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 election with traverse of Group I, claims 1-10, 17-19, to the variant of SEQ ID NO: 1 having a V187C substitution, in the reply filed on August 17, 2026, is acknowledged. The traversal is on the ground(s) that the office has not established that there is a serious burden for any variant of SEQ ID NO: 1. See also Applicants’ remarks. Applicants’ remarks are found persuasive regarding the V187 variants of SEQ ID NO: 1 recited in instant claim 1. However, as noted in the reasons noted on at least p. 6-7 of the restriction requirement, each variant and its sequence are viewed as a distinct biomolecule and would impose a serious burden as each variant/sequence would need to be individually searched. Search and consideration will be extended to the other variants (F242C, P313S, A47S of SEQ ID NO: 1) if the V187C/T variants are deemed to be patentable.
The requirement is still deemed proper and is therefore made FINAL.
Claims 11-16, 20 have been withdrawn from the examiner because they are drawn to non-elected inventions. Claims 1-10, 17-19, to the variant of SEQ ID NO: 1 having a V187C/T substitution, are under consideration.
Priority: This application is a 371 of PCT/EP2022/085534, filed December 13, 2022, which claims benefit to foreign application EP 21214446.3, filed December 14, 2021. A copy of the foreign priority document has been received in the instant application on October 14, 2024, and is in the English language.
Specification
The disclosure is objected to because it contains an embedded hyperlink and/or other form of browser-executable code: see at least paragraphs 0046, 0142 (of the application publication US20250051751). Applicant is required to delete the embedded hyperlink and/or other form of browser-executable code; references to websites should be limited to the top-level domain name without any prefix such as http:// or other browser-executable code. See MPEP § 608.01.
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 1-10, 17-19 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
In analyzing the claims for compliance with the written description requirements of 35 U.S.C. 112(a), a determination is made as to whether the specification contains a written description sufficient to show they had possession of the full scope of their claimed invention at the time the application was filed. The factors to be considered include disclosure of a complete or partial structure, physical and/or chemical properties, functional characteristics, structure/function correlation, and any combination thereof.
In the present situation, the claims are drawn to a glucose isomerase comprising an amino acid sequence having at least 80% identity to SEQ ID NO: 1 and comprising at least one substitution selected from V187C, wherein the glucose isomerase has at least one of the characteristics of (A), (B), (C), (D), and (E), or any combination thereof. The characteristics of (A), (B), (C), (D), and (E) are increased enzymatic activities under various conditions in comparison to the amino acid sequence of SEQ ID NO: 1.
Accordingly, the claims encompass a significantly large genus of engineered and variant amino acid sequences having glucose isomerase activity or increased enzymatic activity, the amino acid sequences having only at least 80% identity with SEQ ID NO: 1 and comprising amino acid mutations, including insertions, deletions, and/or substitutions with any natural or unnatural amino acids at any number of positions and/or at indicated positions, in addition to the V187C substitution.
All the engineered polypeptides having glucose isomerase activity or increased enzymatic activity are amino acid sequences comprising SEQ ID NO: 1 and having specific amino acid substitutions at noted positions, i.e. V187C, or combinations of specific amino acid substitutions (see specification examples and tables). Other than the specific engineered polypeptides, the specification fails to disclose any other engineered polypeptides having glucose isomerase activity or increased enzymatic activity comprising any number of amino acid mutations, including insertions, deletions, and/or substitutions with any natural or unnatural amino acids at any number of positions and/or at indicated positions to SEQ ID NO: 1 in combination with the selected substitution V187C. There is no guidance in the specification regarding which 20% may vary from SEQ ID NO: 1. The specification has described in terms of its complete structure only the wild type polypeptide with activity and specific amino acid substitutions therein. The specification does not describe by other relevant identifying characteristics a representative number of additional species within the broadly claimed genus.
It is noted that the specification also teaches the general methodology for performing mutagenesis to obtain modified glucose isomerases and methods for measuring or detecting activity. However, possession may not be shown by merely describing how to obtain possession of members of the claimed genus or how to identify their common structural features. See University of Rochester, 358 F.3d at 927, 69 USPQ2d at 1895.
This finding is also emphasized in Ex Parte Kubin (No. 2007-0819, Bd. Pat. Ann. & Int. May 31. 2007), wherein it is stated that:
“Although there is often significant overlap” between the enablement and written description requirements, “they are nonetheless independent of each other.” University of Rochester, 358 F.3d at 921, 69 USPQ2d at 1891. An “invention may be enabled even though it has not been described.” Id. Such is the situation here. While we conclude one skilled in the art would have been able to make and use the full scope of claim 73 through routine experimentation, we find Appellants did not describe the invention of claim 73 sufficiently to show they had possession of the claimed genus of nucleic acids. See, e.g., Noelle v. Lederman, 355 F.3d 1343, 1348, 69 USPQ2d 1508, 1513 (Fed. Cir. 2004) (“invention is, for purposes of the ‘written description’ inquiry, whatever is now claimed”).
Thereby, a showing of how to potentially identify and make other nucleic acids/polypeptides is not sufficient to establish that Applicants were in possession of the invention as broadly claimed.
The skilled artisan cannot necessarily envision the detailed structures of ALL the variant polypeptides having glucose isomerase or increased enzymatic activity comprising any number of amino acid mutations, including insertions, deletions, and/or substitutions with any natural or unnatural amino acids and having at least 80% identity with SEQ ID NO: 1 in combination with the selected substitution V187C, because the specification provides minimal guidance as to which amino acid substitutions at which positions, and which amino acids are essential and critical for all variant polypeptides having increased enzymatic activity, and therefore conception is not achieved until reduction to practice has occurred, regardless of the complexity or simplicity of the methods of making the claimed invention. Adequate written description requires more than a mere statement that it is part of the invention and reference to a potential method of isolating or making it. The compound itself is required. See Fiers v. Revel, 25 USPQ2d 1601 at 1606 (CAFC 1993) and Amgen Inc. V. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016.
Claims 1-10, 17-19 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for a glucose isomerase polypeptide comprising the amino acid sequence of SEQ ID NO: 1 and select amino acid substitutions (V187C), wherein the glucose isomerase has increased enzymatic activity under specific noted conditions compared to SEQ ID NO: 1, does not reasonably provide enablement for a glucose isomerase polypeptide comprising an amino acid sequence having at least 80% identity to SEQ ID NO: 1 and select amino acid substitutions (V187C). The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention commensurate in scope with these claims.
The scope of the instant claims is not commensurate with the enablement of the instant disclosure, because practice of the claimed invention would require undue experimentation by an artisan of ordinary skill in the art to ascertain which glucose isomerase variants comprising an amino acid sequence having at least 80% identity to SEQ ID NO: 1, comprising any number of amino acid mutations, including insertions, deletions, and/or substitutions with any natural or unnatural amino acids at any number of positions and/or at indicated positions to SEQ ID NO: 1 in combination with the selected substitution V187C, will have increase enzymatic activity. The claims are drawn to a glucose isomerase comprising an amino acid sequence having at least 80% identity to SEQ ID NO: 1 and comprising at least one substitution selected from V187C, wherein the glucose isomerase has at least one of the characteristics of (A), (B), (C), (D), and (E), or any combination thereof. The characteristics of (A), (B), (C), (D), and (E) are increased enzymatic activities under various conditions in comparison to the amino acid sequence of SEQ ID NO: 1. Accordingly, the claims encompass a significantly large genus of engineered and variant amino acid sequences having glucose isomerase activity or increased enzymatic activity, the amino acid sequences having only at least 80% identity with SEQ ID NO: 1 and comprising amino acid mutations, including insertions, deletions, and/or substitutions with any natural or unnatural amino acids at any number of positions and/or at indicated positions, in addition to the V187C substitution. Thus, there could be a myriad of variants wherein the modified or variant polypeptides may or may not exhibit glucose isomerase activity, much less increased enzymatic activity. Therefore, for the instant claimed invention, it would be an undue burden of experimentation for a skilled artisan to determine exactly which variants have glucose isomerase activity.
The factors to be considered in determining whether undue experimentation is required are summarized in In re Wands 858 F.2d 731, 8 USPQ2nd 1400 (Fed. Cir, 1988). The court in Wands states: “'Enablement is not precluded by the necessity for some experimentation such as routine screening. However, experimentation needed to practice the invention must not be undue experimentation. The key word is 'undue,' not 'experimentation.' " (Wands, 8 USPQ2d 1404). Clearly, enablement of a claimed invention cannot be predicated on the basis of quantity of experimentation required to make or use the invention. ''Whether undue experimentation is needed is not a single, simple factual determination, but rather is a conclusion reached by weighing many factual considerations.” (Wands, 8 USPQ2d 1404). The factors to be considered in determining whether undue experimentation is required include: (1) the quantity of experimentation necessary, (2) the amount of direction or guidance presented, (3) the presence or absence of working examples, (4) the nature of the invention, (5) the state of the prior art, (6) the relative skill of those in the art, (7) the predictability or unpredictability of the art, and (8) the breadth of the claims.
In the instant case, the quantity of experimentation would be large since there are myriad amino acid modifications (including insertions, deletions, substitutions) and amino acid residues to choose from to obtain variants comprising an amino acid sequence having at least 80% identity with SEQ ID NO: 1 and which have glucose isomerase activity and increased enzymatic activity. The amount of guidance in the specification is minimal as to which amino acid substitutions at which positions, and which amino acids are essential and critical for all variant polypeptides having glucose isomerase activity. In particular, the specification discloses engineered polypeptides having glucose isomerase activity disclosed in the instant specification are amino acid sequences comprising SEQ ID NO: 1 and having specific amino acid substitutions at noted positions, i.e. V187C, or combinations of specific amino acid substitutions (see specification examples and tables).
The specification fails to disclose any other engineered polypeptides having glucose isomerase activity or increased enzymatic activity comprising any number of amino acid mutations, including insertions, deletions, and/or substitutions with any natural or unnatural amino acids at any number of positions and/or at indicated positions to SEQ ID NO: 1 in combination with the selected substitution V187C. There is no guidance in the specification regarding which 20% may vary from SEQ ID NO: 1.
The nature of the invention is such that many different polypeptides that are substantially similar to glucose isomerase may or may not have glucose isomerase activity. The state of the prior art is that even proteins that are highly similar to the wild type protein are at times not fully active. In this instance, it is known that protein activity depends on the nature of the amino acid substitution and its positions. For instance, Miyamoto et al. (2022 Critical Reviews in Biotechnology 42(5): 693-712, published online October 12, 2021) disclose protein engineering to optimize xylose (glucose) isomerases and introducing amino acid substitutions into various wild type xylose isomerase polypeptides, where it is shown that only variant xylose isomerases comprising specific amino acid substitutions have improved functional properties compared to the wild type xylose isomerase activity (at least p. 699-700). A single amino acid substitution at the same position can render the variant xylose isomerase has higher activity or lower activity depending on the amino acid residue that is substituted (p. 700). The relative level of skill in this art is very high. The predictability as to what substantially similar protein will have which activity is zero.
When the factors are considered in their entirety, the Wands analysis dictates a finding of undue experimentation and thus, the claims are not enabled.
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 1-10, 17-19 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 1 recites the glucose isomerase comprises an amino acid sequence having at least 80% identity to SEQ ID NO: 1. It is not sure what is meant by identity, i.e. has 80% sequence identity, 80% functionality, structural identity, etc. Further clarification and/or correction is requested.
Claim 4 is dependent on claim 1 and recites wherein the amino acid sequence further comprises at least one…at least eight substitutions at a position selected from the noted group. The Markush group recites positions V187, F242, P313, A47. However, claim 1 already recites that the noted positions have specific amino acid substitutions. It is not clear how the V187, F242, P313, A47 positions can be selected again to be substituted with any amino acid residue now in claim 4. Further clarification and/or correction is requested.
Claim 5 is included in this rejection for the reasons similarly noted above for claim 4.
Claims 2-3, 6-10, 17-19 are included in this rejection because they are dependent on the above claim(s).
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.
Claims 1-10, 17-19 are rejected under 35 U.S.C. 103 as being unpatentable over Miyamoto et al. (2022 Critical Reviews in Biotechnology 42(5): 693-712, published online October 12, 2021) in view of Viitanen et al. (WO 2009120731; IDS 06.12.24). Miyamoto et al. disclose xylose isomerase (XI), also known as glucose isomerase, catalyzes the reversible conversion of D-glucose and D-xylose into D-fructose and D-xylulose, respectively (p. 693) and are well studied due to their extensive application in industrial processes to produce high-fructose corn syrups (p. 693). Miyamoto et al. disclose that protein engineering is a useful tool to optimize XIs (at least p. 699). Miyamoto et al. disclose that a considerable number oof XIs have been subject to evolutionary steps to improve their functional properties (Table 2) (p. 699-700). Miyamoto et al. disclose that using directed evolution and semi-rational strategies, the optimization of XIs with improved thermostability and efficiency at varied pH and/or under mild conditions (in terms of pH and temperature) is possible (p. 699). Miyamoto et al. disclose various XI mutations and their effects (p. 700 Table 2). Miyamoto et al. disclose the XI of Clostridium thermosulfurigenes having a V186T mutation, having higher activity in glucose, and the XI of Thermotoga neapolitana having a V185T mutation, having higher activity at low temperatures (p. 700 Table 2). Miyamoto et al. do not teach instant SEQ ID NO: 1 (the amino acid sequence of Bifidobacterium adolescentis XI).
Viitanen et al. disclose xylose-utilizing recombinant bacterial strains that are genetically engineered to have high expression of xylose isomerase (at least paragraph 0007). Viitanen et al. disclose the amino acid sequences for known XIs, including the Clostridium thermosulfurigenes XI (SEQ ID NO: 48) and the Thermotoga neapolitana XI (SEQ ID NO: 80) (p. 8-10 Table 1) (disclosed in Miyamoto et al.), where other known XI polypeptides include Bifidobacterium adolescentis (SEQ ID NO: 64) (p. 9 Table 1). Viitanen et al. disclose that SEQ ID NO: 64 is the amino acid sequence for Bifidobacterium adolescentis XI (Table 1), where it is disclosed that SEQ ID NO: 64 comprises the V187 residue (see appendix A).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to combine the prior art references and arrive at the claimed glucose isomerase comprising an amino acid sequence having at least 80% sequence identity to instant SEQ ID NO: 1 (Bifidobacterium adolescentis XI) and comprising the amino acid substitution V187T (instant claims 1-10, 17-19). The motivation to do so is given by the prior art. Miyamoto et al. disclose engineering XIs to improve their functional properties, where an amino acid substitution at a Valine residue at positions 185-186 of known XI polypeptides show higher activity, i.e. V186T, V185T, of Clostridium thermosulfurigenes XI and Thermotoga neapolitana XI, respectively. Viitanen et al. disclose other known XI amino acid sequences, in addition to Clostridium thermosulfurigenes XI and Thermotoga neapolitana XI, including the amino acid sequence for Bifidobacterium adolescentis XI (SEQ ID NO: 64), where it is disclosed that SEQ ID NO: 64 comprises the V187 residue (see appendix A). Therefore, one of ordinary skill would have reasonable motivation to incorporate the Bifidobacterium adolescentis XI of Viitanen et al. into the teachings of Miyamoto et al. and to further modify the valine residue at position 187 with a threonine residue, to thereby arrive at the claimed glucose isomerase comprising a V187T substitution, because the V187 position is similar to the valine residue at positions 185-186 of other known XI polypeptides to have improved activity and there was interest in protein engineering to optimize XIs. One of ordinary skill would have a reasonable expectation of success because the prior art identifies similar positions to the recited V187 position for substitution to improve activity of a XI.
Regarding the characteristics (A) to (E) recited in instant claim 1, it is submitted that these are properties and/or actions of the V187T XI variant. Since the teachings of the prior art disclose arriving at the same V187T substitution in a Bifidobacterium adolescentis XI, it is submitted that the properties and/or characteristics (A) to (E) of instant claim 1 would be naturally present in the V187T Bifidobacterium adolescentis XI variant of Miyamoto et al. in view of Viitanen et al. noted above. Mere recognition of latent properties in the prior art does not render nonobvious an otherwise known invention. MPEP 2145.
Regarding instant claims 2-3, MPEP 2144.09 notes that a prima facie case of obviousness may be made when chemical compounds have very close structural similarities and similar utilities. Miyamoto et al. disclose mutagenesis with different amino acid substitutions and/or residues at the same positions (Table 1). Therefore, it would have been obvious to arrive at the recited V187C substitution by incorporation of other known amino acid residues and by routine optimization.
Regarding instant claims 9-10, 17-20, as similarly noted above for the characteristics (A) to (E) recited in instant claim 1, it is submitted that these are properties and/or actions of the V187T XI variant. Since the teachings of the prior art disclose arriving at the same V187T substitution in a Bifidobacterium adolescentis XI, it is submitted that any properties and/or characteristics of instant claims 9-10, 17-20 would be naturally present in the V187T Bifidobacterium adolescentis XI variant of Miyamoto et al. in view of Viitanen et al. noted above. Mere recognition of latent properties in the prior art does not render nonobvious an otherwise known invention. MPEP 2145.
No claim is allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Marsha Tsay whose telephone number is (571)272-2938. The examiner can normally be reached M-F.
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, Manjunath N. Rao can be reached on 571-272-0939. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/Marsha Tsay/Primary Examiner, Art Unit 1656
Appendix A
ID AXR32105 standard; protein; 449 AA.
XX
DT 26-NOV-2009 (first entry)
XX
DE B. adolescentis xylose isomerase, SEQ ID 64.
XX
KW Xylose isomerase; ethanol; fermentation;
KW genetically engineered microorganism.
XX
OS Bifidobacterium adolescentis ATCC 15703.
XX
CC PN WO2009120731-A2.
XX
CC PD 01-OCT-2009.
XX
CC PF 25-MAR-2009; 2009WO-US038164.
XX
PR 27-MAR-2008; 2008US-0039878P.
XX
CC PA (DUPO ) DU PONT DE NEMOURS&CO E I.
CC PA (ALLI-) ALLIANCE SUSTAINABLE ENERGY LLC.
XX
CC PI Caimi PG, Chou Y, Franden MA, Mccole L, Mccutchen C, Tao L;
CC PI Viitanen PV, Zhang M, Zhang Y;
XX
DR WPI; 2009-P13455/66.
DR N-PSDB; AXR32106.
XX
CC PS Claim 7; SEQ ID NO 64; 92pp; English.
XX
SQ Sequence 449 AA;
Query Match 99.0%; Score 2363; Length 449;
Best Local Similarity 98.7%;
Matches 443; Conservative 3; Mismatches 3; Indels 0; Gaps 0;
Qy 1 MGLWDIEKIPYVGREKGPQEGLAFHYYDADKVVAGKKMKDWLRFGVAWWHTFDQELVDPF 60
||||||:|||||||||||||||||||||||||||||||||||||||||||||||:|||||
Db 1 MGLWDIDKIPYVGREKGPQEGLAFHYYDADKVVAGKKMKDWLRFGVAWWHTFDQQLVDPF 60
Qy 61 GTGTAQRPWYGKYSNAEDEALAKVDYAFEFFQKLGVEYFCFHDRDIAPEGDTLRETDKNL 120
||||||||||||||: ||||||||||||||||||||||||||||||||||||||||||||
Db 61 GTGTAQRPWYGKYSDPEDEALAKVDYAFEFFQKLGVEYFCFHDRDIAPEGDTLRETDKNL 120
Qy 121 DKVVDKIEENMKSTGIKLLWNTSSLFTNPRFVSGASTSPFADIYAYAGGQLKHSLEIAKR 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 DKVVDKIEENMKSTGIKLLWNTSSLFTNPRFVSGASTSPFADIYAYAGGQLKHSLEIAKR 180
Qy 181 LGAENYTFWGGREGYENLWNTQMKREQEHMAKFFHMCHDYAKEIGLDAQFLIEPKAKEPT 240
|||||| |||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 LGAENYVFWGGREGYENLWNTQMKREQEHMAKFFHMCHDYAKEIGLDAQFLIEPKAKEPT 240
Qy 241 MFQYDFDAATAINFLRTYDLMDVFKLNLEGNHANLAGHTYQHEIRTAREAGVLGSLDANQ 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 MFQYDFDAATAINFLRTYDLMDVFKLNLEGNHANLAGHTYQHEIRTAREAGVLGSLDANQ 300
Qy 301 GDKLIGWDMDEFPTDLYETSTVMWEVLAEGQIGPHGGLNFDAKPRRTSFAAEDLFRSHIA 360
||||||||||||||||||||||||||||||||||||||||||||||||| ||||||||||
Db 301 GDKLIGWDMDEFPTDLYETSTVMWEVLAEGQIGPHGGLNFDAKPRRTSFTAEDLFRSHIA 360
Qy 361 GMDSFAAGLLVAAKMHEDKVIENLQAERYSSFDSGIGATVENGTASLASLEEYALDIPQS 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 GMDSFAAGLLVAAKMHEDKVIENLQAERYSSFDSGIGATVENGTASLASLEEYALDIPQS 420
Qy 421 KLIEATKSDHLESVKATINNYMIDALAEA 449
|||||||||||||||||||||||||||||
Db 421 KLIEATKSDHLESVKATINNYMIDALAEA 449
Prosecution Insights