGTAPKLLIYYNDQ RPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLFGTGTK VTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWV RQAPGKGLEWVAFIdYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAE DTAVYYCKTHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 224</td><td> ACP276</td><td> QSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQQLPGTAPKLLIYYNDQ RPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLFGTGTK VTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWV RQAPGKGLEWVAFIRYDGSNdYYADSVKGRFTISRDNSKNTLYLQMNSLRAE DTAVYYCKTHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 225</td><td> ACP277</td><td> QSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQQLPGTAPKLLIYYNDQ RPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLFGTGTK VTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWV RQAPGKGLEWVAFIRYDGSNeYYADSVKGRFTISRDNSKNTLYLQMNSLRAE DTAVYYCKTHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 226</td><td> ACP278</td><td> QSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQQLPGTAPKLLIYYNDQ RPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLFGTGTK VTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWV RQAPGKGLEWVAFIRYDGSNKYYADSVeGRFTISRDNSKNTLYLQMNSLRAE DTAVYYCKTHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 227</td><td> ACP279</td><td> QSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQQLPGTAPKLLIYYNDQ RPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLFGTGTK VTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWV RQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAE DTAVYYCKTHGSeDNWGQGTMVTVSSHHHHHH</td>

<td> 228</td><td> ACP280</td><td> QSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQQLPGTAPKLLIYYNDQ RPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLFGTGTK VTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWV RQAPGKGLEWVAFIeYDGSNKYYADSVeGRFTISRDNSKNTLYLQMNSLRAED TAVYYCKTHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 229</td><td> ACP281</td><td> QSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQQLPGTAPKLLIYYNDQ RPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLFGTGTK VTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWV RQAPGKGLEWVAFIeYDGSNKYYADSVeGRFTISRDNSKNTLYLQMNSLRAED TAVYYCKTHGSeDNWGQGTMVTVSSHHHHHH</td>

<td> 230</td><td> ACP282</td><td> QSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQQLPGTAPKLLIYYNDQ RPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLFGTGTK VTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWV RQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAE DTAVYYCKTHGSHDNWGQGTMVTVSSHHHHHH</td>

<td> 231</td><td> ACP283 (WW0617)</td><td> iwelkkdvyweldwypdapgemwltcdtpeedgitwtldqssevlgsgktltiqvkefgdagqytchkggevlshs llllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwlttistdltfsvkssrgssdpqgvtcgaatlsaervrgd nkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssffirdiikpdppknlqlkplknsrqvevsweypdt wstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvraqdryyssswsewasvpcs</td>

<td> 232</td><td> 3TOW69sd Ab</td><td> QVQLQESGGGLVQTGGSLRLSCTTSGTIFSGYTMGWYRQAPGEQRELVAVISG GGDTNYADSVKGRFTISRDNTKDTMYLQMNSLKPEDTAVYYCYSREVTPPW KLYWGQGTQVTVSSAAAYPYDVPDYGSHHHHHH</td>

<td> 233</td><td> 3TOW85sd Ab</td><td> QVQLQESGGGLVQEGGSLRLSCAASERIFSTDVMGWYRQAAEKQRELVAWS ARGTTNYLDAVKGRFTISRDNARNTLTLQMNDLKPEDTASYYCYVRETTSPW RIYWGQGTQVTVSSAAAYPYDVPDYGSHHHHHH</td>

<td> 234</td><td> 2TOW91sd Ab</td><td> QVQLQESGGGLVQAGGSLRLSCAASGSIFSANAMGWYRQAPGKQRELVAVIS SGGSTNYADSVKGRFTISRDNAKNTVYLQMNSLKPEDTAVYYCMYSGSYYY TPNDYWGQGTQVTVSSAAAYPYDVPDYGSHHHHHH</td>

<td> 235</td><td> ACP301</td><td> evqlvesggglvqpggslrlscaasgftfssytlawvrqapgkglewvaaidsssytyspdtvrgrftisrdnaknslylq mnslraedtavyycardsnwdaldywgqgttvtvssggggsggggsggggsdiqmtqspsslsasvgdrvtitckasq nvgtnvgwyqqkpgkapkaliysasfiysgvpsrfsgsgsgtdftltisslqpedfatyycqqyytypytfgggtkveik hhhhhh</td>

<td> 236</td><td> Hu2TOW9 1_A</td><td> evqllesggglvqpggslrlscaasGSIFSANAMGwYrqapgkQReLvAVISSGGSTNYADSVK GrftisrdnskntVylqnmslraedtavyycMYSGSYYYTPNDYwgqgtlvtvssAAAYPYDVPD YGSHHHHHH**</td>

<td> 237</td><td> Hu2TOW9 IB</td><td> evqllesggglvqpggslrlscaasGSIFSANAMGwYrqapgkgleLvAVISSGGSTNYADSVKG rftisrdnskntVylqnmslraedtavyycMYSGSYYYTPNDYwgqgtlvtvssAAAYPYDVPDY GSHHHHHH**</td>

<td> 238</td><td> Hu2TOW9 1_c</td><td> evqllesggglvqpggslrlscaasGSIFSANAMGwvrqapgkglewvsVISSGGSTNYADSVKGrf tisrdnskntlylqmnslraedtavyycMYSGSYYYTPNDYwgqgtlvtvssAAAYPYDVPDYGS HHHHHH**</td>

<td> 239</td><td> Hu2TOW9 ID</td><td> QvqllesggglvqpggslrlscaasGSIFSANAMGwYrqapgkQReLvAVISSGGSTNYADSVK GrftisrdnskntVylqnmslraedtavyycMYSGSYYYTPNDYwgqgtlvtvssAAAYPYDVPD YGSHHHHHH**</td>

<td> 240</td><td> HELM2 TOW91</td><td> evqllesggglvqpggslrlscaasgSIfsANamGwYrqapgkgReLvAVissggstNyadsvkgrftisrdns kntVylqmnslraedtavyycMYSGSYYYTPNDYWgqgtlvtvssAAAYPYDVPDYGSHHH HHH**</td>

<td> 241</td><td> HEL2T OW91</td><td> QvqllesggglvqAggslrlscaasgSIfsANamGwYrqapgkQReLvAVissggstNyadsvkgrftisrdn skntVylqmnslraedtavyycMYSGSYYYTPNDYwgqgtlvtvssAAAYPYDVPDYGSHHH HHH**</td>

<td> 242</td><td> Hu3TOW8 5_A</td><td> evqllesggglvqpggslrlscaasERIFSTDVMGwYrqapgkQReLvAVVSARGTTNYLDAV KGrftisrdnskntlylqmnslraedtavyycYVRETTSPWRIYwgqgtlvtvssAAAYPYDVPDYG SHHHHHH**</td>

<td> 243</td><td> Hu3TOW8 5 B</td><td> evqllesggglvqpggslrlscaasERIFSTDVMGwYrqapgkgleLvAVVSARGTTNYLDAVK GrftisrdnskntlylqnmslraedtavyycYVRETTSPWRIYwgqgtlvtvssAAAYPYDVPDYGS HHHHHH**</td>

<td> 244</td><td> Hu3TOW8 5 C</td><td> evqllesggglvqpggslrlscaasERIFSTDVMGwvrqapgkglewvsVVSARGTTNYLDAVKG rftisrdnskntlylqnmslraedtavyycYVRETTSPWRIYwgqgtlvtvssAAAYPYDVPDYGSH HHHHH**</td>

<td> 245</td><td> Hu3TOW8 5 D</td><td> QvqllesggglvqpggslrlscaasERIFSTDVMGwYrqapgkQReLvAVVSARGTTNYLDAV KGrftisrdnskntlylqmnslraedtavyycYVRETTSPWRIYwgqgtlvtvssAAAYPYDVPDYG SHHHHHH**</td>

<td> 246</td><td> HELM3 TOW85</td><td> evqllesggglvqpggslrlscaasERIfsTDVmGwYrqapgkgReLvAWsARgTtNyLdsvkgrftisr dnskntlylqnmslraedtavyycYVRETTSPWRIywgqgtlvtvssAAAYPYDVPDYGSHHHH hh**</td>

<td> 247</td><td> HEL3T OW85</td><td> QvqllesggglvqEggslrlscaasERIfsTDVmGwYrqaAgkQReLvAWsARgTtNyLdAvkgrf tisrdnskntlylqmnslraedtaSyycYVRETTSPWRIywgqgtlvtvssAAAYPYDVPDYGSHH HHHH**</td>

<td> 248</td><td> HELMR 45L3TO W85</td><td> evqllesggglvqpggslrlscaasERIfsTDVmGwYrqapgkgleLvAWsARgTtNyLdsvkgrftisr dnskntlylqnmslraedtavyycYVRETTSPWRIywgqgtlvtvssAAAYPYDVPDYGSHHHH HH**</td>

<td> 249</td><td> Hu3TOW6 9_A</td><td> evqllesggglvqpggslrlscaTsGTIFSGYTMGwYrqapgkQReLvAVISGGGDTNYADSV KGrftisrdnskDtMylqnmslraedtavyycYSREVTPPWKLYwgqgtlvtvssAAAYPYDVPD YGSHHHHHH**</td>

<td> 250</td><td> Hu3TOW6 9 B</td><td> evqllesggglvqpggslrlscaTsGTIFSGYTMGwYrqapgkgleLvAVISGGGDTNYADSVK GrftisrdnskDtMylqmnslraedtavyycYSREVTPPWKLYwgqgtlvtvssAAAYPYDVPDY GSHHHHHH**</td>

<td> 251</td><td> Hu3TOW6 9 C</td><td> evqllesggglvqpggslrlscaasGTIFSGYTMGwvrqapgkglewvsVISGGGDTNYADSVKGr ftisrdnskntlylqmnslraedtavyycYSREVTPPWKLYwgqgtlvtvssAAAYPYDVPDYGSH HHHHH**</td>

<td> 252</td><td> Hu3TOW6 9 D</td><td> QvqllesggglvqpggslrlscaTsGTIFSGYTMGwYrqapgkQReLvAVISGGGDTNYADSV KGrftisrdnskDtMylqnmslraedtavyycYSREVTPPWKLYwgqgtlvtvssAAAYPYDVPD YGSHHHHHH**</td>

<td> 253</td><td> Hu3TOW6 9_E</td><td> evqllesggglvqpggslrlscaTsGTIFSGYTMGwYrqapgkQReLvAVISGGGDTNYADSV KGrftisrdnskntMylqmnslraedtavyycYSREVTPPWKLYwgqgtlvtvssAAAYPYDVPD YGSHHHHHH**</td>

<td> 254</td><td> HELM3 TOW69</td><td> evqllesggglvqpggslrlscaTsgTIfsGyTmGwYrqapgkgReLvAVisGggDtNyadsvkgrftisrd nskntMylqmnslraedtavyycYSREVTPPWKLywgqgtlvtvssAAAYPYDVPDYGSHHH HHH**</td>

<td> 255</td><td> HEL3T OW69</td><td> QvqllesggglvqTggslrlscaTsgTIfsGyTmGwYrqapgkQReLvAVisGggDtNyadsvkgrftisr dnskDtMylqnmslraedtavyycYSREVTPPWKLywgqgtlvtvssAAAYPYDVPDYGSHH HHHH**</td>

<td> 256</td><td> HELMR 45L3TO W69</td><td> evqllesggglvqpggslrlscaTsgTIfsGyTmGwYrqapgkgleLvAVisGggDtNyadsvkgrftisrdn skntMylqmnslraedtavyycYSREVTPPWKLywgqgtlvtvssAAAYPYDVPDYGSHHHH hh**</td>

<td> 257</td><td> ACP363 (WW0441)</td><td> EVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAID SSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDAL DYWGQGTTVTVSSggggsggggsggggsDIQMTQSPSSLSASVGDRVTITCKAREKL WSAVAWYQQKPGKAPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDF ATYYCQQYYTYPYTFGGGTKVEIKHHHHHH</td>

<td> 258</td><td> ACP364 (WW0442)</td><td> EVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAID SSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDAL DYWGQGTTVTVSSggggsggggsggggsDIQMTQSPSSLSASVGDRVTITCKAREKL WSAVAWYQQKPGKAPKsLIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDF ATYYCQOYYTYPYTFGGGTKVEIKHHHHHH</td>

<td> 259</td><td> ACP367 (WW0445)</td><td> EVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAID SSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDAL DYWGQGTTVTVSSggggsggggsggggsDIQMTQSPSSLSASVGDRVTITCKVTEKV WGNVAWYQQKPGKAPISLIYSPSLRKSGVPSRFSGSGSGTDFTLTISSLQPEDF ATYYCQQYYTYPYTFGGGTKVEIKHHHHHH</td>

<td> 260</td><td> ACP369 (WW0449)</td><td> EVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAID SSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDAL DYWGQGTTVTVSSggggsggggsggggsDIQMTQSPSSLSASVGDRVTITCKSSEKL WANVAWYQQKPGKAPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPED F ATYYCQQYYTYPYTFGGGTKVEIKHHHHHH</td>

<td> 261</td><td> ACP370 (WW0450)</td><td> EVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAID SSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDAL DYWGQGTTVTVSSggggsggggsggggsDIQMTQSPSSLSASVGDRVTITCKSSEKL WANVAWYQQKPGKAPKsLIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDF ATYYCQQYYTYPYTFGGGTKVEIKHHHHHH</td>

<td> 262</td><td> ACP380 (WW0522)</td><td> DIQMTQSPSSLSASVGDRVTITCKASQNVGTNVGWYQQKPGKAPKALIYSASF RYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIKr tvaapsvfilppsdeqlksgtaswcllnniypreakvqwkvdnalqsgnsqesvteqdskdstyslsstltlskadyekh kvyacevthqglsspvtksfiirgec</td>

<td> 263</td><td> ACP381 (WW0523)</td><td> DIQMTQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPGKAPKsLIYSASF RYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIKr tvaapsvfilppsdeqlksgtaswcllnniypreakvqwkvdnalqsgnsqesvteqdskdstyslsstltlskadyekh kvyacevthqglsspvtksfiirgec</td>

<td> 264</td><td> ACP382 (WW0524)</td><td> DIQMTQSPSSLSASVGDRVTITCKVTEKVWGNVAWYQQKPGKAPISLIYSPSL RKSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIKr</td>

<td></td><td></td><td> tvaapsvfitppsdeqlksgtaswcllnniypreakvqwkvdnalqsgnsqesvteqdskdstyslsstltlskadyekh kvyacevthqglsspvtksfiirgec</td>

<td> 265</td><td> ACP435</td><td> DIQMTQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPGKAPKsLIYSASF RYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIKr tvaapsvfitppsdeqlksgtaswcllnniypreakvqwkvdnalqsgnsqesvteqdskdstyslsstltlskadyekh kvyacevthqglsspvtksfiirgecggggsggggsggggsggggsggggsggggsevqllesggglvqpggslrlsca asgsifsanamgwyrqapgkqrelvavissggstnyadsvkgrftisrdnskntvylqnmslraedtavyycmysgsy yytpndywgqgtlvtvss**</td>

<td> 266</td><td> ACP436 (WW0578)</td><td> DIQMTQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPGKAPKsLIYSASF RYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIKr tvaapsvfitppsdeqlksgtaswcllnniypreakvqwkvdnalqsgnsqesvteqdskdstyslsstltlskadyekh kvyacevthqglsspvtksfiirgecggggsggggsggggsggggsggggsggggsevqllesggglvqpggslrlsca asgsifsanamgwyrqapgkglelvavissggstnyadsvkgrftisrdnskntvylqmnslraedtavyycmysgsy yytpndywgqgtlvtvss**</td>

<td> 267</td><td> ACP437 (WW0579)</td><td> DIQMTQSPSSLSASVGDRVTITCKVTEKVWGNVAWYQQKPGKAPISLIYSPSL RKSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIKr tvaapsvfitppsdeqlksgtaswcllnnlypreakvqwkvdnalqsgnsqesvteqdskdstyslsstltlskadyekh kvyacevthqglsspvtksfiirgecggggsggggsggggsggggsggggsggggsevqllesggglvqpggslrlsca asgsifsanamgwyrqapgkqrelvavissggstnyadsvkgrftisrdnskntvylqnmslraedtavyycmysgsy yytpndywgqgtlvtvss**</td>

<td> 268</td><td> ACP438 (WW0580)</td><td> DIQMTQSPSSLSASVGDRVTITCKVTEKVWGNVAWYQQKPGKAPISLIYSPSL RKSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIKr tvaapsvfitppsdeqlksgtaswcllnniypreakvqwkvdnalqsgnsqesvteqdskdstyslsstltlskadyekh kvyacevthqglsspvtksfiirgecggggsggggsggggsggggsggggsggggsevqllesggglvqpggslrlsca asgsifsanamgwyrqapgkglelvavissggstnyadsvkgrftisrdnskntvylqmnslraedtavyycmysgsy yytpndywgqgtlvtvss**</td>

<td> 269</td><td> ACP448 (WW0590)</td><td> DIQMTQSPSSLSASVGDRVTITCKSSEKLWANVAWYQQKPGKAPKsLIYSASF RYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIKr tvaapsvfitppsdeqlksgtaswcllnniypreakvqwkvdnalqsgnsqesvteqdskdstyslsstltlskadyekh kvyacevthqglsspvtksfiirgec**</td>

<td> 270</td><td> ACP449 (WW0591)</td><td> DIQMTQSPSSLSASVGDRVTITCKSSEKLWANVAWYQQKPGKAPKLLIYSASF RYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIKr tvaapsvfitppsdeqlksgtaswcllnniypreakvqwkvdnalqsgnsqesvteqdskdstyslsstltlskadyekh kvyacevthqglsspvtksfiirgec**</td>

<td> 271</td><td> ACP450 (WW0592)</td><td> DIQMTQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPGKAPKLLIYSASF RYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIKr tvaapsvfitppsdeqlksgtaswcllnniypreakvqwkvdnalqsgnsqesvteqdskdstyslsstltlskadyekh kvyacevthqglsspvtksfiirgec**</td>

<td> 272</td><td> ACP439 (WW0581)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsEVQLVESGG GLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTL VTVSS ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGS LRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISR DNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGG SGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKSSEKLWANVAWYQQKPG KAPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYP YTFGGGTKVEIK</td>

<td> 273</td><td> ACP440 (WW0582)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsEVQLVESGG GLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTL VTVSS ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGS LRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISR DNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGG SGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKSSEKLWANVAWYQQKPG KAPKsLIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPY TFGGGTKVEIK</td>

<td> 274</td><td> ACP441 (WW0583)</td><td> aptssstkktqlqlehllldlqmilngiimyknpkltrmltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsEVQLVESGG GLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGS LRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISR DNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGG SGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKSSEKLWANVAWYQQKPG KAPKLLIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPY TFGGGTKVEIK</td>

<td> 275</td><td> ACP442 (WW0584)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsEVQLVESGG GLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGS LRLSCAASGFTFSSYTLAWVRQAPGKcLEWVAAIDSSSYTYSPDTVRGRFTISR DNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGG SGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKSSEKLWANVAWYQQKPG KAPKsLIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPY TFGcGTKVEIK</td>

<td> 276</td><td> ACP443 (WW0585)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsEVQLVESGG GLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGS LRLSCAASGFTFSSYTLAWVRQAPGKcLEWVAAIDSSSYTYSPDTVRGRFTISR DNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGG SGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKSSEKLWANVAWYQQKPG KAPKLLIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPY TFGcGTKVEIK</td>

<td> 277</td><td> ACP444 (WW0586)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsEVQLVESGG GLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGS LRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISR DNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGcGTTVTVSSGGGG SGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKSSEKLWANVAWYQQKPG KcPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPY TFGGGTKVEIK</td>

<td> 278</td><td> ACP445 (WW0587)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsEVQLVESGG GLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGS LRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISR DNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSsggpG PAGLYAQpgsDIQMTQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPGKA PKLLIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTF GGGTKVEIK</td>

<td> 279</td><td> ACP446 (WW0588)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsEVQLVESGG GLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGS LRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISR DNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGG SGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPG</td>

<td></td><td></td><td> KAPKLLIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPY TFGGGTKVEIK</td>

<td> 280</td><td> ACP447 (WW0589)</td><td> aptssstkktqlqlehllldlqmilngiimyknpkltrmltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsEVQLVESGG GLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGS LRLSCAASGFTFSSYTLAWVRQAPGKcLEWVAAIDSSSYTYSPDTVRGRFTISR DNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGG SGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPG KAPKLLIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPY TFGcGTKVEIK</td>

<td> 281</td><td> ACP451 (WW0615)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpALFKSSFPpgsEVQLVESGGG LVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAES VKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSgg ggsggggsggggsggggsggggsggggssggpALFKSSFPpgsEVQLVESGGGLVQPGGSLRL SCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDN AKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSG GGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPGKA PKsLIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTF GGGTKVEIK**</td>

<td> 282</td><td> ACP452 (WW0616)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpALFKSSFPpgsEVQLVESGGG LVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAES VKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSgg ggsggggsggggsggggsggggsggggssggpALFKSSFPpgsEVQLVESGGGLVQPGGSLRL SCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDN AKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSG GGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKVTEKVWGNVAWYQQKPGK APISLIYSPSLRKSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTF GGGTKVEIK**</td>

<td> 283</td><td> ACP453 (WW0617)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpALFKSSFPpgsEVQLVESGGG LVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAES VKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSgg ggsggggsggggsggggsggggsggggssggpALFKSSFPpgsEVQLVESGGGLVQPGGSLRL SCAASGFTFSSYTLAWVRQAPGKcLEWVAAIDSSSYTYSPDTVRGRFTISRDNA KNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGG GGSGGGGSDIQMTQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPGKAP KsLIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFG cGTKVEIK**</td>

<td> 284</td><td> ACP454 (WW0618)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpALFKSSFPpgsEVQLVESGGG LVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAES VKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSgg ggsggggsggggsggggsggggsggggssggpALFKSSFPpgsEVQLVESGGGLVQPGGSLRL SCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDN AKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGcGTTVTVSSGGGGSG GGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPGKc PKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTF GGGTKVEIK**</td>

<td> 285</td><td> ACP455 (WW0619)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpALFKSSFPpgsEVQLVESGGG LVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAES VKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSgg ggsggggsggggsggggsggggsggggssggpALFKSSFPpgsEVQLVESGGGLVQPGGSLRL SCAASGFTFSSYTLAWVRQAPGKcLEWVAAIDSSSYTYSPDTVRGRFTISRDNA</td>

<td></td><td></td><td> KNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGG GGSGGGGSDIQMTQSPSSLSASVGDRVTITCKVTEKVWGNVAWYQQKPGKA PISLIYSPSLRKSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFG cGTKVEIK**</td>

<td> 441</td><td> ACP456 (WW0620)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpALFKSSFPpgsEVQLVESGGG LVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAES VKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSgg ggsggggsggggsggggsggggsggggssggpALFKSSFPpgsEVQLVESGGGLVQPGGSLRL SCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDN AKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGcGTTVTVSSGGGGSG GGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKVTEKVWGNVAWYQQKPGKc PISLIYSPSLRKSGVPSRFSGSGSGTDFTLTISSLQPEDFAIYYCQQYYTYPYTFG GGTKVEIK**</td>

<td> 286</td><td> ACP457 (WW0621)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpALFKSSFPpgsEVQLVESGGG LVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAES VKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSgg ggsggggsggggsggggsggggsggggssggpALFKSSFPpgsEVQLVESGGGLVQPGGSLRL SCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDN AKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSastkgpsvfp lapsskstsggtaalgclvkdylpepvtvswnsgaltsgvhtlpavlqssglyslssvvtvpssslgtqtyicnvnhkpsnt kvdkrvepksc**</td>

<td> 287</td><td> ACP458 (WW0622)</td><td> eskygppcppcpapeflggpsvflfppkpkdtlmisrtpevtcvwdvsqedpevqfnwyvdgvevhnaktkpree qfiistyrwsvltvlhqdwlngkeykckvsnkglpssiektiskakgqprepqvytlppsqeemtknqvsltclvkgfy psdiavewesngqpennykttppvldsdgsfflysrltvdksrwqegnvfscsvmhealhnhytqkslslslgksggp ALFKSSFPpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkplee vlnlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsggggsggg gsggggsggggssggpALFKSSFPpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSY TLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNS LRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSastkgpsvlplapsskstsggtaalgclv kdyfpepvtvswnsgaltsgvhtfpavlqssglyslsswtvpssslgtqtyicnvnhkpsntkvdkrvepksc**</td>

<td> 288</td><td> ACP459 (WW0623)</td><td> eskygppcppcpapeflggpsvflfppkpkdtlmisrtpevtcvwdvsqedpevqfnwyvdgvevhnaktkpree qfiistyrwsvltvlhqdwlngkeykckvsnkglpssiektiskakgqprepqvytlppsqeemtknqvsltclvkgfy psdiavewesngqpennykttppvldsdgsfflysrltvdksrwqegnvfscsvmhealhnhytqkslslslgksggp ALFKSSFPpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkplee vlnlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsggggsggg gsggggsggggssggpALFKSSFPpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSY TLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNS LRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDI QMTQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPGKAPKsLIYSASFRY SGVPSRFSGSGSGTDFTLTISSLQPEDFAIYYCQQYYTYPYTFGGGTKVEIK**</td>

<td> 289</td><td> ACP460 (WW0624)</td><td> eskygppcppcpapeflggpsvflfppkpkdtlmisrtpevtcvwdvsqedpevqfnwyvdgvevhnaktkpree qfiistyrwsvltvlhqdwlngkeykckvsnkglpssiektiskakgqprepqvytlppsqeemtknqvsltclvkgfy psdiavewesngqpennykttppvldsdgsfflysrltvdksrwqegnvfscsvmhealhnhytqkslslslgksggp ALFKSSFPpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkplee vlnlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsggggsggg gsggggsggggssggpALFKSSFPpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSY TLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNS LRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDI QMTQSPSSLSASVGDRVTITCKVTEKVWGNVAWYQQKPGKAPISLIYSPSLRK SGVPSRFSGSGSGTDFTLTISSLQPEDFAIYYCQQYYTYPYTFGGGTKVEIK**</td>

<td> 290</td><td> ACP461 (WW0625)</td><td> eskygppcppcpapeflggpsvflfppkpkdtlmisrtpevtcvwdvsqedpevqfnwyvdgvevhnaktkpree qfiistyrwsvltvlhqdwlngkeykckvsnkglpssiektiskakgqprepqvytlppsqeemtknqvsltclvkgfy psdiavewesngqpennykttppvldsdgsfflysrltvdksrwqegnvfscsvmhealhnhytqkslslslgksggp ALFKSSFPpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkplee vlnlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsggggsggg gsggggsggggssggpALFKSSFPpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSY</td>

<td></td><td></td><td> TLAWVRQAPGKcLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSL RAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQ MTQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPGKAPKsLIYSASFRYS GVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGcGTKVEIK**</td>

<td> 291</td><td> ACP462 (WW0626)</td><td> eskygppcppcpapeflggpsvflfppkpkdtlmisrtpevtcvwdvsqedpevqfnwyvdgvevhnaktkpree qfiistyrwsvltvlhqdwlngkeykckvsnkglpssiektiskakgqprepqvytlppsqeemtknqvsltclvkgfy psdiavewesngqpennykttppvldsdgsfflysrltvdksrwqegnvfscsvmhealhnhytqkslslslgksggp ALFKSSFPpgsaptssstkktqlqlehllldlqmilnginnyknpkltrmltfkfympkkatelkhlqcleeelkplee vlnlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsggggsggg gsggggsggggssggpALFKSSFPpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSY TLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNS LRAEDTAVYYCARDSNWDALDYWGcGTTVTVSSGGGGSGGGGSGGGGSDIQ MTQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPGKcPKALIYSASFRYS GVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIK**</td>

<td> 292</td><td> ACP463 (WW0627)</td><td> eskygppcppcpapeflggpsvflfppkpkdtlmisrtpevtcvwdvsqedpevqfnwyvdgvevhnaktkpree qfiistyrwsvltvlhqdwlngkeykckvsnkglpssiektiskakgqprepqvytlppsqeemtknqvsltclvkgfy psdiavewesngqpennykttppvldsdgsfflysrltvdksrwqegnvfscsvmhealhnhytqkslslslgksggp ALFKSSFPpgsaptssstkktqlqlehllldlqmilnginnyknpkltrmltfkfympkkatelkhlqcleeelkplee vlnlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsggggsggg gsggggsggggssggpALFKSSFPpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSY TLAWVRQAPGKcLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSL RAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQ MTQSPSSLSASVGDRVTITCKVTEKVWGNVAWYQQKPGKAPISLIYSPSLRKS GVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGcGTKVEIK**</td>

<td> 293</td><td> ACP464 (WW0628)</td><td> eskygppcppcpapeflggpsvflfppkpkdtlmisrtpevtcvwdvsqedpevqfnwyvdgvevhnaktkpree qfiistyrwsvltvlhqdwlngkeykckvsnkglpssiektiskakgqprepqvytlppsqeemtknqvsltclvkgfy psdiavewesngqpennykttppvldsdgsfflysrltvdksrwqegnvfscsvmhealhnhytqkslslslgksggp ALFKSSFPpgsaptssstkktqlqlehllldlqmilnginnyknpkltrmltfkfympkkatelkhlqcleeelkplee vlnlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsggggsggg gsggggsggggssggpALFKSSFPpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSY TLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNS LRAEDTAVYYCARDSNWDALDYWGcGTTVTVSSGGGGSGGGGSGGGGSDIQ MTQSPSSLSASVGDRVTITCKVTEKVWGNVAWYQQKPGKcPISLIYSPSLRKS GVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIK**</td>

<td> 294</td><td> ACP465 (WW0629)</td><td> vprdcgckpcictvpevssvfifppkpkdvltitltpkvtcvwdiskddpevqfswfvddvevhtaqtqpreeqfnstf rsvselpimhqdwlngkefkcrvnsaalpapiektisktkgrpkapqvytipppkeqmakdkvsltcmitdflpeditv ewqwngqpaenykntqpimdtdgsyfvysklnvqksnweagntftcsvlheglhnhhtekslshspgksggpAL FKSSFPpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfklympkkatelkhlqcleeelkpleevln laqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsggggsggggsg gggsggggssggpALFKSSFPpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTL AWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLR AEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQM TQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPGKAPKsLIYSASFRYSG VPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIK**</td>

<td> 295</td><td> ACP466 (WW0630)</td><td> vprdcgckpcictvpevssvfifppkpkdvltitltpkvtcvwdiskddpevqfswfvddvevhtaqtqpreeqfnstf rsvselpimhqdwlngkefkcrvnsaalpapiektisktkgrpkapqvytipppkeqmakdkvsltcmitdflpeditv ewqwngqpaenykntqpimdtdgsyfvysklnvqksnweagntftcsvlheglhnhhtekslshspgksggpAL FKSSFPpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfklympkkatelkhlqcleeelkpleevln laqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsggggsggggsg gggsggggssggpALFKSSFPpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTL AWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLR AEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQM TQSPSSLSASVGDRVTITCKVTEKVWGNVAWYQQKPGKAPISLIYSPSLRKSG VPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIK**</td>

<td> 296</td><td> ACP467 (WW0631)</td><td> vprdcgckpcictvpevssvfifppkpkdvltitltpkvtcvwdiskddpevqfswfvddvevhtaqtqpreeqfnstf rsvselpimhqdwlngkefkcrvnsaalpapiektisktkgrpkapqvytipppkeqmakdkvsltcmitdflpeditv ewqwngqpaenykntqpimdtdgsyfvysklnvqksnweagntftcsvlheglhnhhtekslshspgksggpAL FKSSFPpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfklympkkatelkhlqcleeelkpleevln</td>

<td></td><td></td><td> laqsknfhlrprdlisninvivlelkgsettfmceyadetativeflnrwitfcqsiistltggggsggggsggggsggggsg gggsggggssggpALFKSSFPpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTL AWVRQAPGKcLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLR AEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQM TQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPGKAPKsLIYSASFRYSG VPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGcGTKVEIK**</td>

<td> 297</td><td> ACP468 (WW0632)</td><td> vprdcgckpcictvpevssvfilppkpkdvltitltpkvtcvwdiskddpevqfswfvddvevhtaqtqpreeqfiistf rsvselpimhqdwlngkefkcrvnsaalpapiektisktkgrpkapqvytipppkeqmakdkvsltcmitdflpeditv ewqwngqpaenykntqpimdtdgsyfvysklnvqksnweagntftcsvlheglhnhhtekslshspgksggpAL FKSSFPpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfkiympkkatelkhlqcleeelkpleevln laqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsggggsggggsg gggsggggssggpALFKSSFPpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTL AWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLR AEDTAVYYCARDSNWDALDYWGcGTTVTVSSGGGGSGGGGSGGGGSDIQMT QSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPGKcPKALIYSASFRYSGV PSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIK**</td>

<td> 298</td><td> ACP469 (WW0633)</td><td> vprdcgckpcictvpevssvfilppkpkdvltitltpkvtcvwdiskddpevqfswfvddvevhtaqtqpreeqfiistf rsvselpimhqdwlngkefkcrvnsaalpapiektisktkgrpkapqvytipppkeqmakdkvsltcmitdflpeditv ewqwngqpaenykntqpimdtdgsyfvysklnvqksnweagntftcsvlheglhnhhtekslshspgksggpAL FKSSFPpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfkiympkkatelkhlqcleeelkpleevln laqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsggggsggggsg gggsggggssggpALFKSSFPpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTL AWVRQAPGKcLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLR AEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQM TQSPSSLSASVGDRVTITCKVTEKVWGNVAWYQQKPGKAPISLIYSPSLRKSG VPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGcGTKVEIK**</td>

<td> 299</td><td> ACP470 (WW0634)</td><td> vprdcgckpcictvpevssvfilppkpkdvltitltpkvtcvwdiskddpevqfswfvddvevhtaqtqpreeqfiistf rsvselpimhqdwlngkefkcrvnsaalpapiektisktkgrpkapqvytipppkeqmakdkvsltcmitdflpeditv ewqwngqpaenykntqpimdtdgsyfvysklnvqksnweagntftcsvlheglhnhhtekslshspgksggpAL FKSSFPpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfkiympkkatelkhlqcleeelkpleevln laqsknfhlrprdlisninvivlelkgsettfmceyadetativeflnrwitfcqsiistltggggsggggsggggsggggsg gggsggggssggpALFKSSFPpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTL AWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLR AEDTAVYYCARDSNWDALDYWGcGTTVTVSSGGGGSGGGGSGGGGSDIQMT QSPSSLSASVGDRVTITCKVTEKVWGNVAWYQQKPGKcPISLIYSPSLRKSGVP SRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIK**</td>

<td> 300</td><td> ACP471 (WW0642)</td><td> mdmrvpaqllgllllwlrgarcvprdcgckpcictvpevssvfilppkpkdvltitltpkvtcvwdiskddpevqfswf vddvevhtaqtqpreeqfiistfrsvselpimhqdwlngkefkcrvnsaalpapiektisktkgrpkapqvytipppkeq makdkvsltcmitdflpeditvewqwngqpaenykntqpimdtdgsyfvysklnvqksnweagntftcsvlheglh nhhtekslshspgksggpALFKSSFPpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympk katelkhlqcleeelkpleevlnlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltg gggsggggsggggsggggsggggsggggssggpALFKSSFPpgsEVQLVESGGGLVQPGGSLR LSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRD NAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSastkgpsv iplapsskstsggtaalgclvkdylpepvtvswnsgaltsgvhtlpavlqssglyslssvvtvpssslgtqtyicnvnhkps ntkvdkrvepksc* *</td>

<td> 301</td><td> ACP382 (WW0524)</td><td> DIQMTQSPSSLSASVGDRVTITCKVTEKVWGNVAWYQQKPGKAPISLIYSPSL RKSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYIYPYTFGGGTKVEIKr tvaapsvfilppsdeqlksgtaswcllnniypreakvqwkvdnalqsgnsqesvteqdskdstyslsstltlskadyekh kvyacevthqglsspvtksfiirgec**</td>

<td> 302</td><td> ACP383 (WW0525)</td><td> eskygppcppcpapeflggpsvflfppkpkdtlmisrtpevtcvwdvsqedpevqfnwyvdgvevhnaktkpree qfiistyrwsvltvlhqdwlngkeykckvsnkglpssiektiskakgqprepqvytlppsqeemtknqvsltclvkgfy psdiavewesngqpennykttppvldsdgsfflysrltvdksrwqegnvfscsvmhealhnhytqkslslslgksggp GPAGLYAQpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfkiympkkatelkhlqcleeelkpl eevlnlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsggggsgg ggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFS SYTLAWVRQAPGKcLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQM NSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGS</td>

<td></td><td></td><td> DIQMTQSPSSLSASVGDRVTITCKASQNVGTNVGWYQQKPGKAPKALIYSASF RYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGcGTKVEIK* *</td>

<td> 303</td><td> ACP384 (WW0526)</td><td> eskygppcppcpapeflggpsvflfppkpkdtlmisrtpevtcvwdvsqedpevqfnwyvdgvevhnaktkpree qfiistyrwsvltvlhqdwlngkeykckvsnkglpssiektiskakgqprepqvytlppsqeemtknqvsltclvkgfy psdiavewesngqpennykttppvldsdgsfflysrltvdksrwqegnvfscsvmhealhnhytqkslslslgksggp GPAGLYAQpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpl eevlnlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsggggsgg ggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFS SYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQM NSLRAEDTAVYYCARDSNWDALDYWGcGTTVTVSSGGGGSGGGGSGGGGSD IQMTQSPSSLSASVGDRVTITCKASQNVGTNVGWYQQKPGKcPKALIYSASFR YSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIK**</td>

<td> 304</td><td> ACP385 (WW0527)</td><td> eskygppcppcpapeflggpsvflfppkpkdtlmisrtpevtcvwdvsqedpevqfnwyvdgvevhnaktkpree qfiistyrwsvltvlhqdwlngkeykckvsnkglpssiektiskakgqprepqvytlppsqeemtknqvsltclvkgfy psdiavewesngqpennykttppvldsdgsfflysrltvdksrwqegnvfscsvmhealhnhytqkslslslgksggp GPAGLYAQpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpl eevlnlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsggggsgg ggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFS SYTLAWVRQAPGKcLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQM NSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGS DIQMTQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPGKAPKALIYSASF RYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGcGTKVEIK* *</td>

<td> 305</td><td> ACP386 (WW0528)</td><td> eskygppcppcpapeflggpsvflfppkpkdtlmisrtpevtcvwdvsqedpevqfnwyvdgvevhnaktkpree qfiistyrwsvltvlhqdwlngkeykckvsnkglpssiektiskakgqprepqvytlppsqeemtknqvsltclvkgfy psdiavewesngqpennykttppvldsdgsfflysrltvdksrwqegnvfscsvmhealhnhytqkslslslgksggp GPAGLYAQpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpl eevlnlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsggggsgg ggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFS SYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQM NSLRAEDTAVYYCARDSNWDALDYWGcGTTVTVSSGGGGSGGGGSGGGGSD IQMTQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPGKcPKALIYSASFR YSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIK**</td>

<td> 306</td><td> ACP387 (WW0529)</td><td> eskygppcppcpapeflggpsvflfppkpkdtlmisrtpevtcvwdvsqedpevqfnwyvdgvevhnaktkpree qfiistyrwsvltvlhqdwlngkeykckvsnkglpssiektiskakgqprepqvytlppsqeemtknqvsltclvkgfy psdiavewesngqpennykttppvldsdgsfflysrltvdksrwqegnvfscsvmhealhnhytqkslslslgksggp GPAGLYAQpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpl eevlnlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsggggsgg ggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFS SYTLAWVRQAPGKcLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQM NSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGS DIQMTQSPSSLSASVGDRVTITCKVTEKVWGNVAWYQQKPGKAPISLIYSPSL RKSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGcGTKVEIK* *</td>

<td> 307</td><td> ACP388 (WW0530)</td><td> eskygppcppcpapeflggpsvflfppkpkdtlmisrtpevtcvwdvsqedpevqfnwyvdgvevhnaktkpree qfiistyrwsvltvlhqdwlngkeykckvsnkglpssiektiskakgqprepqvytlppsqeemtknqvsltclvkgfy psdiavewesngqpennykttppvldsdgsfflysrltvdksrwqegnvfscsvmhealhnhytqkslslslgksggp GPAGLYAQpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpl eevlnlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsggggsgg ggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFS SYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQM NSLRAEDTAVYYCARDSNWDALDYWGcGTTVTVSSGGGGSGGGGSGGGGSD IQMTQSPSSLSASVGDRVTITCKVTEKVWGNVAWYQQKPGKcPISLIYSPSLRK SGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIK**</td>

<td> 308</td><td> ACP389 (WW0531)</td><td> eskygppcppcpapeflggpsvflfppkpkdtlmisrtpevtcvwdvsqedpevqfnwyvdgvevhnaktkpree qfiistyrwsvltvlhqdwlngkeykckvsnkglpssiektiskakgqprepqvytlppsqeemtknqvsltclvkgfy psdiavewesngqpennykttppvldsdgsfflysrltvdksrwqegnvfscsvmhealhnhytqkslslslgksggp</td>

<td></td><td></td><td> GPAGLYAQpgsaptssstkktqlqlehllldlqmilngmnyknpkltnnltfldympkkatelkhlqcleeelkpl eevlnlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsggggsgg ggsggggsggggssggpGPAGLYAQpgsevqllesggglvqpggslrlscaasgsifsanamgwyrqapgkqr elvavissggstnyadsvkgrftisrdnskntvylqnmslraedtavyycmysgsyyytpndywgqgtlvtvss**</td>

<td> 309</td><td> ACP390 (WW0532)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsEVQLVESGG GLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGS LRLSCAASGFTFSSYTLAWVRQAPGKcLEWVAAIDSSSYTYSPDTVRGRFTISR DNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGG SGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPG KAPKsLIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPY TFGcGTKVEIK**</td>

<td> 310</td><td> ACP391 (WW0533)</td><td> eskygppcppcpapeflggpsvflfppkpkdtlmisrtpevtcvwdvsqedpevqfnwyvdgvevhnaktkpree qfiistyrwsvltvlhqdwlngkeykckvsnkglpssiektiskakgqprepqvytlppsqeemtknqvsltclvkgfy psdiavewesngqpennykttppvldsdgsfflysrltvdksrwqegnvfscsvmhealhnhytqkslslslgksggp GPAGLYAQpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfldympkkatelkhlqcleeelkpl eevlnlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsggggsgg ggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFS SYTLAWVRQAPGKcLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQM NSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGS DIQMTQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPGKAPKsLIYSASF RYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGcGTKVEIK* *</td>

<td> 311</td><td> ACP392 (WW0534)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsggggsggggsggg gsggggsggggsggggselcdddppeiphatfkamaykegtmlnceckrgfrriksgslymlctgnsshsswdnqc qctssatmttkqvtpqpeeqkerkttemqspmqpvdqaslpghcrepppweneateriyhfwgqmvyyqcvqgy ralhrgpaesvckmthgktrwtqpqlictgemetsqlpgeekpqaspegrpesetsSlvtttdfqiqtemaatmetsiftt eyqsggpGPAGLYAQpgsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWV RQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPED TAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggsggggsggggsggggssggpGPAG LYAQpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKcLE WVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARD SNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGD RVTITCKAREKLWSAVAWYQQKPGKAPKsLIYSASFRYSGVPSRFSGSGSGTD FTLTISSLQPEDFATYYCQQYYTYPYTFGcGTKVEIK**</td>

<td> 312</td><td> ACP393 (WW0535)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsggggsggggsggg gsggggsggggsggggselcdddppeiphatfkamaykegtmlnceckrgfrriksgslymlctgnsshsswdnqc qctssatmttkqvtpqpeeqkerkttemqspmqpvdqaslpghcrepppweneateriyhfwgqmvyyqcvqgy ralhrgpaesvckmthgktrwtqpqlictgemetsqlpgeekpqaspegrpesetsSlvtttdfqiqtemaatmetsiftt eyqsggpGPAGLYAQpgsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWV RQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPED TAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggsggggsggggsggggssggpGPAG LYAQpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLE WVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARD SNWDALDYWGcGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDR VTITCKAREKLWSAVAWYQQKPGKcPKALIYSASFRYSGVPSRFSGSGSGTDF TLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIK**</td>

<td> 313</td><td> ACP394 (WW0536)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsggggsggggsggg gsggggsggggsggggselcdddppeiphatfkamaykegtmlnceckrgfrriksgslymlctgnsshsswdnqc qctssatmttkqvtpqpeeqkerkttemqspmqpvdqaslpghcrepppweneateriyhfwgqmvyyqcvqgy ralhrgpaesvckmthgktrwtqpqlictgemetsqlpgeekpqaspegrpesetsSlvtttdfqiqtemaatmetsiftt eyqsggpGPAGLYAQpgsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWV RQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPED</td>

<td></td><td></td><td> TAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggsggggsggggsggggssggpGPAG LYAQpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKcLE WVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARD SNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGD RVTITCKVTEKVWGNVAWYQQKPGKAPISLIYSPSLRKSGVPSRFSGSGSGTD FTLTISSLQPEDFATYYCQQYYTYPYTFGcGTKVEIK**</td>

<td> 314</td><td> ACP395 (WW0537)</td><td> aptssstkktqlqlehllldlqmilngiimyknpkltrmltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsggggsggggsggg gsggggsggggsggggselcdddppeiphatfkamaykegtmlnceckrgfrriksgslymlctgnsshsswdnqc qctssatmttkqvtpqpeeqkerkttemqspmqpvdqaslpghcrepppweneateriyhfwgqmvyyqcvqgy ralhrgpaesvckmthgktrwtqpqlictgemetsqlpgeekpqaspegrpesetsSlvtttdfqiqtemaatmetsiftt eyqsggpGPAGLYAQpgsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWV RQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPED TAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggsggggsggggsggggssggpGPAG LYAQpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLE WVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARD SNWDALDYWGcGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDR VTITCKVTEKVWGNVAWYQQKPGKcPISLIYSPSLRKSGVPSRFSGSGSGTDFT LTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIK**</td>

<td> 315</td><td> ACP396 (WW0538)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsggggsggggsggg gsggggsggggsggggselcdddppeiphatfkamaykegtmlnceckrgfrriksgslymlctgnsshsswdnqc qctssatmttkqvtpqpeeqkerkttemqspmqpvdqaslpghcrepppweneateriyhfwgqmvyyqcvqgy ralhrgpaesvckmthgktrwtqpqlictgemetsqlpgeekpqaspegrpesetsSlvtttdfqiqtemaatmetsiftt eyqsggpGPAGLYAQpgsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWV RQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPED TAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggsggggsggggsggggssggpGPAG LYAQpgsevqllesggglvqpggslrlscaasgsifsanamgwyrqapgkqrelvavissggstnyadsvkgrftisr dnskntvylqnmslraedtavyycmysgsyyytpndywgqgtlvtvss**</td>

<td> 316</td><td> ACP397 (WW0539)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsggggsggggsggg gsggggsggggsggggselcdddppeiphatfkamaykegtmlnceckrgfrriksgslymlctgnsshsswdnqc qctssatmttkqvtpqpeeqkerkttemqspmqpvdqaslpghcrepppweneateriyhfwgqmvyyqcvqgy ralhrgpaesvckmthgktrwtqpqlictgemetsqlpgeekpqaspegrpesetsSlvtttdfqiqtemaatmetsiftt eyqsggpGPAGLYAQpgsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWV RQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPED TAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggsggggsggggsggggssggpGPAG LYAQpgsevqllesggglvqpggslrlscaasgsifsanamgwyrqapgkglelvavissggstnyadsvkgrftisr dnskntvylqnmslraedtavyycmysgsyyytpndywgqgtlvtvss**</td>

<td> 317</td><td> ACP398 (WW0540)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsggggsggggsggg gsggggsggggsggggselcdddppeiphatfkamaykegtmlnceckrgfrriksgslymlctgnsshsswdnqc qctssatmttkqvtpqpeeqkerkttemqspmqpvdqaslpghcrepppweneateriyhfwgqmvyyqcvqgy ralhrgpaesvckmthgktrwtqpqlictgemetsqlpgeekpqaspegrpesetsSlvtttdfqiqtemaatmetsiftt eyqsggpGPAGLYAQpgsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWV RQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPED TAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggsggggsggggsggggssggpGPAG LYAQpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLE WVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARD SNWDALDYWGQGTTVTVSSastkgpsvlplapsskstsggtaalgclvkdyipepvtvswnsgaltsgv htfpavlq ssglyslssvvtvpssslgtqtyicnvnhkpsntkvdkrvepksc* *</td>

<td> 318</td><td> ACP399</td><td> EVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKcLEWVAAIDS SSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALD YWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKA REKLWSAVAWYQQKPGKAPKsLIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQ PEDFAIYYCQQYYTYPYTFGcGTKVEIKsggpGPAGLYAQpgsggggsggggsggggsg gggsggggsggggsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPG KGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYY</td>

<td></td><td></td><td> CTIGGSLSVSSQGTLVTVSSsggpGPAGLYAQpgstfkfympkkatelkhlqcleeelkpleevlnl aqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltGGssstkktqlqlehllldlqmiln ginnyknpkltrmlsggpGPAGLYAQpgsEVQLVESGGGLVQPGNSLRLSCAASGFTFS KFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQ MNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS**</td>

<td> 319</td><td> ACP400</td><td> EVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAID SSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDAL DYWGcGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKA REKLWSAVAWYQQKPGKcPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQ PEDFAIYYCQQYYTYPYTFGGGTKVEIKsggpGPAGLYAQpgsggggsggggsggggsg gggsggggsggggsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPG KGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYY CTIGGSLSVSSQGTLVTVSSsggpGPAGLYAQpgstfkfympkkatelkhlqcleeelkpleevlnl aqsknfhlrprdlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltGGssstkktqlqlehllldlqmiln ginnyknpkltrmlsggpGPAGLYAQpgsEVQLVESGGGLVQPGNSLRLSCAASGFTFS KFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQ MNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS**</td>

<td> 320</td><td> ACP401</td><td> EVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKcLEWVAAIDS SSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALD YWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKV TEKVWGNVAWYQQKPGKAPISLIYSPSLRKSGVPSRFSGSGSGTDFTLTISSLQ PEDFAIYYCQQYYTYPYTFGcGTKVEIKsggpGPAGLYAQpgsggggsggggsggggsg gggsggggsggggsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPG KGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYY CTIGGSLSVSSQGTLVTVSSsggpGPAGLYAQpgstfkfympkkatelkhlqcleeelkpleevlnl aqsknfhlrprdlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltGGssstkktqlqlehllldlqmiln ginnyknpkltrmlsggpGPAGLYAQpgsEVQLVESGGGLVQPGNSLRLSCAASGFTFS KFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQ MNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS**</td>

<td> 321</td><td> ACP402</td><td> EVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAID SSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDAL DYWGcGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKV TEKVWGNVAWYQQKPGKcPISLIYSPSLRKSGVPSRFSGSGSGTDFTLTISSLQP EDFAIYYCQQYYTYPYTFGGGTKVEIKsggpGPAGLYAQpgsggggsggggsggggsgg ggsggggsggggsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGK GLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYC TIGGSLSVSSQGTLVTVSSsggpGPAGLYAQpgstfkfympkkatelkhlqcleeelkpleevlnla qsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltGGssstkktqlqlehllldlqmiln ginnyknpkltrmlsggpGPAGLYAQpgsEVQLVESGGGLVQPGNSLRLSCAASGFTFS KFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQ MNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS**</td>

<td> 322</td><td> ACP403</td><td> evqllesggglvqpggslrlscaasgsifsanamgwyrqapgkqrelvavissggstnyadsvkgrftisrdnskntvyl qmnslraedtavyycmysgsyyytpndywgqgtlvtvsssggpGPAGLYAQpgsggggsggggsggggsg gggsggggsggggsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPG KGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYY CTIGGSLSVSSQGTLVTVSSsggpGPAGLYAQpgstfkfympkkatelkhlqcleeelkpleevlnl aqsknfhlrprdlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltGGssstkktqlqlehllldlqmiln ginnyknpkltrmlsggpGPAGLYAQpgsEVQLVESGGGLVQPGNSLRLSCAASGFTFS KFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQ MNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS**</td>

<td> 323</td><td> ACP404</td><td> evqllesggglvqpggslrlscaasgsifsanamgwyrqapgkglelvavissggstnyadsvkgrftisrdnskntvyl qmnslraedtavyycmysgsyyytpndywgqgtlvtvsssggpGPAGLYAQpgsggggsggggsggggsg gggsggggsggggsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPG KGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYY CTIGGSLSVSSQGTLVTVSSsggpGPAGLYAQpgstfkfympkkatelkhlqcleeelkpleevlnl aqsknfhlrprdlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltGGssstkktqlqlehllldlqmiln ginnyknpkltrmlsggpGPAGLYAQpgsEVQLVESGGGLVQPGNSLRLSCAASGFTFS</td>

<td></td><td></td><td> KFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQ MNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS**</td>

<td> 324</td><td> ACP405</td><td> EVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAID SSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDAL DYWGQGTTVTVSSastkgpsvfplapsskstsggtaalgclvkdyipepvtvswnsgaltsgvhtipavlqss glyslsswtvpssslgtqtyicnvnhkpsntkvdkrvepkscsggpGPAGLYAQpgsggggsggggsggggs ggggsggggsggggsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAP GKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVY YCTIGGSLSVSSQGTLVTVSSsggpGPAGLYAQpgstfklympkkatelkhlqcleeelkpleevl nlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltGGssstkktqlqlehllldlqmi IngmnyknpkltrmlsggpGPAGLYAQpgsEVQLVESGGGLVQPGNSLRLSCAASGFTF SKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYL QMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS**</td>

<td> 325</td><td> ACP406 (WW0548)</td><td> vprdcgckpcictvpevssvfifppkpkdvltitltpkvtcvwdiskddpevqfswfvddvevhtaqtqpreeqfnstf rsvselpimhqdwlngkefkcrvnsaalpapiektisktkgrpkapqvytipppkeqmakdkvsltcmitdflpeditv ewqwngqpaenykntqpimdtdgsyfvysklnvqksnweagntftcsvlheglhnhhtekslshspgksggpGP AGLYAQpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfldympkkatelkhlqcleeelkpleev Inlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsggggsggggs ggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYT LAWVRQAPGKGLEWVAAIDSSSYIYSPDTVRGRFTISRDNAKNSLYLQMNSL RAEDTAVYYCARDSNWDALDYWGQGTTVTVSSastkgpsvfplapsskstsggtaalgclvk dyfpepvtvswnsgaltsgvhtlpavlqssglyslssvvtvpssslgtqtyicnvnhkpsntkvdkrvepksc**</td>

<td> 326</td><td> ACP407 (WW0549)</td><td> vprdcgckpcictvpevssvfifppkpkdvltitltpkvtcvwdiskddpevqfswfvddvevhtaqtqpreeqfnstf rsvselpimhqdwlngkefkcrvnsaalpapiektisktkgrpkapqvytipppkeqmakdkvsltcmitdflpeditv ewqwngqpaenykntqpimdtdgsyfvysklnvqksnweagntftcsvlheglhnhhtekslshspgksggpGP AGLYAQpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfldympkkatelkhlqcleeelkpleev Inlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsggggsggggs ggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYT LAWVRQAPGKcLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLR AEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQM TQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPGKAPKALIYSASFRYSG VPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGcGTKVEIK**</td>

<td> 327</td><td> ACP408 (WW0550)</td><td> vprdcgckpcictvpevssvfifppkpkdvltitltpkvtcvwdiskddpevqfswfvddvevhtaqtqpreeqfnstf rsvselpimhqdwlngkefkcrvnsaalpapiektisktkgrpkapqvytipppkeqmakdkvsltcmitdflpeditv ewqwngqpaenykntqpimdtdgsyfvysklnvqksnweagntftcsvlheglhnhhtekslshspgksggpGP AGLYAQpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfldympkkatelkhlqcleeelkpleev Inlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsggggsggggs ggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYT LAWVRQAPGKcLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLR AEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQM TQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPGKAPKsLIYSASFRYSG VPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGcGTKVEIK**</td>

<td> 328</td><td> ACP409 (WW0551)</td><td> vprdcgckpcictvpevssvfifppkpkdvltitltpkvtcvwdiskddpevqfswfvddvevhtaqtqpreeqfnstf rsvselpimhqdwlngkefkcrvnsaalpapiektisktkgrpkapqvytipppkeqmakdkvsltcmitdflpeditv ewqwngqpaenykntqpimdtdgsyfvysklnvqksnweagntftcsvlheglhnhhtekslshspgksggpGP AGLYAQpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfldympkkatelkhlqcleeelkpleev Inlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsggggsggggs ggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYT LAWVRQAPGKGLEWVAAIDSSSYIYSPDTVRGRFTISRDNAKNSLYLQMNSL RAEDTAVYYCARDSNWDALDYWGcGTTVTVSSGGGGSGGGGSGGGGSDIQ MTQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPGKcPKALIYSASFRYS GVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIK**</td>

<td> 329</td><td> ACP410 (WW0552)</td><td> vprdcgckpcictvpevssvfifppkpkdvltitltpkvtcvwdiskddpevqfswfvddvevhtaqtqpreeqfnstf rsvselpimhqdwlngkefkcrvnsaalpapiektisktkgrpkapqvytipppkeqmakdkvsltcmitdflpeditv ewqwngqpaenykntqpimdtdgsyfvysklnvqksnweagntftcsvlheglhnhhtekslshspgksggpGP AGLYAQpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfldympkkatelkhlqcleeelkpleev Inlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsggggsggggs ggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYT</td>

<td></td><td></td><td> LAWVRQAPGKcLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLR AEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQM TQSPSSLSASVGDRVTITCKVTEKVWGNVAWYQQKPGKAPISLIYSPSLRKSG VPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGcGTKVEIK**</td>

<td> 330</td><td> ACP411 (WW0553)</td><td> vprdcgckpcictvpevssvfiippkpkdvltitltpkvtcvwdiskddpevqfswfvddvevhtaqtqpreeqfiistf rsvselpimhqdwlngkefkcrvnsaaipapiektisktkgrpkapqvytipppkeqmakdkvsltcmitdfipeditv ewqwngqpaenykntqpimdtdgsyfvysklnvqksnweagntftcsvlheglhnhhtekslshspgksggpGP AGLYAQpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpleev Inlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsggggsggggs ggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYT LAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSL RAEDTAVYYCARDSNWDALDYWGcGTTVTVSSGGGGSGGGGSGGGGSDIQ MTQSPSSLSASVGDRVTITCKVTEKVWGNVAWYQQKPGKcPISLIYSPSLRKS GVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIK**</td>

<td> 331</td><td> ACP412 (WW0554)</td><td> vprdcgckpcictvpevssvfiippkpkdvltitltpkvtcvwdiskddpevqfswfvddvevhtaqtqpreeqfiistf rsvselpimhqdwlngkefkcrvnsaaipapiektisktkgrpkapqvytipppkeqmakdkvsltcmitdfipeditv ewqwngqpaenykntqpimdtdgsyfvysklnvqksnweagntftcsvlheglhnhhtekslshspgksggpGP AGLYAQpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpleev Inlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsggggsggggs ggggsggggssggpGPAGLYAQpgsevqllesggglvqpggslrlscaasgsifsanamgwyrqapgkqrelv avissggstnyadsvkgrftisrdiiskntvylqnmslraedtavyycmysgsyyytpndywgqgtlvtvss**</td>

<td> 332</td><td> ACP413 (WW0555)</td><td> elcdddppeiphatfkamaykegtmlnceckrgfrriksgslymlctgnsshsswdnqcqctssatnittkqvtpqpee qkerkttemqspmqpvdqaslpghcrepppweneateriyhfwgqmvyyqcvqgyralhrgpaesvckmthgk trwtqpqlictgemetsqipgeekpqaspegrpesetsSlvtttdfqiqtemaatmetsiftteyqggggsggggsgggg sggggsggggsggggsDIQMTQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPG KAPKsLIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPY TFGGGTKVEIKrtvaapsvfiippsdeqlksgtaswclliiniypreakvqwkvdnalqsgnsqesvteqdskd styslsstltlskadyekhkvyacevthqglsspvtksfiirgec**</td>

<td> 333</td><td> ACP414 (WW0556)</td><td> elcdddppeiphatfkamaykegtmlnceckrgfrriksgslymlctgnsshsswdnqcqctssatnittkqvtpqpee qkerkttemqspmqpvdqaslpghcrepppweneateriyhfwgqmvyyqcvqgyralhrgpaesvckmthgk trwtqpqlictgemetsqipgeekpqaspegrpesetsSlvtttdfqiqtemaatmetsiftteyqggggsggggsgggg sggggsggggsggggsDIQMTQSPSSLSASVGDRVTITCKVTEKVWGNVAWYQQKP GKAPISLIYSPSLRKSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYP YTFGGGTKVEIKrtvaapsvfiippsdeqlksgtaswcllmiiypreakvqwkvdnalqsgnsqesvteqds kdstyslsstltlskadyekhkvyacevthqglsspvtksfnrgec**</td>

<td> 334</td><td> ACP415 (WW0557)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfkiympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsggggsggggsggg gsggggsggggsggggsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQA PGKcLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVY YCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLS ASVGDRVTITCKAREKLWSAVAWYQQKPGKAPKsLIYSASFRYSGVPSRFSGS GSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGcGTKVEIKggggsggggsggggsgg ggsggggsggggsggggsggggsggggselcdddppeiphatfkamaykegtmlnceckrgfrriksgslymlctg nsshsswdnqcqctssatmttkqvtpqpeeqkerkttemqspmqpvdqaslpghcrepppweneateriyhfwgq mvyyqcvqgyralhrgpaesvckmthgktrwtqpqlictgemetsqipgeekpqaspegrpesetsSlvtttdfqiqte maatmetsiftteyqsggpGPAGLYAQpgsEVQLVESGGGLVQPGNSLRLSCAASGFTFS KFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQ MNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS**</td>

<td> 335</td><td> ACP416 (WW0558)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfkiympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsggggsggggsggg gsggggsggggsggggsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQA PGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVY YCARDSNWDALDYWGcGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSA SVGDRVTITCKAREKLWSAVAWYQQKPGKcPKALIYSASFRYSGVPSRFSGSG SGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIKggggsggggsggggsggg gsggggsggggsggggsggggsggggselcdddppeiphatfkamaykegtmlnceckrgfrriksgslymlctgns shsswdnqcqctssatmttkqvtpqpeeqkerkttemqspmqpvdqaslpghcrepppweneateriyhfvvgqm vyyqcvqgyralhrgpaesvckmthgktrwtqpqlictgemetsqfpgeekpqaspegrpesetsSlvtttdfqiqtem</td>

<td></td><td></td><td> aatmetsiftteyqsggpGPAGLYAQpgsEVQLVESGGGLVQPGNSLRLSCAASGFTFSK FGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQM NSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS**</td>

<td> 336</td><td> ACP417 (WW0559)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsggggsggggsggg gsggggsggggsggggsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQA PGKcLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVY YCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLS ASVGDRVTITCKVTEKVWGNVAWYQQKPGKAPISLIYSPSLRKSGVPSRFSGS GSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGcGTKVEIKggggsggggsggggsgg ggsggggsggggsggggsggggsggggselcdddppeiphatfkamaykegtmlnceckrgfrriksgslymlctg nsshsswdnqcqctssatmttkqvtpqpeeqkerkttemqspmqpvdqaslpghcrepppweneateriyhfwgq mvyyqcvqgyralhrgpaesvckmthgktrwtqpqlictgemetsqlpgeekpqaspegrpesetsSlvtttdfqiqte maatmetsiftteyqsggpGPAGLYAQpgsEVQLVESGGGLVQPGNSLRLSCAASGFTFS KFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQ MNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS**</td>

<td> 337</td><td> ACP418 (WW0560)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsggggsggggsggg gsggggsggggsggggsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQA PGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVY YCARDSNWDALDYWGcGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSA SVGDRVTITCKVIEKVWGNVAWYQQKPGKcPISLIYSPSLRKSGVPSRFSGSGS GTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIKggggsggggsggggsgggg sggggsggggsggggsggggsggggselcdddppeiphatfkamaykegtmlnceckrgfrriksgslymlctgnss hsswdnqcqctssatmttkqvtpqpeeqkerkttemqspmqpvdqaslpghcrepppweneateriyhfwgqmv yyqcvqgyralhrgpaesvckmthgktrwtqpqlictgemetsqlpgeekpqaspegrpesetsSlvtttdfqiqtema atmetsiftteyqsggpGPAGLYAQpgsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKF GMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMN SLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS**</td>

<td> 338</td><td> ACP419 (WW0561)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsggggsggggsggg gsggggsggggsggggsevqllesggglvqpggslriscaasgsifsanamgwyrqapgkqrelvavissggstnyad svkgrftisrdnskntvylqnmslraedtavyycmysgsyyytpndywgqgtlvtvssggggsggggsggggsggg gsggggsggggsggggsggggsggggselcdddppeiphatfkamaykegtmlnceckrgfrriksgslymlctgns shsswdnqcqctssatmttkqvtpqpeeqkerkttemqspmqpvdqaslpghcrepppweneateriyhfvvgqm vyyqcvqgyralhrgpaesvckmthgktrwtqpqlictgemetsqlpgeekpqaspegrpesetsSlvtttdfqiqtem aatmetsiftteyqsggpGPAGLYAQpgsEVQLVESGGGLVQPGNSLRLSCAASGFTFSK FGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQM NSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS**</td>

<td> 339</td><td> ACP420 (WW0562)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsggggsggggsggg gsggggsggggsggggsevqllesggglvqpggslriscaasgsifsanamgwyrqapgkglelvavissggstnyad svkgrftisrdnskntvylqnmslraedtavyycmysgsyyytpndywgqgtlvtvssggggsggggsggggsggg gsggggsggggsggggsggggsggggselcdddppeiphatfkamaykegtmlnceckrgfrriksgslymlctgns shsswdnqcqctssatmttkqvtpqpeeqkerkttemqspmqpvdqaslpghcrepppweneateriyhfvvgqm vyyqcvqgyralhrgpaesvckmthgktrwtqpqlictgemetsqlpgeekpqaspegrpesetsSlvtttdfqiqtem aatmetsiftteyqsggpGPAGLYAQpgsEVQLVESGGGLVQPGNSLRLSCAASGFTFSK FGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQM NSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS**</td>

<td> 340</td><td> ACP421 (WW0563)</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFS SYTLAWVRQAPGKcLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQM NSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGS DIQMTQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPGKAPKsLIYSASF RYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGcGTKVEIKg gggsggggsggggsggggsggggsggggsggggsggggsggggselcdddppeiphatfkamaykegtmlncec krgfmksgslymlctgnsshsswdnqcqctssatmttkqvtpqpeeqkerkttemqspmqpvdqaslpghcrepp</td>

<td></td><td></td><td> pweneateriyhfwgqmvyyqcvqgyralhrgpaesvckmthgktrwtqpqlictgemetsqfpgeekpqaspeg rpesetsSlvtttdfqiqtemaatmetsiftteyqggggsggggsggggsggggsggggsggggssggpGPAGLY AQpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfklympkkatelkhlqcleeelkpleevlnlaqsk nfhlrprdlisninvivlelkgsettfmceyadetativeflnrwitfcq siistlt* *</td>

<td> 341</td><td> ACP422 (WW0564)</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFS SYTLAWVRQAPGKGLEWVAAIDSSSYIYSPDTVRGRFTISRDNAKNSLYLQM NSLRAEDTAVYYCARDSNWDALDYWGcGTTVTVSSGGGGSGGGGSGGGGSD IQMTQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPGKcPKALIYSASFR YSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYIYPYTFGGGTKVEIKgg ggsggggsggggsggggsggggsggggsggggsggggsggggselcdddppeiphatfkamaykegtmlnceck rgfrriksgslymlctgnsshsswdnqcqctssatmttkqvtpqpeeqkerkttemqspmqpvdqaslpghcreppp weneateriyhfwgqmvyyqcvqgyralhrgpaesvckmthgktrwtqpqlictgemetsqfpgeekpqaspegr pesetsSlvtttdfqiqtemaatmetsiftteyqggggsggggsggggsggggsggggsggggssggpGPAGLYA Qpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknf hlrprdlisninvivlelkgsettfmceyadetativeflnrwitfcq siistlt* *</td>

<td> 342</td><td> ACP423 (WW0565)</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFS SYTLAWVRQAPGKcLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQM NSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGS DIQMTQSPSSLSASVGDRVTITCKVTEKVWGNVAWYQQKPGKAPISLIYSPSL RKSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYIYPYTFGcGTKVEIKg gggsggggsggggsggggsggggsggggsggggsggggsggggselcdddppeiphatfkamaykegtmlncec krgfrriksgslymlctgnsshsswdnqcqctssatmttkqvtpqpeeqkerkttemqspmqpvdqaslpghcrepp pweneateriyhfwgqmvyyqcvqgyralhrgpaesvckmthgktrwtqpqlictgemetsqfpgeekpqaspeg rpesetsSlvtttdfqiqtemaatmetsiftteyqggggsggggsggggsggggsggggsggggssggpGPAGLY AQpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfklympkkatelkhlqcleeelkpleevlnlaqsk nfhlrprdlisninvivlelkgsettfmceyadetativeflnrwitfcq siistlt* *</td>

<td> 343</td><td> ACP424 (WW0566)</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFS SYTLAWVRQAPGKGLEWVAAIDSSSYIYSPDTVRGRFTISRDNAKNSLYLQM NSLRAEDTAVYYCARDSNWDALDYWGcGTTVTVSSGGGGSGGGGSGGGGSD IQMTQSPSSLSASVGDRVTITCKVIEKVWGNVAWYQQKPGKcPISLIYSPSLRK SGVPSRFSGSGSGTDFTLTISSLQPEDFAIYYCQQYYTYPYTFGGGTKVEIKggg gsggggsggggsggggsggggsggggsggggsggggsggggselcdddppeiphatfkamaykegtmlnceckr gfrriksgslymlctgnsshsswdnqcqctssatmttkqvtpqpeeqkerkttemqspmqpvdqaslpghcrepppw eneateriyhfwgqmvyyqcvqgyralhrgpaesvckmthgktrwtqpqlictgemetsqfpgeekpqaspegrpe setsSlvtttdfqiqtemaatmetsiftteyqggggsggggsggggsggggsggggsggggssggpGPAGLYAQ pgsaptssstkktqlqlehllldlqmilnginnyknpkltrmltfldympkkatelkhlqcleeelkpleevlnlaqsknfh Irprdlisnmvivlelkgsettfinceyadetativeflnrwitfcq siistlt* *</td>

<td> 344</td><td> ACP425 (WW0567)</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsevqllesggglvqpggslrlscaasgsifsanamgwyrqapgkq relvavissggstnyadsvkgrftisrdnskntvylqnmslraedtavyycmysgsyyytpndywgqgtlvtvssggg gsggggsggggsggggsggggsggggsggggsggggsggggselcdddppeiphatfkamaykegtmlnceckr gfrriksgslymlctgnsshsswdnqcqctssatmttkqvtpqpeeqkerkttemqspmqpvdqaslpghcrepppw eneateriyhfwgqmvyyqcvqgyralhrgpaesvckmthgktrwtqpqlictgemetsqfpgeekpqaspegrpe setsSlvtttdfqiqtemaatmetsiftteyqggggsggggsggggsggggsggggsggggssggpGPAGLYAQ pgsaptssstkktqlqlehllldlqmilnginnyknpkltrmltfldympkkatelkhlqcleeelkpleevlnlaqsknfh Irprdlisnmvivlelkgsettfinceyadetativeflnrwitfcq siistlt* *</td>

<td> 345</td><td> ACP426 (WW0568)</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsevqllesggglvqpggslrlscaasgsifsanamgwyrqapgkg lelvavissggstnyadsvkgrftisrdnskntvylqmnslraedtavyycmysgsyyytpndywgqgtlvtvssgggg sggggsggggsggggsggggsggggsggggsggggsggggselcdddppeiphatfkamaykegtmlnceckrgf</td>

<td></td><td></td><td> rriksgslymlctgnsshsswdnqcqctssatmttkqvtpqpeeqkerkttemqspmqpvdqaslpghcrepppwe neateriyhfvvgqmvyyqcvqgyralhrgpaesvckmthgktrwtqpqlictgemetsqlpgeekpqaspegrpes etsSlvtttdfqiqtemaatmetsiftteyqggggsggggsggggsggggsggggsggggssggpGPAGLYAQp gsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlr prdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistlt**</td>

<td> 346</td><td> ACP427 (WW0569)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsEVQLVESGG GLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGS LRLSCAASGFIFSSYTLAWVRQAPGKcLEWVAAIDSSSYTYSPDTVRGRFTISR DNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGG SGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPG KAPKsLIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFAIYYCQQYYTYPY TFGcGTKVEIKggggsggggsggggsggggsggggsggggsevqllesggglvqpggslrlscaasgsifsana mgwyrqapgkqrelvavissggstnyadsvkgrftisrdnskntvylqmnslraedtavyycmysgsyyytpndyw gqgtlvtvss**</td>

<td> 347</td><td> ACP428 (WW0570)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsEVQLVESGG GLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGS LRLSCAASGFIFSSYTLAWVRQAPGKGLEWVAAIDSSSYIYSPDTVRGRFTISR DNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGcGTTVTVSSGGGG SGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPG KcPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFAIYYCQQYYTYPY TFGGGTKVEIKggggsggggsggggsggggsggggsggggsevqllesggglvqpggslrlscaasgsifsan amgwyrqapgkqrelvavissggstnyadsvkgrftisrdnskntvylqmnslraedtavyycmysgsyyytpndy wgqgtlvtvss**</td>

<td> 348</td><td> ACP429 (WW0571)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsEVQLVESGG GLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGS LRLSCAASGFIFSSYTLAWVRQAPGKcLEWVAAIDSSSYTYSPDTVRGRFTISR DNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGG SGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKVTEKVWGNVAWYQQKP GKAPISLIYSPSLRKSGVPSRFSGSGSGTDFTLTISSLQPEDFAIYYCQQYYTYP YTFGcGTKVEIKggggsggggsggggsggggsggggsggggsevqllesggglvqpggslrlscaasgsifsa namgwyrqapgkqrelvavissggstnyadsvkgrftisrdnskntvylqmnslraedtavyycmysgsyyytpndy wgqgtlvtvss**</td>

<td> 349</td><td> ACP430 (WW0572)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsEVQLVESGG GLVQPGNSLRLSCAASGFIFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGS LRLSCAASGFIFSSYTLAWVRQAPGKGLEWVAAIDSSSYIYSPDTVRGRFTISR DNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGcGTTVTVSSGGGG SGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKVTEKVWGNVAWYQQKP GKcPISLIYSPSLRKSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYIYPY TFGGGTKVEIKggggsggggsggggsggggsggggsggggsevqllesggglvqpggslrlscaasgsifsan amgwyrqapgkqrelvavissggstnyadsvkgrftisrdnskntvylqmnslraedtavyycmysgsyyytpndy wgqgtlvtvss**</td>

<td> 350</td><td> ACP431 (WW0573)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsEVQLVESGG GLVQPGNSLRLSCAASGFIFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGS</td>

<td></td><td></td><td> LRLSCAASGFTFSSYTLAWVRQAPGKcLEWVAAIDSSSYTYSPDTVRGRFTISR DNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGG SGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPG KAPKsLIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPY TFGcGTKVEIKggggsggggsggggsggggsggggsggggsevqllesggglvqpggslrlscaasgsifsana mgwyrqapgkglelvavissggstnyadsvkgrftisrdnskntvylqmnslraedtavyycmysgsyyytpndyw gqgtlvtvss**</td>

<td> 351</td><td> ACP432 (WW0574)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisninvivlelkgsettlmceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsEVQLVESGG GLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTL VTVSS ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGS LRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISR DNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGcGTTVTVSSGGGG SGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPG KcPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPY TFGGGTKVEIKggggsggggsggggsggggsggggsggggsevqllesggglvqpggslrlscaasgsifsan amgwyrqapgkglelvavissggstnyadsvkgrftisrdnskntvylqmnslraedtavyycmysgsyyytpndy wgqgtlvtvss**</td>

<td> 352</td><td> ACP433 (WW0575)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisninvivlelkgsettlmceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsEVQLVESGG GLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTL VTVSS ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGS LRLSCAASGFTFSSYTLAWVRQAPGKcLEWVAAIDSSSYTYSPDTVRGRFTISR DNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGG SGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKVTEKVWGNVAWYQQKP GKAPISLIYSPSLRKSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYP YTFGcGTKVEIKggggsggggsggggsggggsggggsggggsevqllesggglvqpggslrlscaasgsifsa namgwyrqapgkglelvavissggstnyadsvkgrftisrdnskntvylqmnslraedtavyycmysgsyyytpndy wgqgtlvtvss**</td>

<td> 353</td><td> ACP434 (WW0576)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsEVQLVESGG GLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTL VTVSS ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGS LRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISR DNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGcGTTVTVSSGGGG SGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKVTEKVWGNVAWYQQKP GKcPISLIYSPSLRKSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPY TFGGGTKVEIKggggsggggsggggsggggsggggsggggsevqllesggglvqpggslrlscaasgsifsan amgwyrqapgkglelvavissggstnyadsvkgrftisrdnskntvylqmnslraedtavyycmysgsyyytpndy wgqgtlvtvss**</td>

<td> 265</td><td> ACP435 (WW0577)</td><td> DIQMTQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPGKAPKsLIYSASF RYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIKr tvaapsvfitppsdeqlksgtaswcllnniypreakvqwkvdnalqsgnsqesvteqdskdstyslsstltlskadyekh kvyacevthqglsspvtksfiirgecggggsggggsggggsggggsggggsggggsevqllesggglvqpggslrlsca asgsifsanamgwyrqapgkqrelvavissggstnyadsvkgrftisrdnskntvylqnmslraedtavyycmysgsy yytpndywgqgtlvtvss**</td>

<td> 355</td><td> ACP371 (WW0513)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsEVQLVESGG GLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTL VTVSS ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGS LRLSCAASGFTFSSYTLAWVRQAPGKcLEWVAAIDSSSYTYSPDTVRGRFTISR DNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGG SGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKASQNVGTNVGWYQQKPG</td>

<td></td><td></td><td> KAPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYP YTFGcGTKVEIK**</td>

<td> 356</td><td> ACP372 (WW0514)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsEVQLVESGG GLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGS LRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISR DNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGcGTTVTVSSGGGG SGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKASQNVGTNVGWYQQKPG KcPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPY TFGGGTKVEIK**</td>

<td> 357</td><td> ACP373 (WW0515)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfkiympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsEVQLVESGG GLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGS LRLSCAASGFTFSSYTLAWVRQAPGKcLEWVAAIDSSSYTYSPDTVRGRFTISR DNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGG SGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPG KAPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYP YTFGcGTKVEIK**</td>

<td> 358</td><td> ACP374 (WW0516)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsEVQLVESGG GLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGS LRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISR DNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGcGTTVTVSSGGGG SGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPG KcPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPY TFGGGTKVEIK**</td>

<td> 359</td><td> ACP375 (WW0517)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsEVQLVESGG GLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGS LRLSCAASGFTFSSYTLAWVRQAPGKcLEWVAAIDSSSYTYSPDTVRGRFTISR DNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGG SGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKVTEKVWGNVAWYQQKP GKAPISLIYSPSLRKSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYP YTFGcGTKVEIK**</td>

<td> 360</td><td> ACP376 (WW0521)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsEVQLVESGG GLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGS LRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISR DNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGcGTTVTVSSGGGG SGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKVTEKVWGNVAWYQQKP GKcPISLIYSPSLRKSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPY TFGGGTKVEIK**</td>

<td> 361</td><td> ACP377 (WW0519)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsEVQLVESGG GLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsevqllesggglvqpggslrlscaasgsi</td>

<td></td><td></td><td> fsanamgwyrqapgkqrelvavissggstnyadsvkgrftisrdnskntvylqnmslraedtavyycmysgsyyytp ndywgqgtlvtvss**</td>

<td> 362</td><td> ACP378 (WW0520)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsEVQLVESGG GLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGS LRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYIYSPDTVRGRFTISR DNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSastkgps vlplapsskstsggtaalgclvkdyipepvtvswnsgaltsgvhtlpavlqssglyslssvvtvpssslgtqtyicnvnhkp sntkvdkrvepksc**</td>

<td> 363</td><td> ACP379 (WW0521)</td><td> eskygppcppcpapeflggpsvflfppkpkdtlmisrtpevtcvwdvsqedpevqfnwyvdgvevhnaktkpree qfiistyrwsvltvlhqdwlngkeykckvsnkglpssiektiskakgqprepqvytlppsqeemtknqvsltclvkgfy psdiavewesngqpennykttppvldsdgsfflysrltvdksrwqegnvfscsvmhealhnhytqkslslslgksggp GPAGLYAQpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfldympkkatelkhlqcleeelkpl eevlnlaqsknfhlrprdlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltggggsggggsggggsgg ggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFS SYTLAWVRQAPGKGLEWVAAIDSSSYIYSPDTVRGRFTISRDNAKNSLYLQM NSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSastkgpsvfplapsskstsggtaal gclvkdyfpepvtvswnsgaltsgvhtlpavlqssglyslssvvtvpssslgtqtyicnvnhkpsntkvdkrvepksc**</td>

<td> 364</td><td> ACP368 (WW0446)</td><td> EVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAID SSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDAL DYWGQGTTVTVSSsggpGPAGLYAQpgsDIQMTQSPSSLSASVGDRVTITCKVTE KVWGNVAWYQQKPGKAPISLIYSPSLRKSGVPSRFSGSGSGTDFTLTISSLQPE DFATYYCQQYYTYPYTFGGGTKVEIKHHHHHH</td>

<td> 365</td><td> ACP365 (WW0443)</td><td> EVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAID SSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDAL DYWGQGTTVTVSSsggpGPAGLYAQpgsDIQMTQSPSSLSASVGDRVTITCKARE KLWSAVAWYQQKPGKAPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPE DFATYYCQQYYTYPYTFGGGTKVEIKHHHHHH</td>

<td> 366</td><td> ACP366 (WW0444)</td><td> EVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAID SSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDAL DYWGQGTTVTVSSsggpGPAGLYAQpgsDIQMTQSPSSLSASVGDRVTITCKARE KLWSAVAWYQQKPGKAPKsLIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPE DFATYYCQQYYTYPYTFGGGTKVEIKHHHHHH</td>

<td> 367</td><td> ACP284</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPGPAGMKGLPGSrvipvsgparclsqsmllkttddmvktareklkhysctaedi dheditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqi ildkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssaSGGPGPAG MKGLPGSggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGS RSNIGSNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGL QAEDEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGG GVVQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYDGSNKYY ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMV TVSS</td>

<td> 368</td><td> ACP285</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPGPAGMKGLPGSiwelkkdvyweldwypdapgemwltcdtpeedgitwtl dqssevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcw wlttistdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsaSpaaeeslpievmvdavhklkyeny tssffirdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrkna sisvraqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhyscta edidheditrdqtstlktclplelhknesSlatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnh qqiildkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssaSGGPGPA GMKGLPGSggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCS GSRSNIGSNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAIT GLQAEDEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVES</td>

<td></td><td></td><td> GGGWQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYDGSNK YYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGT MVTVSS</td>

<td> 369</td><td> ACP286</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPGPAGMKGLPGSiwelkkdvyweldwypdapgemwltcdtpeedgitwtl dqssevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcw wlttistdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyeny tssffirdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrkna sisvraqdryyssswsewasvpcsggggsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklk hysctaedidheditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqainaal qnhnhqqiildkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtinrvmgylssaSGG PGPAGMKGLPGSggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVT ISCSGSRSNIGSNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSAS LAITGLQAEDEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQ LVESGGGWQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYDG SNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWG QGTMVTVSS</td>

<td> 370</td><td> ACP287</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPGPAGMKGLPGSiwelkkdvyweldwypdapgemwltcdtpeedgitwtl dqssevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcw wlttistdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyeny tssffirdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrkna sisvraqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhyscta edidheditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnh qqiildkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssaSGGPGPA GMKGLPGSggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCS GSRSNIGSNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAIT GLQAEDEADYYCQSYDRYTHPALLFGcGTKVTVLggggsggggsggggsQVQLVES GGGWQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKcLEWVAFIRYDGSNKY YADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTM VTVSS</td>

<td> 371</td><td> ACP288</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPGPAGMKGLPGSiwelkkdvyweldwypdapgemwltcdtpeedgitwtl dqssevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcw wlttistdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyeny tssffirdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrkna sisvraqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhyscta edidheditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnh qqiildkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssaSGGPGPA GMKGLPGSggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCS GSRSNIGSNTVKWYQQLPGTcPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAIT GLQAEDEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVES GGGWQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYDGSNK YYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGcGT MVTVSS</td>

<td> 372</td><td> ACP289 (WW0233)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpgpagmkglpgsevqlvesggglvqpgns Irlscaasgftfskfgmswvrqapgkglewvssisgsgrdtlyaesvkgrftisrdnakttlylqmnslrpedtavyyctig gslsvssqgtlvtvssggggsggggsggggsggggsggggsggggssggpgpagmkglpgsevqlvesggglvqpg gslrlscaasgftfssytlawvrqapgkglewvaaidsssytyspdtvrgrftisrdnaknslylqnmslraedtavyycar dsnwdaldywgqgttvtvssggggsggggsggggsdiqmtqspsslsasvgdrvtitckasqnvgtnvgwyqqkpg kapkaliysasfrysgvpsrfsgsgsgtdftltisslqpedfatyycqqyytypytfgggtkveikhhhhhh</td>

<td> 373</td><td> ACP290 (WW0234)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpgpagmkglpgsevqlvesggglvqpgns Irlscaasgftfskfgmswvrqapgkglewvssisgsgrdtlyaesvkgrftisrdnakttlylqmnslrpedtavyyctig</td>

<td></td><td></td><td> gslsvssqgtlvtvssggggsggggsggggsggggsggggsggggssggpgpagmkglpgQVQLQESGGG LVQTGGSLRLSCTTSGTIFSGYTMGWYRQAPGEQRELVAVISGGGDTNYADS VKGRFTISRDNTKDTMYLQMNSLKPEDTAVYYCYSREVTPPWKLYWGQGTQ VTVSSAAAYPYDVPDYGSHHHHHH</td>

<td> 374</td><td> ACP291 (WW0235)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfkiympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpgpagmkglpgsevqlvesggglvqpgns Irlscaasgftfskfgmswvrqapgkglewvssisgsgrdtlyaesvkgrftisrdnakttlylqmnslrpedtavyyctig gslsvssqgtlvtvssggggsggggsggggsggggsggggsggggssggpgpagmkglpgQVQLQESGGG LVQEGGSLRLSCAASERIFSTDVMGWYRQAAEKQRELVAWSARGTTNYLDA VKGRFTISRDNARNTLTLQMNDLKPEDTASYYCYVRETTSPWRIYWGQGTQV TVSSAAAYPYDVPDYGSHHHHHH</td>

<td> 375</td><td> ACP292 (WW0236)</td><td> aptssstkktqlqlehllldlqmilnginnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpgpagmkglpgsevqlvesggglvqpgns Irlscaasgftfskfgmswvrqapgkglewvssisgsgrdtlyaesvkgrftisrdnakttlylqmnslrpedtavyyctig gslsvssqgtlvtvssggggsggggsggggsggggsggggsggggssggpgpagmkglpgQVQLQESGGG LVQAGGSLRLSCAASGSIFSANAMGWYRQAPGKQRELVAVISSGGSTNYADS VKGRFTISRDNAKNTVYLQMNSLKPEDTAVYYCMYSGSYYYTPNDYWGQGT Q VTVSSAAAYPYDVPDYGSHHHHHH</td>

<td> 376</td><td> ACP296 (WW0250)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfkiympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltSGGPGPAGMKGLPGSEVQLVES GGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTL YAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVT VSSggggsggggsggggsggggsggggsggggsSGGPGPAGMKGLPGSEVQLVESGGGLV QPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRG RFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVS SSGGPGPAGMKGLPGSDIQMTQSPSSLSASVGDRVTITCKASQNVGTNVGWY QQKPGKAPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQ YYTYPYTFGGGTKVEIKHHHHHHEPEA**</td>

<td> 377</td><td> ACP297 (WW0251)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfkiympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltSGGPGPAGMKGLPGSEVQLVES GGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTL YAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVT VSSggggsggggsggggsggggsggggsggggsSGGPGPAGMKGLPGSEVQLVESGGGLV QPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRG RFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVS SGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKASQNVGTNVGWY QQKPGKAPKLLIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQ YYTYPYTFGGGTKVEIKHHHHHHEPEA**</td>

<td> 378</td><td> ACP298 (WW0252)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfkiympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltSGGPGPAGMKGLPGSEVQLVES GGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTL YAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVT VSSggggsggggsggggsggggsggggsggggsSGGPGPAGMKGLPGSEVQLVESGGGLV QPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRG RFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVS SGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKASQNVGTNVGWY QQKPGKAPKGLIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQ YYTYPYTFGGGTKVEIKHHHHHHEPEA**</td>

<td> 379</td><td> ACP299 (WW0253)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfkiympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfSqsiistltSGGPGPAGMKGLPGSEVQLVES GGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTL YAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVT VSSggggsggggsggggsggggsggggsggggsSGGPGPAGMKGLPGSEVQLVESGGGLV QPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRG RFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVS SGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKASQNVGTNVGWY QQKPGKAPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQ YYTYPYTFGGGTKVEIKHHHHHHEPEA**</td>

<td> 380</td><td> ACP300 (WW0255)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltrmltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltSGGPGPAGMKGLPGSdahksevahrf kdlgeenfkalvliafaqylqqcpfedhvklvnevtefaktcvadesaencdkslhtlfgdklctvatlretygemadcca kqepemecflqhkddnpnlprlvrpevdvmctafhdneetflkkylyeiarrhpyfyapellffakrykaafteccqaa dkaacllpkldelrdegkassakqrlkcaslqkfgerafkawavarlsqrlpkaefaevsklvtdltkvhtecchgdlleca ddradlakyicenqdsissklkeccekpllekshciaevendempadlpslaadfveskdvcknyaeakdvflgmfly eyarrhpdyswlllrlaktyettlekccaaadphecyakvfdefkplveepqnlikqncelfeqlgeykfqnallvrytkk vpqvstptlvevsmlgkvgskcckhpeakrmpcaedylswlnqlcvlhektpvsdrvtkccteslvnrrpcfsalevd etyvpkefnaetftfhadictlsekerqikkqtalvelvkhkpkatkeqlkavmddfaafvekcckaddketcfaeegkk IvaasqaalglggggsggggsggggsggggsggggsggggsSGGPGPAGMKGLPGSEVQLVESGG GLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDT VRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTV TVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKASQNVGTNVG WYQQKPGKAPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYC QQYYTYPYTFGGGTKVEIKHHHHHHEPEA* *</td>

<td> 381</td><td> ACP302 (WW0296)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltSGGPGPAGMKGLPGSEAHKSEIA HRYNDLGEQHFKGLVLIAFSQYLQKCSYDEHAKLVQEVTDFAKTCVADESAA NCDKSLHTLFGDKLCAIPNLRENYGELADCCTKQEPERNECFLQHKDDNPSLP PFERPEAEAMCTSFKENPTTFMGHYLHEVARRHPYFYAPELLYYAEQYNEILT QCCAEADKESCLTPKLDGVKEKALVSSVRQRMKCSSMQKFGERAFKAWAVA RLSQTFPNADFAEITKLATDLTKVNKECCHGDLLECADDRAELAKYMCENQA TISSKLQTCCDKPLLKKAHCLSEVEHDTMPADLPAIAADFVEDQEVCKNYAEA KDVFLGTFLYEYSRRHPDYSVSLLLRLAKKYEATLEKCCAEANPPACYGTVL AEFQPLVEEPKNLVKTNCDLYEKLGEYGFQNAILVRYTQKAPQVSTPTLVEAA RNLGRVGTKCCTLPEDQRLPCVEDYLSAILNRVCLLHEKTPVSEHVTKCCSGS LVERRPCFSALTVDETYVPKEFKAETFTFHSDICTLPEKEKQIKKQTALAELVK HKPKATAEQLKTVMDDFAQFLDTCCKAADKDTCFSIEGPNLVTRCKDALAgg ggsggggsggggsggggsggggsggggsSGGPGPAGMKGLPGSEVQLVESGGGLVQPGGS LRLSCAASGFIESSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISR DNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGG SGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKASQNVGTNVGWYQQKPG KAPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYP YTFGGGTKVEIKHHHHHH**</td>

<td> 382</td><td> ACP303</td><td> EAHKSEIAHRYNDLGEQHFKGLVLIAFSQYLQKCSYDEHAKLVQEVTDFAKT CVADESAANCDKSLHTLFGDKLCAIPNLRENYGELADCCTKQEPERNECFLQH KDDNPSLPPFERPEAEAMCTSFKENPTTFMGHYLHEVARRHPYFYAPELLYYA EQYNEILTQCCAEADKESCLTPKLDGVKEKALVSSVRQRMKCSSMQKFGERA FKAWAVARLSQTFPNADFAEITKLATDLTKVNKECCHGDLLECADDRAELAK YMCENQATISSKLQTCCDKPLLKKAHCLSEVEHDTMPADLPAIAADFVEDQE VCKNYAEAKDVFLGTFLYEYSRRHPDYSVSLLLRLAKKYEATLEKCCAEANP PACYGTVLAEFQPLVEEPKNLVKTNCDLYEKLGEYGFQNAILVRYTQKAPQV STPTLVEAARNLGRVGTKCCTLPEDQRLPCVEDYLSAILNRVCLLHEKTPVSE HVTKCCSGSLVERRPCFSALTVDETYVPKEFKAETFTFHSDICTLPEKEKQIKK QTALAELVKHKPKATAEQLKTVMDDFAQFLDTCCKAADKDTCFSIEGPNLVT RCKDALASGGPGPAGMKGLPGStfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrprdlis ninvivlelkgsettfmceyadetativefliirwitfcqsiistltGGssstkktqlqlehllldlqmilnginnyknpkltrm 1SGGPGPAGMKGLPGSEAHKSEIAHRYNDLGEQHFKGLVLIAFSQYLQKCSYD EHAKLVQEVTDFAKTCVADESAANCDKSLHTLFGDKLCAIPNLRENYGELAD CCTKQEPERNECFLQHKDDNPSLPPFERPEAEAMCTSFKENPTTFMGHYLHEV ARRHPYFYAPELLYYAEQYNEILTQCCAEADKESCLTPKLDGVKEKALVSSVR QRMKCSSMQKFGERAFKAWAVARLSQTFPNADFAEITKLATDLTKVNKECC HGDLLECADDRAELAKYMCENQATISSKLQTCCDKPLLKKAHCLSEVEHDTM PADLPAIAADFVEDQEVCKNYAEAKDVFLGTFLYEYSRRHPDYSVSLLLRLAK KYEATLEKCCAEANPPACYGTVLAEFQPLVEEPKNLVKTNCDLYEKLGEYGF QNAILVRYTQKAPQVSIPTLVEAARNLGRVGTKCCTLPEDQRLPCVEDYLSAI LNRVCLLHEKIPVSEHVTKCCSGSLVERRPCFSALTVDETYVPKEFKAETFTFH</td>

<td></td><td></td><td> SDICTLPEKEKQIKKQTALAELVKHKPKATAEQLKTVMDDFAQFLDTCCKAA DKDTCFSTEGPNLVTRCKDALAHHHHHH**</td>

<td> 383</td><td> ACP304 (WW0302)</td><td> aptssstkktqlqlehllldlqmilngiimyknpkltrmltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltSGGPGPAGMKGLPGSEVQLVES GGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTL YAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVT VSSggggsggggsggggsggggsggggsggggsSGGPGPAGMKGLPGSEVQLVESGGGLV QPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRG RFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVS SGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKASQNVGTNVGWY QQKPGKAPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQ YYTYPYTFGGGTKVEIKSGGPGPAGMKGLPGSggggsggggsggggsggggsggggsggg gselcdddppeiphatfkamaykegtmlnceckrgfrriksgslymlctgnsshsswdnqcqctssatnittkqvtpqp eeqkerkttemqspmqpvdqaslpghcrepppweneateriyhfwgqmvyyqcvqgyralhrgpaesvckmth gktrwtqpqlictgemetsqipgeekpqaspegrpesetsclvtttdfqiqtemaatmetsiftteyqHHHHHH**</td>

<td> 384</td><td> ACP305 (WW0303)</td><td> elcdddppeiphatfkamaykegtmlnceckrgfrriksgslymlctgnsshsswdnqcqctssatnittkqvtpqpee qkerkttemqspmqpvdqaslpghcrepppweneateriyhfwgqmvyyqcvqgyralhrgpaesvckmthgk trwtqpqlictgemetsqipgeekpqaspegrpesetsclvtttdfqiqtemaatmetsiftteyqggggsggggsgggg sggggsggggsggggsSGGPGPAGMKGLPGSaptssstkktqlqlehllldlqmilnginnyknpkltrmltf kfympkkatelkhlqcleeelkpleevlnlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfc qsiistltSGGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFG MSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNS LRPEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggsggggsggggsggggsSG GPGPAGMKGLPGSEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQ APGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAV YYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSL SASVGDRVTITCKASQNVGTNVGWYQQKPGKAPKALIYSASFRYSGVPSRFSG SGSGTDFTLTISSLQPEDFATYYCQQYYIYPYTFGGGTKVEIKHHHHHH**</td>

<td> 385</td><td> ACP306 (WW0304)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfkiympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltSGGPGPAGMKGLPGSggggsggggs ggggsggggsggggsggggselcdddppeiphatfkamaykegtmlnceckrgfrriksgslymlctgnsshsswd nqcqctssatmttkqvtpqpeeqkerkttemqspmqpvdqaslpghcrepppweneateriyhfwgqmvyyqcv qgyralhrgpaesvckmthgktrwtqpqlictgemetsqipgeekpqaspegrpesetsclvtttdfqiqtemaatmets iftteyqSGGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFG MSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNS LRPEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggsggggsggggsggggsSG GPGPAGMKGLPGSEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQ APGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAV YYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSL SASVGDRVTITCKASQNVGTNVGWYQQKPGKAPKALIYSASFRYSGVPSRFSG SGSGTDFTLTISSLQPEDFATYYCQQYYIYPYTFGGGTKVEIKHHHHHH**</td>

<td> 386</td><td> ACP307</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPGPAGMKGLPGStfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltGGssstkktqlqlehllldlqmilngmnyknpkl trmlSGGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMS WVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLR PEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggsggggsggggsggggsSGGP GPAGMKGLPGSEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAP GKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVY YCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLS ASVGDRVTITCKASQNVGTNVGWYQQKPGKAPKALIYSASFRYSGVPSRFSGS GSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIKHHHHHH**</td>

<td> 387</td><td> ACP308</td><td> EVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAID SSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDAL DYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCK ASQNVGTNVGWYQQKPGKAPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSL QPEDFATYYCQQYYTYPYTFGGGTKVEIKSGGPGPAGMKGLPGSggggsggggsg</td>

<td></td><td></td><td> gggsggggsggggsggggsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVR QAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDT AVYYCTIGGSLSVSSQGTLVTVSSSGGPGPAGMKGLPGStfkfympkkatelkhlqcleee IkpleevlnlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltGGssstkktqlqle hllldlqmilngmnyknpkltrmlSGGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRLS CAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDN AKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSHHHHHH**</td>

<td> 388</td><td> ACP309 (WW0307)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfkiympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltSGGPGPAGMKGLPGSEVQLVES GGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTL YAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVT VSSggggsggggsggggsggggsggggsggggsSGGPGPAGMKGLPGSEVQLVESGGGLV QPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRG RFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVS SGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKASQNVGTNVGWY QQKPGKAPKSLIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQY YTYPYTFGGGTKVEIKHHHHHH**</td>

<td> 389</td><td> ACP310 (WW0308)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfkiympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltSGGPGPAGMKGLPGSEVQLVES GGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTL YAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVT VSSggggsggggsggggsggggsggggsggggsSGGPGPAGMKGLPGSEVQLVESGGGLV QPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRG RFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVS SGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKASQNVGTNVGWY QQKPGQAPRLLIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQY YTYPYTFGGGTKVEIKHHHHHH**</td>

<td> 390</td><td> ACP311 (WW0316)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfkiympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltSGGPGPAGMKGLPGSeskygppcpp cpapeflggpsvflfppkpkdtlmisrtpevtcvwdvsqedpevqfnwyvdgvevhnaktkpreeqfnstyrwsvl tvlhqdwlngkeykckvsnkglpssiektiskakgqprepqvytlppsqeemtknqvsltclvkglypsdiavewesn gqpennykttppvldsdgsfflysrltvdksrwqegnvfscsvmhealhnhytqkslslslgkggggsggggsggggs ggggsggggsggggsSGGPGPAGMKGLPGSEVQLVESGGGLVQPGGSLRLSCAASG FTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLY LQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGG GGSDIQMTQSPSSLSASVGDRVTITCKASQNVGTNVGWYQQKPGKAPKALIYS ASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKV EIKHHHHHH**</td>

<td> 391</td><td> ACP312 (WW0317)</td><td> eskygppcppcpapeflggpsvflfppkpkdtlmisrtpevtcvwdvsqedpevqfnwyvdgvevhnaktkpree qfiistyrwsvltvlhqdwlngkeykckvsnkglpssiektiskakgqprepqvytlppsqeemtknqvsltclvkgfy psdiavewesngqpennykttppvldsdgsfflysrltvdksrwqegnvfscsvmhealhnhytqkslslslgkSGG PGPAGMKGLPGSaptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeel kpleevlnlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsgggg sggggsggggsggggsSGGPGPAGMKGLPGSEVQLVESGGGLVQPGGSLRLSCAASG FTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLY LQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGG GGSDIQMTQSPSSLSASVGDRVTITCKASQNVGTNVGWYQQKPGKAPKALIYS ASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKV EIKHHHHHH**</td>

<td> 392</td><td> ACP313 (WW0318)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfkiympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisninvivlelkgsettlmceyadetativefliirwitfcqsiistltSGGPGPAGMKGLPGSggggsggggs ggggsggggsggggsggggsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVR QAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTA VYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSS LSASVGDRVTITCKASQNVGTNVGWYQQKPGKAPKALIYSASFRYSGVPSRFS GSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIKSGGPGPAGM KGLPGSeskygppcppcpapeflggpsvflfppkpkdtlmisrtpevtcvwdvsqedpevqfnwyvdgvevh naktkpreeqfhstyrvvsvltvlhqdwlngkeykckvsnkglpssiektiskakgqprepqvytlppsqeemtknqv</td>

<td></td><td></td><td> sltclvkgfypsdiavewesngqpennykttppvldsdgsfflysrltvdksrwqegnvfscsvmhealhnhytqkslsl slgkHHHHHH**</td>

<td> 393</td><td> ACP314 (WW0354)</td><td> vprdcgckpcictvpevssvfilppkpkdvltitltpkvtcvwdiskddpevqfswfvddvevhtaqtqpreeqfiistf rsvselpimhqdwlngkefkcrvnsaalpapiektisktkgrpkapqvytipppkeqmakdkvsltcmitdflpeditv ewqwngqpaenykntqpimdtdgsyfvysklnvqksnweagntftcsvlheglhnhhtekslshspgkSGGPG PAGMKGLPGSaptssstkktqlqlehllldlqmilnginnyknpkltrmltfklympkkatelkhlqcleeelkple evlnlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsggggsgg ggsggggsggggsSGGPGPAGMKGLPGSEVQLVESGGGLVQPGGSLRLSCAASGFT FSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQ MNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGG SDIQMTQSPSSLSASVGDRVTITCKASQNVGTNVGWYQQKPGKAPKALIYSAS FRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEI KHHHHHH**</td>

<td> 394</td><td> ACP336 (WW0414)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsEVQLVESGG GLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGS LRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISR DNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSsggpG PAGLYAQpgsDIQMTQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPGKA PKsLIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTF GGGTKVEIK**</td>

<td> 395</td><td> ACP337 (WW0415)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsEVQLVESGG GLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGS LRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYIYSPDTVRGRFTISR DNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGG SGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPG KAPKsLIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFAIYYCQQYYTYPY TFGGGTKVEIK**</td>

<td> 396</td><td> ACP338 (WW0416)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsEVQLVESGG GLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGS LRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYIYSPDTVRGRFTISR DNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSsggpG PAGLYAQpgsDIQMTQSPSSLSASVGDRVTITCKVTEKVWGNVAWYQQKPGK APISLIYSPSLRKSGVPSRFSGSGSGTDFTLTISSLQPEDFAIYYCQQYYTYPYTF GGGTKVEIK**</td>

<td> 397</td><td> ACP339 (WW0417)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltnnltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsEVQLVESGG GLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGS LRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISR DNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGG SGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKVTEKVWGNVAWYQQKP</td>

<td></td><td></td><td> GKAPISLIYSPSLRKSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYP YTFGGGTKVEIK**</td>

<td> 398</td><td> ACP340 (WW0418)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsEVQLVESGG GLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsevqllesggglvqpggslrlscaasgsi fsanamgwyrqapgkglelvavissggstnyadsvkgrftisrdnskntvylqnmslraedtavyycmysgsyyytp ndywgqgtlvtvss**</td>

<td> 399</td><td> ACP341 (WW0419)</td><td> aptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrpr dlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltsggpGPAGLYAQpgsEVQLVESGG GLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsevqllesggglvqpggslrlscaaseri fstdvmgwyrqapgkqrelvawsargttnyldavkgrftisrdnskntlylqnmslraedtavyycyvrettspwriy wgqgtlvtvss**</td>

<td> 400</td><td> ACP342 (WW0420)</td><td> elcdddppeiphatfkamaykegtmlnceckrgfrriksgslymlctgnsshsswdnqcqctssatnittkqvtpqpee qkerkttemqspmqpvdqaslpghcrepppweneateriyhfwgqmvyyqcvqgyralhrgpaesvckmthgk trwtqpqlictgemetsqipgeekpqaspegrpesetsSlvtttdfqiqtemaatmetsiftteyqggggsggggsgggg sggggsggggsggggssggpGPAGLYAQpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfy mpkkatelkhlqcleeelkpleevlnlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsii stltsggpGPAGLYAQpgsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWV RQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPED TAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggsggggsggggsggggssggpGPAG LYAQpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLE WVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARD SNWDALDYWGQGTTVTVSSsggpGPAGLYAQpgsDIQMTQSPSSLSASVGDRVT ITCKAREKLWSAVAWYQQKPGKAPKsLIYSASFRYSGVPSRFSGSGSGTDFTLT ISSLQPEDFATYYCQQYYTYP YTFGGGTKVEIK**</td>

<td> 401</td><td> ACP343 (WW0421)</td><td> elcdddppeiphatfkamaykegtmlnceckrgfrriksgslymlctgnsshsswdnqcqctssatnittkqvtpqpee qkerkttemqspmqpvdqaslpghcrepppweneateriyhfwgqmvyyqcvqgyralhrgpaesvckmthgk trwtqpqlictgemetsqipgeekpqaspegrpesetsSlvtttdfqiqtemaatmetsiftteyqggggsggggsgggg sggggsggggsggggssggpGPAGLYAQpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfy mpkkatelkhlqcleeelkpleevlnlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsii stltsggpGPAGLYAQpgsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWV RQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPED TAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggsggggsggggsggggssggpGPAG LYAQpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLE WVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARD SNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGD RVTITCKAREKLWSAVAWYQQKPGKAPKsLIYSASFRYSGVPSRFSGSGSGTD FTLTISSLQPEDFATYYCQQYYTYP YTFGGGTKVEIK**</td>

<td> 402</td><td> ACP344 (WW0422)</td><td> elcdddppeiphatfkamaykegtmlnceckrgfrriksgslymlctgnsshsswdnqcqctssatnittkqvtpqpee qkerkttemqspmqpvdqaslpghcrepppweneateriyhfwgqmvyyqcvqgyralhrgpaesvckmthgk trwtqpqlictgemetsqipgeekpqaspegrpesetsSlvtttdfqiqtemaatmetsiftteyqggggsggggsgggg sggggsggggsggggssggpGPAGLYAQpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfkfy mpkkatelkhlqcleeelkpleevlnlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsii stltsggpGPAGLYAQpgsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWV RQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPED TAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggsggggsggggsggggssggpGPAG LYAQpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLE WVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARD SNWDALDYWGQGTTVTVSSsggpGPAGLYAQpgsDIQMTQSPSSLSASVGDRVT ITCKVTEKVWGNVAWYQQKPGKAPISLIYSPSLRKSGVPSRFSGSGSGTDFTLT ISSLQPEDFATYYCQQYYTYP YTFGGGTKVEIK**</td>

<td> 403</td><td> ACP345 (WW0423)</td><td> elcdddppeiphatfkamaykegtmlnceckrgfrriksgslymlctgnsshsswdnqcqctssatnittkqvtpqpee qkerkttemqspmqpvdqaslpghcrepppweneateriyhfwgqmvyyqcvqgyralhrgpaesvckmthgk trwtqpqlictgemetsqfpgeekpqaspegrpesetsSlvtttdfqiqtemaatmetsiftteyqggggsggggsgggg</td>

<td></td><td></td><td> sggggsggggsggggssggpGPAGLYAQpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfldy mpkkatelkhlqcleeelkpleevlnlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsii stltsggpGPAGLYAQpgsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWV RQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPED TAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggsggggsggggsggggssggpGPAG LYAQpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLE WVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARD SNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGD RVTITCKVTEKVWGNVAWYQQKPGKAPISLIYSPSLRKSGVPSRFSGSGSGTD FTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIK**</td>

<td> 404</td><td> ACP346 (WW0424)</td><td> elcdddppeiphatfkamaykegtmlnceckrgfrriksgslymlctgnsshsswdnqcqctssatnittkqvtpqpee qkerkttemqspmqpvdqaslpghcrepppweneateriyhfwgqmvyyqcvqgyralhrgpaesvckmthgk trwtqpqlictgemetsqlpgeekpqaspegrpesetsSlvtttdfqiqtemaatmetsiftteyqggggsggggsgggg sggggsggggsggggssggpGPAGLYAQpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfldy mpkkatelkhlqcleeelkpleevlnlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsii stltsggpGPAGLYAQpgsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWV RQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPED TAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggsggggsggggsggggssggpGPAG LYAQpgsevqllesggglvqpggslrlscaasgsifsanamgwyrqapgkglelvavissggstnyadsvkgrftisr dnskntvylqnmslraedtavyycmysgsyyytpndywgqgtlvtvss**</td>

<td> 405</td><td> ACP347 (WW0425)</td><td> elcdddppeiphatfkamaykegtmlnceckrgfrriksgslymlctgnsshsswdnqcqctssatnittkqvtpqpee qkerkttemqspmqpvdqaslpghcrepppweneateriyhfwgqmvyyqcvqgyralhrgpaesvckmthgk trwtqpqlictgemetsqlpgeekpqaspegrpesetsSlvtttdfqiqtemaatmetsiftteyqggggsggggsgggg sggggsggggsggggssggpGPAGLYAQpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfldy mpkkatelkhlqcleeelkpleevlnlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsii stltsggpGPAGLYAQpgsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWV RQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPED TAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsggggsggggsggggsggggssggpGPAG LYAQpgsevqllesggglvqpggslrlscaaserifstdvmgwyrqapgkqrelvawsargttnyldavkgrftisrd nskntlylqnmslraedtavyycyvrettspwriywgqgtlvtvss**</td>

<td> 406</td><td> ACP348 (WW0426)</td><td> eskygppcppcpapeflggpsvflfppkpkdtlmisrtpevtcvwdvsqedpevqfnwyvdgvevhnaktkpree qfiistyrwsvltvlhqdwlngkeykckvsnkglpssiektiskakgqprepqvytlppsqeemtknqvsltclvkgfy psdiavewesngqpennykttppvldsdgsfflysrltvdksrwqegnvfscsvmhealhnhytqkslslslgksggp GPAGLYAQpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfldympkkatelkhlqcleeelkpl eevlnlaqsknfhlrprdlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltggggsggggsggggsgg ggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFS SYTLAWVRQAPGKGLEWVAAIDSSSYIYSPDTVRGRFTISRDNAKNSLYLQM NSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSsggpGPAGLYAQpgsDIQ MTQSPSSLSASVGDRVTITCKAREKLWSAVAWYQQKPGKAPKsLIYSASFRYS GVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIK**</td>

<td> 407</td><td> ACP349 (WW0427)</td><td> eskygppcppcpapeflggpsvflfppkpkdtlmisrtpevtcvwdvsqedpevqfnwyvdgvevhnaktkpree qfiistyrwsvltvlhqdwlngkeykckvsnkglpssiektiskakgqprepqvytlppsqeemtknqvsltclvkgfy psdiavewesngqpennykttppvldsdgsfflysrltvdksrwqegnvfscsvmhealhnhytqkslslslgksggp GPAGLYAQpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfldympkkatelkhlqcleeelkpl eevlnlaqsknfhlrprdlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltggggsggggsggggsgg ggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFS SYTLAWVRQAPGKGLEWVAAIDSSSYIYSPDTVRGRFTISRDNAKNSLYLQM NSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGS DIQMTQSPSSLS ASVGDRVTITCKAREKLWSAVAWYQQKPGKAPKsLIYSASF RYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIK **</td>

<td> 408</td><td> ACP350 (WW0428)</td><td> eskygppcppcpapeflggpsvflfppkpkdtlmisrtpevtcvwdvsqedpevqfnwyvdgvevhnaktkpree qfiistyrwsvltvlhqdwlngkeykckvsnkglpssiektiskakgqprepqvytlppsqeemtknqvsltclvkgfy psdiavewesngqpennykttppvldsdgsfflysrltvdksrwqegnvfscsvmhealhnhytqkslslslgksggp GPAGLYAQpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfldympkkatelkhlqcleeelkpl eevlnlaqsknfhlrprdlisnmvivlelkgsettfmceyadetativeflnrwitfcqsiistltggggsggggsggggsgg ggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFS SYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQM</td>

<td></td><td></td><td> NSLRAEDTAVYYCARDSbTWDALDYWGQGTTVTVSSsggpGPAGLYAQpgsDIQ MTQSPSSLSASVGDRVTITCKVTEKVWGNVAWYQQKPGKAPISLIYSPSLRKS GVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIK**</td>

<td> 409</td><td> ACP351 (WW0429)</td><td> eskygppcppcpapeflggpsvflfppkpkdtlmisrtpevtcvwdvsqedpevqfnwyvdgvevhnaktkpree qfiistyrwsvltvlhqdwlngkeykckvsnkglpssiektiskakgqprepqvytlppsqeemtknqvsltclvkgfy psdiavewesngqpennykttppvldsdgsfflysrltvdksrwqegnvfscsvmhealhnhytqkslslslgksggp GPAGLYAQpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfkiympkkatelkhlqcleeelkpl eevlnlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsggggsgg ggsggggsggggssggpGPAGLYAQpgsEVQLVESGGGLVQPGGSLRLSCAASGFTFS SYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQM NSLRAEDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGS DIQMTQSPSSLSASVGDRVTITCKVTEKVWGNVAWYQQKPGKAPISLIYSPSL RKSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYIYPYTFGGGTKVEIK **</td>

<td> 410</td><td> ACP352 (WW0430)</td><td> eskygppcppcpapeflggpsvflfppkpkdtlmisrtpevtcvwdvsqedpevqfnwyvdgvevhnaktkpree qfiistyrwsvltvlhqdwlngkeykckvsnkglpssiektiskakgqprepqvytlppsqeemtknqvsltclvkgfy psdiavewesngqpennykttppvldsdgsfflysrltvdksrwqegnvfscsvmhealhnhytqkslslslgksggp GPAGLYAQpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfkiympkkatelkhlqcleeelkpl eevlnlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsggggsgg ggsggggsggggssggpGPAGLYAQpgsevqllesggglvqpggslrlscaasgsifsanamgwyrqapgkgl elvavissggstnyadsvkgrftisrdnskntvylqnmslraedtavyycmysgsyyytpndywgqgtlvtvss**</td>

<td> 411</td><td> ACP353 (WW0431)</td><td> eskygppcppcpapeflggpsvflfppkpkdtlmisrtpevtcvwdvsqedpevqfnwyvdgvevhnaktkpree qfiistyrwsvltvlhqdwlngkeykckvsnkglpssiektiskakgqprepqvytlppsqeemtknqvsltclvkgfy psdiavewesngqpennykttppvldsdgsfflysrltvdksrwqegnvfscsvmhealhnhytqkslslslgksggp GPAGLYAQpgsaptssstkktqlqlehllldlqmilngmnyknpkltrmltfkiympkkatelkhlqcleeelkpl eevlnlaqsknfhlrprdlisnmvivlelkgsettfinceyadetativeflnrwitfcqsiistltggggsggggsggggsgg ggsggggsggggssggpGPAGLYAQpgsevqllesggglvqpggslrlscaaserifstdvmgwyrqapgkqr elvawsargttnyldavkgrftisrdnskntlylqnmslraedtavyycyvrettspwriywgqgtlvtvss**</td>

<td> 412</td><td> ACP354 (WW0432)</td><td> eskygppcppcpapeflggpsvflfppkpkdtlmisrtpevtcvwdvsqedpevqfnwyvdgvevhnaktkpree qfiistyrwsvltvlhqdwlngkeykckvsnkglpssiektiskakgqprepqvytlppsqeemtknqvsltclvkgfy psdiavewesngqpennykttppvldsdgsfflysrltvdksrwqegnvfscsvmhealhnhytqkslslslgksggp GPAGLYAQpgselcdddppeiphatfkamaykegtmlnceckrgfrriksgslymlctgnsshsswdnqcqcts satmttkqvtpqpeeqkerkttemqspmqpvdqaslpghcrepppweneateriyhfwgqmvyyqcvqgyralh rgpaesvckmthgktrwtqpqlictgemetsqlpgeekpqaspegrpesetsSlvtttdfqiqtemaatmetsiftteyq ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsaptssstkktqlqlehllldlqmilngin nyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrprdlismnvivlelkgsettfinceyadet ativeflnrwitfcqsiistltggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEVQLV ESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTY SPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQ GTTVTVSSsggpGPAGLYAQpgsDIQMTQSPSSLSASVGDRVTITCKAREKLWSA VAWYQQKPGKAPKsLIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATY YCQQYYTYPYTFGGGTKVEIK**</td>

<td> 413</td><td> ACP355 (WW0433)</td><td> eskygppcppcpapeflggpsvflfppkpkdtlmisrtpevtcvwdvsqedpevqfnwyvdgvevhnaktkpree qfiistyrwsvltvlhqdwlngkeykckvsnkglpssiektiskakgqprepqvytlppsqeemtknqvsltclvkgfy psdiavewesngqpennykttppvldsdgsfflysrltvdksrwqegnvfscsvmhealhnhytqkslslslgksggp GPAGLYAQpgselcdddppeiphatfkamaykegtmlnceckrgfrriksgslymlctgnsshsswdnqcqcts satmttkqvtpqpeeqkerkttemqspmqpvdqaslpghcrepppweneateriyhfwgqmvyyqcvqgyralh rgpaesvckmthgktrwtqpqlictgemetsqlpgeekpqaspegrpesetsSlvtttdfqiqtemaatmetsiftteyq ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsaptssstkktqlqlehllldlqmilngin nyknpkltrmltfkfympkkatelkhlqcleeelkpleevlnlaqsknfhlrprdlismnvivlelkgsettfinceyadet ativeflnrwitfcqsiistltggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEVQLV ESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTY SPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQ GTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKAREKLW SAVAWYQQKPGKAPKsLIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFAT YYCQQYYTYPYTFGGGTKVEIK**</td>

<td> 414</td><td> ACP356</td><td> eskygppcppcpapeflggpsvflfppkpkdtlmisrtpevtcvwdvsqedpevqfnwyvdgvevhnaktkpree qfiistyrwsvltvlhqdwlngkeykckvsnkglpssiektiskakgqprepqvytlppsqeemtknqvsltclvkgfy</td>

<td></td><td> (WW0434)</td><td> psdiavewesngqpennykttppvldsdgsfflysrltvdksrwqegnvfscsvmhealhnhytqkslslslgksggp GPAGLYAQpgselcdddppeiphatfkamaykegtmlnceckrgfrriksgslymlctgnsshsswdnqcqcts satmttkqvtpqpeeqkerkttemqspmqpvdqaslpghcrepppweneateriyhfwgqmvyyqcvqgyralh rgpaesvckmthgktrwtqpqlictgemetsqlpgeekpqaspegrpesetsSlvtttdfqiqtemaatmetsiftteyq ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsaptssstkktqlqlehllldlqmilngin nyknpkltrmltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrprdlismnvivlelkgsettlmceyadet ativeflnrwitfcqsiistltggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEVQLV ESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTY SPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQ GTTVTVSSsggpGPAGLYAQpgsDIQMTQSPSSLSASVGDRVTITCKVTEKVWGN VAWYQQKPGKAPISLIYSPSLRKSGVPSRFSGSGSGTDFTLTISSLQPEDFATYY CQQYYTYPYTFGGGTKVEIK**</td>

<td> 415</td><td> ACP357 (WW0435)</td><td> eskygppcppcpapeflggpsvflfppkpkdtlmisrtpevtcvwdvsqedpevqfnwyvdgvevhnaktkpree qfiistyrwsvltvlhqdwlngkeykckvsnkglpssiektiskakgqprepqvytlppsqeemtknqvsltclvkgfy psdiavewesngqpennykttppvldsdgsfflysrltvdksrwqegnvfscsvmhealhnhytqkslslslgksggp GPAGLYAQpgselcdddppeiphatfkamaykegtmlnceckrgfrriksgslymlctgnsshsswdnqcqcts satmttkqvtpqpeeqkerkttemqspmqpvdqaslpghcrepppweneateriyhfwgqmvyyqcvqgyralh rgpaesvckmthgktrwtqpqlictgemetsqlpgeekpqaspegrpesetsSlvtttdfqiqtemaatmetsiftteyq ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsaptssstkktqlqlehllldlqmilngin nyknpkltrmltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrprdlismnvivlelkgsettlmceyadet ativeflnrwitfcqsiistltggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsEVQLV ESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTY SPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQ GTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKVTEKV WGNVAWYQQKPGKAPISLIYSPSLRKSGVPSRFSGSGSGTDFTLTISSLQPEDF ATYYCQQYYTYPYTFGGGTKVEIK**</td>

<td> 416</td><td> ACP358 (WW0436)</td><td> eskygppcppcpapeflggpsvflfppkpkdtlmisrtpevtcvwdvsqedpevqfnwyvdgvevhnaktkpree qfiistyrwsvltvlhqdwlngkeykckvsnkglpssiektiskakgqprepqvytlppsqeemtknqvsltclvkgfy psdiavewesngqpennykttppvldsdgsfflysrltvdksrwqegnvfscsvmhealhnhytqkslslslgksggp GPAGLYAQpgselcdddppeiphatfkamaykegtmlnceckrgfrriksgslymlctgnsshsswdnqcqcts satmttkqvtpqpeeqkerkttemqspmqpvdqaslpghcrepppweneateriyhfwgqmvyyqcvqgyralh rgpaesvckmthgktrwtqpqlictgemetsqlpgeekpqaspegrpesetsSlvtttdfqiqtemaatmetsiftteyq ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsaptssstkktqlqlehllldlqmilngin nyknpkltrmltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrprdlismnvivlelkgsettlmceyadet ativeflnrwitfcqsiistltggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsevqllesg gglvqpggslrlscaasgsifsanamgwyrqapgkglelvavissggstnyadsvkgrftisrdnskntvylqmnslrae dtavyycmysgsyyytpndywgqgtlvtvss**</td>

<td> 417</td><td> ACP359 (WW0437)</td><td> eskygppcppcpapeflggpsvflfppkpkdtlmisrtpevtcvwdvsqedpevqfnwyvdgvevhnaktkpree qfiistyrwsvltvlhqdwlngkeykckvsnkglpssiektiskakgqprepqvytlppsqeemtknqvsltclvkgfy psdiavewesngqpennykttppvldsdgsfflysrltvdksrwqegnvfscsvmhealhnhytqkslslslgksggp GPAGLYAQpgselcdddppeiphatfkamaykegtmlnceckrgfrriksgslymlctgnsshsswdnqcqcts satmttkqvtpqpeeqkerkttemqspmqpvdqaslpghcrepppweneateriyhfwgqmvyyqcvqgyralh rgpaesvckmthgktrwtqpqlictgemetsqlpgeekpqaspegrpesetsSlvtttdfqiqtemaatmetsiftteyq ggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsaptssstkktqlqlehllldlqmilngin nyknpkltrmltfldympkkatelkhlqcleeelkpleevlnlaqsknfhlrprdlismnvivlelkgsettlmceyadet ativeflnrwitfcqsiistltggggsggggsggggsggggsggggsggggssggpGPAGLYAQpgsevqllesg gglvqpggslrlscaaserifstdvmgwyrqapgkqrelvawsargttnyldavkgrftisrdnskntlylqnmslraed tavyycyvrettspwriywgqgtlvtvss**</td>

<td> 418</td><td> ACP360 (WW0438)</td><td> EVQLVESGGGLVQPGGSLRLSCAASGFIFSSYTLAWVRQAPGKGLEWVAAID SSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDAL DYWGQGTTVTVSSggggsggggsggggsDIQMTQSPSSLSASVGDRVTITCKASQNV GTNVGWYQQKPGKAPKsLIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDF ATYYCQQYYTYPYTFGGGTKVEIKHHHHHH**</td>

<td> 419</td><td> ACP361 (WW0439)</td><td> EVQLVESGGGLVQPGGSLRLSCAASGFIFSSYTLAWVRQAPGKGLEWVAAID SSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDAL DYWGQGTTVTVSSsggpGPAGLYAQpgsDIQMTQSPSSLSASVGDRVTITCKASQ NVGTNVGWYQQKPGKAPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPE DF ATYYCQQYYTYPYTFGGGTKVEIKHHHHHH**</td>

<td> 420</td><td> ACP362 (WW0440)</td><td> EVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAID SSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDAL DYWGQGTTVTVSSsggpGPAGLYAQpgsDIQMTQSPSSLSASVGDRVTITCKASQ NVGTNVGWYQQKPGKAPKsLIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPE DFATYYCQQYYTYPYTFGGGTKVEIKHHHHHH**</td>

<td> 421</td><td> ACP200</td><td> Iveepknlvktncdlyeklgeygfqnailvrytqkapqvstptlveaamlgrvgtkcctlpedqrlpcvedylsailnrvcl Ihektpvsehvtkccsgslverrpcfsaltvdetyvpkefkaetftfhsdictlpekekqikkqtalaelvkhkpkataeqlk tvmddfaqfldtcckaadkdtcfstegpnlvtrckdalaSGGPGPAGMKGLPGScdlpqthnlmkraltllvq mrrlsplscikdrkdfgipqekvdaqqikkaqaipviseltqqilmftskdssaawnttlldsfcndihqqindiqgclmq qvgvqelpltqedallavrkyfhritvylrekkhspcawevvraevwralsssanvlgrlreekSGGPGPAGMK GLPGSlveepknlvktncdlyeklgeygfqnailvrytqkapqvstptlveaamlgrvgtkcctlpedqrlpcvedyl sailnrvcllhektpvsehvtkccsgslverrpcfsaltvdetyvpkefkaetftfhsdictlpekekqikkqtalaelvkhkp kataeq IktvmddfaqfldtcckaadkdtcfstegpnlvtrckdalaHHHHHH**</td>

<td> 422</td><td> ACP201</td><td> eahkseiahryndlgeqhfkglvliafsqylqkcsydehaklvqevtdfaktcvadesaancdkslhtlfgdklcaipnlr enygeladcctkqepemecflqhkddnpslppferpeaeamctsfkenpttimghyllievarrhpyiyapellyyaeq yneiltqccaeadkescltpkldgvkekalvssvrqGGGGSGGGGSGGSlveepknlvktncdlyeklgeygf qnailvrytqkapqvstptlveaamlgrvgtkcctlpedqrlpcvedylsailnrvcllhektpvsehvtkccsgslverrp cfsaltvdetyvpkefkaetftfhsdictlpekekqikkqtalaelvkhkpkataeqlktvmddfaqfldtcckaadkdtcf stegpnlvtrckdalaSGGPGPAGMKGLPGScdlpqthnlmkraltllvqnm-lsplsclkdrkdfglpqekv daqqikkaqaipvlseltqqilmftskdssaawnttlldsfcndlhqqlndlqgclmqqvgvqelpltqedallavrkyfh ritvylrekkhspcawewraevwralsssanvlgrlreekSGGPGPAGMKGLPGSeahkseiahryndlge qhfkglvliafsqylqkcsydehaklvqevtdfaktcvadesaancdkslhtlfgdklcaipnlrenygeladcctkqepe mecflqhkddnpslppferpeaeamctsfkenpttfinghylhevarrhpyfyapellyyaeqyneiltqccaeadkes cltpkldgvkekalvssvrqGGGGSGGGGSGGSlveepknlvktncdlyeklgeygfqnailvrytqkapqvs tptlveaamlgrvgtkcctlpedqrlpcvedylsailnrvcllhektpvsehvtkccsgslverrpcfsaltvdetyvpkefk aetftfhsdictlpekekqikkqtalaelvkhkpkataeqlktvmddfaqfldtcckaadkdtcfstegpnlvtrckdalaFT HHHHH**</td>

<td> 423</td><td> ACP202</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSggggsgggSGGPGPAGMKGLPGSggggsgggscdlpqthnlmkraltllvqmrrls plscikdrkdfgipqekvdaqqikkaqaipviseltqqilmftskdssaawnttlldsfcndihqqindiqgclmqqvgv qelpltqedallavrkyfhritvylrekkhspcawevvraevwralsssanvlgrlreekggggsgggSGGPGPAG MKGLPGSggggsgggsEVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVR QAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDT AVYYCTIGGSLSVSSQGTLVTVSSHHHHHH**</td>

<td> 424</td><td> ACP203</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgscdlpqthnlrnkraltllvqmrrlsplsclkdrkdfglpqekvdaq qikkaqaipvlseltqqilmftskdssaawnttlldsfcndlhqqlndlqgclmqqvgvqelpltqedallavrkyfhritv ylrekkhspcawewraevwralsssanvlgrlreeksggpGPAGLYAQpgsEVQLVESGGGLVQP GNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKG RFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS**</td>

<td> 425</td><td> ACP204</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgscdlpqthnlrnkraltllvqmrrlsplsclkdrkdfglpqekvdaqqi kkaqaipvlseltqqilmftskdssaawnttlldsfcndlhqqlndlqgclmqqvgvqelpltqedallavrkyfhritvyl rekkhspcawewraevwralsssanvlgrlreeksggpALFKSSFPpgsEVQLVESGGGLVQPGNS LRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTI SRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS**</td>

<td> 426</td><td> ACP205</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpPLAQKLKSSpgscdlpqthnlmkraltllvqmrrlsplsclkdrkdfglpqekvdaq qikkaqaipvlseltqqilmftskdssaawnttlldsfcndlhqqlndlqgclmqqvgvqelpltqedallavrkyfhritv ylrekkhspcawewraevwralsssanvlgrlreeksggpPLAQKLKSSpgsEVQLVESGGGLVQP GNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKG RFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS**</td>

<td> 427</td><td> ACP206</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS</td>

<td></td><td></td><td> SQGTLVTVSSsggpGPAGLYAQpgscdlpqthslgsrrtlmllaqmrrislfsclkdrhdfgipqeefgnqf qkaetipvlhemiqqifiilfstkdssaawdetlldkfytelyqqlndleacviqgvgvtetplmkedsilavrkyfqritlyl kekkyspcawewraeimrsfslstnlqeslrskesggpGPAGLYAQpgsEVQLVESGGGLVQPGN SLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFT ISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS**</td>

<td> 428</td><td> ACP207</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgscdlpqthslgsrrtlmllaqmrrislfsclkdrhdfgipqeefgnqfq kaetipvlhemiqqifiilfstkdssaawdetlldkfytelyqqlndleacviqgvgvtetplmkedsilavrkyfqritlylk ekkyspcawewraeimrsfslstnlqeslrskesggpALFKSSFPpgsEVQLVESGGGLVQPGNSL RLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTIS RDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS**</td>

<td> 429</td><td> ACP208</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpPLAQKLKSSpgscdlpqthslgsrrtlmllaqmrrislfsclkdrhdfgipqeefgnqf qkaetipvlhemiqqifiilfstkdssaawdetlldkfytelyqqlndleacviqgvgvtetplmkedsilavrkyfqritlyl kekkyspcawewraeimrsfslstnlqeslrskesggpPLAQKLKSSpgsEVQLVESGGGLVQPG NSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRF TISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS**</td>

<td> 430</td><td> ACP211</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPGPAGMKGLPGShgtviesleslnnyfiissgidveekslfldiwmwqkdgdm kilqsqiisfylrlfevlkdnqaisnnisvieshlittffsnskakkdafinsiakfevnnpqvqrqafiielirwhqllpesslr krkrsrcSGGPGPAGMKGLPGScdlpqthnlmkraltllvqnm-lsplsclkdrkdfglpqekvdaqqikka qaipvlseltqqilniftskdssaawnttlldsfcndlhqqlndlqgclmqqvgvqelpltqedallavrkyfhritvylrek khspcawewraevwralsssanvlgrlreekSGGPGPAGMKGLPGShgtviesleslnnyfiissgidveek slfldiwmwqkdgdmkilqsqiisiylrlfevlkdnqaismiisvieshlittffsnskakkdafinsiakfevnnpqvqr qafhelirwhqllpesslrkrkrsrcSGGPGPAGMKGLPGSEVQLVESGGGLVQPGNSLRLS CAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISRDN AKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSHHHHHH</td>

<td> 431</td><td> ACP213</td><td> Iveepknlvktncdlyeklgeygfqnailvi-ytqkapqvstptlveaamlgrvgtkcctlpedqrlpcvedylsailnrvcl Ihektpvsehvtkccsgslverrpcfsaltvdetyvpkefkaetftfhsdictlpekekqikkqtalaelvldikpkataeqlk tvmddfaqfldtcckaadkdtcfstegpnlvtrckdalaSGGPGPAGMKGLPGShgtviesleslnnyfiissgi dveekslfldiwrnwqkdgdmkilqsqiisfylrlfevlkdnqaismiisvieshlittffsnskakkdafmsiakfevmi pqvqrqafiielirwhqllpesslrkrkrsrcSGGPGPAGMKGLPGSlveepknlvktncdlyeklgeygfqn ailvi-ytqkapqvstptlveaamlgrvgtkcctlpedqrlpcvedylsailnrvcllhektpvsehvtkccsgslvenpcfs altvdetyvpkefkaetftfhsdictlpekekqikkqtalaelvkhkpkataeqlktvmddfaqfldtcckaadkdtcfste gpnlvtrckdalaSGGPGPAGMKGLPGShgtviesleslnnyfiissgidveekslfldiwmwqkdgdmkil qsqiisfylrlfevlkdnqaisnnisvieshlittffsnskakkdafinsiakfevnnpqvqrqafiielirwhqllpesslrkr krsrcSGGPGPAGMKGLPGSlveepknlvktncdlyeklgeygfqnailvrytqkapqvstptlveaamlgr vgtkcctlpedqrlpcvedylsailnrvcllhektpvsehvtkccsgslverrpcfsaltvdetyvpkefkaetftfhsdictl pekekqikkqtalaelvkhkpkataeqlktvmddfaqfldtcckaadkdtcfstegpnlvtrckdalaHHHHHH**</td>

<td> 432</td><td> ACP214</td><td> eahkseiahryndlgeqhfkglvliafsqylqkcsydehaklvqevtdfaktcvadesaancdkslhtlfgdklcaipnlr enygeladcctkqepemecflqhkddnpslppfeipeaeamctsfkenpttfrnghylhevarrhpyfyapellyyaeq yneiltqccaeadkescltpkldgvkekalvssvrqGGGGSGGGGSGGSlveepknlvktncdlyeklgeygf qnailvi-ytqkapqvstptlveaamlgrvgtkcctlpedqrlpcvedylsailnrvcllhektpvsehvtkccsgslverrp cfsaltvdetyvpkefkaetftfhsdictlpekekqikkqtalaelvkhkpkataeqlktvmddfaqfldtcckaadkdtcf stegpnlvtrckdalaSGGPGPAGMKGLPGShgtviesleslnnyfhssgidveekslfldiwmwqkdgdm kilqsqiisfylrlfevlkdnqaisnnisvieshlittffsnskakkdafinsiakfevnnpqvqrqafiielirwhqllpesslr krkrsrcSGGPGPAGMKGLPGSeahkseiahryndlgeqhfkglvliafsqylqkcsydehaklvqevtdfa ktcvadesaancdkslhtlfgdklcaipnlrenygeladcctkqepemecflqhkddnpslppferpeaeamctsfken pttfmghylhevarrhpyfyapellyyaeqyneiltqccaeadkescltpkldgvkekalvssvrqGGGGSGGGG SGGSlveepknlvktncdlyeklgeygfqnailvrytqkapqvstptlveaamlgrvgtkcctlpedqrlpcvedylsa</td>

<td></td><td></td><td> ilnrvcllhektpvsehvtkccsgslverrpcfsaltvdetyvpkefkaetftfhsdictlpekekqikkqtalaelvldikpk ataeqlktvmddfaqfldtcckaadkdtcfstegpnlvtrckdalaSGGPGPAGMKGLPGShgtviesleslnn yfiissgidveekslfldiwmwqkdgdmkilqsqiisfylrlfevlkdnqaisnnisvieshlittffsnskakkdafinsia kfevnnpqvqrqafhelirwhqllpesslrkrkrsrcSGGPGPAGMKGLPGSeahkseiahryndlgeqhfk glvliafsqylqkcsydehaklvqevtdfaktcvadesaancdkslhtlfgdklcaipnlrenygeladcctkqepemec flqhkddnpslppferpeaeamctsfkenpttfmghylhevarrhpyiyapellyyaeqyneiltqccaeadkescltpk IdgvkekalvssvrqGGGGSGGGGSGGSlveepknlvktncdlyeklgeygfqnailvrytqkapqvstptlv eaamlgrvgtkcctlpedqrlpcvedylsailnrvcllhektpvsehvtkccsgslverrpcfsaltvdetyvpkefkaetft fhsdictlpekekqikkqtalaelvkhkpkataeqlktvmddfaqfldtcckaadkdtcfstegpnlvtrckdalaHHH HHH**</td>

<td> 433</td><td> ACP215</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSggggsgggSGGPGPAGMKGLPGSggggsgggshgtviesleslnnyfiissgidvee kslfldiwmwqkdgdmkilqsqiisfylrlfevlkdnqaisnnisvieshlittffsnskakkdafinsiakfevnnpqvq rqafiielirwhqllpesslrkrkrsrcggggsgggSGGPGPAGMKGLPGSggggsgggsEVQLVESG GGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLY AESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTV SSggggsgggSGGPGPAGMKGLPGSggggsgggshgtviesleslnnyfiissgidveekslfldiwmwq kdgdmkilqsqiisfylrlfevlkdnqaisnnisvieshlittfFsnskakkdafinsiakfevnnpqvqrqafiielirwhq UpesslrkrkrsrcggggsgggSGGPGPAGMKGLPGSggggsgggsEVQLVESGGGLVQPGN SLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFT ISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSHHHHHH* *</td>

<td> 434</td><td> ACP240</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSggggsggggsggggsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqssevl gsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwlttistd Itfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssffirdi ikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvraqd ryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedidhedi trdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiildkg mlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssaggggsggggsggggsg gggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNT VKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAEDEAD YYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGWQPGR SLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYDGSNKYYADSVKGR FTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVSSHHH HHH</td>

<td> 435</td><td> ACP241</td><td> EAHKSEIAHRYNDLGEQHFKGLVLIAFSQYLQKCSYDEHAKLVQEVTDFAKT CVADESAANCDKSLHTLFGDKLCAIPNLRENYGELADCCTKQEPERNECFLQH KDDNPSLPPFERPEAEAMCTSFKENPTTFMGHYLHEVARRHPYFYAPELLYYA EQYNEILTQCCAEADKESCLTPKLDGVKEKALVSSVRQRMKCSSMQKFGERA FKAWAVARLSQTFPNADFAEITKLATDLTKVNKECCHGDLLECADDRAELAK YMCENQATISSKLQTCCDKPLLKKAHCLSEVEHDTMPADLPAIAADFVEDQE VCKNYAEAKDVFLGTFLYEYSRRHPDYSVSLLLRLAKKYEATLEKCCAEANP PACYGTVLAEFQPLVEEPKNLVKTNCDLYEKLGEYGFQNAILVRYTQKAPQV STPTLVEAARNLGRVGTKCCTLPEDQRLPCVEDYLSAILNRVCLLHEKTPVSE HVTKCCSGSLVERRPCFSALTVDETYVPKEFKAETFTFHSDICTLPEKEKQIKK QTALAELVKHKPKATAEQLKTVMDDFAQFLDTCCKAADKDTCFSTEGPNLVT RCKDALASGGPGPAGMKGLPGSiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt</td>

<td></td><td></td><td> istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkpUmsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedi dheditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqi ildkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssaSGGPGPAG MKGLPGSggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGS RSNIGSNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGL QAEDEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGG GWQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYDGSNKYY ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMV TVSSHHHHHH**</td>

<td> 436</td><td> ACP242</td><td> iwelkkdvyweldwypdapgemwltcdtpeedgitwtldqssevlgsgktltiqvkefgdagqytchkggevlshs llllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwlttistdltfsvkssrgssdpqgvtcgaatlsaervrgd nkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssffirdiikpdppknlqlkplknsrqvevsweypdt wstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvraqdryyssswsewasvpcsggggsggggsgg ggsrvipvsgparclsqsmllkttddmvktareklkhysctaedidheditrdqtstlktclplelhknesclatretssttrgs clppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiildkgmlvaidelmqslnhngetlrqkppvgead pyrvkmklcillhafstrwtmrvmgylssaSGGPGPAGMKGLPGSggggsggggsggggsggggsggg gsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQQLPGTAPKLLI YYNDQRPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLF GTGTKVTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYG MHWVRQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMN SLRAEDTAVYYCKTHGSHDNWGQGTMVTVSSSGGPGPAGMKGLPGSEAHKS EIAHRYNDLGEQHFKGLVLIAFSQYLQKCSYDEHAKLVQEVTDFAKTCVADE SAANCDKSLHTLFGDKLCAIPNLRENYGELADCCTKQEPERNECFLQHKDDNP SLPPFERPEAEAMCTSFKENPTTFMGHYLHEVARRHPYFYAPELLYYAEQYNE ILTQCCAEADKESCLTPKLDGVKEKALVSSVRQRMKCSSMQKFGERAFKAWA VARLSQTFPNADFAEITKLATDLTKVNKECCHGDLLECADDRAELAKYMCEN QATISSKLQTCCDKPLLKKAHCLSEVEHDTMPADLPAIAADFVEDQEVCKNY AEAKDVFLGTFLYEYSRRHPDYSVSLLLRLAKKYEATLEKCCAEANPPACYG TVLAEFQPLVEEPKNLVKTNCDLYEKLGEYGFQNAILVRYTQKAPQVSTPTLV EAARNLGRVGTKCCTLPEDQRLPCVEDYLSAILNRVCLLHEKTPVSEHVTKCC SGSLVERRPCFSALTVDETYVPKEFKAETFTFHSDICTLPEKEKQIKKQTALAEL VKHKPKATAEQLKTVMDDFAQFLDTCCKAADKDTCFSTEGPNLVTRCKDAL AHHHHHH**</td>

<td> 437</td><td> ACP243</td><td> vprdcgckpcictvpevssvfifppkpkdvltitltpkvtcvwdiskddpevqfswfvddvevhtaqtqpreeqfnstf rsvselpimhqdwlngkefkcrvnsaalpapiektisktkgrpkapqvytipppkeqmakdkvsltcmitdflpeditv ewqwngqpaenykntqpimdtdgsyfvysklnvqksnweagntftcsvlheglhnhhtekslshspgkSGGPG PAGMKGLPGSiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqssevlgsgktltiqvkefgda gqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwlttistdltfsvkssrgssdpqg vtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssffirdiikpdppknlqlkplk nsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvraqdryyssswsewasvp csggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedidheditrdqtstlktclplelh knesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiildkgmlvaidelmqslnh ngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssaSGGPGPAGMKGLPGSggggsgggg sggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQ QLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQS YDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLS CAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRD NSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVSSHHHHHH**</td>

<td> 438</td><td> ACP244</td><td> iwelkkdvyweldwypdapgemwltcdtpeedgitwtldqssevlgsgktltiqvkefgdagqytchkggevlshs llllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwlttistdltfsvkssrgssdpqgvtcgaatlsaervrgd nkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssffirdiikpdppknlqlkplknsrqvevsweypdt wstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvraqdryyssswsewasvpcsggggsggggsgg ggsrvipvsgparclsqsmllkttddmvktareklkhysctaedidheditrdqtstlktclplelhknesclatretssttrgs clppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiildkgmlvaidelmqslnhngetlrqkppvgead pyrvkmklcillhafstrwtmrvmgylssaSGGPGPAGMKGLPGSggggsggggsggggsggggsggg gsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQQLPGTAPKLLI YYNDQRPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYTHPALLF</td>

<td></td><td></td><td> GTGTKVTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGFTFSSYG MHWVRQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMN SLRAEDTAVYYCKTHGSHDNWGQGTMVTVSSSGGPGPAGMKGLPGSvprdcgc kpcictvpevssvfifppkpkdvltitltpkvtcvwdiskddpevqfswfvddvevhtaqtqpreeqfnstfrsvselpi mhqdwlngkefkcrvnsaalpapiektisktkgrpkapqvytipppkeqmakdkvsltcmitdflpeditvewqwn gqpaenykntqpimdtdgsyfvysklnvqksnweagntftcsvlheglhnhhtekslshspgkHHHHHH**</td>

<td> 439</td><td> ACP245</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPGPAGMKGLPGSiwelkkdvyweldwypdapgemwltcdtpeedgitwtl dqssevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcw wlttistdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyeny tssffirdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrkna sisvraqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhyscta edidheditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnh qqiildkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssaSGGPGPA GMKGLPGSggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCS GSRSNIGSNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAIT GLQAEDEADYYCQSYDRYTHPALLFGTGTKVTVLSGGPGPAGMKGLPGSQV QLVESGGGWQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYD GSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNW GQGTMVTVSSHHHHHH</td>

<td> 440</td><td> ACP247</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPGPAGMKGLPGSiwelkkdvyweldwypdapgemwltcdtpeedgitwtl dqssevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcw wlttistdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyeny tssffirdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrkna sisvraqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhyscta edidheditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnh qqiildkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssaSGGPGPA GMKGLPGSggggsggggsggggsggggsggggsggggsQVQLQESGGGLVQAGGSLRLSC AASGRTFSSVYDMGWFRQAPGKDREFVARITESARNTRYADSVRGRFTISRDN AKNTVYLQMNNLELEDAAVYYCAADPQTVWGTPDYWGQGTQVTVSSHHH HHH</td>

<td> 636</td><td> WW0301</td><td> APTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATEL KHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEY ADETATIVEFLNRWITFCQSIISTLTSGGPGPAGMKGLPGSEVQLVESGGGLVQ PGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKG RFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSGGGGS GGGGSGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSEVQLVESGGGL VQPGGSLRLSCAASGFIESSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDTVR GRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTV SSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKASQNVGTNVGW YQQKPGKAPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQ qyytypytfgggtkveikhhhhhh</td>

<td> 637</td><td> WW0353</td><td> APTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATEL KHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEY ADETATIVEFLNRWITFCQSIISTLTSGGPGPAGMKGLPGSVPRDCGCKPCICTV PEVSSVFIFPPKPKDVLTITLTPKVTCWVDISKDDPEVQFSWFVDDVEVHTAQ TQPREEQFNSIERSVSELPIMHQDWLNGKEFKCRVNSAAFPAPIEKTISKTKGR PKAPQVYTIPPPKEQMAKDKVSLTCMITDFFPEDITVEWQWNGQPAENYKNT QPIMDTDGSYFVYSKLNVQKSbTWEAGNTFTCSVLHEGLHNHHTEKSLSHSPG KGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSSGGPGPAGMKGLPGSEVQLV ESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTY SPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQ GTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKASQNVG TNVGWYQQKPGKAPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFA TYYCQQYYIYPYTFGGGTKVEIKHHHHHH</td>

<td> 638</td><td> WW0355</td><td> APTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATEL KHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEY ADETATIVEFLNRWITFCQSIISTLTSGGPGPAGMKGLPGSGGGGSGGGGSGGG GSGGGGSGGGGSGGGGSEVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTLA WVRQAPGKGLEWVAAIDSSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRA EDTAVYYCARDSNWDALDYWGQGTTVTVSSGGGGSGGGGSGGGGSDIQMT QSPSSLSASVGDRVTITCKASQNVGTNVGWYQQKPGKAPKALIYSASFRYSGV PSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYTYPYTFGGGTKVEIKSGGPG PAGMKGLPGSVPRDCGCKPCICTVPEVSSVFIFPPKPKDVLTITLTPKVTCVW DISKDDPEVQFSWFVDDVEVHTAQTQPREEQFNSTFRSVSELPIMHQDWLNGK EFKCRVNSAAFPAPIEKTISKTKGRPKAPQVYTIPPPKEQMAKDKVSLTCMITD FFPEDITVEWQWNGQPAENYKNTQPIMDTDGSYFVYSKLNVQKSNWEAGNT FTCSVLHEGLHNHHTEKSLSHSPGKHHHHHH</td>

<td> 639</td><td> WW0365</td><td> APTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATEL KHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEY ADETATIVEFLNRWITFCQSIISTLTGGGSGGGSGGGSGGGSEVQLVESGGGLV QPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVK GRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSGGG GSGGGGSGGGGSGGGGSGGGGSGGGGSSGGPGPAGMKGLPGSEVQLVESGG GLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTYSPDT VRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTV TVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKASQNVGTNVG WYQQKPGKAPKALIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYC QQYYTYPYTFGGGTKVEIKHHHHHHEPEA</td>

<td> 640</td><td> WW0366</td><td> APTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATEL KHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEY ADETATIVEFLNRWITFCQSIISTLTSGGPGPAGMKGLPGSEVQLVESGGGLVQ PGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKG RFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSHHHH HHEPEA</td>

<td> 641</td><td> WW0472</td><td> VPRDCGCKPCICTVPEVSSVFIFPPKPKDVLTITLTPKVTCVWDISKDDPEVQF SWFVDDVEVHTAQTQPREEQFNSTFRSVSELPIMHQDWLNGKEFKCRVNSAA FPAPIEKTISKTKGRPKAPQVYTIPPPKEQMAKDKVSLTCMITDFFPEDITVEWQ WNGQPAENYKNTQPIMDTDGSYFVYSKLNVQKSNWEAGNTFTCSVLHEGLH NHHTEKSLSHSPGKSGGPGPAGLYAQPGSAPTSSSTKKTQLQLEHLLLDLQMI LNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSK NFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFCQSIISTL TGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSSGGPGPAGLYAQPGSEVQLV ESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTY SPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQ GTTVTVSSSGGPGPAGLYAQPGSDIQMTQSPSSLSASVGDRVTITCKAREKLW SAVAWYQQKPGKAPKSLIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFA TYYCQQYYIYPYTFGGGTKVEIK</td>

<td> 642</td><td> WW0473</td><td> VPRDCGCKPCICTVPEVSSVFIFPPKPKDVLTITLTPKVTCVWDISKDDPEVQF SWFVDDVEVHTAQTQPREEQFNSTFRSVSELPIMHQDWLNGKEFKCRVNSAA FPAPIEKTISKTKGRPKAPQVYTIPPPKEQMAKDKVSLTCMITDFFPEDITVEWQ WNGQPAENYKNTQPIMDTDGSYFVYSKLNVQKSNWEAGNTFTCSVLHEGLH NHHTEKSLSHSPGKSGGPGPAGLYAQPGSAPTSSSTKKTQLQLEHLLLDLQMI LNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSK NFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFCQSIISTL TGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSSGGPGPAGLYAQPGSEVQLV ESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTY SPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQ GTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKAREKLW SAVAWYQQKPGKAPKSLIYSASFRYSGVPSRFSGSGSGTDFTLTISSLQPEDFA TYYCQQYYIYPYTFGGGTKVEIK</td>

<td> 643</td><td> WW0474</td><td> VPRDCGCKPCICTVPEVSSVFIFPPKPKDVLTITLTPKVTCVWDISKDDPEVQF SWFVDDVEVHTAQTQPREEQFNSTFRSVSELPIMHQDWLNGKEFKCRVNSAA</td>

<td></td><td></td><td> FPAPIEKTISKTKGRPKAPQVYTIPPPKEQMAKDKVSLTCMITDFFPEDITVEWQ WNGQPAENYKNTQPIMDTDGSYFVYSKLNVQKSNWEAGNTFTCSVLHEGLH NHHTEKSLSHSPGKSGGPGPAGLYAQPGSAPTSSSTKKTQLQLEHLLLDLQMI LNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSK NFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFCQSIISTL TGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSSGGPGPAGLYAQPGSEVQLV ESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTY SPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQ GTTVTVSSSGGPGPAGLYAQPGSDIQMTQSPSSLSASVGDRVTITCKVIEKVW GNVAWYQQKPGKAPISLIYSPSLRKSGVPSRFSGSGSGTDFTLTISSLQPEDFAT YYCQQYYTYPYTFGGGTKVEIK</td>

<td> 644</td><td> WW0475</td><td> VPRDCGCKPCICTVPEVSSVFIFPPKPKDVLTITLTPKVTCVWDISKDDPEVQF SWFVDDVEVHTAQTQPREEQFNSTFRSVSELPIMHQDWLNGKEFKCRVNSAA FPAPIEKTISKTKGRPKAPQVYTIPPPKEQMAKDKVSLTCMITDFFPEDITVEWQ WNGQPAENYKNTQPIMDTDGSYFVYSKLNVQKSNWEAGNTFTCSVLHEGLH NHHTEKSLSHSPGKSGGPGPAGLYAQPGSAPTSSSTKKTQLQLEHLLLDLQMI LNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSK NFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFCQSIISTL TGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSSGGPGPAGLYAQPGSEVQLV ESGGGLVQPGGSLRLSCAASGFTFSSYTLAWVRQAPGKGLEWVAAIDSSSYTY SPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQ GTTVTVSSGGGGSGGGGSGGGGSDIQMTQSPSSLSASVGDRVTITCKVTEKV WGNVAWYQQKPGKAPISLIYSPSLRKSGVPSRFSGSGSGTDFTLTISSLQPEDF ATYYCQQYYTYPYTFGGGTKVEIK</td>

<td> 645</td><td> WW0476</td><td> VPRDCGCKPCICTVPEVSSVFIFPPKPKDVLTITLTPKVTCVWDISKDDPEVQF SWFVDDVEVHTAQTQPREEQFNSTFRSVSELPIMHQDWLNGKEFKCRVNSAA FPAPIEKTISKTKGRPKAPQVYTIPPPKEQMAKDKVSLTCMITDFFPEDITVEWQ WNGQPAENYKNTQPIMDTDGSYFVYSKLNVQKSNWEAGNTFTCSVLHEGLH NHHTEKSLSHSPGKSGGPGPAGLYAQPGSAPTSSSTKKTQLQLEHLLLDLQMI LNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSK NFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFCQSIISTL TGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSSGGPGPAGLYAQPGSEVQLL ESGGGLVQPGGSLRLSCAASGSIFSANAMGWYRQAPGKGLELVAVISSGGSTN YADSVKGRFTISRDNSKNTVYLQMNSLRAEDTAVYYCMYSGSYYYTPNDYW GQGTLVTVSS</td>

<td> 646</td><td> WW0477</td><td> VPRDCGCKPCICTVPEVSSVFIFPPKPKDVLTITLTPKVTCVWDISKDDPEVQF SWFVDDVEVHTAQTQPREEQFNSTFRSVSELPIMHQDWLNGKEFKCRVNSAA FPAPIEKTISKTKGRPKAPQVYTIPPPKEQMAKDKVSLTCMITDFFPEDITVEWQ WNGQPAENYKNTQPIMDTDGSYFVYSKLNVQKSNWEAGNTFTCSVLHEGLH NHHTEKSLSHSPGKSGGPGPAGLYAQPGSAPTSSSTKKTQLQLEHLLLDLQMI LNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSK NFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFCQSIISTL TGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSSGGPGPAGLYAQPGSEVQLL ESGGGLVQPGGSLRLSCAASERIFSTDVMGWYRQAPGKQRELVAWSARGTT NYLDAVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCYVRETTSPWRIYWG QGTLVTVSS</td>

<td> 647</td><td> WW0649 Monomeric IL-12 (chimeric) polypeptide , anti-HSA sdAb, scFv Blocker, 2 cleavage sites</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt istdltfsvkssrgssdpqgvtcgaatisaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedi dheditrdqtstlktclplelhknesclatretssttrgsclppqktslmmticlgsiyedlkmyqtefqainaalqnhnhqqi ildkgmlvaidelmqslnhngetirqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpGPAGLY AQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSN IGSNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAE DEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGW QPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYDGSNKYYADS</td>

<td></td><td></td><td> VKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVS g**</td>

<td> 454</td><td> WW0650</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgernwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytclikggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsmipvatpdpgmipcihhsqnllravsnmiqkarqtleiypc tseeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktmnakllm dpkrqifldqnmlavidelmqalnfiisetvpqkssleepdfyktkiklcillhafriravtidrvmsylnassggpGPA GLYAQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSG SRSNIGSNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITG LQAEDEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESG GGWQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYDGSNKY YADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTM VTVSS**</td>

<td> 455</td><td> WW0651</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshslllllikkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr aqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedid heditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiil dkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpALFKSSF PpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNI GSNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAE DEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGW QPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYDGSNKYYADS VKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVS g**</td>

<td> 456</td><td> WW0652</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshslllllikkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr aqdryyssswsewasvpcsggggsggggsggggsmlpvatpdpgmfpclhhsqnllravsnmlqkarqtlefypct seeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktmnakllm dpkrqifldqnmlavidelmqalnfiisetvpqkssleepdfyktkiklcillhafriravtidrvmsylnassggpALFK SSFPpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRS NIGSNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQ AEDEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGG WQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYDGSNKYYA DSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVT VSS**</td>

<td> 457</td><td> WW0662</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytclikggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedi dheditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqi ildkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpGPAGLY AQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSN IGSNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAE DEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGW</td>

<td></td><td></td><td> QPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYeGSNKYYAeSV KGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVSS **</td>

<td> 458</td><td> WW0663</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsmlpvatpdpgmlpclhhsqnllravsnmlqkarqtleiypc tseeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktmnakllm dpkrqifldqnmlavidelmqalnfiisetvpqkssleepdfyktkiklcillhafriravtidrvmsylnassggpGPA GLYAQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSG SRSNIGSNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITG LQAEDEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESG GGWQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYeGSNKYY AeSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMV TVSS**</td>

<td> 459</td><td> WW0664</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedi dheditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqi ildkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpGPAGLY AQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSN IGSeTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAE DEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGW QPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYeGSNKYYAeSV KGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVSS **</td>

<td> 460</td><td> WW0665</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsmlpvatpdpgmlpclhhsqnllravsnmlqkarqtleiypc tseeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktmnakllm dpkrqifldqnmlavidelmqalnfiisetvpqkssleepdfyktkiklcillhafriravtidrvmsylnassggpGPA GLYAQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSG SRSNIGSeTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITG LQAEDEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESG GGWQPGRSLRLSCAASGFIESSYGMHWVRQAPGKGLEWVAFIRYeGSNKYY AeSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMV TVSS**</td>

<td> 461</td><td> WW0666</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedi dheditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqi ildkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpGPAGLY AQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSN IGdNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAE</td>

<td></td><td></td><td> DEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGW QPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYeGSNKYYAeSV KGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVSS **</td>

<td> 462</td><td> WW0667</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkpUmsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsmipvatpdpgmipcihhsqnllravsnmiqkarqtleiypc tseeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktmnakllm dpkrqifldqnmlavidelmqalnfiisetvpqkssleepdfyktkiklcillhafnravtidrvmsylnassggpGPA GLYAQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSG SRSNIGdNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITG LQAEDEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESG GGVVQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYeGSNKYY AeSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMV TVSS**</td>

<td> 463</td><td> WW0668</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkpUmsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedi dheditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqi ildkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpGPAGLY AQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSN IGdeTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAE DEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGW QPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYDGSNKYYADS VKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVS g**</td>

<td> 464</td><td> WW0669</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkpUmsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsmipvatpdpgmipcihhsqnllravsnmiqkarqtleiypc tseeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktmnakllm dpkrqifldqnmlavidelmqalnfiisetvpqkssleepdfyktkiklcillhafnravtidrvmsylnassggpGPA GLYAQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSG SRSNIGdeTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITG LQAEDEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESG GGWQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYDGSNKY YADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTM VTVSS**</td>

<td> 465</td><td> WW0670</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkpUmsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedi dheditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqi ildkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpGPAGLY AQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSN</td>

<td></td><td></td><td> IGdeTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAE DEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGW QPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYeGSNKYYAeSV KGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVSS **</td>

<td> 466</td><td> WW0671</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkpUmsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsmipvatpdpgmipcihhsqnllravsnmiqkarqtleiypc tseeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktmnakllm dpkrqifldqnmlavidelmqalnfiisetvpqkssleepdfyktkiklcillhafnravtidrvmsylnassggpGPA GLYAQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSG SRSNIGdeTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITG LQAEDEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESG GGWQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYeGSNKYY AeSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMV TVSS**</td>

<td> 467</td><td> WW0672</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkpUmsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedi dheditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqi ildkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpGPAGLY AQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSeSN IGSNdVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAE DEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGW QPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYDGSNKYYADS VKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVS g**</td>

<td> 468</td><td> WW0673</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkpUmsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsmipvatpdpgmipcihhsqnllravsnmiqkarqtleiypc tseeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktmnakllm dpkrqifldqnmlavidelmqalnfiisetvpqkssleepdfyktkiklcillhafnravtidrvmsylnassggpGPA GLYAQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSG SeSNIGSNdVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITG LQAEDEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESG GGWQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYDGSNKY YADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTM VTVSS**</td>

<td> 469</td><td> WW0674</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkpUmsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedi dheditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqi ildkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpGPAGLY</td>

<td></td><td></td><td> AQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSN IGeNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAE DEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGW QPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYeGSNKYYAeSV KGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVSS **</td>

<td> 470</td><td> WW0675</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsmlpvatpdpgmlpclhhsqnllravsnmlqkarqtleiypc tseeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktmnakllm dpkrqifldqnmlavidelmqalnfiisetvpqkssleepdfyktkiklcillhafnravtidrvmsylnassggpGPA GLYAQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSG SRSNIGeNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITG LQAEDEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESG GGWQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYeGSNKYY AeSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMV TVSS**</td>

<td> 471</td><td> WW0676</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedi dheditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqi ildkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpGPAGLY AQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSN IGeeTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAE DEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGW QPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYDGSNKYYADS VKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVS g**</td>

<td> 472</td><td> WW0677</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsmlpvatpdpgmlpclhhsqnllravsnmlqkarqtleiypc tseeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktmnakllm dpkrqifldqnmlavidelmqalnfiisetvpqkssleepdfyktkiklcillhafnravtidrvmsylnassggpGPA GLYAQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSG SRSNIGeeTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGL QAEDEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGG GWQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYDGSNKYY ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMV TVSS**</td>

<td> 473</td><td> WW0678</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedi dheditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqi</td>

<td></td><td></td><td> ildkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpGPAGLY AQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSN IGSeTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAE DEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGW QPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYeGSNKYYADSV KGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVSS **</td>

<td> 474</td><td> WW0679</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsmlpvatpdpgmlpclhhsqnllravsnmlqkarqtleiypc tseeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktmnakllm dpkrqifldqnmlavidelmqalnfiisetvpqkssleepdfyktkiklcillhafriravtidrvmsylnassggpGPA GLYAQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSG SRSNIGSeTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITG LQAEDEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESG GGWQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYeGSNKYY ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMV TVSS**</td>

<td> 475</td><td> WW0680</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr aqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedid heditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiil dkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpALFKSSF PpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNI GSNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAE DEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGW QPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYeGSNKYYAeSV KGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVSS **</td>

<td> 476</td><td> WW0681</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr aqdryyssswsewasvpcsggggsggggsggggsmlpvatpdpgmfpclhhsqnllravsnmlqkarqtleiypct seeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktamakllm dpkrqifldqnmlavidelmqalnfiisetvpqkssleepdfyktkiklcillhafriravtidrvmsylnassggpALFK SSFPpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRS NIGSNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQ AEDEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGG WQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYeGSNKYYAe SVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTV SS**</td>

<td> 477</td><td> WW0682</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr aqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedid</td>

<td></td><td></td><td> heditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiil dkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpALFKSSF PpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNI GSeTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAE DEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGW QPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYeGSNKYYAeSV KGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVSS **</td>

<td> 635</td><td> WW0683</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr aqdiyyssswsewasvpcsggggsggggsggggsmlpvatpdpgmfpclhhsqnllravsnmlqkarqtlefypct seeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktmnakllm dpkrqifldqnmlavidelmqalnfhsetvpqkssleepdfyktkiklcillhafriravtidrvmsylnassggpALFK SSFPpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRS NIGSeTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQA EDEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGV VQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYeGSNKYYAeS VKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVS g**</td>

<td> 478</td><td> WW0684</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr aqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedid heditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiil dkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpALFKSSF PpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNI GdNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAE DEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGW QPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYeGSNKYYAeSV KGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVSS **</td>

<td> 479</td><td> WW0685</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr aqdiyyssswsewasvpcsggggsggggsggggsmlpvatpdpgmfpclhhsqnllravsnmlqkarqtlefypct seeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktmnakllm dpkrqifldqnmlavidelmqalnfhsetvpqkssleepdfyktkiklcillhafriravtidrvmsylnassggpALFK SSFPpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRS NIGdNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQA EDEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGV VQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYeGSNKYYAeS VKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVS g**</td>

<td> 480</td><td> WW0686</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr</td>

<td></td><td></td><td> aqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedid heditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiil dkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpALFKSSF PpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNI GdeTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAED EADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGWQ PGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYDGSNKYYADSV KGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVSS **</td>

<td> 481</td><td> WW0687</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr aqdiyyssswsewasvpcsggggsggggsggggsmlpvatpdpgmfpclhhsqnllravsnmlqkarqtlefypct seeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktmnakllm dpkrqifldqnmlavidelmqalnfhsetvpqkssleepdfyktkiklcillhafriravtidrvmsylnassggpALFK SSFPpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRS NIGdeTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQA EDEAD YYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGV VQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYDGSNKYYAD SVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTV SS**</td>

<td> 482</td><td> WW0688</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr aqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedid heditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiil dkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpALFKSSF PpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNI GdeTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAED EADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGWQ PGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYeGSNKYYAeSVK GRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVSS**</td>

<td> 483</td><td> WW0689</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr aqdiyyssswsewasvpcsggggsggggsggggsmlpvatpdpgmfpclhhsqnllravsnmlqkarqtlefypct seeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktmnakllm dpkrqifldqnmlavidelmqalnfhsetvpqkssleepdfyktkiklcillhafriravtidrvmsylnassggpALFK SSFPpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRS NIGdeTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQA EDEAD YYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGV VQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYeGSNKYYAeS VKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVS g**</td>

<td> 484</td><td> WW0690</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr</td>

<td></td><td></td><td> aqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedid heditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiil dkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpALFKSSF PpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSeSNIG SNdVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAED EADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGVVQ PGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYDGSNKYYADSV KGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVSS **</td>

<td> 485</td><td> WW0691</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr aqdiyyssswsewasvpcsggggsggggsggggsmlpvatpdpgmfpclhhsqnllravsnmlqkarqtlefypct seeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktmnakllm dpkrqifldqnmlavidelmqalnfhsetvpqkssleepdfyktkiklcillhafriravtidrvmsylnassggpALFK SSFPpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSeS NIGSNdVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQA EDEAD YYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGV VQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYDGSNKYYAD SVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTV SS**</td>

<td> 486</td><td> WW0692</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr aqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedid heditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiil dkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpALFKSSF PpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNI GeNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAE DEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGVV QPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYeGSNKYYAeSV KGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVSS **</td>

<td> 487</td><td> WW0693</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr aqdiyyssswsewasvpcsggggsggggsggggsmlpvatpdpgmfpclhhsqnllravsnmlqkarqtlefypct seeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktmnakllm dpkrqifldqnmlavidelmqalnfhsetvpqkssleepdfyktkiklcillhafriravtidrvmsylnassggpALFK SSFPpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRS NIGeNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQA EDEAD YYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGV VQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYeGSNKYYAeS VKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVS g**</td>

<td> 488</td><td> WW0694</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff</td>

<td></td><td></td><td> irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr aqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedid heditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiil dkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpALFKSSF PpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNI GeeTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAED EADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGWQ PGRSLRLSCAASGFIESSYGMHWVRQAPGKGLEWVAFIRYDGSNKYYADSV KGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVSS **</td>

<td> 489</td><td> WW0695</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr aqdiyyssswsewasvpcsggggsggggsggggsmlpvatpdpgmfpclhhsqnllravsnmlqkarqtlefypct seeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktamakllm dpkrqifldqnmlavidelmqalnfiisetvpqkssleepdfyktkiklcillhafnravtidrvmsylnassggpALFK SSFPpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRS NIGeeTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQA EDEAD YYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGV VQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYDGSNKYYAD SVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTV SS**</td>

<td> 490</td><td> WW0696</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr aqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedid heditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiil dkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpALFKSSF PpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNI GSeTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAE DEADYYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGW QPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYeGSNKYYADSV KGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVSS **</td>

<td> 491</td><td> WW0697</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr aqdiyyssswsewasvpcsggggsggggsggggsmlpvatpdpgmfpclhhsqnllravsnmlqkarqtlefypct seeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktamakllm dpkrqifldqnmlavidelmqalnfiisetvpqkssleepdfyktkiklcillhafnravtidrvmsylnassggpALFK SSFPpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRS NIGSeTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQA EDEAD YYCQSYDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGV VQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYeGSNKYYADS VKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVS g**</td>

<td> 492</td><td> WW0698</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt</td>

<td></td><td></td><td> istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkpUmsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedi dheditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqainaalqnhnhqqi ildkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpGPAGLY AQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSN IGSNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAE DEADYYCQSYDRYTHPALLFGTGTKVTVLgqpkaapsvtllppsseelqankatlvclisdiypg avtvawkadsspvkagvetttpskqsnnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs**</td>

<td> 493</td><td> WW0699</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkpUmsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsmlpvatpdpgmlpclhhsqnllravsnmlqkarqtleiypc tseeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktmnakllm dpkrqifldqnmlavidelmqalnfiisetvpqkssleepdfyktkiklcillhafnravtidrvmsylnassggpGPA GLYAQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSG SRSNIGSNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITG LQAEDEADYYCQSYDRYTHPALLFGTGTKVTVLgqpkaapsvtltppsseelqankatlvcli sdfypgavtvawkadsspvkagvetttpskq snnkyaassylsltpeq wkshrsyscq vthegstvektvaptecs* *</td>

<td> 494</td><td> WW0700</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkpUmsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedi dheditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqainaalqnhnhqqi ildkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpGPAGLY AQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSN IGSeTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAE DEADYYCQSYDRYTHPALLFGTGTKVTVLgqpkaapsvtllppsseelqankatlvclisdiypg avtvawkadsspvkagvetttpskqsnnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs**</td>

<td> 495</td><td> WW0701</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkpUmsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsmlpvatpdpgmlpclhhsqnllravsnmlqkarqtleiypc tseeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktmnakllm dpkrqifldqnmlavidelmqalnfiisetvpqkssleepdfyktkiklcillhafnravtidrvmsylnassggpGPA GLYAQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSG SRSNIGSeTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITG LQAEDEADYYCQSYDRYTHPALLFGTGTKVTVLgqpkaapsvtlfppsseelqankatlvcli sdfypgavtvawkadsspvkagvetttpskq snnkyaassylsltpeq wkshrsyscq vthegstvektvaptecs* *</td>

<td> 496</td><td> WW0702</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedi dheditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqi ildkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpGPAGLY AQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSN IGdNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAE</td>

<td></td><td></td><td> DEADYYCQSYDRYTHPALLFGTGTKVTVLgqpkaapsvtlfppsseelqankatlvclisdfypg avtvawkadsspvkagvetttpskqsnnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs**</td>

<td> 497</td><td> WW0703</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytclikggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsmipvatpdpgmipcihhsqnllravsnmiqkarqtleiypc tseeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktmnakllm dpkrqifldqnmlavidelmqalnfiisetvpqkssleepdfyktkiklcillhafriravtidrvmsylnassggpGPA GLYAQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSG SRSNIGdNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITG LQAEDEADYYCQSYDRYTHPALLFGTGTKVTVLgqpkaapsvtlfppsseelqankatlvcli sdfypgavtvawkadsspvkagvetttpskq snnkyaassylsltpeq wkshrsyscq vthegstvektvaptecs* *</td>

<td> 498</td><td> WW0704</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytclikggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedi dheditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqi ildkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpGPAGLY AQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSN IGdeTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAE DEADYYCQSYDRYTHPALLFGTGTKVTVLgqpkaapsvtlfppsseelqankatlvclisdfypg avtvawkadsspvkagvetttpskqsnnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs**</td>

<td> 499</td><td> WW0705</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytclikggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsmipvatpdpgmipcihhsqnllravsnmiqkarqtleiypc tseeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktmnakllm dpkrqifldqnmlavidelmqalnfiisetvpqkssleepdfyktkiklcillhafriravtidrvmsylnassggpGPA GLYAQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSG SRSNIGdeTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITG LQAEDEADYYCQSYDRYTHPALLFGTGTKVTVLgqpkaapsvtlfppsseelqankatlvcli sdfypgavtvawkadsspvkagvetttpskqsnnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs**</td>

<td> 500</td><td> WW0706</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytclikggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedi dheditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqi ildkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpGPAGLY AQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSeSN IGSNdVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAE</td>

<td></td><td></td><td> DEADYYCQSYDRYTHPALLFGTGTKVTVLgqpkaapsvtllppsseelqankatlvclisdiypg avtvawkadsspvkagvetttpskqsnnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs**</td>

<td> 501</td><td> WW0707</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsmipvatpdpgmipcihhsqnllravsnmiqkarqtleiypc tseeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktmnakllm dpkrqifldqnmlavidelmqalnfiisetvpqkssleepdfyktkiklcillhafriravtidrvmsylnassggpGPA GLYAQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSG SeSNIGSNdVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITG LQAEDEADYYCQSYDRYTHPALLFGTGTKVTVLgqpkaapsvtlippsseelqankatlvcli sdiypgavtvawkadsspvkagvetttpskqsnnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs**</td>

<td> 502</td><td> WW0708</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedi dheditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqi ildkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpGPAGLY AQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSN IGeNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAE DEADYYCQSYDRYTHPALLFGTGTKVTVLgqpkaapsvtUppsseelqankatlvclisdiypg avtvawkadsspvkagvetttpskqsnnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs**</td>

<td> 503</td><td> WW0709</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsmipvatpdpgmipcihhsqnllravsnmiqkarqtleiypc tseeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktmnakllm dpkrqifldqnmlavidelmqalnfiisetvpqkssleepdfyktkiklcillhafriravtidrvmsylnassggpGPA GLYAQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSG SRSNIGeNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITG LQAEDEADYYCQSYDRYTHPALLFGTGTKVTVLgqpkaapsvtlippsseelqankatlvcli sdfypgavtvawkadsspvkagvetttpskq snnkyaassylsltpeq wkshrsyscq vthegstvektvaptecs* *</td>

<td> 504</td><td> WW0710</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs sevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedi dheditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqi ildkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpGPAGLY AQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSN IGeeTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAE DEADYYCQSYDRYTHPALLFGTGTKVTVLgqpkaapsvtUppsseelqankatlvclisdiypg avtvawkadsspvkagvetttpskqsnnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs**</td>

<td> 505</td><td> WW0711</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpGPAGLYAQpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqs</td>

<td></td><td></td><td> sevlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltt istdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssf firdiikpdppknlqlkpUmsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisv raqdryyssswsewasvpcsggggsggggsggggsmipvatpdpgmipcihhsqnllravsnmiqkarqtleiypc tseeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktmnakllm dpkrqifldqnmlavidelmqalnfiisetvpqkssleepdfyktkiklcillhafnravtidrvmsylnassggpGPA GLYAQpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSG SRSNIGeeTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGL QAEDEADYYCQSYDRYTHPALLFGTGTKVTVLgqpkaapsvtlfppsseelqankatlvclis dfypgavtvawkadsspvkagvetttpskq snnkyaassylsltpeqwkshrsyscq vthegstvektvaptecs* *</td>

<td> 506</td><td> WW0712</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshslllllikkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr aqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedid heditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiil dkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpALFKSSF PpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNI GSNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAE DEADYYCQSYDRYTHPALLFGTGTKVTVLgqpkaapsvtllppsseelqankatlvclisdiypg avtvawkadsspvkagvetttpskqsnnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs**</td>

<td> 507</td><td> WW0713</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshslllllikkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr aqdryyssswsewasvpcsggggsggggsggggsmlpvatpdpgmfpclhhsqnllravsnmlqkarqtleiypct seeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktmnakllm dpkrqifldqnmlavidelmqalnfiisetvpqkssleepdfyktkiklcillhafriravtidrvmsylnassggpALFK SSFPpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRS NIGSNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQ AEDEADYYCQSYDRYTHPALLFGTGTKVTVLgqpkaapsvtlfppsseelqankatlvclisdf ypgavtvawkadsspvkagvetttpskqsnnkyaassylsltpeqwkshrsyscq vthegstvektvaptecs**</td>

<td> 508</td><td> WW0714</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr aqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedid heditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiil dkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpALFKSSF PpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNI GSeTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAE DEADYYCQSYDRYTHPALLFGTGTKVTVLgqpkaapsvtllppsseelqankatlvclisdiypg avtvawkadsspvkagvetttpskqsnnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs**</td>

<td> 509</td><td> WW0715</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr aqdryyssswsewasvpcsggggsggggsggggsmlpvatpdpgmipclhhsqnllravsnmlqkarqtleiypct seeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktmnakllm dpkrqifldqnmlavidelmqalnfiisetvpqkssleepdfyktkiklcillhafriravtidrvmsylnassggpALFK SSFPpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRS</td>

<td></td><td></td><td> NIGSeTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQA EDEADYYCQSYDRYTHPALLFGTGTKVTVLgqpkaapsvtlfppsseelqankatlvclisdfyp gavtvawkadsspvkagvetttpskqsnnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs**</td>

<td> 510</td><td> WW0716</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr aqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedid heditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiil dkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpALFKSSF PpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNI GdNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAE DEADYYCQSYDRYTHPALLFGTGTKVTVLgqpkaapsvtllppsseelqatikatlvclisdiypg avtvawkadsspvkagvetttpskqsnnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs**</td>

<td> 511</td><td> WW0717</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr aqdryyssswsewasvpcsggggsggggsggggsmlpvatpdpgmfpclhhsqnllravsnmlqkarqtlefypct seeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktmnakllm dpkrqifldqnmlavidelmqalnfiisetvpqkssleepdfyktkiklcillhafriravtidrvmsylnassggpALFK SSFPpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRS NIGdNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQA EDEADYYCQSYDRYTHPALLFGTGTKVTVLgqpkaapsvtlfppsseelqankatlvclisdfyp gavtvawkadsspvkagvetttpskqsnnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs**</td>

<td> 512</td><td> WW0718</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr aqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedid heditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiil dkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpALFKSSF PpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNI GdeTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAED EADYYCQSYDRYTHPALLFGTGTKVTVLgqpkaapsvtllppsseelqankatlvclisdiypga vtvawkadsspvkagvetttpskqsnnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs**</td>

<td></td><td></td><td></td>

<td> 513</td><td> WW0719</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshslllllikkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr aqdryyssswsewasvpcsggggsggggsggggsmlpvatpdpgmfpclhhsqnllravsnmlqkarqtlefypct seeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktmnakllm dpkrqifldqnmlavidelmqalnfiisetvpqkssleepdfyktkiklcillhafriravtidrvmsylnassggpALFK SSFPpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRS NIGdeTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQA EDEADYYCQSYDRYTHPALLFGTGTKVTVLgqpkaapsvtlfppsseelqankatlvclisdfyp gavtvawkadsspvkagvetttpskqsnnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs**</td>

<td> 514</td><td> WW0720</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshslllllikkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr aqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedid heditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiil dkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpALFKSSF PpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSeSNIG SNdVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAED EADYYCQSYDRYTHPALLFGTGTKVTVLgqpkaapsvtllppsseelqankatlvclisdiypga vtvawkadsspvkagvetttpskqsnnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs**</td>

<td> 515</td><td> WW0721</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshslllllikkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff</td>

<td></td><td></td><td> irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr aqdryyssswsewasvpcsggggsggggsggggsmlpvatpdpgmfpclhhsqnllravsnmlqkarqtlefypct seeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktmnakllm dpkrqifldqnmlavidelmqalnfiisetvpqkssleepdfyktkiklcillhafriravtidrvmsylnassggpALFK SSFPpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSeS NIGSNdVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQA EDEADYYCQSYDRYTHPALLFGTGTKVTVLgqpkaapsvtlfppsseelqankatlvclisdfyp gavtvawkadsspvkagvetttpskqsnnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs**</td>

<td> 516</td><td> WW0722</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr aqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedid heditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiil dkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpALFKSSF PpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNI GeNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAE DEADYYCQSYDRYTHPALLFGTGTKVTVLgqpkaapsvtlippsseelqatikatlvclisdiypg avtvawkadsspvkagvetttpskqsnnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs**</td>

<td> 517</td><td> WW0723</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr aqdryyssswsewasvpcsggggsggggsggggsmlpvatpdpgmfpclhhsqnllravsnmlqkarqtlefypct seeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktmnakllm dpkrqifldqnmlavidelmqalnfiisetvpqkssleepdfyktkiklcillhafriravtidrvmsylnassggpALFK SSFPpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRS NIGeNTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQA EDEADYYCQSYDRYTHPALLFGTGTKVTVLgqpkaapsvtlfppsseelqankatlvclisdfyp gavtvawkadsspvkagvetttpskqsnnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs**</td>

<td> 518</td><td> WW0724</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff</td>

<td></td><td></td><td> irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr aqdryyssswsewasvpcsggggsggggsggggsrvipvsgparclsqsmllkttddmvktareklkhysctaedid heditrdqtstlktclplelhknesclatretssttrgsclppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiil dkgmlvaidelmqslnhngetlrqkppvgeadpyrvkmklcillhafstrwtmrvmgylssasggpALFKSSF PpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNI GeeTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAED EADYYCQSYDRYTHPALLFGTGTKVTVLgqpkaapsvtllppsseelqankatlvclisdiypga vtvawkadsspvkagvetttpskqsnnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs**</td>

<td> 519</td><td> WW0725</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSsggpALFKSSFPpgsiwelkkdvyweldwypdapgemwltcdtpeedgitwtldqss evlgsgktltiqvkefgdagqytchkggevlshsllllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwltti stdltfsvkssrgssdpqgvtcgaatlsaervrgdnkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssff irdiikpdppknlqlkplknsrqvevsweypdtwstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvr aqdryyssswsewasvpcsggggsggggsggggsmlpvatpdpgmfpclhhsqnllravsnmlqkarqtleiypct seeidheditkdktstveaclpleltknesclnsretsfitngsclasrktsfmmalclssiyedlkmyqvefktamakllm dpkrqifldqnmlavidelmqalnfiisetvpqkssleepdfyktkiklcillhafriravtidrvmsylnassggpALFK SSFPpgsggggsggggsggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRS NIGeeTVKWYQQLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQA EDEADYYCQSYDRYTFTPALLFGTGTKVTVLgqpkaapsvtlfppsseelqankatlvclisdiyp gavtvawkadsspvkagvetttpskqsnnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs**</td>

<td> 520</td><td> WW0726</td><td> QVQLVESGGGVVQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIR YDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHD NWGQGTMVTVSSastkgpsvlplapsskstsggtaalgclvkdyipepvtvswnsgaltsgvhtlpavlqssgl yslsswtvpssslgtqtyicnvnhkpsntkvdkrvepksc* *</td>

<td> 521</td><td> WW0727</td><td> QVQLVESGGGVVQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIR YeGSNKYYAeSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDN WGQGTMVTVSSastkgpsvlplapsskstsggtaalgclvkdyipepvtvswnsgaltsgvhtipavlqssgly slsswtvpssslgtqtyicnvnhkpsntkvdkrvepksc**</td>

<td> 522</td><td> WW0728</td><td> QVQLVESGGGVVQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIR YeGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCKTHGSHDN WGQGTMVTVSSastkgpsvlplapsskstsggtaalgclvkdyipepvtvswnsgaltsgvhtipavlqssgly slsswtvpssslgtqtyicnvnhkpsntkvdkrvepksc**</td>

<td></td><td></td><td></td>

<td> 523</td><td> WW0765</td><td> iwelkkdvyweldwypdapgemwltcdtpeedgitwtldqssevlgsgktltiqvkefgdagqytchkggevlshs llllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwlttistdltfsvkssrgssdpqgvtcgaatlsaervrgd nkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssffirdiikpdppknlqlkplknsrqvevsweypdt wstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvraqdryyssswsewasvpcsggggsggggsgg ggsrvipvsgparclsqsmllkttddmvktareklkhysctaedidheditrdqtstlktclplelhknesclatretssttrgs clppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiildkgmlvaidelmqslnhngetlrqkppvgead pyrvkmklcillhafstrwtmrvmgylssasggpGPAGLYAQpgsEVQLVESGGGLVQPGNSL RLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTIS RDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsgg ggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQQLP GTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDR YTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAA SGFTFSSYGMHWVRQAPGKGLEWVAFIRYeGSNKYYAeSVKGRFTISRDNSKN tlylomnslraedtavyyckthgshdnwgqgtmvtvss**</td>

<td> 524</td><td> WW0766</td><td> iwelkkdvyweldwypdapgemwltcdtpeedgitwtldqssevlgsgktltiqvkefgdagqytchkggevlshs llllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwlttistdltfsvkssrgssdpqgvtcgaatlsaervrgd nkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssffirdiikpdppknlqlkplknsrqvevsweypdt wstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvraqdryyssswsewasvpcsggggsggggsgg ggsmipvatpdpgmipcihhsqiillravsnmiqkarqtleiypctseeidheditkdktstveacipleltknescinsre tsfitngsclasrktsfinmalclssiyedlkmyqvefktmnakllmdpkrqifldqnmlavidelmqalnfiisetvpqk ssleepdfyktkiklcillhafriravtidrvmsylnassggpGPAGLYAQpgsEVQLVESGGGLVQPG nslrlscaasgftfskfgmswvrqapgkglewvssisgsgrdtlyaesvkgrf TISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsgggg sggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQ qlpgtapklliyyndqrpsgvpdrfsgsksgtsaslaitglqaedeadyycqs YDRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLS CAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYeGSNKYYAeSVKGRFTISRD nskntlylqmnslraedtavyyckthgshdnwgqgtmvtvss**</td>

<td> 525</td><td> WW0767</td><td> iwelkkdvyweldwypdapgemwltcdtpeedgitwtldqssevlgsgktltiqvkefgdagqytchkggevlshs llllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwlttistdltfsvkssrgssdpqgvtcgaatlsaervrgd nkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssffirdiikpdppknlqlkplknsrqvevsweypdt wstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvraqdryyssswsewasvpcsggggsggggsgg ggsrvipvsgparclsqsmllkttddmvktareklkhysctaedidheditrdqtstlktclplelhknesclatretssttrgs clppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiildkgmlvaidelmqslnhngetlrqkppvgead pyrvkmklcillhafstrwtmrvmgylssasggpGPAGLYAQpgsEVQLVESGGGLVQPGNSL rlscaasgftfskfgmswvrqapgkglewvssisgsgrdtlyaesvkgrftis RDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsgg ggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNIGdeTVKWYQQLP gtapklliyyndqrpsgvpdrfsgsksgtsaslaitglqaedeadyycqsydr YTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAA SGFTFSSYGMHWVRQAPGKGLEWVAFIRYeGSNKYYAeSVKGRFTISRDNSKN tlylomnslraedtavyyckthgshdnwgqgtmvtvss**</td>

<td> 526</td><td> WW0768</td><td> iwelkkdvyweldwypdapgemwltcdtpeedgitwtldqssevlgsgktltiqvkefgdagqytchkggevlshs llllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwlttistdltfsvkssrgssdpqgvtcgaatlsaervrgd nkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssffirdiikpdppknlqlkplknsrqvevsweypdt wstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvraqdryyssswsewasvpcsggggsggggsgg ggsmipvatpdpgmipcihhsqiillravsnmiqkarqtleiypctseeidheditkdktstveacipleltknescinsre tsfitngsclasrktsfinmalclssiyedlkmyqvefktmnakllmdpkrqifldqnmlavidelmqalnfiisetvpqk ssleepdfyktkiklcillhafriravtidrvmsylnassggpGPAGLYAQpgsEVQLVESGGGLVQPG nslrlscaasgftfskfgmswvrqapgkglewvssisgsgrdtlyaesvkgrf TISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsgggg</td>

<td></td><td></td><td> sggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNIGdeTVKWYQQ LPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSY DRYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSC AASGFTFSSYGMHWVRQAPGKGLEWVAFIRYeGSNKYYAeSVKGRFTISRDNS KNTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVSS**</td>

<td> 527</td><td> WW0769</td><td> iwelkkdvyweldwypdapgemwltcdtpeedgitwtldqssevlgsgktltiqvkefgdagqytchkggevlshs llllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwlttistdltfsvkssrgssdpqgvtcgaatlsaervrgd nkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssffirdiikpdppknlqlkplknsrqvevsweypdt wstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvraqdryyssswsewasvpcsggggsggggsgg ggsrvipvsgparclsqsmllkttddmvktareklkhysctaedidheditrdqtstlktclplelhknesclatretssttrgs clppqktslmmtlclgsiyedlkmyqtefqainaalqnhnhqqiildkgmlvaidelmqslnhngetlrqkppvgead pyrvkmklcillhafstrwtmrvmgylssasggpGPAGLYAQpgsEVQLVESGGGLVQPGNSL RLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTIS RDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsgg ggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQQLP GTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDR YTHPALLFGTGTKVTVLgqpkaapsvtltppsseelqankatlvclisdlypgavtvawkadsspvkagv etttpskq snnkyaassylsltpeq wkshrsyscq vthegstvektvaptecs* *</td>

<td> 528</td><td> WW0770</td><td> iwelkkdvyweldwypdapgemwltcdtpeedgitwtldqssevlgsgktltiqvkefgdagqytchkggevlshs llllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwlttistdltfsvkssrgssdpqgvtcgaatlsaervrgd nkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssffirdiikpdppknlqlkplknsrqvevsweypdt wstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvraqdryyssswsewasvpcsggggsggggsgg ggsmlpvatpdpgmtpclhhsqnllravsnmlqkarqtlelypctseeidheditkdktstveaclpleltknesclnsre tsfitngsclasrktsfinmalclssiyedlkmyqvefktmnakllmdpkrqifldqnmlavidelmqalnfiisetvpqk ssleepdfyktkiklcillhafriravtidrvmsylnassggpGPAGLYAQpgsEVQLVESGGGLVQPG NSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRF TISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsgggg sggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQ QLPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQS YDRYTHPALLFGTGTKVTVLgqpkaapsvtltppsseelqankatlvclisdlypgavtvawkadsspv kagvetttpskq snnkyaassylsltpeq wkshrsyscq vthegstvektvaptecs* *</td>

<td> 529</td><td> WW0771</td><td> iwelkkdvyweldwypdapgemwltcdtpeedgitwtldqssevlgsgktltiqvkefgdagqytchkggevlshs llllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwlttistdltfsvkssrgssdpqgvtcgaatlsaervrgd nkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssffirdiikpdppknlqlkplknsrqvevsweypdt wstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvraqdryyssswsewasvpcsggggsggggsgg ggsrvipvsgparclsqsmllkttddmvktareklkhysctaedidheditrdqtstlktclplelhknesclatretssttrgs clppqktslmmtlclgsiyedlkmyqtefqainaalqnhnhqqiildkgmlvaidelmqslnhngetlrqkppvgead pyrvkmklcillhafstrwtmrvmgylssasggpGPAGLYAQpgsEVQLVESGGGLVQPGNSL RLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTIS RDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsgg ggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNIGdeTVKWYQQLP GTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDR YTHPALLFGTGTKVTVLgqpkaapsvtltppsseelqankatlvclisdlypgavtvawkadsspvkagv etttpskq snnkyaassylsltpeq wkshrsyscq vthegstvektvaptecs* *</td>

<td> 530</td><td> WW0772</td><td> iwelkkdvyweldwypdapgemwltcdtpeedgitwtldqssevlgsgktltiqvkefgdagqytchkggevlshs llllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwlttistdltfsvkssrgssdpqgvtcgaatlsaervrgd nkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssffirdiikpdppknlqlkplknsrqvevsweypdt wstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvraqdryyssswsewasvpcsggggsggggsgg ggsmlpvatpdpgmfpclhhsqnllravsnmlqkarqtlefypctseeidheditkdktstveaclpleltknesclnsre tsfitngsclasrktsfinmalclssiyedlkmyqvefktmnakllmdpkrqifldqnmlavidelmqalnfiisetvpqk ssleepdfyktkiklcillhafriravtidrvmsylnassggpGPAGLYAQpgsEVQLVESGGGLVQPG NSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRF TISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsgggg sggggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNIGdeTVKWYQQ LPGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSY DRYTHPALLFGTGTKVTVLgqpkaapsvtltppsseelqankatlvclisdlypgavtvawkadsspvka gvetttpskq snnkyaassylsltpeq wkshrsyscq vthegstvektvaptecs* *</td>

<td> 531</td><td> WW0796</td><td> iwelkkdvyweldwypdapgemwltcdtpeedgitwtldqssevlgsgktltiqvkefgdagqytchkggevlshs llllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwlttistdltfsvkssrgssdpqgvtcgaatlsaervrgd nkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssffirdiikpdppknlqlkplknsrqvevsweypdt wstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvraqdryyssswsewasvpcsggggsggggsgg ggsrvipvsgparclsqsmllkttddmvktareklkhysctaedidheditrdqtstlktclplelhknesclatretssttrgs clppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiildkgmlvaidelmqslnhngetlrqkppvgead pyrvkmklcillhafstrwtmrvmgylssasggpALFKSSFPpgsEVQLVESGGGLVQPGNSLR LSCAASGFIFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISR DNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsgggg sggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQQLPG TAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRY THPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAAS GFTFSSYGMHWVRQAPGKGLEWVAFIRYeGSNKYYAeSVKGRFTISRDNSKN TLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVSS**</td>

<td> 532</td><td> WW0797</td><td> iwelkkdvyweldwypdapgemwltcdtpeedgitwtldqssevlgsgktltiqvkefgdagqytchkggevlshs llllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwlttistdltfsvkssrgssdpqgvtcgaatlsaervrgd nkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssffirdiikpdppknlqlkplknsrqvevsweypdt wstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvraqdryyssswsewasvpcsggggsggggsgg ggsmipvatpdpgmipcihhsqiillravsnmiqkarqtleiypctseeidheditkdktstveacipleltknescinsre tsfitngsclasrktsfinmalclssiyedlkmyqvefktmnakllmdpkrqifldqnmlavidelmqalnfiisetvpqk ssleepdfyktkiklcillhafriravtidrvmsylnassggpALFKSSFPpgsEVQLVESGGGLVQPGN SLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFT ISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsg gggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQQL PGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYD RYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCA ASGFTFSSYGMHWVRQAPGKGLEWVAFIRYeGSNKYYAeSVKGRFTISRDNSK NTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVSS**</td>

<td> 533</td><td> WW0798</td><td> iwelkkdvyweldwypdapgemwltcdtpeedgitwtldqssevlgsgktltiqvkefgdagqytchkggevlshs llllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwlttistdltfsvkssrgssdpqgvtcgaatlsaervrgd nkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssffirdiikpdppknlqlkplknsrqvevsweypdt wstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvraqdryyssswsewasvpcsggggsggggsgg ggsrvipvsgparclsqsmllkttddmvktareklkhysctaedidheditrdqtstlktclplelhknesclatretssttrgs clppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiildkgmlvaidelmqslnhngetlrqkppvgead pyrvkmklcillhafstrwtmrvmgylssasggpALFKSSFPpgsEVQLVESGGGLVQPGNSLR LSCAASGFIFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISR DNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsgggg sggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNIGdeTVKWYQQLPGT APKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYT HPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCAASGF</td>

<td></td><td></td><td> TFSSYGMHWVRQAPGKGLEWVAFIRYeGSNKYYAeSVKGRFTISRDNSKNTL YLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVSS**</td>

<td> 534</td><td> WW0799</td><td> iwelkkdvyweldwypdapgemwltcdtpeedgitwtldqssevlgsgktltiqvkefgdagqytchkggevlshs llllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwlttistdltfsvkssrgssdpqgvtcgaatlsaervrgd nkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssffirdiikpdppknlqlkplknsrqvevsweypdt wstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvraqdryyssswsewasvpcsggggsggggsgg ggsmipvatpdpgmipcihhsqiillravsnmiqkarqtleiypctseeidheditkdktstveacipleltknescinsre tsfitngsclasrktsfinmalclssiyedlkmyqvefktmnakllmdpkrqifldqnmlavidelmqalnfiisetvpqk ssleepdfyktkiklcillhafriravtidrvmsylnassggpALFKSSFPpgsEVQLVESGGGLVQPGN SLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFT ISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsg gggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNIGdeTVKWYQQL PGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYD RYTHPALLFGTGTKVTVLggggsggggsggggsQVQLVESGGGWQPGRSLRLSCA ASGFTFSSYGMHWVRQAPGKGLEWVAFIRYeGSNKYYAeSVKGRFTISRDNSK NTLYLQMNSLRAEDTAVYYCKTHGSHDNWGQGTMVTVSS**</td>

<td> 535</td><td> WW0800</td><td> iwelkkdvyweldwypdapgemwltcdtpeedgitwtldqssevlgsgktltiqvkefgdagqytchkggevlshs llllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwlttistdltfsvkssrgssdpqgvtcgaatlsaervrgd nkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssffirdiikpdppknlqlkplknsrqvevsweypdt wstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvraqdryyssswsewasvpcsggggsggggsgg ggsrvipvsgparclsqsmllkttddmvktareklkhysctaedidheditrdqtstlktclplelhknesclatretssttrgs clppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiildkgmlvaidelmqslnhngetlrqkppvgead pyrvkmklcillhafstrvvtmrvmgylssasggpALFKSSFPpgsEVQLVESGGGLVQPGNSLR LSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISR DNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsgggg sggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQQLPG TAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRY THPALLFGTGTKVTVLgqpkaapsvtUppsseelqankatlvclisdiypgavtvawkadsspvkagvett tpskqsnnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs**</td>

<td> 536</td><td> WW0801</td><td> iwelkkdvyweldwypdapgemwltcdtpeedgitwtldqssevlgsgktltiqvkefgdagqytchkggevlshs llllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwlttistdltfsvkssrgssdpqgvtcgaatlsaervrgd nkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssffirdiikpdppknlqlkplknsrqvevsweypdt wstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvraqdryyssswsewasvpcsggggsggggsgg ggsmipvatpdpgmipcihhsqiillravsnmiqkarqtleiypctseeidheditkdktstveacipleltknescinsre tsfitngsclasrktsfinmalclssiyedlkmyqvefktmnakllmdpkrqifldqnmlavidelmqalnfiisetvpqk ssleepdfyktkiklcillhafriravtidrvmsylnassggpALFKSSFPpgsEVQLVESGGGLVQPGN SLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFT ISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsg gggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNIGSNTVKWYQQL PGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYD RYTHPALLFGTGTKVTVLgqpkaapsvtUppsseelqankatlvclisdiypgavtvawkadsspvkag vetttpskqsnnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs**</td>

<td></td><td></td><td></td>

<td> 537</td><td> WW0802</td><td> iwelkkdvyweldwypdapgemwltcdtpeedgitwtldqssevlgsgktltiqvkefgdagqytchkggevlshs llllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwlttistdltfsvkssrgssdpqgvtcgaatlsaervrgd nkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssffirdiikpdppknlqlkplknsrqvevsweypdt wstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvraqdryyssswsewasvpcsggggsggggsgg ggsrvipvsgparclsqsmllkttddmvktareklkhysctaedidheditrdqtstlktclplelhknesclatretssttrgs clppqktslmmtlclgsiyedlkmyqtefqamaalqnhnhqqiildkgmlvaidelmqslnhngetlrqkppvgead pyrvkmklcillhafstrwtmrvmgylssasggpALFKSSFPpgsEVQLVESGGGLVQPGNSLR LSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFTISR DNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsgggg sggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNIGdeTVKWYQQLPGT APKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDRYT HPALLFGTGTKVTVLgqpkaapsvtllppsseelqankatlvclisdiypgavtvawkadsspvkagvettt pskqsnnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs**</td>

<td> 538</td><td> WW0803</td><td> iwelkkdvyweldwypdapgemwltcdtpeedgitwtldqssevlgsgktltiqvkefgdagqytchkggevlshs llllhkkedgiwstdilkdqkepknktflrceaknysgrftcwwlttistdltfsvkssrgssdpqgvtcgaatlsaervrgd nkeyeysvecqedsacpaaeeslpievmvdavhklkyenytssffirdiikpdppknlqlkplknsrqvevsweypdt wstphsyfsltfcvqvqgkskrekkdrvftdktsatvicrknasisvraqdryyssswsewasvpcsggggsggggsgg ggsmipvatpdpgmipcihhsqiillravsnmiqkarqtleiypctseeidheditkdktstveacipleltknescinsre tsfitngsclasrktsfinmalclssiyedlkmyqvefktmnakllmdpkrqifldqnmlavidelmqalnfiisetvpqk ssleepdfyktkiklcillhafriravtidrvmsylnassggpALFKSSFPpgsEVQLVESGGGLVQPGN SLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKGRFT ISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSggggsggggsg gggsggggsggggsggggsQSVLTQPPSVSGAPGQRVTISCSGSRSNIGdeTVKWYQQL PGTAPKLLIYYNDQRPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYD RYTHPALLFGTGTKVTVLgqpkaapsvtllppsseelqankatlvclisdiypgavtvawkadsspvkag vetttpskqsnnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs**</td>

<td> 539</td><td> WW0643</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPGPAGLYAQPGSCDLPHTYNLRNKRALKVLAQMRRLTPL SCLKDRKDFGFPLEKVDAQQIQKAQSIPVLRDLTQQILNLFASKDSSAAWNAT LLDSFCNDLHQQLNDLQGCLMQQVGVQESPLTQEDSLLAVRIYFHRITVFLRE KKHSPCAWEVVRAEVWRALSSSANVLGRLREEKASGGPGPAGLYAQPGSEV QLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGS GRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQ GTLVTVSS</td>

<td> 540</td><td> WW0644</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPALFKSSFPPGSCDLPHTYNLRNKRALKVLAQMRRLTPLS CLKDRKDFGFPLEKVDAQQIQKAQSIPVLRDLTQQILNLFASKDSSAAWNATL LDSFCNDLHQQLNDLQGCLMQQVGVQESPLTQEDSLLAVRIYFHRITVFLREK KHSPCAWEVVRAEVWRALSSSANVLGRLREEKASGGPALFKSSFPPGSEVQL VESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGR DTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGT LVTVSS</td>

<td> 541</td><td> WW0645</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPGPAGLYAQPGSCNLSQTHSLNNRRTLMLMAQMRRISPFS CLKDRHDFEFPQEEFDGNQFQKAQAISVLHEMMQQTFNLFSTKNSSAAWDET LLEKFYIELFQQMNDLEACVIQEVGVEETPLMNEDSILAVKKYFQRITLYLME KKYSPCAWEWRAEIMRSLSFSTNLQKRLRRKDSGGPGPAGLYAQPGSEVQL VESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGR DTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGT LVTVSS</td>

<td> 542</td><td> WW0646</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPALFKSSFPPGSCNLSQTHSLNNRRTLMLMAQMRRISPFSC LKDRHDFEFPQEEFDGNQFQKAQAISVLHEMMQQTFNLFSTKNSSAAWDETL LEKFYIELFQQMNDLEACVIQEVGVEEIPLMNEDSILAVKKYFQRITLYLMEK KYSPCAWEWRAEIMRSLSFSTNLQKRLRRKDSGGPALFKSSFPPGSEVQLVES GGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTL YAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVT VSS</td>

<td> 543</td><td> WW0647</td><td> CDLPHTYNLRNKRALKVLAQMRRLTPLSCLKDRKDFGFPLEKVDAQQIQKAQ SIPVLRDLTQQILNLFASKDSSAAWNATLLDSFCNDLHQQLNDLQGCLMQQV GVQESPLTQEDSLLAVRIYFHRITVFLREKKHSPCAWEWRAEVWRALSSSAN VLGRLREEKAHHHHHH</td>

<td> 544</td><td> WW0648</td><td> CNLSQTHSLNNRRTLMLMAQMRRISPFSCLKDRHDFEFPQEEFDGNQFQKAQ AISVLHEMMQQTFNLFSTKNSSAAWDETLLEKFYIELFQQMNDLEACVIQEVG VEETPLMNEDSILAVKKYFQRITLYLMEKKYSPCAWEWRAEIMRSLSFSTNL QKRLRRKDHHHHHH</td>

<td> 545</td><td> WW0781</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPGPAGLYAQPGSCDLPQTHSLGSRRTLMLLAQMRRISLFS CLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLD KFYTELYQQLNDLEACVIQGVGVEETPLMKEDSILAVRKYFQRITLYLKEKKY SPCAWEWRAEIMRSFSLSTNLQESLRSKESGGPGPAGLYAQPGSEVQLVESG GGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLY AESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTV SS</td>

<td> 546</td><td> WW0782</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPGPAGLYAQPGSCNLSQTHSLNNRRTLMLMAQMRRISPFS CLKDRHDFEFPQEEFDGNQFQKAQAISVLHEMMQQTFNLFSTKDSSAAWDET LLEKFYIELFQQMNDLEACVIQEVGVEETPLMNEDSILAVKKYFQRITLYLME KKYSPCAWEWRAEIMRSLSFSTNLQKRLRRKDSGGPGPAGLYAQPGSEVQL VESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGR DTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGT LVTVSS</td>

<td></td><td></td><td></td>

<td> 547</td><td> WW0783</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPGPAGLYAQPGSCDLPQTHSLNNRRTLMLMAQMRRISPFS CLKDRHDFEFPQEEFDGNQFQKAQAISVLHEMMQQTFNLFSTKDSSAAWDET LLEKFYIELFQQMNDLEACVIQEVGVEETPLMNEDSILAVKKYFQRITLYLME KKYSPCAWEWRAEIMRSLSFSTNLQKRLRRKDSGGPGPAGLYAQPGSEVQL VESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGR DTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGT LVTVSS</td>

<td> 548</td><td> WW0784</td><td> CDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIP VLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVEE TPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEWRAEIMRSFSLSTNLQESL RSKEHHHHHH</td>

<td> 549</td><td> WW0785</td><td> CNLSQTHSLNNRRTLMLMAQMRRISPFSCLKDRHDFEFPQEEFDGNQFQKAQ AISVLHEMMQQTFNLFSTKDSSAAWDETLLEKFYIELFQQMNDLEACVIQEVG VEETPLMNEDSILAVKKYFQRITLYLMEKKYSPCAWEWRAEIMRSLSFSTNL QKRLRRKDHHHHHH</td>

<td> 550</td><td> WW0786</td><td> CDLPQTHSLNNRRTLMLMAQMRRISPFSCLKDRHDFEFPQEEFDGNQFQKAQ AISVLHEMMQQTFNLFSTKDSSAAWDETLLEKFYIELFQQMNDLEACVIQEVG VEETPLMNEDSILAVKKYFQRITLYLMEKKYSPCAWEWRAEIMRSLSFSTNL QKRLRRKDHHHHHH</td>

<td> 551</td><td> WW0815</td><td> EAHKSEIAHRYNDLGEQHFKGLVLIAFSQYLQKCSYDEHAKLVQEVTDFAKT CVADESAANCDKSLHTLFGDKLCAIPNLRENYGELADCCTKQEPERNECFLQH KDDNPSLPPFERPEAEAMCTSFKENPTTFMGHYLHEVARRHPYFYAPELLYYA EQYNEILTQCCAEADKESCLTPKLDGVKEKALVSSVRQRMKCSSMQKFGERA FKAWAVARLSQTFPNADFAEITKLATDLTKVNKECCHGDLLECADDRAELAK YMCENQATISSKLQTCCDKPLLKKAHCLSEVEHDTMPADLPAIAADFVEDQE VCKNYAEAKDVFLGTFLYEYSRRHPDYSVSLLLRLAKKYEATLEKCCAEANP PACYGTVLAEFQPLVEEPKNLVKTNCDLYEKLGEYGFQNAILVRYTQKAPQV STPTLVEAARNLGRVGTKCCTLPEDQRLPCVEDYLSAILNRVCLLHEKTPVSE HVTKCCSGSLVERRPCFSALTVDEIYVPKEFKAETFTFHSDICTLPEKEKQIKK QTALAELVKHKPKATAEQLKTVMDDFAQFLDTCCKAADKDTCFSTEGPNLVT RCKDALASGGPALFKSSFPPGSCDLPQTHNLRNKRALTLLVQMRRLSPLSCLK DRKDFGFPQEKVDAQQIKKAQAIPVLSELTQQILNIFTSKDSSAAWNTTLLDSF CNDLHQQLNDLQGCLMQQVGVQEFPLTQEDALLAVRKYFHRITVYLREKKH SPCAWEWRAEVWRALSSSANVLGRLREEKSGGPALFKSSFPPGSEAHKSEIA HRYNDLGEQHFKGLVLIAFSQYLQKCSYDEHAKLVQEVTDFAKTCVADESAA NCDKSLHTLFGDKLCAIPNLRENYGELADCCTKQEPERNECFLQHKDDNPSLP PFERPEAEAMCTSFKENPTTFMGHYLHEVARRHPYFYAPELLYYAEQYNEILT QCCAEADKESCLTPKLDGVKEKALVSSVRQRMKCSSMQKFGERAFKAWAVA RLSQTFPNADFAEITKLATDLTKVNKECCHGDLLECADDRAELAKYMCENQA TISSKLQTCCDKPLLKKAHCLSEVEHDTMPADLPAIAADFVEDQEVCKNYAEA KDVFLGTFLYEYSRRHPDYSVSLLLRLAKKYEATLEKCCAEANPPACYGTVL AEFQPLVEEPKNLVKTNCDLYEKLGEYGFQNAILVRYTQKAPQVSTPTLVEAA RNLGRVGTKCCTLPEDQRLPCVEDYLSAILNRVCLLHEKTPVSEHVTKCCSGS LVERRPCFSALTVDEIYVPKEFKAETFTFHSDICTLPEKEKQIKKQTALAELVK HKPKATAEQLKTVMDDFAQFLDTCCKAADKDTCFSTEGPNLVTRCKDALAH HHHHH</td>

<td> 552</td><td> WW0816</td><td> EAHKSEIAHRYNDLGEQHFKGLVLIAFSQYLQKCSYDEHAKLVQEVTDFAKT CVADESAANCDKSLHTLFGDKLCAIPNLRENYGELADCCTKQEPERNECFLQH KDDNPSLPPFERPEAEAMCTSFKENPTTFMGHYLHEVARRHPYFYAPELLYYA EQYNEILTQCCAEADKESCLTPKLDGVKEKALVSSVRQRMKCSSMQKFGERA FKAWAVARLSQTFPNADFAEITKLATDLTKVNKECCHGDLLECADDRAELAK YMCENQATISSKLQTCCDKPLLKKAHCLSEVEHDTMPADLPAIAADFVEDQE VCKNYAEAKDVFLGTFLYEYSRRHPDYSVSLLLRLAKKYEATLEKCCAEANP PACYGTVLAEFQPLVEEPKNLVKTNCDLYEKLGEYGFQNAILVRYTQKAPQV STPTLVEAARNLGRVGTKCCTLPEDQRLPCVEDYLSAILNRVCLLHEKTPVSE HVTKCCSGSLVERRPCFSALTVDEIYVPKEFKAETFTFHSDICTLPEKEKQIKK QTALAELVKHKPKATAEQLKTVMDDFAQFLDTCCKAADKDTCFSTEGPNLVT RCKDALASGGPALFKSSFPPGSCDLPHIYNLRNKRALKVLAQMRRLTPLSCLK DRKDFGFPLEKVDAQQIQKAQSIPVLRDLTQQILNLFASKDSSAAWNATLLDS FCNDLHQQLNDLQGCLMQQVGVQESPLTQEDSLLAVRIYFHRITVFLREKKHS PCAWEWRAEVWRALSSSANVLGRLREEKASGGPALFKSSFPPGSEAHKSEIA HRYNDLGEQHFKGLVLIAFSQYLQKCSYDEHAKLVQEVTDFAKTCVADESAA NCDKSLHTLFGDKLCAIPNLRENYGELADCCTKQEPERNECFLQHKDDNPSLP PFERPEAEAMCTSFKENPTTFMGHYLHEVARRHPYFYAPELLYYAEQYNEILT QCCAEADKESCLTPKLDGVKEKALVSSVRQRMKCSSMQKFGERAFKAWAVA RLSQTFPNADFAEITKLATDLTKVNKECCHGDLLECADDRAELAKYMCENQA TISSKLQTCCDKPLLKKAHCLSEVEHDTMPADLPAIAADFVEDQEVCKNYAEA KDVFLGTFLYEYSRRHPDYSVSLLLRLAKKYEATLEKCCAEANPPACYGTVL AEFQPLVEEPKNLVKTNCDLYEKLGEYGFQNAILVRYTQKAPQVSTPTLVEAA RNLGRVGTKCCTLPEDQRLPCVEDYLSAILNRVCLLHEKTPVSEHVTKCCSGS LVERRPCFSALTVDEIYVPKEFKAETFTFHSDICTLPEKEKQIKKQTALAELVK HKPKATAEQLKTVMDDFAQFLDTCCKAADKDTCFSTEGPNLVTRCKDALAH HHHHH</td>

<td> 553</td><td> WW0817</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPALFKSSFPPGSCDLPQTHNLRNKRALTLLVQMRRLSPLSC LKDRKDFGFPQEKVDAQQIKKAQAIPVLSELTQQILNIFTSKDSSAAWNTTLLD SFCNDLHQQLNDLQGCLMQQVGVQEFPLTQEDALLAVRKYFHRITVYLREKK</td>

<td></td><td></td><td> HSPCAWEVVRAEVWRALSSSANVLGRLREEKSGGPALFKSSFPPGSEAHKSEI AHRYNDLGEQHFKGLVLIAFSQYLQKCSYDEHAKLVQEVTDFAKTCVADESA ANCDKSLHTLFGDKLCAIPNLRENYGELADCCTKQEPERNECFLQHKDDNPSL PPFERPEAEAMCTSFKENPTTFMGHYLHEVARRHPYFYAPELLYYAEQYNEIL TQCCAEADKESCLTPKLDGVKEKALVSSVRQRMKCSSMQKFGERAFKAWAV ARLSQTFPNADFAEITKLATDLTKVNKECCHGDLLECADDRAELAKYMCENQ ATISSKLQTCCDKPLLKKAHCLSEVEHDTMPADLPAIAADFVEDQEVCKNYAE AKDVFLGTFLYEYSRRHPDYSVSLLLRLAKKYEATLEKCCAEANPPACYGTV LAEFQPLVEEPKNLVKTNCDLYEKLGEYGFQNAILVRYTQKAPQVSTPTLVEA ARNLGRVGTKCCTLPEDQRLPCVEDYLSAILNRVCLLHEKTPVSEHVTKCCSG SLVERRPCFSALTVDETYVPKEFKAETFTFHSDICTLPEKEKQIKKQTALAELV KHKPKATAEQLKTVMDDFAQFLDTCCKAADKDTCFSIEGPNLVTRCKDALA HHHHHH</td>

<td> 554</td><td> WW0818</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPALFKSSFPPGSCDLPHIYNLRNKRALKVLAQMRRLTPLS CLKDRKDFGFPLEKVDAQQIQKAQSIPVLRDLTQQILNLFASKDSSAAWNATL LDSFCNDLHQQLNDLQGCLMQQVGVQESPLTQEDSLLAVRIYFHRITVFLREK KHSPCAWEWRAEVWRALSSSANVLGRLREEKASGGPALFKSSFPPGSEAHK SEIAHRYNDLGEQHFKGLVLIAFSQYLQKCSYDEHAKLVQEVTDFAKTCVAD ESAANCDKSLHTLFGDKLCAIPNLRENYGELADCCTKQEPERNECFLQHKDD NPSLPPFERPEAEAMCTSFKENPTTFMGHYLHEVARRHPYFYAPELLYYAEQY NEILTQCCAEADKESCLTPKLDGVKEKALVSSVRQRMKCSSMQKFGERAFKA WAVARLSQTFPNADFAEITKLATDLTKVNKECCHGDLLECADDRAELAKYM CENQATISSKLQTCCDKPLLKKAHCLSEVEHDTMPADLPAIAADFVEDQEVCK NYAEAKDVFLGTFLYEYSRRHPDYSVSLLLRLAKKYEATLEKCCAEANPPAC YGTVLAEFQPLVEEPKNLVKTNCDLYEKLGEYGFQNAILVRYTQKAPQVSTPT LVEAARNLGRVGTKCCTLPEDQRLPCVEDYLSAILNRVCLLHEKTPVSEHVTK CCSGSLVERRPCFSALTVDETYVPKEFKAETFTFHSDICTLPEKEKQIKKQTAL AELVKHKPKATAEQLKTVMDDFAQFLDTCCKAADKDTCFSIEGPNLVTRCK DALAHHHHHH</td>

<td> 555</td><td> WW0819</td><td> EAHKSEIAHRYNDLGEQHFKGLVLIAFSQYLQKCSYDEHAKLVQEVTDFAKT CVADESAANCDKSLHTLFGDKLCAIPNLRENYGELADCCTKQEPERNECFLQH KDDNPSLPPFERPEAEAMCTSFKENPTTFMGHYLHEVARRHPYFYAPELLYYA EQYNEILTQCCAEADKESCLTPKLDGVKEKALVSSVRQRMKCSSMQKFGERA FKAWAVARLSQTFPNADFAEITKLATDLTKVNKECCHGDLLECADDRAELAK YMCENQATISSKLQTCCDKPLLKKAHCLSEVEHDTMPADLPAIAADFVEDQE VCKNYAEAKDVFLGTFLYEYSRRHPDYSVSLLLRLAKKYEATLEKCCAEANP PACYGTVLAEFQPLVEEPKNLVKTNCDLYEKLGEYGFQNAILVRYTQKAPQV STPTLVEAARNLGRVGTKCCTLPEDQRLPCVEDYLSAILNRVCLLHEKTPVSE HVTKCCSGSLVERRPCFSALTVDETYVPKEFKAETFTFHSDICTLPEKEKQIKK QTALAELVKHKPKATAEQLKTVMDDFAQFLDTCCKAADKDTCFSIEGPNLVT RCKDALASGGPALFKSSFPPGSCDLPQTHNLRNKRALTLLVQMRRLSPLSCLK DRKDFGFPQEKVDAQQIKKAQAIPVLSELTQQILNIFTSKDSSAAWNTTLLDSF CNDLHQQLNDLQGCLMQQVGVQEFPLTQEDALLAVRKYFHRITVYLREKKH SPCAWEWRAEVWRALSSSANVLGRLREEKSGGPALFKSSFPPGSEVQLVESG GGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLY AESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTV SSHHHHHH</td>

<td> 556</td><td> WW0820</td><td> EAHKSEIAHRYNDLGEQHFKGLVLIAFSQYLQKCSYDEHAKLVQEVTDFAKT CVADESAANCDKSLHTLFGDKLCAIPNLRENYGELADCCTKQEPERNECFLQH KDDNPSLPPFERPEAEAMCTSFKENPTTFMGHYLHEVARRHPYFYAPELLYYA EQYNEILTQCCAEADKESCLTPKLDGVKEKALVSSVRQRMKCSSMQKFGERA FKAWAVARLSQTFPNADFAEITKLATDLTKVNKECCHGDLLECADDRAELAK YMCENQATISSKLQTCCDKPLLKKAHCLSEVEHDTMPADLPAIAADFVEDQE VCKNYAEAKDVFLGTFLYEYSRRHPDYSVSLLLRLAKKYEATLEKCCAEANP PACYGTVLAEFQPLVEEPKNLVKTNCDLYEKLGEYGFQNAILVRYTQKAPQV STPTLVEAARNLGRVGTKCCTLPEDQRLPCVEDYLSAILNRVCLLHEKTPVSE HVTKCCSGSLVERRPCFSALTVDETYVPKEFKAETFTFHSDICTLPEKEKQIKK</td>

<td></td><td></td><td> QTALAELVKHKPKATAEQLKTVMDDFAQFLDTCCKAADKDTCFSTEGPNLVT RCKDALASGGPALFKSSFPPGSCDLPHTYNLRNKRALKVLAQMRRLTPLSCLK DRKDFGFPLEKVDAQQIQKAQSIPVLRDLTQQILNLFASKDSSAAWNATLLDS FCNDLHQQLNDLQGCLMQQVGVQESPLTQEDSLLAVRIYFHRITVFLREKKHS PCAWEVVRAEVWRALSSSANVLGRLREEKASGGPALFKSSFPPGSEVQLVESG GGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLY AESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTV SSHHHHHH</td>

<td> 557</td><td> WW0821</td><td> DAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKT CVADESAENCDKSLHTLFGDKLCTVATLREIYGEMADCCAKQEPERNECFLQ HKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFF AKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGER AFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADL AKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKD VCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAAD PHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQV STPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVS DRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIK KQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKL VAASQAALGLSGGPALFKSSFPPGSCDLPQTHSLGSRRTLMLLAQMRRISLFSC LKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDK FYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYS PCAWEWRAEIMRSFSLSTNLQESLRSKESGGPALFKSSFPPGSDAHKSEVAHR FKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENC DKSLHTLFGDKLCTVATLREIYGEMADCCAKQEPERNECFLQHKDDNPNLPR LVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTE CCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVAR LSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSI SSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKD VFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDE FKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRN LGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESL VNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKH KPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL</td>

<td> 558</td><td> WW0822</td><td> DAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKT CVADESAENCDKSLHTLFGDKLCTVATLREIYGEMADCCAKQEPERNECFLQ HKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFF AKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGER AFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADL AKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKD VCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAAD PHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQV STPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVS DRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIK KQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKL VAASQAALGLSGGPALFKSSFPPGSCNLSQTHSLNNRRTLMLMAQMRRISPFS CLKDRHDFEFPQEEFDGNQFQKAQAISVLHEMMQQTFNLFSTKNSSAAWDET LLEKFYIELFQQMNDLEACVIQEVGVEETPLMNEDSILAVKKYFQRITLYLME KKYSPCAWEVVRAEIMRSLSFSTNLQKRLRRKDSGGPALFKSSFPPGSDAHKS EVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADE SAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDN PNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYK AAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKA WAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYIC ENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKN YAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECY AKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTL VEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVT KCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTA</td>

<td></td><td></td><td> LVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAAS QAALGL</td>

<td> 559</td><td> WW0831</td><td> DAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKT CVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQ HKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFF AKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGER AFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADL AKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKD VCKNYAEAKDVFLGMFLYEYARRHPDYSWLLLRLAKTYETTLEKCCAAAD PHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQV STPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSWLNQLCVLHEKTPVS DRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIK KQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKL VAASQAALGLSGGPALFKSSFPPGSCDLPQTHSLGNRRALILLAQMRRISPFSC LKDRHDFEFPQEEFDDKQFQKAQAISVLHEMIQQTFNLFSTKDSSAALDETLL DEFYIELDQQLNDLESCVMQEVGVIESPLMYEDSILAVRKYFQRITLYLIEKKY SSCAWEWRAEIMRSFSLSINLQKRLKSKESGGPALFKSSFPPGSDAHKSEVAH RFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAEN CDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLP RLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFT ECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVA RLSQRFPKAEFAEVSKLVTDLTKVHIECCHGDLLECADDRADLAKYICENQD SISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEA KDVFLGMFLYEYARRHPDYSWLLLRLAKTYETTLEKCCAAADPHECYAKVF DEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVS RNLGKVGSKCCKHPEAKRMPCAEDYLSWLNQLCVLHEKIPVSDRVTKCCTE SLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELV KHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALG L</td>

<td> 560</td><td> WW0832</td><td> DAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKT CVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQ HKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFF AKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGER AFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADL AKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKD VCKNYAEAKDVFLGMFLYEYARRHPDYSWLLLRLAKTYETTLEKCCAAAD PHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQV STPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSWLNQLCVLHEKTPVS DRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIK KQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKL VAASQAALGLSGGPALFKSSFPPGSCDLPQTHSLGNRRALILLAQMGRISHFSC LKDRYDFGFPQEVFDGNQFQKAQAISAFHEMIQQTFNLFSTKDSSAAWDETLL DKFYIELFQQLNDLEACVTQEVGVEEIALMNEDSILAVRKYFQRITLYLMGKK YSPCAWEWRAEIMRSFSFSTNLQKGLRRKDSGGPALFKSSFPPGSDAHKSEV AHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESA ENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPN LPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAA FTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWA VARLSQRFPKAEFAEVSKLVTDLTKVHIECCHGDLLECADDRADLAKYICEN QDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYA EAKDVFLGMFLYEYARRHPDYSWLLLRLAKTYETTLEKCCAAADPHECYAK VFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVE VSRNLGKVGSKCCKHPEAKRMPCAEDYLSWLNQLCVLHEKTPVSDRVTKC CTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALV ELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQA ALGL</td>

<td> 561</td><td> WW0833</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPALFKSSFPPGSCDLPQTHSLGNRRALILLAQMRRISPFSCL</td>

<td></td><td></td><td> KDRHDFEFPQEEFDDKQFQKAQAISVLHEMIQQTFNLFSTKDSSAALDETLLD EFYIELDQQLNDLESCVMQEVGVIESPLMYEDSILAVRKYFQRITLYLIEKKYS SCAWEWRAEIMRSFSLSINLQKRLKSKESGGPALFKSSFPPGSEVQLVESGGG LVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAES VKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS</td>

<td> 562</td><td> WW0834</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPALFKSSFPPGSCDLPQTHSLGNRRALILLAQMGRISHFSCL KDRYDFGFPQEVFDGNQFQKAQAISAFHEMIQQTFNLFSTKDSSAAWDETLLD KFYIELFQQLNDLEACVTQEVGVEEIALMNEDSILAVRKYFQRITLYLMGKKY SPCAWEWRAEIMRSFSFSTNLQKGLRRKDSGGPALFKSSFPPGSEVQLVESGG GLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS</td>

<td> 563</td><td> WW0737</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPGPAGLYAQPGSINYKQLQLQERTNIRKCQELLEQLNGKIN LTYRADFKIPMEMTEKMQKSYTAFAIQEMLQNVFLVFRNNFSSTGWNETIW RLLDELHQQTVFLKTVLEEKQEERLTWEMSSTALHLKSYYWRVQRYLKLMK YNSYAWMWRAEIFRNFLIIRRLTRNFQNSGGPGPAGLYAQPGSEVQLVESGG GLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS</td>

<td> 564</td><td> WW0738</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPALFKSSFPPGSINYKQLQLQERTNIRKCQELLEQLNGKINL TYRADFKIPMEMTEKMQKSYTAFAIQEMLQNVFLVFRNNFSSTGWNETIWR LLDELHQQTVFLKTVLEEKQEERLTWEMSSTALHLKSYYWRVQRYLKLMKY NSYAWMVVRAEIFRNFLIIRRLTRNFQNSGGPALFKSSFPPGSEVQLVESGGGL VQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESV KGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS</td>

<td> 565</td><td> WW0739</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPGPAGLYAQPGSINYKQLQLQERTNIRKSQELLEQLNGKIN LTYRADFKIPMEMTEKMQKSYTAFAIQEMLQNVFLVFRNNFSSTGWNETIW RLLDELHQQTVFLKTVLEEKQEERLTWEMSSTALHLKSYYWRVQRYLKLMK YNSYAWMWRAEIFRNFLIIRRLTRNFQNSGGPGPAGLYAQPGSEVQLVESGG GLVQPGNSLRLSCAASGFIESKFGMSWVRQAPGKGLEWVSSISGSGRDTLYA ESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS</td>

<td> 566</td><td> WW0740</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPALFKSSFPPGSINYKQLQLQERTNIRKSQELLEQLNGKINL TYRADFKIPMEMTEKMQKSYTAFAIQEMLQNVFLVFRNNFSSTGWNETIWR LLDELHQQTVFLKTVLEEKQEERLTWEMSSTALHLKSYYWRVQRYLKLMKY NSYAWMVVRAEIFRNFLIIRRLTRNFQNSGGPALFKSSFPPGSEVQLVESGGGL VQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESV KGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSS</td>

<td> 567</td><td> WW0741</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPGPAGLYAQPGSMSYNLLGFLQRSSNFQCQKLLWQLNGR LEYCLKDRMNFDIPEEIKQLQQFQKEDAALTIYEMLQNIFAIFRQDSSSTGWNE TIVENLLANVYHQINHLKTVLEEKLEKEDFIRGKLMSSLHLKRYYGRILHYLK AKEYSHCAWTIVRVEILRNFYFINRLTGYLRNSGGPGPAGLYAQPGSEVQLVE SGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTL YAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVT VSS</td>

<td> 568</td><td> WW0742</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPALFKSSFPPGSMSYNLLGFLQRSSNFQCQKLLWQLNGRL EYCLKDRMNFDIPEEIKQLQQFQKEDAALTIYEMLQNIFAIFRQDSSSTGWNET</td>

<td></td><td></td><td> IVENLLANVYHQINHLKTVLEEKLEKEDFTRGKLMSSLHLKRYYGRILHYLKA KEYSHCAWTIVRVEILRNFYFINRLTGYLRNSGGPALFKSSFPPGSEVQLVESG GGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLY AESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTV SS</td>

<td> 569</td><td> WW0743</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPGPAGLYAQPGSMSYNLLGFLQRSSNFQSQKLLWQLNGR LEYCLKDRMNFDIPEEIKQLQQFQKEDAALTIYEMLQNIFAIFRQDSSSTGWNE TIVENLLANVYHQINHLKTVLEEKLEKEDFTRGKLMSSLHLKRYYGRILHYLK AKEYSHCAWTIVRVEILRNFYFINRLTGYLRNSGGPGPAGLYAQPGSEVQLVE SGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTL YAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVT VSS</td>

<td> 570</td><td> WW0744</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPALFKSSFPPGSMSYNLLGFLQRSSNFQSQKLLWQLNGRL EYCLKDRMNFDIPEEIKQLQQFQKEDAALTIYEMLQNIFAIFRQDSSSTGWNET IVENLLANVYHQINHLKTVLEEKLEKEDFTRGKLMSSLHLKRYYGRILHYLKA KEYSHCAWTIVRVEILRNFYFINRLTGYLRNSGGPALFKSSFPPGSEVQLVESG GGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLY AESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTV SS</td>

<td> 571</td><td> WW0745</td><td> INYKQLQLQERTNIRKCQELLEQLNGKINLIYRADFKIPMEMTEKMQKSYTAF AIQEMLQNVFLVFRNNFSSTGWNETIWRLLDELHQQTVFLKTVLEEKQEERL TWEMSSTALHLKSYYWRVQRYLKLMKYNSYAWMWRAEIFRNFLIIRRLTR NFQNHHHHHH</td>

<td> 572</td><td> WW0746</td><td> INYKQLQLQERTNIRKSQELLEQLNGKINLTYRADFKIPMEMTEKMQKSYTAF AIQEMLQNVFLVFRNNFSSTGWNETIWRLLDELHQQTVFLKTVLEEKQEERL TWEMSSTALHLKSYYWRVQRYLKLMKYNSYAWMWRAEIFRNFLIIRRLTR NFQNHHHHHH</td>

<td> 573</td><td> WW0747</td><td> MSYNLLGFLQRSSNFQCQKLLWQLNGRLEYCLKDRMNFDIPEEIKQLQQFQK EDAALTIYEMLQNIFAIFRQDSSSTGWNETIVENLLANVYHQINHLKTVLEEKL EKEDFTRGKLMSSLHLKRYYGRILHYLKAKEYSHCAWTIVRVEILRNFYFINR LTGYLRNHHHHHH</td>

<td> 574</td><td> WW0748</td><td> MSYNLLGFLQRSSNFQSQKLLWQLNGRLEYCLKDRMNFDIPEEIKQLQQFQKE DAALTIYEMLQNIFAIFRQDSSSTGWNETIVENLLANVYHQINHLKTVLEEKLE KEDFTRGKLMSSLHLKRYYGRILHYLKAKEYSHCAWTIVRVEILRNFYFINRL TGYLRNHHHHHH</td>

<td> 575</td><td> WW0787</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPGPAGLYAQPGSMSYNLLGFLQRSSNFQCQKLLWQLNGR LEYCLKDRMNFDIPEEIKQLQQFQKEDAALTIYEMLQNIFAIFRQDSSSTGWQE TIVENLLANVYHQINHLKTVLEEKLEKEDFTRGKLMSSLHLKRYYGRILHYLK AKEYSHCAWTIVRVEILRNFYFINRLTGYLRNSGGPGPAGLYAQPGSEVQLVE SGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTL YAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVT VSS</td>

<td> 576</td><td> WW0788</td><td> EVQLVESGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSIS GSGRDTLYAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVS SQGTLVTVSSSGGPGPAGLYAQPGSMSYNLLGFLQRSSNFQSQKLLWQLNGR LEYCLKDRMNFDIPEEIKQLQQFQKEDAALTIYEMLQNIFAIFRQDSSSTGWQE TIVENLLANVYHQINHLKTVLEEKLEKEDFTRGKLMSSLHLKRYYGRILHYLK AKEYSHCAWTIVRVEILRNFYFINRLTGYLRNSGGPGPAGLYAQPGSEVQLVE SGGGLVQPGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTL YAESVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVT VSS</td>

<td> 577</td><td> WW0789</td><td> MSYNLLGFLQRSSNFQCQKLLWQLNGRLEYCLKDRMNFDIPEEIKQLQQFQK EDAALTIYEMLQNIFAIFRQDSSSTGWQETIVENLLANVYHQINHLKTVLEEKL EKEDFTRGKLMSSLHLKRYYGRILHYLKAKEYSHCAWTIVRVEILRNFYFINR LTGYLRNHHHHHH</td>

<td> 578</td><td> WW0790</td><td> MSYNLLGFLQRSSNFQSQKLLWQLNGRLEYCLKDRMNFDIPEEIKQLQQFQKE DAALTIYEMLQNIFAIFRQDSSSTGWQETIVENLLANVYHQINHLKTVLEEKLE KEDFTRGKLMSSLHLKRYYGRILHYLKAKEYSHCAWTIVRVEILRNFYFINRL TGYLRNHHHHHH</td>

<td> 579</td><td> WW0729</td><td> APTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLIFKFYMPKKATEL KHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEY ADETATIVEFLNRWITFCQSIISTLTSGGPGGGGSGGGPGSEVQLVESGGGLVQ PGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKG RFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSGGGGS GGGGSGGGGSGGGGSGGGGSGGGGSSGGPGGGGSGGGPGSEVQLVESGGGL VQPGGSLRLSCAASGFIFSSYTLAWVRQAPGKGLEWVAAIDSSSYIYSPDTVR GRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTV SSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVH TFPAVLQSSGLYSLSSWTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSC</td>

<td> 580</td><td> WW0734</td><td> APTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLIFKFYMPKKATEL KHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEY ADETATIVEFLNRWITFCQSIISTLTSGGPGPAGMKGLPGSEVQLVESGGGLVQ PGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKG RFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSGGGGS GGGGSGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSEVQLVESGGGL VQPGGSLRLSCAASGFIFSSYTLAWVRQAPGKGLEWVAAIDSSSYIYSPDTVR GRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTV SSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVH TFPAVLQSSGLYSLSSWTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSC</td>

<td> 581</td><td> WW0735</td><td> APTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATEL KHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEY ADETATIVEFLNRWITFCQSIISTLTSGGPGPAGLYAQPGSEVQLVESGGGLVQP GNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKG RFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSGGGGS GGGGSGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSEVQLVESGGGL VQPGGSLRLSCAASGFIFSSYTLAWVRQAPGKGLEWVAAIDSSSYIYSPDTVR GRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTV SSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVH TFPAVLQSSGLYSLSSWTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSC</td>

<td> 582</td><td> WW0736</td><td> APTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLIFKFYMPKKATEL KHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEY ADETATIVEFLNRWITFCQSIISTLTSGGPALFKSSFPPGSEVQLVESGGGLVQP GNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKG RFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSGGGGS GGGGSGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSEVQLVESGGGL VQPGGSLRLSCAASGFIFSSYTLAWVRQAPGKGLEWVAAIDSSSYIYSPDTVR GRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDALDYWGQGTTVTV SSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVH TFPAVLQSSGLYSLSSWTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSC</td>

<td> 583</td><td> WW0792</td><td> EVQLVESGGGLVQPGGSLRLSCAASGFIFSSYTLAWVRQAPGKGLEWVAAID SSSYTYSPDTVRGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDSNWDAL DYWGQGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVS</td>

<td></td><td></td><td> WNSGALTSGVHTFPAVLQSSGLYSLSSWTVPSSSLGTQTYICNVNHKPSNTK VDKRVEPKSCHHHHHH</td>

<td> 584</td><td> WW0061</td><td> APTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATEL KHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEY ADETATIVEFLNRWITFCQSIISTLTSGGPGPAGMKGLPGSEVQLVESGGGLVQ PGNSLRLSCAASGFTFSKFGMSWVRQAPGKGLEWVSSISGSGRDTLYAESVKG RFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSVSSQGTLVTVSSHHHH HH</td>

<td> 585</td><td> ACP293 (WW0237)</td><td> QVQLQESGGGLVQTGGSLRLSCTTSGTIFSGYTMGWYRQAPGEQRELVAVISG GGDTNYADSVKGRFTISRDNTKDTMYLQMNSLKPEDTAVYYCYSREVTPPW KLYWGQGTQVTVSSAAAYPYDVPDYGSHHHHHH</td>

<td> 586</td><td> ACP294 (WW0238)</td><td> QVQLQESGGGLVQEGGSLRLSCAASERIFSTDVMGWYRQAAEKQRELVAWS ARGTTNYLDAVKGRFTISRDNARNTLTLQMNDLKPEDTASYYCYVRETTSPW RIYWGQGTQVTVSSAAAYPYDVPDYGSHHHHHH</td>

<td> 587</td><td> ACP295 (WW0239)</td><td> QVQLQESGGGLVQAGGSLRLSCAASGSIFSANAMGWYRQAPGKQRELVAVIS SGGSTNYADSVKGRFTISRDNAKNTVYLQMNSLKPEDTAVYYCMYSGSYYY TPNDYWGQGTQVTVSSAAAYPYDVPDYGSHHHHHH</td>

<td> 588</td><td> ACP315 (WW0368)</td><td> EVQLLESGGGLVQPGGSLRLSCAASGSIFSANAMGWYRQAPGKQRELVAVISS GGSTNYADSVKGRFTISRDNSKNTVYLQMNSLRAEDTAVYYCMYSGSYYYTP NDYWGQGTLVTVSSAAAYPYDVPDYGSHHHHHH</td>

<td> 589</td><td> ACP316 (WW0369)</td><td> EVQLLESGGGLVQPGGSLRLSCAASGSIFSANAMGWYRQAPGKGLELVAVISS GGSTNYADSVKGRFTISRDNSKNTVYLQMNSLRAEDTAVYYCMYSGSYYYTP NDYWGQGTLVTVSSAAAYPYDVPDYGSHHHHHH</td>

<td> 590</td><td> ACP317 (WW0370)</td><td> EVQLLESGGGLVQPGGSLRLSCAASGSIFSANAMGWVRQAPGKGLEWVSVIS SGGSTNYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCMYSGSYYYT PNDYWGQGTLVTVSSAAAYPYDVPDYGSHHHHHH</td>

<td> 591</td><td> ACP318 (WW0371)</td><td> QVQLLESGGGLVQPGGSLRLSCAASGSIFSANAMGWYRQAPGKQRELVAVIS SGGSTNYADSVKGRFTISRDNSKNTVYLQMNSLRAEDTAVYYCMYSGSYYYT PNDYWGQGTLVTVSSAAAYPYDVPDYGSHHHHHH</td>

<td> 592</td><td> ACP319 (WW0372)</td><td> EVQLLESGGGLVQPGGSLRLSCAASGSIFSANAMGWYRQAPGKGRELVAVISS GGSTNYADSVKGRFTISRDNSKNTVYLQMNSLRAEDTAVYYCMYSGSYYYTP NDYWGQGTLVTVSSAAAYPYDVPDYGSHHHHHH</td>

<td> 593</td><td> ACP320 (WW0373)</td><td> QVQLLESGGGLVQAGGSLRLSCAASGSIFSANAMGWYRQAPGKQRELVAVIS SGGSTNYADSVKGRFTISRDNSKNTVYLQMNSLRAEDTAVYYCMYSGSYYYT PNDYWGQGTLVTVSSAAAYPYDVPDYGSHHHHHH</td>

<td> 594</td><td> ACP321 (WW0374)</td><td> EVQLLESGGGLVQPGGSLRLSCAASERIFSTDVMGWYRQAPGKQRELVAWS ARGTTNYLDAVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCYVRETTSPW RIYWGQGTLVTVSSAAAYPYDVPDYGSHHHHHH</td>

<td> 595</td><td> ACP322 (WW0375)</td><td> EVQLLESGGGLVQPGGSLRLSCAASERIFSTDVMGWYRQAPGKGLELVAVVS ARGTTNYLDAVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCYVRETTSPW RIYWGQGTLVTVSSAAAYPYDVPDYGSHHHHHH</td>

<td> 596</td><td> ACP323 (WW0376)</td><td> EVQLLESGGGLVQPGGSLRLSCAASERIFSTDVMGWVRQAPGKGLEWVSWS ARGTTNYLDAVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCYVRETTSPW RIYWGQGTLVTVSSAAAYPYDVPDYGSHHHHHH</td>

<td> 597</td><td> ACP324 (WW0377)</td><td> QVQLLESGGGLVQPGGSLRLSCAASERIFSTDVMGWYRQAPGKQRELVAWS ARGTTNYLDAVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCYVRETTSPW RIYWGQGTLVTVSSAAAYPYDVPDYGSHHHHHH</td>

<td> 598</td><td> ACP325 (WW0378)</td><td> EVQLLESGGGLVQPGGSLRLSCAASERIFSTDVMGWYRQAPGKGRELVAWS ARGTTNYLDSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCYVRETTSPW RIYWGQGTLVTVSSAAAYPYDVPDYGSHHHHHH</td>

<td> 599</td><td> ACP326 (WW0379)</td><td> QVQLLESGGGLVQEGGSLRLSCAASERIFSTDVMGWYRQAAGKQRELVAWS ARGTTNYLDAVKGRFTISRDNSKNTLYLQMNSLRAEDTASYYCYVRETTSPW RIYWGQGTLVTVSSAAAYPYDVPDYGSHHHHHH</td>

<td> 600</td><td> ACP327 (WW0380)</td><td> EVQLLESGGGLVQPGGSLRLSCAASERIFSTDVMGWYRQAPGKGLELVAVVS ARGTTNYLDSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCYVRETTSPW RIYWGQGTLVTVSSAAAYPYDVPDYGSHHHHHH</td>

<td> 601</td><td> ACP328 (WW0381)</td><td> EVQLLESGGGLVQPGGSLRLSCATSGTIFSGYTMGWYRQAPGKQRELVAVISG GGDTNYADSVKGRFTISRDNSKDTMYLQMNSLRAEDTAVYYCYSREVTPPW KLYWGQGTLVTVSSAAAYPYDVPDYGSHHHHHH</td>

<td> 602</td><td> ACP329 (WW0382)</td><td> EVQLLESGGGLVQPGGSLRLSCATSGTIFSGYTMGWYRQAPGKGLELVAVISG GGDTNYADSVKGRFTISRDNSKDTMYLQMNSLRAEDTAVYYCYSREVTPPW KLYWGQGTLVTVSSAAAYPYDVPDYGSHHHHHH</td>

<td> 603</td><td> ACP330 (WW0383)</td><td> EVQLLESGGGLVQPGGSLRLSCAASGTIFSGYIMGWVRQAPGKGLEWVSVIS GGGDTNYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCYSREVTPPW KLYWGQGTLVTVSSAAAYPYDVPDYGSHHHHHH</td>

<td> 604</td><td> ACP331 (WW0384)</td><td> QVQLLESGGGLVQPGGSLRLSCATSGTIFSGYIMGWYRQAPGKQRELVAVIS GGGDTNYADSVKGRFTISRDNSKDTMYLQMNSLRAEDTAVYYCYSREVTPP WKLYWGQGTLVTVSSAAAYPYDVPDYGSHHHHHH</td>

<td> 605</td><td> ACP332 (WW0385)</td><td> EVQLLESGGGLVQPGGSLRLSCATSGTIFSGYTMGWYRQAPGKQRELVAVISG GGDTNYADSVKGRFTISRDNSKNTMYLQMNSLRAEDTAVYYCYSREVTPPW KLYWGQGTLVTVSSAAAYPYDVPDYGSHHHHHH</td>

<td> 606</td><td> ACP333 (WW0386)</td><td> EVQLLESGGGLVQPGGSLRLSCATSGTIFSGYTMGWYRQAPGKGRELVAVISG GGDTNYADSVKGRFTISRDNSKNTMYLQMNSLRAEDTAVYYCYSREVTPPW KLYWGQGTLVTVSSAAAYPYDVPDYGSHHHHHH</td>

<td> 607</td><td> ACP334 (WW0387)</td><td> QVQLLESGGGLVQTGGSLRLSCATSGTIFSGYTMGWYRQAPGKQRELVAVIS GGGDTNYADSVKGRFTISRDNSKDTMYLQMNSLRAEDTAVYYCYSREVTPP WKLYWGQGTLVTVSSAAAYPYDVPDYGSHHHHHH</td>

<td> 608</td><td> ACP335 (WW0388_</td><td> EVQLLESGGGLVQPGGSLRLSCATSGTIFSGYTMGWYRQAPGKGLELVAVISG GGDTNYADSVKGRFTISRDNSKNTMYLQMNSLRAEDTAVYYCYSREVTPPW KLYWGQGTLVTVSSAAAYPYDVPDYGSHHHHHH</td>

<td> 609</td><td> MMP141</td><td> GPAGLYAQ</td>

<td> 610</td><td> MMP91</td><td> GPAGMKGL</td>

<td> 611</td><td> FAPa 1</td><td> PGGPAGIG</td>

<td> 612</td><td> CTSL1 1</td><td> ALFKSSFP</td>

<td> 613</td><td> CTSL12</td><td> ALFFSSPP</td>

<td> 614</td><td> ADAMI 7 1</td><td> LAQRLRSS</td>

<td> 615</td><td> ADAMI 7 2</td><td> LAQKLKSS</td>

<td> 616</td><td> ALU30-1</td><td> GALFKSSFPSGGGPAGLYAQGGSGKGGSGK</td>

<td> 617</td><td> ALU30-2</td><td> RGSGGGPAGLYAQGSGGGPAGLYAQGGSGK</td>

<td> 618</td><td> ALU30-3</td><td> KGGGPAGLYAQGPAGLYAQGPAGLYAQGSR</td>

<td> 619</td><td> ALU30-4</td><td> RGGPAGLYAQGGPAGLYAQGGGPAGLYAQK</td>

<td> 620</td><td> ALU30-5</td><td> KGGALFKSSFPGGPAGIGPLAQKLKSSGGS</td>

<td> 621</td><td> ALU30-6</td><td> SGGPGGPAGIGALFKSSFPLAQKLKSSGGG</td>

<td> 622</td><td> ALU30-7</td><td> RGPLAQKLKSSALFKSSFPGGPAGIGGGGK</td>

<td> 623</td><td> ALU30-8</td><td> GGGALFKSSFPLAQKLKSSPGGPAGIGGGR</td>

<td> 624</td><td> ALU30-9</td><td> RGPGGPAGIGPLAQKLKSSALFKSSFPGGG</td>

<td> 625</td><td> ALU30-10</td><td> RGGPLAQKLKSSPGGPAGIGALFKSSFPGK</td>

<td> 626</td><td> ALU30-11</td><td> RSGGPAGLYAQALFKSSFPLAQKLKSSGGG</td>

<td> 627</td><td> ALU30-12</td><td> GGPLAQKLKSSALFKSSFPGPAGLYAQGGR</td>

<td> 628</td><td> ALU30-13</td><td> GGALFKSSFPGPAGLYAQPLAQKLKSSGGK</td>

<td> 629</td><td> ALU30-14</td><td> RGGALFKSSFPLAQKLKSSGPAGLYAQGGK</td>

<td> 630</td><td> ALU30-15</td><td> rgggpaglyaqplaqklkssalfkssfpgg</td>

<td> 631</td><td> ALU30-16</td><td> sgplaqklkssgpaglyaqalfkssfpgsk</td>

<td> 632</td><td> ALU30-17</td><td> kggpggpagigplaqrlrssalfkssfpgr</td>

<td> 633</td><td> ALU30-18</td><td> ksgpggpagigalffsspplaqklkssggr</td>

<td> 634</td><td> ALU30-19</td><td> sggfprsggsfnprtfgskrkrrgsrgggg</td>

INCORPORATION BY REFERENCE

[363] The entire disclosures of all patent and non-patent publications cited herein are each incorporated by reference in their entireties for all purposes.

OTHER EMBODIMENTS

[364] The disclosure set forth above may encompass multiple distinct inventions with independent utility. Although each of these inventions has been disclosed in its preferred form(s), the specific embodiments thereof as disclosed and illustrated herein are not to be considered in a limiting sense, because numerous variations are possible. The subject matter of the inventions includes all novel and nonobvious combinations and subcombinations of the various elements, features, functions, and/or properties disclosed herein. The following claims particularly point out certain combinations and subcombinations regarded as novel and nonobvious. Inventions embodied in other combinations and subcombinations of features, functions, elements, and/or properties may be claimed in this application, in applications claiming priority from this application, or in related applications. Such claims, whether directed to a different invention or to the same invention, and whether broader, narrower, equal, or different in scope in comparison to the original claims, also are regarded as included within the subject matter of the inventions of the present disclosure.