Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
DETAILED ACTION
This application is a 371 of PCT/CN2020/082594.
The response filed on February 6, 2026 has been entered.
Election/Restrictions
Applicant’s election without traverse of the species (A) chiral diamines, (B) transaminase, (C) substrate of Formula I, and (D) amino donors:
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in the reply filed on February 6, 2026 is acknowledged.
Claim 3 is withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected species, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on February 6, 2026.
Status of Claims
Claims 1-17 are pending.
Claim 3 is withdrawn.
Claims 1-2 and 4-17 are under examination.
Foreign Priority
Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on August 26, 2022 and September 24, 2024 are in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statements are being considered by the examiner.
Claim Objections
Claims 1, 4, 7, and 14 are objected to because of the following informalities:
Claim 1 recites microorganisms, which should be italicized.
Claim 1 does not recite a conjunction between the “substrate..” and “..transaminase..”.
Claim 4 does not recite a conjunction between “mixture;” and “isolating..”
Claim 7 does not recite a conjunction between “filtrate;” and “extracting..”.
Claim 14 does not recite a conjunction between “product;” and “concentrating.”.
Appropriate correction is required.
Claim Rejections - 35 USC § 112
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.
Claim 1 and claims 2 and 4-17 depending therefrom 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 limitation “the transaminase is derived from Chromobacterium violaceum DSM3019 (CVTA)….Geobacillus toebii, and Talaromyces cellulyticus”. The metes and bounds of the limitation in the context of the above claim are not clear. The recitation of “and” in the last line of claim 1 renders ambiguity. It is unclear if the transaminase is derived from each of the recited microorganism or if the transaminase is a chimera transaminase derived from all the recited microorganism. Clarification is requested.
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 and 4-17 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 pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention.
MPEP 2111.01 states that ''[d]uring examination, the claims must be interpreted as broadly as their terms reasonably allow.'' The limitation transaminase “derived from” has been broadly interpreted as transaminase isolated from one of the microorganisms recited in claim 1 or variants and/or fragments derived from said transaminase. Therefore, the encompass a method of synthesizing (A) any chiral amine or
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comprising using (B) any transaminase derived from Chromobacterium violaceum DSM30191 (CVTA), including variants and fragments thereof to convert (C) any substrate having Formula I or
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into the chiral amine. Therefore, the claims are drawn to a method of synthesizing (A) genus of chiral amines or
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comprising using (B) genus of transaminases having unknown structure to convert (C) genus of substrates having Formula I or
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.
MPEP 2163 I. states that to “satisfy the written description requirement, a patent specification must describe the claimed invention in sufficient detail that one skilled in the art can reasonably conclude that the inventor had possession of the claimed invention.
MPEP 2163. II.A.3.(a) sates that “Possession may be shown in many ways. For example, possession may be shown by describing an actual reduction to practice of the claimed invention. Possession may also be shown by a clear depiction of the invention in detailed drawings or in structural chemical formula which permit a person skilled in the art to clearly recognize that inventor had possession of the claimed invention. An adequate written description of the invention may be shown by any description of sufficient, relevant, identifying characteristics so long as a person skilled in the art would recognize that the inventor had possession of the claimed invention.
According to MPEP 2163.II.A.3.(a).ii), “Satisfactory disclosure of a ‘representative number’ depends on whether one of skill in the art would recognize that the applicant was in possession of the necessary common attributes or features possessed by the members of the genus in view of the species disclosed. For inventions in an unpredictable art, adequate written description of a genus which embraces widely variant species cannot be achieved by disclosing only one species within the genus…Instead, the disclosure must adequately reflect the structural diversity of the claimed genus, either through the disclosure of sufficient species that are ‘representative of the full variety or scope of the genus,’ or by the establishment of ‘a reasonable structure-function correlation.’"
The recitations of “transaminase derived from Chromobacterium violaceum DSM30191 (CVTA)” fail to provide a sufficient description of the genus of the transaminase used in the claimed method as it merely describes the functional features of the genus without providing any definition of the structural features of the species within the genus. The specification does not specifically define any of the species that fall within the genus. The specification does not define any structural features commonly possessed by members of the genus that distinguish them from others. One skilled in the art therefore cannot, as one can do with a fully described genus, visualize or recognize the identity of the members of the genus.
Kaulmann (Substrate spectrum of ω-transaminase from Chromobacterium violaceum DSM30191 and its potential for biocatalysis. Enzyme and Microbial Technology, Volume 41, Issue 5, 2007, Pages 628-637 – form PTO-1449) discloses Chromobacterium violaceum DSM30191 (CVTA) transaminase (abstract and Fig. 2. At page 631). Chen (Stabilization of an amine transaminase for biocatalysis. Journal of Molecular Catalysis B: Enzymatic, Volume 124, 2016, 20-28 – form PTO-892) discloses that low operational stability of Chromobacterium violaceum transaminase limits the enzyme applicability on larger scales (abstract). Hong (WO 2021/081713 – form PTO-892 and English Translation of WO 2021/081713. Retrieved on May 13, 2026 – form PTO-892) discloses that in the industrial application and production, most wild-type transaminases have the shortcomings of low catalytic efficiency, poor stereoselectivity, and weak stability, so that there are not many transaminases that can really be used (page 2, 3rd full paragraph). Therefore, even though Chromobacterium violaceum DSM30191 transaminase and other wildtype transaminases were known in the prior art, a method of producing the genus of chiral diamines from the genus of substrates of Formula I using the genus of transaminase was not known.
The specification is limited to a method of producing a chiral diamine by reacting the transaminase mutant of Chromobacterium violaceum DSM30191, wherein the transaminase mutant has the amino acid sequence of SEQ ID NO:1, 2, 3, or 4, and a substrate having Formula I. While MPEP 2163 acknowledges that in certain situations “one species adequately supports a genus,” it also acknowledges that “[f]or inventions in an unpredictable art, adequate written description of a genus which embraces widely variant species cannot be achieved by disclosing only one species within the genus.” In view of the widely variant species encompassed by the genus, the examples described above is not enough and does not constitute a representative number of species to describe the whole genus. Therefore, the specification fails to describe a representative species of the claimed genus.
The claimed invention requires a defined set of substrates of Formula I, amino donors, and transaminases. A “laundry list” disclosure of every possible moiety does not necessarily constitute a written description of every species in a genus because it would not “reasonably lead” those skilled in the art to any particular species, see Fujikawa v. Wattanasin, 93 F.3d 1559, 1571, 39 USPQ2d 1895, 1905 (Fed. Cir. 1996) or MPEP 2163. While the exemplary substrates of Formula I, amino donors, and transaminases were known in the art, this knowledge alone would not allow one level of skill in the art to immediately envisage the claimed method. Therefore, the level of skill and knowledge in the art is such that one of ordinary skill would not be able to identify without further testing which combination of substrates of Formula I, amino donors, and transaminases to use in the claimed method.
Fransceus (J Ind Microbiol Biotechnol. 2017 May;44(4-5):687-695. – form PTO-892) reviews protein engineering techniques, such as random mutagenesis and recombination, directed evolution and iterative or combinatory saturation “hotspots”. Fransceus states that “a recurring problem, however, is choosing which amino acid positions should be targeted. Answering this question is not an easy feat and requires substantial insight in the relationship between an enzyme’s sequence or structure and its properties.” Sanavia (Computational and Structural Biotechnology Journal, Volume 18, 2020, Pages 1968-1979. – form PTO-892) discloses challenges in the prediction of protein stability in the occurrence of multiple mutations. “Multiple-point mutations are common variations of the protein sequence that may be needed in protein engineering when a single-point mutation is not enough to yield the desired stability change. Dealing with multiple-site variations adds another level of complexity beyond the prediction of the effect of a single variant on protein stability, since it requires the learning of many types of combinatorial effects”.
An important consideration is that structure is not necessarily a reliable indicator of function. In the instant case, there is no disclosure relating similarity of structure to conservation of function. Conservation of structure is not necessarily a surrogate for conservation of function.
While general knowledge in the art may have allowed one of skill in the art to identify other polypeptides expected to have the same or similar tertiary structure, there was no general knowledge in the art in the ability of the claimed genus of transaminases to produce the claimed genus of chiral diamines.
Given this lack of description of the representative species encompassed by the genus of the claims, the specification fails to sufficiently describe the claimed invention in such full, clear, concise, and exact terms that a skilled artisan would recognize that applicants were in possession of the inventions of claims 1-2 and 4-17.
Claims 1-2 and 4-17 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 method of producing a chiral diamine by reacting the transaminase mutant of Chromobacterium violaceum DSM30191, wherein the transaminase mutant has the amino acid sequence of SEQ ID NO:1, 2, 3, or 4, and a substrate having Formula I, does not reasonably provide enablement for a method of producing any chiral diamine by converting any substrate having Formula I and any transaminase. 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 use the invention commensurate in scope with these claims.
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). They 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.
The breadth of the claims.
MPEP 2111.01 states that ''[d]uring examination, the claims must be interpreted as broadly as their terms reasonably allow.'' The limitation transaminase “derived from” has been broadly interpreted as transaminase isolated from one of the microorganisms recited in claim 1 or variants and/or fragments derived from said transaminase. Therefore, the encompass a method of synthesizing (A) any chiral amine or
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comprising using (B) any transaminase derived from Chromobacterium violaceum DSM30191 (CVTA), including variants and fragments thereof to convert (C) any substrate having Formula I or
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into the chiral amine. Therefore, the claims are drawn to a method of synthesizing (A) any chiral amine or
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comprising using (B)any transaminase having unknown structure to convert (C) any substrate having Formula I or
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.
The claim is not commensurate with the enablement provided by the disclosure with regard to the extremely large number of substrates of Formula I and transaminase. The specification is limited to a method of producing a chiral diamine by reacting the transaminase mutant of Chromobacterium violaceum DSM30191, wherein the transaminase mutant has the amino acid sequence of SEQ ID NO:1, 2, 3, or 4, and a substrate having Formula I.
The quantity of experimentation required to practice the claimed invention based on the teachings of the specification.
While enzyme isolation techniques, recombinant and mutagenesis techniques were known in the art at the time of the invention, e.g. mutagenesis, and it is routine in the art to screen for variants comprising multiple substitutions or multiple modifications as encompassed by the instant claims, the specific amino acid positions within the protein's sequence where amino acid modifications can be made with a reasonable expectation of success in obtaining the desired activity/utility are limited in any protein and the result of such modifications is unpredictable. In addition, one skilled in the art would expect any tolerance to modification for a given protein to diminish with each further and additional modification, e.g. multiple substitutions.
In the absence of: (a) rational and predictable scheme for producing chiral amines by reacting any substrate of Formula I and any transaminase and (b) a correlation between structure and the function of a transaminase to produce chiral diamines from the substrate of Formula I, the specification provides insufficient guidance as to which of the essentially infinite possible choices is likely to be successful. One of skill in the art would have to test these infinite possible polypeptides to determine which transamines, when reacted with any substrate of formula I results in the production of chiral diamines. While enablement is not precluded by the necessity for routine screening, if a large amount of screening is required, as is the case herein, the specification must provide a reasonable amount of guidance which respect to the direction in which the experimentation should proceed so that a reasonable number of species can be selected for testing. In view of the fact that such guidance has not been provided in the instant specification, it would require undue experimentation to enable the full scope of the claims.
The state of prior art, the relative skill of those in the art, and predictability or unpredictability of the art.
Kaulmann (Substrate spectrum of ω-transaminase from Chromobacterium violaceum DSM30191 and its potential for biocatalysis. Enzyme and Microbial Technology, Volume 41, Issue 5, 2007, Pages 628-637 – form PTO-1449) discloses Chromobacterium violaceum DSM30191 (CVTA) transaminase (abstract and Fig. 2. At page 631). Chen (Stabilization of an amine transaminase for biocatalysis. Journal of Molecular Catalysis B: Enzymatic, Volume 124, 2016, 20-28 – form PTO-892) discloses that low operational stability of Chromobacterium violaceum transaminase limits the enzyme applicability on larger scales (abstract). Hong (WO 2021/081713 – form PTO-892 and English Translation of WO 2021/081713. Retrieved on May 13, 2026 – form PTO-892) discloses that in the industrial application and production, most wild-type transaminases have the shortcomings of low catalytic efficiency, poor stereoselectivity, and weak stability, so that there are not many transaminase that can really be used (page 2, 3rd full paragraph). Therefore, even though Chromobacterium violaceum DSM30191 transaminase and other wildtype transaminase were known in the prior art, a method of producing any chiral diamines from any substrate of Formula I using any transaminase was not known.
Since the amino acid sequence of the transaminase determines its structural and functional properties, predictability of which changes can be tolerated in a protein's amino acid sequence and obtain the desired activity requires a knowledge of and guidance with regard to which amino acids in the protein's sequence, if any, are tolerant of modification and which are conserved (i.e. expectedly intolerant to modification), and detailed knowledge of the ways in which the proteins' structure relates to its function. In the instant case, neither the specification or the art provides a correlation between structure and activity such that one of skill in the art can envision the structure of any transaminase having the function of converting any substrate of Formula I to its corresponding chiral diamine or predict said function of a polypeptide from its primary structure. In addition, the art does not provide any teaching or guidance as to (1) which amino acids within a transaminase hat can be modified and which ones are conserved such that one of skill in the art can make and use the polypeptide to produce chiral deaminase from the substrate of Formula I, (2) which segments of a transaminase that are essential for having the function of converting any substrate of Formula I to its corresponding chiral amine, and (3) the general tolerance of transaminases to structural modifications and the extent of such tolerance. The art clearly teaches that changes in a protein's amino acid sequence to obtain the desired activity without any guidance/knowledge as to which amino acids in a protein are required for that activity is highly unpredictable. At the time of the invention there was a high level of unpredictability associated with altering a polypeptide sequence with an expectation that the polypeptide will maintain the desired activity. For example, Studer (Residue mutations and their impact on protein structure and function: detecting beneficial and pathogenic changes. Biochem. J. (2013) 449, 581–594. – form PTO-892) teach that (1) protein engineers are frequently surprised by the range of effects caused by single mutations that they hoped would change only one specific and simple property in enzymes, (2) the often surprising results obtained by experiments where single mutations are made reveal how little is known about the rules of protein stability, and (3) the difficulties in designing de novo stable proteins with specific functions.
Fransceus (J Ind Microbiol Biotechnol. 2017 May;44(4-5):687-695. – form PTO-892) reviews protein engineering techniques, such as random mutagenesis and recombination, directed evolution and iterative or combinatory saturation “hotspots”. Fransceus states that “a recurring problem, however, is choosing which amino acid positions should be targeted. Answering this question is not an easy feat and requires substantial insight in the relationship between an enzyme’s sequence or structure and its properties.” Sanavia (Computational and Structural Biotechnology Journal, Volume 18, 2020, Pages 1968-1979. – form PTO-892) discloses challenges in the prediction of protein stability in the occurrence of multiple mutations. “Multiple-point mutations are common variations of the protein sequence that may be needed in protein engineering when a single-point mutation is not enough to yield the desired stability change. Dealing with multiple-site variations adds another level of complexity beyond the prediction of the effect of a single variant on protein stability, since it requires the learning of many types of combinatorial effects”.
The amount of direction or guidance presented and the existence of working examples.
The specification is limited to a method of producing a chiral diamine by reacting the transaminase mutant of Chromobacterium violaceum DSM30191, wherein the transaminase mutant has the amino acid sequence of SEQ ID NO:1, 2, 3, or 4, and a substrate having Formula I. However, the speciation fails to provide any information as to the structural elements required in a transaminase having the function of converting any substrate of Formula I to its corresponding chiral diamine. No correlation between structure and function of converting any substrate of Formula I to its corresponding chiral diamine has been presented.
Thus, in view of the overly broad scope of the claims, the lack of guidance and working examples provided in the specification, the high level of unpredictability of the prior art in regard to structural changes and their effect on function and the lack of knowledge about a correlation between structure and function, an undue experimentation would be necessary one having ordinary skill in the art to make and use the claimed invention in a manner reasonably correlated with the scope of the claims. The scope of the claims must bear a reasonable correlation with the scope of enablement (In re Fisher, 166 USPQ 19 24 (CCPA 1970)). Without sufficient guidance, determination of polypeptides having the desired biological characteristics recited in the claims are unpredictable and the experimentation left to those skilled in the art is unnecessarily, and improperly, extensive and undue. See In re Wands 858 F.2d 731, 8 USPQ2nd 1400 (Fed. Cir, 1988).
Other Relevant Art
Hong (WO 2021/081713 – form PTO-892 and English Translation of WO 2021/081713. Retrieved on May 13, 2026 – form PTO-892) discloses a transaminase mutant having 100% sequence identity to the transaminase mutant of SEQ ID NO:4 of the instant application (see the sequence alignment below). However, Hong does not disclose that the transaminase mutant is able to convert the substrate of Formula I into its corresponding chiral diamine.
Conclusion
Claims 1-17 are pending.
Claim 3 is withdrawn.
Claims 1-2 and 4-17 are rejected.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to YONG D PAK whose telephone number is (571)272-0935. The examiner can normally be reached M-Th: 5:30 am - 3:30 pm.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Robert Mondesi can be reached on 408-918-7584. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/YONG D PAK/Primary Examiner, Art Unit 1652
Sequence alignment of the mutant transaminase of SEQ ID NO:4 of the instant application (“Qy”) and the mutant transaminase of Hong (“Db”)
BJH95901
ID BJH95901 standard; protein; 459 AA.
XX
AC BJH95901;
XX
DT 24-JUN-2021 (first entry)
XX
DE Mutant aminotransferase (T7C/S47C/Q380L/V379L/M166F/R416D/N151W/F409H).
XX
KW Aminotransferase; chiral amine; enzyme engineering; mutein.
XX
OS Chromobacterium violaceum.
OS Synthetic.
XX
CC PN WO2021081713-A1.
XX
CC PD 06-MAY-2021.
XX
CC PF 28-OCT-2019; 2019WO-CN113743.
XX
PR 28-OCT-2019; 2019WO-CN113743.
XX
CC PA (ASYM-) ASYMCHEM LAB TIANJIN CO LTD.
XX
CC PI Hong H, James G, Yi H, Ma Y, Zhang N, Jiao X, Mou H, Cheng Y;
CC PI Cao S;
XX
DR WPI; 2019-A7561E/005.
XX
CC PT New transaminase mutant, obtained by mutating the amino acid in the
CC PT mutated amino acid sequence.
XX
CC PS Example 1; Page; 31pp; Chinese.
XX
CC The present invention relates to a novel aminotransferase mutant useful
CC for producing chiral amines. The method involves performing transaminase
CC catalyzed transaminase reaction of ketone compounds and amino group
CC donors. The invention further provides: DNA molecule encoding the
CC aminotransferase mutant; a recombinant plasmid comprising the DNA
CC molecule; a host cell comprising the recombinant plasmid; and a method
CC for producing the chiral amines. Note: This sequence is a mutant of the
CC parent sequence shown in SEQ ID NO: 1 (see BJH95840).
XX
SQ Sequence 459 AA;
Query Match 100.0%; Score 2482; Length 459;
Best Local Similarity 100.0%;
Matches 459; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MQKQRTCSQWRELDAAHHLHPFTDTASLNQAGARVMTRGEGVYLWDCEGNKIIDGMAGLW 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MQKQRTCSQWRELDAAHHLHPFTDTASLNQAGARVMTRGEGVYLWDCEGNKIIDGMAGLW 60
Qy 61 CVNVGYGRKDFAEAARRQMEELPFYNTFYKTTHPAVVELSSLLAEVTPAGFDRVFYTNSG 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 CVNVGYGRKDFAEAARRQMEELPFYNTFYKTTHPAVVELSSLLAEVTPAGFDRVFYTNSG 120
Qy 121 SESVDTMIRMVRRYWDVQGKPEKKTLIGRWWGYHGSTIGGASLGGFKYMHEQGDLPIPGM 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 SESVDTMIRMVRRYWDVQGKPEKKTLIGRWWGYHGSTIGGASLGGFKYMHEQGDLPIPGM 180
Qy 181 AHIEQPWWYKHGKDMTPDEFGVVAARWLEEKILEIGADKVAAFVGEPIQGAGGVIVPPAT 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 AHIEQPWWYKHGKDMTPDEFGVVAARWLEEKILEIGADKVAAFVGEPIQGAGGVIVPPAT 240
Qy 241 YWPEIERICRKYDVLLVADEVICGFGRTGEWFGHQHFGFQPDLFTAAKGLSSGYLPIGAV 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 YWPEIERICRKYDVLLVADEVICGFGRTGEWFGHQHFGFQPDLFTAAKGLSSGYLPIGAV 300
Qy 301 FVGKRVAEGLIAGGDFNHGFTYSGHPVCAAVAHANVAALRDEGIVQRVKDDIGPYMQKRW 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 FVGKRVAEGLIAGGDFNHGFTYSGHPVCAAVAHANVAALRDEGIVQRVKDDIGPYMQKRW 360
Qy 361 RETFSRFEHVDDVRGVGMLLAFTLVKNKAKRELFPDFGEIGTLCRDIFHRNNLIMDSCGD 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 RETFSRFEHVDDVRGVGMLLAFTLVKNKAKRELFPDFGEIGTLCRDIFHRNNLIMDSCGD 420
Qy 421 HIVSAPPLVMTRAEVDEMLAVAERCLEEFEQTLKARGLA 459
|||||||||||||||||||||||||||||||||||||||
Db 421 HIVSAPPLVMTRAEVDEMLAVAERCLEEFEQTLKARGLA 459
Prosecution Insights