DETAILED ACTION The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA. Applicant’s preliminary amendments received May 10, 2023 are acknowledged. Claims 5, 6, 8-11, 23, and 31 have been amended. Claims 1-31 are pending in the instant application. Information Disclosure Statement The IDS forms received 9/17/2024, 7/30/2025, and 11/7/2025 are acknowledged and the references cited therein have been considered. Claim Rejections - 35 USC § 103 In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis ( i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status. The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action: A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made. This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention. Claim s 1- 5 are rejected under 35 U.S.C. 103 as being unpatentable over Hust et al. in view of Xiong et al. (WO 2020/185533) . Hust et al. disclose single chain Fab ( scFab ) fragments wherein the C terminal end of the light chain is joined to the N terminus of the VH-CH1 fragment via a peptide linker (see entire document, particularly the abstract and Figure 1). They tested multiple linkers ranging between 32-36 amino acids in length and found them to be equivalent in terms of their impact on antigen binding activity (see particularly pages 5 and 6 of 15). Note that such a length was chosen based upon X ray crystallographic data of a Fab fragment so as to cover the space between the C terminus of the LC and the beginning of the VH-CH1 without introducing steric strain or disruptions (see particularly the first full paragraph of the right column of page 2 or 15). These teachings differ from the instant claimed invention in that Hust et al. did not use (GGGGQ) 7 (i.e. SEQ ID NO:1) as the linker sequence when making scFab . Xiong et al. disclose that (GGGGQ)n, wherein N is 7, is a linker sequence that can be used in making recombinant fusion proteins (see entire document, particularly page 9). Therefore, it would have been obvious to ordinary artisans that the 35 amino acid residues of the linker of SEQ ID NO:1 (i.e. (GGGGQ) 7 ) could be used in place of the linkers in the scFab constructs of Hust et al. This is because Hust observed no statistically significant difference when using various linker sequences in the range or 32-36 residues in their scFab constructs and the length of SEQ ID NO:1 is within this range. Applicant is reminded that as per MPEP 2144.06, a n express suggestion to substitute one equivalent component or process for another is not necessary to render such substitution obvious. In re Fout , 675 F.2d 297, 213 USPQ 532 (CCPA 1982). Claim s 1- 7 are rejected under 35 U.S.C. 103 as being unpatentable over Schirrman et al. in view of Xiong et al. (WO 2020/185533) . Schirrman et al. disclose single chain immunoglobulins ( scIg ) wherein a linker peptide is present connecting the C terminus of the light chain to the amino terminus of the heavy chain, effectively making a molecule wherein a scFab is joined to a human IgG1 hinge-CH2-CH3 constant domain (see entire document, particularly the abstract and Figure 1, most particularly Figure 1A, and note that instant SEQ ID NO:5 is human IgG1). It is disclosed that such scIgG are to be used to make bispecific antibodies (see particularly the left column of page 75). These teachings differ from the instant claimed invention in that Schirrman et al. did not use (GGGGQ) 7 (i.e. SEQ ID NO:1) as the linker sequence when making the scFab for use in their single chain antibody. Xiong et al. disclose that (GGGGQ)n, wherein N is 7, is a linker sequence that can be used in making recombinant fusion proteins (see entire document, particularly page 9). Therefore, it would have been obvious to ordinary artisans that the 35 amino acid residues of the linker of SEQ ID NO:1 (i.e. (GGGGQ) 7 ) could be used in place of the linker in the scFab constructs of Schirrman et al. This is because both sequences are taught as successfully being used as linker sequences when making fusion proteins (i.e. making a continuous polypeptide sequences out of what otherwise would be discontinuous sequences). Applicant is reminded that as per MPEP 2144.06, a n express suggestion to substitute one equivalent component or process for another is not necessary to render such substitution obvious. In re Fout , 675 F.2d 297, 213 USPQ 532 (CCPA 1982). Claim s 1- 9 and 12 are rejected under 35 U.S.C. 103 as being unpatentable over WO 2011/117330 in view of Xiong et al. (WO 2020/185533) . The ‘330 WIPO publication discloses bispecific antibodies wherein the C terminus of a light chain is joined to the amino terminus of a heavy chain via a linker, effectively making a single chain immunoglobulin ( scIg ) wherein a scFab is joined to a human IgG1 hinge-CH2-CH3 constant domain (see entire document, particularly the title, abstract, Figures 1-4, and page 8, and note that instant SEQ ID NO:5 is human IgG1 while instant SEQ ID NOs:2 and 3 are human kappa and lambda respectively) . The linkers are disclosed as being between 32-50 amino acids in length and include G 4 S repeated 3, 4, and 5 times which are instant SEQ ID NOs:14, 16, and 18 respectively (ibid) . The ‘33 0 publication further discloses knobs in holes technology to control preferential pairings of Fc domains in the disclosed multispecific antibodies including R409D and D399K (see particularly page 11 ). These teachings differ from the instant claimed invention in that the ‘330 publication does not disclose (GGGGQ) 7 (i.e. SEQ ID NO:1) as the linker sequence when making the scFab and in that while one side of the bispecific antibody is a scIg , the other side is a conventional antibody half molecule made up of an heavy and light chain joined via disulfide bonds. Xiong et al. disclose that (GGGGQ)n, wherein N is 7, is a linker sequence that can be used in making recombinant fusion proteins (see entire document, particularly page 9). They also disclose the use of K392D, K409D mutations in one Fc and complementary E356K, D399K in a second Fc to control Fc paining when making fusion proteins comprising Fc domains (see particularly page 11). Therefore, it would have been obvious to ordinary artisans that the 35 amino acid residues of the linker of SEQ ID NO:1 (i.e. (GGGGQ) 7 ) could be used in place of the linker in the scFab constructs of the ‘330 publication . This is because both sequences are taught as successfully being used as linker sequences when making fusion proteins (i.e. making a continuous polypeptide sequences out of what otherwise would be discontinuous sequences). Applicant is reminded that as per MPEP 2144.06, a n express suggestion to substitute one equivalent component or process for another is not necessary to render such substitution obvious. In re Fout , 675 F.2d 297, 213 USPQ 532 (CCPA 1982). Further, while the bispecifics disclosed by the ‘330 document are not disclosed as comprising two different scIg , it would have bene obvious to use such a format rather than the one side scIg one side conventional that is disclosed since a) a scIg ensures proper pairing between the heavy and light chains such that a proper antigen binding domain is always formed and b) techniques to ensure heterodimerization of Fc, such as knobs-in-holes are disclosed by both the ‘330 document and Xiong et al. are disclosed such that a bispecific constructs will be strongly favored to form. Claim s 1- 5, 8, 9, 24 , and 31 are rejected under 35 U.S.C. 103 as being unpatentable over US 2010/0256338 in view of Xiong et al. (WO 2020/185533) . The ‘338 publication disclose s recombinantly produced multispecific antibodies comprising single chain Fab fragments (see entire document, particularly the title, abstract, claims, and Figures 2-7). Notably, it disclose s that the scFab are to be created by joining the C terminal end of the LC to the N terminal of the VH-CH1 fragment (see particularly Figure 2 as well as paragraphs [0028-0029]). Such linkers are disclosed as being between 32-50 amino acids in length (see particularly paragraph s [0028] and [0035]) . The scFab are disclosed as being fused to the C terminal end of an full length antibody heavy chain wherein the full length heavy chain associated with a light chain (see particularly paragraphs [0045-0047] and Figures 3-7). Disclosed linker sequences include G 4 S repeated 3, 4, and 5 times which are instant SEQ ID NOs:14, 16, and 18 respectively. The ‘338 publication further discloses knobs in holes technology to control preferential pairings of Fc domains in the disclosed multispecific antibodies including R409D, D399 K, ( see particularly paragraphs [0063- 0071] and Figures 6 and 7). The Fc domains of such multispecific constructs are disclosed as being human IgG1 (see particularly paragraphs [0079-0082] as well as the working examples, and note that instant SEQ ID NO:5 is human IgG1) while the light chains are human kappa or lambda sequences ( ibid, and note that instant SEQ ID NOs:2 and 3 are kappa and lambda respectively) . These teachings differ from the instant claimed invention in that Schirrman et al. did not use (GGGGQ) 7 (i.e. SEQ ID NO:1) as the linker sequence when making the scFab for use in their single chain antibody. Xiong et al. disclose that (GGGGQ)n, wherein N is 7, is a linker sequence that can be used in making recombinant fusion proteins (see entire document, particularly page 9). They also disclose the use of K392D, K409D mutations in one Fc and complementary E356K, D399K in a second Fc to control Fc paining when making fusion proteins comprising Fc domains (see particularly page 11). Therefore, it would have been obvious to ordinary artisans that the 35 amino acid residues of the linker of SEQ ID NO:1 (i.e. (GGGGQ) 7 ) could be used in place of the linker in the scFab constructs of the ‘338 publication . This is because both sequences are taught as successfully being used as linker sequences when making fusion proteins (i.e. making a continuous polypeptide sequences out of what otherwise would be discontinuous sequences). Applicant is reminded that as per MPEP 2144.06, a n express suggestion to substitute one equivalent component or process for another is not necessary to render such substitution obvious. In re Fout , 675 F.2d 297, 213 USPQ 532 (CCPA 1982). Claim s 1-9, 12, 16 , 23 , 24, and 31 are rejected under 35 U.S.C. 103 as being unpatentable over Brinkmann et al. (WO 2011/117330) in view of US 2010/0256338 in view of Xiong et al. (WO 2020/185533) . Brinkmann et al. disclose bispecific antibodies comprising a single chain Ig, which is a molecule wherein the C terminus of the light chain is joined via a linker to the amino terminus of the antibody heavy chain via a polypeptide linker (see entire document, particularly the title, abstract, claims, and Figures 1-4). In other words, the molecules of Brinkmann et al. comprise a scFab joined to a hinge-CH2-CH3 (as can be clearly seen graphically in Figure 2). Notably the peptide linkers joining the LC to the amin terminus of the HC are disclosed as having a length of between 32-50 residues including the linker (G4S) 7 (see particularly the paragraph spanning pages 8 and 9). The use of knobs in holes technology to favor heterodimerization of Fc domains, and hence formation of bispecific rather than monospecific antibodies, is also disclosed (see particularly pages 9-12). These teachings differ from the instant claimed invention in that Brinkmann et al. do not disclose (GGGGQ) 7 (i.e. SEQ ID NO:1) as the linker sequence when making the scFab in their single chain antibody, nor do they disclose adding additional Fab antigen binding domains to the C terminus of the antibody heavy chain (whether scFab or conventional ) . The ‘338 publication discloses recombinantly produced multispecific antibodies comprising single chain Fab fragments (see entire document, particularly the title, abstract, claims, and Figures 2-7). Notably, it discloses that the scFab are to be created by joining the C terminal end of the LC to the N terminal of the VH-CH1 fragment (see particularly Figure 2 as well as paragraphs [0028-0029]). Such linkers are disclosed as being between 32-50 amino acids in length (see particularly paragraphs [0028] and [0035]). The scFab are disclosed as being fused to the C terminal end of an full length antibody heavy chain wherein the full length heavy chain associated with a light chain (see particularly paragraphs [0045-0047] and Figures 3-7). Disclosed linker sequences include G 4 S repeated 3, 4, and 5 times which are instant SEQ ID NOs:14, 16, and 18 respectively. The ‘338 publication further discloses knobs in holes technology to control preferential pairings of Fc domains in the disclosed multispecific antibodies including R409D, D399 K, ( see particularly paragraphs [0063-0071] and Figures 6 and 7). The Fc domains of such multispecific constructs are disclosed as being human IgG1 (see particularly paragraphs [0079-0082] as well as the working examples, and note that instant SEQ ID NO:5 is human IgG1) while the light chains are human kappa or lambda sequences ( ibid, and note that instant SEQ ID NOs:2 and 3 are kappa and lambda respectively). These teachings differ from the instant claimed invention in that Schirrman et al. did not use (GGGGQ) 7 (i.e. SEQ ID NO:1) as the linker sequence when making the scFab for use in their single chain antibody. Xiong et al. disclose that (GGGGQ)n, wherein N is 7, is a linker sequence that can be used in making recombinant fusion proteins (see entire document, particularly page 9). They also disclose the use of K392D, K409D mutations in one Fc and complementary E356K, D399K in a second Fc to control Fc paining when making fusion proteins comprising Fc domains (see particularly page 11). Therefore, it would have been obvious to ordinary artisans that the 35 amino acid residues of the linker of SEQ ID NO:1 (i.e. (GGGGQ) 7 ) could be used in place of the linker in the scFab constructs of the Brinkmann et al. as well as those of the ‘338 publication. This is because all of such sequences are taught as successfully being used as linker sequences when making fusion proteins (i.e. making a continuous polypeptide sequences out of what otherwise would be discontinuous sequences). Applicant is reminded that as per MPEP 2144.06, a n express suggestion to substitute one equivalent component or process for another is not necessary to render such substitution obvious. In re Fout , 675 F.2d 297, 213 USPQ 532 (CCPA 1982). With regard to the ordering of conventional Fab versus scFab in the claimed multispecifc antibodies, while the ‘338 publication discloses a molecule wherein the scFab is joined to the C terminal of the HC of a conventional antibody structure (such that the conventional antibody has a typical fab as its antigen binding domain) the opposite arrangement as recited in instant claim 16, which basically swaps where the conventional Fab and scFab reside the in the multispecifc construct as compared to that of the ‘338 is obvious. This is because antigen binding constructs wherein a scFab is N terminal to a hinge-CH2-CH3 were known and in use in the art as taught by Brinkmann et al. and thus artisans would readily conceive of swapping the convention Fab and scFab domains when evaluating the teachings of the ‘338 publication with a reasonable expectation of success as the use of scFab at the N terminal as well as the C terminal are both known to work as per the teachings of Brinkmann et al. and the ‘338 publication respectively. Note further that given that light chains naturally associate with heavy chains, joining the VH-CH1 to the N terminal of a Brinkmann et al. scIg is the most obvious solution as heavy chain domains remain on the heavy chain of the multispecifc construct whiel the LC has its normal structure and pairing function as known in the art. Claim s 13-15 are rejected under 35 U.S.C. 103 as being unpatentable over WO 2011/117330 in view of Xiong et al. (WO 2020/185533) FILLIN "Insert the prior art reference(s) relied upon for the obviousness rejection." \d "[ 2 ]" as applied to claim s 1-9 and 12 above, and further in view of Kannan et al. (US 10,233,237). The inventions rendered obvious by the combined teachings of the prior art have been discussed above, and differ from the inventions as presently claimed in that electrostatic steering mutations designed to promote desired pairings between and antibody CH1 and light chain constant domain are not disclosed. Kannan et al. disclose making multiple mutations in antibody heavy and light chains in order to promote desire d pairings when making bispecific antibodies , including S183E, E356K, and D399K in a first heavy chain, S176K in a first light chain, S183K, K392D, and K409D in a second heavy chain, and S176E in a second light chain wherein the first heavy and light chains make up a first antigen binding domain and the second heavy and light chains make up a second antigen binding domain (see entire document, particularly the abstract and claims) Note that as graphically shown in Figure 4, pairing is achieved by a positive charge on one face of a domain interface (such as CH1 to lambda/kappa) matching a negative charge on the other face such that opposite charges attract while like charges repel and that assignment of a specific charge is arbitrary so long as its complementary position is opposite in charge. Additionally, it is well known that D (aspartic acid) and E (glutamic acid) are negatively charged residues while R (arginine) and K (lysine) are positively charged residues. Therefore , it would have been obvious to ordinary artisans to add charged residues into the constant regions of a Fab domain in order to enhance the desired associations between VH-CH1 and VL-CL sequences to aid in the assembly of properly formed scFab constructs. Claims 25-30 are rejected under 35 U.S.C. 103 as being unpatentable over US 2010/0256338 in view of Xiong et al. (WO 2020/185533) as applied to claim s 1-5, 8, 9, 24, and 31 above, and further in view of Kannan et al. The inventions rendered obvious by the combined teachings of the prior art have been discussed above, and differ from the inventions as presently claimed in that electrostatic steering mutations designed to promote desired pairings between and antibody CH1 and light chain constant domain are not disclosed. Kannan et al. disclose making multiple mutations in antibody heavy and light chains in order to promote desired pairings when making bispecific antibodies, including S183E, E356K, and D399K in a first heavy chain, S176K in a first light chain, S183K, K392D, and K409D in a second heavy chain, and S176E in a second light chain wherein the first heavy and light chains make up a first antigen binding domain and the second heavy and light chains make up a second antigen binding domain (see entire document, particularly the abstract and claims) Note that as graphically shown in Figure 4, pairing is achieved by a positive charge on one face of a domain interface (such as CH1 to lambda/kappa) matching a negative charge on the other face such that opposite charges attract while like charges repel and that assignment of a specific charge is arbitrary so long as its complementary position is opposite in charge. Additionally, it is well known that D (aspartic acid) and E (glutamic acid) are negatively charged residues while R (arginine) and K (lysine) are positively charged residues. Therefore, it would have been obvious to ordinary artisans to add charged residues into the constant regions of a Fab domain in order to enhance the desired associations between VH-CH1 and VL-CL sequences to aid in the assembly of properly formed scFab constructs. Claims 10, 11, 13-15, 17-22, 25-30 are rejected under 35 U.S.C. 103 as being unpatentable over Brinkmann et al. (WO 2011/117330) in view of US 2010/0256338 in view of Xiong et al. (WO 2020/185533) as applied to claim s 1-9, 12, 16, 23, 24, and 31 above, and further in view of Kannan et al. The inventions rendered obvious by the combined teachings of the prior art have been discussed above, and differ from the inventions as presently claimed in that electrostatic steering mutations designed to promote desired pairings between and antibody CH1 and light chain constant domain are not disclosed. Kannan et al. disclose making multiple mutations in antibody heavy and light chains in order to promote desired pairings when making bispecific antibodies, including S183E, E356K, and D399K in a first heavy chain, S176K in a first light chain, S183K, K392D, and K409D in a second heavy chain, and S176E in a second light chain wherein the first heavy and light chains make up a first antigen binding domain and the second heavy and light chains make up a second antigen binding domain (see entire document, particularly the abstract and claims) Note that as graphically shown in Figure 4, pairing is achieved by a positive charge on one face of a domain interface (such as CH1 to lambda/kappa) matching a negative charge on the other face such that opposite charges attract while like charges repel and that assignment of a specific charge is arbitrary so long as its complementary position is opposite in charge. Additionally, it is well known that D (aspartic acid) and E (glutamic acid) are negatively charged residues while R (arginine) and K (lysine) are positively charged residues. Therefore, it would have been obvious to ordinary artisans to add charged residues into the constant regions of a Fab domain in order to enhance the desired associations between VH-CH1 and VL-CL sequences to aid in the assembly of properly formed scFab constructs. Double Patenting The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg , 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman , 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi , 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum , 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel , 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington , 418 F.2d 528, 163 USPQ 644 (CCPA 1969). A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA. A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b). The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13. The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA/25, or PTO/AIA/26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer . Claim s 1- 5, 8, and 9 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim s 1-15, 17, 18, 38-44, and 58 of copending Application No. 18/566,228 . Although the claims at issue are not identical, they are not patentably distinct from each other because the copending claims anticipate that which is presently claimed. Specifically the copending claims recite a T cell engager comprising a scFab and a scFv, wherein the CH1 and VL domains of the scFab are joined by a (G4Q)7 linker sequence (see all copending claims, most notably claims 1, 7, and 8) . The copending scFab is further recited as comprising human IgG1 CH1 and either CKappa or Clambda domains, and note that such sequences are instant SEQ ID NOs: 4, 2, and 3 respectively. Given that the copending molecules necessarily comprise a scFv in addition to the scFab , such molecules comprise more limitations and thus anticipate that which is presently claimed. This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented. Claim s 10 and 11 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim s 1-15, 17, 18, 38-44, and 58 of copending Application No. 18/566,228 as applied to claim s 1-5, 8, and 9 above, and further in view of Kannan et al. The inventions of the copending claims have been discussed above and differ from the inventions as presently claimed in that electrostatic steering mutations designed to promote desired pairings between and antibody CH1 and light chain constant domain are not disclosed. Kannan et al. disclose making multiple mutations in antibody heavy and light chains in order to promote desired pairings when making bispecific antibodies, including S183E, E356K, and D399K in a first heavy chain, S176K in a first light chain, S183K, K392D, and K409D in a second heavy chain, and S176E in a second light chain wherein the first heavy and light chains make up a first antigen binding domain and the second heavy and light chains make up a second antigen binding domain (see entire document, particularly the abstract and claims) Note that as graphically shown in Figure 4, pairing is achieved by a positive charge on one face of a domain interface (such as CH1 to lambda/kappa) matching a negative charge on the other face such that opposite charges attract while like charges repel and that assignment of a specific charge is arbitrary so long as its complementary position is opposite in charge. Additionally, it is well known that D (aspartic acid) and E (glutamic acid) are negatively charged residues while R (arginine) and K (lysine) are positively charged residues. Therefore, it would have been obvious to ordinary artisans to add charged residues into the constant regions of a Fab domain in order to enhance the desired associations between VH-CH1 and VL-CL sequences to aid in the assembly of properly formed scFab constructs. This is a provisional nonstatutory double patenting rejection. No claims are allowable. Any inquiry concerning this communication or earlier communications from the examiner should be directed to FILLIN "Examiner name" \* MERGEFORMAT Michael Szperka whose telephone number is FILLIN "Phone number" \* MERGEFORMAT (571)272-2934 . The examiner can normally be reached FILLIN "Work Schedule?" \* MERGEFORMAT Monday-Friday 8:30-5:00 . Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice. If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, FILLIN "SPE Name?" \* MERGEFORMAT Misook Yu can be reached at FILLIN "SPE Phone?" \* MERGEFORMAT 571-272-0839 . The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300. Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000. FILLIN "Examiner Stamp" \* MERGEFORMAT Michael Szperka Primary Examiner Art Unit 1641 /MICHAEL SZPERKA/ Primary Examiner, Art Unit 1641