Ex Parte Livshits et al

Patent Trials and Appeals Board

Mar 22, 2019

15185371 - (D) (P.T.A.B. Mar. 22, 2019)

UNITED STA TES p A TENT AND TRADEMARK OFFICE
APPLICATION NO. FILING DATE
15/185,371 06/17/2016
38108 7590 03/26/2019
CERMAK NAKAJIMA MCGOWAN LLP
127 S. Peyton Street
Suite 210
ALEXANDRIA, VA 22314
FIRST NAMED INVENTOR
Vitaliy Arkadyevich Livshits
UNITED STATES DEPARTMENT OF COMMERCE
United States Patent and Trademark Office
Address: COMMISSIONER FOR PATENTS
P.O. Box 1450
Alexandria, Virginia 22313-1450
www .uspto.gov
ATTORNEY DOCKET NO. CONFIRMATION NO.
US-126C 9962
EXAMINER
STEADMAN, DAVID J
ART UNIT PAPER NUMBER
1656
NOTIFICATION DATE DELIVERY MODE
03/26/2019 ELECTRONIC
Please find below and/or attached an Office communication concerning this application or proceeding.
The time period for reply, if any, is set in the attached communication.
Notice of the Office communication was sent electronically on above-indicated "Notification Date" to the
following e-mail address(es):
cgoode@cnmiplaw.com
ip@cnmiplaw.com
scermak@cnmiplaw.com
PTOL-90A (Rev. 04/07)
UNITED STATES PATENT AND TRADEMARK OFFICE
BEFORE THE PATENT TRIAL AND APPEAL BOARD
Ex parte VIT ALIY ARKADYEVICH LIVSHITS,
NATALIAPAVLOVNAZAKATAEVA,
VLADIMIR VENIAMINOVICH ALESHIN,
ALLA V ALENTINOVNA BELAREV A, and
IRINA L YVOVNA TOKHMAKOV A 1
Appeal2018-001581
Application 15/185,371
Technology Center 1600
Before RICHARD M. LEBOVITZ, JEFFREY N. FREDMAN, and
JOHN G. NEW, Administrative Patent Judges.
LEBOVITZ, Administrative Patent Judge.
DECISION ON APPEAL
This appeal involves claims directed to methods for producing amino
acids in Escherichia. The Examiner rejected the claims as lacking written
description and enablement under 35 U.S.C. § 112, as obvious under 35
U.S.C. § 103, and under obviousness-type double-patenting. Pursuant to 35
U.S.C. § 134, Appellant appeals the Examiner's determination that the
claims are unpatentable. We have jurisdiction under 35 U.S.C. § 6(b ). The
Examiner's decision is AFFIRMED.
1 The Appeal Brief ("Br." entered Jun. 2, 2017) lists Ajinomoto Co., Inc., as
the real party in interest.
Appeal2018-001581
Application 15/185,371
STATEMENT OF THE CASE
The Examiner finally rejected the claims as follows:
1. Claims 1-7 under 35 U.S.C. § 112 (pre-AIA), first paragraph, as
failing to comply with the written description requirement. Ans. 2.
2. Claims 2 and 4--6 under 35 U.S.C. § 112 (pre-AIA), first
paragraph, as failing to enable the full scope of the claim. Ans. 13.
3. Claims 1--4 and 7 under 35 U.S.C. § I03(a) as obvious in view of
Debabov et al. (US Patent 4,321,325, issued Mar. 23, 1982) ("Debabov"),
Vrlijc et al. (US Patent 6,858,406 Bl, issued Feb. 22, 2005) ("Vrlijc"), and
Zakataeva et al. (FEES Lett. 452:228-232, 1999) ("Zakataeva"). Ans. 21.
4. Claims 4--7 under 35 U.S.C. § I03(a) as obvious in view of
Nakano et al. (US Patent 5,629,180, issued May 13, 1997) ("Nakano") and
Zakataeva. Ans. 28.
5. Claims 1-7 under the judicially created doctrine of obviousness-
type double-patenting as obvious over claims 1-6 of U.S. Patent 9,394,346
B2, issued Jul. 19, 2016). Ans. 33.
Appellants did not provide arguments as to why the obviousness-type
double-patenting rejection should be reversed. Accordingly, we summarily
affirm the rejection for the reasons set forth by the Examiner. Final Act. 43-
45.
Independent claim 1, which is illustrative of the rejected claims, is
reproduced below:
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Application 15/185,371
1. A method for producing the amino acid L-homoserine or L-
threonine, comprising the steps of:
i) cultivating a bacterium belonging to the genus
Escherichia, which has the ability to produce the amino acid, in
a culture medium, to produce and accumulate the amino acid in
the medium, and
ii) recovering the amino acid from the medium,
wherein L-threonine resistance of said bacterium is
enhanced by increasing the activity of a first protein in said
bacterium as compared to a corresponding wild-type
Escherichia bacterium by increasing the copy number of a
DNA encoding said first protein or replacing a promoter
sequence of said DNA, wherein said first protein is selected
from the group consisting of:
(A) a protein comprising the amino acid sequence shown
in SEQ ID NO: 4; and
(B) a protein comprising the amino acid sequence shown
in SEQ ID NO: 4, but which includes deletion, substitution,
insertion or addition of one amino acid in the amino acid
sequence, and which has the activity of conferring resistance to
L-threonine to the bacterium
wherein the DNA encoding said first protein is selected
from the group consisting of:
(a) a DNA comprising nucleotides 187 to 804 in SEO ID
NO: 3; and
(b) a DNA which hybridizes with the complete
complement of the nucleotide sequence of nucleotides 187 to
804 in SEQ ID NO: 3 under conditions of washing at 60°C, and
at a salt concentration of 1 x SSC and 0.1 % SDS, and wherein
said DNA encodes a protein having the activity of conferring
resistance to L-threonine to the bacterium.
THE CLAIMS
Independent claim 1 is directed to a method for producing the amino
acid L-homoserine or L-threonine. The method comprises cultivating
Escherichia to produce the amino acid. L-threonine resistance is enhanced
in the Escherichia by increasing the activity of:
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Application 15/185,371
(A) a protein comprising the amino acid sequence of SEQ ID NO: 4,
which is encoded by a DNA comprising nucleotides 187 to 804 in SEO ID
NO: 3; or
(B) a protein comprising the amino acid sequence of SEQ ID NO: 4,
"but which includes deletion, substitution, insertion or addition of one amino
acid in the amino acid sequence, and which has the activity of conferring
resistance to L-threonine to the bacterium", and which is encoded by "a
DNA which hybridizes with the complete complement of the nucleotide
sequence of nucleotides 187 to 804 in SEQ ID NO: 3" (emphasis added)
under specifically recited washing conditions.
The activity is increased "by increasing the copy number of a DNA
encoding said first protein or replacing a promoter sequence of said DNA."
SEQ ID NOS: 3 (nucleotide sequence) and 4 (amino acid sequence)
correspond to the rhtC gene which codes for a protein having resistance to
threonine or "Rt" activity. Spec. ,r,r 31, 35, 36, 41.
Independent claim 4 has the same steps as claim 1, but further
comprises cultivating Escherichia to produce an amino acid using an amino
acid sequence of SEQ ID NO: 2. The claim comprises:
(1) utilizing a DNA coding for a protein of SEQ ID NO: 4 or a protein
as in part (B) of claim 1; and
(2) (C) a protein comprising the amino acid sequence shown in SEQ
ID NO: 2 and (D) "a protein comprising the amino acid sequence of SEQ ID
NO: 4, but which includes deletion, substitution, insertion or addition of one
amino acids in the amino acid sequence shown in SEQ ID NO: 2, and which
has the activity of conferring resistance to L-threonine to the bacterium."
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Application 15/185,371
(D), unlike (B) is claim 1, is not limited to hybridization to a DNA
sequence.
SEQ ID NO: 2 corresponds to the rhtB gene and represents a protein
having resistance to L-homoserine or "Rh" activity. Spec. ,r,r 31, 36, 37.
WRITTEN DESCRIPTION REJECTION
The Examiner rejected claims 1-7 under 35 U.S.C. § 112, first
paragraph, as failing to comply with the written description requirement.
Part (B) of claim 1 recites that the protein of SEQ ID NO: 4 (the rhtC
gene) "includes deletion, substitution, insertion or addition of one amino
acid in the amino acid sequence." The claim also recites that the DNA
coding for (B) must be either SEQ ID NO: 3 or a DNA which hybridizes to
it under specific washing conditions. The Examiner found that the term
"includes" is open-ended language that would encompass proteins having
more than one deletion, substitution, etc., of an amino acid. Final Act. 7-8.
The Examiner thus construed the claim scope to include numerous species,
limited only by the ability to confer resistance to L-threonine and to
hybridize to SEQ ID NO: 3.
Independent claim 4 has similar breadth to claim 1, but is directed to
an embodiment utilizing the DNA sequence coding for SEQ ID NO: 2
(protein sequence of the rhtB gene), and amino acid modifications of it.
Claim 4 is does not limit the DNA coding for SEQ ID NO: 2 to DNAs that
hybridize to its coding nucleotide sequence as does claim 1.
Although each of the claims define a genus of rhtC and rhtB proteins,
the Examiner found that the Specification only discloses one representative
species of each, namely an Escherichia coli transformed with vectors
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Application 15/185,371
comprising a DNA coding for the amino acid sequence of SEQ ID NO: 4
and/or SEQ ID NO 2. Final Act. 15-16. The Examiner therefore concluded
that the claimed genus of rhtB and rhtC proteins are not described in the
Specification.
Discussion
35 U.S.C. § 112 requires a patentee to provide a written description of
the claimed subject matter that allows a person of ordinary skill in the art to
recognize that the patentee invented what is claimed. Ariad Pharms., Inc. v.
Eli Lilly & Co., 598 F.3d 1336, 1351 (Fed. Cir. 2010) (en bane). In
University of California v. Eli Lilly & Co. ("Lilly"), 119 F.3d 1559 (Fed. Cir.
1997), the Federal Circuit set forth a test for compliance with the written
description requirement when a genus of recombinant nucleotide sequences
is claimed. In Lilly, only a single cDNA to rat insulin was described in the
patent specification, but the Patentee had claims that covered broader genera
of cDNAs, coding for mammalian and vertebrate insulins, respectively.
Lilly, 119 F.3d at 1563, 1567. In an infringement suit, the validity of these
claims was challenged. The Lilly court held the claims invalid for failing to
provide an adequate written description of the claimed genus. The court
wrote:
In claims to genetic material, however, a generic statement such
as "vertebrate insulin cDNA" or "mammalian insulin cDNA,"
without more, is not an adequate written description of the
genus because it does not distinguish the claimed genus from
others, except by function. It does not specifically define any
of the genes that fall within its definition. It 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.
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Application 15/185,371
Id. at 119 F.3d at 1568.
Consistent with Lilly, it was held in Enzo Biochem, Inc. v. Gen-Probe
Inc., 323 F.3d 956, 964 (Fed. Cir. 2002):
[T]he written description requirement can be met by "show[ing]
that an invention is complete by disclosure of sufficiently
detailed, relevant identifying characteristics ... i.e., complete or
partial structure, other physical and/or chemical properties,
functional characteristics when coupled with a known or
disclosed correlation between function and structure, or some
combination of such characteristics."
In sum, to meet the written description requirement, the Specification
must describe "structural features commonly possessed by members of the
genus that distinguish them from others" (Lilly, 119 F.3d at 1568), such as
"a known or disclosed correlation between function and structure." Enzo
Biochem, 323 F.3d at 964.
In this case, the Specification discloses only a single protein species
for each genus of rhtB and rhtC proteins, namely SEQ ID NOS: 2 and 4,
respectively. A representative number of species for each genus has not
been disclosed. Appellants have provided no guidance on where amino acid
modifications can be made in the protein without destroying its activity.
Appellants have also not described "structural features commonly possessed
by members of the [ claimed] genus [ of rhtB and rhtC proteins] that
distinguish them from others" (Lilly, 119 F.3d at 1568), such as "a known or
disclosed correlation between function [ amino acid efflux] and [protein]
structure." Enzo Biochem, 323 F.3d at 964. Final Act. 17-18. Thus, the
Examiner's decision to reject the claims as lacking a written description is
supported by a preponderance of the evidence.
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Application 15/185,371
Appellants contend that the Examiner misconstrued the claims and
that the claims allow only one amino acid alteration. Br. 8. Appellants
argue:
the current language of the claims omits the phrase 'or several',
the language clearly indicates that only one amino acid can be
altered. If the interpretation as alleged by the Examiner were
adopted, this would be in direct contradiction to the
specification, which states that one or several amino acids can
be altered as alternative embodiments.
Br. 8-9.
During patent examination proceedings, claim terms are given "the
broadest reasonable meaning ... in their ordinary usage as they would be
understood by one of ordinary skill in the art, taking into account whatever
enlightenment by way of definitions or otherwise that may be afforded by
the written description contained in the applicant's specification." In re
Morris, 127 F.3d 1048, 1054 (Fed. Cir. 1997). However, "a particular
embodiment appearing in the written description may not be read into a
claim when the claim language is broader than the embodiment."
SuperGuide Corp. v. DirecTV Enters., Inc., 358 F.3d 870, 875 (Fed. Cir.
2004). Appellants' interpretation improperly attempts to import a limitation
into the claim from the Specification. The claim expressly states "includes,"
which the Examiner interpreted to be open-ended and permit additional
amino acid alterations. Appellants have not explained why this definition is
incorrect. Appellants have also not provided an adequate reason, based on
the actual language in the claim, to interpret "includes deletion, substitution,
insertion or addition of one amino acid in the amino acid sequence" to
exclude more than one amino acid modification when "includes" is
understood to be an open-ended, inclusive term. Had Appellants intended
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Application 15/185,371
the claim to exclude all other amino acid modifications, the claim language
could have been amended to replaced "includes" with "consisting of," or
otherwise made clear by the claim language that only one modification of
the protein sequence is permitted. 2
Even if Appellants' interpretation is adopted, there are still numerous
species encompassed by the claims because a single deletion, substitution,
insertion, or addition of an amino acid could occur anywhere in the
sequence, and comprise any one of the twenty naturally-occurring amino
acids. Yet, as stated above, Appellants have provided no guidance on where
in the protein amino acid modification can be made without destroying its
activity. Appellants have also not described "structural features commonly
possessed by members of the [ claimed] genus [ of rhtB and rhtC proteins]
that distinguish them from others" (Lilly, 119 F.3d at 1568), such as "a
known or disclosed correlation between function and structure." Enzo
Biochem, 323 F.3d at 964.
Appellants argue "that description of a representative number of
species does not require the description to be of such specificity that it would
provide individual support for each species that the genus embraces." Br.
10. However, there is only single species disclosed for each genus. A
representative number has not been disclosed.
2 "[T]he PTO gives a disputed claim term its broadest reasonable
interpretation during patent prosecution .... The 'broadest reasonable
interpretation' rule recognizes that 'before a patent is granted the claims are
readily amended as part of the examination process.' Burlington Indus. v.
Quigg, 822 F.2d 1581, 1583 (Fed. Cir. 1987). Thus, a patent applicant has
the opportunity and responsibility to remove any ambiguity in claim term
meaning by amending the application." In re Bigio, 381 F.3d 1320, 1324
(Fed. Cir. 2004).
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For the foregoing reason, we affirm the Examiner's determination that
claims 1-7 lack a written description as required by 35 U.S.C. § 112, first
paragraph.
ENABLEMENT REJECTION
Claims 2 and 4---6 stand rejected by the Examiner for lack of
enablement. The Examiner states the claims involve expression of both rhtC
(SEQ ID NO: 4) and rhtB (SEQ ID NO: 2). Ans. 14. The Examiner found
the claims do not limit the DNA coding for the amino acid alterations in the
amino acid sequence of SEQ ID NO: 2 to a DNA which hybridizes to SEQ
ID NO: 2 under specific washing conditions and therefore lack enablement
because, without a hybridization restriction, the claim scope "encompass any
conceivable mutants or variants of the amino acid sequence of SEQ ID NO:
2, provided the protein confers the phenotype of resistance to L-
homoserine." Ans. 17.
The Examiner considered the factors set forth in In re Wands, 858
F .2d 731 (Fed. Cir. 1988) for determining whether undue experimentation
was required to enable the full scope of the claims. Final Act. 19-20. After
reviewing all the factors (id. at 20, 23-25), the Examiner determined that
there was "a high level of unpredictability in altering the sequence of SEQ
ID NO: 2" while still "maintaining the desired activity" because of the broad
scope of the claim, the lack of working examples, and the lack of guidance
in what amino acids could be changed while still preserving the protein's
rhtB efflux activity. Final Act. 25.
Appellants do not identify a deficiency in the Examiner's findings nor
reasoning. Instead, Appellants contend, as they did in the written
description rejection, that the Examiner misconstrued the claim scope and
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Application 15/185,371
that they are limited to alterations of only one amino acid at a time. Br. 11.
For the reasons already discussed, this interpretation is not the broadest
reasonable interpretation of the claim language.
In sum, for the reasons set forth by the Examiner, the enablement
rejection of claims 2 and 4---6 are affirmed.
OBVIOUSNESS REJECTION BASED ON DEBABOV, VRLIJC, AND
ZAKATAEVA
The Examiner found that Debabov describes a method for producing
L-threonine in Escherichia. Final Act. 32. The Examiner found that
Debabov differs from the claim method in not over-expressing "a DNA
encoding a threonine efflux protein of SEQ ID NO: 4." Id. The Examiner
found that Vrlijc describes "enhancing expression of an L-amino acid export
[efflux] polypeptide for improving L-amino acid production," but not the
claimed threonine efflux protein of SEQ ID NO: 4. Id. at 33. However, the
Examiner found that Zakataeva describes the rhtB and rhtC genes of E. coli
that encode amino acid efflux proteins and confer resistance to homoserine
and threonine, respectively. Id. at 33-34. The Examiner recognized that
Zakataeva does not expressly disclose SEQ ID NO: 4, but found that the
Specification discloses that SEQ ID NO: 4 corresponds to the rhtC gene, the
same gene described in Zakataeva. Id. at 34. The Examiner determined that
Vrlijc provides the reason to have used the rhtC amino acid efflux gene of
Zakataeva in Debabov's method because Vrlijc teaches that increased
expression of L-amino acid exporters result in increased accumulation of the
amino acid in culture medium. Id. at 33.
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Appellants contend that "none of the references disclose or suggest ...
[the rhtC gene's], or the encoded protein's, involvement in the increased
production of amino acids, including L-threonine." Br. 12. Further,
Appellants argue:
[T]here is no teaching of the production of L-amino acids using
the rhtC gene, nor that such production can be increased by
increasing expression of this gene. Therefore, there is no
motivation or reason to combine these references with each
other. It certainly could not have been obvious to use the gene
of Zakataeva in an effort to increase amino acid production
since there is no suggestion or teaching of this function of the
specific claimed sequence.
Br. 13.
This argument does not persuade us the Examiner erred in rejecting
the claims as obvious. The Examiner set forth a detailed and well-reasoned
explanation as to why the claimed method would have been obvious to one
of ordinary skill in the art. Final Act. 32-37. Specifically, while there is no
teaching of utilizing the claimed rhtC gene sequence to increase threonine
production, the Examiner cited Vrlijc as a reason to have used the gene for
this purpose.
Vrlijc describes the microbial production of amino acid. Vrlijc 1: 10-
15. Vrlijc describes efforts to increase amino acid production by bacteria.
Id. at 2:8-10. Vrlijc, as found by the Examiner (Final Act. 33), teaches that
improving amino acid export is one approach to increasing amino acid
production:
However, as a further limitation basically also the export of the
amino acids formed in the interior of a cell into the culture
medium should be taken into consideration. As a result, it has
been tried to improve this export and, consequently, the
efficiency of the amino acid production.
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Application 15/185,371
Vrlijc 2:10-13 (emphasis added).
Vrlijc acknowledges:
Altogether, the attempts to increase the secretion of amino-
acids formed within the cell have all in common that an
increase ejjlux of amino acids on the basis of the selected non-
directed and non-specific methods could be achieved only
accidentally.
Vrlijc 2:25-29 ( emphasis added).
However, Vrlijc addressed this problem in a directed way by
identifying a gene responsible for amino acid export and found that its
increased expression resulted in increased accumulation of the exported
amino acid in the medium:
It has now been found surprisingly that only a single specific
gene is responsible for the export of amino acids so that, in
accordance with the invention, for the first time a method for
the microbial manufacture of amino acids is provided wherein
clearly the export gene expression and/or the export carrier
activity of a microorganism producing amino acids is increased.
The increased export expression or respectively, activity of the
export carrier resulting from this process leads to an increased
secretion rate so that the export of the respective amino acid is
increased. The microorganisms so modified also accumulate an
increased part of the respective amino acid in the culture
medium.
Vrlijc 2:62-3:6.
Zakataeva teaches that the product of the rhtC gene, the same gene
which is claimed, provides resistance to threonine (Abstract) and "conducts
the efflux of threonine" (Zakataeva 228, col. 2). Thus, as found by the
Examiner, Vrlijc's teaching that an increase in amino acid ejjlux using an
amino export carrier provides strong reason to have used the rhtC ejjlux
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gene of Zakataeva to improve amino acid production. Appellants do not
identify a defect in the Examiner's factual findings or reasoning.
Appellants' contention that it would not have been obvious "to use the
gene of Zakataeva in an effort to increase amino acid production since there
is no suggestion or teaching of this function of the specific claimed
sequence" (Br. 13) is not persuasive because Zakataeva describes the
function of the gene ("conducts the efflux of threonine") and the gene has
the same sequence as the clamed SEQ NO: 4. Specifically, the Specification
discloses that SEQ ID NO: 4 is derived from GenBank accession number
M87049. Spec. ,r 41. Zakataeva teaches the same accession number.
Zakataeva 229 (Section 3.1). Appellants' argument regarding the failure of
Vrlijc to disclose the claimed sequence (Br. 12) ignores that Zakataeva
discloses a clone having the same sequence as claimed.
Appellants contend that "there is no evidence that the sequence taught
by Zakataeva would function if expressed, nor what its function would be,
other than generally involved in efflux, which is very different from
production of amino acids which involves complex metabolic pathways."
Br. 13. This argument is not supported by persuasive evidence. First, as
explained above, Zakataeva expressly teaches that "the product of the rhtC
gene conducts the efflux of threonine" (Zakataeva 228 (in section titled
"Introduction"). Second, Vrlijc teaches that an amino acid exporter
improved amino acid production, providing a reasonable expectation that the
rhtC gene, which has the same basic function of the gene in Zakataeva,
would likewise improve production of threonine. Appellants have not
provided adequate evidence to the contrary, nor a reason why one of
ordinary skill in the art would have doubted that the gene described in
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Zakataeva would increase amino acid production when expressed in
Escherichia.
For the foregoing reasons, the rejection of claim 1 is affirmed. Claims
2--4 and 7 fall with claim 1 because separate reason for their patentability
were not provided. 37 C.F.R. § 4I.37(c)(iv)(l).
OBVIOUSNESS REJECTION BASED ON
NAKANOANDZAKATAEVA
The Examiner rejected claims 4--7 as obvious in view of Nakano and
Zakataeva. Independent claim 4 is similar to claim 1, but in addition to the
requirement that L-threonine resistance is enhanced utilizing SEQ ID NO: 4,
further requires enhanced L-homoserine resistance utilizing SEQ ID NO: 2.
The Examiner found Nakano describes a method for producing L-amino
acids in Escherichia. Final Act. 39. The Examiner recognized that Nakano
does not teach "overexpress[ing] a DNA encoding a protein comprising the
amino acid sequence of SEQ ID N0:4 and a DNA encoding a protein
comprising the amino acid sequence of SEQ ID NO: 2" as required by claim
4. Id. at 39--40. The Examiner cited Zakataeva for teaching the rhtB and
rhtC genes which have the same sequences recited in the claims. Id. at 40.
The Examiner determined it would have been obvious to one of ordinary
skill in the art to have utilized the rhtB and rhtC genes in Nakano's method
to "avoid suppressing growth of the E. coli because Zakataeva teaches that
exogenetic [exogenous] homo serine and threonine suppress growth of E.
coli in a nutritional medium and rhtB and rhtC genes of E. coli confer
resistance to homo serine and threonine." Id. at 41.
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Appellants contend that Zakataeva is deficient for the same reasons
already argued in the first rejection. Br. 14. Accordingly, the rejection of
claim 4 is affirmed for reasons set forth above and those set forth by the
Examiner (Final Act. 37--42; Ans. 28-33). Claims 5-7 fall with claim 4
because separate reason for their patentability were not provided. 37 C.F.R.
§ 4I.37(c)(iv)(l).
TIME PERIOD
No time period for taking any subsequent action in connection with
this appeal may be extended under 37 C.F.R. § 1.136(a)(l)(iv).
AFFIRMED
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