(en)A novel bacteriophage RM 378 of Rhodothermus marinus, the nucleic acids of its genome, nucleic acids comprising nucleotide sequences of open reading frames (ORFs) of its genome, and polypeptides encoded by the nucleic acids, are described.

1.ApplicationNumber: US-27071002-A
1.PublishNumber: US-2003092128-A1
2.Date Publish: 20030515
3.Inventor: HJORLEIFSDOTTIR SIGRIDUR
HREGGVIDSSON GUDMUNDUR O.
FRIDJONSSON OLAFUR H.
AEVARSSON ARNTHOR
KRISTJANSSON JAKOB K.

4.Inventor Harmonized: HJORLEIFSDOTTIR SIGRIDUR(IS)
HREGGVIDSSON GUDMUNDUR O(IS)
FRIDJONSSON OLAFUR H(IS)
AEVARSSON ARNTHOR(IS)
KRISTJANSSON JAKOB K(IS)

5.Country: US
6.Claims:
(en)A novel bacteriophage RM 378 of Rhodothermus marinus, the nucleic acids of its genome, nucleic acids comprising nucleotide sequences of open reading frames (ORFs) of its genome, and polypeptides encoded by the nucleic acids, are described.

7.Description:
(en)RELATED APPLICATIONS
[0001] This application is a Divisional of U.S. application Ser. No.: 09/585,858, filed Jun. 1, 2000, which claims the benefit of U.S. Provisional Application No. 60/137,120, filed Jun. 2, 1999, the entire teachings of which are incorporated herein by reference. Five separate divisional applications are being filed concurrently herewith.



BACKGROUND OF THE INVENTION
[0002] The use of thermophilic enzymes has revolutionized the field of recombinant DNA technology. Polymerases (DNA and RNA), ligases, exonucleases, reverse transcriptases, polynucleotide kinases and lysozymes, as well as many other thermophilic enzymes, are of great importance in the research industry today. In addition, thermophilic enzymes are also used in commercial settings (e.g., proteases and lipases used in washing powder, hydrolidic enzymes used in bleaching). Identification of new thermophilic enzymes will facilitate continued DNA research as well as assist in improving commercial enzyme-based products.
SUMMARY OF THE INVENTION
[0003] This invention pertains to a novel bacteriophage of Rhodothermus marinus, bacteriophage RM 378, which can be isolated from its native environment or can be recombinantly produced. The invention additionally pertains to the nucleic acids of the genome of bacteriophage RM 378 as deposited, as well as to the nucleic acids of a portion of the genome of bacteriophage RM 378 as shown in FIG. 1; to isolated nucleic acid molecules containing a nucleotide sequence of an open reading frame (or more than one open reading frame) of the genome of bacteriophage RM 378, such as an open reading frame as set forth in FIG. 2; to isolated nucleic acid molecules encoding a polypeptide obtainable from bacteriophage RM 378 or an active derivative or fragment of the polypeptide (e.g., a DNA polymerase, such as a DNA polymerase lacking exonuclease domains; a 3′-5′ exonuclease, such as a 3′-5′ exonuclease lacking DNA polymerase domain; a 5′-3′ exonuclease (RNase H); a DNA helicase; or an RNA ligase); to DNA constructs containing the isolated nucleic acid molecule operatively linked to a regulatory sequence; and also to host cells comprising the DNA constructs. The invention further pertains to isolated polypeptides encoded by these nucleic acids, as well as active derivatives or fragments of the polypeptides.
[0004] Because the host organism of the RM 378 bacteriophage is a thermophile, the enzymes and proteins of the RM 378 bacteriophage are expected to be significantly more thermostable than those of other (e.g., mesophilic) bacteriophages, such as the T4 bacteriophage of Escherichia coli. The enhanced stability of the enzymes and proteins of RM 378 bacteriophage allows their use under temperature conditions which would be prohibitive for other enzymes, thereby increasing the range of conditions which can be employed not only in DNA research but also in commercial settings.



BRIEF DESCRIPTION OF THE DRAWINGS
[0005] FIGS. 1 A- 1 Q 2 are a depiction of the nucleic acid sequence (SEQ ID NO:1) of the genome of bacteriophage RM 378.
[0006] FIGS. 2 A- 2 C delineate the open reading frames (ORFs) in the genome of bacteriophage RM 378.
[0007] FIGS. 3 A- 3 W depict a sequence alignment of the predicted gene products of ORF056e and ORF632e and sequences of DNA polymerases of family B. The sequence marked RM378 (SEQ ID NO:36) is the combined sequences of the gene products of ORF056e and ORF632e in bacteriophage RM378. The end of one sequence and the beginning of another is indicated. Other sequences are: Vaccinia virus (strain Copenhagen) DNA polymerase (DPOL_VACCC) (SEQ ID NO:2); Vaccinia virus (strain WR) DNA polymerase (DPOL_V ACCV) (SEQ ID NO:3); Variola virus DNA polymerase (DPOL_VARV) (SEQ ID NO:4); Fowlpox virus DNA polymerase (DPOL_FOWPV) (SEQ ID NO:5); Bos taurus (Bovine) DNA polymerase delta catalytic chain (DPOD_BOVIN) (SEQ ID NO:6); Human DNA polymerase delta catalytic chain (DPOD_HUMAN) (SEQ ID NO:7); Candida albicans (Yeast) DNA polymerase delta large chain (DPOD_CANAL) (SEQ ID NO:8); Saccharomyces cerevisiae DNA polymerase delta large chain (DPOD_YEAST) (SEQ ID NO:9); Schizosaccharomyces pombe DNA polymerase delta large chain (DPOD_SCHPO) (SEQ ID NO:10); Plasmodium falciparum DNA polymerase delta catalytic chain (DPOD_PLAFK) (SEQ ID NO:11); Chlorella virus NY-2A DNA polymerase (DPOL_CHVN2) (SEQ ID NO:12); Paramecium bursaria chlorella virus 1 DNA polymerase (DPOL_CHVP1) (SEQ ID NO:13); Epstein-barr virus (strain B95-8) DNA polymerase (DPOL_EBV) (SEQ ID NO:14); Herpesvirus saimiri (strain 11) DNA polymerase (DPOL_HSVSA) (SEQ ID NO:15); Herpes simplex virus (type 1/strain 17) DNA polymerase (DPOL_HSV11) (SEQ ID NO:16); Herpes simplex virus (type 2/strain 186) DNA polymerase (DPOL_HSV21) (SEQ ID NO:17); Equine herpesvirus type 1 (strain Ab4p) (EHV-1) DNA polymerase (DPOL_HSVEB) (SEQ ID NO:18); Varicella - zoster virus (strain Dumas) (VZV) DNA polymerase (DPOL_VZVD) (SEQ ID NO:19); Human cytomegalovirus (strain AD 169) DNA polymerase (DPOL_HCMVA) (SEQ ID NO:20); Murine cytomegalovirus (strain Smith) DNA polymerase (DPOL_MCMVS) (SEQ ID NO:21); Herpes simplex virus (type 6/strain Uganda-1102) DNA polymerase (DPOL_HSV6U) (SEQ ID NO:22); Human DNA polymerase alpha catalytic subunit (DPOA_HUMAN) (SEQ ID NO:23); Mouse DNA polymerase alpha catalytic subunit (DPOA_MOUSE) (SEQ ID NO:24); Drosophila melanogaster DNA polymerase alpha catalytic subunit (DPOA_DROME) (SEQ ID NO:25); Schizosaccharomyces pombe DNA polymerase alpha catalytic subunit (DPOA SCHPO) (SEQ ID NO:26); Saccharomyces cerevisiae DNA polymerase alpha catalytic subunit (DPOA_YEAST) (SEQ ID NO:27); Trypanosoma brucei DNA polymerase alpha catalytic subunit (DPOA_TRYBB) (SEQ ID NO:28); Autographa californica nuclear polyhedrosis virus DNA polymerase (DPOL_NPVAC) (SEQ ID NO:29); Lymantria dispar multicapsid nuclear polyhedrosis virus DNA polymerase (DPOL_NPVLD) (SEQ ID NO:30); Saccharomyces cerevisiae DNA polymerase zeta catalytic subunit (DPOZ_YEAST) (SEQ ID NO:31); Pyrococcus woesei DNA polymerase (DPOL_PYRFU) (SEQ ID NO:32);. Sulfolobus solfataricus DNA polymerase I (DPO1_SULSO) (SEQ ID NO:33); Escherichia coli DNA polymerase II (DPO2_ECOLI) (SEQ ID NO:34); Desilforococcus strain Tok DNA polymerase (Dpol_Dtok) (SEQ ID NO:35); and bacteriophage RB69 DNA polymerase (RB69) (SEQ ID NO:37). Most of the sequences are partial as found in the Protein Families Data Base of Alignments and HMMs (Sanger Institute), family DNA_pol_B, accession no. PF00136.
[0008]FIG. 4 depicts a sequence alignment of the predicted gene product of ORF739f from bacteriophage RM378 (ORF-739f) (SEQ ID NO:40), Autographa californica nucleopolyhedrovirus putative bifunctional polynucleotide kinase and RNA ligase (ACNV-RNAlig) (SEQ ID NO:38); and bacteriophage T4 RNA ligase (T4-RNAlig) (SEQ ID NO:39).
[0009]FIG. 5 depicts a sequence alignment of the predicted gene product of ORF1218a from bacteriophage RM378 (ORF-1218a) (SEQ ID NO:43) with proteins or domains with 5′-3′ exonuclease activity, including: Escherichia coli DNA polymerase I (Ecoli-polI) (SEQ ID NO:41), Thermus aquaticus DNA polymerase I (Taq-polI) (SEQ ID NO:42), bacteriophage T4 ribonuclease H (T4-RNaseH) (SEQ ID NO:44) and bacteriophage T7 gene6 exonuclease (T7-gp6exo) (SEQ ID NO:45). Conservation of acidic residues mainly clustered at the proposed active site are seen.
[0010] FIGS. 6 A- 6 B depict a sequence alignment of the predicted gene product of ORF1293b (SEQ ID NO:55) from bacteriophage RM378 (ORF1293b) with sequences of replicative DNA helicases of the DnaB family, including: Escherichia coli (DnaB-Ecoli) (SEQ ID NO:46), Haemophilus influenza (DnaB-Hinflu) (SEQ ID NO:47), Chlamydomonas trachomatis (DnaB-Ctracho) (SEQ ID NO:48), Bacillus stearothermophilus (DnaB-Bstearo) (SEQ ID NO:49), Halobacter pylori (DnaB-Hpylor) (SEQ ID NO:50), Mycoplasma genitalium (DnaB-Mgenital) (SEQ ID NO:51), Borrelia burgdorferi (DnaB-Bburgdor) (SEQ ID NO:52), bacteriophage T4 gene 41 (T4-gp41) (SEQ ID NO:53), bacteriophage T7 gene 4 (T7-gp4) (SEQ ID NO:54) (from the Protein Families Data Base of Alignments and HMMS (Sanger Institute), family DnaB, accession no. PF00772). The sequences have been truncated at the N-termini, and conserved sequence motifs are indicated.
[0011] FIGS. 7 A- 7 B depict the nucleic acid sequence of open reading frame ORF 056e (nucleotides 21993-23042 of the genome) (SEQ ID NO:56) with flanking sequences, and the putative encoded polypeptide (SEQ ID NO:57) which displays amino acid sequence similarity to polymerase 3′-5′ exonucleases.
[0012] FIGS. 8 A- 8 B depict the nucleic acid sequence of open reading frame ORF 632e (nucleotides 79584-81152 of the genome) (SEQ ID NO:58) with flanking sequences, and the putative encoded polypeptide (SEQ ID NO:59) which displays amino acid sequence similarity to polymerases.
[0013] FIGS. 9 A- 9 B depict the nucleic acid sequence of open reading frame ORF 739f (nucleotides 90291-91607 of the genome) (SEQ ID NO:60) with flanking sequences, and the putative encoded polypeptide (SEQ ID NO:40) which displays amino acid sequence similarity to RNA ligase.
[0014] FIGS. 10 A- 10 B depict the nucleic acid sequence of open reading frame ORF 1218a (nucleotides 8212-9168 of the genome) (SEQ ID NO:61) with flanking sequences, and the putative encoded polypeptide (SEQ ID NO:43) which displays amino acid sequence similarity to 5′-3′ exonuclease of DNA polymerase I and T4 RNase H.
[0015] FIGS. 11 A- 11 B depict the nucleic acid sequence of open reading frame ORF 1293b (nucleotides 15785-17035 of the genome) (SEQ ID NO:62) with flanking sequences, and the putative encoded polypeptide (SEQ ID NO:55) which displays amino acid sequence similarity to T4 DNA helicase.


DETAILED DESCRIPTION OF THE INVENTION
[0016] The present invention relates to a bacteriophage, the nucleic acid sequence of the bacteriophage genome as well as portions of the nucleic acid sequence of the bacteriophage genome (e.g., a portion containing an open reading frame), and proteins encoded by the nucleic acid sequences, as well as nucleic acid constructs comprising portions of the nucleic acid sequence of the bacteriophage genome, and host cells comprising such nucleic acid constructs. As described herein, Applicants have isolated and characterized a novel bacteriophage active against the slightly halophilic, thermophilic eubacterium Rhodothermus marinus. The bacteriophage, RM 378, is a member of the Myoviridae family, with an A2 morphology. RM 378, which is completely stable up to about 65° C., appears to consist of approximately 16 proteins with one major protein of molecular weight of 61,000 daltons. RM 378 can be replicated in Rhodothermus marinus species ITI 378.
Rhodothermus marinus ITI 378
[0017] Accordingly, one embodiment of the invention is the bacterium, Rhodothermus marinus species ITI 378. Rhodothermus marinus, and particularly species ITI 378, can be cultured in a suitable medium, such as medium 162 for Thermus as described by Degryse et al. ( Arch. Microbiol. 117:189-196 (1978)), with {fraction (1/10)} buffer and with 1% NaCl. Rhodothermus marinus species ITI 378 can be used in replication of bacteriophage RM 378, as described herein, or in replication or identification of other bacteriophages, particularly thermophilic bacteriophages. Rhodothermus marinus species ITI 378 can also used in the study of the relationship between the bacteriophages and their host cells (e.g., between bacteriophage RM 378 and Rhodothermus marinus species ITI 378).
Bacteriophage RM 378
[0018] Another embodiment of the invention is isolated RM 378 bacteriophage. “Isolated” RM 378 bacteriophage refers to bacteriophage that has been separated, partially or totally, from its native environment (e.g., separated from Rhodothermus marinus host cells) (“native bacteriophage”), and also refers to bacteriophage that has been chemically synthesized or recombinantly produced (“recombinant bacteriophage”). A bacteriophage that has been “recombinantly produced” refers to a bacteriophage that has been manufactured using recombinant DNA technology, such as by inserting the bacteriophage genome into an appropriate host cell (e.g., by introducing the genome itself into a host cell, or by incorporating the genome into a vector, which is then introduced into the host cell).
[0019] Isolated bacteriophage RM 378 can be used in the study of the relationship between the bacteriophages and their host cells (e.g., Rhodothermus marinus, such as Rhodothermus marinus species ITI 378). Isolated bacteriophage RM 378 can also be used as a vector to deliver nucleic acids to a host cell; that is, the bacteriophage can be modified to deliver nucleic acids comprising a gene from an organism other than the bacteriophage (a “foreign” gene). For example, nucleic acids encoding a polypeptide (e.g., an enzyme or pharmaceutical peptide) can be inserted into the genome of bacteriophage RM 378, using standard techniques. The resultant modified bacteriophage can be then used to infect host cells, and the protein encoded by the foreign nucleic acids can then be produced.
[0020] Bacteriophage RM 378 can be produced by inoculating appropriate host cells with the bacteriophage. Representative host cells in which the bacteriophage can replicate include Rhodothermus marinus, particularly species isolated in a location that is geographically similar to the location where bacteriophage RM 378 was isolated (e.g., northwest Iceland). In a preferred embodiment, the host cell is Rhodothermus marinus species ITI 378. The host cells are cultured in a suitable medium (e.g., medium 162 for Thermus as described by Degryse et al., Arch. Microbiol. 117:189-196 (1978), with {fraction (1/10)} buffer and with 1% NaCl). In addition, the host cells are cultured under conditions suitable for replication of the bacteriophage. For example, in a preferred embodiment, the host cells are cultured at a temperature of at least approximately 50° C. In a more preferred embodiment, the host cells are cultured at a temperature between about 50° C. and about 80° C. The bacteriophage can also be stored in a cell lysate at about 4° C.
Nucleic Acids of the Invention
[0021] Another embodiment of the invention pertains to isolated nucleic acid sequences obtainable from the genome of bacteriophage RM 378. As described herein, approximately 130 kB of the genome of bacteriophage RM 378 have been sequenced. The sequence of this 130 kB is set forth in FIG. 1. There are at least approximately 200 open reading frames (ORFs) in the sequence; of these, at least approximately 120 putatively encode a polypeptide of 100 amino acids in length or longer. These 120 are set forth in FIG. 2. FIG. 2 sets forth the locus of each ORF; the start and stop nucleotides in the sequence of each ORF; the number of nucleotides in the ORF, and the expected number of amino acids encoded therein; the direction of the ORF; the identity of the putative protein encoded therein; the protein identified by a BLAST search as being the closest match to the putative protein; the percentage identity at the amino acid level of the putative protein (based on partial sequence similarity; the overall similarity is lower); the organism from which the closest matching protein is derived; and other information relating to the ORFs.
[0022] The invention thus pertains to isolated nucleic acid sequence of the genome (“isolated genomic DNA”) of the bacteriophage RM 378 that has been deposited with the Deutsche Sammlung Von Mikroorganismen und Zellkulturen GmbH (DSMZ) as described below. The invention also pertains to isolated nucleic acid sequence of the genome of bacteriophage RM 378 as is shown in FIG. 1 (SEQ ID NO:1).
[0023] The invention additionally pertains to isolated nucleic acid molecules comprising the nucleotide sequences of each of the ORFs described above or fragments thereof, as well as nucleic acid molecules comprising nucleotide sequences of more than one of the ORFs described above or fragments of more than one of the ORFs. The nucleic acid molecules of the invention can be DNA, or can also be RNA, for example, mRNA. DNA molecules can be double-stranded or single-stranded; single stranded RNA or DNA can be either the coding, or sense, strand or the non-coding, or antisense, strand. Preferably, the nucleic acid molecule comprises at least about 100 nucleotides, more preferably at least about 150 nucleotides, and even more preferably at least about 200 nucleotides. The nucleotide sequence can be only that which encodes at least a fragment of the amino acid sequence of a polypeptide; alternatively, the nucleotide sequence can include at least a fragment of a coding sequence along with additional non-coding sequences such as non-coding 3′ and 5′ sequences (including regulatory sequences, for example).
[0024] In certain preferred embodiments, the nucleotide sequence comprises one of the following ORFs: ORF 056e, 632e, 739f, 1218a, 1293b. For example, the nucleotide sequence can consist essentially of one of the ORFs and its flanking sequences, such as are shown in FIGS. 7 - 11 (e.g., ORF 056e (SEQ ID NO:56), 632e (SEQ ID NO:58), 739f (SEQ ID NO:60), 1218a (SEQ ID NO:61), 1293b (SEQ ID NO:62)).
[0025] Additionally, the nucleotide sequence(s) can be fused to a marker sequence, for example, a sequence which encodes a polypeptide to assist in isolation or purification of the polypeptide. Representative sequences include, but are not limited to, those which encode a glutathione-S-transferase (GST) fusion protein. In one embodiment, the nucleotide sequence contains a single ORF in its entirety (e.g., encoding a polypeptide, as described below); or contains a nucleotide sequence encoding an active derivative or active fragment of the polypeptide; or encodes a polypeptide which has substantial sequence identity to the polypeptides described herein. In a preferred embodiment, the nucleic acid encodes a polymerase (e.g., DNA polymerase); DNA polymerase accessory protein; dsDNA binding protein; deoxyribonucleotide-3-phosphatase; DNA topoisomerase; DNA helicase; an exonuclease (e.g., 3′-5′ exonuclease, 5′-3′ exonuclease (RNase H)); RNA ligase; site-specific RNase inhibitor of protease; endonuclease; exonuclease; mobility nuclease; reverse transcriptase; single-stranded binding protein; endolysin; lysozyme; helicase; alpha-glucosyltransferase; or thymidine kinase, as described herein. In a particularly preferred embodiment, the nucleic acid encodes a DNA polymerase, 3′-5′ exonuclease, 5′-3 exonuclease (RNase H), DNA helicase or RNA ligase. In another particularly preferred embodiment, the nucleic acid encodes a DNA polymerase that lacks exonuclease domains, or a 3′-5′ exonuclease that lacks DNA polymerase domain, as described below.
[0026] The nucleic acid molecules of the invention are “isolated;” as used herein, an “isolated” nucleic acid molecule or nucleotide sequence is intended to mean a nucleic acid molecule or nucleotide sequence which is not flanked by nucleotide sequences which normally (in nature) flank the gene or nucleotide sequence (as in genomic sequences) and/or has been completely or partially purified from other transcribed sequences (e.g., as in an RNA library). For example, an isolated nucleic acid of the invention may be substantially isolated with respect to the complex cellular milieu in which it naturally occurs. In some instances, the isolated material will form part of a composition (for example, a crude extract containing other substances), buffer system or reagent mix. In other circumstance, the material may be purified to essential homogeneity, for example as determined by PAGE or column chromatography such as HPLC. Thus, an isolated nucleic acid molecule or nucleotide sequence can include a nucleic acid molecule or nucleotide sequence which is synthesized chemically or by recombinant means. Therefore, recombinant DNA contained in a vector are included in the definition of “isolated” as used herein. Also, isolated nucleotide sequences include recombinant DNA molecules in heterologous organisms, as well as partially or substantially purified DNA molecules in solution. In vivo and in vitro RNA transcripts of the DNA molecules of the present invention are also encompassed by “isolated” nucleotide sequences.
[0027] The present invention also pertains to nucleotide sequences which are not necessarily found in nature but which encode the polypeptides described below. Thus, DNA molecules which comprise a sequence which is different from the naturally-occurring nucleotide sequence but which, due to the degeneracy of the genetic code, encode the polypeptides of the present invention are the subject of this invention. The invention also encompasses variations of the nucleotide sequences of the invention, such as those encoding active fragments or active derivatives of the polypeptides as described below. Such variations can be naturally-occurring, or non-naturally-occurring, such as those induced by various mutagens and mutagenic processes. Intended variations include, but are not limited to, addition, deletion and substitution of one or more nucleotides which can result in conservative or non-conservative amino acid changes, including additions and deletions. Preferably, the nucleotide or amino acid variations are silent or conserved; that is, they do not alter the characteristics or activity of the encoded polypeptide.
[0028] The invention described herein also relates to fragments of the isolated nucleic acid molecules described herein. The term “fragment” is intended to encompass a portion of a nucleotide sequence described herein which is from at least about 25 contiguous nucleotides to at least about 50 contiguous nucleotides or longer in length; such fragments are useful as probes and also as primers. Particularly preferred primers and probes selectively hybridize to the nucleic acid molecule encoding the polypeptides described herein. For example, fragments which encode polypeptides that retain activity, as described below, are particularly useful.
[0029] The invention also pertains to nucleic acid molecules which hybridize under high stringency hybridization conditions, such as for selective hybridization, to a nucleotide sequence described herein (e.g., nucleic acid molecules which specifically hybridize to a nucleotide sequence encoding polypeptides described herein, and, optionally, have an activity of the polypeptide). Hybridization probes are oligonucleotides which bind in a base-specific manner to a complementary strand of nucleic acid. Suitable probes include polypeptide nucleic acids, as described in (Nielsen et al., Science 254, 1497-1500 (1991)).
[0030] Such nucleic acid molecules can be detected and/or isolated by specific hybridization (e.g., under high stringency conditions). “Stringency conditions” for hybridization is a term of art which refers to the incubation and wash conditions, e.g., conditions of temperature and buffer concentration, which permit hybridization of a particular nucleic acid to a second nucleic acid; the first nucleic acid may be perfectly (i.e., 100%) complementary to the second, or the first and second may share some degree of complementarity which is less than perfect (e.g., 60%, 75%, 85%, 95%). For example, certain high stringency conditions can be used which distinguish perfectly complementary nucleic acids from those of less complementarity.
[0031] “High stringency conditions”, “moderate stringency conditions” and “low stringency conditions” for nucleic acid hybridizations are explained on pages 2.10.1-2.10.16 and pages 6.3.1-6 in Current Protocols in Molecular Biology (Ausubel, F. M. et al., “ Current Protocols in Molecular Biology”, John Wiley & Sons, (1998)) the teachings of which are hereby incorporated by reference. The exact conditions which determine the stringency of hybridization depend not only on ionic strength (e.g., 0.2×SSC, 0.1×SSC), temperature (e.g., room temperature, 42° C., 68° C.) and the concentration of destabilizing agents such as formamide or denaturing agents such as SDS, but also on factors such as the length of the nucleic acid sequence, base composition, percent mismatch between hybridizing sequences and the frequency of occurrence of subsets of that sequence within other non-identical sequences. Thus, high, moderate or low stringency conditions can be determined empirically.
[0032] By varying hybridization conditions from a level of stringency at which no hybridization occurs to a level at which hybridization is first observed, conditions which will allow a given sequence to hybridize (e.g., selectively) with the most similar sequences in the sample can be determined.
[0033] Exemplary conditions are described in Krause, M. H. and S. A. Aaronson, Methods in Enzymology, 200:546-556 (1991). Also, in, Ausubel, et al., “ Current Protocols in Molecular Biology”, John Wiley & Sons, (1998), which describes the determination of washing conditions for moderate or low stringency conditions. Washing is the step in which conditions are usually set so as to determine a minimum level of complementarity of the hybrids. Generally, starting from the lowest temperature at which only homologous hybridization occurs, each ° C. by which the final wash temperature is reduced (holding SSC concentration constant) allows an increase by 1% in the maximum extent of mismatching among the sequences that hybridize. Generally, doubling the concentration of SSC results in an increase in T m of ˜17° C. Using these guidelines, the washing temperature can be determined empirically for high, moderate or low stringency, depending on the level of mismatch sought.
[0034] For example, a low stringency wash can comprise washing in a solution containing 0.2×SSC/0.1% SDS for 10 min at room temperature; a moderate stringency wash can comprise washing in a prewarmed solution (42° C.) solution containing 0.2×SSC/0.1% SDS for 15 min at 42° C.; and a high stringency wash can comprise washing in prewarmed (68° C.) solution containing 0.1×SSC/0.1%SDS for 15 min at 68° C. Furthermore, washes can be performed repeatedly or sequentially to obtain a desired result as known in the art.
[0035] Equivalent conditions can be determined by varying one or more of the parameters given as an example, as known in the art, while maintaining a similar degree of identity or similarity between the target nucleic acid molecule and the primer or probe used. Hybridizable nucleic acid molecules are useful as probes and primers, e.g., for diagnostic applications.
[0036] Such hybridizable nucleotide sequences are useful as probes and primers for diagnostic applications. As used herein, the term “primer” refers to a single-stranded oligonucleotide which acts as a point of initiation of template-directed DNA synthesis under appropriate conditions (e.g., in the presence of four different nucleoside triphosphates and an agent for polymerization, such as, DNA or RNA polymerase or reverse transcriptase) in an appropriate buffer and at a suitable temperature. The appropriate length of a primer depends on the intended use of the primer, but typically ranges from 15 to 30 nucleotides. Short primer molecules generally require cooler temperatures to form sufficiently stable hybrid complexes with the template. A primer need not reflect the exact sequence of the template, but must be sufficiently complementary to hybridize with a template. The term “primer site” refers to the area of the target DNA to which a primer hybridizes. The term “primer pair” refers to a set of primers including a 5′ (upstream) primer that hybridizes with the 5′ end of the DNA sequence to be amplified and a 3′ (downstream) primer that hybridizes with the complement of the 3′ end of the sequence to be amplified.
[0037] The invention also pertains to nucleotide sequences which have a substantial identity with the nucleotide sequences described herein; particularly preferred are nucleotide sequences which have at least about 10%, preferably at least about 20%, more preferably at least about 30%, more preferably at least about 40%, even more preferably at least about 50%, yet more preferably at least about 70%, still more preferably at least about 80%, and even more preferably at least about 90% identity, with nucleotide sequences described herein. Particularly preferred in this instance are nucleotide sequences encoding polypeptides having an activity of a polypeptide described herein. For example, in one embodiment, the nucleotide sequence encodes a DNA polymerase, 3′-5′ exonuclease, 5′-3′ exonuclease (RNase H), DNA helicase, or RNA ligase, as described below. In a preferred embodiment, the nucleotide encodes a DNA polymerase lacking exonuclease domains, or a 3′-5′ exonuclease lacking DNA polymerase domain, as described below.
[0038] To determine the percent identity of two nucleotide sequences, the sequences are aligned for optimal comparison purposes (e.g., gaps can be introduced in the sequence of a first nucleotide sequence). The nucleotides at corresponding nucleotide positions are then compared. When a position in the first sequence is occupied by the same nucleotide as the corresponding position in the second sequence, then the molecules are identical at that position. The percent identity between the two sequences is a function of the number of identical positions shared by the sequences (i.e., % identity=# of identical positions/total # of positions×100).
[0039] The determination of percent identity between two sequences can be accomplished using a mathematical algorithm. A preferred, non-limiting example of a mathematical algorithm utilized for the comparison of two sequences is the algorithm of Karlin et al., Proc. Natl. Acad. Sci. USA, 90:5873-5877 (1993). Such an algorithm is incorporated into the NBLAST program which can be used to identify sequences having the desired identity to nucleotide sequences of the invention. To obtain gapped alignments for comparison purposes, Gapped BLAST can be utilized as described in Altschul et al., Nucleic Acids Res, 25:3389-3402 (1997). When utilizing BLAST and Gapped BLAST programs, the default parameters of the respective programs (e.g., NBLAST) can be used. See the programs provided by National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health. In one embodiment, parameters for sequence comparison can be set at W=12. Parameters can also be varied (e.g., W=5 or W=20). The value “W” determines how many continuous nucleotides must be identical for the program to identify two sequences as containing regions of identity.
[0040] The invention also provides expression vectors containing a nucleic acid sequence encoding a polypeptide described herein (or an active derivative or fragment thereof), operably linked to at least one regulatory sequence. Many expression vectors are commercially available, and other suitable vectors can be readily prepared by the skilled artisan. “Operably linked” is intended to mean that the nucleotide sequence is linked to a regulatory sequence in a manner which allows expression of the nucleic acid sequence. Regulatory sequences are art-recognized and are selected to produce the polypeptide or active derivative or fragment thereof. Accordingly, the term “regulatory sequence” includes promoters, enhancers, and other expression control elements which are described in Goeddel, Gene Expression Technology: Methods in Enzymology 185, Academic Press, San Diego, Calif. (1990). For example, the native regulatory sequences or regulatory sequences native to bacteriophage RM 378 can be employed. It should be understood that the design of the expression vector may depend on such factors as the choice of the host cell to be transformed and/or the type of polypeptide desired to be expressed. For instance, the polypeptides of the present invention can be produced by ligating the cloned gene, or a portion thereof, into a vector suitable for expression in an appropriate host cell (see, for example, Broach, et al., Experimental Manipulation of Gene Expression, ed. M. Inouye (Academic Press, 1983) p. 83; Molecular Cloning: A Laboratory Manual, 2 nd Ed., ed. Sambrook et al. (Cold Spring Harbor Laboratory Press, 1989) Chapters 16 and 17). Typically, expression constructs will contain one or more selectable markers, including, but not limited to, the gene that encodes dihydrofolate reductase and the genes that confer resistance to neomycin, tetracycline, ampicillin, chloramphenicol, kanamycin and streptomycin resistance. Thus, prokaryotic and eukaryotic host cells transformed by the described expression vectors are also provided by this invention. For instance, cells which can be transformed with the vectors of the present invention include, but are not limited to, bacterial cells such as Rhodothermus marinus, E. coli (e.g., E. coli K12 strains), Streptomyces, Pseudomonas, Bacillus, Serratia marcescens and Salmonella typhimurium. The host cells can be transformed by the described vectors by various methods (e.g., electroporation, transfection using calcium chloride, rubidium chloride, calcium phosphate, DEAE-dextran, or other substances; microprojectile bombardment; lipofection, infection where the vector is an infectious agent such as a retroviral genome, and other methods), depending on the type of cellular host. The nucleic acid molecules of the present invention can be produced, for example, by replication in such a host cell, as described above. Alternatively, the nucleic acid molecules can also be produced by chemical synthesis.
[0041] The isolated nucleic acid molecules and vectors of the invention are useful in the manufacture of the encoded polypeptide, as probes for isolating homologous sequences (e.g., from other bacteriophage species), as well as for detecting the presence of the bacteriophage in a culture of host cells.
[0042] The nucleotide sequences of the nucleic acid molecules described herein (e.g., a nucleic acid molecule comprising any of the open reading frames shown in FIG. 2, such as a nucleic acid molecule comprising the open reading frames depicted in FIGS. 7 - 11 (SEQ ID NO:56, 58, 60, 61 and 62, respectively)) can be amplified by methods known in the art. For example, this can be accomplished by e.g., PCR. See generally PCR Technology: Principles and Applications for DNA Amplification (ed. H. A. Erlich, Freeman Press, NY, N.Y., 1992); PCR Protocols: A Guide to Methods and Applications (eds. Innis, et al., Academic Press, San Diego, Calif., 1990); Mattila et al., Nucleic Acids Res. 19, 4967 (1991); Eckert et al., PCR Methods and Applications 1, 17 (1991); PCR (eds. McPherson et al., IRL Press, Oxford); and U.S. Pat. No. 4,683,202.
[0043] Other suitable amplification methods include the ligase chain reaction (LCR) (see Wu and Wallace, Genomics 4, 560 (1989), Landegren et al., Science 241, 1077 (1988), transcription amplification (Kwoh et al., Proc. Natl. Acad. Sci. USA 86, 1173 (1989)), and self-sustained sequence replication (Guatelli et al., Proc. Nat. Acad. Sci. USA, 87, 1874 (1990)) and nucleic acid based sequence amplification (NASBA). The latter two amplification methods involve isothermal reactions based on isothermal transcription, which produce both single stranded RNA (ssRNA) and double stranded DNA (dsDNA) as the amplification products in a ratio of about 30 or 100 to 1, respectively.
[0044] The amplified DNA can be radiolabelled and used as a probe for screening a library or other suitable vector to identify homologous nucleotide sequences. Corresponding clones can be isolated, DNA can be obtained following in vivo excision, and the cloned insert can be sequenced in either or both orientations by art recognized methods, to identify the correct reading frame encoding a protein of the appropriate molecular weight. For example, the direct analysis of the nucleotide sequence of homologous nucleic acid molecules of the present invention can be accomplished using either the dideoxy chain termination method or the Maxam Gilbert method (see Sambrook et al., Molecular Cloning, A Laboratory Manual (2nd Ed., CSHP, New York 1989); Zyskind et al., Recombinant DNA Laboratory Manual, (Acad. Press, 1988)). Using these or similar methods, the protein(s) and the DNA encoding the protein can be isolated, sequenced and further characterized.
Polypeptides of the Invention
[0045] The invention additionally relates to isolated polypeptides obtainable from the bacteriophage RM 378. The term, “polypeptide,” as used herein, includes proteins, enzymes, peptides, and gene products encoded by nucleic acids described herein. In one embodiment, the invention pertains to the polypeptides encoded by the ORFs as described above. In addition, as described in detail below, bacteriophage RM 378 is similar to the well-known E. coli bacteriophage T4. Thus, it is expected that bacteriophage RM 378 comprises additional polypeptides that are homologous to those found in bacteriophage T4.
[0046] For example, representative proteins expected to be encoded by genes of bacteriophage RM 378 include the following: DNA topoisomerase; exonuclease (e.g., 3′-5′ exonuclease, 5′-3′ exonuclease (RNase H)); helicase; enzymes related to DNA or RNA synthesis (e.g., dCTPase, dUTPase, dCDPase, dUDPase, GTPase, dGTPase, ATPase, dATPase); transposase; reverse transcriptase; polymerase (e.g., DNA polymerase, RNA polymerase); DNA polymerase accessory protein; DNA packaging protein; DNA topoisomerase; RNA polymerase binding protein; RNA polymerase sigma factor; site-specific RNase inhibitor of protease; recombinant protein; alpha-glucosyltransferase; mobility nuclease; endonuclease (e.g., endonuclease II, endonuclease V, endonuclease VII); inhibitor of Lon protease; thymidine kinase; site-specific RNase; N-glycosidase; endolysin; lysozyme; dNMP kinase; DNA ligase; deoxyribonucleotide-3′-phosphatase; ssDNA binding protein; dsDNA binding protein; and RNA ligase.
[0047] In a particularly preferred embodiment, the polypeptide is polymerase (e.g., DNA polymerase); DNA polymerase accessory protein; dsDNA binding protein; deoxyribonucleotide-3-phosphatase; DNA topoisomerase; RNA ligase; site-specific RNase inhibitor of protease; endonuclease; exonuclease (e.g., 3′-5′ exonuclease, 5′-3′ exonuclease (RNase H)); nobility nuclease; reverse transcriptase; single-stranded binding protein; enolysin; lysozyme; helicase; alpha-glucosyltransferase; or thymidine kinase. In an especially preferred embodiment, the polypeptide is a DNA polymerase, a 3′-5′ exonuclease, a 5′-3′ exonuclease (RNase H), a DNA helicase, or an RNA ligase, such as those shown in FIGS. 7 - 11 (e.g., for a DNA polymerase, SEQ ID NO:58; a 3′-5′ exonuclease, SEQ ID NO:56; a 5′-3′ exonuclease (RNase H) (SEQ ID NO:61); a DNA helicase (SEQ ID NO:62), or an RNA ligase (SEQ ID NO:60)). In a most preferred embodiment, the polypeptide is a DNA polymerase that lacks exonuclease domains, or a 3′-5′ exonuclease that lacks DNA polymerase domain, as described in the examples below. As used herein, the term, “lacking exonuclease domains,” indicates that the polypeptide does not contain an amino acid domain (e.g., a consecutive or closely spaced series of amino acids) homologous to domains where such exonuclease activity resides in other similar polymerases (such as polymerases in the same family); it does not refer to the presence of a non-functional domain homologous to domains where exonuclease activity resides. Similarly, the term, “lacking DNA polymerase domain,” indicates that the polypeptide does not contain an amino acid domain (e.g., a consecutive or closely spaced series of amino acids) homologous to domains where such DNA polymerase activity resides in other similar exonucleases (such as exonucleases in the same family); it does not refer to the presence of a non-functional domain homologous to domains where DNA polymerase activity resides.
[0048] These polypeptides can be used in a similar manner as the homologous polypeptides from bacteriophage T4; for example, polymerases and ligases of bacteriophage RM 378 can be used for amplification or manipulation of DNA and RNA sequences. The polymerases and ligases of bacteriophage RM 378, however, are expected to be much more thermostable than those of bacteriophage T4, because of the thermophilic nature of the host of bacteriophage RM 378 (in contrast with the mesophilic nature of E. coli, the host of bacteriophage T4).
[0049] The polypeptides of the invention can be partially or substantially purified (e.g., purified to homogeneity), and/or are substantially free of other polypeptides. According to the invention, the amino acid sequence of the polypeptide can be that of the naturally-occurring polypeptide or can comprise alterations therein. Polypeptides comprising alterations are referred to herein as “derivatives” of the native polypeptide. Such alterations include conservative or non-conservative amino acid substitutions, additions and deletions of one or more amino acids; however, such alterations should preserve at least one activity of the polypeptide, i.e., the altered or mutant polypeptide should be an active derivative of the naturally-occurring polypeptide. For example, the mutation(s) can preferably preserve the three dimensional configuration of the binding site of the native polypeptide, or can preferably preserve the activity of the polypeptide (e.g., if the polypeptide is a DNA polymerase, any mutations preferably preserve the ability of the enzyme to catalyze combination of nucleotide triphosphates to form a nucleic acid strand complementary to a nucleic acid template strand). The presence or absence of activity or activities of the polypeptide can be determined by various standard functional assays including, but not limited to, assays for binding activity or enzymatic activity.
[0050] Additionally included in the invention are active fragments of the polypeptides described herein, as well as fragments of the active derivatives described above. An “active fragment,” as referred to herein, is a portion of polypeptide (or a portion of an active derivative) that retains the polypeptide'activity, as described above.
[0051] Appropriate amino acid alterations can be made on the basis of several criteria, including hydrophobicity, basic or acidic character, charge, polarity, size, the presence or absence of a functional group (e.g., —SH or a glycosylation site), and aromatic character. Assignment of various amino acids to similar groups based on the properties above will be readily apparent to the skilled artisan; further appropriate amino acid changes can also be found in Bowie et al. ( Science 247:1306-1310(1990)). For example, conservative amino acid replacements can be those that take place within a family of amino acids that are related in their side chains. Genetically encoded amino acids are generally divided into four families: (1) acidic=aspartate, glutamate; (2) basic=lysine, arginine, histidine; (3) nonpolar=alanine, valine, leucine, isoleucine, proline, phenylalanine, methionine, tryptophan; and (4) uncharged polar=glycine, asparagine, glutamine, cystine, serine, threonine, tyrosine. Phenylalanine, tryptophan and tyrosine are sometimes classified jointly as aromatic amino acids. For example, it is reasonable to expect that an isolated replacement of a leucine with an isoleucine or valine, an aspartate with a glutamate, a threonine with a serine or a similar conservative replacement of an amino acid with a structurally related amino acid will not have a major effect on activity or functionality.
[0052] The polypeptides of the invention can also be fusion polypeptides comprising all or a portion (e.g., an active fragment) of the native bacteriophage RM 378 polypeptide amino acid sequence fused to an additional component, with optional linker sequences. Additional components, such as radioisotopes and antigenic tags, can be selected to assist in the isolation or purification of the polypeptide or to extend the half life of the polypeptide; for example, a hexahistidine tag would permit ready purification by nickel chromatography. The fusion protein can contain, e.g., a glutathione-S-transferase (GST), thioredoxin (TRX) or maltose binding protein (MBP) component to facilitate purification; kits for expression and purification of such fusion proteins are commercially available. The polypeptides of the invention can also be tagged with an epitope and subsequently purified using antibody specific to the epitope using art recognized methods. Additionally, all or a portion of the polypeptide can be fused to carrier molecules, such as immunoglobulins, for many purposes, including increasing the valency of protein binding sites. For example, the polypeptide or a portion thereof can be linked to the Fe portion of an immunoglobulin; for example, such a fusion could be to the Fe portion of an IgG molecule to create a bivalent form of the protein.
[0053] Also included in the invention are polypeptides which are at least about 90% identical (i.e., polypeptides which have substantial sequence identity) to the polypeptides described herein. However, polypeptides exhibiting lower levels of identity are also useful, particular if they exhibit high, e.g., at least about 90%, identity over one or more particular domains of the polypeptide. For example, polypeptides sharing high degrees of identity over domains necessary for particular activities, such as binding or enzymatic activity, are included herein. Thus, polypeptides which are at least about 10%, preferably at least about 20%, more preferably at least about 30%, more preferably at least about 40%, even more preferably at least about 50%, yet more preferably at least about 70%, still more preferably at least about 80%, and even more preferably at least about 90% identity, are encompassed by the invention.
[0054] Polypeptides described herein can be isolated from naturally-occurring sources (e.g., isolated from host cells infected with bacteriophage RM 378). Alternatively, the polypeptides can be chemically synthesized or recombinantly produced. For example, PCR primers can be designed to amplify the ORFs from the start codon to stop codon, using DNA of RM378 or related bacteriophages or respective recombinant clones as a template. The primers can contain suitable restriction sites for an efficient cloning into a suitable expression vector. The PCR product can be digested with the appropriate restriction enzyme and ligated between the corresponding restriction sites in the vector (the same restriction sites, or restriction sites producing the same cohesive ends or blunt end restriction sites).
[0055] Polypeptides of the present invention can be used as a molecular weight marker on SDS-PAGE gels or on molecular sieve gel filtration columns using art-recognized methods. They are particularly useful for molecular weight markers for analysis of proteins from thermophilic organisms, as they will behave similarly (e.g., they will not denature as proteins from mesophilic organisms would).
[0056] The polypeptides of the present invention can be isolated or purified (e.g., to homogeneity) from cell culture (e.g., from culture of host cells infected with bacteriophage RM 378) by a variety of processes. These include, but are not limited to, anion or cation exchange chromatography, ethanol precipitation, affinity chromatography and high performance liquid chromatography (HPLC). The particular method used will depend upon the properties of the polypeptide; appropriate methods will be readily apparent to those skilled in the art. For example, with respect to protein or polypeptide identification, bands identified by gel analysis can be isolated and purified by HPLC, and the resulting purified protein can be sequenced. Alternatively, the purified protein can be enzymatically digested by methods known in the art to produce polypeptide fragments which can be sequenced. The sequencing can be performed, for example, by the methods of Wilm et al. ( Nature 379(6564):466-469 (1996)). The protein may be isolated by conventional means of protein biochemistry and purification to obtain a substantially pure product, i.e., 80, 95 or 99% free of cell component contaminants, as described in Jacoby, Methods in Enzymology Volume 104, Academic Press, New York (1984); Scopes, Protein Purification, Principles and Practice, 2nd Edition, Springer-Verlag, New York (1987); and Deutscher (ed), Guide to Protein Purification, Methods in Enzymology, Vol. 182 (1990).
[0057] The following Examples are offered for the purpose of illustrating the present invention and are not to be construed to limit the scope of this invention. The teachings of all references cited are hereby incorporated herein by reference in their entirety.
EXAMPLE 1
Isolation, Purification and Characterization of Bacteriophage
[0058] A. Materials and Methods
Bacterial Strains and Growth Media
[0059] The thermophilic, slightly halophilic eubacterium, Rhodothermus marinus was first isolated from shallow water submarine hot springs in Isafjardardjup in northwest Iceland (Alfredsson, G. A. et al., J. Gen. Microbiol. 134:299-306 (1988)). Since then Rhodothermus has also been isolated from two other areas in Iceland (Petursdottir et al., in prep.), from the Azores and the Bay of Naples in Italy (Nunes, O. C. et al., Syst. Appl. Microbiol. 15:92-97 (1992); Moreira, L. et al., Syst. Appl. Microbiol. 19:83-90 (1996)). Rhodothermus is distantly related to the group containing Flexibacter, Bacterioides and Cytophaga species (Anderson, O. S. and Fridjonsson, O. H., J. Bacteriol. 176:6165-6169 (1994)).
[0060] Strain ITI 378 (originally R-21) is one of the first Rhodothermus strains isolated from submarine hot springs in Isafjardardjup in northwest Iceland. The strain was grown at 65° C. in medium 162 for Thermus (Degryse et al., Arch. Microbiol. 117:189-196 (1978)), with {fraction (1/10)} the buffer and with 1% NaCl. Strain ITI 378 is phenotypically and phylogenetically similar (over 99% similarity in 16s rRNA sequence) to type strain DSM 4252.
Bacteriophage Isolation
[0061] A water sample with some sand and mud was collected from a hot spring (62° C.) appearing at low tide in Isafjardardjup at the same site as the bacterium was originally isolated. The same kind of samples were collected from the Blue Lagoon and the Salt factory on Reykjanes in southwest Iceland.
[0062] After mixing a sample in a Waring blender, the sample was filtered through a Buchner funnel, followed by centrifugation, before filtering the water through a 0.45 μm membrane. After centrifuging again, the sample was filtered through a sterile 0.2 μm membrane. This filtrate was used for infecting 18 different Rhodothermus strains (8 from Isafjardardjup in northwest Iceland, and 10 from Reykjanes in southwest Iceland). The sample (4 ml) was mixed with 5 ml of soft agar A (the above growth medium with 2% agar) and 1 ml of overnight culture of different Rhodothermus strains. After pouring the sample onto a thin layer agar plate, the plates were incubated for 1-2 days at 65° C. A single, well-isolated plaque was stabbed with a sterile Pasteur pipette and dissolved in 100 μl of 10 mM MgCl 2 solution (forming the plaque solution).
[0063] The bacteriophage is sensitive to freezing; it can be stored in a cell lysate at 4° C. (e.g., as described below under “Liquid Lysate”).
Plate Lysate
[0064] Overnight culture (0.9 ml) was mixed with 100 μl of the plaque solution and incubated for 15 minutes at 65° C. before adding 3 ml of soft agar B (same as A, but 1% agar and 10 mM MgCl 2 ). After mixing and pouring onto thin layer agar plates, the plates were incubated for 1-2 days at 65° C. To nearly totally lysed plates was added 1 ml of 10 mM MgCl 2 , and after incubating at 4° C. for a few hours, the top layer was scraped off and put into a sterile tube. After adding 100 μl chloroform and mixing it, the sample was centrifuged and the supernatant collected. The sample was centrifuged again and filtered through a 0.2 μm filter; the filtrate was stored at 4° C. This lysate was used for testing host specificity.
Liquid Lysate
[0065] Liquid cultures were infected when they had reached an absorbance of 0.5 at 600 nm (expected to contain 2.5×10 8 cells/ml). The phage ratio was 0.1 pfu/cell culture. The cultures were incubated at high shaking (300 rpm) and growth was followed by measuring absorbance at 600 nm. When lysis had occurred, chloroform was added to the cultures (10 μl/ml) and shaking continued for 1 hour. Cell debris was removed by centrifugation and titer estimation was performed on the supernatant. large-scale purification from 300 ml culture was undertaken for DNA isolation and for protein composition analysis, as well as for electron microcopy.
Bacteriophage Purification
[0066] For electron microscopy, the bacteriophages were precipitated using PEG 8000 (Sambrook, J. et al., Molecular Cloning, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., 1989) and resuspended in SM buffer (Sambrook, J. et al., Molecular Cloning, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., 1989) before loading on the top of CsCl (0.75 g/ml). This sample was centrifuged for 23 hours at 38,000 rpm in TY-64 rotor (Sorvall Ultracentrifuge). The layer of bacteriophage was collected using a syringe.
Protein Determination and DNA Isolation
[0067] Purified bacteriophage supernatant with a titer of approximately 10 13 pfu/ml was boiled for 5 minutes in SDS and β-mercaptoethanol loading puffer according to the method of Laemmli (Laemmli, U. K., Nature 227:680-685 (1970)) using 10% polyacrylamide gel, and stained with Coomassie brilliant blue. Bio-Rad pre-stained low molecular weight standards (7.7-204 kDa) were used as size markers. Bacteriophage DNA was isolated from a purified phage lysate containing approximately 10 13 pfu/ml using the Qiagen lambda kit (Catolog No. 12543, Qiagen) according to manufacturer'instructions.
Temperature and Chloroform Sensitivity
[0068] Bacteriophage RM 378 at approximately 10 11 pfu/ml was incubated for 30 minutes over a temperature range of 50-96° C. before the remaining bacteriophage titer was determined. The bacteriophage lysate at approximately 10 11 pfu/ml was mixed with an equal volume of chloroform, and incubated at room temperature. After 30 minutes, the remaining viable bacteriophage were titrated with strain ITI 378 as a host.
Determination of G+C Content
[0069] The mole percent guanine plus cytosine content of the bacteriophage was determined by CSM with HPLC according to Mesbah (Mesbah, M. U. et al., Int. J. Syst. Bacteriol. 39:159-167 (1989)).
Estimation of Genome Size
[0070] Bacteriophage DNA was digested individually with a variety of restriction endonucleases, and the fragments separated by electrophoresis on 0.5-0.8% (w/v) agarose gel. Pulsed-field gel electrophoresis (PFGE) was also used for size estimation. Pulsed Field Certified Agarose from BioRad (Catalog No. 162-0137, Bio Rad) (1%) was used for the gel, and low-melt agarose (Catalog No. 162-0017, Bio Rad) (1%) for filling the wells when using marker plugs. Samples of 1.0 and 0.5 μg DNA were used and Bio Rad low range marker (#350) as well as λ-ladder (Catalog No. 170-3635, Bio Rad) was employed. The running buffer was 0.5×TBE (Sambrook, J. et al., Molecular Cloning, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., 1989). Bio Rad Pulsed Field Electrophoresis system (CHEF-DRIII) was used with an initial switch time of 60 seconds, final switch time of 60 seconds, 6 V/cm angle of 120° and 21 hour run time. Gels were stained with ethidium bromide and washed in distilled water for 3 hours before photographing under a UV light illuminator.
Electron Microscopy
[0071] The bacteriophage was stained with 2.5% phosphotungstic acid and the grids examined with a Philips EM 300 electron microscope. Bacteriophage samples from CsCl purification, as well as directly from a liquid lysed culture with titer of 10 13 pfu/ml, were used for microscopy studies.
DNA Sequencing and Genome Analysis
[0072] The phage genome was sequenced using the “shot gun sequencing” technique (see, e.g., Fleischmann, R. D. et al., Science 269:496-512 (1995)). The sequences were aligned (Ewing, B., et al., Genome Research 8:175-185 (1998)); Ewing, B. and Green, P., Genome Research 8:186-194 (1998)). The consensus sequence of 130,480 bp was visualized with the program XBB-Tools (Sicheritz-Ponten, T., Department of Molecular Evolution, Uppsala, Sweden) for open reading frames (ORFs).
[0073] B. Results
Bacteriophage Isolation
[0074] The phage sample from the southwest area of Iceland, prepared as described above, infected 4 strains of Rhodothermus, all from Reykjanes in southwest Iceland. The phage sample from the northwest area of Iceland, prepared as described above, infected 7 strains of Rhodothermus, all from Isafjardardjup in northwest Iceland. Bacteriophages were isolated from two of the strains infected with the sample from the southwest, and from all 7 of the strains infected with the sample from the northwest. Of these, one of the bacteriophages from the sample from the northwest was isolated from strain ITI 378 and designated RM 378. The titer of this bacteriophage was estimated; in liquid culture it repeatedly gave titers of 5-8×10 13 pfu/ml.
[0075] Attempts to isolate the bacteriophages from Rhodothermus by subjecting it to stress such as ultraviolet (UV) exposure did not succeed. Because such stress would have excised a prophage from the chromosome and have initiated a lytic response, the failed attempts suggest that Rhodothermus did not contain prophages.
Bacteriophage Morphology
[0076] Bacteriophage RM 378 is a tailed phage with a moderately elongated head. It is a T4-like phage, resembling the T4 phage of Escherichia coli both in morphology and genome size, and has a double-stranded DNA genome. RM 378 belongs to the Myoviridae family and has the A2 morphology (Ackermann, H. W., Arch. Virol. 124:201-209 (1992)). The bacteriophage head measures 85 nm on one side and 95 nm on the other. The tail is 150 nm in length, with a clear right-handed spiral to the tail sheath. The head/tail ratio is 0.63 and the total length is 245 nm.
Host Specificity and Infection
[0077] RM 378 concentrated bacteriophage was tested against 9 different Rhodothermus strains from the two different areas (Isafjardardjup in northwest Iceland, and Reykjanes in southwest Iceland). It infected 5 strains from the northwest, but no strains from the southwest. Thus, the bacteriophage infected only strains of Rhodothermus from the same geographical area from which the bacteriophage was isolated. It did not infect any of the 6 Thermus strains that were tested.
[0078] Growth of bacteria was followed at 65° C. in a liquid. Uninfected culture was used as control, and growth was followed until the control culture had reached stationary phase. Cell lysis started 9 hours after infection of the culture, and stationary phase in the control was reached about 14 hours after infection.
Stability of the Bacteriophage
[0079] Bacteriophage RM 378 was stable to 30 minutes exposure to chloroform, indicating that it probably does not contain lipids. Heat stability of the phage was tested at 50° C.-96° C. by incubating the phage concentrate for 30 minutes, followed by estimation of titer. There was no change of the titer up to 65° C., but at 70° C. and 80° C. a 100-fold drop in pfu/ml was measured. Linear decrease of the titer was observed up to 96° C., where it was 10,000 times lower after 30 minutes than in the starting solution. After 3 months of storage at 4° C. the titer dropped 100-fold (down to 10 11 pfu/ml). After 27 months of storage the titer had fallen from 10 11 pfu/ml to 10 5 pfu/ml in a CsCl-purified sample.
Composition of Bacteriophage RM 378
[0080] Purified bacteriophage was subjected to SDS-PAGE analysis for examination of its protein composition. The phage was composed of at least 16 proteins with apparent molecular weights from 23-150 kDa. The five main bands were at 92, 61, 52, 50 and 26 kDa, and were in a ratio of 0.14:0.45:0.21:0.13:0.06. The major protein band of 61 kDa accounted for about 20% of the total protein; the five main bands together represented about 50% of total proteins.
[0081] The average G+C mol % of the RM 378 phage was 42.0±0.1. The DNA was digested with a variety of restriction enzymes (HindIII, XhoI, ClaI, AluI, NotI, SacI, PstI, BamHI, SmaI, SpeI, EcoRV). Three of the enzymes (NotI, SmaI, SpeI) did not cleave RM 378, and the rest resulted in multiple fragments. Because the addition of the fragment sizes resulted in a variable amount for the total genome size, the phage DNA was also run on PFGE, which estimated the size of the DNA to be about 150 kb.
Characteristics of the Bacteriophage
[0082] The RM 378 bacteriophage is a virulent bacteriophage following a lytic cycle of infection. Very high titer lysates of up to 10 13 pfu/ml could be obtained, which indicated a large burst size of more than 100. Because no bacteriophages have been reported against this bacterial genus, RM 378 represents a new species.
Genome Analysis and Comparison to T4 Bacteriophage
[0083] The nucleic acid sequence of RM 378 is set forth in FIG. 1. The nucleic acid sequence of RM 378 contains at least 200 open reading frames (ORFs); see, for example, the ORFs described in FIG. 2. Of these, five were identified in more detail, as described in Example 2, including the ORFs expected to encode DNA polymerase, 3′-5′ exonuclease, 5′-3′ exonuclease, RNA ligase and DNA helicase.
[0084] RM 378 belongs in the T-even family, in that it is similar to bacteriophage T4 of Escherichia coli. Bacteriophage T4 of E. coli is a well-studied phage which, together with T2 and T6, belongs to the family of bacteriophages known as T-even phages. T-even phages are nearly identical not only in structure and composition, but also in properties. Several enzymes isolated from bacteriophage T4 are used in the field of recombinant DNA technology as well as in other commercial applications. For example, T4 DNA polymerase, T4 DNA ligase and T4 RNA ligase are frequently used in the research industry today.
[0085] The genome of RM 378 was aligned in a consensus sequence, and the open reading frames (ORFs) were analyzed and compared to the T4 bacteriophage genome. The overall genome arrangement seemed to be different and the overall similarity to known proteins was low. However, despite this apparently high genetic divergence, several structural and morphological features were highly conserved. Furthermore, homologs to proteins in T4 were identified in the RM 378 bacteriophage. These similarities are set forth in Table 1, below.
[0086] In view of the similarities between bacteriophage T4 and bacteriophage RM 378, it is reasonable to expect that bacteriophage RM 378 comprises genes that are homologous to those found in bacteriophage T4, and that these genes in bacteriophage RM 378 encode proteins and enzymes that correlate to those proteins and enzymes found in bacteriophage T4.
EXAMPLE 2
Detailed Analysis of Five Open Reading Frames (ORFs)
[0087] A. Selection of Reading Frames for Analysis
[0088] Five open reading frames (ORFs) of the numerous ORFs described above in the genome of bacteriophage RM378, have been further characterized and the corresponding genes cloned and expressed. The genes include a DNA polymerase, 3′-5′ exonuclease, 5′-3′-exonuclease (RNase H), replicative DNA helicase and RNA ligase. These genes were chosen as examples of the many valuable genes encoded by the bacteriophage genome. The corresponding polypeptide products of these genes are mainly components of the bacteriophage replication machinery and can be utilized in various molecular biology applications as evident by the current use of homologous counterparts from other sources. The sequences of the five ORFs show low similarity to sequences in public databases indicative of distant relationship to known proteins; however, probable homology to known sequences can be established by comparison with families of sequences showing overall sequence similarity as well as conservation of shorter regions, sequence motifs and functionally important residues, in some cases aided by three-dimensional structural information. The limited sequence similarity or these sequences to publicly available sequences suggests that these gene products have functional properties very different from corresponding proteins currently in use in molecular biology applications. Together with the presumed thermostability, the properties of these gene products render them valuable in various applications in molecular biology.
DNA Polymerase
[0089] DNA polymerases have evolved to accommodate the varied tasks required for replication and repair. DNA replication involves 1) local melting of the DNA duplex at an origin of the replication, 2) synthesis of a primer and Okazaki fragment, 3) DNA melting and unwinding at the replication fork, 4) extension of the primer on the leading strand and discontinuous synthesis of primers followed by extension of the lagging strand, 5) removal of RNA primers and 6) sealing of nicks. (Perler et al., Adv Protein Chem 48:377-435 (1996)).
[0090] The different types of DNA polymerases have been grouped into Families A, B, C and X corresponding to similarity with E. coli pol I, II and III and pol b respectively (Braithwaite, D. K. and Ito, J., Nucleic Acids Res. 21:787-802 (1993)). Each of these Families contains conserved sequence regions (Perler et al., Adv Protein Chem. 48:377-435 (1996); Blanco L., et al., Gene 100:27-38 (1991); Morrison A. et al., Proc Natl Acad Sci USA. 88:9473-9477 (1991)). Family B DNA polymerasese are also called Pol α Family DNA polymerases.
[0091] The DNA polymerases of family B type include bacteriophage T4 and bacteriophage RB69 DNA polymerase as well as archaeal polymerases and E. coli polymerase II. Polymerases of this type normally have two activities, the polymerase activity and the proofreading 3′-5′ exonuclease activity, found in different domains within the same polypeptide with the exonuclease domain being N-terminal to the polymerase domain (Steitz, T. A., J Biol Chem 274:17395-8 (1999); Kornberg, A. and Baker, T. A., DNA Replication, Freeman, New York (1992); Brautigam, C. A. and Steitz, T. A., Curr.Opin.Struct.Biol. 8:45-63 (1998) ). Polymerases of family B have an overall domain architecture different from polymerases of family A and do not have a 5′-3′ exonuclease activity which is normally found in polymerases in family A. The determined structure of RB69 DNA polymerase is a representative structure of family B type polymerase and shows clearly the modular organization of the enzyme with separate domains (Wang, J. et al., Cell 89:1087-99 (1997), Protein data bank (PDB) accession code 1WAJ). The structure of the archaeal DNA polymerase from Desulfurococcus strain Tok was shown to have the same overall structure (Zhao, Y. et al., Structure Fold Des 7:1189-99 (1999), PDB accession code 1QQC ). The alignment of polymerases in this family indicates the presence of several conserved region in the sequences with characteristic sequence motifs both belonging to both the exonuclease domain and the polymerase domain (Hopfner, K. P. et al., Proc Natl Acad Sci USA 96:3600-3605 (1999)).
Exonucleases
[0092] Besides the basic polymerization function, DNA polymerases may contain 5′-3′ and a 3′-5′ exonuclease activity. The 3′-5′ exonuclease activity is required for proofreading. In general the family B polymerases have 3′-5′ exonuclease activity, but not 5′-3′ exonuclease activity. If both exonucleases are present, the 5′-3′ exonuclease domain is at the N-terminal followed by the 3′-5′ exonuclease domain and the C-terminal polymerase domain. The structure of the polymerases can be defined further in terms of domain structure. The polymerase domain is thus composed of a number of smaller domains, often referred to as the palm, fingers and thumb, and although these parts are not homologous across families, they do show analogous structural features (Steitz, T. A., J Biol Chem 274:17395-8 (1999); Kornberg, A. & Baker, T. A., DNA Replication, Freeman, New York (1992); Brautigam, C. A. & Steitz, T. A., Curr.Opin.Struct.Biol. 8:45-63 (1998)).
[0093] RNase H ( Ribonuclease H), e.g. from bacteriophage T4, removes the RNA primers that initiate lagging strand fragments, during DNA replication of duplex DNA. The enzyme has a 5′-3′ exonuclease activity on double-stranded DNA and RNA-DNA duplexes. Further, T4 RNase H has a flap endonuclease activity that cuts preferentially on either side of the junction between single and double-stranded DNA in flap and fork DNA structures. Besides replication, T4 RNase H also plays a role in DNA repair and recombination. (Bhagwat, M., et al., J. Biol. Chem. 272:28531-28538 (1997); Bhagwat, M., et al. J. Biol. Chem. 272:28523-28530 (1997)).
[0094] T4 RNase H shows sequence similarity to other enzymes with a demonstrated role in removing RNA primers, including phage T7 gene 6 exonuclease, the 5′-3′ nuclease domain of E. coli DNA polymerase I, and human FEN-1 (flap endonuclease). These enzymes have 5′-3′-exonuclease activity on both RNA-DNA and DNA-DNA duplexes and most of them have a flap endonuclease activity that removes the 5-ssDNA tail of flap or fork structures. The T4 enzyme homologous to members of the RAD2 family of prokaryotic and eukaryotic replication and repair nucleases (Mueser T. C., et al., Cell. 85:1101-1112 (1996)).
[0095] RNase H is a part of the reverse transcriptase complex of various retroviruses. The HIV-1 RT associated ribonuclease H displays both endonuclease and 3′-5′ exonuclease activity (Ben-Artzi, H., et al., Nucleic Acids Res. 20:5115-5118 (1992); Schatz, O., et al., EMBO J. 4:1171-1176 (1990)).
[0096] In molecular biology, RNase H is applied to the replacement synthesis of the second strand of cDNA. The enzyme produces nicks and gaps in the mRNA strand of the cDNA:mRNA hybrid, creating a series of RNA primers that are used by the corresponding DNA polymerase during the synthesis of the second strand of cDNA (Sambrook, J., et al., Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbour Laboratory Press (1989)). The RNase H of E. coli can promote the formation and cleavage of RNA-DNA hybrid between an RNA site and a base paired strand of a stable hairpin or duplex DNA at temperature below their Tm (Li. J., and R. M. Wartell, Biochemistry 37:5154-5161 (1998); Shibahara, S., et al., Nucleic Acids Res. 15:4403-4415 (1987)). Thus, the enzyme has been used for site-directed cleavage of RNA using chimeric DNA splints (presence of complementary chimeric oligonucleotides) (Inoue, H., et al., Nucleic Acids Symp Ser. 19:135-138 (1988)) or oligoribonucleotide capable of forming a stem and loop structure (Hosaka H., et al., J. Biol. Chem. 269: 20090-20094 (1994)).
DNA Helicase
[0097] DNA helicases use energy derived from hydrolysis of nucleoside triphosphate to catalyze the disruption of the hydrogen bonds that hold the two strands of double-stranded DNA together. The reaction results in the formation of the single-stranded DNA required as a template or reaction intermediate in DNA replication, repair or recombination (Matson, S. W., et al., BioEssays. 16:13-21 (1993)).
[0098] The bacteriophage T4 Gp41 is a highly processive replicative helicase (similar to the DNA B protein of E. coli ) and has been shown to form hexamer in the presence of ATP (Dong, F., and P. H. von Hippel, J. Biol. Chem. 271:19625-19631 (1996)). The enzyme facilitates the unwinding of DNA helix ahead of the advancing DNA polymerase and accelerates the movement of the replication fork. It has been suggested that gp41 interacts with the polymerase holoenzyme at the replication fork (Schrock R. D. and B. Alberts, J. Biol. Chem. 271:16678-16682 (1996)). Gp41 has a 5′-3′ polarity and requires a single stranded region on the 5′ side of the duplex to be unwound. The ATP-activated helicase binds to a single gp61 primase molecule on appropriate DNA template (Morris, P. D., and K. D. Raney, Biochemistry. 38:5164-5171 (1999)) to reconstitute a stable primosome (Richardson, R. W. and N. G. Nossal, J. Biol. Chem. 264:4725-4731 (1989)). Although the gp41 alone does not form a stable complex with DNA template, this helicase by itself can carry out moderately processive ATP-driven translocation along single strand DNA (Dong, F., and P. H. von Hippel. J. Biol. Chem. 271:19625-19631 (1996)). The T4 gene 59 protein accelerates the loading of gp41 onto DNA, when it is covered with 32 protein (the T4 single strand binding protein), and stimulates the helicase activity to catalyze replication fork movement through a DNA double helix, even through a promoter-bound RNA polymerase molecule (Barry, J., and B. Alberts. J. Biol. Chem. 269:33063-33068 (1994); Tarumi, K., and T. Yonesaki, J Biol Chem. 270:2614-2619 (1995)). The T4 gp41 helicase has also been disclosed to participate in DNA recombination. Following exonuclease nicking of ds DNA and further expansion into a gap, gp41 creates a free 3′ end, which is required as a substrate by recombination proteins (RecA like) (Tarumi, K., and T. Yonesaki. J Biol Chem. 270:2614-2619 (1995)).
RNA Ligase
[0099] RNA ligase is abundant in T4-infected cells and has been purified in high yields. Bacteriophage T4 RNA ligase catalyzes the ATP-dependent ligation of a 5′-phosphoryl-terminated nucleic acid donor (i.e. RNA or DNA) to a 3′-hydroxyl-terminated nucleic acid acceptor. The reaction can be either intramolecular or intermolecular, i.e., the enzyme catalyzes the formation of circular DNA/RNA, linear DNA/RNA dimers, and RNA-DNA or DNA-RNA block co-polymers. The use of a 5′-phosphate, 3′-hydroxyl terminated acceptor and a 5′-phosphate, 3′-phosphate terminated donor limits the reaction to a unique product. Thus, the enzyme can be an important tool in the synthesis of DNA of defined sequence (Marie I., et al., Biochemistry 19:635-642 (1980), Sugion, A. et al., J. Biol. Chem. 252:1732-1738 (1977)).
[0100] The practical use of T4 RNA ligase has been demonstrated in many ways. Various ligation-anchored PCR amplification methods have been developed, where an anchor of defined sequence is directly ligated to single strand DNA (following primer extension, e.g. first strand cDNA). The PCR resultant product is amplified by using primers specific for both the DNA of interest and the anchor (Apte, A. N., and P. D. Siebert, BioTechniques. 15:890-893 (1993); Troutt, A. B., et al., Proc. Natl. Acad. Sci. USA. 89: 9823-9825 (1992); Zhang, X. H., and V. L. Chiang, Nucleic Acids Res. 24:990-991(1996)). Furthermore, T4 RNA ligase has been used in fluorescence-, isotope- or biotin- labeling of the 5′-end of single stranded DNA/RNA molecules (Kinoshita Y., et al., Nucleic Acid Res. 25: 3747-3748 (1997)), synthesis of circular hammer head ribozymes (Wang, L., and D. E. Ruffner. Nucleic Acids Res 26: 2502-2504 (1998)), synthesis of dinucleoside polyphosphates (Atencia, E. A., et al. Eur. J. Biochem. 261: 802-811 (1999)), and for the production of composite primers (Kaluz, S., et al., BioTechniques. 19: 182-186 (1995)).
[0101] B. DNA Polymerase Activity and 3′-5′ Exonuclease Activity Are Found in Gene Products of Separate Genes in the Phage RM378 Genome
[0102] The predicted gene products of two open reading frames (ORF056e and ORF632e), which are widely separated in the genome of phage RM378, both showed similarity to family B type polymerases as shown below.
Identification of the ORF056e Gene Product as 3′-5′ Exonuclease
[0103] The predicted gene product of ORF056e (locus GP43a) was run against a sequence database (NCBI nr) in a similarity search using BLAST ( Altschul, S. F. et al., J. Mol. Biol. 215:403-410 (1990)) (Table 2). Out of 64 hits with E value lower (better) than 1, all sequences were of DNA polymerases of family B type including DNA polymerase from bacteriophage RB69, archaeal DNA polymerases and E. coli polymerase II. Importantly, all these sequences are DNA polymerase sequences having the sequence characteristics of the DNA polymerase domain as well as the 3′-5′ exonuclease domain and are considerably longer (excluding partial sequences) than the predicted gene product of ORF056e which has a length of 349 residues. The similarity is restricted to the N-terminal halves of these sequences corresponding to the part of the protein where the 3′-5′ proofreading exonuclease domain is located.
[0104] Table 2 lists the 20 sequences with strongest similarity to the ORF056e sequence together with the length and E-value according to BLAST search. The sequence identity with the ORF056e sequence ranges from 21 to 27 %. Of the 64 sequences identified in the sequence database, 34 are of viral origin and 15 of archaeal origin. Out of the twenty top scoring sequences, 16 are of viral origin.
Identification of the ORF632e Gene Product as DNA Polymerase
[0105] The sequence similarity program BLAST (Altschul, S. F. et al., J. Mol. Biol. 215:403-410 (1990)) was also used to identify potential homologues of the ORF632e (locus GP43b) gene product. The 100 sequences in the sequence database (NCBI nr) with the strongest similarity to the ORF632e sequence were all defined as DNA polymerase sequences. These sequences all had an E value lower than 10-5 and are considerably longer (excluding partial sequences) than the predicted gene product of ORF632e which has a length of 522 residues (Table 3). Sequence alignments between the ORF632e sequence and the sequences identified in the database shows that the similarity is restricted to a domain with the DNA polymerase activity as characterized by conserved sequence motifs such as DxxSLYPS (Hopfner, K. P. et al., Proc Natl Acad Sci USA 96:3600-3605 (1999)). In these sequences this domain is always preceded by a long N-terminal region where the 3′-5′ exonuclease activity normally is found. The corresponding N-terminal region is lacking in ORF362e which consists only of the DNA polymerase domain (family B type polymerases). The sequence motif DXXSLYPS (SEQ ID NO:63) in the ORF632e sequence is found very close to its N-terminus unlike its location in all the 100 analyzed sequences in the public database.
[0106] Table 3 lists the 20 sequences with strongest similarity to the ORF632e sequence together with the length and E-value according to a BLAST search. The sequence identity with the ORF632e sequence rages from 23 to 28 % within aligned regions of 300 to 428 residues. The majority of these 20 sequences are of archaeal DNA polymerases of family B type.
[0107] The results of the similarity searches indicated that gene products of ORF056e and ORF632e correspond to the exonuclease domain and the polymerase domain of family B type polymerases, respectively. Partial alignment of sequences of a number of members of this family was obtained from the Protein Families Data Bases of Alignments and HMMs (Sanger Institute), accession number PF00136). The sequences of ORF056e and ORF632e could be combined as one continuous polypeptide and aligned to the previous set of sequences. The coordinates of the three-dimensional structures of DNA polymerases from bacteriophage RB69 (PDB ID 1WAJ), the archaea Thermococcus gorgonarius (PDB ID 1TGO) and the archaea Desulforococcus strain Tok (PDB ID 1QQc) were structurally aligned and the sequence alignment produced from the structural alignment. The corresponding sequences were added to the previous alignment and the alignment adjusted, guided by the alignment from the structural superposition, mainly in regions which are less conserved. The resulting alignment, shown in FIG. 3, strongly supports the previous interpretation that 3′-5′ proofreading activity and DNA polymerase activity are found in two proteins encoded by separate genes in bacteriophage RM378. As seen in the alignment (FIG. 3), the major conserved regions in this protein family in the 5′-3′ exonuclease domain and in the polymerase domain are also conserved in the gene products of ORF056e and ORF632e, respectively. As defined by Hopfner et al. (Hopfner, K. P. et al., Proc Natl Acad Sci USA 96:3600-3605 (1999)), this includes regions exo I, -II and -III in the exonuclease domain and motifs A, -B and -C in the polymerase protein. Motif A corresponds to the DxxSLYPS motif mentioned above and includes an aspartic acid residue, involved in coordinating one of the two Mg2+ ions which are essential for the polymerase activity, and a tyrosine residue which stacks it side chain against an incoming nucleotide in the polymerase reaction. Another aspartic residue which also acts as Mg2+ ion ligand (motif C), and is essential for the catalytic mechanism, is also found in the sequence of ORF632e (D215). Inspection of the three-dimensional structure of bacteriophage RM69 DNA polymerase (PDB ID 1WAJ), with respect to the alignment, shows that the end of the ORF056e sequence and the beginning of the ORF632e sequence are found between the 3′-5′ exonuclease domain and the DNA polymerase domain.
[0108] The polymerase activity encoded by bacteriophage RM378 thus resides in an enzyme which is relatively short corresponding only to the polymerase domain of other members in this family and unlike those relatives does not have an 3′-5′ exonuclease domain. The 3′-5′ exonuclease is found as another protein encoded by a separate gene elsewhere in the genome. The natural form of DNA polymerase from Thermus aquaticus (Taq) also lacks the proofreading 3′-5′ exonuclease activity but this polymerase differs from the polymerase of RM378 in several aspects: i) it belong to a different family of polymerase (family A) which have a different general architecture, ii) the lack of 3′-5′ exonuclease activity is due to a non-functional domain since it still contains a structural domain homologous to a domain where this activity resides in other polymerase in this family, and iii) naturally occurring Taq has 5′-3′ exonuclease activity besides its polymerase activity (Kim, Y. et al., Nature 376:612-616 (1995)). Thus, the current protein is the only known example of a DNA polymerase which by nature lacks proofreading activity and the corresponding structural domain present in other polymerases of this type, and therefore represents the discovery of a unique compact type of DNA polymerase found in nature lacking both 3′-5′ and 5′-3′ exonuclease activity.
[0109] C. ORF739f Encodes an RNA Ligase
[0110] Several sequences of RNA ligases in a protein sequence database showed similarity to the ORF739f sequence (locus GP63) as identified in a similarity search using BLAST (Altschul, S. F. et al., J. Mol. Biol. 215:403-410 (1990)). The top scoring sequences found in the BLAST search are show in Table 4. Only 3 sequences showed a score with E-avlue below 1.0. The two most significant and extensive similarities were found to the sequences of RNA ligases from Autographa californica nucleopolyhedrovirus and bacteriophage T4. The similarity to the third sequence, that of a DNA helicase, is much less extensive and has considerable higher E-value. The sequence identity between the ORF739f sequence and the two RNA ligase sequences is 23% over regions of 314 and 381 residues. A sequence alignment of these three sequences is shown in FIG. 4.
[0111] The site of covalent reaction with ATP (adenylation) has been located at residue K99 in bacteriophage T4 RNA ligase (Thogersen H C, et al., Eur J Biochem 147:325-9 (1985);Heaphy, S., Singh, M. and Gait, M. J., Biochemistry 26:1688-96 (1999)). A corresponding Lysine residue (K126) is also found in the sequence of ORF739f. An aspartic residue close to the adenylation site in T4 RNA ligase has also been implied as important for the catalytic mechanism (Heaphy, S., Singh, M. and Gait, M. J., Biochemistry 26:1688-96 (1999)). This residue is also conserved in ORF739f (D128). It has been suggested that the motif KX(D/N)G may be a signature element for covalent catalysis in nucleotidyl transfer (Cong, P., and Shuman, S., J Biol Chem 268:7256-60 (1993)). The conservation of these active site residues supports the interpretation of ORF739f gene product as RNA ligase having catalytic mechanism in common with other RNA ligases and involving covalent reaction with ATP.
[0112] Table 4 shows sequences with strongest similarity ( E-value cutoff of 1.0) to the ORF739f sequence together with their length and E-value according to BLAST search.
[0113] D. Orf 1218a Encodes a Gene Product with 5′-3′ Exonuclease Activity A BLAST search (Altschul, S. F. et al., J. Mol. Biol. 215:403-410 (1990)) identified about 60 sequences in the database (NCBI nr) with significant similarity (corresponding to E-value lower than 1) to the sequence of the predicted gene product of ORF 1218a (locus DAS). Almost all the identified sequences are of DNA polymerase I from bacterial species (DNA polymerase family A) and the similarity is restricted to the N-terminal halves of these sequences and the ORF 1218a sequence is much shorter, 318 residues, compared to the identified sequences which usually are between 800 and 900 residues (Table 5).
[0114] Structural and functional studies of DNA polymerases of this type (family A) have defined the different structural domains and how these correlate with the different activities of the enzyme. Polymerases of this type normally have a polymerase activity located in a C-terminal domain and two exonuclease activities, a 3′-5′ exonuclease proofreading activity in a central domain and a 5′-3 exonuclease activity in an N-terminal domain (Kornberg, A. and Baker, T. A., DNA Replication, Freeman, New York (1992); Brautigam, C. A. and Steitz, T. A., Curr. Opin. Struct. Biol. 8:45-63 (1998)). The sequence of ORF 1218a corresponds to the 5′-3′ exonuclease domain of these polymerases.
[0115] The 5′-3′ exonuclease domain of DNA polymerase I belongs to a large family of proteins which also include ribonuclease H (RNase H) including bacteriophage T4 RNase H. The analysis of the structure of bacteriophage T4 RNase H revealed the conservation of a several acidic residues in this family of proteins. These residues are clustered at the active site, some of which help coordinate two functionally important Mg2+ ions (Mueser, T. C., et al., Cell 85:1101-12 (1996)). The corresponding alignment shown in FIG. 5, including the sequence of the ORF 1218a gene product, shows that these acidic residues (possibly with the exception of one) are also found in the gene product of ORF1218a thus further supporting its proposed activity as 5′-3′ exonuclease.
[0116] The 5′-3′ exonuclease of polymerase I and RNase H both remove RNA primers that have been formed during replication but T4 DNA polymerases and other polymerases of the same type (family B), including the identified polymerase of phage RM378 identified here (see above), lack the 5′-3′ exonuclease activity. T4 RNase H (305 residues) and the ORF1218a gene product (318 residues) are of similar size with conserved regions scattered throughout most of the sequences (FIG. 5). These proteins are likely to have a very similar structure given the structural similarity between T4 RNase H and 5′-3′ exonuclease domain of polymerase I (Mueser, T. C., et al., Cell 85:1101-12 (1996)). The gene product of ORF1218a probably has a function analogous to the function of RNase H in bacteriophage T4.
[0117] Table 5 sets forth the 21 sequences with strongest similarity to the ORF1218a sequence together with the length and E-value according to BLAST search. The sequence identity with the ORF1218a sequence ranges from 31 to 41 % within aligned regions of 82 to 145 residues.
[0118] E. A Replicative DNA Helicase Is Part of the Replication Machinery of Phage RM378
[0119] Several sequences of replicative DNA helicases were identified in a similarity search using BLAST (Altschul, S. F., et al., J. Mol. Biol. 215:403-410 (1990)) with the ORF1293b (locus GP41) sequence as query sequence. 15 sequences had an E-value lower than 1.0 with the sequence of bacteriophage T4 replicative DNA helicase (product of gene 41, accession number P04530) having by far the lowest E-value. Some of the sequences found in the similarity search are hypothetical proteins and some are defined as RAD4 repair protein homologues. However, the most extensive similarity was found with the replicative helicase sequences, with sequence identity of 20-23% spanning 210-295 residues, and these sequences are all of length similar to the length of the ORF1293b gene product (416 residues). Table 6 shows the identified sequences of the similarity search.
[0120] The replicative DNA helicases with similarity to the ORF1293b sequence are of the same protein family often named after the corresponding helicase in E. coli encoded by the DnaB gene (e.g. DnaB-like helicases). The Protein Families Data Base of Alignments and HMMs (Sanger Institute), holds 37 sequences in this family (family DnaB, accession number PF00772;) and the alignment of these sequences shows clearly several regions with conserved sequence motifs. One of this motif is characteristic for ATPases and GTPases (Walker A motif, P-loop) and forms a loop that is involved in binding the phosphates of the nucleotide (Sawaya, M. R. et al., Cell 99:167-77 (1999)). The replicative helicases bind single stranded DNA (at the replication fork) and translocate in the 5′-3′ direction with ATP (GTP) driven translocation (Matson, S. W., et al., BioEssays 16:13-22 (1993)). The significant similarity found in the BLAST search to sequences other than helicase sequences is partly due to the presence of an ATP/GTP binding sequence motif in these sequences.
[0121]FIG. 6 shows the sequence alignment of some members of the DnaB protein family together with the sequence of ORF1293b. Sawaya et al. have shown how several conserved motifs and functionally important residues of the DnaB family relate to the crystal structure of the helicase domain of the T7 helicase-primase (Sawaya, M. R. et al., Cell 99:167-77 (1999)). The alignment in FIG. 6 shows how these conserved motifs are present in the ORF1293b sequence thereby supporting its role as replicative helicase.
[0122] The bacteriophage T4 replicative helicase sequence was indicated as most closely related to the ORF1293b sequence in the similarity search. The structure and function of the corresponding helicases may be very similar in these two bacteriophages and, together with the similarity of numerous other components of these phages, may be indicative of other similarities of their replication machinery. T4 replicative helicase is known to be an essential protein in the phage replication and interact with other proteins at the replication fork such as the primase to form the primosome (Nossal, N. G., FASEB J. 6:871-8 (1992)). Similarly, the helicase encoded by ORF1293b may have an essential function in bacteriophage RM378. Other homologues of components of the T4 replication system have been detected as well as shown above and still others may also be expected to be encoded by the bacteriophage genome.
[0123] Table 6 sets forth sequences with strongest similarity ( E-value cutoff of 1.0) to the ORF1293b sequence together with the length and E-value according to BLAST search.
[0124] F. Subcloning of Selected ORFs from RM378
[0125] Plasmids were designated pSH1, pGK1, pOL6, pJB1 and pJB2, were generated for the genes encoding the 3′-5′ exonuclease, the DNA polymerase, the RNA-ligase gene, the RNaseH gene and the helicase gene, respectively. The correct insertion of the ORFs into the expression vector was verified by DNA sequencing, and the expression of the genes was verified by SDS gel electrophoresis of respective host strain crude extracts.
[0126] E. coli strain JM109 [supE44Δ(lac-proAB), hsdR17, recA1, endA1, gyrA96, thi-1, relA1 (F'traD36, proAB, lacIqZΔM15)] (Viera and Messing, Gene, 19:259-268 (1982)) and strain XL10-Gold [TetrΔ (mcrA)183 Δ(mcrCB-hsdSMR-nrr)173 endA1 supE44 thi-1 recA1 gyrA96 relA1 lac Hte (F' proAB lacIqZΔM15 Tn10 (Tetr) Amy Camr)] (Stratagene) were used as hosts for expression plasmids.
[0127] Restriction enzyme digestions, plasmid preparations, and other in vitro manipulation of DNA were performed using standard protocols (Sambrook et al., Molecular Cloning 2nd Ed. Cold Spring Harbor Press, 1989).
[0128] The PCR amplification of the nucleic acids sequence containing the open reading frame (ORF) 056e, which displayed similarity to 3′-5′ exonuclease domain of family B polymerase genes was as follows. The forward primer exo-f: CACGAGCTC ATG AAG ATC ACG CTA AGC GCA AGC (SEQ ID NO:64), spanning the start codon (underlined) and containing restriction enzyme site, was used with the reverse primer exo-r: ACAGGTACC TTA CTC AGG TAT TTT TTT GAA CAT (SEQ ID NO:65), containing restriction site and spanning the stop codon (underlined, reverse complement) [codon 350 of ORF 056E shown in FIG. 7]. The PCR amplification was performed with 0.5 U of Dynazyme DNA polymerase (Finnzyme), 10 ng of RM378 phage DNA, a 1 μM concentration of each synthetic primer, a 0.2 mM concentration of each deoxynucleoside triphosphate, and 1.5 mM MgCl 2 in the buffer recommended by the manufacturer. A total of 30 cycles were performed. Each cycle consisted of denaturing at 94° C. for 50 s, annealing at 50° C. for 40 s, and extension at 72° C. for 90 The PCR products were digested with Kpn I and Sac I and ligated into Kpn I and Sac I digested pTrcHis A (Invitrogen) to produce pSH1. Epicurian Coli XL10-Gold (Stratagene) were transformed with pSH1 and used for induction of protein expression, although any host strain carrying a lac repressor could be used.
[0129] The PCR amplification of the nucleic acids sequence containing ORF 632e, which exhibited similarity to DNA polymerase domain of family B polymerase genes was similar as described above for the putative 3′-5′ exonuclease gene except that other PCR-primers were used. The forward primer pol-f: CACGAGCTCA TGA ACATCAACAAGTATCGTTAT (SEQ ID NO:66), spanning the start codon (underlined) and containing restriction enzyme sites was used with the reverse primer pol-r: ACAGGTACC TTA GTTTTCACTCTCTACAAG (SEQ ID NO:67), containing restriction site and spanning the stop codon (underlined reverse complement) [codon 523 of ORF 632e shown in FIG. 8]. The PCR products were digested with Kpn I and Sac I and ligated into Kpn I and Sac I digested pTrcHis A (Invitrogen) to produce pGK1. Epicurian Coli XL10-Gold (Stratagene) were transformed with pGK1 and used for induction of protein expression. The expressed protein was observed with Anti-Xpress Antibody (Invitrogen) after Western Blot.
[0130] The PCR amplification of the nucleic acid sequence containing ORF 739f, (which displayed similarity to the T4 RNA ligase gene) was similar to the procedure described above for the putative 3′-5′ exonuclease gene. The forward primer Rlig-f: GGG AAT TCT T AT G AA CGT AAA ATA CCC G (SEQ ID NO:68), spanning the start codon (underlined) and containing restriction enzyme sites was used with the reverse primer Rlig-r: GGA GAT C TT A TT TAA ATA ACC CCT TTT C (SEQ ID NO:69), containing restriction site and spanning the stop codon (underlined reverse complement) [codon 437 of the ORF shown in FIG. 9]. The PCR products were digested with EcoRI and BglII. Subsequently the amplified products were cloned into EcoRI and BamHI digested pBTac1 (Amann et al., Gene 25:167-178 (1983)) to produce pOL6. Cells of E. coli strain JM109 were transformed with pOL6 and used for induction of protein expression, although any host strain carrying a lac repressor could be used.
[0131] The PCR amplification of the nucleic acid sequence containing ORF 1218a, (which displayed similarity to the T4 RNaseH gene) was similar to the procedure described above for the putative 3′-5′ exonuclease gene except that other PCR-primers were used. The forward primer RnH-f: GGGAATTCTT ATG AAA AGA CTG AGG AAT AT (SEQ ID NO:70), spanning the start codon (underlined) and containing restriction enzyme sites was used with the reverse primer RnH-r: GGA GAT C TC A TA GTC TCC TCT TTC TT (SEQ ID NO:71), containing restriction site and spanning the stop codon (underlined reverse complement) [codon 319 of the ORF shown in FIG. 10]. The PCR products were digested with EcoRI and BglII and ligated into EcoRI and BamHI digested pBTac1 (Amann et al. Gene 25:167-178. 1983) to produce pJB1. As for the RNA ligase clone, cells of E. coli strain JM109 were transformed with pJB 1 and used for induction of protein expression.
[0132] The PCR amplification of the nucleic acid sequence containing ORF 1293b, which displayed similarity to the dnaB like helicase genes was as described above for the putative 3′-5′ exonuclease gene except other PCR-primers were used. The forward primer Hell-f: GGGCAATTGTT ATG GAA ACG ATT GTA ATT TC (SEQ ID NO:72), spanning the start codon (underlined) and containing restriction enzyme sites was used with the reverse primer HelI-r: CGGGATCC TCA TTT AAC AGC AAC GTC (SEQ ID NO:73), containing restriction site and spanning the stop codon (underlined reverse complement) [codon 417 of the ORF shown in FIG. 11]. The PCR products were digested with EcoRI and BglII and ligated into EcoRI and BamHI digested pBTac1 (Amann et al. Gene 25:167-178 (1983)) to produce pJB2. Cells of E. coli strain JM109 were transformed with pJB2 and used for induction of protein expression.
Deposit of Biological Material
[0133] A deposit of Rhodothermus marinus strain ITI 378, and a deposit Rhodothermus marinus strain ITI 378 infected with bacteriophage RM 378, was made at the following depository under the terms of the Budapest Treaty:
[0134] Deutsche Sammlung Von Mikroorganismen und Zellkulturen GmbH
[0135] (DSMZ)
[0136] Mascheroder Weg 1b
[0137] D-38124 Braunschweig, Germany.
[0138] The deposit of Rhodothermus marinus strain ITI 378 received accession number DSM 12830, with an accession date of May 28 th , 1999. The infected strain ( Rhodothermus marinus strain ITI 378 infected with bacteriophage RM 378) received accession number DSM 12831, with an accession date of May 31 st , 1999.
[0139] During the pendency of this application, access to the deposits described herein will be afforded to the Commissioner upon request. All restrictions upon the availability to the public of the deposited material will be irrevocably removed upon granting of a patent on this application, except for the requirements specified in 37 C.F.R. 1.808(b) and 1.806. The deposits will be maintained in a public depository for a period of at least 30 years from the date of deposit or for the enforceable life of the patent or for a period of five years after the date of the most recent request for the furnishing of a sample of the biological material, whichever is longer. The deposits will be replaced if they should become nonviable or nonreplicable.
TABLE 1 Comparison of Structural Features of T4 and RM 378 Feature T4 RM 378 Phage type T-even, A2 morphology T-even, A2 morphology Family Myoviridae Myoviridae Genome size 168,900 bases ca 130,480 bases Number of ca 300 >200 ORFs Character- GP3, GP13, GP17, GP18, Putative homologs of the istic GP20, GP21, GP23 same were identified structural proteins Arrangement All of the above genes are on All of the above genes of structural the same strand and clustered were dispersed over the proteins in a region covering 35 kb whole genome and found on both strands Representa- lysozyme and thymidine kinase lysozyme and thymidine tive enzymes (on same strand) kinase (on different strands)

[0140] TABLE 2 E- Source: Accession #: Definition: Length: value*: Spodoptera litura AAC33750.1 DNA 603 9e-08 nucleopolyhedrovirus polymerase (partial) Spodoptera littoralis AAF61904.1 DNA 998 9e-08 nucleopolyhedrovirus polymerase Sulfurisphaera O50607 DNA POLY- 872 3e-07 ohwakuensis MERASE I (DNA POLY- MERASE B1) Xestia c-nigrum AAC06350.1 DNA 1098 4e-07 granulovirus polymerase Lymantria dispar T30431 DNA-direc- 1014 5e-07 nucleopolyhedrovirus ted DNA polymerase Lymantria dispar P30318 DNA POLY- 1013 5e-07 nucleopolyhedrovirus MERASE Buzura suppressaria AAC33747.1 DNA 647 8e-07 nucleopolyhedrovirus polymerase (partial) Sulfolobus P95690 DNA POLY- 875 4e-06 acidocaldarius MERASE I Bacteriophage RB69 Q38087 DNA POLY- 903 5e-06 MERASE Spodoptera exigua AAC33749.1 DNA 636 2e-04 nucleopolyhedrovirus polymerase (partial) Spodoptera exigua AAF33622.1 DNA 1063 2e-04 nucleopolyhedrovirus polymerase Mamestra brassicae AAC33746.1 DNA 628 9e-04 nucleopolyhedrovirus polymerase (partial) Melanoplus sanguinipes AAC97837.1 putative 1079 9e-04 entomopoxvirus DNA polymerase Orgyia anartoides AAC33748.1 DNA 658 0.003 nucleopolyhedrovirus polymerase Sulfolobus solfataricus AAB53090.1 DNA 882 0.003 polymerase Sulfolobus solfataricus P26811 DNA POLY- 882 0.003 MERASE I Human herpesvirus 7 AAC40752.1 catalytic sub- 1013 0.004 unit of repli- cative DNA polymerase Human herpesvirus 7 AAC40752.1 catalytic sub- 1013 0.004 unit of repli- cative DNA polymerase Methanococcus voltae P52025 DNA POLY- 824 0.010 MERASE Bombyx mori nuclear P41712 DNA POLY- 986 0.013 polyhedrosis virus MERASE Bombyx mori nuclear BAA03756.1 DNA 986 0.051 polyhedrosis virus polymerase
[0141] TABLE 3 E- Source: Accession #: Definition: Length: value*: Aeropyrum pernix 093745 DNA POLY- 959 4e-20 MERASE I Aeropyrum pernix BAA75662.1 DNA 923 4e-20 polymerase Aeropyrum pernix BAA75663.1 DNA poly- 772 7e-14 merase II Aeropyrum pernix O93746 DNA POLY- 784 7e-14 MERASE II Pyrodictium BAA07579.1 DNA 914 2e-16 occultum polymerase Pyrodictium A56277 DNA-direc- 879 2e-16 occultum ted DNA polymerase Pyrodictium B56277 DNA-direc- 803 6e-11 occultum ted DNA polymerase Sulfolobus P95690 DNA POLY- 875 5e-16 acidocaldarius MERASE I Archaeoglobus O29753 DNA POLY- 781 1e-14 fulgidus MERASE Chlorella virus P30320 DNA POLY- 913 3e-14 NY2A MERASE Thermococcus P56689 DNA POLY- 773 4e-14 gorgonarius MERASE Paramecium bursaria A42543 DNA-direc- 913 9e-14 Chlorella virus 1 ted DNA polymerase Paramecium bursaria P30321 DNA POLY- 913 4e-13 Chlorella virus 1 MERASE Pyrobaculum AAF27815.1 family B 785 9e-14 islandicum DNA polymerase Homo sapiens P09884 DNA POLY- 1462 1e-13 MERASE ALPHA CATALY- TIC SUB- UNIT Homo sapiens NP_002682.1 polymerase 1107 6e-07 (DNA direc- ted), delta 1, catalytic subunit Homo sapiens S35455 DNA-direc- 107 9e -07 ted DNA polymerase delta 1 Chlorella virus K2 BAA35142.1 DNA 913 3e-13 polymerase Sulfolobus AAB53090.1 DNA 882 3e-13 solfataricus polymerase Sulfolobus P26811 DNA POLY- 882 3e-13 solfataricus MERASE I
[0142] TABLE 4 Accession E- Source: #: Definition: Length: value*: Autographa P41476 PUTATIVE BI- 694 3e-07 californica FUNCTIONAL nucleopolyhedrovirus POLYNUCLEO- TIDE KINASE/ RNA LIGASE Coliphage T4 P00971 RNA LIGASE 374 0.002 Aguifex acolicus D70476 DNA helicase 530 0.25
[0143] TABLE 5 E- Source: Accession #: Definition: Length: value*: Streptococcus P13252 DNA POLY- 877 2e-08 pneumoniae MERASE I Lactococcus lactis O32801 DNA POLY- 877 2e-06 subsp. cremoris MERASE I Bacillus AAB52611.1 DNA poly- 876 1e-05 stearothermophilus merase I Bacillus AAB62092.1 DNA poly- 877 2e-05 stearothermophilus merase I Bacillus S70368 DNA poly- 876 2e-05 stearothermophilus merase I Bacillus P52026 DNA POLY- 876 2e-05 stearothermophilus MERASE I Bacillus JC4286 DNA-direc- 879 4e-05 stearothermophilus ted DNA polymerase Bacillus AAA85558.1 DNA poly- 954 4e-05 stearothermophilus merase Thermus thermophilus 2113329A DNA poly- 834 3e-05 merase Thermus thermophilus P52028 DNA POLY- 834 3e-05 MERASE I Thermus thermophilus BAA85001.1 DNA poly- 834 3e-05 merase Bacillus subtilis O34996 DNA POLY- 880 4e-05 MERASE I Bacillus caldotenax Q04957 DNA POLY- 877 4e-05 MERASE I Deinococcus A40597 DNA-direc- 921 4e-05 radiodurans ted DNA polymerase Deinococcus P52027 DNA POLY- 956 4e-05 radiodurans MERASE I Aquifex aeolicus D70440 DNA poly- 289 7e-05 merase I 3′-5′ exo domain Thermus filiformis O52225 DNA POLY- 833 7e-05 MERASE I Anaerocellum Q59156 DNA POLY- 850 3e-04 thermophilum MERASE I Rickettsia felis CAB56067.1 DNA poly- 922 3e-04 merase I Rhodothermus sp. ‘ITI AAC98908.1 DNA poly- 924 4e-04 518’ merase type I Thermus aquaticus P19821 DNA POLY- 832 4e-04 MERASE I
[0144] TABLE 6 E- Source: Accession #: Definition: Length: value*: coliphage T4 P04530 PRIMASE- 475 3e-06 HELICASE (PROTEIN GP41) Campylobacter CAB75198.1 replicative 458 0.003 jejuni DNA helicase Listeria Q48761 DNA RE- 452 0.003 monocytogenes PAIR PRO- TEIN RADA HOMOLOG Listeria AAC33293.1 RadA 457 0.016 monocytogenes homolog Mycoplasma AAC33767.1 putative 276 .007 arthritidis replication bacteriophage protein MAV 1 Aeropyrum pernix B72665 hypothetical 726 0.016 protein Porphyra purpurea P51333 PROBABLE 568 0.027 REPLICA- TIVE DNA HELICASE Escherichia coli P03005 REPLICA- 471 0.047 TIVE DNA HELICASE Saccharomyces NP_011861.1 SH3 domain 452 0.047 cerevisiae Chlamydia O84300 DNA RE- 454 0.14 trachomatis PAIR PRO- TEIN RADA HOMOLOG Haemophilus P45256 REPLICA- 504 0.14 influenzae TIVE DNA HELICASE Caenorhabditis T16375 hypothetical 566 0.18 elegans protein Pyrococcus E71133 hypothetical 483 0.18 horikoshii protein Cyanidium AAF12980.1 unknown; 489 0.53 caldarium replication helicase subunit Rickettsia Q9ZD04 DNA RE- 448 0.69 prowazekii PAIR PRO- TEIN RADA HOMOLOG
[0145] While this invention has been particularly shown and described with references to preferred embodiments thereof, it will be understood by those skilled in the art that various changes in form and details may be made therein without departing from the spirit and scope of the invention as defined by the appended claims.



1


73


1
129908
DNA
Bacteriophage RM378

1

cgggtctgct tttccttcac ggacccaatt ctccgtgaaa gaaatacgac attcatactg 60

cacctcctgg ttggtttaat tagggttaat gttatacctt ttcaggaact tcgatcgctt 120

taactccctc tgatgaagca cggtttccac cgcggcaaaa atcaccagca gcagaaacca 180

cgctcctatc agaagcagcg ccgtttcaaa ataaacccac ttcatcacaa gccccgccag 240

tacgaaggcg ggcaaaaaac ctgttataac gtaaacagcg ctcatggttc acccctgagt 300

ctggagtgca aaggcacctg taatatccac ccaaccctca tgacgaaata ccgtcttctt 360

gaccacggtt ccgtcgggct gctgctcctc caccgacacc ctcttcgtaa aggaaaacag 420

aggaatgata cagaaagcca tcagagcatt gaccagaaac ggcatgaagt agggcgcgcc 480

tccaatcatg gcggcaccca gcaaaatatc ctccgtctcc ccactcttct tgaaaaaccc 540

ggcggcaaga gcggcaatct cccacgcgcg agacatcatc tgatcgaaat caggaatttc 600

ctcgaacgta agaagctcct tcacccgatt ccactgatca tcaggaaggt ttacaacccc 660

cgcctccatc tgttcgggag tcggattgtg ctgggtgaga ttcagaatcg tcatggcttg 720

tacctccgtt tgtttgttaa gtgatccaca gccagtatac gcataaagcg gaaaaaagtc 780

aatcggtatt ttctttcttc atcttaattt catttttttc cttgagggaa atatccgccg 840

catacatttt ttcggcttcc ttcagcacct cagagactct gctgaagatc tccctgagct 900

gaaccattga ccactccgga tcgtcaagca ccagtggaag cgcgtagccg tcttcatacg 960

tttcatagtt atcctcaaac agatcttcca gcagacgatc cagcagtgca ggaatttcat 1020

atcggtaact cataactcct ccggcggtta acttatcggt aaaccttcac ggatgaaggt 1080

ctcatgtgaa tgaacacttt tgctcccgga tacacttcat ccagaaccat aagcgccaca 1140

agcgaagcaa gcgtcatgta caccccctgg atacctccca ccgtcatata atccagaaat 1200

ctgatcgtac ccgccgaaat ggtatcttca agccccccat cccagataag atattccacg 1260

atggagggaa tctgaaccct gatcttttcc agctcccgct cgatatggat atgcggatcc 1320

gaactacgcg ctgcttccct gcagatacct tccgccagaa caagcaacgt ttcatttcga 1380

ttctgataaa aataattcag agcaccctcg aacagcgctt caggatctgt agccgcacgc 1440

ggaacgcttc tggaaacgtc tttcagaatc tgcatcatga cgcacctcca ttttttccaa 1500

cataaccttc ttatttcctt ttcggttcca cgcaatccca attaccacta ttaatctcca 1560

tcaagtcaga aacccgaatt caatttaaaa cttttctgtc tgaaattccc ttataaccct 1620

taaaacttaa cactaccctt tcaacacaat cccaatcacc agtaaaaacc tacctgcatt 1680

agatctacta ctcccctttg aagcaaaaag gaaaaaacca aaaatcaaaa ttctataacc 1740

cctacaggat acgctcagct ttaagtcgca tattacccat tgggatttta gaattttaaa 1800

attttgtttt tctttaatct ccatagggta cgcttagcat tgagtcttaa tttaccattt 1860

gagggatttt aatttagaag tttttgtttt tctttaatct ccatagggta cgcttagcat 1920

tgagtcttaa tttaccattt gagggatttt aatttagaaa ttcaaaaatt taattttttc 1980

ataaccttga gtggcttatt tacctgtaga gcgtcattca aaaaacaccc catttcaaga 2040

aaccttcaca ttgatctgtc gttttacaac ataaaacctt taagtggtat atgatcagaa 2100

agcgtaaaaa atctgaacat atcggagcgg atgcgattcc aaagggattg gtctatgatg 2160

ttttaaatct tgggtatacc gataagctca aatcccgcat gattgctata ctgagcattc 2220

ttatctacca tcgccaccgg gaagatcaca cctacgagat tgaaacagga tcgaaatgca 2280

agcgcatggt ggaagttaaa aaaggggagt cctggatcag cattccaacg cttattgagc 2340

gggtttacaa cacatttgga attaagctta ccagggagca ggttaaatat gcccttcgtt 2400

tgcttttaca gcatggtctg atttcggtaa aggaagcaac cggtggggtt tcgaaaggtc 2460

attttggaaa catttataca ttcagagaaa cggattttga aggagagttt gtcgatcctg 2520

tggattttgt gagggaaaat agtgaaagtg aagaagaaat ctggtatgca gattatacgg 2580

aaagtcggta ttcgaatcgc gtaaccgtca gagaaggagc atttcatccg attatgaaaa 2640

gtaggacact tctaaaaacg catgtgctta gaaatcatcc agatagagaa aaagctacga 2700

agttttaccc gaaagagatt gttgtggata tcgaagcggg tggatatcgc gtagatgaaa 2760

cagagcggta cagacgcttt agactcttcg tgataaaccg cgctgcgaag tttgcgagaa 2820

agttcagagc acgctacggg gggaaagttg atatatgttt taccggaggt aggggaattc 2880

atctgcatat tacgggaagt gtgctcaatg ttccaatgaa ccgcagtcaa ttcgacagga 2940

ttttgaaaga agcaattgtt cgtatgctta aagatacgga actatggcgg tttttcgatc 3000

cttccacgct gaatcctttt cagcttgccg gggttcgcgg aaaacttcat gataaggctc 3060

cttttgacga ctgggtgtat gtgaagcgta cctatcaaac gattaagccg ctcaaagccg 3120

gaagtctgct ttcgagtttt gaggaggcgg ctttctggat ttcgcgtagc ttcgtcagaa 3180

aagcggctaa aggcaatcca tttagaacgt acagtctggt aaaggaaggg ctactggaag 3240

gggagccgtg gagcgatcac catgcgggaa gagatacggc tgctttctgc atggcatgcg 3300

atcttctgga agccggatac atgacggatc aggtgttgct gtttctgaaa gattgggata 3360

agaaaaacaa accttctctt ggagataaga ttatcgcgca gaaggtaaga tcggcgcggc 3420

ggcttcttgc gcgaaaagga aagcttaaag caaacccttc tctacagctt ctctaattgt 3480

tttgaaaaag tgatagaatc tttccgggga aaagctgtat ccgatcatgt cggtgataac 3540

gctcatcaca ttgaaaaatc gttggacttc atccggattt cttctgtcga ttttgataag 3600

aagttcgatt atacgtttaa acgatttagg ataatcgtac cacagaaagg aaagatatgc 3660

acccgacgat ccttcttcct cttctttttt catgtaagaa cgaatatctt catacagata 3720

ccatatatcc acaatgcttt gagcgagttt ctccataatt ctggtggcgg tgttgctgaa 3780

cgtattgata tactcacagg taacaacata catattcttt ttgatttctt cgataatttc 3840

aacatgaata tttgtttcca gaagataaac agggaaagaa attgaaagtt tttcaagctg 3900

cacaatttta tgcagaaagg tgttttcgcg cacttcccaa tcccacagac atttcacagt 3960

cagatatatt tcatttctta taactttctc cagttcgacg aaaatatacg atttattttc 4020

tataaagccg ggtaactctt catgaatgat gcggtttaag ttgctgtgtt ttttcatacg 4080

ggtgttatct ctcagcaatt ttcttttagc atttgccaca aatctctgat atctttcttc 4140

aaaatcttct tttttgaatt ggatgttggc ttcattttgc aattgtctgg ttcttatagc 4200

aagcgtctca atgaacgttt tgattagaag tattgctccc ttagccatat cctgaatggt 4260

ggaatcggcg ggtaaatcca cacgaaagat ttttcgagtt tcttcgtttt tgatcagtgc 4320

gacgttccat cccattctct tttccatgaa aaacctgagc gcccagacca gatattcgta 4380

gaagttttca gtcattttat tttaaatatt cccttatctg tattccactt ccggagattc 4440

tatatggatg taaagtatat tttttcgtgg tataaaattc atctgagcgt gcaccgcaat 4500

tttcaggtcg ttctcgctca aatgatgctc gccccacctg aacgatccga taaactgcag 4560

cgtgatatgg tgcgtgatca aatccgtaga aaactccagc ttatcatctg tttcgggtgg 4620

aagcacatcg gtagagggaa accgggattt cacatcaaga cgtgcaagca ccagataatg 4680

atggtaattc tcgacgtttg atgccggtga tatgtttttg agtttgtcgt ttaatgtgcg 4740

gattacttct ttcatttcct tttcgatggt ggtatcctct gattcttttc tggagaaaat 4800

gtttttataa gagggtcctt ttttgatatg ttctaccggg gaaatggctt taagcagtct 4860

gtaggcataa tgcaacgtgt cgtttatcat ctttatgaat tttctgatcg caacgcttac 4920

aggtgtatcc tcagagatgc tcaggtagac cagatcgggg tgttttctca aatgataatc 4980

aggtggagag aagccgggat atttttccag atagtttttg atggtgtttg taagcagttc 5040

ctgatacgat ggcattttat tttaaataag tgttgataaa caaacaggct tttttcacat 5100

attcgaacaa ttcatctttg gaaagatggt gtggtttgta ctgacgatgc ataaacttat 5160

aagcaatatc aaacaatacc ctaccctttt cctcactttc tttaataata tctataatgc 5220

tgtctatttc ctctttcagt tctctgtaaa tggttcggta tcggtttatg tcctgctctg 5280

tcaggtgttc actattttca tattttatcc cgaatacaga cataatacct attgttcctc 5340

cgataaattc cagtgttcca ttccgggtag aggcgcttac aaatgagttg cgaatcttca 5400

atgttttatc tgaaacgaaa cttttaaaac ttaagtcaag gagcatttct gtaacaaaca 5460

gaggagcatt caggtggaaa atttttgcaa attttgaatt ttctcgggga aaccatttaa 5520

caaaaccgat tatcattata ccaagatgag cttcctttgc aaaaaccggc ataatgtaaa 5580

gatgaatttc gtttcgaaat tctatttcgt ctgtgaagtg ggtgattaat tttttatcga 5640

tattattgta gtgtatagta tcgtctttaa gttctttcat ttttttctga agtttcttta 5700

atgcctgttg aaacttctcc tcaatttgat ctacagctat tttttcaact ccgatatctt 5760

cttcgaagtg tctgattttg gtaagtgata gttctatagt ctttttaagc gtatgaacat 5820

acatccgcgt aaaatctctg ggtaactgct tttcggcggg aataagacgc acttttacat 5880

aagaaggtcg tttctctata atttctacac tggaaaattc cgatcttttt tttaaaatat 5940

tcaatgatgt tcattgcaag tagtgcttca acaacgcctt ccatagtttt tttagctaag 6000

gttttttgtt tacagttttg tagttttcgt taattaaggt gtttaatgct attggttttt 6060

ttaactattc cccacgaact atctgtttca atacacgata tctttccacc atatcgaggt 6120

ttataatatc cagcgctcta cctatttcat caaacatttc gatcacgcgt tcatcctgat 6180

tgtttttgct gtgttcgata aggtttctga gttcaaaagc tccccgtata ccactggaat 6240

acagaaatgc gatttttgga atatcagggt gtccgggatt aataagagat agaaaatgtt 6300

caatgttttt tatgagttca tgaaggcgat tatactgcat gttgaaataa gcgtgggctt 6360

ttgtcagcct gatgttttct tctatcatgg ggcgcacgta aaaactccca tgcagagcgg 6420

ttccgatatt ggtaaaaact gtctcgtgaa acagaatagc ggaaagtgcg gcgtttttaa 6480

ccggatagag agaacttgca ccaataaccg atatatcaaa cagagcagga aaaaactcga 6540

aaagactctg atcattaaag aaaatatgca tttcgttttt tcgatatacc agatcagggt 6600

atttatgtgt ggtgttaaat attttctgta ttttctgaac cgtttctttc tccttattta 6660

ttttttcttt aaacttctca atagcctgct ggtacttatc atttattttg ctgtctacag 6720

aaaacccgga ataaatggtt cgtgtctttt ttataaaaaa ctcgatcagt tctttgaaca 6780

tgcgcggcgt ttcttttata atctcttttg cggttgcgtt ttcaccgatg tcaaggatta 6840

tggttacatg tttatcgccg gcgtctatgt ttaccggata ctttttttga aatctgtaat 6900

actgctgaat tgcacttaaa atctctttac ggtatttttt cggagtcata aggtgtcggg 6960

tttgatttta ttaaatcact caggttttta agtcgtgcat gtttaaccca gttttttaac 7020

caccctgtta ttccaccata tgacttttcc atctgatctt acgattcctc cgtatcccat 7080

gcggctcagg atctcattga tttttccgtt ttgaggaacg ttgagtgcac caaaatagag 7140

ttcagtaagt tgcttcataa aacggtttct atcctgattc agatcttctt ctatcatcat 7200

ctgaatgcgg gttggaaatg tatctacgat caggtttacg acgtagactc tatcgctggc 7260

ttcccatctt gaaaggaaaa aggaatcata tcgaagcaac cggtcaaacg tttcgtcaac 7320

gacggttttg acaaatgtcg caagttttcg ggtgaaaacg gctccggttt gctcgaaagt 7380

gataagcaac cctttgaaaa gcatttttcg gagtgcggag aggctgtagg gaacgtcaaa 7440

atgaattccc ctttcgacga atccatatgg cggctttcca aataccccct gaagtttcat 7500

tcggtgaagt tcccagccgc ttccaagaaa ttcgtcaatc tgaagttttt taagtttttt 7560

gagatcggag gagttaaggt gcacgccgaa atagttaagt gcgcccccgg tggacgcgaa 7620

aagggggagg ttgtaaaaat cttttggata atcgttttcc tttttgacgt tgagaaattc 7680

ctccggctcg atgatatagt agaggtgata cccgcgctcc aagatttccc gaagggtttt 7740

ttcgtttaac gggatttcgc tcataaggag tccgtttccc tccacagaag acacaatcag 7800

gtttgaggga tcaagcgttt cgattttttc aaggagctct ttcatacggg tatctgcagg 7860

gttatctgtt cgcggttaat ctgcacaacg attttgagaa ggtgtgtggc ttcgtcaaaa 7920

ctcacgtcta tagtatctat gtcgtagggt tcgaggttgg aggcaatcag gttgaacagt 7980

tcatcataat cataattctc gaaaagaatg ttgcgaatac cgatccctct ttctggatcg 8040

tagggatatt cccccggctc gatgaaaagc aggagtttta tcttatcgat caggagtttt 8100

accgggtcat caggaaatct gaaattcggt gcagtgtcgt tcagatagaa catttcattt 8160

ttgtttaaat aaatcctcga ggaatcttca aataaagagg ggcgttaatg gatgaaaaga 8220

ctgaggaata tggtcaatct tatcgatctc aaaaatcagt attatgctta ctctttcaag 8280

tttttcgact cctatcagat cagctgggat aattacccgc atcttaaaga gttcgtcatt 8340

gaaaactatc ccggcactta tttttcatgc tacgctccgg ggattctgta caagcttttc 8400

ctcaaatgga agcggggtat gatcattgac gactatgacc gacacccgct ccgaaagaag 8460

ttacttcctc agtacaaaga gcaccgctat gaatacattg agggaaaata cggtgtggtt 8520

cctttccccg ggtttctgaa atatctgaag ttccactttg aggacttgcg gtttaaaatg 8580

cgcgatcttg gaatcaccga tttcaaatat gcacttgcca tttctctttt ttacaaccgg 8640

gtaatgctca gagattttct gaaaaacttt acctgttatt acattgccga atatgaagct 8700

gacgatgtaa tcgcacatct ggcgcgtgag attgcacgaa gcaatatcga cgtaaacatc 8760

gtctcaacgg ataaagatta ttaccagcta tgggatgaag aggatataag agaaagggtt 8820

tatatcaatt ctctttcatg tagtgatgtg aagacacccc gctacggatt tcttaccatt 8880

aaagcacttc ttggagacaa aagcgataac attcccaaat ctctggaaaa aggaaaaggc 8940

gaaaagtatc ttgaaaagaa aggatttgcg gaggaagatt acgataagga actattcgag 9000

aataatctga aggtgatcag gtttggagac gaatatcttg gagaaaggga taaaagcttt 9060

atagaaaatt tttctacggg ggatactctg tggaactttt atgaattttt ttactatgac 9120

cctttgcatg aacttttcct cagaaatata agaaagagga gactatgaaa gtactcgcat 9180

ttaccgatgc acctacgttt cccacggggg tgggtcatca gcttcacaac attatcaatt 9240

acgggtttga cgcaaccgat cgctgggttg tggtgcaccc gccccggtcg ccaagggctg 9300

gagagactaa aaacgtcgtt attggaaaca ctccagtcaa gcttatcaat tctccgcgag 9360

gatatgcgga tgatccggcg tttgtgatga aggtggtgga agatgaaaag ccggatgtgc 9420

ttgtaatttt taccgatccg tgggcttacc acccctttat gcaacaactt tcttactgga 9480

ttatcgagcg gaatctcccg ctggtatatt atcatgtgtg ggataatttt ccggctcctc 9540

tgtacaacat ccccttctgg cacacctgca atgaagtgat aggaatttcg atgaaatcga 9600

cgatcaacgt gcagcttgcg aaggagtatg tggaggcgta tgaaatcacc atgtatcgcg 9660

atccggaggt attctatctt ccgcatgcgg tcgaacccaa tgtattcaaa cgcatggatc 9720

gcaagaaagc acgtgaattt gtgcggggac ttgtcggaga taggatgttt gatgacagcg 9780

tgatctggct ttacaacaat cgaaatattt cacgcaagaa tctgatggat accatttatg 9840

cttttctggt atacatgctc aaaaactaca ggaaacatca ccttttgatt ataaagtctg 9900

acccggttgt accggtggga acggatattc ccgcgtttct tgccgatatt aattcgtttt 9960

tccactaccg ggatattgac cttcgggaac acattgtttt catttccaat gacgaagtat 10020

ttcacaacgg cggattttca agggaggaaa tcgcattgct ttataacggc gccgatgtgg 10080

tgctgcagct ttcatctaat gaggggttcg ggatcgcttc gcttgaggcg tcgctgtgtg 10140

gagccccggt ggttgctact atgacgggtg gtattgcaga tcagtactcc ctctacgaaa 10200

tggattatga ggtggcggat ggaagtgatg aagatataat ctgcaagatt tatgaggaag 10260

tgcaccgtca ggtgctcaat cagtatctcg atatgctccg tcaaaacgga aaggatccgg 10320

aaagcgctcc ccgcaaaaat catatgatgc ggatggtgaa accttatcgt cattatcagg 10380

gatcgccggc tactccctac attcttgacg acagggttcc tatccgggac gtattcccga 10440

agttcgatga agcgctggcg ctgaggaatc gtgaggatta cgaaaaactt tatgaagaat 10500

cggttgagta catcaccatg cacttcgatg tagaggtgct cggaaaagag ttcaagaaat 10560

cccttagccg tgccattaag aataaccaga aaaccacaag acaggttgtc gtgctatgaa 10620

gaagaaagtg cttcttgttt cgccgcttcg ttccgttagc ggctatggaa ccgtaagtcg 10680

cggaatttat cgcattctga agcgaatgga aaaagagggg ttgatcgatt ttgatgtgat 10740

ggtattgcgg tggggtacgt tttcggaaac cacccacctt gatgatgaaa tcaagaagag 10800

aattcaggag aagtatgatc aggtgtacga tgttgcgatc atggtttctt ctccctacga 10860

ctatcgctac tggaacaaca tcttcagagc gaaacacctg ctctttttca atgcgatggt 10920

ggaaacgaaa ccgttccatc cgaatctgtt ccagcagctt ttcaacttca tgcttcaggt 10980

tcccaccgcg caccttgtgt ttccttcttc cgaaatcaag aggatctggg aagaaatcat 11040

caattcccaa cccatccatc cggcaatggg tgctgcagtg ctctcccgca ttcatgtagt 11100

acccaacccg gtagatgaag tttactatac ttcgaacttc gggaataaaa acgttcgtaa 11160

aaatgtgatc ggcgcgattc gaaagaagat tgaggaaatc cgtcgatcct atgaactgga 11220

gcgggtgttt ctgacttttg cgcctatggg agtagatcga aagaacacca gggttttacc 11280

cgaacttatc gaaatggtgg ggcgggttgg aattctggcg ctggcgggcg gaacaaattc 11340

ttttatactt tacgactttc agcggcttat ctggatggaa ggtgagaaag cctataagcg 11400

gcttccgctt caccgatcga tcgacgttac cccggaagag cttatgttcg tttttggatc 11460

gctgacggtg gaagagctga gtgcggtgat ggatatggtg gatggtggaa tcaacctttc 11520

gcatggagaa tcgtgggatt acctgttgca caacatgatg ctactgggca aaccctgtct 11580

ttacgtcgac ttcttccgtc gggattatat cccttcggag cttcgtgatg tgctgggggt 11640

ggatttcaat atggtacccc tcccgaaggt ggttcccaac attccgcacg atcatccgtt 11700

cttccacccg caaacgatgg tggcggaacc caatttgcag gatgcagcgg aaaagctcga 11760

ctgggtgttg cggaactacg gtgaagtctc aaagatgatt accagccata gagacgcttt 11820

caaaaccgac gatacgatct atgaatttct ggttgacgca ctggagtcga tcgaagaacc 11880

acaggcggca taaaaatttc acattctgga taaaccgggg gaattcgggc atttatcccg 11940

aaaatccccc ttttttgtct caaaaccgtt ttggcggggt agatatttaa tatcaccccg 12000

tggaaagttt aaccccaaaa caggagtgga tatgtcgtac tatactgaag tcggcgcacc 12060

ctactttaca cgtgaagagc agtttgttcg gaatttgctg ttcgacgtaa cttttaattc 12120

caaatattct ttcttcgatc tgacgctgca gcgtcgtctt acctttgagg aagtgctgga 12180

agaggtgctg gcggtgtttc atgcccgaat cgaggaagtc tgcaaaccca tttatcgcca 12240

gcaggcgcac cagtacgtgg agaagttcgg cgagtatttc cgccagcgca agctttttcc 12300

ctcgatgcgc cttgtgcagt tttcgcgcat ggttccttac aaccacaccc gtctttacaa 12360

ttgctcttat actcccgttg attccattga ttcgatcgcg gagcttttct acctgatgtt 12420

gtgtggcgtg ggtgtgggat acagcgtgga gcgtaaatat atcgaacagc ttcctgttgt 12480

atatcccgaa agtgaggggc agacaatcac ctatcaggtg gaggattcga tcgagggatg 12540

gtgctcggcg ctcaagcgtt atctctatgc gcggtttacg cccaaccacc cgaagattgt 12600

atttgactat tctcttttga gaccggaggg aagtgtgatt ggaaagcgtt acaatgctgc 12660

atttggttat actaaaaaca atcccatcaa agaagcaatc gaggcggtaa aggggatttt 12720

cgacaaagca gtaggaagga aactcaagcc gatcgaggta catgatctca ttacaacgtt 12780

cggcatgatt atcaatcgtg cgaacgtgcg cggaatggcg gcgatcgtct ttttcgatta 12840

tgatgatgaa gaaatgcttc gctgcaagga tttcacgcgc ggcgaagtcc ctcagaaccg 12900

ctggtatgcc aacaactctg tcgtgttgta tagagacggc gataaacttc gcggagtgcg 12960

cggggaaatc gtcgatcttc gggatatttt catggaagcc tattgtggga agtctggtga 13020

acccggcgtc tttgtaacca acgacgaaca ttatcgcacg aacccgtgtg gtgaagcttc 13080

tctttatcgc aatttctgca accttacgga gatcgccatt ccccgtgttc atcagagtga 13140

gatcgcggat gtgttgaaca cagctatctt cattggtgtg cttcagtcta cgtttaccga 13200

ctttaagttc cttcgcgatg tgtggaaaga gcgcaccgaa gaagacaact tgcttggcgt 13260

ttcgctgacc ggcatttacg aaaatctgga tgcgctcaaa gagtacatga agctttcttc 13320

gaaaggtcat gtcaaattca tggcggctca atttgccggt tggttcgggt tgaacaaccc 13380

ggctcgcatt acgctggtca agccctccgg cacggtgtcg ctgcttgccg gggtttctcc 13440

gggttgccac ccaccctatt ccgaatattt tatccggaga aaccgggtgg atatgaatca 13500

catgctggtt gaagttttga aggattatcc gtttatcatt gatgatgaag tgtatcccga 13560

taagaaagtg atcgaatttc cgcttcgggc gcaacgccac tttacgcacg atcccatgtt 13620

tcaggtgcgt cttcgcaacc agatcatgag gggctgggtg gaaccctcgc ataatcgcgg 13680

caaaaacaca cacaacgtat cgattacggt ttatgtaaga gatgaagggg aagtggagat 13740

tgtaagtcgc gaactcaaaa atgagcgaaa catttcggga atcacgattc ttccggtggt 13800

tgagaatggc tataaactgg caccattcga agcaattccc agggaaaagt atgccgacat 13860

gatgggcgaa atccacgtgt accttgatag aatcaaacac cagctaaacg gcacgcccga 13920

ctccccgcgt ctgaaactga tctccgattc cgacgttttt gagggagaga aaggttgtgc 13980

cggtctgcaa tgctatttcg acatgtaaca tgaaactcgt acttaaacac tccagagaag 14040

agtctttcta tcctgaaaca ataaaaactc ttgatcatct tagagagaat gggtgggaaa 14100

tcgttctcct acaggataat cgttttaata tcatagaagg ttacgatttc gatatggtga 14160

ttaccacgtc gaaccctcaa tacagctttg cggatttcca caatgaagca ttgaaatttg 14220

ccaagcacgg ggagtggctt ttttatcttg atttcgatga atatttatgt gataattttt 14280

gtgaaagggt taaaaaatat atcaacagag atgttcattg ttacaacatc gcacgcataa 14340

acattataat tcctcaggag aaaacgggtg atgtgtgcgg gatgtacgga tggcgtagtt 14400

ttaatatcaa tatacctgag gaagggagtg taaaagcgat aaatttcccc gattaccaga 14460

cgcgtctggt tcgcgccgga accggcaaat ggtacgggaa cgcccacgaa cgctttgtgt 14520

gcgataatgc ttttaaacac aaaacgttac cgtttgatgg tggatatatt atccaccgta 14580

aatcttttga gaaacagatt accgataacg cgctctggtc aacctataca ccgtgatata 14640

tgttcagcgt aattctcata cacggaaacg aggatcttat caataaagaa ctgatagata 14700

atcttaatga attcagggaa gcaggatgtg aactcatttt gctgcaggat gatcgttttt 14760

caccgcccga ctttttcaaa tttgatattg ttataaaaca ttccgtttcc gaagggatgg 14820

accgtcatcg aaattttgcc aatcaacatg cttcttttga atgggtgttg tggttggatt 14880

ttgacgaata tctattcccc ggatttacag aacgagctcc tgaatacatg aaaagggata 14940

tatgggggta tggattttac agattgaaca tgatcgttcc acctgaaaaa acttcatggt 15000

tcgttcagaa ttatggctgg tatgaaatgg ttgggtgggt ttcaaccata tcgatcaggg 15060

gggtttctta tcaggctata aattacccgg aggttcatta tcgttttgtt cgaagagatt 15120

gcggcaagtg ggttggtaaa agacatgaat actggtattc aggtgatttt cgtaaaaaag 15180

ccatatttcc ggcggatcga gaaacacttt tccacgttaa acccattgac aaagcaataa 15240

gagacaacta taaatggagg gcactatgat gaaccccgaa atgaaagaga ttctgaagaa 15300

gcttatgaaa cccttccacc ctgatcgcca ttcctatcgc gttaccggaa ccttccggac 15360

tcgggaaggg cggaacatgg gggtggtggc attttacatt tcatcacgcg acgtgatgga 15420

tcggttggat gcggtggtgg gaccagagaa ctggcgagac gaatatgaag tgccggctcc 15480

gggggtgatg aagtgtgtgc tttatttgcg tataggtggg gagtgggttg gaaagagtga 15540

tgtggggacc ggcaacatag aaaaccctga aagtggatgg aaaggcgccg cttctgacgc 15600

cttgaagcga gcggcggtca agtggggaat cgggcgttat ctctatgcac ttcccaaatg 15660

ctatgtggag gtggatgata gaaagcgtat tgttaatgaa gaggcggtca agtcttttct 15720

ccataagcat gttaccgaac tgctgaagaa ttatcagtaa cccaaaccta aacccgaaaa 15780

atatatggaa acgattgtaa tttcccaaaa caatacgacg gagatgacgg aaccccccca 15840

gaacatttcc gattcggtta aaagcgggtt tatctatctt atcgaaaagt ctcatttcct 15900

tgaaaagaaa aacttcctta aaatcatatc gaacatggac ccccgccgca tttccaatcc 15960

ggaggtgcgc gtggtggcgg agtacatata tgattatttc aaaagtcata gtaatttccc 16020

ttctaaaaga aatctttgcc atcactttga gtggagcgaa gatctggaag gagaccccgc 16080

cgattatcag cgtatcattc agtatctcaa atcttcttac attcgatcct ctataacaaa 16140

aacgctttca tatcttgaga aggatgacct ttccgcgttg aaagaaattg tcagagccat 16200

tcgggtggtg gaggatagtg gggtgtcgct ggtggaggaa ttcgatcttg caaccagcga 16260

gtttaatgaa ctttttgtta aagaagaacg cattcccacc ccctgggaga gtgtaaacaa 16320

aaatatggcg ggcggtcttg gtcggggaga gcttggaatc gttatgcttc cttcggggtg 16380

gggtaagtca tggttccttg tttcacttgg tcttcatgcc tttcgaacgg gtaagcgcgt 16440

gatttatttc actctggagc ttgaccaaaa atatgtgatg aagcggtttt taaagatgtt 16500

tgcaccttat tgcaaaggac gcgcttcttc ctatcgcgac gtttatcaaa taatgaaaga 16560

gcttatgttt tctcaggata atcttttgaa gattgttttc tgtaatgcga tggaagatat 16620

tgagcactat attgcgctgt ataaccccga cgttgtgctg attgactatg ccgatcttat 16680

ttatgatgtg gaaaccgaca aagagaaaaa ttatctgctt ttgcaaaaaa tttataggaa 16740

acttcgtctc attgcaaagg tatataatac agcagtatgg agcgcctctc agcttaatcg 16800

cggttccctt tcaaagcaag ccgacgtcga tttcattgag aaatacattg ccgattcatt 16860

tgcaaaagtt gttgaaatcg acttcgggat ggcgtttatt ccggatagcg agaactcaac 16920

ccccgatatt cacgtcggat tcggtaaaat cttcaaaaac cgtatgggtg cggtaagaaa 16980

gctggaatat acaattaact ttgaaaacta tacggtagac gttgctgtta aatgacacaa 17040

gttaagacaa aagggcttaa agacatcaga ataggtagaa aggagggtaa gttcacacat 17100

gtaaatacaa caaagaaagg aaagaataag aaatatttca gggcggaaca tgaacgcctg 17160

tttctcaacc ttattcgagc acttcaggtt ggggattatg ccgaaatcaa ttctcttttt 17220

cctcttgtcg aaaagcaact ccgatggatg gtacgaaaga tagtgaaccg actcaatctc 17280

acttcacttg tttcatatta tgaccacggc gaatgggagc atgatattgt aagttatgtg 17340

ttctccaaac tcgataacta ttctcccgaa aagggaaggg tgttcagtta tatcagtgtt 17400

atcatagtca attatgctat caatttgaac aataaaattt attataaccg ggtggggtat 17460

cattcagatt tctatgcaga taatcctacc accgaagact acaagggtct ggatgaaaag 17520

gaagagttga gttatgaaat agacgatcag attaatctga agattgattt tgagcatttc 17580

tgcaatctgt ttttaaatgc ttccgaagaa actttactca agcattttca ggaagacgaa 17640

gtttttattg ttaaaaatat tgcgctttct ctgaaatatg atccggatat tatcacgacg 17700

ccttttctgg gggttgtaca tcggatgatc tgtgagtttt gtggggtgga attttcccgc 17760

tataagtttt ccaaagtgtt caagaaaatg gttcaactat accacgaagt ttttaacggg 17820

gggtaaaggt tatttaaata aaaaatatgt tttcggcttc tgattataaa ggaaacgtaa 17880

cttttagttt tcacttccct tcgcttctca ccaatgccgg atcgcaccca aataaggcat 17940

atgtgtatta cgactatatg ggtagtgatc tggtgttcac tttttctcga ataagattca 18000

gcctgtcggc acccggcacc tacgatgctt attttgacgc tcatattcag gatgttgaca 18060

ccattacctt cgattcaaac ggataccgtg agctttattt cattttcagc gtttcctggg 18120

aaggatccaa cacttcgggc accatttcgg gtgccaatct tatcagcgta tcttcctttg 18180

ttactggata ccccgaaaac agttttcttg cctatacgct ttccgtttac tctgcttccg 18240

ccacaaccta tcttaacctt aatgatgctt acagaattta cgtagggaac attttcggca 18300

ccccgcaatg ggaagttggt tttaccggta gtttcacggt ttctgctacg ccttcaattt 18360

ctcacaaccg tttcaggatt ttacttcttt ctaactttga tagtgcactt aattactata 18420

ttactacgtt cagcgcacca gcattcgcct cacattcatt tcaggttatc aggaaaatat 18480

atgaagttga gccactttct gcttacacag taccgtctat cgtgtttttc tacacggttt 18540

cagctactaa cagcttcggg tggagctatt ccaatataga aatggggtct ctttacagaa 18600

tatcaactat gtccattcta agttatcctt acccctacac ggcaccggct ataacgtata 18660

tcactttttc tggcggaatt gtttcggatg aagaatttat tgtaaaggtg cccataaccc 18720

tttcttatat taacaacata ataccgtatt tcatcggcaa ccccactacc acttcaaaca 18780

ttgacgatgt gaatgctact gaagataaaa ttatccctac ttcgataagt aactttaaaa 18840

caaccctttc atttcaggtt tttgcttttc cgaacacact ccctgttaaa acggaacaag 18900

tatcaattcc cgttaccttc agtccggaaa cgggcaacat ttctattcct gtttccatct 18960

catttcctgc gtttgtaaga actgctgcgg ctacaatgga taatccgggc aatttttcca 19020

cttctgtcgg aaatggtatc gtggttagcg atcttgtgtg tcagaataca gggaatatac 19080

ctattacatt tagtggtgtc agtcttgcaa tagacgatgg taactggtat gtggacaccc 19140

cctccgtggg atatggtttt aacccgaaca gcgggttttg gttcgatgtt cactttatgc 19200

cttatgggga tgtaaactac agtcaatcca tttattttac gttttcgttc aattatccaa 19260

caaattatgg aaatatattg tcaggtagtt ttgttgaatc catttctttc catgcggttg 19320

ctacaggaac cgccccttcc ggtcaggtgg gtattacggt gtccaactgg aatgtggaca 19380

accctaacac cgttatggtt ggtaaatatg ttaccggttc cttcagcatc acggcaagtg 19440

ctacaaacaa tcagatcgct caggttaccc tgacttcatc aacccccaat ctgtatttca 19500

cgacggtttc aggtgttggt attaacaatc ttcatgctac ggcggtaaat tctctggcgc 19560

tacaggttgc tcccggagct tctctttctg tttataccca gtggtatatg aatatggttt 19620

atacggcttc ggctcctgat gtaaccatat cggtaacgtc ttctaatgct acggaaatga 19680

acggcgtgcc gggattgacg gaagttaagc gatcgcattc gctgacgaac cctgctcgat 19740

atgcaaattt gaatatagga attttttcac tcagtgctta tggtcccttc tatcaatcaa 19800

ccgcctctat tttgccgttc ccttattctt ttagtcttgg gggcatcaac gtcgttagaa 19860

atgttggttt ggcttggctt gatttttatc caacgaacag cactcattct gaaatgtatg 19920

ttaaattgac catgtctctg acaggatcgg ctttaaatgt tcatagcgta gtaacttcat 19980

cgtatttttc tgatccttct aatttcgagt gggaagtcaa cactttgcag catactctgt 20040

tcagcccccc ttatggatat tttcttcata ttagaataag accgactcca agtgatatta 20100

acataatacc gacttcaagt gcatatggat atggtacgtt tgttgtaagt tggagcatga 20160

gtcttatttc ccatataaat ggggtaagcg tggcttctct tggacagggg tattcaaatg 20220

ctttgagttt gtggtttgat catactgttt tctatgaagc accatagtaa tttcttatct 20280

atacgacaca tacttgataa aattgccgct ttctcccatt tcaaaatatt ttctgagcgt 20340

agaaggagta aaatccgtgg cgtctccaag ctttcgagtg ggggtgatca gtgttgcgtt 20400

gattttgaca tagtggcttt tgatcatttt gttgtggggg aaaagcaggt tgtaaagcgc 20460

catctggttt acgtcgttca aaagatgttc atgccagaga atatcgtaag tgcgggtaag 20520

cagcgcaaga agattggtgt agtagttccg ttcttcctta atggtgtaaa gcggcgtgca 20580

ggaaatgatg atcgcttgaa tttcctcacc cggctttaat tctttaagtt taataaggtt 20640

ttcaatggta aacccaagcg gaatcacttc tcttacccca ccgtctacat aggtgttgtc 20700

tccgatttta accggaggaa agaccagcgg aatgctacaa gaagcaagaa tggatttgag 20760

aagaagttcc tctttttgct cttccgggat ttcctgatct tcaaaaaggt agttaccgtc 20820

ttttacaacg attccggtgg atttgccgtt ttgcaaattc acagaacaat tgatatagat 20880

tttattgaaa ttcagaagcg ggagcacgtt tttctcaagg tatttcccaa gaggggaaaa 20940

atcatacaga taatttcgtt tgagaataag tgttttgaga agggcaaacc actcaggctg 21000

ctgtttgtaa acctgtttcg gggaaagaga aagccacatt tgcttcatga gatcggtacc 21060

tttcggggta agcgccgcgc gggaagcaca ccacacgccg ttgatacttc ccaccgaagt 21120

tccggctaca gcaagaattt cgttgtcttt aagcgctcct tccctcacca gacaggaaat 21180

gacgcccgcc tgaaaagcac ctttggctcc tccccccgac aggatcagca gttttttcat 21240

ttttaattaa ataatgctca ttttcccgat ggaagcatgg aaatccactt caatttggca 21300

aatccgtctt ccgttttccc gttgatcata tatgcgtagg ctccaaagac gtgagctatc 21360

ttgcaatact cctcttcgtt gtcaataaag attgtatagt ggttgggtgg aatgattcca 21420

tagatgagtt cgtttacttt cccgattttt ttgcccccga caatgcggtt gggaagtgga 21480

agattatgtt ttttcaaata cgactcgatg ttttcccggt ggtttgcgct caggatgtaa 21540

aggcggtgat agttcggatt tctttttacc agatcgtaaa gataggtgta caggttatga 21600

aatttcgtaa tcgttccgtc gaagtctata cacaccgcca ccttgattgg tttgacaaga 21660

atccgggaga gcaatatatg agcggatttg tgcatagtca tagacacctg atccggtgaa 21720

agatcgataa tgcggggaaa tttgtaaatg cggcggagac ggttggtaag gtagcggatg 21780

tatctatcca ttcccatgta cttctcgata atatcaaggt attccggatt tttccttaca 21840

aacacctctt tcatcaggtg tttaatatga atggtttccc gtcgggtgag aagaagtttt 21900

gttaaacctc tcacccgcaa ctcttcgaga atctccggag ataaatcttc gaactggaga 21960

taaagcgttt cgtcaatggt ctgcatattc atagtttact caggtatttt tttgaacatt 22020

gtattaatgg tgtcgatttt cttgatgtaa tcaacgaatt tgacaccaag ttttcctgta 22080

acatttccga taagaatatt ggaagcgttc aatgccagtg cgggagtcag atttgaaagt 22140

cttgcaattt caaacagcgt cgggagaata tggtttttat tttcgatttc ttccatcaaa 22200

atggcgtcta cggcgttgta ttccaccaac tttttatccg ggtagacagg aatctcatga 22260

tagaatctta cgtcgaaatc caccttacct tctcctattt cctctcgcgc aatatagtcg 22320

agccggtagg actccaactc tttgtatgcc acaaaggagc gataaagccg catgtaatca 22380

aaaaacacaa attctacagg ggtacgggga ttgaaataga atggtaggtt tcgatcggaa 22440

attttccgca ccagcttcca gtccggaagc aacttatcac taatgacatt cacctcatgg 22500

atatgactac gaatgagcag gtagggataa tcgaactgat aaccgttcca tgcgagcatg 22560

aaagtaaatt ttggtttcag cacattccag aaatactcga gcaatctttt ttccgaaagg 22620

aatgttctgt aatgaatttc aaatgtgtta tcccctacgc tggtggtaaa tttgttaaag 22680

ttatcgatat gagcctccgg gttggtgata aggagaagca ctaccaccac cggttttcca 22740

tacggtttga tggaaatgga ataaactggg tctctccacg ggtcgggaaa gctttttttc 22800

ggggaaatcg tctcaatatc gataaagacg cactgagaca aagcttccgg cgtgatgtgg 22860

cttttttgtt ctctgatgta ataggatata gcctcagcct caatcttccc tcgattctgc 22920

tgagcgatgc gcttcaaatg tgggggtacg ggtgattgaa ataagtgttt tttcccctcg 22980

attagctcca ctccgtaaat tttcatcgat cgggggtata cgcttgcgct tagcgtgatc 23040

ttcataattc tccttcaggt cttcttcgag gaaatcgttt aacgattgaa gcaactgata 23100

ataagcttcg cgggtttcga gcatgtcgaa tacttgcctg tgaaaaaaca gaaaatctct 23160

tatcttgcgc gtggctccga tcagaagacg gtgtttccgc tggaggatgt tataccttat 23220

gatataagta atcagcaccc cacttacggt tgccgcaata gcaaccccca accagaaata 23280

tacttcctgc atggtttctt tttttcttca aaaaaacctt tccgtgaaaa aatagtttca 23340

actggtaact gcaaacaaac ataaggagag agtcatgctc gacttttatc gctgctttgt 23400

caaaatcttt cagaatagct acttcgccaa cccaacaaaa taccggtttg gcgaaaaggt 23460

cagagaagca gtgttcaact ggggagcacg cgtggcacac cacgacatca attcgcgaga 23520

aaccgaaatc gttgcagatc cggagatgga tgattatttc agaagatcat ttttctccga 23580

aaacccctat atgcttgtta aaattaccca tcccgatgaa tcgatgataa atacggtaat 23640

atggcaaagc aagcgatatg aaaacttttc ccgcgtctat caactcattc gcacaattgc 23700

acagatgaga gaagaagaag tcgataacta catgaatcag atcatgccgt ttattgcgtt 23760

gaatctcaat acgatcaatc gctatatgaa caaaacaaat cttctctttc aaacccctta 23820

tgatgagtta tacggtttca ctctgctttt caagtcggta attcgcattg ccgaagaaga 23880

aaacgaactg gagtatcttg cgaataaaga tgtcattgat agttataata agaagattga 23940

ggaatttttc aataccgatg aaaatatcgc tacatttgga tatgttctaa aagatatgct 24000

gtctcactgc attattgcca tcggtatgat cctgctggaa gcgaaggata aaacacacat 24060

gaagttttat gaggaacttg gtgagtttat ggcggaaata ggtaaggtat acttaaaagt 24120

gatagaggaa ggtgagaaag atatgaatgc gctgacgcat ttatacctct ggtgtatgat 24180

tgccggttgt atcattaaca tgttgaacgt caggattccg gatgaattgc ggttggctgc 24240

tatcatggtt gaagaaacgc ttgcctcgca ccaactgcaa ccctttattt cgttaaactg 24300

aagaggggta tgatacagaa aacaaccccg tataaaaact acaaaaagta catggatcag 24360

cggggagaag tgctgagacc gcacccccgc aagaaggtat atatcccatt tcttattgcg 24420

gaatgtggaa cttatctatg gaacgacata agaaacatga tgtttgcgct tccggggtgg 24480

aaagatgtgg tgaaaaaata cggtgtgggg gaaaaatcca ccccggagcc tttctatgat 24540

ttcctttcgc tttttatcaa gaatactacg ctttacagtg attatagaac caaacaaacg 24600

ctttttcaat cgcgaataga gcgcataaaa atggaagagg aagtctggaa tctttccaat 24660

gcactgatca atctgttctt ttatctgaaa gagcattatc cctattattt ctcaaaagag 24720

tttgtctttt actttgacat taatttctat ttcaggaagc tcacatttta tgatattctt 24780

gccggggaag atttgcggaa taaaatcaac gacacatttc agaaaatgct ctctaaaggt 24840

tacacggtac acctttcaaa aatgaaacct cagagtagag aagattatct atgtttgcgt 24900

tatgccgaat atatggaagc tattatggct cgagatgagt tcaagcagga aatggatatg 24960

aaagggagtg ggaatctttt ttatcttatt gatggtttta aatgggggtt gataaataga 25020

aaagatgaag tagaatttgt tgtactggta aggtaaaaac tatataaata aaaggggtta 25080

gtttatggcg agctggactt acgataccac ttcgcgtatt ctgtcaatta ccgttagtgt 25140

ggtggatctc gacaataacg atgtactggt ttacaccggt agcaattatc ctacatggtt 25200

gagtccgccg accacttcgt acgtttccgg ttcgttgtct ccaaagcagt ttgatgtgta 25260

tatcagcggt agcacgctca acgttcagac agggtcttat caggttgatt tgcttgccat 25320

tgaacagggt gtgtcgttcc cgctcacctc ttcggcaagc ttcacgatta cggttacggc 25380

ggtttaacaa attttaggca agaagtctcc atcctctaca gggtggagat gaattgccta 25440

ttgacaaaat tcagtggtgt attacaataa aagcaagatg tttagagcat acaaatacag 25500

gatatatcct aacaaaaaac aaaaagaacc cttagagaaa acttttggtt gtgtggggtt 25560

ctactggaac agggcattag aaatcaaact caaagcttta ggaaataaag agaaaatacc 25620

acaggtcttg cccgccttaa gggtggtagg gtcggaacga cccgaactta tgcctgtgga 25680

ggagcgggta gctccgatga agcaggaagc tccatcttct acaagatgga gtagttcact 25740

tcacagaaac tttatttctg ttttatcgtt ttttccgtaa aaaaaaagaa attatggttg 25800

taaaactacc gctgcatgat ttttaccctg aaggttcacc tttcaaaacc gaaaacttta 25860

cggtaaaaga ccccaccatt gaagacgaag accgcctttt caacccggat cgcatcaagg 25920

ggggatatgc tctggatgat tttgtgagag gactccttcc cgaagaggct cagcgccagt 25980

acggaaacat gttcctcatt gacaggaatt tcattctgta tgccgtcagg gtggcaatgt 26040

tcggagacac cattgaattt cgggaaaaca tcgaatgttc tcattgcggc gcttcgcttc 26100

gggaggctac catagacagc gaggttttta ttcccgaaaa tcgtaagttt gagttaaaag 26160

aagggggtta ttttatccgt tttaagttgc ttaccgtttc agatcagaat gttatgagaa 26220

aagatccact catgaaaagc aactttctga cgcgcacgct ttattacgta atcgatacga 26280

ttgaaaaaga agagagcgac attaccgaca aatatgcgct tatccgttct attcctattt 26340

cacttggcac caagatcaga gagtttctga atacacaata tcctcgattt gatattttca 26400

tcaaatgcgg ttcgtgcgaa agcaccatcc cctttgagat gaacgaatcc tttttttgga 26460

ataagttatg attcagaaga agagcttgaa aaaatcgtgg tagaacggta tgaagcccga 26520

aggaaattgc ttctctttct gaaagaactg gatacctatt ccagtttaaa aacgaaaatt 26580

tctatatcag aactccgggt aattgcctat atgtataccc agcaactgga agagcaggaa 26640

agagagttca agcgttttcg gggaccgcac tgaagtcaag cgtggcgtag tcaaattgaa 26700

gggtaagctg cacgttcaca agacccgaag catcggagaa gtcgagcgag tcgccgttga 26760

tgtcggcaac ccaggctccg tggaaagtcc attgttcaat tacggcaccc tgaggatcaa 26820

gaagcagaag ctggatattt ttcttgtaaa catcctgata gccgtcgcgc ccggtggtag 26880

gatcgtggtg tgcaagtacc cactggtaaa ccgccatcat ccccgattcc tcgattggat 26940

cataaagcgt caggttgatt gggttccagc taatttttcc cttatatttg aagtaggtgt 27000

taatgtggtg cacttcgccg acggcaaagc tgaaattagg acgcgccgaa gcgtagacca 27060

tgtaggcggg aatcccgtcg atctgcatga ggaaaaggcg tttctgcttg ggttcaaaac 27120

gccggaaaag catgttttca acaacgcgtg ccatatcgtt cctttttctt taaatatgta 27180

taaatcgttt ttcaaaaaaa tgacagggaa aaatatttaa agttgacaat taacaacaaa 27240

accggaaaaa atatgtatag ggtaaacgta aaagaagtag acctttcgat tacccctgaa 27300

gtcgggacac cggtccaaac ggcgcttgta ggtgcgttcg atctaccgat tcccagcgaa 27360

cttccggtat cggtaacccc cgatgaattc cgccgcgtcg gatcaaccga actcagtctc 27420

attgcagatt cgctggtggg tggtcaggag gttacggtga tcagaccgcg aggagaaacg 27480

caatcgctga atgcggcatt tgttgtggtg ggtggttata atgtaaccct tggtgccttc 27540

aacgttttct atctgatgtt tctggggtat gatcctcaga aaggatatac tgatgtgtct 27600

tatgtagatg tgcaattggc tggtacccca acggatacca ttctgttcag ctactcgctg 27660

gacggttctt cgacaacgca ttcacttacc ataaatctaa acgcccccag tgttacgcta 27720

ccttctaata tcgtaccgct ctttttctac tatgaacctt atacgggttc gattacgctc 27780

cagagttccg ttaactatag tggattaaca ctgaattata cggtcagcaa agcgaccact 27840

ccttgggtgt attttgctga atatggcacg ccaacatctt ctcttacgct ttataaagga 27900

ttttatctgg aaggaattga cctgaacagc tttaacaaac aatttgttgt atctatcgaa 27960

aatattacgg taaatagaga aaaaggtcag gtgctttatc cttcgtttga tgtggtggta 28020

cacttccggg atattagggg ggtcagtgcc aataccgaat atattcgctt ccgtcaggtc 28080

aatctcaacc ctgaatctcc gaattatatc gagcgcgtaa ttggcaacat gacctttgag 28140

tttgacggtg agcgcattgt tacaggcggt gaatacccca atcaggtacc cttcctccgc 28200

gtggtggtct ctcaggatat taagcaaaac gtcgccgggg ttgaaaagtg ggttccggtt 28260

ggatttgaag gtatttattc tgtaggcgac ttcactgtta ttgttaacga attgaccaat 28320

gtgtcaatcc cggttacgga ttcggctatt attccgccca tgcggtttac ccgcattgaa 28380

cagattacgc tgtcgggcgg tgcttcgttc agcgtgatca gcaatcaacc gtatggtttc 28440

aatattcagg attctcgtca tagctactgg ctctcacctt tcaaagatga tgaactgata 28500

atcggaaccg aactggtact tccggctctg gatgtttcaa cggaattcgg agtttcaagt 28560

tgggaagaag cacttcctga attcagcttc ctgatgccgt tccagggcgg ttcagacgga 28620

tacattcgcg ttgatgaaaa tgagccggat acaatcgggc gcgtgaagat cactccggca 28680

ttgcttgcca actatgaaag gttgcttccg cttctgacgg aagatcaatt cgatctggtg 28740

ctcacgccct atctgacgtt tgctgatcat gccggaacgg tgaatgcttt catcaatcgc 28800

gccgaaaaca ggttcctata tctgtttgac attgccggag atgatgatac cgaaaatctg 28860

gctatttcgc ttgctggata tatcaactcc agcttcgcaa ctacgttctt tccgtgggtg 28920

cgtcgtctga ccaataaggg aatgcgtacg gttccggctt ctcttgcagc ctaccggagc 28980

attcgcacca ccgatccgga gacgggtctg gctccggtgg gagcgcggcg cggcgtggta 29040

acgggcgagc cggtgcgtca ggtggattgg gaagacctgt acaacaaccg aatcaacccg 29100

atcgttcgcg tcggaaacga tgtgcttctc ttcggtcaga agacgatgct caatgtcaat 29160

tcggcgctca atcgaatcaa cgtgcgtcga ctcctgattg ttatgcgcaa tcggatttct 29220

cagattcttt ccagctacct gtttgagaac aacaccagtg aaaaccggct tcgtgccgaa 29280

gcgctggtgc gccagtattt ggaatcactc cgtctccggg gcgctgtaac cgactatgag 29340

gtggcgatcg attcggttac cacaccgacg gatatcgaca acaacacgct ccgcgcacgg 29400

gttacggtgc agcccgcccg ctcgatcgaa tacatcgata ttacctttgt tatcacgccg 29460

acaggcgtag aaatcacctg agaaataaac ctttcaaaat ataaacccgc ctatcaaaag 29520

gggcgggttt ttttatttaa aataaaatga agtttaacaa ctgggttgag tataccgacg 29580

acgtactccg acttgagtat taccttgagt acgaaattcg ccggtggaga tatcagtatt 29640

gtgatccgtt ccccactttt gaagatttca aagaggcggt caaaaaagcc cctcgaatta 29700

tcgtaacgcc ggaacttgat aaaattataa gaaatcgttc tcgaacccgc acgtttgacg 29760

aactgcttgc attgattaaa acttaccggg gatatccgaa atttcgcaat gaaaagacgc 29820

ttcaggctat atatgacggg tttaaaaaca ataaacccat gaaaatgccg atcgtgttgg 29880

agcttcccga cggaacatta cgggttatgt ctggaaatac ccgtatggat gtggcattcc 29940

agctcgggat aaaccccaaa gttattctgg tgaaggttcc tgataggtgc cattaatcca 30000

cactttccat atcaccatac tgatctacaa tgtaaatctt gttgcagaat tctttaaatt 30060

tattcagcgg aaccactttg gggttggtga tagcccattc gtttacgata aatgcgtgga 30120

gacgcgatcc catttctttc aaatccctct ggatttgttc aacttcatca tcccattccc 30180

catcacttat cttatggatt cctccacttg gtacgggttt gccaagatag tgaaaaatga 30240

aagggtggga ggagtcgttt ttaagccgct gcaggatttt ctgacctgct ttcgaggaaa 30300

cgctgaacat tttcttttaa ataagattca taatcttcaa ttagcggaaa gtgttcaagc 30360

tgtttgagca gggtgttaac ttcataggca aaacgaaagc gggagttctg gtagaagtct 30420

ccgattgtta ccggaattct gaaatcagga atgtttttga tttcattgtc ttcaatattg 30480

aagacgaaat agcagtgaat gagcgggttt tgaagctctt gcttgataac ataacgatcg 30540

aacattttga tatatttcca gatcacttcc cggttgttca aatagatttc ttttgcccga 30600

ttcgggagaa actttgttat gaagaaatcg tcaagcagct cttcgatctc acttagtgca 30660

ctggtctgct tgttaataaa gcttttaatt actccgttga aatccccaag cacacattcg 30720

gagctatcgt gcatgagcac acaatagccg aaaagcgcat cgctacacac ttcgcgagcc 30780

acgtcgtaaa caatcagact atgttcgagc acggaataaa aatattttcc tccgtttccc 30840

tgatagcggc aaatgttgga gagccttgca gcaacatctt caatggtaat acggtgaagg 30900

ctcgggtgca attcgagttt catggtgtta tgactgtttg gttcacacga cacaatcctt 30960

aaagaggata aggttaaaag aggttccctt ccttcaatta aaattcaaaa atgtcaatat 31020

caatgtcaag atcagtgtcg tcttcggttt tacgttttcg aagaacataa tcgacgtaat 31080

ctatatggac cacaaagtag gaggtatcgt aaatctgaac caaaatcgca ttgacaaacc 31140

gttcaacata ctttttggag gaaaagaaag catttatcaa aatatctaac atcatcttat 31200

aatacctatc gtctgtgttc attacatttt taacaagtac atctttaatt tcatctaata 31260

tagatttgtt ttgaggtata gtttttattg cttgatctgt gatagctttc aataattcat 31320

cgtcattaag tattgttatt acagttttcc ataaatttgt aatcatattg ctgttatttg 31380

aagagaaaaa gttgcgtggg tcacttaaat gcaaaactac acttggtata aataaacggt 31440

aagtattact tacattatct tttaatccat tatcttttaa tcccagaaga gatttatagg 31500

tatcgataat tatagaaatt ttgtcaacat ccattataat atctttgtat ttaagtatat 31560

tttctctggt ggcgtcatta aaatctcttg tcggggtacc aaacagcgtt ttaataatct 31620

catctttcag tttaggtata atctcattta aaatttcctc tctttttgat tcgtattgtt 31680

ttactttgtt ttctataact aaagacgcga gaaatgtaga aaaaaggtca aatactgttt 31740

ttttggtctt ttcattatta ggtctcacca gatcttgata tttataatct ataaaaaatt 31800

tcaaattgtt ttctattttt tttctgttta tgttaataaa tttatctctg agcgttttat 31860

atacgacttc gttttgaaga tggaaatctc ccacaagatc tatggctgac gaactttctg 31920

gtggtatgaa ttgaagtttg acgttcttca caaggggaga atcctcttca tagttggctt 31980

ctgcaattct aaacgtttcg gagctaatta tatctgaaat aacttccagt tgggactctc 32040

tgataaagaa ggaaataaaa tcttttattt tatctttcaa ttgattccag agatcgtaac 32100

cgggtacgta ttcctgaaaa tctgtattca accatatatt aagtactttt cccacacttt 32160

ctattccctc ctttatttcc ttactattaa cagataaacc aatgactttg ttaataacat 32220

tttgtgcaat agttttaact ataccctcaa tgactttttc atccaaactc tgagagggtt 32280

gaagaatata gatgttagat acaaggttct ggagtaatag tagggcttcg ggggaaacat 32340

ttttcatgaa tttatctaaa gtggagtaaa gctcttcgag ttctttcttt gctttatcac 32400

tgagaccgat tatttccgct attttaaagt taatctcttt aataatgggc aaaggtagcg 32460

aaagtgtttc gagattttga ttgaactggt ttttatactc tctgatatcg gttgatttgt 32520

aagtaatgac atgggcaatg acgccgctgg tttcaattgt tccggtaaat gtggatactt 32580

ttattttatg gtaaaagtca tttctcgggt gtataaagag aataaaaaca taatcatgtt 32640

tataattatc ccaatagcta tcgttttgag caatacagac ggtggtactt ttgttggtgt 32700

tggtttcggt taacatttct ttgattcctt gataggatat ttcaggtaaa agtcgaacaa 32760

gtacggcatc gctatcttcc atttccggtt tattatgata gacaagttct atgtccccgt 32820

tcttgatata ttttctgacg gcttccatgg tgttgttcca gcgatccagg tagcgaaccg 32880

tataagaggg gaggtatgta tcgatgatct gctcgagatc gataaagctt ttaataaact 32940

tgaacttcat agaatgaagt tcgtcttttc ttccctcctg actcaatttt ttattgataa 33000

caaaaagagc cgccagttta tctacattgc tgagcatgtt atgataataa aaacgattct 33060

ccaccggaat atgactttca tccgatcgat ttgtatacat tgctacaata ccctgtagaa 33120

taaaaacctg agcctgctcc ggaagaggtg tgttgtaggt ggtttttgcc gattgcataa 33180

ttcgatcgac aagttctttt ttgaccttat cttttacaaa actgaaaaac atacttttaa 33240

gctcttgctc tgtagccgtt tccggatcaa tttctatatt gagtgtgggg tcttcgttta 33300

ttttttgtgc cagcttacgt gcaaaattaa tatcgaattg catatttgta gacttttatt 33360

ttaaataact tttcgttttc gggtataaaa aggtctggtt ttgctggtgg attcctccac 33420

ctgaatgttc agcgagaagt tcggatcacg cggaaattcc tgatagtttt ccatatgcat 33480

taaaattttc aggtgatagt ttatttccgc cacaaatacc agttcatcag acgacgggtt 33540

gatcatacga tcggaaattc cttctacgac aatatcccat accgccgcat tgtctttggt 33600

aaggataaga tcgggtctta cgtttgagag aatctgagtg atctcgcttt cttttgtaag 33660

ataataaaaa gcacgatagt tgactttata gggaaccggc accctgtact gaatggtgga 33720

ttggtgttga ttttccgtaa aggtaagaaa agcaggaaaa ttctgtataa cttcgattcc 33780

ttctcgcatg acaacaacga agggatactc cactttgaac atatccgtta ccatcgattt 33840

cctttgcgcc tgagatttgt cgaaaataat gcgcggtttg gtgccaagag ccttttgata 33900

gatttctttt gcaaaaacta cggcaaagta atcggctgta ataatttcgt tcattcttct 33960

tcagggaatg gaagttcttc ttcaccacca cccgtttctt cttcgaattc ttcgaaggct 34020

ccgccaagat taagttcgcc gcccagttct tctccgcctt ccgttccgaa atcgaattcc 34080

gttcttcctc ttggcgattc gatcggggag ccgcgctcgc caaggaagtc ggcgggggtt 34140

gtttcctcac cgaatccgcc cgtgtcgaaa agaccgccgc caccggctgc ttccgccact 34200

tcctcctggg gcttgagatc gtagggaatc tgaagaatgt tactataaat ccagtcttca 34260

cgaacccagc ctttgaggcg ttcggcaata ccgattcgct gctcaatcac ggcaaagcgc 34320

tcaccttcca caatcgaatt cgagcggttc attaccaggc ggaaatcctg atcggcaaac 34380

tctttgttca tgcgcaccat gcgttcgagt tcttccacaa agaacccctg aatgcgtttg 34440

atcgtgttgt tgaatttgat atcctgagta gccagtgtgt ttttagcatt cacgtctcct 34500

tcataaccaa tgaacgcctt tggtaccttg agtgcggaga tgagtcggtt gagcatgtat 34560

tccacatctt cagcaagatc tactttggaa ccctgaagaa tatcgatttc caccgcacga 34620

cgatctccgc gccggggaat gaagtaatct ttgagaatgc tttcgataga aaagtagtta 34680

tcgattccga gaaattgatt ctgattattt cttacccaat agtctcgctt atactgcatg 34740

gcaatattgg tcagatattc gttgatcttg tcgggcggca cgtttccgac atctacgtaa 34800

aacacccgtc tatcgacact acgaaccaca cggtaaagca tgagcgcatc ttccatgagt 34860

cgaagctggt tccatatcgc tcgagcactt tcaaggtagc ttctaccata ggggaagaag 34920

ttggtgtcga ttttgtgaga aaagtgaatg acatcttcct caggaatatc ttcgttaaag 34980

tatccgctta caacgttacg gtaaacgtcg gtaataacat aataccaggt atccgtttcg 35040

gggttatatc gctttgagaa aatgtaagga gagaccacct gaaatttttc gatcgtgcca 35100

tccgaacctt tttcaagaat atgaagaaac atatctccgt atttgatcat gttgcgaatg 35160

ataggatagg cgttcttttc aatatttata acataatcca gataggagag tattgctttt 35220

gcaagctcaa tgtcttttgt taccacatcc acaatattac cgttttcgtt gggaatcgtg 35280

cattcatctg caatgatatc cagcaccgtg gaaataagcg gatcggtata atccatgcga 35340

tcgtacatat cgtagaggaa aaaccggttg aattctattc ctccgtagaa cctgctcgca 35400

taccccgctg tcgcaaacgg gtggtacatg ttaatcggaa tcatggaaga gccacccgca 35460

ccgtgcggcg ctcccatacc atacatcgga gaaaggaaat tggtgaagtt gacagcttcg 35520

ttcagttttt tatatttttc cagagacggc atattctcca cttttttgtt aaataacatt 35580

aacctaataa tgtaccaaat aacgaaatgg tttcgtttat ttaaaagaaa atgacctatc 35640

gggaagccag agcacttttc aacaagatca aaacactccc tgattataga aaccgcgttg 35700

tcattcggat gtctgaaatc agagaaagac ccaccttcaa ccctcgagga caatataata 35760

ccacaccccc cggcacttat gcctatccac ttggcttcgt actggacatc gggggtgggg 35820

gcgaggattt tgtcgatttt attgcgggta ttatgctttt gccctacgct tcacatgccg 35880

aatgggtaca tatcttttac ataaaagaca tgggttgttt tctgaatctt ggggataaag 35940

aggatacaga ggaattcctg agaaagtatg cagagaaaaa tccttttata aatactttaa 36000

tagagcacat tcgcatttat cagccgataa atgataatac gctctttccc attctaaacc 36060

gctatcttgt cggaatgcct tatgaaaaca tatcaagcga agagtttcac cagagtttca 36120

acagggttct ggaaaagctg aaagaaggat acatagacat tttcaaaggt gtttaccagc 36180

atatcacccc agatgacgca cctgctgttg ctttcgtgaa cgaattcaga gattttattt 36240

ccaatctggg ggattatcac actggaaaaa atatactgga agtggcaata gcccgaattg 36300

tgttcgccgt tttcagacgt catgaactta tagaaatgat cgaagcaatg atcggtaatg 36360

caccgggaga aattacctcc tcacgcttta tcaactatct tccggtttct gattccagaa 36420

gtctgagtgc atttacccga tggtttgcca ttacacatcg cctgttttac tatgctttca 36480

ataaaggggt aatcagagag caatatcttg aagaatcggc tacgctgttt gtggatatga 36540

ttttcaccat tgccttttca aaggaaaaaa taagagctgc tatggataca atgttcagaa 36600

tgttaataga tcaaatcaaa gataaaggta tacccaaatc ctatcgggtt tacagcgaac 36660

ttggttattg cggaatatac gatccgggaa ccggcggtgt gcatgaagcc gaacctgctc 36720

aggtggtctg gtgggatccc tccgtggtgg aatactacgg ggcgattccc aacataggga 36780

tgcgagaacg taaaattcag aacctgaagg attatataac cgcccttgac gtggtcagat 36840

tttttgtcaa ggtgtttata tacaataaac atttacttac acaagaaccc cgtttgttta 36900

atcaatcggc tgaggatatt gcttggcatt ttaaaagaat attttataag aaagaattca 36960

tttacctttt tgaaaaaggt ttgcggatga ttagtagatt tatcaaaaca ggaaatgtaa 37020

atcagttgat gtctcttatt catgatgtac tcatgttgca ccttagaaca gatctcctcg 37080

cgagggtatc tgcagtttat agatcatact ctcttgaaga ttattataac gaagaactca 37140

aacatatgaa gagggtggta ggtgatattg ccgataacat ggttgcactt cttacaaatt 37200

acgccgtgga tattctgacc ggtaaagagc aggttaagga tatagacagc gcattttccc 37260

attatctcga tcatctcaga gaaaaacttc aagaattgtt agataagtct gctttagagt 37320

tgcgcggaaa agcaggtaca aaaacactat tgcaaagatc tttagcagta gagtcgggga 37380

tagagtctat tctttcagga attatcttca tgagaaagtt tctggaagct tatgattcgg 37440

atagagagaa gattgaggaa gcgttcaggg tggtaaaaga aagactaagg gattaaatac 37500

tggtaattgg gattgtgtgg aatgggtatt tttgaaaaga aggtgaatct gaaagagggg 37560

tggatccacc ttacaacatt tccgtagaaa gaggcaaaaa ggggagaatg ctatgaagat 37620

caaaaaggta attatagcgc tgctgtttct actcacagcc ttccagcttg gggggattat 37680

ggcattgtat ctttttccgc gataagcgcc tgtagctcaa ccggaaagag caccagcctt 37740

ctaagctggt ggttgtgggt tcgagtccca ccgggcgctc aggtgtaatc agaaacaaaa 37800

aaagggaggg agtcatgaca gtcatatggg caatcttttt tatagtcatg gtgttgatgg 37860

aaattcgaac ctttcgggta aagaggtatc tggaagatca ctccacccga caaggttctt 37920

atgcaaccga atggtattac cgggtggtga atgaaaagga ggaacgtaaa aaaccgggtt 37980

cgcaatggga tttgtaagaa aaaaagagcg ccttattatc aagcgtgatt tcgacgcgct 38040

taaatttgaa gacgcgttcg atcttgagat cgtgtttcac gtcaaccccg aagttgaaat 38100

tattgatcgg ggagaagacg tggttgtcgt atatgccccg cttggcattt tgggaagcgg 38160

ggaaacagtt gaagaggcaa tgaatagttt gcttcttcag gctgtaaagg aatataaaga 38220

gagcacttat gaaggagagc gagagatact tcgttccttt ataaagttgt acacgtcgtt 38280

tctcccgccc gactggaaaa gtcgggtttg agtaataggg cattcgtctg ctctcatgag 38340

taaccgataa ccaaacaaac ggaggtagcc atgaaagagg tcagcgtcac ccatgtcgtc 38400

gtttgcccct tctgtggcaa gacgggcgaa gtcaccatta cggcggatgg gagtggtccc 38460

cgcctcgtgg aaatggagcg catttgcccc cacgtagata ctgaatacga cgaaagaaag 38520

cgggggattt acgtacattt cagtgacggc gaaagggggg actacgtctt cctatacgcc 38580

ccccttgcgc tgtacgtccg ggagggcgat ccccatctga tcgcccgtgc gctccgccgg 38640

cggggcttta aggtacgggt cgacgggcgc cacatcatct tcaagacacc cgtctacccg 38700

tatccggtgg acttggcgct taggcagtat atgcttaacg ccgggcgcac ggtctcatac 38760

aaacacgtgc atctgtgaag attatgtgag ggggttgcgc ggcgcttggc attttcgtat 38820

attagaactg tcaccaacca aacaaaccaa ggaggtagcc acgaaagcga ttgacgttct 38880

caagacattc ccagccccgg acagcttcga gggcgtctat tactgtccgg agcatccaga 38940

ggttgaaatc aaagaaaccg tccgttggac ggaggttcca aaccccaacc ccgacgcccg 39000

caacccggtc gcagtacacc gggttgtgga ccgctggtgc ccggtctgcg ggagaccggc 39060

tgttctggga gctcgatccg catgacgggt gtttcggcga tattcgcaat cttcgcaacg 39120

ccgaagcaaa gcttgcccgc cacattttaa agtaatttcc gtttatattt acttatattt 39180

acataggggt ttagaacaaa ccggaagata ttatgaagtg gtttaaacga cttacgacgc 39240

tggagatttc ccttcttatt cctctcttta tttccttgag cgtttacttc tccactcagg 39300

gagtcgccaa atttgtggcg cttcctgtgt gggtggtggc actggtaata gcggctattg 39360

acgtggcaaa gttcgtaagt gtgggtctcc ttgttaccac aaggggatgg ctgctcaaaa 39420

caattctgat tccggtcatc ctgtgcgccg tctttgccac ttctttcagt ttttatgcgg 39480

cacttgttta ttcacacgcg gagtcggtgt cttcagagaa agttgaaaac atcacagaag 39540

ctaccataac tcgtgaaacc gttcagcgtc agatcgcgcg ttatgagcag cttcttgagg 39600

aggttgaccg ttctattgaa aatatgaaca acacaaccac agagagcatc tggcaagaac 39660

gtctccgcaa gcgagagttg gagtcgctgg tgaatcgaaa ggaggagtac cttgccgcta 39720

ttgactctct tgaagccgtt cttgtaagca gcacggtgga atcgaatcag cgtcaaaatc 39780

tatttttcct caactatatt actcccaact tctatttcgt gcttcttacg atcattttcg 39840

atccgcttgc cgttcttctt tacgcgctgt ttgtgcgcat gctgaagcaa aatgcgcgtg 39900

aggaagatga aaaagaagtg aaagaggaaa aaacgggagt ggaggttgtg aaacctaatg 39960

aacccgaaga gcaggatttc gtttccaagc aagaggaagc ggagcagctg ctgatggata 40020

aagtttttca aaccaaacgc tttgcatttg atccaacccg aatgcaaccc cagaaggtgg 40080

ttatacggga aaaaaggagg aggtgatatg tacattgtaa aaaaagtcag gatattgagt 40140

gagacggcaa cggtaatcgt cgaatattca gattacaggg caaatgtatg ggttgggaag 40200

ggaatctcct gtagagcctt tctcaaaagc aaagaggtta gaacaggggt aatcccttac 40260

ctgaccattt acaaaagata ccccagaaat ggaaagctac tggaagattt cttaaaatcg 40320

atggaacaac aatatgtaca acatacgcgt caacacatat agtgtagggc tgcattcgca 40380

ccaagttccg attctcaaag cagccaacga tccttccatt gttgatcaca acatgtatct 40440

gtacattacc gcccgccacc cctttttgcg gctcaagata gatttcacgt ttaacggcaa 40500

caaaagggtg gcgtcatcgg caattatttc catgcacaac agggggaaag atctgattaa 40560

agaatataag ctgttcgatc ttgatatata caaaccgaca actgcttcgt ataaaccctc 40620

agataagacc aagactgtaa agttgattta taacttttaa atgataatag acgttgggtg 40680

attatgtatt gtcttcgata taaaatagca gatatacgtt gtgccgccct taacgtacat 40740

gcgtcgaaag tggcaccccc ctcctatgta gacatagtga ttaagggggt ttttaagata 40800

aaaaaagggg cgctcagtat cgcggttcat cctgatacac ctgtgggaga cataaggttt 40860

gattgtctca tgaaggttta tggaagcgga gatgtgtttg aaatacactg ttttaaaatc 40920

atttttcatt tgaatgatat taaaaagagg tgttatcgga atcttttaaa gttggttata 40980

agttagtgta aatatgtggg ttctaaaacg gcaagagcag gaaataggga taaagagtca 41040

ggatacgccg attctggctc ctattaatgc tgaggtggaa atacacatag aaaagtatat 41100

aggcggattt ccgaagacaa aaggcttgta tgcagaagtg atctatgcgt caaaatataa 41160

caaaccggtt gtttttgcgc aaaccttaaa tgcgaactac gaaatgtact tatgttctat 41220

tggtatttat aaaaacgtcg gaagacagaa taacattata aacatcttaa aactttatgt 41280

aaacctgtaa caccatgtac gttttaaaaa ttaaaaaata cagctttcat accggatttt 41340

acaaaattcc ggcaaatggt atggtacggg atcctgagaa tgggtatatt gatctttgtc 41400

tcaaaacgga actcccgtta tgtgctttct ttgtaaacta tgaggaagaa gatgaaccgc 41460

gcgtttttgt tataaaagag gctggaaaag atcctcagga aactatcgta gaatttattg 41520

taagtaaaaa ctttcccatt aataggaatt tcaacataat caaactgata tttgcgccat 41580

gatggttgtt gccggtagaa attacaagct ggaatccagc gaaatgctga ttcccaacgt 41640

ggtggttaca tccaaaaacc gaatctataa cgtttcgata tgggttatag acatcggata 41700

tttctatgcg ggaaatgaac gggggtatct tggattaaga tgtggggttg aaaaaacgtt 41760

tactggcttt aaaattaatg tctataaaac cacaaatcgc gggaagtgat atgtatatga 41820

taagattgaa atgccacgat tatcccaata cggtcaacag caaaaaaatg gttaattaca 41880

aaataactct gaaatcagaa cacccatcaa acacacttac cattctgata aactgggttt 41940

caaccaatat cgaaagatat ggcaaccata ttatgtttca gcgtcccggt tattacctga 42000

gcgctacgtt tttgtttaaa aaacatcttt atttcaaagg cggttaccat ctacaaagct 42060

ttcgactgta aaaaatgtaa accgatatgt atctcataag acatagtctc aaaaataggg 42120

ttgcctatcc agaggatcct tactacaaac caccggtttc caccggcggg aaatgggtta 42180

cgcatctggg aaagctttgt aaaatagaat ttcacgcact ggttttgcag aaggaaatgt 42240

gggaagagat aagaagtagg aacaaatcac tattcaacga tcggattcgc aaagtacttt 42300

tgtacgatac tgaagaaaac ctatttgcca tatataagat aatctgatgt ttctgcttaa 42360

gacaacaccg cgcaatcaca atccgcgtca ggtatggttg aaactacctg accagagacg 42420

ggtgtttttt gaggtttcct acagattcgt agaaatttca catgcgactg gaaaccgtgt 42480

taacagaatt ctattacaac tcctgtcgga atatcatttt acatttgtaa aaaaggcgga 42540

ctatgctgct ggtcaaaaac agccacatcg atcccaatga tggtgaaatg cggctaaaat 42600

acagccgcgt tatggatgtt aaaatttatc ttggggcgtt tgggaaatac ccaaaccccc 42660

gaagggtgtc ttatagtctg gcaccctttg atgaactgtt tgagtttgca agctggatgt 42720

cacttttgat gatagaaaag cacataaacc ggaaaaagta atatgtacgt gtttaaagta 42780

agttatttta tgaacggcga gccgataggc atacgtaccc tttcaaggtg ggtgcaggtt 42840

gaaattgcct actggggtaa agaaggtaca cgttataaaa gagttaccgg tgggagattt 42900

gaggaaaatg attactggta cgaaatagag ataaaaaaat agaatgtgtc attatgtatc 42960

ttatgagaat gaataaaagt gtaccaataa cacccatttc cgggaggggg agtacactga 43020

gcgggcatag cgagattaga ataggagccg cgtgttttcg cgccatgcac tggacttata 43080

taataagtgt acacataccg aacaatcagt ttagtgtttg tttaatggaa aaaagagaat 43140

taataaacgt atttttagac aagcatataa aatgtacgta ttaagtacag gtgttgatga 43200

tccactattt atgaccggaa cttctacacc gggtgtgatc actcccaaag agggttttta 43260

tacaacccag aagtttattc gtgtgtggtt ttttgtacgc tactacagtg ttcccccaaa 43320

atcccacaac gttgtacatt ttaccagcgc caaccattat aaacttataa aaaaattcta 43380

ttatgtatac tattaaatta aacaaagggg ttaaaaacaa cgaatgtttt gtggttgtcg 43440

gaaacgaaat tctctccaat gaccccattg taaactataa tatatttagc aaacaggatg 43500

atctgttcgc atttacaatt caatactggc atagcttaag aacactggga ccagaaggca 43560

caccacttga tctggaactg acgtctaatg cgataaatct tggaaggatt tataacgaag 43620

aagatgaacc cttcccggat ttcatttttg aaaaactgat atataaagac tttcaagaaa 43680

gctctaaatt tgggtggtga tgtatataac aatcagaaaa caaatcgaat cggtagtata 43740

cgtagaacct gaattgctat atcatatgtt cgtagaaatg ctgggatacg atgtggtagt 43800

ttatacgcta tatgccgccc aatgtaccaa atatcccgat aataaaacgg gggtggttaa 43860

gatgtttagt aaaaagaagg tgttttatgt gctgaaggtg ataaaagtga gcaggaaacc 43920

ttctttctgg aaacgtcttt tagaatgggt aaaagctatt atcagggggt gatatgtatt 43980

acctcaagtt gccggtagca aagcactcac cctttgattg tatctgggtg ttgtttatga 44040

tacattactt tcctgtaagt gtttctttaa acaccccgaa cgctgtatat tttaacatca 44100

aaaattttaa acttattaag agaatttatc aaaggttata atgtggaaca atcaactttg 44160

gggtgatcac aatgattgta cttaaaacac cgatactcag agttacttcg tggttagata 44220

ttagaaccgt tttgtacgtt gaggggattg gatttgttac cagaatcccc tggatgtggg 44280

atattatctt tgaaattgtt tacgtttata ataaaattga gcgtaatgct tgttattata 44340

ccaattacat caatttcact ttgaatcttg attcagtagg cggtaaagcg tttgctgtgt 44400

tgaaaggggt cgcaccagaa caggtttttt ccattattat ggtggttaga agatagaaag 44460

gtgtcatgtt cgtattgaaa atgcgtgttg tcgaaaagat tagagatcat tatgtacctt 44520

ccgactatag atcttttata cgtcttggta actatacttg gttctatctt ttttatcatg 44580

acacccatga cataccgttg acaccggcgc ataatacctt cccacaaacg tttgccgcca 44640

tgcagacgct cacggtcaaa tgcaagctgg tcctctctaa ggagcagcga gaagcacttg 44700

acaccaccat gcgagcgttt gccgccgcgt gcaacgatgc aatcgccgtc ggtcgaagac 44760

tgaataccgc gtcgaacatt cgcatccacc gcgtctgcta cagcgacctc agagcaaggc 44820

atggtcttac agccaacctt gccgtccgtg ccattgcccg agcagcaggc attctcaaag 44880

tcaagaagcg ccagtgcagt acagtacgcc cgacaagcat cgactacgac gcccgcatct 44940

tctccttccg agaagccaac aagcgccgtg gtctggaaga cgcggcaagg agactactac 45000

atcggtatcc acattaacgt agagacgccc ccacctgaag atgagcacgg gtggattggc 45060

gtcgaccttg gaatcgcgag cattgccacg ctgagcgacg gcacggtgtt cagcggcgac 45120

cagatagagc gggtccgtgc tcggtatgaa agaacccgcc gctccctcca gcgaaaaggc 45180

acgaggggcg caaagcgcgt cctgaaacgg ctctcgggaa gggagcggcg cttccagcag 45240

gcgatcaacc acaccatcag tcgccgtatc gtagaccggg ctatcgccga gggtaagggt 45300

gtccggctcg aagacctcag cggcattcgc aaaagtgtgc gcgttcgaaa atcgcagcgc 45360

agaagaatcc accgctgggc gttctatgat ttgcgcatta aaatcgcgta caagtgcgcc 45420

cttgccgggg tgcccttcga gctgattgat ccccgatata cgtctcagcg ctgtccggtc 45480

tgcgggcata ccgagagggc aaaccgcaag agccagagca agtttgtctg ccgctcgtgc 45540

ggattggaag cgaacgccga tgtggttggc gcaattaaca ttgcactcgg gggcgttgtc 45600

aaccgtcccg aagtagcgcc cgatgatgtc gaagcggtgt tgcatggtca gcgccgaact 45660

gagacggagg gcagctacaa gcccacgact gaagtcgtgg gtagttgatg aatatccata 45720

gccatttatt taatcaaaaa tgcttctcga aagccgaaaa ggagaattcc tacaacagga 45780

aattcttcgg ttgtataaaa cctatgggga tcgtcttctg gtaagatttt ccagcgccga 45840

acgcgaaacc ttcaatcccg acgccgacta tttcacaacg cctatcggta cttacgccta 45900

tcctgtcggt gctatcttcc acatttcgga agacgatgtg gtgatcgatc ccgacatgta 45960

cggggtttcc gaaagaaaat atatttattt ttttgtggca agtaaagatg cttcttggct 46020

taacatatcc tctcaacatc cggcgtttga aattcccctt gttttgtaca accagttcag 46080

aaattatgcc gatctctatg acgtttcact ggatgatgtt ttccggaatc gaaacagtat 46140

ggaaagctat cttacctact ggtgctttgc cattgcatcc cgtgttttct ccgatcttac 46200

agagacactc aagcagaact tgatggaatt gcttcgaaaa gatcttcccc gtatgcgggg 46260

atattatcag gagctttcaa atatttgcag ggaatttgac gtcgatgttt caagattcta 46320

tcatgcacgt aacaatcccg aagaatggct caatttgctg attgcagaac ttcttgaccg 46380

gctcaacagc ggcttcagac acatgaaatc agccggggat gtaaagcata agtatttcat 46440

gtatcctctg atcgttttta taacattgct tcacaacagg tatgcacctt atccgaattc 46500

cattgaagcg gcttataata taggagccaa aaaagaccct gttgttctga cgggtttcct 46560

tcgaaaggtg ggatatgatg gaatctggga tcatggcacc ggagccattc actccaatga 46620

acccgctcag gtggtctggt ggaaacccac tgctgcaagg ctggtgaaca aaatggataa 46680

ccctctttat gtttcgcctt cctccatagg attcggttat cttgcgtttg ccgatgaagg 46740

ggttgcaccc tccaatgaaa aacagaaaaa atatttatgg aatctgattt taagtggtaa 46800

aatggatgag tttattgaaa tcatggatat gatcatgtac cgtaagtatc ttgcagcgct 46860

tttcaacgcg tttttgaatg aaagacgggt ggctctcaaa cacgctatcg gattcaaggc 46920

attcaaggaa tatctcaagc aaaatgcaga ggaaatcaga aactttttca gagtgagcag 46980

caatgcgccg gtgcagcttg tatgggaccg gttcagaaaa gcattcagaa tttctgaatt 47040

acttcgaaac tacgaagaat tgattgaccg gcacccttat gaggtggatg attttgccca 47100

caagcttctt ggtaatttta actttttgaa agaactgatt aagcccacca gactataaaa 47160

cgcaaaataa ttaaaaaaat gaaagttaat taaaataaaa ggaggtcaaa atgaagaggt 47220

tgacaaaaga acagtttatt aacaattttc acgagcccaa ctcgctgcat ttgttcccat 47280

ctatagagga tttcattaac cctcgacaag gagatattac tcaatcctac tgttatgtat 47340

tacctgttca ggatttaaaa atcgacaaca aaatgggcat accggtaaat tttgatttat 47400

cacaggcttt aaataagatg ataggttcta aaggtgagtt gaacaaaaat ttgatcaaac 47460

aaaaaaactc ggcacttaag gaattaaaaa atatattaca gaagtttcac aaaattttac 47520

aatcattaaa atctaatttt aatgaaggga tagcactggt ttttcattcc ttttttttta 47580

tgaaaaagtg cactcctttg atcatgctcg cgcatcgtat gattatgtaa aaagcaaccc 47640

caaaagtgtt ttagagccac tcaatgaagc attaaaatac gatgaagaaa tcgtcgagga 47700

agctattaga gaaacagtat cagattatct ggaaagtgga gactggtatg atatgattga 47760

aaatgcagtc gaaaagtatt tgaggggtta attaaaagaa aaccatgctt gatcagcttc 47820

tttctctttc cgggctttac tttgatcaac agctttttgc gggttcaccg ggagagttgt 47880

ttttgcggtt ggtggcggaa gcactcgatg aagcggagtt caatgtaagg agtctgcaga 47940

accgaagcta tccgctgact gtagagaata ctgatgatct gctgagactg gcacacctga 48000

acggtgtaag tattaccccc tacgttcagg gaattgtcaa agcagaactt cttgttactt 48060

tccccatttc ggttaccaca tctgttcctg acttgacaac acatgcaccg gaaattctct 48120

acatggatat tcttgccgat acggattatt tctatctgga ttataccgat ttccgccaga 48180

ccgatacccg tatcattacc accagcacca atcttatcta ctcaagagac gtagtctttc 48240

gtcatggtag ggttgagcgg agaagctatc cggtaagtca gacgatcccc ttcatgatgt 48300

tagaacttga ggaagatgtg gtggatgtta agaacgtttt cgtggaatac cctgatggaa 48360

ggctggtcaa gttttaccgc tcacgtaatc ttcatgaaaa tctggtggtt gaaaatgcgg 48420

taatttacaa cacccgccac atttacgacg tggtgttttc ctcggggaga gtgcatttgc 48480

ttttcggtag aaagatttct ctggaagacc cgatttcaca taccggctat acttttcccg 48540

ccggaagcac catatatgtc gacacggttg caatcgatcc gactaccctg aacagcttca 48600

ttccggaact tgaagcagat atcaaaaccg ttaagatcaa caaccgtatt ggggcaaccc 48660

ctcagattca ggtgctcacc gaaggtggat acacttcccg tcttaaagac atcgaatatc 48720

tcaaacggga actgcttgtc gctcttcaga aagacgaact ggaaagagaa atcgcaaaat 48780

atttcgataa atacagattc gttcgagaag atgatattgt ctatgtggaa ggagccatat 48840

accgcaacgg tagattcacc ttccacgaag ccgatcgatt ctatatgcag aaagtggttt 48900

ccacctacaa ccgcaacatg atcgtcagga aaattccgat cacccccctc aagatcatca 48960

ttcgcgcttc caacattctg aaccccggag aactgatcac tttcgtaaaa gattatatca 49020

gaaaacttcc gatcggtgga acgtggatca caaatgaact tgtggggtta ataaaagaaa 49080

aattcaatgt cgtatgtgtg ctggaaattt attttggaga aacttatgcc cgaaaggttt 49140

cggaagatat tatcatctac gacggcgtac tcgacgttga aagtgtagaa gtcaaacccg 49200

tactggtttg atggggcgct atgcaaaaac caagggaagg aaatttcaga actttgtaaa 49260

atcgctgctt gaatccacct tcaaaaattg gagcttcaag acagcaatca tgggcgaatc 49320

aggttcagat gtcaagatat ttccggagca gattttttcg gttgaagtaa aacaccacaa 49380

aaacggattg atcagaaagg atgatatgcc ttctgaaacc gtactcaagc aagcacgcga 49440

gcttatccgt aaggaaaaca gtcatttctg tttgatcgtt ttgaaggaga attacaaaac 49500

cccacaatat tttgtgcttt atcgaaacgg aaagctgaga aagctggaag atatatcgga 49560

gcttaaggaa attgtaaaaa gatataaatg atagttactt tgagagaaag accgtattgg 49620

agatatattt acctgttgaa aattccatag cggcgcttaa gcaaaaactg gcaaggttag 49680

ccgctgcaaa cgaaaccgca ggtggaacgc ctggaccccc cattttgctg aactcctgag 49740

caaacttgcg catcatcttc gtcatgaaag aattgaaaga ttttccaaga agcgcatttt 49800

cggtagcgct actggtattg cctatataaa ccctgtctcc atgtagatac atccgttcgg 49860

tggaaatcct cacctttctc tccgcaccca ttagcaattc ttcctgcatg gcaaggtgca 49920

atttttttgc agccacaagg attcgctcac gttgcagcag gtgcagtgaa tccgatctta 49980

ttttaacaac gtaaccgcca ctttcttcat ccaccgactc attcttgaaa gatattttat 50040

atgatttcag atttacctga tcgccgtcta ttttaccata gattccatac ggggatttat 50100

cttcgtcgac agaagtggtt aaatcgtcag agacttcatc actgtacttt ccaagaaaca 50160

gatttccctc ttcgtcaaac catagcgcct gcattccctt tccgttgaga aaatattcac 50220

ccggaaacga tcttatccgt gcccgtttca attgattaat cgtaacacca ctttcattgt 50280

cgttggtggt ttgaaggtag tttgacatgt tgacggggaa ggggaaatac cagagccttc 50340

cattgatttc cacataagca aggagatcac ccacctcagg ataaaatcct atgtgcacga 50400

aaaatggata ggctacacca atcacttctt cagaaatgtc tttgattctg accgccatgt 50460

atctttcggg agtatcgaca tcatctactt ccagtaccaa tccgaatttt accggagatg 50520

aaaagaaaga tattttgctg cttttgttag aaaagaattc ctgagtgttg aaccccattt 50580

tttattttat ttttgttagt taaacatata aactatatag ttttctttta aataaaacac 50640

caaatgattt ttaacacttc atactattga agatttttca gaatacgatc cacgacctgt 50700

ttccattttc ggttatcctt atattcacca acaatctctc ctgctatctc gaataccgct 50760

tctccaaaat accacaaatg tttttccagt tctacgtgca catgatattc gttcctttca 50820

atatagtctt caattaatcg tttgataaaa tgatgtaaaa cgtattcacc ttcgaatctt 50880

tctttaacat aaaacaccac aatttctgct cccagagata ccgcatctgt acctctttga 50940

ctgataggtt catcataacg cattccaacc acaatactca taagaacttc tgagggtaat 51000

ggatgacctt catgagagtg gaaaagatag tggttagtta ttttagtcag cagctttttt 51060

accgtctctc tatccagaaa gtgtgtgtag ttattgattc tatcttcaat atagtcaacg 51120

aattccaatt gcagtttggt gaatataaat tcttcttggg cgtatagttt atcatataca 51180

aaatctacaa gatcatcatt ttgttcattg tactgatcaa taatggaagt aacaattttt 51240

tctatcttat tctctataaa tttatctacg ttcaatgcgt gttttaaacc ttcctttata 51300

atctctaaaa tttcggggtc tgataaataa tcttcccaca aatcatcttt aagcatatct 51360

ttataaacaa tgaaggcaat cgcatctttt accggttcgg gaatgtgtgg aataaggtct 51420

tcaggttcat ttatgcgtat tgctctttcg atcaacaaac gaatataaaa atctatagat 51480

tcgggggttt gaatattaaa gtcaagtatc ctatcaaggt ctgttctgtc atcaatgcca 51540

tattttagca acagtctctg cttataagat ggaatagacg gcacctgttc cacaataaat 51600

tcataaagag gagaaccctc tttaagattg attacaaaaa ggtctctcaa ataattagca 51660

gccgtcatct ttactcgagc attgacaaac gccattttta taacgtgggg ttcattatag 51720

ttttgaacaa cattaaaaag tgaatggaaa tgttcagttg attcggctac tattagtttc 51780

ccatttctgg ttcccactat cataaaagaa taaaacaggg atgtgaaata ttccttgccg 51840

gttatgctgt atggaaaatt agactttcgt agtccacaaa aaacaagggc tacgcccctg 51900

tcaacaattg atttcaactt gtttaatatt tgcgaacctt tggtttttat ctcattttgt 51960

ttatgaataa tgaagtttct aagttgcaaa aattgatctt gggtgaccct tgatgaatgc 52020

ttatagatat aattgaatgt ttctaataag tggtgattca agggaatgcc ttcttgggga 52080

tgaaaactaa gtttttctac gggtaaaaca taacacctta aaaacagcga atccccacta 52140

tcgtttggta aaacatacat gaaccagtta attgaagaaa aaaagcttaa cgcctctttg 52200

ctgtggaagt tatccgcaaa ttgttctctt gtcagtatca gcatataacc taagcaaagt 52260

ttattataca aggtaaattt ggattaaata ataaccagac ttctcagatg taattattcg 52320

tcttttccaa ccacatcaga ataaaacgtt tctatttcgt taagatcttt gttgatcaga 52380

gtttcaattt gtttttttca gccccatgac acaccctcca ttttttggca tactaaacaa 52440

ggcaaaaccc agacagttcc atagccgccg acttatttaa agaaaaataa atgaaaaatg 52500

cttcaagtac tgaaagacac ctatttaaac agcgcttccc cgcataacaa ctatggagcc 52560

gacgaaattc tccggctcaa tgccacttcc agcattgcat tgcagtttga aaacccgatt 52620

ggaacgggtt atgagattcg cctgtttgtt gccgacgcgt ggattcccca tgtagaatat 52680

ctgggtgggg gaagctatca ccggctgctc ctcaccgttt cgctctacag cttttctatg 52740

gatgaaggat atggaaccga agtagaaccg cttataagcc agagtttcaa ctatgcgtcg 52800

ctgtcaacgc ttcctttacc actggaagtt cgcacggtaa gcgcatttat tcatctggca 52860

ccgctcaagc ggcgtatggt aagcattcca cttacaaact ttttcaacgc cggaaacttt 52920

gttcttatcg aatcggctga ggaaatggcg gtcaactttt tcagcagaca gacgcgcacg 52980

gctttcattc cctatactat tccgacagta tccttgcagc ccccggcgct ttcagacttc 53040

gtatacgata cccgcataga cgactacgga gtatatctgc aggcttggga gcggaagatt 53100

cccattgcgg taaggggtta tctcatgcag acgctgtcat acatagacct ctcaaccgta 53160

tggtttgaag tatacgtgtt cgacatgatc accggtgagg aacactatta tacatcgctg 53220

cttcccactc ccgttgggaa taactggtac tatattgaca tgagccgtgt caatatgaaa 53280

agaacccagt atgtgagact caaaccggtt ggaagcacca acgacatttt cctttccttc 53340

cacaaccgct atctgagact atgaacaccc aacagattat aaaacaggag cttgaaaaat 53400

gtaaaaacga tccgatttat ttcattcgta aatatgtgaa aatccagcac ccgatcaagc 53460

gcgtcatacc gttcgatcta tacccgattc aggagaaact cattaacttt tatcatacac 53520

accgatatgt aatcacggaa aaaccccgcc agatgggtgt aacgtggtgt gcagtggcgt 53580

atgcacttca tcagatgatc ttcaactcca actacaaggt actgattgca gccaacaagg 53640

aagccacggc aaaaaacgtg ctggaacgta tcaagtttgc ttatgagcag cttcccagat 53700

ttcttcagat taaaaaacgt acatggaata aaacctatat cgaattttcc aactattctt 53760

ccgcaagagc cgtctcttcc aaaagtgatt ctggacgttc ggaaagtatt acgcttctga 53820

ttgtggaaga agccgcgttc atttccaaca tggaggaact ctgggcttcg gtgcagcaga 53880

cgcttgccac cggtggtaaa tgtatcgtca actccaccta caacggggtt ggaaactggt 53940

acgaacgcac aatccgagcc gccaaggaag gaaaaagcga attcaagtat tttggtatca 54000

aatggagtga tcatcctgag cgagatgaaa aatggtttga ggagcaaaaa agattgcttc 54060

ccccacgtgt gtttgctcag gagattctct gcattcctca gggttcggga gaaaacgtca 54120

ttccgttcca tttgatcaga gaagaagaat ttatcgatcc gtttgtggta aaatacggtg 54180

gagattactg ggagtggtac cgcaaacccg gttattactt tatcagcgta gaccctgctt 54240

cgggtagagg ggaagatcga tccgccgtag gtgtgcaggt gctgtgggta gaccctcaga 54300

cgctcaccat tgaacaggtg gcggaattcg cctccgataa aacctcgctt cccgtcatgc 54360

gtcaggtgat caagcagatt tatgacgaat tcaaaccaca actcattttc atcgagacaa 54420

acggtatcgg catggggctc tatcagttca tggaagctta cacgcccagt attgtaggat 54480

actataccac acagcggaaa aaggtgcacg gatcggacct tctggcaaaa ctctacgaag 54540

acggtagatt gattctgaga tcgaaaagac tcttggagca gcttcagcgc acaacatggg 54600

ttaaaaacaa agtggaaaca gcaggaagaa atgaccttta catggcgctt atcaacggtc 54660

tcatggctat cgctactcac gaaatcatgg aagccaaccc tgaatgggaa aagattaacg 54720

taaccttcaa cagttatctt gggaataagg taacccccag cacgctcgac atcaaccaag 54780

agtttggagg agaatttacc tatatcgcca caccgaaggt aaatcctgat ctgaacaaaa 54840

atctattaat tcaaaaaaaa tccgaagatt tcatctggta tatctgaaaa cggctttcca 54900

cacaatccca attaccagta tttaatatcc ctctctgata tactcccccg ttatttaaaa 54960

gaaaatgcca ctgagtagag acatcataaa tcgaatcaaa gagaaacagg atactctcag 55020

agagaatatt acctacagcg caaagcttct caagaagatt acagaaacca accttcagaa 55080

attcttttca gagacgctta catgggggat aagggaagcc aaaaaccttg tactggcaca 55140

acttcctcct gaatacagaa ctcaaaatct aaacaacccc acacttactc ttcactggtt 55200

taccttcaat ttcaatccct ttgtttacaa acgcgaagtt aaaagcaaac tttatgattc 55260

tccgactccc aaggtttatc ctcttaaaag ccatgattat gggtatagaa cggagctttt 55320

gagtgggtct ccggttcctg ctcccaacct tcgctatatt gtcagataca atcctgaaac 55380

cgatcgtctt gaagctcgca cggtggatat taccaccgaa gaaggaatca gatatgtgtg 55440

gggtgcgtcg ggtaatattc ctcaggatac gctcgagttt acatcgctac gtggtcttgg 55500

taaagacgat atgatcgatc tggctcagag cggcgttccc tatgagaact cgctggtgca 55560

gcttttccga aacagagctt ccattgggtt tcagtatgat gaagaccttc gcaaacccat 55620

tcaggtggat cgtatcaata tggaaggatt tactcagaac gaatcggaga ttatcaatga 55680

ttatgttacg ttctatttca agagcgtagt gagcggctgg atatgtcagt tcagagcttt 55740

tatcaacagt tttggtgaat ccaccaacgc ttcatacaac actcaggatt atatcttcaa 55800

catcatcaaa atgtattcgt atatcaatgt agagaccacc tataacattt cgttcaccct 55860

gtttcctatg agtaagcagg agctttcaaa aatatggggt aagctctcat ttctcaaagc 55920

acacctgttt ccggcaaagc gggtaacacc cggcggcaac tttgtacctc cggtacttga 55980

agtaacgctt ggcaacgtct ggagaaaaag gaaggtgctt cttacttctc tcaatatctc 56040

attcggggaa gataccgtat gggaactgga tccaggtatg caacttcccc agtggatcaa 56100

agtggatctg aatttgattt tgctgtacga acagaatatt accacggaag actggcttca 56160

aaaccgcgtt aaaatgttcg attatacgac aaacaagccg ccttctacgc ttgccgcctc 56220

cgactccatg atcgatcccg caacaggcgt ggcacttgac atttcgacgt tcaaataccc 56280

ggaacccgaa agttttaacc tgaaacttgc aaaactcgat atacttaaaa accttggata 56340

aattatgaaa gtatattctt tttcgggaac gcgacgcgct cagaacatag ccgtacagga 56400

atatggagat tactcctact ggcaagatat gctgcttgca aacggtattt actccggatc 56460

gatcattccc ccgtatgttc cgtcgctttc catttacacc ccggaggaac tcgagaaccg 56520

tctggtagat aaataccata ttcccgatct gaaatatttt taacctatgc tgataagaag 56580

cctgcaccct tccgttgtaa agtatatcag acaatttgct tcgacatcga cggttcagaa 56640

gatttccgca aggcttgtgt tcatggtgcg cgtgagagac gccgcacctt tcagagcgta 56700

caacattgtc ttaaacaaca taaatttcta taccattgaa aacgaaatca ctcctgatct 56760

ccagtcgtac tacgattatc ttccggctcc agctattctt tcggtggacg tcgatccggc 56820

tcctgacggg atatacggta tgatggcgcg tgccaccgtc aatgtgcgtt gcttttctct 56880

caaacaactt cgggaactgg agtggagcct gtttccggga attacggcgc tcattgaagt 56940

agtgcgcaca aacaatgaaa ttcccgtgga ttttatttct gatcgctatg tgcgaaatcc 57000

ttcgcttctg aaagacattc tttttagccc gcaatcggta atcaaactcc atgagagaga 57060

tgaaggcaat aggatatttt tccccggaat acttaaaaga acaaatgttt cgtataacaa 57120

caataccttt gacattacct ttgagtttag taattttagt atagcttccg tatttttttc 57180

tcgaaactac gatattaagg atgtagagac ggctcgaaaa acgctggctg gtttctacaa 57240

tgagcgctgg agtacgcttt ccagccagaa gaaagtcaga tcgggtcagg atctgaacct 57300

tgacagaacc tatcagatgt tcggtggggg gaataaagca tttcccgccg aaaagggtat 57360

tgaagtgggc gtgggtactc atttcgatac aggcgacaaa actttcgccc cttcgcttcc 57420

ttccaacacc ttcgagtcgc tggaatatat tcgttttgaa gatttcctga aggaaattct 57480

gattccctat attcgggaca cctacccgga agatgttcct ccggaaatgg caattctacc 57540

gatcgacata gacaactcct atatgttcat tcataaacac ttgagaacca acaacgtaga 57600

tatcattttc ccaaccgaat acatggtgtt cgattctacg aatatgacgc cggattacat 57660

tatgggattt tcagattatg aggatcatgc agagtggttc gagaagaatt tcgggaaacc 57720

ttacacccgt cacccgattg gatcagttgg taaagtgggg aaagtgatgt tggctcgaaa 57780

gtatctttcc gaactgatcg gagaattcga acgcggcgac gacaagccgt tcagtttcat 57840

tattgataga atcattcagg atataataaa atccacctat ggcttttctc agcttttcct 57900

gatgaaggtg ggagagcaat acgtcattta tgataataga cttctggatg tagagacgcc 57960

tgttcagcag gtggaaaaca aatcccgtct tgaaccggaa gaaatcaaga tatgggaact 58020

tcacgacatc agctatacgc tggatattcc tgaatatctt gcgatggcgg taatgatgaa 58080

gcgtctttca gactcgctga atacctacgt caacgatcca gtggatttcc ttattcccgg 58140

ttccgttgag gatgtggtgc tgaagacgct taccggagag cgtgtgaaag gaaccgcgct 58200

ggaagatacc acggaaagtt cggatgtggt tgttaccaag gtgaacctga gcgctgaagt 58260

aatccgtgca ctcatgaaca atcccaattt cagagcgctc atgaatgtaa tcaaagaaaa 58320

tgaatcgggg ggcaactacg aagccattga aatagaacat attatagcaa aacacggaag 58380

ttatgataac gcttttgcgc tggcgcggct ggcgaacacc cgctttgcgc ggggtaaagt 58440

gtggtatcgg gtaagaggcg atcagaaaga ggaaattacc ggagagcttg taagaaaggt 58500

cgaacaggct tccagcttca gcgatctggt tacgcacccg ttcgtcgatg tgccgaaatc 58560

tcaggtgtcg cttccggttt ctcccggaag atataccacc gcctgtggcg cttaccagtt 58620

tacggaaaca acatggcggt ggatcgagag agagtacgcc gatctgtggc gggagcttag 58680

taagaaagcg gatgtggcgg tggattccgc cggaaatgaa atggtggtta ccggtcttcc 58740

acccgctacg gtatatgaat atcaggcggt tgtcgacact accgttcagt ctcgaattgt 58800

ggttcctccc acccccgtca atcaggatta catggtggca atttatctca cgatcattct 58860

caacaacgca aaccttaccg aagaagagtg gaatctgttt ttgaacgaag gattcgggtt 58920

taagcgtgag gaaatagtta aagaaaaact taccacccat tttgcttccc tcagaaaagt 58980

caatctcaat gcttcaatca gaagagacgc gtttgagcgc aaaggaaatg tcagtacatt 59040

tttgagtata aaacataagg atctgagcga aacaaaaagt gttaaatcta ttacatttga 59100

tgtaacgaag gttgacgata gatatgtagc ctacattccc atgcacctgt caacctatta 59160

caaagtgctt ctttatatgg gcacgctccc ggaaagacag cgggggaagg gtgctcagta 59220

tctgaccggt attacactca acataacggt tccgggtaat tcgctctgga ggatttttga 59280

cacgttcaaa atagaaggta ttcccgaaat ctattatgaa aacggctatt tcattgtaac 59340

gaaaatctcc cacaacatat caggcggaac atggaccacc ggggttacgg caaaatactt 59400

ttacacgggc aaaacgtaaa aaaaaactat gagcaagtac tttctaaaac caacttctta 59460

cgcttccgac gtttatcttg caccacacgt tcccgaactg gaatacgttc caaaggaact 59520

gataaaaggg tttgacatgc tcctcaactg gatcagtgca ctggaaacaa atcatctgtt 59580

ttacagcgca atcaactatc tggctaaaga ttaccatgta aagaaacacc gcgaatatgt 59640

gatccatttc atttatccta aattcaatct ttcggaaaag gattatccag aaaaagatga 59700

agattccctt attatgcttc ccgatcaccc ttttgctcgg caccgcaaag aggaaatctt 59760

aaaaccattt aagggtagat atcttgcgtt taccgcttcc ggaagatatc agtttattcg 59820

atccacatgg aaacatcttg taatgaatta tcacactcag aaaattaccg ccttttcttc 59880

gctaaatcag gattatcttg cgctgtgtct tgtaagggaa gccttaatgc gcgttaaggc 59940

aacggggaat aaacggtata tgaacctctg ggagtatttt atagactacg gatatattca 60000

tttcgatgaa ttcatgcacc ataaacaggt agtatatgcc ctttcaatgg tatgggaagc 60060

tttccagaaa tttcctgagg ggcttcagag tgatgaattt attaaagaat atgaaaagct 60120

ctatcgctga cgagtttctg ttacataccc cgtcgatttg atctgcataa tcgcttctct 60180

tctggtagag tcgtacagga tagaagtctc atgatccatg taacccaact ctccggcttt 60240

ttcatgaagg ataccgctca gcgtctgcgc caggttcgag ttgggaagaa tacccggcgt 60300

gatttcgata agatattttc ctccctgttt cgatccgttg agtttgccgc ccccaagacc 60360

aaattcccgc aaaacagatt tcaacctttc gacgttaatt tctttgcttt gagccgtaac 60420

gtatatcgag atcgtattcc gctctttttc ctgctggtat ttgtggttga acaccacttc 60480

gatcttttca ggggtttcaa aagcagtttg cagtctggag acaaaacgct caagtaccgg 60540

aatgcggagc gcggctttta caagttgacg cgttcccttc ttctggataa ttttgtgaga 60600

gcgctgaatg atgaatgaaa gatgctgaag cacttccaca gtgaattcgg caatgctttc 60660

gtctacttcg gcaagctgat cgtcgggtaa attgtcggct tcttccagcg attgataaag 60720

tgcgttaatg tattgcctta cttcatcagg gatatagaaa tgcatgaccg gctcaactct 60780

gaaaggtagc gtgccgtaaa aaagtacggc atgaccgttt tctctgttaa tttcgatcat 60840

ggtggtaccg atattctgta aataattacc ttcaatcggc acccttcttt tggacgcccg 60900

ctccagagga atctccatct cctcctgttc gatttcttcc tcttcttcct cctcttcttc 60960

ctgagctaaa acaagcatgt catcttcttc ttcctcgaca taagcaggct caccggtggt 61020

cttgaagaat tggagcgtaa tgattgccac ctcttgcggc tgaggaagtc tgatcacacc 61080

accttctccc caccccggcg gcggctcaaa acccatgcga atcagcgctt gcatttcctc 61140

cggggttgga gccggaagtt ccataccccc ttcggtaatc tgacagataa ttgaaagctc 61200

cgggggattg atgcgcctta cgtaaacgat gcgatcgtaa gggctgtacg caccgacgta 61260

ttcgtgctcc tgcaaagtgg aaaaatagga aagaaatgtc tgtattccct ttagcggatt 61320

cattttcttt taaatatatg cttcttcagg aacaagcgaa atggtgggag gagacgtgat 61380

tcgggaaaaa tctttaaatt cataatcatt cccacgatac agtagatatg gagagattcc 61440

ccctacaggc aaaggtggtg tgggttttct tgggggagta ccaccgccgc cgggttcatc 61500

ttcatcgtca tccatatctt tgtttctttt tccaccaaac agattttggc ggtattttgc 61560

ctcgaaaata atttcaataa tgtagtaaag aacaacgcac atgacgatac aggcgagcag 61620

aaaaacgctg acgacaaata tgtactggat caggtactcc atgttacaaa ccgttcaaaa 61680

caacttttac atacgggttt ataatggctt acctccggca caattaaata agggtcttcc 61740

agagggttca ggtaacccat tcccctcaaa tccacacttc cattcacaaa tcgtatgttg 61800

tattgcgttg gattaccgca ctcacaacga ctggaaatgt ttattttaat gggattgtat 61860

ttttcttcga tctgtttcca taccggaaat tctcttccaa gatagtcggt tctgagaccg 61920

ctgagcacca cttctatttt ccacgaaaaa ataaattcga tctcttcagg tgttgcaaac 61980

tggaattcat caacggctat gagcgaacac ctaccggttt taagctggag atattcggct 62040

tcataaaatg tggggttttg aatgaagtcg gtaagattgt aaacgcaaga atgggtaaat 62100

ccgcttcgag atttcaaggt aggggaatag ccgtaaatgc ttccgggttt aaagacaaga 62160

taatcgtcaa agttttctaa aagttttata agaaaatgag ttttacccga tgccatcgcc 62220

ccgttgatga cggtaacgga gcgggttgag cgttccttca gaaattttat aacagcctta 62280

tccagttcga tattgtgcag ggtggtatct ccggaaagcg tctcagggaa atcgtacttc 62340

atagttgatt tatttttaag ccgaagtctc tgaccacaag gggtttgtca tcggttctac 62400

cccagttgtc gatcagggta aaatcctcac ccagcagatt gaattgccga atcagcctta 62460

cggtttcccg gattacagga tttttaagaa cggtgaagta aaaagtgtgc ctatcttcta 62520

cgcttacgtt gtcaagcgtg agtctattaa tggcatttcc aaatatatcg gcaaaacgcc 62580

tatcataagc agaaaccacc tcgaaaccct cgaacgttgc gtcttcccgt aagtagcgtt 62640

tccggataaa cccttcaatc agaacactat aaacatcaaa gtcaatatca gcgacacttt 62700

caaaataggc ttcattgaca ggtgcgacaa attcggtgat tagaacccca ccttctttga 62760

aaacctgagc gtagtcgacg gcgatttcac ttcctgacct acgcaccacc tcatattcgg 62820

taatgttctg tttgattcca ttgtcattat gagcaatttt caaaaccagt tcggtgtcgg 62880

gtattctgaa tacttctctc cctcttcccc ttttgacggg ttcaaggtat ttcttttgag 62940

ccagaaggta agccgcgcga agcgggtttt cacttcgctg aaagtaagtc agaatatccc 63000

ggagcgtgtc tgtttctttt aaggttatca taggctaatc cagtgttata tcatacatga 63060

tttgtgcggc aaccacttct ttaaaatatt caacgaaatc tctgtcgtct ctaacgtcct 63120

ttaaatactt ttctatttcc ggttttacat attcaaaaaa ctcatccata ataacttgtt 63180

tgataaataa tgtaaaatga tccccctctt catccatatt gagtttgtta atgataacac 63240

cataagcaat tcgtataaag gtttgtacat ctattacgtg gcgaaggtct ttctgaataa 63300

ggatattttc tatcttatgc tttattggaa aatatccgga aagaaaccga atcgcttcct 63360

caagattttt gctgacaaaa gctataatat cgctctgcag ttttcgcaaa atataatgat 63420

aatgtgcatc ttcgatttta taataagccg catctctgag ataatcgtat atctgatccg 63480

cgatattaag atgatctatt gcttccttta tggcttttgc tttgaaattt ctgtcaaaga 63540

aaattgggtg ttgccttctt tcctcttctt caaatttacg tacaacatat tgtgcgatcg 63600

gatttaaatg atcttgcccg taatgataag ccgcgaatct tatgacattt gaccagaaat 63660

attcgatttg gggaggaaaa agcacattta ttagactggt tccaccgtat tcttcataaa 63720

gaaaagagcg aacacaccag cggataatgt cttcgttatt tttataatcc gacagaatca 63780

aataaacctg attggtggga tcgaagccgc caagtacatc tcgagtcaat tttgagattg 63840

tctctttcag ttcaaaagaa ggggtggttt cttttagcag gaatatcatt ccgtccccgc 63900

ggggtatttt accttcgtgg atgtaaaaat agtagtacat ttcacgggtt acaatgatat 63960

tccagagagg agtagccacc cattgataaa cttcgtcatc ataccgcgcc cctataagta 64020

tagaacccat aaacagaaaa tctatatctc gatacttttc attgagcgtg cttacctcaa 64080

taatcacaaa aaaatggtct gtcatggact tcaattttct ttccaataac accaatgttt 64140

ttcctgtttt tatcaacgct ttccgtgttt cttcaagtag ttcacccgcc cattggtgct 64200

gtcttaattt ttcttcaatg aaatttttgt aaatctgttg gtacataaca tttgacaggc 64260

ttgttctggt aagatcctct gaagtcaata tgaaatagtt ggtgttgtaa taatatgggg 64320

tgtttggggg caaattggtt ttaataaact gttgacttaa cccgttgaac aacggtttat 64380

taagaacaaa ggtatcggtg tttatcgttt ccattggttt ttatttaaat aaaaagaacg 64440

tatgagagaa ccttttctgt ttcgagatcc gacaatcgaa agctttggaa gctttttatt 64500

ggaatacctt gacattcagg aagttcgtgt taaaaccgaa tttttcggcg gtaaactgca 64560

aaaactcaaa gatggttatc attttccgga tgtaaaactt aaacccggta aagatgtcga 64620

aaagttccga actctgtgca acgcattcgg gtttgatgtg gaaatatccg aaaacgggat 64680

aacgttcaca aaaagacagg aatattgttt tatcgaggag gctctgaaaa aggcgacaga 64740

gaaatatcag attttcgttc ttgcaccaat agaagttgat cttgttttta catgttgcaa 64800

ccagatattt gtcgaatatg aaatatgagc actgttaaaa tacctttagc cgttaacata 64860

tacgacccca agggcgacga atgggaattt atctacagca actatgcggt agaagttgta 64920

ggaagtgaat atctggttcc ggttgtaaca ctgaaaaccg gatcggttaa ctatttcaga 64980

ttcaatgtgc ttctaaccta ctctcagacc gggtctttcc ccctttatct gaattttctg 65040

aacaaaaaca ccaatcagat caatgtagtt taccgaaata tcagttacag ttatatcagt 65100

tccagcaatg tgaactggta tcccacaagt atatccggtc ttcttggttg gtggcaagca 65160

tatcatccgt cacgtgttaa agattacatc atagaccgca ctgaaaacca gagccatctg 65220

gtaaaaattg aaaggtatac ctataatgat cagtggctta accctacaac aacattcgtt 65280

tctcatgaga gtaataggat aaaaatgatg cttccaatga atgatttgat tgataatcac 65340

gggaataact gggtgtcaga accccgaaat tcttatgtag gatatgtttc acaatctcag 65400

aaattcctgt cgaaggaata cacttttttc tatgtttttt cggtagttga aaaaaacccc 65460

tatgtaacag taagtgggga gccgctgata ccgggtgctg catatcccgc cctttcaaca 65520

agctattact ctattattcc caagggtggc gaatatctgg ctggtttaca tatatttcgt 65580

tctaaaactt atagttctgt aaacgataaa atgaatacgg cttctcttat gattcttttt 65640

accacctatc ccgttataag tagttctacg tttgctccgg aatataaggg ggataatgaa 65700

aacgcttttt ccaatacaca atatcgcata caccccgcta tagcggctat cggagagaaa 65760

gatttaaagt ctcattatgt tccgggaata agaatagtct atcatacaga atctacaatg 65820

aacccgggag ttcagcttta tgagctttat cttggttata agaataccac ttcactttat 65880

gaactggaag taacttcttc agatatagca cgttttgatg tacctaccat tgtagggtac 65940

cgcattaaac aaagtggtag cgttatttct tattctgtta ctttgaacaa tgaaccgccg 66000

gtatggtatg taattacggc aagcattcct tccatcgatc tttctgatcc gatttttacc 66060

gatcatagaa acgaagccgg cattattata gggtcgctgt acgggtatct atatgattat 66120

cagcttggag atgtcggaaa tctttcggct atttatcggt ggggatccaa gggtatttac 66180

ttttatgaag cactgttata tacccgctcg cttgacgatg cagaatacca gcaagtgaac 66240

gaacaccttg ttaagaaata ccgattcggg ctgtaatggg aagaataaat acgacatatt 66300

ttatttatct gtatttcccg cgtatagata taagcggtct tgataatata catattgaaa 66360

tagaaatatt gggtggcttt agttttacac ccgtttctta tacctacaat acatctggct 66420

cttttattac aacagaaacc cccgttgtca gggtgatgga aaatcgcaca ccggatatat 66480

accttcatgt tgtgagttta agtgctttat atagtaattt cgacccctct cttcattctt 66540

ggcatatctg gcttgatttc acaaggctta cggcttctaa aaccgacggt caacctgttt 66600

atacatcgga tatacaatcc attcagagtg atatatctat ggaaaactcc ggaggctata 66660

cgtattatga aaatattatg aatgggcttc ctatggtgcg aaccaacaat acaggattga 66720

caaaaaccgg tggcattctg acggatgatc cgatcatggt agtcgcagcg gtttatatca 66780

gccaatccgc tacatattgt cgtcttataa gctggggata tagtattaat gaagcatggg 66840

atgtatatgc tgagttttct ggcgcgttgg taagatttat atttgtcacc gatacggcga 66900

cggctgggag cggtcctact ataaccagtg actggttcag ttatcctcag gggtttgtac 66960

ttgccgcatg gcaagaggat gacgaaacca tgcatttccg gattatggat gaaagcggaa 67020

atgagtacga ttatcctgta attaccggac gcgggggcgg attttcaaac ttcagattgt 67080

tcgatattta ttatccaagt tacaactggg gatttaataa ttatgtggga gaaatcattg 67140

ttcacaatga tatatatatg gttgaagacg tctttcatta tatggctttc aaatgggtgc 67200

cgggattaac cggaagggtg cggataaatc gcttgtggga aaatctttat aaacctgaat 67260

tatatacatc gctcaatagt gttgtactta ttacaggctc aacatctttt accggttcta 67320

ttattaataa cgatccaatt attctaactt caataaataa catagataca ctacaatgga 67380

acccgcaatt taccggatct attgtcaata acaacccaat catcctaacc ccggtaaaca 67440

acatagatac actacaatgg aacccgcaat ttaccggatc tattgtcaat aacaaccctg 67500

ttttgttaac aacgataagt aacgtattac ttttgatgtt taattaataa aaaaaccacg 67560

aaagctatgc cttattattt cgagtttaaa gttagagaac tggatcttga accggtaagt 67620

gtaacgctct ctccggctcc aagttgggtt tcggtttata aatacaacac ccagcctttt 67680

gaccaatttt acggaactta tgacattaca gtgtttctgg tagcaaaccc acccccggga 67740

acaccggatg gtacctattc gatagggctt actttgagcg acgcgctggg cggaataacc 67800

acacattcag tcaatttcat aatcaacact tctggaacca ttacatttga tcctgtttcg 67860

gtgccggggc tctggggttg gtggcaaccc ggaaactggc ttactcagag cagtgatact 67920

ttcaatgatg tggctatatg gtatgacgct tctccggggg cacatcatct tacacttgat 67980

aggagaatta ctattttacc atggaatagt acagatgctg gaagtgctta tgtcggatct 68040

tacataaaaa cactttcgga taattcactt ctgttttcat ggagccatgt caatcaccaa 68100

tttgccaata tgaattattc gtcgggggct gataactaca aacccgaaaa tgttttgatt 68160

acaaaagata cttcttttta ctccaatcag tactctattt tctttgttta tagaaatcat 68220

ctcgactggt tttctcatcg tataaccgga atgagattaa ctataaatca ctatgaatac 68280

tgggcaacca atatatggga ctttgatgtt gaacggggta ataatcatct tgcaatgccg 68340

gtctattccc cggtggtgat taacagagcg gcgccttata caaccgtctc ttatggatca 68400

tactggaatg acgattataa tcacgggttt gtcggcggct ggtttattgc gttctgtctt 68460

cctccctatg ccgctaatcc gtcagccaga gacgcttatt actatgatga cgggggcgga 68520

cttaccacca tgagcgtatt caactatgcc cccggctatt accagaataa tgttccgcat 68580

caaccttata ttaccatatt caaagttaat aaatatgctt ctcaaacaga tgggtctctc 68640

ggtattcacc ctattaaatt gttttattac accaatgaag aatatgcgtc tatgtcgcta 68700

attgaaagaa acaacaggtt cagcagattt gtctttacta aagatcagtg gaatgctgtt 68760

ggatatattg ttgaggaaaa tccccttatt tccaacagcg ttgttatcgg ttattcctac 68820

acttacagca tttatttcaa cgaaacaact tccgttacaa aatctctgga agtaacattt 68880

tatgacataa atggcaattt cagacccccg acaacttatg cttatattga cggttcagac 68940

aaccagcagg catatataga cgtatatggt gggtttggca taggaacacg ttttgcgaca 69000

gctcagagtc aatattatgc caacaccggt actataggat ggagaactta taactttaca 69060

cccggggtgt tttctctctc tttcaaggaa tgtctgtttt atacccgcgc attatggaac 69120

gaagcgcccc agatcatgga ttatcttatg aaaaaacacg gtatcccgtt tgtaagctga 69180

tatgctggaa tttacctaca gtggtacgtt ttcatacccg gatagtcaaa cactttccag 69240

tttttactgg attattaacg ccccgtctgg aagtgttgtt acttattccg aaattttaaa 69300

ccccccgctt aaagaaatcc ctattgaagt aaccatttcc ctcgatacca caagtatacc 69360

gtcaggaaat gtaacatgga gtgttaactt ttttgcatat acaaccacct ctattacagg 69420

agaagtttat ctttatattt ccaatatctc aggattggaa ccatatagca tatctatctt 69480

tctgacttca agttatgaga aagaagggct ctggagaaat ctcgggttgg gtgaatcttt 69540

ttactgctat tcgctttcca ccactccgaa tgtacgattt atcaaacaca ccatttctct 69600

tcagagtatc agtttgatac cagccggtgg tagtatcaaa tgggaaaaac ccccggaaaa 69660

aacttattat tctttttcga ttttcgccaa agggtttttc cttagaacag ttgattttga 69720

ggggttgact acaagtcagc ttagctggta taatgatatt ccatttgctg tttcaggagc 69780

ctatctgtat accggatcag gatttccgct cattactttt atcaaccaga gtatgcttta 69840

tctggtaact tcatcggggg acttcagtaa ctttgttttt agagatctga caactaacac 69900

cgatgtgttt tctttcagtg tggaatatcc aacgctttct cttgcaagaa tatatatcac 69960

ctacgatggg aatgattttg tcataacatt cagcagtact gttagtgatt attactatac 70020

ctataatttg cccggactca gtttttctga tcatctactt attgggaatt atcaatcttt 70080

ttcgggtcat tccgcatgga actcttttat tgtacttgac tataatgcga caggaagtgc 70140

gtaccagaca ataagcaacc tgatatgagc cattttgatg aactacacga acattacagc 70200

accaccacgc tcagcgttaa cggggtagtg gtaagtcata gttacagagc atttccttcg 70260

cttagctacg ttgaaattac gctgtacaac gtacctgcac ctactggatc aaattatttc 70320

tttgtttatg atcacgttta caatcaaaac atatttcttt atgcgctgaa acctcaggat 70380

atagggaaag aaattctgga aacggttagt ttcaggatta ttgttgattg atcatcaata 70440

gataataaat tctggttttg taagcgtaat attgatctca aaccacccgt cttcgataaa 70500

cagtgcccct gctcctgaaa gtgtgtaatt tcctgtaatt atattgattc ttctgttgaa 70560

atgggatgta gtcaattccc atatactacc acccgaaaca aacgtctcaa attcttcttc 70620

ctctataaca ggttgatgtt ctatctcaac cagactcata gaagcaatta tggtgcgcct 70680

gtagttgaat tcagatatat gattcatttc tattgtgctg taggaaacga gtcggaattg 70740

ttgatgttcg ggaatggtga taaccgaaag agatatcccg tctactttgt gagaaaagaa 70800

aattctgttt tgagcgaagt ttgagtaaat agagtcgtgg gttttggtat atgtcccaag 70860

cccgatatat ctcaaataat atcttaccgg atattccaga ctaccgctga agttgtagat 70920

tttatcaaga atgcgttcct gaagtgcagc atatcgtatt tcacttgctg taaatacata 70980

aggtatggtg gtgcggatat acgggaatgt aatataatcc agttcagagc cggtaagtgc 71040

tatgatacct ttgaaaatct catttggaaa cgtgatataa cttatagata attgtgtata 71100

ggtataaaga taggtaagtc tcctgttttc aaacgtttct acaaaggaaa tggtatccat 71160

tgaatggctt gcgaagaaaa agagataatt ttcaatcaga tgctgtaaag tagcattaac 71220

aagagatttt gttaaacgat taaaatagag ggttctgttg aaatgaaaag atacataatc 71280

taacccgtaa ttattggttc gaagtgcaat aagatcagtg ttttgctcaa caggagcatt 71340

tacaaaccct gaaagcgttc taaaaagggt atatattttc cccgtctgaa aagcctctaa 71400

gttcaatccg atcggatcgg taagatatcc cctgaaatat ttttcattgc gcaattgtgt 71460

attgaagctt acgtaatagc tgaaggagta aagggtagtt ggatcaactg tatcgtgaac 71520

aggaggaaca atcaaatcat aagtcatggg gagaaagtct attttttcaa tgctgattgg 71580

atcataaaac tcatttttcc acccaatgcg gttgaacaca aagaacggag gaactccttc 71640

ggtggaataa gtgccagcgg gtatggaacc agacaaaacg aattctgaat aagtgggtct 71700

gtaggtgtaa agccgataga tgatagattg ggaatactga gatgtagtag actgatgata 71760

taccgaaacg gtgaacgaat gggttccgga tacgaaccca ctcattgtga tataaagaac 71820

caattctttg tattcaggat ttccctgata gaaattatca attatgctgt gcgaaaaaac 71880

aaaaggtgga agggatgata ccacttccac ctgattgaga aatacccttc ttacagggta 71940

agaaactgaa taagtcatgg tttcatatca tcacttaagg attacaaagt ggtcagcatg 72000

aacgtctgca cggttcataa gcgtgaagct acgcgcggca agatactgtt caagcaggat 72060

aatatcgcgc tccgtcggtg atttgataat aaccagttcg taaatgctac cgacaagcgg 72120

gcgcacgccg tcggtaccaa ttgtgagaat attgattccg tctggaccca ccgccacatt 72180

gttcatcaag gggataccgg aaatccggag cgaactgttc ccgctgaaca cacccactac 72240

cacctgatcg cgggtagcga gtgaaagcgt atattccgtg ctggagcctc cgattcccca 72300

gttgtggggc atttcacaga aaatatgggg gttgacagaa agtgtaccac cggagaacaa 72360

cccaccgttg gcgaaagaac ccacaatacc gatagcgaac ggctgctcga tttccagacc 72420

ggtaccttcg agacccatcg accgaagcca ttcgtttcca cggaacacca ccgccgacaa 72480

tccgttgtat gcatcccgca cgaaaatggg ctggttatcc gggttggatt gtgtgaggga 72540

gtaagataga taagccgatg ttgaaacata tgctggcacc cacgcatcaa ccttatcgcc 72600

cgtgttgtag gaagccgtga gggtgttcgc atcaaagcga agcaccactt tgggcaccca 72660

gctttcaatg gtttccgccg gatcgacaaa ataggggatg ttatatttct tagccagata 72720

gttttcaacg ttctgacgtt cagcgttggt aagtttacgg tcaaacacgc atagctcagc 72780

aatatagcct ctcaggttcc accctatgaa catattcgat tcaacacggt taccggtctt 72840

accttccata taccgcacac cgttgatgta aatgcggtca agcggatatt tggggtggga 72900

agtagcaaag cgaacatcgt tggttgttgg cgaaccagag agaccactaa tgtggtacag 72960

attgacatat gaacctgttt cattttcaag tatcaccgta atgatattcc agtcattcag 73020

gggtacaaaa gcgtctgcgg gttgtggaac agtattgtac ccaccgtaag agtccggtag 73080

tgcgttggag actcgagggt tgcgatatga agagttcaaa taaatccagt gttcaacctg 73140

attttctttt acttcaaggc ggggcacaat tactgaataa ctgtgaacat tattttcatc 73200

aaccattctg aaataaggta catccgtatc gtctgtgttg tgagtatccg actttggttg 73260

aggatcccac atggagaaca tccacagaaa cctacccgga atgtttccgt aatttactga 73320

attgttagga atgggattag aagaattggt tgtaatattg ctgtaattcg gatgataaac 73380

ccacaccgat ccactctgca caaacacccc agatgtcgta tccgggagtc tatccagttt 73440

ggcaaccatg ataatggtgc gttcagtatt ctgagaataa tctccggtgc ccggatagtt 73500

aatacgcata accgaaccgg aaccgaaata ccaagccgga taaccgttga caatattttc 73560

gacgaaaata ggtttgcgga aatcgttaac ctgagtagct ttaaatccgg aatatgcggg 73620

aacaaggttg ggaatttcgt caacgtaatc gccggtttca agctgaggag tggagccgtc 73680

ggcgctcatc cagattttgc agttggggac gtccgacggc gaagaatacg cattgatcgt 73740

ctgaacataa atgggataag tgcgaactgt ttccggggta acgccatcgg tagagcgtac 73800

cgtaatgctg taggtgcccg gcgctacacc cgacagatca ccgtatacac tcagaatccc 73860

ttcggtgcgc ccgtcgggaa gaatggactg ggtaaaatca tatccggtaa cccagctcgg 73920

ggcggcggaa accgtagcag taatcgtatt accgtcgtta tcgtagatat aaatggaaaa 73980

cgttacggtg ttagaactct ggtaagtcgg cattgtttat cccggttttg ttttaaatat 74040

tcttatttca ctcaaaataa aaagtcaaat agagataagg cacagaaata ctgctatagt 74100

cattgatgga gtctatatag tcttttccaa tatacatgtg tgtgataaca tctccgctat 74160

tatagtcata catcaagatg tattcggcta catcgggagg aatgttgttc ataaagaacc 74220

ctgaaaatgt tatggagtaa atatttccgt caaactgttc gtcaatcata ctgacagttt 74280

gcgtcagatc cccccccact acccgttaca acatacaaac tgaaagatga gtgtgtaacg 74340

ttaaattccg gataataaga attaaccggc accactgaaa gagtttttcc atagaaaata 74400

tttcttaccg cttctttaaa agcattcatt atggtttctt ttcggtaaaa aggttcggtg 74460

ttgtaagata gattgataaa tccatagatt ttatctctgt atagagagta actgtaacct 74520

actctatagt taattaagtt gtattcctga tttagtgtat ggttaacagg ctgactgtat 74580

acccatttgt aagcaagcca gcggtgtttt tcatacatgc tggatataag cggctttcga 74640

gagatcacag gcgatgtgtt tctttgagta gcatttatcc agtaattgat aggcgattcc 74700

acctttctgc tcatgatgtt tgttctattt ccggcaatga tcgctcttct taatgtgtgt 74760

ttattaatcg ttttgaacaa ttgtcgatag atagtgcggg tcttgttttt gacagtgttt 74820

ccggttctat gatatgctat aagtatctgt cggagttggt tgagatcaag gagaaaattt 74880

tgagttttct ttacagaagt gagcaggacg ttaccctgaa aacttggaaa gaagtctctg 74940

gtggtacgga taacttcccg gatttttaaa agtctccggt caaaatgggg gatatcatag 75000

cttgcataaa tgttagtgcc cctgaagaac aatccgatta ttctatcaat ggttgtttta 75060

tagtttaatt ttattgtgcg tatggttaat tttatcaaac gttgcatctg atttgctata 75120

aggttaaggt actttttaaa actcagaagt ctgatggtta catatggctc taaggtggaa 75180

taaatgattt ttccaacaaa tctgacctgt ttaataatct gttggtaaaa acgtagcaca 75240

tagttaaccg gtgtgtatcc ggtcaaagtt ttaaagaaag ttttattcac cagagtcgat 75300

ttaatgagtg atctggtctt gatgatagtt ttaataaaaa agtttttgat tgaattcaac 75360

agactgttaa aggaggtaga tatatttaaa actttaaaaa attcttcagt gctccataca 75420

aaagcggaaa gcaatttatt gaaagttttt aaattgggaa atctcagttt taaagtgggg 75480

gtgtagttga caggtgtgtt ttttgttttc aagatatact tgaactcatt agaactaaga 75540

ggttggttga cagcattata tccattgaaa agcgtaagtg cgtaggggtt gtcgtagttg 75600

ttgtcaagga aaagtcgaag tgctgtcggg tcatcatttt ctatcaacag cggatcatca 75660

atcgggtcta tataaggatc atagggaacg gaaaatatat ccctgaaatc gtttgtcgaa 75720

gtataaatat aagataatgt atagttaaag attaccgact ttgtttcata tttgtcagtt 75780

gaataaaacc tgaaccgtat acttccagta taccagtcag gcggaaagga agatgccgtt 75840

aaaagattga gataggttat agtagacccg gagtgcgata caccaaacca gaacttattg 75900

ggtggggatt gttgaacgat aagtgggctg aatactcctc ttcctttgtg gtctacttta 75960

aatctcattt tgttcgtagg ttatgtcata ttcgtccagt atcaaagcgt tgtcaacaaa 76020

tagagaattt tcatatccgt gcatgaatgg aatgggttct ccatcgagtg atatgtcttg 76080

aataccaatg aatatgggaa aatacagact gatcgatata tccattactt ctataatcgg 76140

ataatgatat tcgatagtta tattgaatac tgttatttca gggtaattca aacttatggt 76200

gaagataaac ccatattcca taagagggtg atatagatta attgaaatgg tgttgaagtt 76260

aatgtcaaaa tcgagggtgg attcatattg tgtgctgaac gttttgccgt ttatgtcgct 76320

gagatcaggt gaataaagat aaatattaaa atcgaggggg gtatctataa tcaaagcttc 76380

catatctata taatagaggt ctatatcggc aatctttttt ccttgataat acacatcata 76440

ttccagatct tttgaaaaac tggtactgaa aaaataccgg taagtgtcaa acagatcaag 76500

aattattgaa actgtgtgtt cgttttggaa gaccagacta taactgacat ctgaaactaa 76560

cgtcagacta ctggtactta caggatatct gaaataaatg tctctataac gtaaatacct 76620

gtcggctgat tcggtatata cttttattat gtaatctgta ttaatactca taatttatcg 76680

atataagttc gtttcccttt ttaaccagaa tagtactgat gggtacattt ccgttcatga 76740

attcaccaag catatcgata ataaaatcta cttcttccct cacttccagc ataagtgtgg 76800

ggggtatttc aagatagaca ataccatctt gataggaacc ttttacatat tcacggtttt 76860

tataccaatt gatatatcgg ctcatagaat gttgaatttt ccaatcgtct tttttaaagg 76920

aaaacattcc ttcatatttg ttgaagggat cgtaaacgaa accgacgtag tctttcatgt 76980

ttttctttaa ataaacaggc ggttgtgttt ttattcagaa aaaacttatt taaagaaaaa 77040

agatgtatac cgaactgttc aagaaaagca acccgcacaa ctcatattac tatcattacg 77100

tgcattttga cagtaattca aacacacatt caatcgatgt tcccggcgga aatgcgctca 77160

aaaacattct tattgtgggt aacgcttcta ccccttattt tgtctctttt aaaatctata 77220

catcgcatag cgggtttgtg ccggttccag tatcctacga ttacgaagcg cttggaaaca 77280

atgcgctgat tacccctaat atctcttcat ttgcagtttt ttcctctatt caaacctcat 77340

cgcttcgcat tagcattacc aatatcaccc cgtttagcgg aagtgtttac atactgttta 77400

aagtcgagta acgtatgttt tacgaacctt ctgtaagctt ttttgcagta tatcctcagt 77460

acagcaccag cgcggctttt ctcacagaat tcaataaatc atcggcgtgg gtgctccaca 77520

aactgggcta cccggtggta tcggtggaat tgacgaaaga tcagcttatg tttctctttc 77580

acgaagcatg gcaagaatac tctcagtata tttcagaatt tctgattcag gaaaactatg 77640

ataacgtttt aataaaaaac attttccaga cggaagggga aatctttgag aagtttccca 77700

aacctaacag ttcgcttatc atcgagcttt ctgatcgcta tggaatgtac gacatgaaca 77760

ccgaatatgt aatcattcca cttaccgctt ctcaatcggt ttatgacttg aagaattaca 77820

ttaccgcatc cggaaaaatt cacgttcagc aggtgcttgt caatagaccg cgcgttggtc 77880

ttggttctac gctgtacggt aatgcttttg tcttcaacaa ctattctccc ttcaccgtag 77940

gatacggcgc gggctggaat atcggtcagg tgctcacgcc gctttcctat cttgccacca 78000

ccatgcaggc taccgatctt gcctacaata tgtatcgcaa gctccacttc tttgaaattg 78060

tctctggaag tatgattcgc atttctcctg ttcccgattc caacgactcc cggcttacaa 78120

tcagatacaa actggaacgg gaagaaggtg atcttattga aatgtacaat tcaatatttt 78180

atacgaaaac aggtctcctc gatctggaaa aactaaatga aaactccctt attgtgcttc 78240

ggcatatctt cctcatgaag gtgatcgata cgcttatttt catccgcaag aagtacgaca 78300

actacgcact tcccaatgcg gaacttacgc tgaacgtcga caacctgaag gaactcaggg 78360

aatccaccaa ggaaaagatc gacaaataca aagagtggct tgacaacatg aaacttcacg 78420

caaggcttca gcggaaagga gaagaagcag aagcgctgga gcgggaactc cagcgctatc 78480

ctatggggtt cctatttatg taatctctca cctgcaatca ctcagcgtgc aggcgcccat 78540

ggggtgatct cctctaccgg gctttttgaa cggcggtgga atcttatgtc ccggtttgtg 78600

gtgtgcagta acttcctcaa cctttccata ggttgtgagc atgggggtaa tccacctttt 78660

catggcttct ccgatttttt attgttggtt cttatagata aataaccctg tggcacgcat 78720

cgtaagtgaa aaaccacccc aacagccacc accggttcac ataacggaaa aattctttgc 78780

cttttttaaa ctctttcatg attgttcttc ttttggaaga ttcagcttaa tggtgatata 78840

atccgagtcg gggaattctt ttcttaaatc ctccagcgac tcatacacaa aaatcatccc 78900

gacggcaccg gtgttagcta tcttagaaag tggatagacg actttctgaa cgccgttatt 78960

gatgacaacc tgcaggtcat ccagaaagtt aagctgcatc gcgacgtaat acacgcgctc 79020

ttcgttattg ttgtcgttca tggcacacag ggttttaagg ttacgcatgg tagtctattt 79080

ttacaatgta ggttttgtcg ttatattcta tcatgtgata atgcgcctga taaatatggg 79140

ttccttccag aaataggggc tcgttacctt caaggtagac gaacaccata tcttcgtctc 79200

cacccccctg agaaaggcgg ataaagggag tgtgctgact ctggtgagta ataccgataa 79260

caacatcggg gtttttctcg ataaaatcga gaatttcccg ctcctgttca gtgggttcaa 79320

aatgcttcca ttgatacacc cggtaggggc gattcgaagc gatgtaatag ggaagagaag 79380

ctacatgtcg gttataaata tccagaacaa tctcttcaat atcagtattt tctttatttt 79440

taatttcttc ctcgagtagc atgttaagat caagtatcat gtgagccagc gtgctgactt 79500

ctgcttcatg cattttaata cctttctttt caaggatacg aacaatgcct tcagtgtcga 79560

atttgagaat catggcgcta atgggtttag ttttcactct ctacaagaaa acgaataaga 79620

tcctcaacgg tttttatctt tgtagtattt tcaacatacc cgagactttt cagcagatca 79680

attgttttct ctgaaatgat ctgacagtat ttgtctctat ctatgtattt tttaacgatt 79740

tcaagaccct cctcatcatc ctcacgtatg ctaagtgcgt ggatattgcg gagcctgttg 79800

atatgcgttt tctttcccgc tttcagaata tcccacacgc cgctcccatg ttcggggtta 79860

acttcttcca gagaaagcgg gagattggtt ctggaaggat ccagcatggt gcagtagaac 79920

cagtagatct tgtctcccat ttgcgggggt ttgcatccta taatggaagc gaaaagcgct 79980

cccttataat gaatgggaag tgtatggtca tacattttta tgaatatctc agagattggg 80040

acattctcct ttttcatctt cataacttcc tctacatact ccacatatct ttcggcgctg 80100

tcagacgaag atattttcat tttgtgatag agatcttcaa tagaccagaa attcttttga 80160

gacacaaagt tattgtagaa cgctatggtg gcggaaatga catcgatgtc gggttggctg 80220

atatacttca ggtaacccct gaaatacttc ttgacaattt caggcaccga agagttgatc 80280

acttcgattc ccttcatctc ttctttaccg tctacagtaa ccgcaaagta gcggttgatt 80340

tctttgataa gaatggattt gaacacgaac tcctgcttta actccagctt gaaatcttct 80400

cttgcattaa agttattttc catatagtca ttgataaaag agttgagatg ttcttgaagc 80460

tcaccggctt ccgccaccgg atcatccgta aaagctttga cgaaaatgga gtcggtatgc 80520

gaataaatga agcgatcgcg aatctgagaa atcacggagc gaatagacat gcgcccggcg 80580

gcggttacac tttccgcaat gggaaggcac cccatgtaca ccgaacggtt tccgaagata 80640

ccgtacatgg agttcatcat aattttaagt gcccattgac ggaaatggtg ttccatgttg 80700

ccagtttctt tgaaaagctt acgttcttcc ttacgtcggg tgaaaatctc ccgaatgata 80760

gaaggaagca cgccaaccgg ctctttcctg taaaaccagc agatacccga cgggttgggc 80820

accataatga tatttcgact ttttaaaaat tgccggagtt cctcaaagct gttgatgaca 80880

aagaggggtt cactccggta agaagggttc atccctgaat cgaagatgta gaggggaaac 80940

ccgaattccg gttcttcctg atctaccgga atcactttgt tctccacccg catacacccg 81000

taaaactccg ttacgaacgt agcgggatcg atattgaatt tgctgattac agaggggtac 81060

agcgatgtaa aatcaagatc gaatacgttg aagtaaatat cggggttggt aagttcaatg 81120

taagcaccgc gataacgata cttgttgatg ttcatagcag aatacgtttg ttttacattg 81180

cgggatcaaa atgggtatct ttcacctcga taaggtaggt gtcttttaaa tcacatttgt 81240

ataatacgcc atcgagtgga gaaagatcaa taattctcaa aacttcatcc gtatagaatt 81300

ttcgctcgat aagattatgc gtttccagac gtttgcagta ctcgaagata gcgtctccaa 81360

caacatagct ttccaggtgc cagcaggcaa gcccatcata atgataaagc ccccaccaac 81420

catttgctct ttccctgacc actgcaggga taacccccag atcttcaaga aatgcttcaa 81480

gtttattttc atccatataa agcaaatcgc gtcgcattat gttttttccc cgctcctcaa 81540

gaaacgcatc aacatacatc cacccggttt catcccggat aagcttgcga agtgaagggt 81600

atgcctcaac cgatgtaaac ccggtcttca aatcggtaat aatatcccgc gaaaaccgca 81660

taacgaaata ataaggggtt tcgtagtcga taagtttttc aataatttta atgatttcgt 81720

acttcatggc taaaacgcta cttcatggct aatacgctac ggttagttta agtgtcgggt 81780

aaacctttcc attaactaat gccacgccca cccccccgta aatggatccg aaaaatctct 81840

tctggaaaga aaagtcgtaa taattgagcc ctacggaagc gctgataagg ttgtgcgttt 81900

ttctaacctt cagcgcaaaa tcttcctgca tgaaacgtcc ggtttccggg ttgaaaaacg 81960

ttacgcggag cgtgttgccc ttccacgtgg catatctttc cggaagaagc ccgtagagtt 82020

tcatgtccac cggcttcgga cactccaccg tgtcaatctt ccccacgggc gtctcccggt 82080

aaatgatctg tttgaccggc tgggcaaact tcccttcaac cttcaattct gaaggaaaaa 82140

ctctgtccga aagttccact ctgacttccg gtctgtaaac ggtgcggttg acgtaaagat 82200

gtatgttaac cgcgatcagg atcaaaagga gtgcttcttt ccagtacttc ataagtcttc 82260

ctcttcttgg aatttgtctt cttcgtctct gatcatagcg tatagaatga tcagatagtt 82320

aattgcgtca atgattctac cttcgacagc atcccgctgg tttttaaccc ctctgatcca 82380

gcgtgccacc cctcttaaat gtttatccag aaatacatac agcacttctt cccttgaaat 82440

acccaatcgc tttgcagttt cttcaaaatt ctgaaataca ttgtcggttt cggcatactc 82500

ctgttgggct tggagtcgga cacgatttac ttctccaata agctctttta caatgcgttc 82560

gaattttgtg gtattcatgg atttcctcca ttaagtttct ggtatttatc ttatttaaag 82620

aaaaagatga atactccccg caaaatattt cttaatccac ccacctcaag atccctacag 82680

gatattgaat acctttacct caccaacaaa cacatcatta ccggcgcgat aaataaagcc 82740

ggtatgagca ttgatgaagc ttgtgaatgt gttgtggggg ggatcgtgct cgaatataaa 82800

gaaacacacg gcatcaatat ttttgataat ctgactatgg cggtggagta tttcattaac 82860

aggtacaaag aggatttaaa aaccgggcgc atttaactca tcatcttttc gttgataaat 82920

tgaatgagtt cctgtacgga aggataaaac tgttcctcga aaatctggtg gtttgtcttt 82980

atcaattctt caagtttatc cacatccgcc ccgatctttt caaaaaaggt acgggcttcg 83040

gaaaacagtt cccctctggt ttcacattcg gtataaacca gaagaggaac cataacccgg 83100

tagaaaaatt cttccggtgc ttccctatca acatactctt caataagttt ctctgtaata 83160

ggaaccccgc acgcctcaaa cacgtcatcc tgcacggcga agtgaatgac gccgttatac 83220

aaaaggtgcc gcaaccgcac cttccacatc agggaagggt cggttacgaa ctcatacacc 83280

atttggagag cattctcgag aggaacctcc tttaacggaa gctcctcaat ttcttcttcg 83340

atcgggtaga agacgttctc ttctttggag aacttacgct ccggggtaat tataatccag 83400

agcgcttctt tgacctgagc agcgttcaag ttgcccatgt tgtacctcct tgtttttgtt 83460

agttacagat taaacaattt gctggttttc tcgaactcct cgaaccactg tttccggagt 83520

tcatccgaac ccctgtattt caggggcttg ctatcttctt taactttcga ttccggttca 83580

ggttgctcct gggtttcgag tttcagggga atttcaactt tccctttgag ttctttgagc 83640

ttgttctcaa tacccggcgg aacaatccga tttttgaaga ccagttccac cgctttgtta 83700

atcacttcat cagcggcttt acgggtgcgc tgataaatgg catcctgctg agcctctttg 83760

agtaaataca aagcgcggcg ttttagataa tcctcgctgg cgcatctctg catggtgaac 83820

tccagcgaac gtcggttgtg gatttcgctg ttagccataa ggctctccca ccacatatac 83880

tctttttcag aattgaggat ataagccccc ttgaatctga cataggtatc ctcatcaagc 83940

ttgaaccagt atgcatcata gaaactgtac ccccgcaagg aatcgtcaat aacgtacccc 84000

gcaaggggtt cgacaaaaac aagctccaga tcggctactg atagtacatc gatcatatag 84060

tcgcatcctt tgttcatagc gtctttgaat ttttctctaa tcatggcttt ttcctccttt 84120

ggtttatcgt taaacccacc aacgtcaaaa agagggagtt tgtttttcgg atggagacag 84180

aattcggagt ttttgggcat accccgcttc cagtgttcca cccagctatg acatacttcc 84240

tcaaacatat cggggtatgt ctctctgaac ttgggaatta cgtatcgata gaattcgata 84300

tcgtatttga atagcgcatt tcttataacc gtaggatctt tttccattgt gctctgtacg 84360

cggagatttc tatgaaaatc aagactctgg tacaggaaga aaaacgttgc gttcacaaca 84420

aaaagatatg ctgtaaactc gatccaacta aatgctctat attcggttgc aacagggtaa 84480

aatttgtaaa gccagtagcc cacgaaacca aacgccacaa ccttcaaagg ttcgtgtacc 84540

ttgttcacaa cacgcgggct gtaaagctta aaacccgaaa gcacgttgta cgtgccggta 84600

acgaaccacc tcccaatcca acacaaaccg atagaacccg atacaagaat ggtgatcatt 84660

gtctggctca tgtgggcgac ggcttcgtgg tgcccgagca taaacgggaa accaataaac 84720

cgcccgaata ttagcaagac cgggaatgac agaaggtccc cggttataat gcagacggcg 84780

gcaatgaatg caatccacgc aataccggcg gcaaacgtaa acgacagata aagggcgtcg 84840

ttaaacgctt ccgcctcctt gcgccacagc ttcaaattat ctccataata aaaccccaga 84900

accggaaccg ctacaagata gcgatccagc ccctccacca cttccttctt gctcaactca 84960

agttcgccct taccccactt gaggagctta tctcgataaa gcttgaaagc tgtaagggcg 85020

tactttcttg ttactccggc gtacatggct ttccgggttt gagttatcaa tctgcttata 85080

acatacgccg gaaatccaga aaagtcaagg ggattacgtt aattttttac gaagaagaag 85140

acgtgctacg tcgtcaaagt aaatggcggt tttagtggcg ttgagacgct tgactttgag 85200

cggtttataa agtctgttct tgataaaaaa cgaagctctg ataattttcc agacgtttac 85260

gtaaaaacta ctattctttt cgtaaaaaat gcagagggcg ataaaatcgt cagattgggg 85320

gttatagaca agccggtcat ttttctgaaa cacccaagac ctctctattc tggtgtatct 85380

atatctgggt acatcctcac aggttttaac atgtatatat ctaccctcgc atatcagatc 85440

agccgcatag gatttgtctg aagtgatagt cagatcgggt ggggtgcatt cataaccaag 85500

gttggtgaga tattcataaa cggcgaattc tcctatttta ccaacaaaat aattccattt 85560

tattctttcg gggttgtgct ggtggcgctt tttgtattgc tcaagcacaa tcccgtcgtt 85620

tatctgattc ttagcatatt ccatgcagat gggcacatac tgatctactt ttatcatctt 85680

acccaccctt acccaagagc gatacttgtg gacggattga taaggtacat caccgccgtt 85740

tcacggtaaa acgttgattt tgtgtaatgg atcccaagcg aagagacaaa gggagttccc 85800

ggataagcca tttgtgtgtt gtatctattg acaccgcttt tcggaaatgt atctgctaca 85860

atggaaaaga ccgcaccctc gcgctctgtt gctatacggt cgactgtaac ggtatccgga 85920

attggaattt caccatcgaa agatttgaac atactgaaag aaaattgctc aaaatgaggg 85980

attgactgag tcatctgaaa tgcgtagaaa ggtttacctt caattaccac tcccgcgaag 86040

aaattctctc cggcaaaaag ctgacgaagc aacaagatag cgtcgcgggt tttgtttacc 86100

acctcaagca tatcctgatt gcgggtttca ataacgtgta cattatcccc ctccgccaga 86160

tttctaacgc ggttggaaag atttcgctgc aaaaacacca cggcggaata aggagtatct 86220

tcgagttttt gaacagggtt ttcggtaatg atatgatccg gttgataaat cgagccttcg 86280

aaagcgttat ccgtaatgac tccgatatgt ctcagattgg attccatgta ggaaagcgtt 86340

gaaacataat aactgtaact gatcgtcgat gtggtaacct ctggaaacat gctgtaggtg 86400

tggttgtcaa tgagccacat tgagatagta ctgtcagatg tacctttcag gtagaaataa 86460

accgaagtgg aaataacagt aggcattacc atcatcatgt agctcatgct gtaaagctga 86520

tctattccgg ggaaaagcag cgtaatcact ttcccctgaa gcaccacatt gaacggaagc 86580

agcgaaagac cattttccaa atctctcatg tagcagacgc cgtggaaatt cagactatct 86640

acaacaaaac cggaattatc aataacattt acagaaactg aagttataag ctcgccgcga 86700

gatgtataga ccggatagtt aaaagccccg gttacataat aggggttggc gttgctgacg 86760

gtaatggaga aggtaataga atcgagaaag ctattggcgg taacttcata atattctcta 86820

atatccttat gttcattata gggaatgaac ccgtaaaacg taaaataatt attcaacaca 86880

atatcttccg gaggaatgtt ttgacttacc ggtataatgt gttccgtgat gtaatactga 86940

tcccccagaa acgcgtcatg aatgatcaca tcaaactgat aatctttatt tcgtaaatcc 87000

agcgattcag ccagcgtgtt taaccattta actttcattt tgcgattgaa ggcgtgatag 87060

gtaatacgat tgatctgatc gtgcagcgcg tcgaacgcat cgagaagttt tccggtaagc 87120

tgctcaagcg tttgagacgg gttctgagtt gtcggttcat tcaaaatatt tgtttccaca 87180

aactgaagat cattgcggaa gtagaaaaca tccatgatat tcccgatcat atccatatag 87240

gtgagatatg aaggatcgaa cacttcttca ggaagtcttg aagaaaggcg atacgggttg 87300

gatacgtcgt attcagtcgc agcataaagg tgcatatcaa gaagcacctg atacggattg 87360

acgcccggat aaattgaaga aaacgaagga aatacttctt cccagaaatg tatggggagc 87420

agataaaagg tacccggaag cgatgtcgag ttgtagtagt aatccagata tcccagcgcg 87480

taactctgac gaatggagtc gtctctaaag taatggttga tgtgcgttac gtcttccgaa 87540

gcaaaccatt taatgaatgg aaggaagcta tcgtagagtt tattttttat ttccttatat 87600

ttttcagcct tctccggata aaaacctgaa agcgtggtga taatctcatc atatttcctg 87660

agcagcgtga ttcctttgaa cgccgcctga atgagcgctt ctgctgaccc gaatttgaca 87720

aatccggaga gcagatggaa attggatttc tgctccatac ttccgaagct aaaagacggg 87780

atataggtgt tgattcgatt gtattcaatg tattccagta gatcgacggg actcctatct 87840

tcaaattcga gatgaaacac gttgttggca aacgcatctt ccctaccccc aatggcgctg 87900

aaggtaaccg tgtctgtttc cgtgagattt accggaatgg attcctgcaa atccacctga 87960

cgcacaagat acacttcttt tgtcgagtga aggagtgatg aagttccata tacataaaac 88020

gtttcctgat aataaaccgg ggtacccagt ttatgaatat tcccgtttac tttaaccaga 88080

atactgtagc tattctggat tcgagcggtt acttcagcgt aatagttgaa caggtcttca 88140

aaagtgatac tggtgctgat gtagttttca aaagcttcgt taatctggtt ttcaagttgt 88200

tctatggctt cgacggcaaa tgaaatggtg aggaatatct gattgagacc ggtttgcgca 88260

gaaaggtatt ctttcgaaag tggttcggct tcttcaagaa cttgctgata agcggaaatt 88320

tcattttgat aaaaattatt gaaaaactcc tgtacatcgt tgaaactgac ggtagaggtg 88380

agttccagcc gggaggttgt aaaactaaac gcctgctctt ctacgtagct gtaagttcct 88440

aattttttga aataagcgta gacgggatag gagtctacag agaaggtata aacaaacgga 88500

agcgaaatgg tgggtttttc aattccttca aaaacttcag ccggaacaga gtcaaccacc 88560

agatagacgt ttccacttct tacatacttg gaggttactt tgccaataaa atcaacggaa 88620

taaatgattt ccccggctga agaaccgctg aagtgttcaa tgtaaatgta aggatttgtg 88680

taggaaagag aatatggagt aaacccggct acaatttgag aacccgaaat aattataaaa 88740

tcttgcattc ctctttttct gttaaataat aacgcaataa gtcaagtgca tctttgggat 88800

agaaaggctg atagtctttc atggaatgtg gatattcgcc ccagtctttg taaccggcgg 88860

gaggaaacag aaaaccaact ttacatacgc cgctatagag ttccaacact ttagaaattt 88920

cttcaacgct tacatccgaa tcaaaacaga acaccagttc tttaaccttt aatttttgca 88980

caacgtagga atccggaata cgattctttc cacagagtac gcacattccc acacccaacc 89040

catccgttgc atggggaagc atatcgaaca ttccctcgaa cagataaatc tttccttttc 89100

gagccgcttc gtagaaatag accgggagct tacccaccat ataggaaaga taccgaacct 89160

tatcgaaagg ttgatagaat tgaacgtttc ctatggaatc accgaaggca acccgctttt 89220

catctaccac cttgaaaaat ccttttgacg acatatagct gagaagttcc ggttttaccc 89280

ggcgctcttc aatgatgtgt ttgataaccg gatattcgat attttcctct gaaagaggag 89340

ccgccttttt aaaaagcgag cggtagtaaa agtttttctt gacgtttgtc tgttcaacat 89400

ccgtaaaatc gatatcaccc gaattcttat aatatgaaat gagttcgaca ggtttaaatc 89460

cgaaaatgcg ctcgaagtct ctataaacgg tgcctgaaaa cccacaacgg aaacagatga 89520

aaagaggggc gtctatggaa aagtaaagcg tgagtcggcg gttgttttta tgcggggcgc 89580

acttagggca caaacaggct acttctttac cgcccccggc aactttagct tcgctgaagt 89640

atttggtgag gatttctaca atcatggttt tttctacaaa aactctaagg aatcacaatg 89700

gttcccggtg tagtaatcac aggatgattt aaagtaatgt tcacatcggt taccgttata 89760

tccggcggaa tcgttgaaat gtcaatcggg atatcgcagt atttgctctg agaaatctct 89820

acggcttcga cggttacgga aaaattgaaa tcatcgtcgg tatcgaatgc agccatgaaa 89880

aactgttcat cggtacgtac gttgacaatt tcataccatc ttctggattc cccaagcacc 89940

agatctcccg gttgtggaaa atagtcgaat tctttcagca cattcctaag aagatgaagt 90000

cggagtttcc gcaccgatcg cattccaacc tcctctgaag ccggttcccc aacctcatat 90060

tccacacgac aggggatccg gtacatttta tattctctaa tatctttctt aggagactct 90120

ccatacagat agtgcaatac gtcgttttcg tcatcttcca ccgcgttttc aataatacga 90180

acaaaaagga agttggcgtt gagaatatcc tcaagcgctt caagggcaaa atgctgaaga 90240

agattgagtt cccgtcttcc ccagaaaaga ggattacgct tttttatcat ttttatttaa 90300

ataacccctt ttcaattctc tccgttagaa gcttcttttc cgacttttgc attttctctt 90360

cgtcgccgtc aaggcgggca aaaaaccaac ttttatcatg ataatccata agtcgaagag 90420

cgaacctttt gcgaaactct ccggggtttt cttccggaga aacctgttcg gaaatctctt 90480

tataaatcgt atcaaaagat gactcaagct gatttcgcat atcggtataa atttctttga 90540

gtttcatcac ggtttcctgt tcatccgggg taagtacaaa atcatcaagt ttgttttcaa 90600

gaaaaagatc ggcgagcttc tcaggagtga ttgtagtttt aatccggtgg agctccagat 90660

ataccgggtg cttgatcttt gtgcggtaat aaacacgcgg ggcaatttcc tgtacggcta 90720

caaatccttc atataccacc tcataaccgt ctctcaggct tttgaaaagc ggtgtaactt 90780

cctcaaatag ttcctgaagg cgattggcac gaaaaagagt atagttttgc tcttgagaca 90840

gaacagccgg tagcttaaga tttatttttc cgccactttc gttgaaaatg cgtacggctt 90900

cttcggaggg acccacctcg aaatatccct tctccggatc caccgaacgc acaccgatca 90960

gaatgatatt tggctcctca taaggaacca ccactcgcgc gtccggatga accatttcaa 91020

atatgtaaca gtatgaggag ttcaaatgat agagaaggta aggcggatat ttcttttcaa 91080

aggtttccca gaacaattct cgatatgttt tatccatatg agtggtaacc attccgtttt 91140

tgacaatgga tccatttgcg tcaatactcc caagagtgtg aattttccac ccttcatcat 91200

aatataaaac cacacaagta ccatccagct tttcaaccag tttcatggga agtttgaaca 91260

tgaaaccggc tttgcgcttt tcattcaggg gagacgcgta acgaagcgtc tgataatagt 91320

ttacgatttc cggctggagt tcttcccccc agttgaaaaa tttgtcaaag ggataagaca 91380

gaactttcca accactatcc gttttgcgga gaatcgcccc gcgacaggca aggtgatata 91440

tcttatcaaa cttacaacca aggtgatatt tgaacatgta tagatcaccc cggtttttgc 91500

acataatccc ctccttgcga agggattcga cggctacttc cggagactca aaagagttca 91560

ggtgttcgat aaggtactca accgggtatt ttacgttcat cgattccata gcgtactata 91620

agtcttgttt tgagttttcg gaagcgtcgg ttgatcaggg agttcgtcta caacttcata 91680

gtttccggat aggaaaccgt agcaatcaca cacctccttc gtaaatctgt ttacgggaat 91740

tggttacaag tttttcagct acgcgcaaca ttttgttact ccacttttca accggggttt 91800

ccacaaggaa atgaccaata cgggtatcaa accggttgaa gcccacattg ttgcgctgag 91860

ccgcgcggtc tttatccagc gccgccacga tcgccagctt ctgctgaagc tccagcgcat 91920

aaccccgctc ttcctccgaa atggttttac tttcttcttc ctcctcccgc tgctgcttct 91980

gctcagacgt agtaatcaca tcgagcagag atacaggctt ctcaagttga gtcttcatac 92040

gctcatgatt gagtgccttt tcgataattt caatcttgcg cgtcaggtaa tcggcaaagt 92100

tttcatccag cgtatgacgc gcaacaatgt agtgaatatc cacacattcg gcttcctgac 92160

caatgcggtg gagacgatct tccgcctgca ggatattgcc gggtacccag tccaattcca 92220

caaacacggc ggtcttagca cgcgtcagcg taatgccgac accagccgcc agaatgctgc 92280

agagcaccac gtccacctta ccactctgaa aatcctccac cgccttttga cgctgcacca 92340

cattttcctc gccggtaatg cgggcgtagg taataccttt agcttcaagc accttctgaa 92400

tgatctcgaa cacatcatga tggtgtgcaa acacaaccaa cccgtccact tcttcctctt 92460

tcacaagaga aacaatatag tcagcagcga acggggcttt gtgaatggca taaaagcgcc 92520

gcatttctgc aacgcgctca aacataacct tcattttttc atcaaactcc gccattgcct 92580

cagccagatc agcgctttca accccaaccc gctcaaactc gcggagaacg gaaatataat 92640

ttttgagatt ctggagatct tcagccagct tgaaaatttc ttcttcagca aacatcttat 92700

taagttttac aggaacgatt ttacggcttt tcggcggaag ctccttgagc acatcttttt 92760

tcaagcgacg aatcatgata gtggagcgaa gctttccctg aagttcttca aggttacttg 92820

caccacgaaa atcccaacca tacccattat agtaagcgtt gcaataccgc ttggcgtagc 92880

cccagaaatt accaaacacc ttcggagccg ccatctcaag aatgggataa agctcaatcg 92940

gtctattgac gataggagta ccggtaagaa agagcacctt cccgccctgt tctatggaag 93000

atttgacaat agattttaca aacccggagc gcttcgtctt cgggtttttg atataatggc 93060

attcgtctac gatcacaaga tcgtaagcat aatcctcttc cgaaatgcgg tggagaatgt 93120

cataattgat aatgtaaatg gtgtttttca gagaaaaatc gacttcattg ccgttaacca 93180

caataatttc tttttcgtga accacccagc gcttcaattc ccgctcccag ttgtacttca 93240

gagaagcggg acacactacc agcacgcgat cggggttcat tacattgata accccggcgc 93300

tctgaattgt ttttccggta cccatttcgt ctgcaatgag agcacccgga tattctttaa 93360

aaacttcggt aacaaaatgc acccccgcct tctgaaatgg gaaataatca tatccggtag 93420

gtgcaggtac ggcaaaatcg ctgctggtga cgctgctgag ctcgagcttg tgattttttt 93480

cttccaggag aaggttgtac tgctgagcag ccttttcgtc gaaataacct ttcagtttac 93540

tcgcataatc gagaattgtc gtataccata ccctcttatc cggatcccac ttccacccgg 93600

catttttggg gatcagacgt tcttcgtagg ttcctttcca ctcgaaccgg ttgttgtaag 93660

taacgtagcc catgaccgcc ctgtctttgg ctgtcaatct gctgataata tacgacactg 93720

aacaagaaaa gtcaacccct tgacagaaat ttcaattaga agggaaacga aagttgaaca 93780

aacaggtgat tgaaatgctt ccgatagcgc gtcggaagat caaaggtgtc gtggataaac 93840

ttttcaaatt catctttttc accctctaaa acatcatcaa gccatagtct tcgacgttca 93900

aggctcccaa taatcgcctc aatcggatat gcttctataa aagcattacc gggataatca 93960

tctacaacac tcctcacaac ttcttcaatg tttgttgtat ctatcaatcc cctttccgta 94020

taatacacta tatgtggttc ttcgtttgat ccgtaatctg attctaagta tactataact 94080

tcatattcta ctatatcttt aacatactcg ataatacttt ctattccact ttcaaccatt 94140

tcctctactt tctcccccca ctcttcatca aaatgatcta aaatatcatc cgagttgatt 94200

attttttcta taagatcata gtttacattt tcaggtttaa ttgtgctgta aaaatattca 94260

aaacagccgg ttgtcgacat atttttataa agagaagcaa ctacatcggg atatgcttcg 94320

tgttccgccc atttaccaat atgttgtttg aaaagaaaat aggcgatacg ataagaacct 94380

ctgttggctc tccttttttc tatatcttct ggcaactcta tattaagata ttcatgaagg 94440

tctttaatac cctccgcttc ccccatatga tcaattgcga tatctacaaa ttgtcttatg 94500

agatcgacaa ccaccgaaag attgatatat tcctcgaatt tattcttctg ataaagcaca 94560

aatacctgca gggtttcagc gggaatataa acagtatcat aattataagc gaggacgctc 94620

cttacactgt ctaaagccat attaatataa tattcgattg catcttctga aggtgcaaga 94680

ttttctacca gatggggata tttttcagca atcacatcca gcatccgcgc cgcataagta 94740

gcatagggtt cttcgtcaat cggtaccatt gtattatcag gaaggtgaaa ttcctttccc 94800

ttaccaaatg tagcgattgc gtaaacaagt ccgtcatacg gattgctact atcggcttcg 94860

aaatctattc ccggtttgat cgccgaagga tgaaataccc ccacgaacaa gggataataa 94920

tagttgaaat gttgatcgcc aagtcccaca cacacatgaa tatgattacc aatcatcccg 94980

agaatacgtc tgttttccac cacattttgg gggtgatata tgatcataga attgtcttcg 95040

tagataatca aatccgcata ttctgtgtgc ataagctgac gaaacttctc ccacaatgcc 95100

agataagaag cccccacctc ttccactttt ccggcgcgtt gatatgcccc aacgactttt 95160

ccgggatcga gaagctgaag gttatccgta agatcaaatt ccctcaaaac ggagggttgg 95220

tgtcgcaccg aaaaatacca gcgaaatggc tcgatgtaaa gagggagatc gatcggatcg 95280

attttgtcgc tcatcaccat acgataaaaa tattcaacca gcgcatttgt cgagataagg 95340

ttatattcgg gattgttgcg aagcggctca aaaatagact gagcaacttt gtgaagaata 95400

tttccaaaaa ataaaatacg ctcccccgga tcacggggaa cttctccaag atttaattgc 95460

tgagccagaa acctgagttt gttttcggga agttttgcaa gtagttcttt acccctacgg 95520

gaccccggag caggaaaagt aaacgccatt tttttatttt aaataactac gccccaaaat 95580

ccacataaag atagcaaatt ttccagctat cctccatcga gatagtatat tttttatccc 95640

cctctttttt aatctgataa tcttccttac cgacataatg taaaaattgc cttataagtt 95700

gccacaacct atcatattcc tccgtttcat cagtgcaagc cagcttgtac tgataatcaa 95760

cgaaggacat atcgtttatt tcatcataaa aattgtcatt gccccccaca atgataactt 95820

ctggatcaaa tacaacccat tcgataaaat caagcataaa ctggcttaat tccggatttt 95880

taagaatata acgccagttc cagcgcgatt catgatcaca tcgatcaagc ctttctatca 95940

ccttataatc ttcattatat ctggcaagta gaaaacgtct catttcggca acgttcatat 96000

cgtagctcag attatctgaa atatcgttca acatctcccg aagtgcgtct ataaagagac 96060

gcttgatagg ctcgcgttca aacatcaatt ctacaaactt cacaaccaca caatccagtt 96120

ctctatgatt tttcagataa gcgtcaatgt atatatccga cgccgcgttg gcaatcagat 96180

agcacatctt agccagcggc gttttgcaga caaaaaattc ccacccgaaa tcgcaagggt 96240

aaaaatcctc cttcacctta tcaggataac ggctgataag gatggagtgg gaagacgatg 96300

aatttgtgga aagaccgaaa cgaatgaatg ctttcatgac ttcctccttt gtttgtcaat 96360

ggttacatag acaacgtaaa aaacaacggt aagaataaaa agaagtaaaa actttatgtt 96420

caaccagaag ggattctctc ctcttagcac cagcgctgca gggtttctca agtataatga 96480

aagataaacc aaatacagcg caagcgccag cgaaatagag cctatcagta ttttgaacac 96540

tttcatagtt ttttccagat gttgagaaaa gttaccggat cgaacagttt ttccctcgac 96600

accctgaaac ccttttcttt caaataggat cccggagcaa caagtgcttc cggctcactc 96660

atgtcgatgt agcaggaaaa aagtccttcc tgatcggtag tgctatgtgg aaattctctt 96720

ttgaacaccg ggtaagtttt aacaaaaagg gaatccaccg aaatggtgag ttctttcata 96780

aaatacttca ccgcttccag tgtcttgttt tctggaattg gtatgttatt ataagtttct 96840

cccctcccca ctttcttaaa accaagtagc agaagatggc tcccctctac ctgagaaagc 96900

atttgcatca tttcaatggt ttcttcaaag ggaacgctcc cccatacgtg ctgagccacc 96960

agttgcacat tggggggctt ctgattcaga agatcgatat acgactccac cgatttcaaa 97020

ccatgcacgc tgaaacctat cccaaaaagc cgattcggaa aataatgccg gtagaacttc 97080

ataagctttc gggcaaacga agcattgaag gtggttacgt taacataacc ccggctgaac 97140

gttttgacaa tgcgatataa ctcttccaga aatctcccct tccagaaaaa gcaggggtct 97200

ccacccccta tgctgagttc gtaggtaccc atttcgttta acattcgtgc gaaccggatc 97260

atgtcacccg gatcacactc tgatccctcc ggggtggagt tttcataaca gaaagcacac 97320

ccaaaattac acacgttgga gggtttgaca tcaacgatat gcggcacctg agtcttaaac 97380

atgattacct ctgagttttg ttttcggtgc gtatgttttc cacaaaaact acataggctg 97440

aaaatacacc aagaataaaa atctgagcaa accccacaac ccccgttttt ggatttactt 97500

ccgcttttac ttcaaaaacg atacatatga ttcaaaggtc tttgattttc ggaatttctt 97560

cacaaactgc tcaagggctt cgtaaacgtc ggggcgaacc aagttcttct ccttcgtgaa 97620

caccacccgc cttgactccc agtcaacccc gaagttaaaa aagttattaa ggctgacaca 97680

aagcgaagtg aggggaaact catatatttt tacaatttcc ccatttctgt ctataagcac 97740

cgaataatat cctctaaaag cgtcgcacag gttgcgcaca gtctccagaa aatccgaaac 97800

cggcgcaaag tcttcaagca catagcaggt tagttgaacg gctttttctt cattcaggtg 97860

cgttacggaa tacattaccg gcttgactac catacttcct ccgttttttt gaccggaaaa 97920

ccgaatcaaa acaccagagt tccattccac acaatactaa ttaccagtat ttaattccct 97980

gttatttcac ataccctctg gatcattctg ttttctttct tatatattcc attgtcagtt 98040

gaaaccaaac agatgagcca tgccgaactt cattacaaac atcaggaatt cccgttttaa 98100

ggaagttctg accgaaatgt accattgcca tcacgaaagc gagtaccacc ttgagggaaa 98160

tgttttaaat cacacgctta tggtattgca ggtggtagat aagataaccg ctgatcaccg 98220

ggagcaaact aatctatcct taaccgccct tcttcatgat agtgggaaac cctatacccg 98280

tgttgtcgaa aggggaagag taatgttccc cggtcatgaa ggggtgtcta cgtatatcgc 98340

tcctcttctg ctgtgtgaag tattgaggga ttccctcatc acaccaaaag acgccattca 98400

aatcctttac ggcgtcaatt accatatgtt gcactggaaa aatccaaacc tttttatgcg 98460

gcttttcacc gaaatggtta attatacctg tttatataac ttcttgaaaa aattcaatca 98520

gtgtgatcta aagggtaggg tttctacaaa accccaaaag caggaattcc ccgtaatcca 98580

ttattttgag aataccccga tcggtactgt tgagcgccat gtttatttta tgatcggggt 98640

tccggggagt ggaaagagca cgtttcttca gaaagttgga gagggggcga ttgtatcccg 98700

tgatgaaatc atgatggaat acgccgctga aatagggatc acaggagact acaatactgt 98760

tttccgggag attcacaaca accctatgca taaaaccaag gtcaacaacc gctacatgaa 98820

cgctttccgt aaggcggttg aagagaatga aaaggtattt gtagacgcaa ccaacatgag 98880

ttataagagc cggagacgtt tttacaatgc gcttcggcgg gatattgcgg aaaccgtggg 98940

ttaccattat atcgtaatgc ttcccgatta ttttacgtgc attgaacgcg ccgaaaatcg 99000

ggaaggaaag tcgatttcaa gggaagtggt aaccgatatt gcgcggagtc tgcttcttcc 99060

gtgcagggaa catcccaaca gcattgatac gacaatttat atgtctgatg ggcatgatga 99120

acatgtgttg agagtagctt ggtagttttt aagattcgac gatgctcccc ctgctcaagc 99180

ggggggattt tttatttaat caaaaagtgg aacctttaga gaaactactt gccgttctca 99240

aaaagcttga agcgtttgag gaatatcttt caaagataga tcttggaacg ctggatcagg 99300

tgattacccg gcttagaaag ctccgggaat ccaacgaaaa actgtacaaa gactatcttg 99360

aagaacttga aaagcttttc agcaccaatc aggaaacgct cgaaaagctg gtagacgccc 99420

tttcggagtt tacggaagag gaaaaggaaa aacttgaaaa tttccttgag acgcaccaga 99480

aagacgccgc acgacttctt ggatatattg acgtttttga agcgtcgtgg aaacacatga 99540

gcgccgaaca acgggcggca tttgaatcct ttatcgacag actcagagaa cttcgtagaa 99600

acctcaatct cgatcgattc aagacggaaa cagcattcga tgttttcgac aaagcacgaa 99660

gagaccttgg ggtgccttat gaatatatca atcggtttgc attagacttt atcagatttc 99720

gccagcgatc agaaattttc ttcaaacaga tcatggcatt tttcacctat gaaagggtga 99780

caaggtatac cgcttatgga atggcaatta atctggtaca gggggcgctt gaacgctaca 99840

ttgaaactac tgatgaagtg atcagagtta ccggtattta caaccggctg cttagggatc 99900

aggcgcttca gttttaccgc gcaaatattg atctgagacg cttcggtgtt cagctccggg 99960

atactacccg ctttattgcc gaattttatg catttacgcg cacgcgcgat ccgttcgcgt 100020

tgatagctca gacagcagcg ggtgctggag acaacatcga cggattcatg cgtcagatga 100080

ttctcttgaa tcagcgcctg aatattgaca gccgcacgct aacacgtaac atgctacttg 100140

cagctaccac gctggaagat aatatcatgc aacatattca gcttatcact gcttttgcaa 100200

atgaagcaaa tttgagcgct accgaactgg tcagcgatct tgttgaaagt tattcagaat 100260

ttgtcgtgct gcttggaagc ggggcgcgtc agatcacgca aactcagatt gcactggcgc 100320

ggtggaatat gtcgctcaga gacggcatga atattctgaa aggtctctat caatctcagg 100380

aatcggtgat cgactcgctc attcagattc agattctctc gcgccagccg gttgatttcg 100440

aacgcttctt tggagccatg ctcaccggcg acattgaagg aatcgtcgat cagcttgcgg 100500

aaatggcaat gcagatgcgg ggcatgatgg atgaactccc catttatcgt atgcagtttg 100560

agcgggcact tgaagggttg ggcttaacct ccgagcagat cgcaacgatt cttggaaagt 100620

ccagagagca gcttacaggg ttcggcacta tcgtggaaga tttccgccgg aagctttcac 100680

ctgaaatgct tatccagact tttgatgaac ttctgagacc caacgaatgg gaagaattga 100740

agaatgcggt ggatgcattc ttcgagacgt ttatgcttta cggcgctgaa ctcattcgca 100800

acatgattcc ggtgcttaga attctgacac agggaatgca attgatgttc aagtggtctc 100860

aggctatgac cgatcttatc gataaggttg gtagccttgg tggattgttg aaagacaacg 100920

ttcttggaga tttcttcaaa agcattttcg cgtttcttgg acccggtgcc gcgctttacg 100980

ctattgcgaa tatcggaaag cttggaactg cactcaagat gttatttgat ttaatcattt 101040

ccattcctcg ccgcattggg ggaggggttg taaaccgtat tggttccttt ttcagtcgtc 101100

ttggagatgt gttcaagaag ttcttcggta gccgggaaat gaaacaggtt gcggaggatg 101160

caacttcaag aagaggaatt ctccgtcgaa tcaccggtgg agtcaaagat tttaccaaaa 101220

acctctttca aagcttttcg cttggatcga tcgttcgttt tacagcagcg gtgggggtgc 101280

tggttggtgg tatttatctt ttcggaaaag ctgtgaaatc acttcaggga atcgactggg 101340

gtgagacttc gaaaggattg cttgccttct ttggagcgct taccactacg gtagggttga 101400

tcagtcttgg tggtcttctt tcacttcccg cacttcttac cggtcttgca gcttccatag 101460

gcgctattgc cgtggtggcg ggcggtctct atctcaccgg tgaagctatg ggagtgtttg 101520

ccagcaacct tcagagactt gcttccacgc tggaaaccta ccccaatctg acttccggta 101580

tattccgtct ggctggagca cttggtacgc ttggtgccgt cggtacgatt gctgctccgg 101640

gcatgctggt tggagctatt accgaagccg taagtgcggc gatcaaaccc gatgtggctg 101700

taaaagccat tatcgatcca gatgtaatta ccgccggaga aaaactgatc gcaaacaaac 101760

ttgaccggat tattgcgctg cttacggaaa tgcaaaatag aacggagcca agagtggtta 101820

cgctgaataa gccggaaaag ccggttgaaa aaccaatctt cagcacattt aacttttaat 101880

cttcatcctt ttcttctccc tttttccaga ccggatgata ccagtcgttt tctttcatca 101940

ggttgatgta aaatacatat ttataatttt caaatttttc attcatgcga agcttataga 102000

gataatcatc tttgaacttt tggataggta ttcttcctcc aacataaagc agaccacctt 102060

ttcccaccac aaagaacata tcttcgggga aacgtttgat ctgaagcact tcgatcacat 102120

cgtcaatggt aaaaaacttg tatgcggttt ctttggatgc gttgtaaatg taataatgat 102180

gcgcaacgtt ggattttctg ttatccgtaa tcatagaagt ttctgcttaa gtagctaaat 102240

atcactatta aataaccgga tttgatattt aaagaaaaag atgaaattaa ccgatctcag 102300

aaataaagtt acaaacgcat ataaccagat ttccaagcag aaccgcgagt taatcgccgc 102360

caaacttcgt aaagactcca gtgccaccat ttacttcggg gctgctgtcg aaaaacttga 102420

cgacgctacg atcaaagaac gtatgatcga cgtttttgcc acgatcattg ctcaggcgta 102480

tgatcgcgcg atttccttgc gcaaaggaaa accgacacat ctaccctccc ctcagtcaat 102540

ggtacttacg ctggcaagat tttacgtgga aaatgaagac attacgctca gcaaacttaa 102600

cgaaatttcc attgcgctgg gctggtatat cgcgctggta aacgaaccga atttgcttca 102660

aaaatacaac ctccccaaac agatcacgga acttgagccg gagcagcttc tgcacactta 102720

caaccagatc gcaagatatt ccgacaccta tcaggtggaa ctggtaaatc gctataaaga 102780

aattatcgat ttcctgacgc aaaacggtga agagttctgg gaaaaagaat acggggttat 102840

tttcaaacct tcctcttacg aaatcaacgc caaagtgctt cagcttgcct ccgatcgtct 102900

ttttatctgc accgcactta accctatttt ccacgacacc tattatcctt actatgtgct 102960

tgtagtcaac ccggcttaca agggagacgg caatgttcac tatatcaaag acggcgtcaa 103020

gggatattca ggtatggagt tttatcttgc caccttctcc gacaaacacc cctaccagaa 103080

gggattattt gctcagtttc gtagccagta taatatcgcc acccctctca gctttatcga 103140

aagcagactg tatctggggg attttatgga gtttttgtgg aaacgtaaag atcttcagcc 103200

gcatatctct aaactcataa acctttacaa acaacacccg gcttatcttt tcgatgagaa 103260

cgcaatgaaa aggtttgtgg aaaatgagct tttcgatttc aaaaatatca acgactcacc 103320

cggcgcacgc gaagccgtag cttattttta ttccaagatc gacaaccgtt cttttatcga 103380

ggggctgact ccgctgatcg gagccgccgt tgaaacggtt atggaatcgg gagaagaccc 103440

caattacaaa aatgtacttc cggtgctggt agagcttatg gtcaaaaaca actacgctat 103500

gaaaaagatt gaagaagctg taatcgaagc ggtgcataga aaagcggaaa acattctcaa 103560

attcaccccg gaagaccata tcagatatat ggcaattcat ttcgctcata aaaatattcc 103620

ttcaaattct gaagaagaag gaagagattt tgccgaacag atttattata acataatcag 103680

acctcagatt acaggcacct caccgtatgc tattatgttt aaacgtttta tatattcaat 103740

cattcttgcc gaaatgaaag gtattctcaa aaacaagata aatcaggtgg ttaaagaaat 103800

ggaagaagaa ttcgggtttg gagacatttc ccttgccgat ttcgactggg ggggcggtga 103860

agaagacgaa gattcgttcg aaatggaact ttaactggaa gtgtacaccg tttctccgac 103920

gatatagaga cgctgtccac gagatgttct tgaaacctga aaggtggcat tgtaaatgtc 103980

gtgatcttca accacttctt caagcttttt cttaatatct cgataaagaa atgacttttc 104040

atccacgtag aagaagtaca tccacgtctg atactcttct ccccccattt tttccgaaga 104100

gtgatcttcc tgatacaggt gaaatccgta atcctttaaa ataggtatat gttttttgat 104160

ggcgtcggat gaagcctcgc ttccgtcata aaataccttg agaatcatat tctccattcc 104220

ggtggaagga atgacaactt tcccttcttc cgtatacgca ccctgaatgg caataagcag 104280

cagccccgga gatatttcat caaagaactg gtaggtatcc tcgacggcgc gaatatcggt 104340

aatcaatgta atcttggttt tacctttttt gacaaggttg cgaagggcaa aaatggaaag 104400

gaaaacaacc gcttcgagaa cctgatccgg agacaaatct tccgatcttc ttatgcttaa 104460

gaaatactcc cggtggtagt ctctcagacg aaatctcaga tcttcctctt tcctcaaaac 104520

cctcgcaatg cgacggtctg tttcaacaat gaagtcggta tgcgttattt ttttctccca 104580

ttctccgtcg aaaaattcta catcgtaaac aataaaacct atcgtgttgt agtggtagtt 104640

gatttctact tcgattcccc atgaactatc aggcgcacga aacagaaagt ttcgcggggt 104700

aagcttccac ttctccagaa ccgcgctttg aaaattgacg aagtttgtaa tgattttcct 104760

gagtgcattc ctcagttcac tcataaatag cgataaagag ttttctcaac cgtttccaat 104820

atctgaagcg actgtttggt tccaaatcga gattcctgaa gcactcttgc actttgaaaa 104880

gaaggaacgg ctacaacatc tatcgctgtg ataaagaagt cgtcaacaat ttctacccgt 104940

ttttgctggc ggtaacctac tttggtttta ccgctcccac gaagggaaaa cccgaaattg 105000

ataccgtttt caagaagcga tttgaccaga tttccgtaag gagttgggag aatgcggaat 105060

tttccgtaca ctttatttcc ttccatccat acgtctaccc actgcacggc aaggcgctca 105120

agcgacacga acccgattcg aaaatcgttc tggtaggggt gatccagctc gccgtacatc 105180

tgaccctttt caatctcctg cttcatacgc tccactgctt tttttacggc ttccggcgtg 105240

tagagtgtac cattgtcgga aatgacgtcg gcttccataa tcagagccgt ataagtttta 105300

tcgttaactt ccatagcggt tattcttcag ttttattgtt ttcttcttcc tttttgtctt 105360

cggcgtacag gaaaacggct tccaccgaag gaagcatttc gcgaagccgc gcaagcacat 105420

cggtaagcgc aaccagcttg gaaacacttc cgcgagaagc ttcgatcgtg ttgataagct 105480

cgcgaatgta attgcgatag ttttcatcca gcgtaatctt gtcaatgatc tcttcgatca 105540

tttcacacaa ttcctcgctc acgcgggcaa tatccttttc cagttcttcc gtgatttttt 105600

cggcttcttt caccctcttt tcttcgggga tttcataact attctgatcg ttttcctcct 105660

ccattaacac cttttcctct tcatctttct tgtcctgctt gacatcttta cggatttttt 105720

ccacatcacg gctggagtaa cctaccggcg cgtcataccc cgcaatgtcg ccggtggtgg 105780

tcatctcctc gatctgtttc aacgccgatt cataaaggtg cgagaggatt gccgccactt 105840

tagcaggttt ccttgcgctc aggaaaagct cagccacacc agccgcgcga taaatgcggg 105900

gatcgatacg ggtttcgtaa acttttgaaa gctgtttttc tccaatgatc ttttccagcg 105960

cttcatggaa accgttgtac tggcgctttt tgcggtattc gtggacgaaa tagggaaccc 106020

tttcatattc ctgatctatg caggcttcga caattttggt aatgtaataa acatcgtcag 106080

attccacgaa attcatcaat tcacttgcgg aagccgactc cagcaatttc ttgtcttccg 106140

aagaagcctt catgaactgg aatagaagga ttatatcctt ctgcttcata acaacctttt 106200

ttttcttaaa taaataaaat cgaaggagaa ttaaacaact acggtattat aaccccatcc 106260

accgatatag ttgtaattgt ggctggtttt atatacgggt aacagtcatg aaatactctg 106320

tttctgatgt ggcgaatttg ttcttgtgtc atatcacccg gtattagagt ggaattcaga 106380

taggctgcat ctttagttat tgctatgtga tacaaaaggg gcgccatttc actgtaagtg 106440

tgtgtatctc taaatataag tctattattc aaataaaatg aaacagtaag atcattacta 106500

agagggtcca tttcataatg aaattcatgg aacacaaaat aagaccggtt tggattataa 106560

aatccccatt cagatactgt tatactatga gttactttct ttgttaaaaa tggggtaact 106620

atagtcgaat aagttactcg aatacccaga ttcccggaag ataatgtaga ataatatatt 106680

gaaataatat tttcaccact taaaattcta cctatgtaac taacatctac attgaacacc 106740

gaagagtcat ctgcataacc gtcaagaaat attgtctgaa ataaatggaa tttttctttt 106800

ttaccattta taaaaagttc gatattgttt acagttcccc aataatccaa atcgtaaaaa 106860

agactaaaag aataattggg gaaatgactc tgatacgccg cttgactacc accagcatag 106920

ctatctgcaa tataaaattg attccatcta cttatagctc cataattgat atttgccctg 106980

gcaataaaag cattatgacc aaaatcatag aaaaaagaag aattaaaaaa ctttgttcta 107040

actgattggg taccatttat tccatctgta tattcggtta ctatataata gcccgaaccc 107100

gtttcaatag tggggtgatc tgttttgatt aaataatata catctctgac gctcatactc 107160

cctttatatc ccccagctac cagatattga ttggaaactg aaaccgtcaa ccagtcgggt 107220

aaaaagggtg taacatcaac accatttata gccgaaacat aagtgttcaa gacactgatg 107280

ttatcttgat ccgggtcaaa taacgaaaat gaaatggtaa catagccgtt tgcatccggg 107340

gtatataaaa tctggtatgc cataacttaa atgtttttta ttaaatatta caagctgtaa 107400

atgaagactg cagccgcaac cgaagaagta aacctgtcaa gtctgaacaa ttcgtaaata 107460

aatttaatat tatcacttcc ggcaactccg ctgtatgaaa acaccccctg tctgcgtgtg 107520

atgatattgt cggtaagcat ataaacatac atgctgttgg taacataagg agggaaacca 107580

tctggattga tccaattgac aacatagcta tgggtttctc ccggagcaat tgatgaagag 107640

ggataagtgt acaccgtaga gttagtaaca aactcaaaat aagatgtact gttatacgta 107700

tcgggtgtgg aaccgctcaa tgtataaaat agagaaaaag tgttgttaat atgagacata 107760

attgaaaggg taaacgaaaa tgtatacggt tgtgtcgaaa gagtccccat taaagacgga 107820

taatcaacag atcgactgct cagtatgttg aatgacttac cttcatataa cagcatattg 107880

tacttatact tatgataata atattttcga atcatagaga ctgtaggagc cgggagagaa 107940

gtactaaaaa cagcgatttc gtaaaattta aaagcagggt ctccagcatg atctctgata 108000

agcaatctgt taatatctcg ccttgtgtct gtattatact tttcaccaac aaaaactccg 108060

ttgatataaa atgatgttgt agaattgtta tgagacactt caaaaagaag aggataagat 108120

aatacatctg agtaagaaaa ctccagacca tagccactac acgtatatgc ggtgctccca 108180

acagaagaac cgctatcaag actgaaaagc actacattta gtttattgtt gttgtttaca 108240

aaccctgttc ctataaagcg gttgttgtct gtactggtat ttaacatcat cacatccata 108300

aactgggaaa tgctatgtag cattgcagga gcaaaaacca taaaaacatg gaatggtgaa 108360

tctgggttat tgtctaacag attaacacta aatgtgttgt tataattata actatttata 108420

tggctggcaa gataagaata gcctttgtcc cagtaataat gccaaccttg ccctgttgaa 108480

tataaagata catggcgatt acccgttaaa gacggtaaaa cagaaatggt tggggtatat 108540

ccactttgtg ttatagttat atactcgaca ctccaaattt cacttaaact actcaaagaa 108600

acaatttcaa aattggaagt aaaaagagac agattataaa actttacgtt attatcaaaa 108660

tacacataaa cacccatatc atacacactt tcaagggaaa aagacgggtg tgtatggtca 108720

aaagatattg taacatcaat gacacttctg gtgccgatgt aatataaaga actggtaaca 108780

accgtaaacc agggcggtgt aacagaaaaa gatatattat tttctttcaa tatggaagca 108840

cttactgaaa agggtattcc ataatcatct ttcactgaaa aggtgataat gatggagtta 108900

ctgcttatta tgtaatctct gttcatctca ttctttaaaa tttaaacctt aaataatcaa 108960

gatcaacttc gggggttgtg gttggataac ttttattggc tgctttaagc tcccatttaa 109020

acccggcatt agaaaatggt ggaacttgag aatatgtatc aaacggataa tttgccgcct 109080

tgagttccca tttaaacccg gcattagaaa atggtggaac ttgagaatat gtatcaaacg 109140

gataatttgc cgccttgagt tcccatttaa acccggcatt agaaaatggt ggaacttgag 109200

aatatgtatc atatggtatt tcagatgata caagttgggt gttaagagca gcggaagggg 109260

ttaaccctaa actctggaag gaatttttca tagaagaatt gctattagtc agataaacgt 109320

tactaacagg cacataattt accaccggag caatctgtct gacaaatttt gataccgctc 109380

caataaacga cacgcttaca ctcgatttgg gagatttgaa aagtccccat gcacttccgg 109440

ttaccgctga aaagaaaagg agattgaccg gctcattcca gacgttttcc caatcgactt 109500

ccagcgcacc catttgagga gatgagtaga aagtcagatt gttacccgta cttttgagaa 109560

caacgtttgc tccggatgac gtcagataga aatactgagt agatgtagag acatatactg 109620

agaagtaaga aagataactt accgtcagaa atcctgaatt aattgggttg aagaaatagg 109680

gtgatgtggt tgtataactg gcatatttca aataaggtgt attatccgtg taatacagaa 109740

cacttgtcga ataattcaaa tccatgaaaa tgcttgccgt tccgaaaaag tcggagaagg 109800

tgactaaata gggtgatttc cgaaccatgt atgttccatt atcagccgaa acgataaaaa 109860

cagattttgt tatatcgtaa agtaatgcgt tgaatgtggt gctaccctga ttggaaaatg 109920

ttatataatc ttcaatatat ccgccgccaa ggaaaagacg tttgattgag acggtttcgg 109980

tgctggatgt cgtgtaataa tccaaccaga acacatcata tccccatgca gctaccccac 110040

cgtattgaat gctggtggtg gtaacctgtt tataacttcc actggaatcc aggagtccca 110100

cttctccgga agatccatcg tgcagattga gaaagagtgc gggagattga tcgtaaaaga 110160

atccaagcga tacgattata tccgaagggg tagtaatatc cgggaagtaa agagagatat 110220

tcgggtctgt agttgtaatg ttcgggaaat acagttctat attaacgtcg gatgtagtaa 110280

tcggaggcgg ttcacttggg gatgggggcg gaggaggaac atacgaataa gaggggatca 110340

gaatcttctg cacgaaaaca taagcttcat ccagcttgat cggttgagaa aacttcgata 110400

caaacaccac gtccccattc tgattcattc catagattcc gctgacataa ggagaaaccc 110460

ccggaacagc cgtgggattg gtggtaaagt ttttggctac aaattcggca acgagaagct 110520

tcagaggctg caattcataa agcgtaaggg taaagaaaag cggggaaata gccggtactt 110580

tctttcccac aaccacaaac gattcatttc gaacaaggat aaaatccggg tgatcataat 110640

aactgtcatt cacaagcgag ataggatttc ctccatacgt aatggaatgt atgtgatagt 110700

actgtcgctt gattctcaca atttcaaaag tgagcgcatc aaaatcgata ttcagcttac 110760

gaaaaagatc gataaaaagc gcacgaatct gagctttgag ttgatcatcc ggggcaattt 110820

ccagttttat attatcattt tcgtagctac cgggagaagg gaaaccaaca acttcggtga 110880

atacttttat atcggtttta taaaaatcct tcgctctcat tttatacttg atgttcttct 110940

ctattaaata agaaaagttt attcaggggc tacctttgat aatattccct gtacacccag 111000

ccggtaaacc caaggtccag aagtttggga atatcccctt ctcttcccca ctgctttttc 111060

tgaaatacat cccccacgtt cagatcaaaa ctcataaccg gatcctgtaa atcttcaatg 111120

taacggctgg cgaaaccgtt atctctgatc ctcaaaattt cttcatcggt tatctgatca 111180

tgaggaagat cataaagctc tatcagctta cgacaggatt gaatatagcg gttatcttca 111240

taaaaattag gcggatgtgg gttaatccag ccggataaaa tatcggaata aaccttaccg 111300

gcaatcagtt cgtgagcttt gtttttcata tcgggttcga gaatatccag aagtatataa 111360

agctcttgat aggttttaac cggctcataa tacctgagta tggaagcgat cgccattctg 111420

gtttttgtgt tctcataaaa agcatggagt tccggtagaa tatactccgc cgaagaatgt 111480

cttattatat ccacttccgc catattctga gccataccct tttgattgta tgcaattttt 111540

ataacataag gagttccaac tatgcgataa accttacgag aagaaccacc tcctatatac 111600

tccacagaag gcaattcatc catcaaagct ttaagtgctc tgaaggaaag atgattgttc 111660

agcaactctt caaaatactc aaataaatcc tgatctaacg atatgttgta accgtaaaca 111720

attttctctt tcattacttc ttcttattgt ttttctccgt tcgcttaaga taagcgcgag 111780

ccgatttgaa aacccgttta ttactggtat ttgctgcaaa attgatcatt ttcatagccc 111840

gatctctacc cacttttctg ataagggcac gcgccagcga ttcacccgac ttgtacacat 111900

catcaatatc tttgtctttg gggattccaa gcacttcatg cattttcccg cgcttgactt 111960

taccgctttt gaatgcttat tgaatccact tttcttcctt tttagcctca gccagtttac 112020

gtttcttgag ttccttgata tacttcagag cgcggtcata aatattgtgt tcagggttga 112080

cgttggcggc aaaaaccaac atccccacgg cttctttgta cgaaactttc ttcaggagat 112140

cacgcaccaa tttgcggtga tctttgtaat gatcgacaat atcttcatct tcggggattc 112200

caagcacttc cttcatgtgc ccggcttcac gcttgacctt gctcacccag tctttttccc 112260

gcgcttctgc aacggtttcc ccaccttcat ccagaagtgc aatagcttcc gtatagaaga 112320

aagaatcccc ctccgtttct tccagaacgc gcaacgcttc tttcagaagc tccttgtgtt 112380

caatatgcat acgctttgcc attttcaaca aatctttgac aaaagaccgg gcatcataac 112440

cgtaatactt ggcgacagaa acgacggaag gaactccaag atacttacgc aacttcattg 112500

ctatgcgttc agccgttgcc tctggattac ccatcttttg aatgagttct tcgcgggtga 112560

cattttcggt cagcagtttc tggcgaaatt cgttaagctt ggttctggtc tcctgcaaaa 112620

gccgcgcaac acggagaatt tcctttcggt tcatatctta ttctcctttt cttttaatta 112680

aagaaaaata aagactctat gaaaacagaa gacagaaaaa aacttgctca ggaaatcctc 112740

gacaaaatcg taaacaaagc catgcagctt gaaacgttga ttgacgatga atacaactat 112800

ctcaacagaa ccagtgtgct ggttgaagag gagagcaatc tgatgtcggc aaaggctcga 112860

atgcttgagc tacatattaa gattctcgac acgctgcaga aagtgtataa agatctgaaa 112920

gaagggattc aggaagaaga cgaaacggaa aagattctca tggagattat caatcagagc 112980

aaggctaacc tgtgaaaaca ggtagttcat tcaatttttt agctatattg attccctgag 113040

ctatcacctg atccatgttg taatagttat aagtagccag tctacccacc agtataatcc 113100

catggcactc cagttcgttc ttcatagaag ccgccttttc tctgtaggtt ttcttgttaa 113160

tcggataggc tttgaacgaa ttttcctgag gatgttgaga gggatactct atggtataaa 113220

ccctgtcaag attcagcctg gagtgatcga taacgcgggt aaagggttct ctatcagagg 113280

aaagatgaaa tccgatggat tcgagcgtac tccactcttt cagtttgcga agcacatagg 113340

gatcggaaga tataccttca agtttttctc tggtttcaat tctgagatga atgtaaggga 113400

gatgttcttc tttacctgtt actctctggt aaagcctatc aaggtccccg gtataaataa 113460

aagggttatt ttttatgtcg tttagatgat caagcgcgtc ttcggaataa actatattga 113520

ctaccggcac ataatttctg atataatcaa tcatccgtat aatcattttc cagtaaccat 113580

caaccgggag cgccaccatt ttatcgtcaa aataagagtg atatcttttc cagtcggtaa 113640

agaagggaac gcgggaagct accgttttta ccatctcttc atcccagtaa tctccccaca 113700

ccttttttga gtaaggggca taccagtttt catagacgaa agatttaagc ggttccggga 113760

gattgcctac cggaattttt ctgttaagaa gttcttcttc cagctcaatt tctccaagat 113820

acagccgcac ccagaaaaga gatgaaggaa taaatgaaca tatatcattt tcggtaacag 113880

cataggcatt gtaactgata gagtaaaagg aagagaatcg cgacacaaat ttgatcactt 113940

cgggggaatt ggtatgaaag atatgaaccc cgtatcggtg atattttttc ccccggtcaa 114000

aatcccagac gttcccaccg gggtggttgc gcttttcaaa aaaagtaatc tcttcaaatc 114060

tgaagccacg atcaaggaga gaaataacgg tgctgagtgc cgcaagacct gttcccccta 114120

caaacaaccg tttcataatt ttctgacctc cgggtctctt agcacttgag gaaacatacc 114180

ctgtacctgc tttccgacaa aataatccat gttgacgcgc cgaacggaga atatccgaga 114240

aggtctgtac atatgtgcgt gagataaata cggaagcgtg gcatatctcc acttgaacgc 114300

atgtgccaca tggattaaaa aagtttccgt gtgggttgga agataatcgt aatactttct 114360

cagagattcg agataatacc tgttaataac gtgccccccg tcaagatgca tgaaaacgcc 114420

gcgcttgtgc agtttgtttg aagtgaaata attgtagaca taatcggcat attcattaaa 114480

aagctttaca tcgaaataat cgagaaaatg ttcttctctg ataacaatct ctctccagtc 114540

tttttttgcg aaagtctcca cataacatgc ggcggcgtaa atgtaatatc cctcaggggt 114600

ttttaacctt tcatcggcaa gatgatcggg aagctcaatt cgctcatacg gatctttgaa 114660

aggtgtttcg ttttgatagg gaacaacccc gtaaggttct accatgttgg agcaaatcat 114720

aaaatattta tcgaaacacc cctcctcgaa tgctttatcc aaccctttca gatatgccgg 114780

gggaatataa acatcgtcgt gcacaaacac cccggcttct acaccaagaa gaccaagtgc 114840

gtcaataaat gcagcaaact gagagtactg aatttcatct acaagaaaaa cattaagttt 114900

gtgatgttcc agttgatttt taagccacga tctccaaact tctttatctt ttaccggttg 114960

aaggttgaaa tgctggagca atttataatc cgggtgaaag cgcatttccg gataaacaaa 115020

aatataaaaa taatcccgaa ggtgtgaaat gtgtgggtaa atatttttaa gccacacttc 115080

gggaatttcc ccgagcgtta tcattacaaa ggcgatttcc ccgcgataaa aagaagggtt 115140

cggggaagaa gaaatcttct caaccttcat tgttttccgc aattttaatt acaacccggt 115200

tttcttcaaa gttaagctcg aattcctttt ccgacgcatt gattccaagt tcttccagtt 115260

ccttttgaag ttcccccatg atcttcatgc gctcccgctt ggctttaagc gcatgctcga 115320

atacgttcac atcgccttca tcgacgattt ccaccagcat atcaaagaca agcaccgcca 115380

tttcaatgta ggcgttgcgg agttgcattt cacgaagtgc aagggatttg agctggtcaa 115440

ccttctcttt gtcttctacg acaatggtat tttcagagcg tgtaacggta ggttcaccca 115500

ctttaatgaa atctttccct ttcatggctt tttttgatga aaaaacgatc gggttcaaga 115560

aaggtttcag aaggtgttaa gcggatattc ttcagacgcc tgagcttccg aagccgcatc 115620

gtaatcgcca accgtaatat aaatatcctc aattccaaaa aattggggcg gatagcgaaa 115680

ttcataaagc gtaagttcag acggcgttac aacaatatca aatatccaca caccaccttc 115740

atcatttcca agaataatcg ctttgcagtt gatcttatcc gattcggtaa agaaaggttt 115800

gcttctgaga acaaatcttc tccctaccgc aacaaaaagg ttggtgccgc tttccgggta 115860

aaaatcgacg tcgttgtctt cagaatcaac gatggtaaac acattgggtt gaatataaag 115920

cgtataagat ttgttgactc cataagcggt ttgtggttcg atgataaagt tctgaggata 115980

ctgtgtttca tagaggatat ttacgtttac gatcatcggc atgaaatccc ttcgatcccc 116040

ttcatccgtt tcatacagcg taaccagatg aaatttgctg tcaaaaatat tccccacttc 116100

gcgaggttga cgaatgatag aaacagttgg ggagtataca ttataaacca cttcgtcatc 116160

tgaaagggcg aattttccca tcgtacgaag ataatcggca atggagattt tctggcgaat 116220

gagctttgca atcaaacgct gaccgtattc tgtaagagac gccgtaacaa gcatatcaga 116280

attccacctt cagtttaatc acgtattcat cttcgttggt cttacgaagc ggagaggaaa 116340

gtcttccaag cgccacaagc tgattgttct gatcatagat tccaacggtg gtaatataag 116400

taccctgatc aggatacaaa atgcgtccgg aagtgggatc gtagaatgtg ggattgagcg 116460

agtaattgaa ttcgccagcc tttacgcgac agaaaataac catagagtga atgttatcca 116520

ccattgaaag cgtcatgtca agaataaggt tggcgatgtt ttcatgaagt ttcgcaacgc 116580

caccgaccgg aggattgctg tcaatcggga atccggttgg atccagcatg taaagcgaag 116640

tgctgtatcc ccccgatcca accccaagcg aatgagagac aaaatcgccg catgcatcca 116700

gatcgatcag aagcagcgcc gactgaggga atacgattcc aaacaccttc tgagttatgg 116760

agtgggttac aggaaccgcc tttccactct gaagtgaacc cgacaccaga tagtagaacg 116820

gctgcacctg ggtgcggatc ggagtagcga ggttggtttc gccgctgttg tcaaccagag 116880

acagggttgc gcggtttgat ccgtcggtga aagacaggtt aatctggaaa ttaccaacat 116940

caattgtatc ggcaaaatta tggaaggaga ctaccatgaa gttcttaagt tcactgaatc 117000

cggcaccggg atttgcggga tcacggggaa cagtaataac atcagaagcc agattggttt 117060

tgaattgatt gataaaagcc agataatgct ttcgagtaat ttcattagtt ccaccgccat 117120

agttcccttt ggaagcaaac gccacggaaa actccggatc ggtggtaagc gatcctttga 117180

agatattcac atagtaatcg ttgtaatgat cgggttgcga agaataagtt acaaaatcgt 117240

ttcgtgcaat aactccgctt ttatcccaga accccggaac ggctacattt ctcgtgctgt 117300

acaccacgtc gtcaatttgc ttgaagacaa acccctgagg ctgcggagcc gtctcagctt 117360

ccgtagcgat gttgttgaca acgtttcgta tagtttcgag ctcttccgta gtgatagaca 117420

gattcgattg cagatagttc agaaatccct gcaaaatctg tcgcttggaa taatcggtaa 117480

ccgttccaag tagcgtggta atgtaggaaa taagttgctc tctcataatc ttatgtaatc 117540

agttttactt tcagttcagc ttgtgcacca ctttcgttgc ccctgataag cacaatggtt 117600

tcggtgttgg gcgtagccgt ttgcgccggt tcgatcacaa acttgcgccc ggaaatcgct 117660

ttatagtcgg ggttgcttgt cgggaagggg aacggcgcct gtgtcgacgg ttcagcaaca 117720

gaaatgttta gctgtttgct atcataaagc aatgaataac caagaatctt atcaagtgca 117780

accacaaact ttgtacttgg gatgaagaga tatcggcgaa ggttatctgt agaagtaacc 117840

ctgagcacga tttcactctg atccagaagc aaaatgggaa tttcgttgac aatgatattc 117900

ggatcgccta ccacactgaa aagatgatag cgcggcactt caaacggctt gggttctacc 117960

agcgaatagc tcagaatttg cggagggtta cccgcgcttg cagaaaacac atattcataa 118020

tcgattccgt cgtcagaaag tgcaaagtag gcaatatcga aactaccgga cgcaaacaac 118080

cttctaccgt atgccgtgag cgtggctacg gaatataccg tgttttctga tttggtgggg 118140

ataaacattt ttttctttaa ataaagtttt cagttaccca ctacaagttt taaaagctca 118200

accagtatcg aagggtctac aatagccagc gcaatgaagg gaaaaagtgg caaaatcaac 118260

ccgacaataa atccggtgag tagcaatttg atgaacagtt gttgttgatc ttttctgttc 118320

tgcaatgcat tgtcataagc gccctgcaat agatcacgat atttttcacc cacctccgtt 118380

ttatctttaa gagactcgat ttgaacgctc agtcgattca atatatcttc tatatcatca 118440

agtttttctc taatgttgtt tctatcctgt acaacggttc tgagcacatc tttaatatct 118500

ttaatcattt caatgatgtt cgatagaatg aaacgtatct gataatctct gtcaaactgt 118560

tcttcgttca tccctgtttt taaattaaat aaaaaagggg agacgacacg tagtacatct 118620

cccccataaa attatttttt atgcgaatta aggcgtgcgc ttttccagaa gatacatcgt 118680

aagaacatcg ccatttacag caagcagttt ggtaccttcc cggttgggga aaggattgat 118740

ccggttgaaa tcaatgcggc gcatttcctg acgactatcc ttttcaaaat ggtttctcag 118800

gaaattcaga gcatttagcg tataatacat gtcattttct ttccagtagt gcgcaatgat 118860

cttgcgtttg tggttcagca cgaaatcctt ttcgcggtgg aattccggaa cggaataaat 118920

gacattatcc accagcgagc agtaatcggc aagatcctga agatgagcat attcagttga 118980

aagaatatca ggaacctcgc tgggaatgta cgtgtcataa tccccgtaaa caattccccg 119040

gatattagcc gcattgtaag tcgaagactc gacaaaatgc gttttcaacc gcttgtctga 119100

gtaatccttg gaaaacagaa atatccggct tggattttca ggatcgtcga acattaaaag 119160

cttttcagcc ttaacaaacc actcatattc cgacttgaat accggcttga aatagaacac 119220

ggtgcggaat tgagtggaac gtcgagagcg tcttggtttt gccaacgtac ccatagtctt 119280

tctcctattt tttttttgtt tggttttaaa tacattctgt gtaacaataa aaattcataa 119340

aggtttcaaa gatttttaca atttcttatt taaagaaaaa tgcccgcaaa atcaagaaaa 119400

caacagagat atatattcta tctcagaaac aaatatggat caccggaaaa aacccccaag 119460

aaatacaaat ggatatggca caaagattgg gagaaactgg aggaagccaa acgtaaaaag 119520

aaaaagaaga aaagacgtaa aaataaacgc tcttacctga agccggattc ctattataag 119580

aaaccatacg gttattacgg aatctggtat taccattatg atgacggtgt ggatgatggg 119640

ggagatgcgg gtgatggtgg aagtggtgct ggtgtgggtg aagctaaagg tgcaaaacct 119700

gctaagaaat ctaaaaaaga agtgctccgc gatcttgagg tcaaactgca cgacttcaac 119760

aaggagttga aaaaactcct cgagaatctc ggattctaaa aaaagaaagc cggggaatca 119820

accccggcat tttttgtttc accaaggtaa atcgttatta tccgtctgac acgactcaat 119880

caattcctct tcttccggtt cttcttcttc ataactgtaa aaccatatat gaaagtaata 119940

tccccgccct tcttcccact ctcgcatttg ctgctcttcg aagacgtctt gcaaaaaacg 120000

ctttgtcaaa ctcatggctc cctcctattt ttggttgaca aatcgattct actggtaata 120060

tacgcattga tcagagaaaa gtcaaatgaa gaatctgtta aacagagata tatccgcact 120120

cagcggaagt gtagatgtca acctcagata caatcttata aagttttttc attagcacca 120180

caaagtcttc ttccggaagc tctaatagca attcctcatt atatttgaga aggggaagca 120240

tagctttact tccgctaccc accgaataat agggatcacg aatgaacatt gtcgtgaaat 120300

tgtcggatac cacaaacacc ccgtgctgac tgattcccat aattttcccg ttcatatccc 120360

cattatcatt cagaagattc aaccccttca gatgatctct ccacttgtac gtaaacgtct 120420

ctacaatcgt gtttttgctg taggattctc tgttaaagat aagcggcgag gaaaattttg 120480

caaaggcgtt ctgatagatt acccttccga caaaaccaag cggaattcga tccaccagtt 120540

cggacggcgt ctgaatatcc agaaaagcgg ctttggggtc atccctgacc accagcatgc 120600

cgtccattgt ggtggtatag tcaaaaaaaa cataccgctt atcggctctg tcaatggcta 120660

ctaccgtgct catgattatt taagggtttg cgttaaggtg tctttcaaat gatacacaat 120720

gtctctaatc tcagcaggta taagttctct gatggtaaaa aattcgtcag gaaatattat 120780

ctgtctcaga ttaatatatc ctattcggtt gtgatagcga actccgttcc ccaccgctac 120840

cacaatatgc tcgaaaggtg agcggtgtcc gtttttgtaa agtcttcttg caagttttaa 120900

atttttatct aagtcggatt catcagaagc ataggaaacg cgggctatac gcgccaccga 120960

tgtaaccagt agtttggaat tcaattcctc cggtgaaata actccctgaa gaggatcgac 121020

aatatctccg ggattggctt cgaaagccgg ggagttgtcg tagatatagc gaatcaggag 121080

cgctattttt cggaattcgg gttgtgcgtc ggaagcgcaa cgaagtctga aaaagttgtc 121140

aagcgaatac ggatcggcaa tggaagcgat gacatctgta tatgcatagg gtgaaagtat 121200

tcgattagcg tgttgcttgt gtacattgag tttctcgagc acaaaatgca accccgctga 121260

tgtatataac ccggtatacc aacaccacct tgccagcaca tctttccacc ctcctatttt 121320

tttatcggaa aacattgccc ctgagttttc cacaaaatca tctggaacaa aggggttttc 121380

aagtacacgc ttccggtatt ttttcaagga aatggctctt gtagaagcgg cattcctcga 121440

aaaggcgcga tgtgtattaa attcagccag tatgactgtg ggaatttgaa agcgaaagca 121500

gaagaagata tcgttattcg tcttcgtttt gatcagatac cacaccattg ctttctgagt 121560

tttttccatt taaaaccgat ccatttaaac aaagtttcat ttctctgatt tcatctttca 121620

gggtttcaga aaggtgtaat atttcatccc actcgcgagt attgcgctca aaaatctcaa 121680

ctccactgga aacatcactc atcatttttt tcctccttgt gtttaatgtt gtggtaaatc 121740

tataatttgc gggtgttgcc agaagcgcat ttcatagata ccccactttc ttttaaataa 121800

aagaaaaata acttttttta aaaaattatt taccccggtc gtcaagtctt ccaatatccg 121860

gctctttata gggatgaatg cgatatttct tctggaaaaa ctccttccac tccggcgatt 121920

tttcaaatac gacatccaga ttgtcgataa gtgcctttgc caccatgtgt ttgcagattc 121980

tcccccggta gtaatgatcc gggcacgtac atttgaatgt gcgggtgtca aaattgacgc 122040

gcgttacgta ttttttgtag gagccgcttt cgagagtatc acgggcgcgt tcaagcagcg 122100

ttctcccctg tttgtctttc tgagtctgac accatttgag aaaagagagg agttgtttat 122160

atcgcttatc gaacgtttca agccgcttgc gctcgcgttc ttcaatagag cgcttgagtt 122220

cttcagcctt ttgctgtctc tcttttatac ttggcggcgg catacgctca gatgtttaaa 122280

attctccgaa gcagactttc gatctgatct tcggtaaaat ctcttttgga tatataaagc 122340

acaagattgc gctccgtgtt gtttttcggt ggggtgtttc ctttgagaag gtttctgaaa 122400

tattcgatga actctttttt aagctctttt tccgactttc cggttttatt ctgcacaagt 122460

gttttttcgg tggaagtagc ctcttcttcg ttgacggcga cattatatat agagagcatg 122520

agaaacatct ctaccgccgg atcggtagca tgacgtgcag ccatatcggc acttcggcgc 122580

tgaatggctt catatagcag tgattcctcg cgggtcattc ttttctgtta aataaatgtg 122640

aatccgtagg aaagggaaaa catcagggga aagcacacat ataagaacca gaacccagaa 122700

caaaaaatag gaggaaggtt atgggtaaga tcgatgtttc gaacatcaaa accgccgttg 122760

ccatctccca gaaagccaat gttcctcttt atctgtgggg tggtgtggga atctccaaaa 122820

cccaacaaat ctatcagtat gccaccagca ccaatcaaaa atgtgctgtc gttacggggt 122880

tggcaataga tccaaccgac gtagtgggtc attacattgc cgacttcaat aaacgtatca 122940

cctaccagac caaaccctat ctttatgaac tcttcggtga ggaagagcgg ggaatcatct 123000

tccttgacga attcaacaac tcagaaagtg atgtgatggg ggtgtttcta aagcttctcg 123060

acgaaaagag gcttggaagc tacaaactcc ctgatggaat tcacatcatt gcagccggta 123120

atccccccga actggctcca aatgcttcct cgcttccgct tgccgtcgct actcgatttg 123180

cccatcttta tgtggaagcg gatttcatct cccttaagag atggttgaaa ggagcggaag 123240

atgaagagga ttatgtaaag attttcaatc ttgaagtcgg ggaagatgtt gttcagcagg 123300

tgttcgatat tttcgttgac tactgcattg aaaacggtct tttcccggct tcagaagatt 123360

ctcgtagttg cgagtgggag gggagcctga attaccgcac attgcactat gcagcaaaaa 123420

tcggggctgt atacaaagtt gcttacaaaa atgtatcaaa tcaatcgaca ctgtataatg 123480

taactgtaga aatgatccac ggtctggttg gaaccatcgc ttccaacctg atggaacatc 123540

ttgaaaacaa gtggcttcca tcggcaaaag agattctcga aaactatgat attgtgctca 123600

agcatcgaga cgcctatgcc gcccttgcct acaaccttat gagcggcatt caggaagaag 123660

actatccgag gttggtggat ttcatgcaat ggttagaaaa gaaaaacgaa cttgtaatgc 123720

ttgcggcgat agtggaatct ttccagtcgt tcattccgaa gaaaaggttt ctgacaagcc 123780

ggttcgaata ctacaaccag attttcaaaa tcattaatcg atcgctggac gtctataaga 123840

aagtcaaacc cacaaacaac aagtgattga ttatggaacc gattgtcgaa aaaaagctct 123900

atgaactgat taactgcatt gtaaaaaatc ataccccact cgccatgatt ctttcccgaa 123960

tcaaagtgcg ggtagggggt agggataaat acacactggg actctgcaaa gaacgggaaa 124020

tcattctcag ccggtgtctc tttgatgatg aaatcgttta tcccaaactt gtatttatca 124080

aagaccccga caccggcgag atcgtagact atgatattga agactatgtt gccaaaatcg 124140

atgatgaagg gcggtatcat accctgctgg aagaaatcat tcatgccggt ctcatgcacc 124200

ccatgcgtgt agaccggttt cagaaaacat atcaggagct ttttgaaaag aacaagcggc 124260

tggtgaattt tctgtacctt tgtcttgagg ttgagcgtca tgcaatacat accgctgtag 124320

ccaacatcga tctacttaag cccgtgttca aagacaacac gcgggatgaa aagattgtgg 124380

aattcattaa agttattcaa catgatcatc ccgatcaaaa gctgtttggg tttacttttg 124440

aaagactgtt tttgaagtat ctcaacgatt ttgagggagg taaaattgca gcccccgcaa 124500

tttacgatct gatggaatac gacgggaata ccgttcccga caagttcata gaagcaatcg 124560

aaaaatctct tcataaaggg aaaaagtatg gaaatcagac actggatgaa atctttgaaa 124620

tccggcgtgt ggatcaaaag gggttgcaat tgacgcaact cctgaagcag atttgcttcc 124680

gcagggcacg taaaaaaccc tcgctgcacg tgctcgacaa aaagcggaag cactacgaac 124740

cgctcaggtt tgggaaaatc aaagaaaaaa cttcaaatat cgccattatt ctggatgtgt 124800

cgggaagtat gcttcgtgat ttcaaaaagc atcgcctgat tgacatcgcg acaagtatga 124860

tcgtggaaac tttcaaaaac gcacccaata tcgatgtata catcggagat accgaaatca 124920

aggataaagc gaagatccgc accctgtttt cccgtttcaa agggggcggt ggaaccgata 124980

tgtctaacat ctataaacaa ctgaaagatc gataccagaa aatactggtt gttaccgacg 125040

gggagacacc cttccccgaa ccaaaagact accgccctca ggatactttt atcatcatta 125100

atgatgaaat gcccgaaatt cccaattaca tcaaaaccct gaaggtgaaa ctatgaacga 125160

aaaagcgttc cagttccgca atcttctaaa ggaagtgatc ggcatgcgaa tcctcgagcg 125220

attcaaccac atagaacctg aaggaaaaag gaaatgggta attttatccg cctacattct 125280

aatagtggaa gaagaaaatg caccccagat ctgcaaggaa cttgttcgaa acaatacaga 125340

gatagatcct ctggaatttg tcagatcttt caaagaagaa cttataaaca tgatcgaaaa 125400

tcaaaattat cgaaatgaat ttgagaaata cgttgcaaac tacgcgatag aaaacgaaat 125460

caattacaga aacatgatag caaacttttt ctgatataaa aaggaaaacc cccggttcat 125520

caccgggggc ttcctcagcg tctattccct atcgggtaag ttccgccatt acggctgcag 125580

gagcttcaca tacagcagac catagaactc tggacgcacc acctccagag cgtagcgggt 125640

catcagacca cgccggtaag agaagttaac gggatcgacg atcgtcggcg tgaacagcag 125700

cggcacatac ggagcgtaaa ccgcacccgt ttgccacggc gtgttcagat cttgattacc 125760

catgatgatc accggctggt tctgatagat gttcttgtac aggcggtagc gtccctgcac 125820

catacctaca tagaagatac cggtaccacc atcgcggttg tcgttacccg gcgtaaagcc 125880

cggcatcgac tccagcagcg cagccacctg tgggctggta acaaggaagt tggcacccgc 125940

aaccgccgtc ttctgctgaa tgcggttgct gaccttgttc agttcgatca tcagggtagc 126000

caaccattcc tgcttcgagc cgtagaagtt gccggcaaca aagttacccg acgtttcatc 126060

gtagtattca ccgaccactt ccgaccagaa gccatagttg tcagtgcgcc gggcatgcgc 126120

catgatcgtc gacaggattt ccagatcgat ctcacgggca atatactgag acatgagcgt 126180

aacgatttcg ttttcaagat cgacgccctt atgataggcg gcgagatcct gcatcgcttc 126240

cggcgtccag gcggcacgca gcttacgggt cttggtagcc accggacggc tccgaagctc 126300

aaggttgatc tccggaatat ccagcgactg gaatccggga tccggatagt caggatccgt 126360

cgactggtct tcgaagtcgt ttcgagcatc gatgtagtag accagatcaa ggtcttgagt 126420

cgacggagta ccaccggcaa cggtcgcaaa gtcagagccg gttacgaaga acaaccgcgc 126480

gtacagcgcc gaaccgacgg caccgacgat ccggttgtag cgcggaagcg ggtaagcgac 126540

cgtgttttca ggatcaccgg aagcgtcgtc atattgccag aagcgcaccg tattcacatc 126600

ggcgacaccg ggaagcgacg caaccggcac atccacatag tacaccgcac cgctcgagac 126660

cagtgaagca atgccggtgt caaaaccgac atcccgcatc gtcgcctgct gggcggtagc 126720

cagatccacg gtgatcgtgg tctcatactc ccgacgcgac aggcgagcgt tttcatcata 126780

cagaccgccc gtagccgtgt cggtggtcag accggtacca ccgtagaccg agccgtttcc 126840

gggaagctca ggcgacttga aatccagata gaagaccaga cctgttggga gcgacagcgg 126900

ctgcaccgac accagatccg tcgcacgcag gttggcgaac acacggcgca caatcggaag 126960

tgccagattc cagccgtcaa cctccgtggt ctgggtggtc tccatcaggt gcttcttagc 127020

ctcgcggtac tggttctcca gcagggtagc gagcgtatgc cgctcccagt cgttacggca 127080

accctccaga agcggttgcc acttctcgat aagttgttcg ttaattttcg gttggctcat 127140

tttactctta tttttttttt gttttaaatc tctaaaaaca ttcggtattt aaccgaatta 127200

gagtccggca agacgcttaa tgcgctccag atccaacagc ggatcctcaa ccgaacccga 127260

cgtgcgggat tcggcgacag gtttcaccac acgggtttcc tgcagcttgc gcttgatccg 127320

ctcacgaatg cgctggcggg taacttcgtc aatgacgggc ttcttcaccc ggctttcccg 127380

catacggcgc ggcgtcggac acgaagcagc ttccgccatt tcctccgtct cctcaccagc 127440

caccttgcga agcagttcga tagcctcctc tacgcgctca agaagcgtgt gcaaaagatc 127500

catttcttca cgcacatgct cctcgctttc gacggcaccc ttgatgtcaa catcaatatc 127560

gagttcttcg tcgtccgaaa gatcggcatc ctttaactcg atttcggctt ccagctcgcc 127620

gtcttcgtcg acgtcttcaa catcgatttt gatgtcttcg tcatccagat ccagttccag 127680

atcctcctca tcgagatcca gttccagatc ttcgtcttcg tgttcggctt cggtaatccg 127740

acgcttcatt ttgtgtttag cttctcgcat ttcttcctgt tgtttagttt cccaggcttt 127800

ttgcaacgtt tgcgcgactt cttcggcaaa cgaagcaagc gtgtcatcgt cagtttcatc 127860

aaccttcgct tccgtcaggg gattaccttc aggctcttcc acctgctcaa gctcttcttc 127920

gagttccttc aaagcctccc gaatttcttc ggtgatcgag tgaatggaag cttcctgaag 127980

atgcctcttc tgcttttcct gacgaagcga ctcaaggtaa cccacaaagt ctttaaattc 128040

ctgcataact caaatttaaa tatatttaat cgccattcat tttaaaaaat ggcacctgct 128100

acgtgggaat attaaacccc acatcaaatt taaatatata tttttccgca cgaaataaaa 128160

aaaagggaga gaaactgatc tctcccccag gggtaacatg tattttataa cttgtgaact 128220

accaccacct atagatgtgg atggcttcgt ggtcaaggta gctcttgcta ccagattccc 128280

cacgctcaaa gggctgttcc atccccgaat ttgccaatta ttggctaatt aaatcacttt 128340

cttcttcaca agcgcctcgc gcaatctatg gcgtgctctg ttgattcgag atttgacggt 128400

tccgatagga atgttgtttt tctcagccag cgcctgcatg gcacattttt ccttcaactc 128460

catgtactgt ttcattatat tgtaaaacgg gttatcgcct ttttcaagtt cttcctgaat 128520

cacctccacc gcacgtttca attcatactg ctcatcaagc agcggctctc cggattcaat 128580

ttctacaggg gtatcccgat ctccaaatgt aatttcttcc atgtaaatcc tgggaccacg 128640

tcgagaattg tatcgataac gggtaattac aacggatttg aatacagtgt aaatatacgt 128700

agcgaaagaa gctccttcaa ccacgctata ggaatcaaat ctaagaagcc ttagaaacgt 128760

atcctgcacc atatcctcga tttcatgctc cgactttgta tatttctttc cgaaattttt 128820

gagccgctca gcatacctac tgtaaagcac ttcataacgg atttcgagcg gaacgttctg 128880

aaggaaaagt tcttcgtcgg tcatctgata gtatttacgc ttatccataa cttctcctct 128940

gttttaaagg ttgaaaatga tttcgtagcc gtcaatgcgg tcatcagtta tgagcttgtc 129000

ataaagatcg tcaatctttt ctatgttgtc ataaatcatg agcatttcat caatatcatg 129060

cacaacaaca gaaatgtaat aaccgttttc ttcatcaaaa cagagttcgg cgtagctttt 129120

atgaagatcc cccacacatt ttttgatatt ctctacaaat acttctacag gataatatct 129180

aaccagacaa aaatcgagat gcggaagcac actgttcatt atctgctcca gcacctcttc 129240

attagaaatc agcagttcat aatcgtcaat ggtatttaca ttgtagacaa gatggttgtt 129300

ggatgtaata gtaggaatga cttcgtgagt tgggttgaaa tatgtgttta ccagatcttg 129360

aacggaatcg agcgcgtcgc gataatcaat tttagtctcc atagccatat cctaaaaggt 129420

tggttgatat ataccggtta tggaaaataa aaaaggggag agagggtgtt tcctttccca 129480

caccctctct ccgcgtttat agggaaagtc gtcatcgaag tagccctcaa tctcctccat 129540

cgaatgagat tctttttcgg gagagattca cctttttctt ggggggatta caaaattcct 129600

cttccgcggg atcaaagccc ctaatggaga atctcttcct ggcgggagcg ggttcatgct 129660

tccccaatca ttgttatttc cccagacaaa cacatggacg tctcttccac caacaaaacg 129720

aacttctccc gaatcggcgg agatgttcgg gagttcaccg cgaacccgga tcagggatcc 129780

caccccggct ttccgcacaa gatcggaagg tcccgttgta aaagtaaatg ttgaaccact 129840

cggtgctttc ttgctgaccg tcccaccgac ggaccgccag ccgtacggtg gtataactgt 129900

ttccgcta 129908



2
892
PRT
Vaccinia virus (strain Copenhagen)

2

Gln Asn Ala Thr Met Asp Glu Phe Leu Asn Ile Ser Trp Phe Tyr Ile
1 5 10 15

Ser Asn Gly Ile Ser Pro Asp Gly Cys Tyr Ser Leu Asp Glu Gln Tyr
20 25 30

Leu Thr Lys Ile Asn Asn Gly Cys Tyr His Cys Asp Asp Pro Arg Asn
35 40 45

Cys Phe Ala Lys Lys Ile Pro Arg Phe Asp Ile Pro Arg Ser Tyr Leu
50 55 60

Phe Leu Asp Ile Glu Cys His Phe Asp Lys Lys Phe Pro Ser Val Phe
65 70 75 80

Ile Asn Pro Ile Ser His Thr Ser Tyr Cys Tyr Ile Asp Leu Ser Gly
85 90 95

Lys Arg Leu Leu Phe Thr Leu Ile Asn Glu Glu Met Leu Thr Glu Gln
100 105 110

Glu Ile Gln Glu Ala Val Asp Arg Gly Cys Leu Arg Ile Gln Ser Leu
115 120 125

Met Glu Met Asp Tyr Glu Arg Glu Leu Val Leu Cys Ser Glu Ile Val
130 135 140

Leu Leu Arg Ile Ala Lys Gln Leu Leu Glu Leu Thr Phe Asp Tyr Val
145 150 155 160

Val Thr Phe Asn Gly His Asn Phe Asp Leu Arg Tyr Ile Thr Asn Arg
165 170 175

Leu Glu Leu Leu Thr Gly Glu Lys Ile Ile Phe Arg Ser Pro Asp Lys
180 185 190

Lys Glu Ala Val His Leu Cys Ile Tyr Glu Arg Asn Gln Ser Ser His
195 200 205

Lys Gly Val Gly Gly Met Ala Asn Thr Thr Phe His Val Asn Asn Asn
210 215 220

Asn Gly Thr Ile Phe Phe Asp Leu Tyr Ser Phe Ile Gln Lys Ser Glu
225 230 235 240

Lys Leu Asp Ser Tyr Lys Leu Asp Ser Ile Ser Lys Asn Ala Phe Ser
245 250 255

Cys Met Gly Lys Val Leu Asn Arg Gly Val Arg Glu Met Thr Phe Ile
260 265 270

Gly Asp Asp Thr Thr Asp Ala Lys Gly Lys Ala Ala Ala Phe Ala Lys
275 280 285

Val Leu Thr Thr Gly Asn Tyr Val Thr Val Asp Glu Asp Ile Ile Cys
290 295 300

Lys Val Ile Arg Lys Asp Ile Trp Glu Asn Gly Phe Lys Val Val Leu
305 310 315 320

Leu Cys Pro Thr Leu Pro Asn Asp Thr Tyr Lys Leu Ser Phe Gly Lys
325 330 335

Asp Asp Val Asp Leu Ala Gln Met Tyr Lys Asp Tyr Asn Leu Asn Ile
340 345 350

Ala Leu Asp Met Ala Arg Tyr Cys Ile His Asp Ala Cys Leu Cys Gln
355 360 365

Tyr Leu Trp Glu Tyr Tyr Gly Val Glu Thr Lys Thr Asp Ala Gly Ala
370 375 380

Ser Thr Tyr Val Leu Pro Gln Ser Met Val Phe Glu Tyr Arg Ala Ser
385 390 395 400

Thr Val Ile Lys Gly Pro Leu Leu Lys Leu Leu Leu Glu Thr Lys Thr
405 410 415

Ile Leu Val Arg Ser Glu Thr Lys Gln Lys Phe Pro Tyr Glu Gly Gly
420 425 430

Lys Val Phe Ala Pro Lys Gln Lys Met Phe Ser Asn Asn Val Leu Ile
435 440 445

Phe Asp Tyr Asn Ser Leu Tyr Pro Asn Val Cys Ile Phe Gly Asn Leu
450 455 460

Ser Pro Glu Thr Leu Val Gly Val Val Val Ser Thr Asn Arg Leu Glu
465 470 475 480

Glu Glu Ile Asn Asn Gln Leu Leu Leu Gln Lys Tyr Pro Pro Pro Arg
485 490 495

Tyr Ile Thr Val His Cys Glu Pro Arg Leu Pro Asn Leu Ile Ser Glu
500 505 510

Ile Ala Ile Phe Asp Arg Ser Ile Glu Gly Thr Ile Pro Arg Leu Leu
515 520 525

Arg Thr Phe Leu Ala Glu Arg Ala Arg Tyr Lys Lys Met Leu Lys Gln
530 535 540

Ala Thr Ser Ser Thr Glu Lys Ala Ile Tyr Asp Ser Met Gln Tyr Thr
545 550 555 560

Tyr Lys Ile Val Ala Asn Ser Val Tyr Gly Leu Met Gly Phe Arg Asn
565 570 575

Ser Ala Leu Tyr Ser Tyr Ala Ser Ala Lys Ser Cys Thr Ser Ile Gly
580 585 590

Arg Arg Met Ile Leu Tyr Leu Glu Ser Val Leu Asn Gly Ala Glu Leu
595 600 605

Ser Asn Gly Met Leu Arg Phe Ala Asn Pro Leu Ser Asn Pro Phe Tyr
610 615 620

Met Asp Asp Arg Asp Ile Asn Pro Ile Val Lys Thr Ser Leu Pro Ile
625 630 635 640

Asp Tyr Arg Phe Arg Phe Arg Ser Val Tyr Gly Asp Thr Asp Ser Val
645 650 655

Phe Thr Glu Ile Asp Ser Gln Asp Val Asp Lys Ser Ile Glu Ile Ala
660 665 670

Lys Glu Leu Glu Arg Leu Ile Asn Asn Arg Val Leu Phe Asn Asn Phe
675 680 685

Lys Ile Glu Phe Glu Ala Val Tyr Lys Asn Leu Ile Met Gln Ser Lys
690 695 700

Lys Lys Tyr Thr Thr Met Lys Tyr Ser Ala Ser Ser Asn Ser Lys Ser
705 710 715 720

Val Pro Glu Arg Ile Asn Lys Gly Thr Ser Glu Thr Arg Arg Asp Val
725 730 735

Ser Lys Phe His Lys Asn Met Ile Lys Thr Tyr Lys Thr Arg Leu Ser
740 745 750

Glu Met Leu Ser Glu Gly Arg Met Asn Ser Asn Gln Val Cys Ile Asp
755 760 765

Ile Leu Arg Ser Leu Glu Thr Asp Leu Arg Ser Glu Phe Asp Ser Arg
770 775 780

Ser Ser Pro Leu Glu Leu Phe Met Leu Ser Arg Met His His Ser Asn
785 790 795 800

Tyr Lys Ser Ala Asp Asn Pro Asn Met Tyr Leu Val Thr Glu Tyr Asn
805 810 815

Lys Asn Asn Pro Glu Thr Ile Glu Leu Gly Glu Arg Tyr Tyr Phe Ala
820 825 830

Tyr Ile Cys Pro Ala Asn Val Pro Trp Thr Lys Lys Leu Val Asn Ile
835 840 845

Lys Thr Tyr Glu Thr Ile Ile Asp Arg Ser Phe Lys Leu Gly Ser Asp
850 855 860

Gln Arg Ile Phe Tyr Glu Val Tyr Phe Lys Arg Leu Thr Ser Glu Ile
865 870 875 880

Val Asn Leu Leu Asp Asn Lys Val Leu Cys Ile Ser
885 890



3
892
PRT
Vaccinia virus (strain WR)

3

Gln Asn Ala Thr Met Asp Glu Phe Leu Asn Ile Ser Trp Phe Tyr Ile
1 5 10 15

Ser Asn Gly Ile Ser Pro Asp Gly Cys Tyr Ser Leu Asp Glu Gln Tyr
20 25 30

Leu Thr Lys Ile Asn Asn Gly Cys Tyr His Cys Asp Asp Pro Arg Asn
35 40 45

Cys Phe Ala Lys Lys Ile Pro Arg Phe Asp Ile Pro Arg Ser Tyr Leu
50 55 60

Phe Leu Asp Ile Glu Cys His Phe Asp Lys Lys Phe Pro Ser Val Phe
65 70 75 80

Ile Asn Pro Ile Ser His Thr Ser Tyr Cys Tyr Ile Asp Leu Ser Gly
85 90 95

Lys Arg Leu Leu Phe Thr Leu Ile Asn Glu Glu Met Leu Thr Glu Gln
100 105 110

Glu Ile Gln Glu Ala Val Asp Arg Gly Cys Leu Arg Ile Gln Ser Leu
115 120 125

Met Glu Met Asp Tyr Glu Arg Glu Leu Val Leu Cys Ser Glu Ile Val
130 135 140

Leu Leu Arg Ile Ala Lys Gln Leu Leu Glu Leu Thr Phe Asp Tyr Val
145 150 155 160

Val Thr Phe Asn Gly His Asn Phe Asp Leu Arg Tyr Ile Thr Asn Arg
165 170 175

Leu Glu Leu Leu Thr Gly Glu Lys Ile Ile Phe Arg Ser Pro Asp Lys
180 185 190

Lys Glu Ala Val Tyr Leu Cys Ile Tyr Glu Arg Asn Gln Ser Ser His
195 200 205

Lys Gly Val Gly Gly Met Ala Asn Thr Thr Phe His Val Asn Asn Asn
210 215 220

Asn Gly Thr Ile Phe Phe Asp Leu Tyr Ser Phe Ile Gln Lys Ser Glu
225 230 235 240

Lys Leu Asp Ser Tyr Lys Leu Asp Ser Ile Ser Lys Asn Ala Phe Ser
245 250 255

Cys Met Gly Lys Val Leu Asn Arg Gly Val Arg Glu Met Thr Phe Ile
260 265 270

Gly Asp Asp Thr Thr Asp Ala Lys Gly Lys Ala Ala Ala Phe Ala Lys
275 280 285

Val Leu Thr Thr Gly Asn Tyr Val Thr Val Asp Glu Asp Ile Ile Cys
290 295 300

Lys Val Ile Arg Lys Asp Ile Trp Glu Asn Gly Phe Lys Val Val Leu
305 310 315 320

Leu Cys Pro Thr Leu Pro Asn Asp Thr Tyr Lys Leu Ser Phe Gly Lys
325 330 335

Asp Asp Val Asp Leu Ala Gln Met Tyr Lys Asp Tyr Asn Leu Asn Ile
340 345 350

Ala Leu Asp Met Ala Arg Tyr Cys Ile His Asp Ala Cys Leu Cys Gln
355 360 365

Tyr Leu Trp Glu Tyr Tyr Gly Val Glu Thr Lys Thr Asp Ala Gly Ala
370 375 380

Ser Thr Tyr Val Leu Pro Gln Ser Met Val Phe Glu Tyr Arg Ala Ser
385 390 395 400

Thr Val Ile Lys Gly Pro Leu Leu Lys Leu Leu Leu Glu Thr Lys Thr
405 410 415

Ile Leu Val Arg Ser Glu Thr Lys Gln Lys Phe Pro Tyr Glu Gly Gly
420 425 430

Lys Val Phe Ala Pro Lys Gln Lys Met Phe Ser Asn Asn Val Leu Ile
435 440 445

Phe Asp Tyr Asn Ser Leu Tyr Pro Asn Val Cys Ile Phe Gly Asn Leu
450 455 460

Ser Pro Glu Thr Leu Val Gly Val Val Val Ser Thr Asn Arg Leu Glu
465 470 475 480

Glu Glu Ile Asn Asn Gln Leu Leu Leu Gln Lys Tyr Pro Pro Pro Arg
485 490 495

Tyr Ile Thr Val His Cys Glu Pro Arg Leu Pro Asn Leu Ile Ser Glu
500 505 510

Ile Ala Ile Phe Asp Arg Ser Ile Glu Gly Thr Ile Pro Arg Leu Leu
515 520 525

Arg Thr Phe Leu Ala Glu Arg Ala Arg Tyr Lys Lys Met Leu Lys Gln
530 535 540

Ala Thr Ser Ser Thr Glu Lys Ala Ile Tyr Asp Ser Met Gln Tyr Thr
545 550 555 560

Tyr Lys Ile Val Ala Asn Ser Val Tyr Gly Leu Met Gly Phe Arg Asn
565 570 575

Ser Ala Leu Tyr Ser Tyr Ala Ser Ala Lys Ser Cys Thr Ser Ile Gly
580 585 590

Arg Arg Met Ile Leu Tyr Leu Glu Ser Val Leu Asn Gly Ala Glu Leu
595 600 605

Ser Asn Gly Met Leu Arg Phe Ala Asn Pro Leu Ser Asn Pro Phe Tyr
610 615 620

Met Asp Asp Arg Asp Ile Asn Pro Ile Val Lys Thr Ser Leu Pro Ile
625 630 635 640

Asp Tyr Arg Phe Arg Phe Arg Ser Val Tyr Gly Asp Thr Asp Ser Val
645 650 655

Phe Thr Glu Ile Asp Ser Gln Asp Val Asp Lys Ser Ile Glu Ile Ala
660 665 670

Lys Glu Leu Glu Arg Leu Ile Asn Asn Arg Val Leu Phe Asn Asn Phe
675 680 685

Lys Ile Glu Phe Glu Ala Val Tyr Lys Asn Leu Ile Met Gln Ser Lys
690 695 700

Lys Lys Tyr Thr Thr Met Lys Tyr Ser Ala Ser Ser Asn Ser Lys Ser
705 710 715 720

Val Pro Glu Arg Ile Asn Lys Gly Thr Ser Glu Thr Arg Arg Asp Val
725 730 735

Ser Lys Phe His Lys Asn Met Ile Lys Thr Tyr Lys Thr Arg Leu Ser
740 745 750

Glu Met Leu Ser Glu Gly Arg Met Asn Ser Asn Gln Val Cys Ile Asp
755 760 765

Ile Leu Arg Ser Leu Glu Thr Asp Leu Arg Ser Glu Phe Asp Ser Arg
770 775 780

Ser Ser Pro Leu Glu Leu Phe Met Leu Ser Arg Met His His Ser Asn
785 790 795 800

Tyr Lys Ser Ala Asp Asn Pro Asn Met Tyr Leu Val Thr Glu Tyr Asn
805 810 815

Lys Asn Asn Pro Glu Thr Ile Glu Leu Gly Glu Arg Tyr Tyr Phe Ala
820 825 830

Tyr Ile Cys Pro Ala Asn Val Pro Trp Thr Lys Lys Leu Val Asn Ile
835 840 845

Lys Thr Tyr Glu Thr Ile Ile Asp Arg Ser Phe Lys Leu Gly Ser Asp
850 855 860

Gln Arg Ile Phe Tyr Glu Val Tyr Phe Lys Arg Leu Thr Ser Glu Ile
865 870 875 880

Val Asn Leu Leu Asp Asn Lys Val Leu Cys Ile Ser
885 890



4
891
PRT
Variola virus

4

Gln Asn Ala Thr Met Asp Glu Phe Leu Asn Ile Ser Trp Phe Tyr Ile
1 5 10 15

Ser Asn Gly Ile Ser Pro Asp Gly Cys Tyr Ser Leu Asp Asp Gln Tyr
20 25 30

Leu Thr Lys Ile Asn Asn Gly Cys Tyr His Cys Gly Asp Pro Arg Asn
35 40 45

Cys Phe Ala Lys Glu Ile Pro Arg Phe Asp Ile Pro Arg Ser Tyr Leu
50 55 60

Phe Leu Asp Ile Glu Cys His Phe Asp Lys Lys Phe Pro Ser Val Phe
65 70 75 80

Ile Asn Pro Ile Ser His Thr Ser Tyr Cys Tyr Ile Asp Leu Ser Gly
85 90 95

Lys Arg Leu Leu Phe Thr Leu Ile Asn Glu Glu Met Leu Thr Glu Gln
100 105 110

Glu Ile Gln Glu Ala Val Asp Arg Gly Cys Leu Arg Ile Gln Ser Leu
115 120 125

Met Glu Met Asp Tyr Glu Arg Glu Leu Val Leu Cys Ser Glu Ile Val
130 135 140

Leu Leu Gln Ile Ala Lys Gln Leu Leu Glu Leu Thr Phe Asp Tyr Ile
145 150 155 160

Val Thr Phe Asn Gly His Asn Phe Asp Leu Arg Tyr Ile Thr Asn Arg
165 170 175

Leu Glu Leu Leu Thr Gly Glu Lys Ile Ile Phe Arg Ser Pro Asp Lys
180 185 190

Lys Glu Ala Val His Leu Cys Ile Tyr Glu Arg Asn Gln Ser Ser His
195 200 205

Lys Gly Val Gly Gly Met Ala Asn Thr Thr Phe His Val Asn Asn Asn
210 215 220

Asn Gly Thr Ile Phe Phe Asp Leu Tyr Ser Phe Ile Gln Lys Ser Glu
225 230 235 240

Lys Leu Asp Ser Tyr Lys Leu Asp Ser Ile Ser Lys Asn Ala Phe Ser
245 250 255

Cys Met Gly Lys Val Leu Asn Arg Gly Val Arg Glu Met Thr Phe Ile
260 265 270

Gly Asp Asp Thr Thr Asp Ala Lys Gly Lys Ala Ala Val Phe Ala Lys
275 280 285

Val Leu Thr Thr Gly Asn Tyr Val Thr Val Asp Asp Ile Ile Cys Lys
290 295 300

Val Ile His Lys Asp Ile Trp Glu Asn Gly Phe Lys Val Val Leu Ser
305 310 315 320

Cys Pro Thr Leu Thr Asn Asp Thr Tyr Lys Leu Ser Phe Gly Lys Asp
325 330 335

Asp Val Asp Leu Ala Gln Met Tyr Lys Asp Tyr Asn Leu Asn Ile Ala
340 345 350

Leu Asp Met Ala Arg Tyr Cys Ile His Asp Ala Cys Leu Cys Gln Tyr
355 360 365

Leu Trp Glu Tyr Tyr Gly Val Glu Thr Lys Thr Asp Ala Gly Ala Ser
370 375 380

Thr Tyr Val Leu Pro Gln Ser Met Val Phe Gly Tyr Lys Ala Ser Thr
385 390 395 400

Val Ile Lys Gly Pro Leu Leu Lys Leu Leu Leu Glu Thr Lys Thr Ile
405 410 415

Leu Val Arg Ser Glu Thr Lys Gln Lys Phe Pro Tyr Glu Gly Gly Lys
420 425 430

Val Phe Ala Pro Lys Gln Lys Met Phe Ser Asn Asn Val Leu Ile Phe
435 440 445

Asp Tyr Asn Ser Leu Tyr Pro Asn Val Cys Ile Phe Gly Asn Leu Ser
450 455 460

Pro Glu Thr Leu Val Gly Val Val Val Ser Ser Asn Arg Leu Glu Glu
465 470 475 480

Glu Ile Asn Asn Gln Leu Leu Leu Gln Lys Tyr Pro Pro Pro Arg Tyr
485 490 495

Ile Thr Val His Cys Glu Pro Arg Leu Pro Asn Leu Ile Ser Glu Ile
500 505 510

Ala Ile Phe Asp Arg Ser Ile Glu Gly Thr Ile Pro Arg Leu Leu Arg
515 520 525

Thr Phe Leu Ala Glu Arg Ala Arg Tyr Lys Lys Met Leu Lys Gln Ala
530 535 540

Thr Ser Ser Thr Glu Lys Ala Ile Tyr Asp Ser Met Gln Tyr Thr Tyr
545 550 555 560

Lys Ile Ile Ala Asn Ser Val Tyr Gly Leu Met Gly Phe Arg Asn Ser
565 570 575

Ala Leu Tyr Ser Tyr Ala Ser Ala Lys Ser Cys Thr Ser Ile Gly Arg
580 585 590

Arg Met Ile Leu Tyr Leu Glu Ser Val Leu Asn Gly Ala Glu Leu Ser
595 600 605

Asn Gly Met Leu Arg Phe Ala Asn Pro Leu Ser Asn Pro Phe Tyr Met
610 615 620

Asp Asp Arg Asp Ile Asn Pro Ile Val Lys Thr Ser Leu Pro Ile Asp
625 630 635 640

Tyr Arg Phe Arg Phe Arg Ser Val Tyr Gly Asp Thr Asp Ser Val Phe
645 650 655

Thr Glu Ile Asp Ser Gln Asp Val Asp Lys Ser Ile Glu Ile Ala Lys
660 665 670

Glu Leu Glu Arg Leu Ile Asn Ser Arg Val Leu Phe Asn Asn Phe Lys
675 680 685

Ile Glu Phe Glu Ala Val Tyr Lys Asn Leu Ile Met Gln Ser Lys Lys
690 695 700

Lys Tyr Thr Thr Met Lys Tyr Ser Ala Ser Ser Asn Ser Lys Ser Val
705 710 715 720

Pro Glu Arg Ile Asn Lys Gly Thr Ser Glu Thr Arg Arg Asp Val Ser
725 730 735

Lys Phe His Lys Asn Met Ile Lys Ile Tyr Lys Thr Arg Leu Ser Glu
740 745 750

Met Leu Ser Glu Gly Arg Met Asn Ser Asn Gln Val Cys Ile Asp Ile
755 760 765

Leu Arg Ser Leu Glu Thr Asp Leu Arg Ser Glu Phe Asp Ser Arg Ser
770 775 780

Ser Pro Leu Glu Leu Phe Met Leu Ser Arg Met His His Leu Asn Tyr
785 790 795 800

Lys Ser Ala Asp Asn Pro Asn Met Tyr Leu Val Thr Glu Tyr Asn Lys
805 810 815

Asn Asn Pro Glu Thr Ile Glu Leu Gly Glu Arg Tyr Tyr Phe Ala Tyr
820 825 830

Ile Cys Pro Ala Asn Val Pro Trp Thr Lys Lys Leu Val Asn Ile Lys
835 840 845

Thr Tyr Glu Thr Ile Ile Asp Arg Ser Phe Lys Leu Gly Ser Asp Gln
850 855 860

Arg Ile Phe Tyr Glu Val Tyr Phe Lys Arg Leu Thr Ser Glu Ile Val
865 870 875 880

Asn Leu Leu Asp Asn Lys Val Leu Cys Ile Ser
885 890



5
874
PRT
Fowlpox virus

5

Glu Lys Gln Tyr Leu Gln Glu Tyr Leu Asp Ile Thr Trp Phe Tyr Leu
1 5 10 15

Leu Asn Asn Ile Thr Pro Asp Gly Cys Tyr Lys Ile Asp Ile Glu His
20 25 30

Leu Thr Pro Ile Lys Lys Asp Cys Tyr His Cys Asp Asp Val Ser Lys
35 40 45

Val Phe Ile Gln Glu Ile Pro Ile Phe Glu Val Lys Phe Thr Tyr Leu
50 55 60

Leu Phe Asp Ile Glu Cys Gln Phe Asp Lys Lys Phe Pro Ser Val Phe
65 70 75 80

Val Asn Pro Ile Ser His Ile Ser Cys Trp Ile Ile Asp Lys Val Thr
85 90 95

Glu Tyr Lys Phe Thr Leu Ile Asn Thr Asp Ile Leu Pro Asp Lys Glu
100 105 110

Pro Ser Ile Leu His His Lys Asp Phe Ser Pro Lys Asp Arg Ile Thr
115 120 125

Tyr Cys Thr Glu Ile Val Met Leu Leu Ile Met Lys Lys Ile Leu Glu
130 135 140

His Arg Phe Asp Phe Val Ile Thr Phe Asn Gly Asn Asn Phe Asp Ile
145 150 155 160

Arg Tyr Ile Ser Gly Arg Leu Glu Ile Leu Glu Lys Ser Phe Ile Tyr
165 170 175

Phe Ser Leu Pro Asp Ala Thr Glu Thr Val Lys Leu Lys Ile Phe Glu
180 185 190

Arg Phe Val Thr Gly Gly Thr Phe Thr Asn Lys Thr Tyr His Ile Asn
195 200 205

Asn Asn Asn Gly Val Met Phe Phe Asp Leu Tyr Ala Phe Ile Gln Lys
210 215 220

Thr Glu Arg Leu Asp Ser Tyr Lys Leu Asp Ser Ile Ser Lys Asn Ile
225 230 235 240

Phe Asn Cys Asn Val Ala Ile Lys Glu Ile Asp Asp Thr Ile Leu Thr
245 250 255

Leu Glu Ala Thr Val Lys Asp Asn Ser Lys Asp Lys Leu Ser Ile Phe
260 265 270

Ser Arg Val Leu Glu Thr Gly Asn Tyr Ile Thr Ile Gly Asp Asn Asn
275 280 285

Val Ser Lys Ile Val Tyr Lys Asp Ile Asn Gln Asp Ser Phe Ile Ile
290 295 300

Lys Val Ile Ser Asn Arg Asp Tyr Glu Ile Gly Ser Val His Asn Ile
305 310 315 320

Ser Phe Gly Lys Asp Asp Val Asp Leu Lys Asp Met Tyr Lys Asn Tyr
325 330 335

Asn Leu Glu Ile Ala Leu Asp Met Glu Arg Tyr Cys Ile His Asp Ala
340 345 350

Cys Leu Cys Lys Tyr Ile Trp Asp Tyr Tyr Arg Val Pro Ser Lys Ile
355 360 365

Asn Ala Ala Ser Ser Thr Tyr Leu Leu Pro Gln Ser Leu Ala Leu Glu
370 375 380

Tyr Arg Ala Ser Thr Leu Ile Lys Gly Pro Leu Leu Lys Leu Leu Leu
385 390 395 400

Glu Glu Arg Val Ile Tyr Thr Arg Lys Ile Thr Lys Val Arg Tyr Pro
405 410 415

Tyr Ile Gly Gly Lys Val Phe Leu Pro Ser Gln Lys Thr Phe Glu Asn
420 425 430

Asn Val Met Ile Phe Asp Tyr Asn Ser Leu Tyr Pro Asn Val Cys Ile
435 440 445

Tyr Gly Asn Leu Ser Pro Glu Lys Leu Val Cys Ile Leu Leu Asn Ser
450 455 460

Asn Lys Leu Glu Ser Glu Ile Asn Met Arg Thr Ile Lys Ser Lys Tyr
465 470 475 480

Pro Tyr Pro Glu Tyr Val Cys Val Ser Cys Glu Ser Arg Leu Ser Asp
485 490 495

Tyr Tyr Ser Glu Ile Ile Val Tyr Asp Arg Arg Glu Lys Gly Ile Ile
500 505 510

Pro Lys Leu Leu Glu Met Phe Ile Gly Lys Arg Lys Glu Tyr Lys Asn
515 520 525

Leu Leu Lys Thr Ala Ser Thr Thr Ile Glu Ser Thr Leu Tyr Asp Ser
530 535 540

Leu Gln Tyr Ile Tyr Lys Ile Ile Ala Asn Ser Val Tyr Gly Leu Met
545 550 555 560

Gly Phe Ser Asn Ser Thr Leu Tyr Ser Tyr Ser Ser Ala Lys Thr Cys
565 570 575

Thr Thr Ile Gly Arg Asn Met Ile Thr Tyr Leu Asp Ser Ile Met Asn
580 585 590

Gly Ala Val Trp Glu Asn Asp Lys Leu Ile Leu Ala Asp Phe Pro Arg
595 600 605

Asn Ile Phe Ser Gly Glu Thr Met Phe Asn Lys Glu Leu Glu Val Pro
610 615 620

Asn Met Asn Glu Ser Phe Lys Phe Arg Ser Val Tyr Gly Asp Thr Asp
625 630 635 640

Ser Ile Phe Ser Glu Ile Ser Thr Lys Asp Ile Glu Lys Thr Ala Lys
645 650 655

Ile Ala Lys His Leu Glu His Ile Ile Asn Thr Lys Ile Leu His Ala
660 665 670

Asn Phe Lys Ile Glu Phe Glu Ala Ile Tyr Thr Gln Leu Ile Leu Gln
675 680 685

Ser Lys Lys Lys Tyr Thr Thr Ile Lys Tyr Leu Ala Asn Tyr Lys Pro
690 695 700

Gly Asp Lys Pro Ile Arg Val Asn Lys Gly Thr Ser Glu Thr Arg Arg
705 710 715 720

Asp Val Ala Leu Phe His Lys His Met Ile Gln Arg Tyr Lys Asp Met
725 730 735

Leu Met Lys Leu Leu Met Gln Ser Lys Gly Gln Gln Glu Ile Thr Arg
740 745 750

Leu Ile Leu Gln Ser Leu Glu Thr Asp Met Ile Ser Glu Phe Thr His
755 760 765

Asn Arg Glu Phe Glu Lys Tyr Leu Leu Ser Arg Lys His His Asn Asn
770 775 780

Tyr Lys Ser Ala Thr His Ser Asn Phe Glu Leu Val Lys Arg Tyr Asn
785 790 795 800

Leu Glu Asn Thr Glu Lys Ile Glu Ile Gly Glu Arg Tyr Tyr Tyr Ile
805 810 815

Tyr Ile Cys Asp Ile Ser Leu Pro Trp Gln Lys Lys Leu Cys Asn Ile
820 825 830

Leu Ser Tyr Glu Val Ile Ala Asp Ser Lys Phe Tyr Leu Pro Lys Asp
835 840 845

Lys Arg Ile Phe Tyr Glu Ile Tyr Phe Lys Arg Ile Ala Ser Glu Val
850 855 860

Val Asn Leu Leu Thr Asp Lys Thr Gln Cys
865 870



6
738
PRT
Bos taurus (Bovine)

6

Pro Ser Phe Ala Pro Tyr Glu Ala Asn Val Asp Phe Glu Ile Arg Phe
1 5 10 15

Met Val Asp Thr Asp Ile Val Gly Cys Asn Trp Leu Glu Leu Pro Ala
20 25 30

Gly Lys Tyr Ile Leu Arg Pro Glu Gly Lys Ala Thr Leu Cys Gln Leu
35 40 45

Glu Ala Asp Val Leu Trp Ser Asp Val Ile Ser His Pro Pro Glu Gly
50 55 60

Glu Trp Gln Arg Ile Ala Pro Leu Arg Val Leu Ser Phe Asp Ile Glu
65 70 75 80

Cys Ala Gly Arg Lys Gly Ile Phe Pro Glu Pro Glu Arg Asp Pro Val
85 90 95

Ile Gln Ile Cys Ser Leu Gly Leu Arg Trp Gly Glu Pro Glu Pro Phe
100 105 110

Leu Arg Leu Ala Leu Thr Leu Arg Pro Cys Ala Pro Ile Leu Gly Ala
115 120 125

Lys Val Gln Ser Tyr Glu Arg Glu Glu Asp Leu Leu Gln Ala Trp Ser
130 135 140

Thr Phe Ile Arg Ile Met Asp Pro Asp Val Ile Thr Gly Tyr Asn Ile
145 150 155 160

Gln Asn Phe Asp Leu Pro Tyr Leu Ile Ser Arg Ala Gln Thr Leu Lys
165 170 175

Val Pro Gly Phe Pro Leu Leu Gly Arg Val Ile Gly Leu Arg Ser Asn
180 185 190

Ile Arg Glu Ser Ser Phe Gln Ser Arg Gln Thr Gly Arg Arg Asp Ser
195 200 205

Lys Val Val Ser Met Val Gly Arg Val Gln Met Asp Met Leu Gln Val
210 215 220

Leu Leu Arg Glu Tyr Lys Leu Arg Ser Tyr Thr Leu Asn Ala Val Ser
225 230 235 240

Phe His Phe Leu Gly Glu Gln Lys Glu Asp Val Gln His Ser Ile Ile
245 250 255

Thr Asp Leu Gln Asn Gly Asn Asp Gln Thr Arg Arg Arg Leu Ala Val
260 265 270

Tyr Cys Leu Lys Asp Ala Phe Leu Pro Leu Arg Leu Leu Glu Arg Leu
275 280 285

Met Val Leu Val Asn Ala Met Glu Met Ala Arg Val Thr Gly Val Pro
290 295 300

Leu Gly Tyr Leu Leu Ser Arg Gly Gln Gln Val Lys Val Val Ser Gln
305 310 315 320

Leu Leu Arg Gln Ala Met Arg Gln Gly Leu Leu Met Pro Val Val Lys
325 330 335

Thr Glu Gly Gly Glu Asp Tyr Thr Gly Ala Thr Val Ile Glu Pro Leu
340 345 350

Lys Gly Tyr Tyr Asp Val Pro Ile Ala Thr Leu Asp Phe Ser Ser Leu
355 360 365

Tyr Pro Ser Ile Met Met Ala His Asn Leu Cys Tyr Thr Thr Leu Leu
370 375 380

Arg Pro Gly Ala Ala Gln Lys Leu Gly Leu Thr Glu Asp Gln Phe Ile
385 390 395 400

Lys Thr Pro Thr Gly Asp Glu Phe Val Lys Ala Ser Val Arg Lys Gly
405 410 415

Leu Leu Pro Gln Ile Leu Glu Asn Leu Leu Ser Ala Arg Lys Arg Ala
420 425 430

Lys Ala Glu Leu Ala Lys Glu Thr Asp Pro Leu Arg Arg Gln Val Leu
435 440 445

Asp Gly Arg Gln Leu Ala Leu Lys Val Ser Ala Asn Ser Val Tyr Gly
450 455 460

Phe Thr Gly Ala Gln Val Gly Arg Leu Pro Cys Leu Glu Ile Ser Gln
465 470 475 480

Ser Val Thr Gly Phe Gly Arg Gln Met Ile Glu Lys Thr Lys Gln Leu
485 490 495

Val Glu Thr Lys Tyr Thr Val Glu Asn Gly Tyr Ser Thr Ser Ala Lys
500 505 510

Val Val Tyr Gly Asp Thr Asp Ser Val Met Cys Arg Phe Gly Val Ser
515 520 525

Ser Val Ala Glu Ala Met Ala Leu Gly Arg Glu Ala Ala Asp Trp Val
530 535 540

Ser Gly His Phe Pro Ser Pro Ile Arg Leu Glu Phe Glu Lys Val Tyr
545 550 555 560

Phe Pro Tyr Leu Leu Ile Ser Lys Lys Arg Tyr Ala Gly Leu Leu Phe
565 570 575

Ser Ser Arg Pro Asp Ala His Asp Arg Met Asp Cys Lys Gly Leu Glu
580 585 590

Ala Val Arg Arg Asp Asn Cys Pro Leu Val Ala Asn Leu Val Thr Ala
595 600 605

Ser Leu Arg Arg Leu Leu Ile Asp Arg Asp Pro Ser Gly Ala Val Ala
610 615 620

His Ala Gln Asp Val Ile Ser Asp Leu Leu Cys Asn Arg Ile Asp Ile
625 630 635 640

Ser Gln Leu Val Ile Thr Lys Glu Leu Thr Arg Ala Ala Ala Asp Tyr
645 650 655

Ala Gly Lys Gln Ala His Val Glu Leu Ala Glu Arg Met Arg Lys Arg
660 665 670

Asp Pro Gly Ser Ala Pro Ser Leu Gly Asp Arg Val Pro Tyr Val Ile
675 680 685

Ile Ser Ala Ala Lys Gly Val Ala Ala Tyr Met Lys Ser Glu Asp Pro
690 695 700

Leu Phe Val Leu Glu His Ser Leu Pro Ile Asp Thr Gln Tyr Tyr Leu
705 710 715 720

Glu Gln Gln Leu Ala Lys Pro Leu Leu Arg Ile Phe Glu Pro Ile Leu
725 730 735

Gly Glu



7
738
PRT
Homo sapiens

7

Pro Ser Phe Ala Pro Tyr Glu Ala Asn Val Asp Phe Glu Ile Arg Phe
1 5 10 15

Met Val Asp Thr Asp Ile Val Gly Cys Asn Trp Leu Glu Leu Pro Ala
20 25 30

Gly Lys Tyr Ala Leu Arg Leu Lys Glu Lys Ala Thr Gln Cys Gln Leu
35 40 45

Glu Ala Asp Val Leu Trp Ser Asp Val Val Ser His Pro Pro Glu Gly
50 55 60

Pro Trp Gln Arg Ile Ala Pro Leu Arg Val Leu Ser Phe Asp Ile Glu
65 70 75 80

Cys Ala Gly Arg Lys Gly Ile Phe Pro Glu Pro Glu Arg Asp Pro Val
85 90 95

Ile Gln Ile Cys Ser Leu Gly Leu Arg Trp Gly Glu Pro Glu Pro Phe
100 105 110

Leu Arg Leu Ala Leu Thr Leu Arg Pro Cys Ala Pro Ile Leu Gly Ala
115 120 125

Lys Val Gln Ser Tyr Glu Lys Glu Glu Asp Leu Leu Gln Ala Trp Ser
130 135 140

Thr Phe Ile Arg Ile Met Asp Pro Asp Val Ile Thr Gly Tyr Asn Ile
145 150 155 160

Gln Asn Phe Asp Leu Pro Tyr Leu Ile Ser Arg Ala Gln Thr Leu Lys
165 170 175

Val Gln Thr Phe Pro Phe Leu Gly Arg Val Ala Gly Leu Cys Ser Asn
180 185 190

Ile Arg Asp Ser Ser Phe Gln Ser Lys Gln Thr Gly Arg Arg Asp Thr
195 200 205

Lys Val Val Ser Met Val Gly Arg Val Gln Met Asp Met Leu Gln Val
210 215 220

Leu Leu Arg Glu Tyr Lys Leu Arg Ser His Thr Leu Asn Ala Val Ser
225 230 235 240

Phe His Phe Leu Gly Glu Gln Lys Glu Asp Val Gln His Ser Ile Ile
245 250 255

Thr Asp Leu Gln Asn Gly Asn Asp Gln Thr Arg Arg Arg Leu Ala Val
260 265 270

Tyr Cys Leu Lys Asp Ala Tyr Leu Pro Leu Arg Leu Leu Glu Arg Leu
275 280 285

Met Val Leu Val Asn Ala Val Glu Met Ala Arg Val Thr Gly Val Pro
290 295 300

Leu Ser Tyr Leu Leu Ser Arg Gly Gln Gln Val Lys Val Val Ser Gln
305 310 315 320

Leu Leu Arg Gln Ala Met His Glu Gly Leu Leu Met Pro Val Val Lys
325 330 335

Ser Glu Gly Gly Glu Asp Tyr Thr Gly Ala Thr Val Ile Glu Pro Leu
340 345 350

Lys Gly Tyr Tyr Asp Val Pro Ile Ala Thr Leu Asp Phe Ser Ser Leu
355 360 365

Tyr Pro Ser Ile Met Met Ala His Asn Leu Cys Tyr Thr Thr Leu Leu
370 375 380

Arg Pro Gly Thr Ala Gln Lys Leu Gly Leu Thr Glu Asp Gln Phe Ile
385 390 395 400

Arg Thr Pro Thr Gly Asp Glu Phe Val Lys Thr Ser Val Arg Lys Gly
405 410 415

Leu Leu Pro Gln Ile Leu Glu Asn Leu Leu Ser Ala Arg Lys Arg Ala
420 425 430

Lys Ala Glu Leu Ala Lys Glu Thr Asp Pro Leu Arg Arg Gln Val Leu
435 440 445

Asp Gly Arg Gln Leu Ala Leu Lys Val Ser Ala Asn Ser Val Tyr Gly
450 455 460

Phe Thr Gly Ala Gln Val Gly Lys Leu Pro Cys Leu Glu Ile Ser Gln
465 470 475 480

Ser Val Thr Gly Phe Gly Arg Gln Met Ile Glu Lys Thr Lys Gln Leu
485 490 495

Val Glu Ser Lys Tyr Thr Val Glu Asn Gly Tyr Ser Thr Ser Ala Lys
500 505 510

Val Val Tyr Gly Asp Thr Asp Ser Val Met Cys Arg Phe Gly Val Ser
515 520 525

Ser Val Ala Glu Ala Met Ala Leu Gly Arg Glu Ala Ala Asp Trp Val
530 535 540

Ser Gly His Phe Pro Ser Pro Ile Arg Leu Glu Phe Glu Lys Val Tyr
545 550 555 560

Phe Pro Tyr Leu Leu Ile Ser Lys Lys Arg Tyr Ala Gly Leu Leu Phe
565 570 575

Ser Ser Arg Pro Asp Ala His Asp Arg Met Asp Cys Lys Gly Leu Glu
580 585 590

Ala Val Arg Arg Asp Asn Cys Pro Leu Val Ala Asn Leu Val Thr Ala
595 600 605

Ser Leu Arg Arg Leu Leu Ile Asp Arg Asp Pro Glu Gly Ala Val Ala
610 615 620

His Ala Gln Asp Val Ile Ser Asp Leu Leu Cys Asn Arg Ile Asp Ile
625 630 635 640

Ser Gln Leu Val Ile Thr Lys Glu Leu Thr Arg Ala Ala Ser Asp Tyr
645 650 655

Ala Gly Lys Gln Ala His Val Glu Leu Ala Glu Arg Met Arg Lys Arg
660 665 670

Asp Pro Gly Ser Ala Pro Ser Leu Gly Asp Arg Val Pro Tyr Val Ile
675 680 685

Ile Ser Ala Ala Lys Gly Val Ala Ala Tyr Met Lys Ser Glu Asp Pro
690 695 700

Leu Phe Val Leu Glu His Ser Leu Pro Ile Asp Thr Gln Tyr Tyr Leu
705 710 715 720

Glu Gln Gln Leu Ala Lys Pro Leu Leu Arg Ile Phe Glu Pro Ile Leu
725 730 735

Gly Glu



8
734
PRT
Candida albicans (Yeast)

8

Ile Asp Pro Cys Ile Thr Tyr Asp Asn Ile Asn Tyr Leu Leu Arg Leu
1 5 10 15

Met Ile Asp Cys Lys Ile Thr Gly Met Ser Trp Ile Thr Leu Pro Arg
20 25 30

Asp Lys Tyr Lys Ile Val Asn Asn Lys Ile Ser Thr Cys Gln Ile Glu
35 40 45

Cys Ser Ile Asp Tyr Arg Asp Leu Ile Ser His Pro Pro Glu Gly Glu
50 55 60

Trp Leu Lys Met Ala Pro Leu Arg Ile Leu Ser Phe Asp Ile Glu Cys
65 70 75 80

Ala Gly Arg Lys Gly Val Phe Pro Glu Ala Glu His Asp Pro Val Ile
85 90 95

Gln Ile Ala Asn Val Val Gln Lys Ser Gly Glu Ser Lys Pro Phe Val
100 105 110

Arg Asn Val Phe Thr Val Asn Thr Cys Ser Ser Ile Ile Gly Ser Gln
115 120 125

Ile Phe Glu His Gln Arg Glu Glu Asp Met Leu Met His Trp Lys Glu
130 135 140

Phe Ile Thr Lys Val Asp Pro Asp Val Ile Ile Gly Tyr Asn Thr Ala
145 150 155 160

Asn Phe Asp Ile Pro Tyr Val Leu Asn Arg Ala Lys Ala Leu Gly Leu
165 170 175

Asn Asp Phe Pro Phe Phe Gly Arg Leu Lys Arg Val Lys Gln Glu Ile
180 185 190

Lys Asp Ala Val Phe Ser Ser Arg Ala Tyr Gly Thr Arg Glu Asn Lys
195 200 205

Val Val Asn Ile Asp Gly Arg Met Gln Leu Asp Leu Leu Gln Phe Ile
210 215 220

Gln Arg Glu Tyr Lys Leu Arg Ser Tyr Thr Leu Asn Ser Val Ser Ala
225 230 235 240

His Phe Leu Gly Glu Gln Lys Glu Asp Val Gln His Ser Ile Ile Thr
245 250 255

Asp Leu Gln Asn Gly Thr Lys Glu Thr Arg Arg Arg Leu Ala Val Tyr
260 265 270

Cys Leu Lys Asp Ala Phe Leu Pro Leu Arg Leu Leu Asp Lys Leu Met
275 280 285

Cys Leu Val Asn Tyr Thr Glu Met Ala Arg Val Thr Gly Val Pro Phe
290 295 300

Ser Tyr Leu Leu Ser Arg Gly Gln Gln Ile Lys Val Ile Ser Gln Leu
305 310 315 320

Phe Arg Lys Cys Leu Gln Glu Asp Ile Val Ile Pro Asn Leu Lys Ser
325 330 335

Glu Gly Ser Asn Glu Glu Tyr Glu Gly Ala Thr Val Ile Glu Pro Glu
340 345 350

Arg Gly Tyr Tyr Asp Val Pro Ile Ala Thr Leu Asp Phe Ser Ser Leu
355 360 365

Tyr Pro Ser Ile Met Met Ala His Asn Leu Cys Tyr Thr Thr Leu Leu
370 375 380

Asn Lys Asn Ser Ile Lys Ala Phe Gly Leu Thr Glu Asp Asp Tyr Thr
385 390 395 400

Lys Thr Pro Asn Gly Asp Tyr Phe Val His Ser Asn Leu Arg Lys Gly
405 410 415

Ile Leu Pro Thr Ile Leu Asp Glu Leu Leu Thr Ala Arg Lys Lys Ala
420 425 430

Lys Ala Asp Leu Lys Lys Glu Thr Asp Pro Phe Lys Lys Asp Val Leu
435 440 445

Asn Gly Arg Gln Leu Ala Leu Lys Ile Ser Ala Asn Ser Val Tyr Gly
450 455 460

Phe Thr Gly Ala Thr Val Gly Lys Leu Pro Cys Leu Ala Ile Ser Ser
465 470 475 480

Ser Val Thr Ala Phe Gly Arg Glu Met Ile Glu Lys Thr Lys Asn Glu
485 490 495

Val Gln Glu Tyr Tyr Ser Lys Lys Asn Gly His Pro Tyr Asp Ala Lys
500 505 510

Val Ile Tyr Gly Asp Thr Asp Ser Val Met Val Lys Phe Gly Tyr Gln
515 520 525

Asp Leu Glu Thr Cys Met Lys Leu Gly Glu Glu Ala Ala Asn Tyr Val
530 535 540

Ser Thr Lys Phe Lys Asn Pro Ile Lys Leu Glu Phe Glu Lys Val Tyr
545 550 555 560

Phe Pro Tyr Leu Leu Ile Asn Lys Lys Arg Tyr Ala Gly Leu Tyr Trp
565 570 575

Thr Arg Pro Glu Lys Phe Asp Lys Met Asp Thr Lys Gly Ile Glu Thr
580 585 590

Val Arg Arg Asp Asn Cys Gln Leu Val Gln Asn Val Ile Thr Lys Val
595 600 605

Leu Glu Phe Ile Leu Glu Glu Arg Asp Val Pro Lys Ala Gln Arg Phe
610 615 620

Val Lys Gln Thr Ile Ala Asp Leu Leu Gln Asn Arg Ile Asp Leu Ser
625 630 635 640

Gln Leu Val Ile Thr Lys Ala Tyr Ser Lys His Asp Tyr Ser Ala Lys
645 650 655

Gln Ala His Val Glu Leu Ala Glu Arg Met Arg Lys Arg Asp Pro Gly
660 665 670

Ser Ala Pro Thr Leu Gly Asp Arg Val Ala Tyr Val Ile Ile Lys Thr
675 680 685

Gly Gly Asp Lys Asn Tyr Glu Lys Ser Glu Asp Pro Leu Tyr Val Leu
690 695 700

Glu Asn Ser Leu Pro Ile Asp Val Lys Tyr Tyr Leu Asp Gln Gln Leu
705 710 715 720

Thr Lys Pro Leu Glu Arg Ile Phe Ile Pro Ile Leu Gly Glu
725 730



9
734
PRT
Saccharomyces cerevisiae

9

Ser Asn Gly Thr Thr Thr Tyr Asp Asn Ile Ala Tyr Thr Leu Arg Leu
1 5 10 15

Met Val Asp Cys Gly Ile Val Gly Met Ser Trp Ile Thr Leu Pro Lys
20 25 30

Gly Lys Tyr Ser Met Ile Glu Pro Asn Asn Arg Val Ser Ser Cys Gln
35 40 45

Leu Glu Val Ser Ile Asn Tyr Arg Asn Leu Ile Ala His Pro Ala Glu
50 55 60

Gly Asp Trp Ser His Thr Ala Pro Leu Arg Ile Met Ser Phe Asp Ile
65 70 75 80

Glu Cys Ala Gly Arg Ile Gly Val Phe Pro Glu Pro Glu Tyr Asp Pro
85 90 95

Val Ile Gln Ile Ala Asn Val Val Ser Ile Ala Gly Ala Lys Lys Pro
100 105 110

Phe Ile Arg Asn Val Phe Thr Leu Asn Thr Cys Ser Pro Ile Thr Gly
115 120 125

Ser Met Ile Phe Ser His Ala Thr Glu Glu Glu Met Leu Ser Asn Trp
130 135 140

Arg Asn Phe Ile Ile Lys Val Asp Pro Asp Val Ile Ile Gly Tyr Asn
145 150 155 160

Thr Thr Asn Phe Asp Ile Pro Tyr Leu Leu Asn Arg Ala Lys Ala Leu
165 170 175

Lys Val Asn Asp Phe Pro Tyr Phe Gly Arg Leu Lys Thr Val Lys Gln
180 185 190

Glu Ile Lys Glu Ser Val Phe Ser Ser Lys Ala Tyr Gly Thr Arg Glu
195 200 205

Thr Lys Asn Val Asn Ile Asp Gly Arg Leu Gln Leu Asp Leu Leu Gln
210 215 220

Phe Ile Gln Arg Glu Tyr Lys Leu Arg Ser Tyr Thr Leu Asn Ala Val
225 230 235 240

Ser Ala His Phe Leu Gly Glu Gln Lys Glu Asp Val His Tyr Ser Ile
245 250 255

Ile Ser Asp Leu Gln Asn Gly Asp Ser Glu Thr Arg Arg Arg Leu Ala
260 265 270

Val Tyr Cys Leu Lys Asp Ala Tyr Leu Pro Leu Arg Leu Met Glu Lys
275 280 285

Leu Met Ala Leu Val Asn Tyr Thr Glu Met Ala Arg Val Thr Gly Val
290 295 300

Pro Phe Ser Tyr Leu Leu Ala Arg Gly Gln Gln Ile Lys Val Val Ser
305 310 315 320

Gln Leu Phe Arg Lys Cys Leu Glu Ile Asp Thr Val Ile Pro Asn Met
325 330 335

Gln Ser Gln Ala Ser Asp Asp Gln Tyr Glu Gly Ala Thr Val Ile Glu
340 345 350

Pro Ile Arg Gly Tyr Tyr Asp Val Pro Ile Ala Thr Leu Asp Phe Asn
355 360 365

Ser Leu Tyr Pro Ser Ile Met Met Ala His Asn Leu Cys Tyr Thr Thr
370 375 380

Leu Cys Asn Lys Ala Thr Val Glu Arg Leu Asn Leu Lys Ile Asp Glu
385 390 395 400

Asp Tyr Val Ile Thr Pro Asn Gly Asp Tyr Phe Val Thr Thr Lys Arg
405 410 415

Arg Arg Gly Ile Leu Pro Ile Ile Leu Asp Glu Leu Ile Ser Ala Arg
420 425 430

Lys Arg Ala Lys Lys Asp Leu Arg Asp Glu Lys Asp Pro Phe Lys Arg
435 440 445

Asp Val Leu Asn Gly Arg Gln Leu Ala Leu Lys Ile Ser Ala Asn Ser
450 455 460

Val Tyr Gly Phe Thr Gly Ala Thr Val Gly Lys Leu Pro Cys Leu Ala
465 470 475 480

Ile Ser Ser Ser Val Thr Ala Tyr Gly Arg Thr Met Ile Leu Lys Thr
485 490 495

Lys Thr Ala Val Gln Glu Lys Tyr Cys Ile Lys Asn Gly Tyr Lys His
500 505 510

Asp Ala Val Val Val Tyr Gly Asp Thr Asp Ser Val Met Val Lys Phe
515 520 525

Gly Thr Thr Asp Leu Lys Glu Ala Met Asp Leu Gly Thr Glu Ala Ala
530 535 540

Lys Tyr Val Ser Thr Leu Phe Lys His Pro Ile Asn Leu Glu Phe Glu
545 550 555 560

Lys Ala Tyr Phe Pro Tyr Leu Leu Ile Asn Lys Lys Arg Tyr Ala Gly
565 570 575

Leu Phe Trp Thr Asn Pro Asp Lys Phe Asp Lys Leu Asp Gln Lys Gly
580 585 590

Leu Ala Ser Val Arg Arg Asp Ser Cys Ser Leu Val Ser Ile Val Met
595 600 605

Asn Lys Val Leu Lys Lys Ile Leu Ile Glu Arg Asn Val Asp Gly Ala
610 615 620

Leu Ala Phe Val Arg Glu Thr Ile Asn Asp Ile Leu His Asn Arg Val
625 630 635 640

Asp Ile Ser Lys Leu Ile Ile Ser Lys Thr Leu Ala Pro Asn Tyr Thr
645 650 655

Asn Pro Gln Pro His Ala Val Leu Ala Glu Arg Met Lys Arg Arg Glu
660 665 670

Gly Val Gly Pro Asn Val Gly Asp Arg Val Asp Tyr Val Ile Ile Gly
675 680 685

Gly Asn Asp Lys Leu Tyr Asn Arg Ala Glu Asp Pro Leu Phe Val Leu
690 695 700

Glu Asn Asn Ile Gln Val Asp Ser Arg Tyr Tyr Leu Thr Asn Gln Leu
705 710 715 720

Gln Asn Pro Ile Ile Ser Ile Val Ala Pro Ile Ile Gly Asp
725 730



10
735
PRT
Schizosaccharomyces pombe

10

Val Gly Val Thr Thr Phe Glu Ser Asn Thr Gln Tyr Leu Leu Arg Phe
1 5 10 15

Met Ile Asp Cys Asp Val Val Gly Met Asn Trp Ile His Leu Pro Ala
20 25 30

Ser Lys Tyr Gln Phe Arg Tyr Gln Asn Arg Val Ser Asn Cys Gln Ile
35 40 45

Glu Ala Trp Ile Asn Tyr Lys Asp Leu Ile Ser Leu Pro Ala Glu Gly
50 55 60

Gln Trp Ser Lys Met Ala Pro Leu Arg Ile Met Ser Phe Asp Ile Glu
65 70 75 80

Cys Ala Gly Arg Lys Gly Val Phe Pro Asp Pro Ser Ile Asp Pro Val
85 90 95

Ile Gln Ile Ala Ser Ile Val Thr Gln Tyr Gly Asp Ser Thr Pro Phe
100 105 110

Val Arg Asn Val Phe Cys Val Asp Thr Cys Ser Gln Ile Val Gly Thr
115 120 125

Gln Val Tyr Glu Phe Gln Asn Gln Ala Glu Met Leu Ser Ser Trp Ser
130 135 140

Lys Phe Val Arg Asp Val Asp Pro Asp Val Leu Ile Gly Tyr Asn Ile
145 150 155 160

Cys Asn Phe Asp Ile Pro Tyr Leu Leu Asp Arg Ala Lys Ser Leu Arg
165 170 175

Ile His Asn Phe Pro Leu Leu Gly Arg Ile His Asn Phe Phe Ser Val
180 185 190

Ala Lys Glu Thr Ser Phe Ser Ser Lys Ala Tyr Gly Thr Arg Glu Ser
195 200 205

Lys Thr Thr Ser Ile Pro Gly Arg Leu Gln Leu Asp Met Leu Gln Val
210 215 220

Met Gln Arg Asp Phe Lys Leu Arg Ser Tyr Ser Leu Asn Ala Val Cys
225 230 235 240

Ser Gln Phe Leu Gly Glu Gln Lys Glu Asp Val His Tyr Ser Ile Ile
245 250 255

Thr Asp Leu Gln Asn Gly Thr Ala Asp Ser Arg Arg Arg Leu Ala Ile
260 265 270

Tyr Cys Leu Lys Asp Ala Tyr Leu Pro Gln Arg Leu Met Asp Lys Leu
275 280 285

Met Cys Phe Val Asn Tyr Thr Glu Met Ala Arg Val Thr Gly Val Pro
290 295 300

Phe Asn Phe Leu Leu Ala Arg Gly Gln Gln Ile Lys Val Ile Ser Gln
305 310 315 320

Leu Phe Cys Lys Ala Leu Gln His Asp Leu Val Val Pro Asn Ile Arg
325 330 335

Val Asn Gly Thr Asp Glu Gln Tyr Glu Gly Ala Thr Val Ile Glu Pro
340 345 350

Ile Lys Gly Tyr Tyr Asp Thr Pro Ile Ala Thr Leu Asp Phe Ser Ser
355 360 365

Leu Tyr Pro Ser Ile Met Gln Ala His Asn Leu Cys Tyr Thr Thr Leu
370 375 380

Leu Asp Ser Asn Thr Ala Glu Leu Leu Lys Leu Lys Gln Asp Val Asp
385 390 395 400

Tyr Ser Val Thr Pro Asn Gly Asp Tyr Phe Val Lys Pro His Val Arg
405 410 415

Lys Gly Leu Leu Pro Ile Ile Leu Ala Asp Leu Leu Asn Ala Arg Lys
420 425 430

Lys Ala Lys Ala Asp Leu Lys Lys Glu Thr Asp Pro Phe Lys Lys Ala
435 440 445

Val Leu Asp Gly Arg Gln Leu Ala Leu Lys Val Ser Ala Asn Ser Val
450 455 460

Tyr Gly Phe Thr Gly Ala Thr Asn Gly Arg Leu Pro Cys Leu Ala Ile
465 470 475 480

Ser Ser Ser Val Thr Ser Tyr Gly Arg Gln Met Ile Glu Lys Thr Lys
485 490 495

Asp Val Val Glu Lys Arg Tyr Arg Ile Glu Asn Gly Tyr Ser His Asp
500 505 510

Ala Val Val Ile Tyr Gly Asp Thr Asp Ser Val Met Val Lys Phe Gly
515 520 525

Val Lys Thr Leu Pro Glu Ala Met Lys Leu Gly Glu Glu Ala Ala Asn
530 535 540

Tyr Val Ser Asp Gln Phe Pro Asn Pro Ile Asn Trp Ser Phe Ser Thr
545 550 555 560

Phe Pro Tyr Leu Leu Ile Ser Lys Lys Arg Tyr Ala Gly Leu Phe Trp
565 570 575

Thr Arg Thr Asp Thr Tyr Asp Lys Met Asp Ser Lys Gly Ile Glu Thr
580 585 590

Val Arg Arg Asp Asn Cys Pro Leu Val Ser Tyr Val Ile Asp Thr Ala
595 600 605

Leu Arg Lys Met Leu Ile Asp Gln Asp Val Glu Gly Ala Gln Leu Phe
610 615 620

Thr Lys Lys Val Ile Ser Asp Leu Leu Gln Asn Lys Ile Asp Met Ser
625 630 635 640

Gln His Val Ile Thr Lys Ala Leu Ser Lys Thr Asp Tyr Ala Ala Lys
645 650 655

Met Ala His Val Glu Leu Ala Glu Arg Met Arg Lys Arg Asp Ala Gly
660 665 670

Ser Ala Pro Ala Ile Gly Asp Arg Val Ala Tyr Val Ile Ile Lys Gly
675 680 685

Ala Gln Gly Asp Gln Phe Tyr Met Arg Ser Glu Asp Pro Ile Tyr Val
690 695 700

Leu Glu Asn Asn Ile Pro Ile Asp Ala Lys Tyr Tyr Leu Glu Asn Gln
705 710 715 720

Leu Ser Lys Pro Leu Leu Arg Ile Phe Glu Pro Ile Leu Gly Glu
725 730 735



11
741
PRT
Plasmodium falciparum

11

Ile Gly Gly Ile Val Tyr Glu Ala Asn Leu Pro Phe Ile Leu Arg Tyr
1 5 10 15

Ile Ile Asp His Lys Ile Thr Gly Ser Ser Trp Ile Asn Cys Lys Lys
20 25 30

Gly His Tyr Tyr Ile Arg Asn Lys Asn Lys Lys Ile Ser Asn Cys Thr
35 40 45

Phe Glu Ile Asp Ile Ser Tyr Glu His Val Glu Pro Ile Thr Leu Glu
50 55 60

Asn Glu Tyr Gln Gln Ile Pro Lys Leu Arg Ile Leu Ser Phe Asp Ile
65 70 75 80

Glu Cys Ile Lys Leu Asp Gly Lys Gly Phe Pro Glu Ala Lys Asn Asp
85 90 95

Pro Ile Ile Gln Ile Ser Ser Ile Leu Tyr Phe Gln Gly Glu Pro Ile
100 105 110

Asp Asn Cys Thr Lys Phe Ile Phe Thr Leu Leu Glu Cys Ala Ser Ile
115 120 125

Pro Gly Ser Asn Val Ile Trp Phe Asn Asp Glu Lys Thr Leu Leu Glu
130 135 140

Ala Trp Asn Glu Phe Ile Ile Arg Ile Asp Pro Asp Phe Leu Thr Gly
145 150 155 160

Tyr Asn Ile Ile Asn Phe Asp Leu Pro Tyr Ile Leu Asn Arg Gly Thr
165 170 175

Ala Leu Asn Leu Lys Lys Leu Lys Phe Leu Gly Arg Ile Lys Asn Val
180 185 190

Ala Ser Thr Val Lys Asp Ser Ser Phe Ser Ser Lys Gln Phe Gly Thr
195 200 205

His Glu Thr Lys Glu Ile Asn Ile Phe Gly Arg Ile Gln Phe Asp Val
210 215 220

Tyr Asp Leu Ile Lys Arg Asp Tyr Lys Leu Lys Ser Tyr Thr Leu Asn
225 230 235 240

Tyr Val Ser Phe Glu Phe Leu Lys Glu Gln Lys Glu Asp Val His Tyr
245 250 255

Ser Ile Met Asn Asp Leu Gln Asn Glu Ser Pro Glu Ser Arg Lys Arg
260 265 270

Ile Ala Thr Tyr Cys Ile Lys Asp Gly Val Leu Pro Leu Arg Leu Ile
275 280 285

Asp Lys Leu Leu Phe Ile Tyr Asn Tyr Val Glu Met Ala Arg Val Thr
290 295 300

Gly Thr Pro Phe Val Tyr Leu Leu Thr Arg Gly Gln Gln Ile Lys Val
305 310 315 320

Thr Ser Gln Leu Tyr Arg Lys Cys Lys Glu Leu Asn Tyr Val Ile Pro
325 330 335

Ser Thr Tyr Met Lys Val Asn Thr Asn Glu Lys Tyr Glu Gly Ala Thr
340 345 350

Val Leu Glu Pro Ile Lys Gly Tyr Tyr Ile Glu Pro Ile Ser Thr Leu
355 360 365

Asp Phe Ala Ser Leu Tyr Pro Ser Ile Met Ile Ala His Asn Leu Cys
370 375 380

Tyr Ser Thr Leu Ile Lys Ser Asn His Glu Val Ser Asp Leu Gln Asn
385 390 395 400

Asp Asp Ile Thr Thr Ile Gln Gly Lys Asn Asn Leu Lys Phe Val Lys
405 410 415

Lys Asn Val Lys Lys Gly Ile Leu Pro Leu Ile Val Glu Glu Leu Ile
420 425 430

Glu Ala Arg Lys Lys Val Lys Leu Leu Ile Lys Asn Glu Lys Asn Asn
435 440 445

Ile Thr Lys Met Val Leu Asn Gly Arg Gln Leu Ala Leu Lys Ile Ser
450 455 460

Ala Asn Ser Val Tyr Gly Tyr Thr Gly Ala Ser Ser Gly Gly Gln Leu
465 470 475 480

Pro Cys Leu Glu Val Ala Val Ser Ile Thr Thr Leu Gly Arg Ser Met
485 490 495

Ile Glu Lys Thr Lys Glu Arg Val Glu Ser Phe Tyr Cys Lys Ser Asn
500 505 510

Gly Tyr Glu His Asn Ser Thr Val Ile Tyr Gly Asp Thr Asp Ser Val
515 520 525

Met Val Lys Phe Gly Thr Asn Asn Ile Glu Glu Ala Met Thr Leu Gly
530 535 540

Lys Asp Ala Ala Glu Arg Ile Ser Lys Glu Phe Leu Ser Pro Ile Lys
545 550 555 560

Leu Glu Phe Glu Lys Val Tyr Cys Pro Tyr Leu Leu Leu Asn Lys Lys
565 570 575

Arg Tyr Ala Gly Leu Leu Tyr Thr Asn Pro Asn Lys His Asp Lys Met
580 585 590

Asp Cys Lys Gly Ile Glu Thr Val Arg Arg Asp Phe Cys Ile Leu Ile
595 600 605

Gln Gln Met Met Glu Thr Val Leu Asn Lys Leu Leu Ile Glu Lys Asn
610 615 620

Leu Asn Ser Ala Ile Glu Tyr Thr Lys Ser Lys Ile Lys Glu Leu Leu
625 630 635 640

Thr Asn Asn Ile Asp Met Ser Leu Leu Val Val Thr Lys Ser Leu Gly
645 650 655

Lys Thr Asp Tyr Glu Thr Arg Leu Pro His Val Glu Leu Ala Lys Lys
660 665 670

Leu Lys Gln Arg Asp Ser Ala Thr Ala Pro Asn Val Gly Asp Arg Val
675 680 685

Ser Tyr Ile Ile Val Lys Gly Val Lys Gly Gln Ala Gln Tyr Glu Arg
690 695 700

Ala Glu Asp Pro Leu Tyr Val Leu Asp Asn Asn Leu Ala Ile Asp Tyr
705 710 715 720

Asn His Tyr Leu Asp Ala Ile Lys Ser Pro Leu Ser Arg Ile Phe Glu
725 730 735

Val Ile Met Gln Asn
740



12
744
PRT
Chlorella virus NY-2A

12

Glu Tyr Gln Ile Tyr Glu Ser Ser Val Asp Pro Ile Ile Arg Ile Phe
1 5 10 15

His Leu Arg Asn Ile Asn Pro Ala Asp Trp Met His Val Ser Lys Ala
20 25 30

Phe Pro Val Glu Thr Arg Ile Ser Asn Ser Asp Ile Glu Val Glu Thr
35 40 45

Ser Phe Gln His Leu Gly Pro Ser Asp Leu Lys Glu Val Pro Pro Leu
50 55 60

Ile Ile Ala Ser Trp Asp Ile Glu Thr Tyr Ser Lys Asp Arg Lys Phe
65 70 75 80

Pro Leu Ala Glu Asn Pro Ala Asp Tyr Cys Ile Gln Ile Ala Thr Thr
85 90 95

Phe Gln Lys Tyr Gly Glu Pro Glu Pro Tyr Arg Arg Val Val Val Cys
100 105 110

Tyr Lys Gln Thr Ala Ser Val Glu Gly Val Glu Ile Ile Ser Cys Ala
115 120 125

Glu Glu Ala Asp Val Met Asn Thr Trp Met Thr Ile Leu Gln Asp Glu
130 135 140

Ile Thr Asp Val Ser Ile Gly Tyr Asn Leu Trp Gln Tyr Asp Leu Arg
145 150 155 160

Tyr Ile His Gly Arg Ser Met Met Cys Val Asp Asp Ile Thr Gly Glu
165 170 175

Asp Asn Val Arg Leu Lys Asn Leu Gly Arg Leu Leu Val Gly Gly Gly
180 185 190

Glu Val Ile Glu Arg Asp Leu Ser Ser Asn Ala Phe Gly Gln Asn Lys
195 200 205

Phe Phe Leu Leu Asp Met Pro Gly Val Met Gln Ile Asp Leu Leu Gln
210 215 220

Trp Phe Arg Lys Asn Arg Asn Leu Glu Ser Tyr Ser Leu Asn Asn Val
225 230 235 240

Ser Lys Leu Tyr Leu Gly Asp Gln Lys Asn Asp Leu Pro Ala Met Gln
245 250 255

Ile Phe Glu Lys Phe Glu Gly Gly Ala Asp Asp Arg Ala Ile Ile Ala
260 265 270

Ala Tyr Ala Arg Lys Asp Thr Asp Leu Pro Leu Lys Leu Leu Lys Lys
275 280 285

Met Ala Ile Leu Glu Asp Ile Thr Glu Met Ala Asn Ala Val Lys Val
290 295 300

Pro Val Asp Tyr Ile Asn Phe Arg Gly Gln Gln Val Arg Ala Phe Ser
305 310 315 320

Cys Leu Val Gly Lys Ala Arg Gln Met Asn Tyr Ala Ile Pro Asp Asp
325 330 335

Lys Met Trp Thr Val Asp Gly Lys Tyr Glu Gly Ala Thr Val Leu Asp
340 345 350

Ala Lys Lys Gly Ala Tyr Phe Thr Ser Ile Ala Ala Leu Asp Phe Ala
355 360 365

Ser Leu Tyr Pro Ser Ile Ile Arg Ala His Asn Met Ser Pro Glu Thr
370 375 380

Leu Val Met Asp Lys Arg Phe Glu Asn Leu Pro Gly Ile Glu Tyr Tyr
385 390 395 400

Glu Ile Glu Thr Gly Leu Gly Thr Phe Lys Tyr Pro Gln Lys Asn Asp
405 410 415

Glu Thr Gly Glu Gly Gln Gly Val Val Pro Ala Leu Leu Asp Asp Leu
420 425 430

Ala Lys Phe Arg Lys Gln Ala Lys Lys His Met Ala Glu Ala Lys Lys
435 440 445

Asn Asp Asp Glu Phe Arg Glu Ala Leu Tyr Asp Ala Gln Gln Arg Ser
450 455 460

Tyr Lys Ile Val Met Asn Ser Val Tyr Gly Phe Leu Gly Ala Ser Arg
465 470 475 480

Gly Phe Ile Pro Cys Val Pro Ile Ala Ala Ser Val Thr Ala Thr Gly
485 490 495

Arg Lys Met Ile Glu His Thr Ala Lys Arg Val Thr Glu Leu Leu Pro
500 505 510

Gly Ser Glu Val Ile Tyr Gly Asp Thr Asp Ser Val Met Ile Arg Met
515 520 525

Lys Leu Pro Asp Asp Lys Ile His Asp Met Asp Glu Gln Phe Lys Met
530 535 540

Ala Lys Trp Leu Ala Gly Glu Ile Thr Lys Asp Phe Lys Ala Pro Asn
545 550 555 560

Asp Leu Glu Phe Glu Lys Ile Tyr Tyr Pro Tyr Ile Leu Tyr Ser Lys
565 570 575

Lys Arg Tyr Ala Ala Ile Lys Phe Glu Asp Pro Asp Glu Lys Gly Lys
580 585 590

Val Asp Val Lys Gly Leu Ala Leu Val Arg Arg Asp Phe Ser Pro Ile
595 600 605

Thr Arg Glu Ile Leu Lys Glu Ser Leu Asp Thr Ile Leu Phe Lys Lys
610 615 620

Asp Thr Pro Thr Ala Val Thr Glu Thr Val Glu Cys Ile Arg Lys Val
625 630 635 640

Leu Asp Asn Glu Tyr Pro Met Glu Lys Phe Thr Met Ser Lys Thr Leu
645 650 655

Lys Thr Gly Tyr Lys Asn Glu Cys Gln Pro His Leu His Val Ser Asn
660 665 670

Lys Ile Phe Glu Arg Thr Gly Phe Pro Val Pro Ser Gly Ala Arg Val
675 680 685

Pro Phe Val Tyr Ile Glu Asp Lys Lys Asn Leu Asp Thr Lys Gln Ser
690 695 700

Phe Arg Ala Glu Asp Pro Thr Phe Ala Gln Glu Asn Asp Leu Ile Val
705 710 715 720

Asp Arg Leu Phe Tyr Ile Glu His Gln Leu Met Lys Pro Ile Cys Ser
725 730 735

Leu Phe Glu Pro Leu Leu Asp Asp
740



13
743
PRT
Paramecium bursaria chlorella virus 1

13

Tyr Gln Ile Tyr Glu Ser Ser Val Asp Pro Ile Ile Arg Val Phe His
1 5 10 15

Leu Arg Asn Ile Asn Pro Ala Asp Trp Ile Arg Val Ser Lys Ala Tyr
20 25 30

Pro Ala Gln Thr Arg Ile Ser Asn Ser Asp Ile Glu Val Glu Thr Ser
35 40 45

Phe Gln His Leu Gly Pro Val Glu Asp Lys Thr Val Pro Pro Leu Val
50 55 60

Ile Ala Ser Trp Asp Ile Glu Thr Tyr Ser Lys Asp Arg Lys Phe Pro
65 70 75 80

Leu Ala Glu Asn Pro Thr Asp Tyr Cys Ile Gln Ile Ala Thr Thr Phe
85 90 95

Gln Lys Tyr Gly Glu Pro Glu Pro Tyr Arg Arg Val Val Val Cys Tyr
100 105 110

Lys Gln Thr Ala Pro Val Glu Gly Val Glu Ile Ile Ser Cys Leu Glu
115 120 125

Glu Ser Asp Val Met Asn Thr Trp Met Lys Ile Leu Gln Asp Glu Lys
130 135 140

Thr Asp Val Ser Ile Gly Tyr Asn Thr Trp Gln Tyr Asp Leu Arg Tyr
145 150 155 160

Val His Gly Arg Thr Gln Met Cys Val Asp Asp Met Thr Gly Glu Asp
165 170 175

Lys Val Lys Leu Ser Asn Leu Gly Arg Leu Leu Ser Gly Gly Gly Glu
180 185 190

Val Val Glu Arg Asp Leu Ser Ser Asn Ala Phe Gly Gln Asn Lys Phe
195 200 205

Phe Leu Leu Asp Met Pro Gly Val Met Gln Ile Asp Leu Leu Gln Trp
210 215 220

Phe Arg Lys Asn Arg Asn Leu Glu Ser Tyr Ser Leu Asn Asn Val Ser
225 230 235 240

Lys Leu Tyr Leu Gly Asp Gln Lys Asn Asp Leu Pro Ala Met Gln Ile
245 250 255

Phe Glu Lys Phe Glu Gly Asn Ala Glu Asp Arg Ala Ile Ile Ala Ala
260 265 270

Tyr Ala Ala Lys Asp Thr Asp Leu Pro Leu Lys Leu Leu Lys Lys Met
275 280 285

Ala Ile Leu Glu Asp Leu Thr Glu Met Ala Asn Ala Val Lys Val Pro
290 295 300

Val Asp Tyr Ile Asn Phe Arg Gly Gln Gln Ile Arg Ala Phe Ser Cys
305 310 315 320

Leu Val Gly Lys Ala Arg Gln Met Asn Tyr Ala Ile Pro Asp Asp Lys
325 330 335

Ala Trp Ala Thr Glu Gly Lys Tyr Glu Gly Ala Thr Val Leu Asp Ala
340 345 350

Lys Lys Gly Ala Tyr Phe Thr Pro Ile Ala Ala Leu Asp Phe Ala Ser
355 360 365

Leu Tyr Pro Ser Ile Ile Arg Ala His Asn Met Ser Pro Glu Thr Leu
370 375 380

Val Met Glu Lys Arg Phe Glu Asn Val Pro Gly Val Glu Tyr Tyr Glu
385 390 395 400

Ile Glu Thr Gly Leu Gly Lys Phe Lys Tyr Ala Gln Lys Asn Asp Glu
405 410 415

Thr Gly Glu Gly Gln Gly Val Val Pro Ala Leu Leu Asp Asp Leu Ala
420 425 430

Lys Phe Arg Lys Leu Ala Lys Lys His Met Ala Glu Ala Lys Arg Asn
435 440 445

Gly Asp Asp Phe Lys Glu Ala Leu Tyr Asp Ala Gln Gln Arg Ser Phe
450 455 460

Lys Val Val Met Asn Ser Val Tyr Gly Phe Leu Gly Ala Ser Lys Gly
465 470 475 480

Phe Ile Pro Cys Val Pro Ile Ala Ala Ser Val Thr Ala Thr Gly Arg
485 490 495

Lys Met Ile Glu His Thr Ala Lys Arg Ala Val Glu Leu Leu Pro Gly
500 505 510

Ser Glu Val Ile Tyr Gly Asp Thr Asp Ser Val Met Val Lys Met Lys
515 520 525

Leu Pro Asp Asp Lys Val His Asp Met Asp Glu Gln Phe Lys Met Ala
530 535 540

Lys Trp Leu Ala Gly Glu Ile Thr Lys Asp Phe Arg Ala Pro Asn Asp
545 550 555 560

Leu Glu Phe Glu Lys Ile Tyr Tyr Pro Tyr Ile Leu Tyr Ser Lys Lys
565 570 575

Arg Tyr Ala Ala Val Lys Phe Glu Glu Pro Asp Glu Lys Gly Lys Val
580 585 590

Asp Val Lys Gly Leu Ala Leu Val Arg Arg Asp Phe Ser Pro Ile Thr
595 600 605

Arg Asp Ile Leu Lys Glu Ser Leu Asp Thr Ile Leu Tyr Lys Lys Asp
610 615 620

Thr Pro Thr Ala Val Ser Glu Thr Leu Glu Arg Ile Arg Lys Val Leu
625 630 635 640

Asp Asn Glu Tyr Pro Met Glu Lys Phe Met Met Ser Lys Leu Leu Lys
645 650 655

Thr Gly Tyr Lys Asn Glu Cys Gln Pro His Leu His Val Ala Asn Lys
660 665 670

Ile Tyr Glu Arg Thr Gly Phe Pro Val Pro Ser Gly Ala Arg Val Pro
675 680 685

Phe Val Tyr Ile Glu Asp Lys Lys Asn Pro Asp Ile Lys Gln Ser Phe
690 695 700

Lys Ala Glu Asp Pro Thr Phe Ala Gln Asp Asn Gly Leu Ile Val Asp
705 710 715 720

Arg Leu Phe Tyr Ile Glu His Gln Leu Leu Lys Pro Ile Cys Ser Leu
725 730 735

Phe Glu Pro Leu Leu Asp Asp
740



14
773
PRT
Epstein-barr virus (strain B95-8)

14

Gly Cys Arg Ile Phe Glu Ala Asn Val Asp Ala Thr Arg Arg Phe Val
1 5 10 15

Leu Asp Asn Asp Phe Val Thr Phe Gly Trp Tyr Ser Cys Arg Arg Ala
20 25 30

Ile Pro Arg Leu Gln His Arg Asp Ser Tyr Ala Glu Leu Glu Tyr Asp
35 40 45

Cys Glu Val Gly Asp Leu Ser Val Arg Arg Glu Asp Ser Ser Trp Pro
50 55 60

Ser Tyr Gln Ala Leu Ala Phe Asp Ile Glu Cys Leu Gly Glu Glu Gly
65 70 75 80

Phe Pro Thr Ala Thr Asn Glu Ala Asp Leu Ile Leu Gln Ile Ser Cys
85 90 95

Val Leu Trp Ser Thr Gly Glu Glu Ala Gly Arg Tyr Arg Arg Ile Leu
100 105 110

Leu Thr Leu Gly Thr Cys Glu Asp Ile Glu Gly Val Glu Val Tyr Glu
115 120 125

Phe Pro Ser Glu Leu Asp Met Leu Tyr Ala Phe Phe Gln Leu Ile Arg
130 135 140

Asp Leu Ser Val Glu Ile Val Thr Gly Tyr Asn Val Ala Asn Phe Asp
145 150 155 160

Trp Pro Tyr Ile Leu Asp Arg Ala Arg His Ile Tyr Ser Ile Asn Pro
165 170 175

Ala Ser Leu Gly Lys Ile Arg Ala Gly Gly Val Cys Glu Val Arg Arg
180 185 190

Pro His Asp Ala Gly Lys Gly Phe Leu Arg Ala Asn Thr Lys Val Arg
195 200 205

Ile Thr Gly Leu Ile Pro Ile Asp Met Tyr Ala Val Cys Arg Asp Lys
210 215 220

Leu Ser Leu Ser Asp Tyr Lys Leu Asp Thr Val Ala Arg His Leu Leu
225 230 235 240

Gly Ala Lys Lys Glu Asp Val His Tyr Lys Glu Ile Pro Arg Leu Phe
245 250 255

Ala Ala Gly Pro Glu Gly Arg Arg Arg Leu Gly Met Tyr Cys Val Gln
260 265 270

Asp Ser Ala Leu Val Met Asp Leu Leu Asn His Phe Val Ile His Val
275 280 285

Glu Val Ala Glu Ile Ala Lys Ile Ala His Ile Pro Cys Arg Arg Val
290 295 300

Leu Asp Asp Gly Gln Gln Ile Arg Val Phe Ser Cys Leu Leu Ala Ala
305 310 315 320

Ala Gln Lys Glu Asn Phe Ile Leu Pro Met Pro Ser Ala Ser Asp Arg
325 330 335

Asp Gly Tyr Gln Gly Ala Thr Val Ile Gln Pro Leu Ser Gly Phe Tyr
340 345 350

Asn Ser Pro Val Leu Val Val Asp Phe Ala Ser Leu Tyr Pro Ser Ile
355 360 365

Ile Gln Ala His Asn Leu Cys Tyr Ser Thr Met Ile Thr Pro Gly Glu
370 375 380

Glu His Arg Leu Ala Gly Leu Arg Pro Gly Glu Asp Tyr Glu Ser Phe
385 390 395 400

Arg Leu Thr Gly Gly Val Tyr His Phe Val Lys Lys His Val His Glu
405 410 415

Ser Phe Leu Ala Ser Leu Leu Thr Ser Trp Leu Ala Lys Arg Lys Ala
420 425 430

Ile Lys Lys Leu Leu Ala Ala Cys Glu Asp Pro Arg Gln Arg Thr Ile
435 440 445

Leu Asp Lys Gln Gln Leu Ala Ile Lys Cys Thr Cys Asn Ala Val Tyr
450 455 460

Gly Phe Thr Gly Val Ala Asn Gly Leu Phe Pro Cys Leu Ser Ile Ala
465 470 475 480

Glu Thr Val Thr Leu Gln Gly Arg Thr Met Leu Glu Arg Ala Lys Ala
485 490 495

Phe Val Glu Ala Leu Ser Pro Ala Asn Leu Gln Ala Leu Ala Pro Ser
500 505 510

Pro Asp Ala Trp Ala Pro Leu Asn Pro Glu Gly Gln Leu Arg Val Ile
515 520 525

Tyr Gly Asp Thr Asp Ser Leu Phe Ile Glu Cys Arg Gly Phe Ser Glu
530 535 540

Ser Glu Thr Leu Arg Phe Ala Asp Ala Leu Ala Ala His Thr Thr Arg
545 550 555 560

Ser Leu Phe Val Ala Pro Ile Ser Leu Glu Ala Glu Lys Thr Phe Ser
565 570 575

Cys Leu Met Leu Ile Thr Lys Lys Arg Tyr Val Gly Val Leu Thr Asp
580 585 590

Gly Lys Thr Leu Met Lys Gly Val Glu Leu Val Arg Lys Thr Ala Cys
595 600 605

Lys Phe Val Gln Thr Arg Cys Arg Arg Val Leu Asp Leu Val Leu Ala
610 615 620

Asp Ala Arg Val Lys Glu Ala Ala Ser Leu Leu Ser His Arg Pro Phe
625 630 635 640

Gln Glu Ser Phe Thr Gln Gly Leu Pro Val Gly Phe Leu Pro Val Ile
645 650 655

Asp Ile Leu Asn Gln Ala Tyr Thr Asp Leu Arg Glu Gly Arg Val Pro
660 665 670

Met Gly Glu Leu Cys Phe Ser Thr Glu Leu Ser Arg Lys Leu Ser Ala
675 680 685

Tyr Lys Ser Thr Gln Met Pro His Leu Ala Val Tyr Gln Lys Phe Val
690 695 700

Glu Arg Asn Glu Glu Leu Pro Gln Ile His Asp Arg Ile Gln Tyr Val
705 710 715 720

Phe Val Glu Pro Lys Gly Gly Val Lys Gly Ala Arg Lys Thr Glu Met
725 730 735

Ala Glu Asp Pro Ala Tyr Ala Glu Arg His Gly Val Pro Val Ala Val
740 745 750

Asp His Tyr Phe Asp Lys Leu Leu Gln Gly Ala Ala Asn Ile Leu Gln
755 760 765

Cys Leu Phe Asp Asn
770



15
764
PRT
Herpesvirus saimiri (strain 11)

15

Gly Cys Glu Val Phe Glu Thr Asn Val Asp Ala Ile Arg Arg Phe Val
1 5 10 15

Ile Asp Asn Asp Phe Ser Thr Phe Gly Trp Tyr Thr Cys Lys Ser Ala
20 25 30

Cys Pro Arg Ile Thr Asn Arg Asp Ser His Thr Asp Ile Glu Phe Asp
35 40 45

Cys Gly Tyr Tyr Asp Leu Glu Phe His Ala Asp Arg Thr Glu Trp Pro
50 55 60

Pro Tyr Asn Ile Met Ser Phe Asp Ile Glu Cys Ile Gly Glu Lys Gly
65 70 75 80

Phe Pro Cys Ala Lys Asn Glu Gly Asp Leu Ile Ile Gln Ile Ser Cys
85 90 95

Val Phe Trp His Ala Gly Ala Leu Asp Thr Thr Arg Asn Met Leu Leu
100 105 110

Ser Leu Gly Thr Cys Ser Ala Val Glu Asn Thr Glu Val Tyr Glu Phe
115 120 125

Pro Ser Glu Ile Asp Met Leu His Gly Phe Phe Ser Leu Ile Arg Asp
130 135 140

Phe Asn Val Glu Ile Ile Thr Gly Tyr Asn Ile Ser Asn Phe Asp Leu
145 150 155 160

Pro Tyr Leu Ile Asp Arg Ala Thr Gln Ile Tyr Asn Ile Lys Leu Ser
165 170 175

Asp Tyr Ser Arg Val Lys Thr Gly Ser Ile Phe Gln Val His Thr Pro
180 185 190

Lys Asp Thr Gly Asn Gly Phe Met Arg Ser Val Ser Lys Ile Lys Ile
195 200 205

Ser Gly Ile Ile Ala Ile Asp Met Tyr Ile Val Cys Lys Asp Lys Leu
210 215 220

Ser Leu Ser Asn Tyr Lys Leu Asp Thr Val Ala Asn His Cys Ile Gly
225 230 235 240

Ala Lys Lys Glu Asp Val Ser Tyr Lys Asp Ile Met Pro Leu Phe Met
245 250 255

Ser Gly Pro Glu Gly Arg Ala Lys Ile Gly Leu Tyr Cys Val Ile Asp
260 265 270

Ser Val Leu Val Met Lys Leu Leu Lys Phe Phe Met Ile His Val Glu
275 280 285

Ile Ser Glu Ile Ala Lys Leu Ala Lys Ile Pro Thr Arg Arg Val Leu
290 295 300

Thr Asp Gly Gln Gln Ile Arg Val Phe Ser Cys Leu Leu Ala Ala Ala
305 310 315 320

Arg Ala Glu Asn Tyr Ile Leu Pro Val Ser Asn Asp Val Asn Ala Asp
325 330 335

Gly Phe Gln Gly Ala Thr Val Ile Asn Pro Ile Pro Gly Phe Tyr Asn
340 345 350

Asn Ala Val Leu Val Val Asp Phe Ala Ser Leu Tyr Pro Ser Ile Ile
355 360 365

Gln Ala His Asn Leu Cys Tyr Ser Thr Leu Ile Pro His His Ala Leu
370 375 380

His Asn Tyr Pro His Leu Lys Ser Ser Asp Tyr Glu Thr Phe Met Leu
385 390 395 400

Ser Ser Gly Pro Ile His Phe Val Lys Lys His Ile Gln Ala Ser Leu
405 410 415

Leu Ser Arg Leu Leu Thr Val Trp Leu Ser Lys Arg Lys Ala Ile Arg
420 425 430

Gln Lys Leu Ala Glu Cys Glu Asp Leu Asp Thr Lys Thr Ile Leu Asp
435 440 445

Lys Gln Gln Leu Ala Ile Lys Val Thr Cys Asn Ala Val Tyr Gly Phe
450 455 460

Thr Gly Val Ala Ser Gly Leu Leu Pro Cys Ile Ser Ile Ala Glu Thr
465 470 475 480

Val Thr Leu Gln Gly Arg Thr Met Leu Glu Lys Ser Lys Ile Phe Ile
485 490 495

Glu Ala Met Thr Pro Asp Thr Leu Gln Glu Ile Val Pro His Ile Val
500 505 510

Lys His Glu Pro Asp Ala Lys Phe Arg Val Ile Tyr Gly Asp Thr Asp
515 520 525

Ser Leu Phe Val Glu Cys Val Gly Tyr Ser Val Asp Thr Val Val Lys
530 535 540

Phe Gly Asp Phe Leu Ala Ala Phe Thr Ser Glu Lys Leu Phe Asn Ala
545 550 555 560

Pro Ile Lys Leu Glu Ser Glu Lys Thr Phe Gln Cys Leu Leu Leu Leu
565 570 575

Ala Lys Lys Arg Tyr Ile Gly Ile Leu Ser Asn Asp Lys Leu Leu Met
580 585 590

Lys Gly Val Asp Leu Val Arg Lys Thr Ala Cys Lys Phe Val Gln Asn
595 600 605

Thr Ser Ser Lys Ile Leu Asn Leu Ile Leu Lys Asp Pro Glu Val Lys
610 615 620

Ala Ala Ala Gln Leu Leu Ser Thr Lys Asp Pro Asp Tyr Ala Phe Arg
625 630 635 640

Glu Gly Leu Pro Asp Gly Phe Leu Lys Val Ile Asp Ile Leu Asn Glu
645 650 655

Ser His Lys Asn Leu Arg Thr Gly Gln Val Pro Val Glu Glu Leu Thr
660 665 670

Phe Ser Thr Glu Leu Ser Arg Pro Ile Ser Ser Tyr Lys Thr Glu Asn
675 680 685

Leu Pro His Leu Thr Val Tyr Lys Lys Ile Ile Thr Arg His Glu Glu
690 695 700

Pro Pro Gln Val His Asp Arg Ile Pro Tyr Val Phe Val Gly Lys Thr
705 710 715 720

Thr Ser Cys Ile Ser Asn Met Ala Glu Asp Pro Thr Tyr Thr Val Gln
725 730 735

Asn Asn Ile Pro Ile Ala Val Asp Leu Tyr Phe Asp Lys Leu Ile His
740 745 750

Gly Val Ala Asn Ile Ile Gln Cys Leu Phe Lys Asp
755 760



16
892
PRT
Herpes simplex virus (type 1/strain 17)

16

Pro Ala Ile Lys Lys Tyr Glu Gly Gly Val Asp Ala Thr Thr Arg Phe
1 5 10 15

Ile Leu Asp Asn Pro Gly Phe Val Thr Phe Gly Trp Tyr Arg Leu Lys
20 25 30

Pro Gly Arg Asn Asn Thr Leu Ala Gln Pro Ala Ala Pro Met Ala Phe
35 40 45

Gly Thr Ser Ser Asp Val Glu Phe Asn Cys Thr Ala Asp Asn Leu Ala
50 55 60

Ile Glu Gly Gly Met Ser Asp Leu Pro Ala Tyr Lys Leu Met Cys Phe
65 70 75 80

Asp Ile Glu Cys Lys Ala Gly Gly Glu Asp Glu Leu Ala Phe Pro Val
85 90 95

Ala Gly His Pro Glu Asp Leu Val Ile Gln Ile Ser Cys Leu Leu Tyr
100 105 110

Asp Leu Ser Thr Thr Ala Leu Glu His Val Leu Leu Phe Ser Leu Gly
115 120 125

Ser Cys Asp Leu Pro Glu Ser His Leu Asn Glu Leu Ala Ala Arg Gly
130 135 140

Leu Pro Thr Pro Val Val Leu Glu Phe Asp Ser Glu Phe Glu Met Leu
145 150 155 160

Leu Ala Phe Met Thr Leu Val Lys Gln Tyr Gly Pro Glu Phe Val Thr
165 170 175

Gly Tyr Asn Ile Ile Asn Phe Asp Trp Pro Phe Leu Leu Ala Lys Leu
180 185 190

Thr Asp Ile Tyr Lys Val Pro Leu Asp Gly Tyr Gly Arg Met Asn Gly
195 200 205

Arg Gly Val Phe Arg Val Trp Asp Ile Gly Gln Ser His Phe Gln Lys
210 215 220

Arg Ser Lys Ile Lys Val Asn Gly Met Val Asn Ile Asp Met Tyr Gly
225 230 235 240

Ile Ile Thr Asp Lys Ile Lys Leu Ser Ser Tyr Lys Leu Asn Ala Val
245 250 255

Ala Glu Ala Val Leu Lys Asp Lys Lys Lys Asp Leu Ser Tyr Arg Asp
260 265 270

Ile Pro Ala Tyr Tyr Ala Ala Gly Pro Ala Gln Arg Gly Val Ile Gly
275 280 285

Glu Tyr Cys Ile Gln Asp Ser Leu Leu Val Gly Gln Leu Phe Phe Lys
290 295 300

Phe Leu Pro His Leu Glu Leu Ser Ala Val Ala Arg Leu Ala Gly Ile
305 310 315 320

Asn Ile Thr Arg Thr Ile Tyr Asp Gly Gln Gln Ile Arg Val Phe Thr
325 330 335

Cys Leu Leu Arg Leu Ala Asp Gln Lys Gly Phe Ile Leu Pro Asp Thr
340 345 350

Gln Gly Arg Phe Arg Gly Ala Gly Gly Glu Ala Pro Lys Arg Pro Ala
355 360 365

Ala Ala Arg Glu Asp Glu Glu Arg Pro Glu Glu Glu Gly Glu Asp Glu
370 375 380

Asp Glu Arg Glu Glu Gly Gly Gly Glu Arg Glu Pro Glu Gly Ala Arg
385 390 395 400

Glu Thr Ala Gly Arg His Val Gly Tyr Gln Gly Ala Arg Val Leu Asp
405 410 415

Pro Thr Ser Gly Phe His Val Asn Pro Val Val Val Phe Asp Phe Ala
420 425 430

Ser Leu Tyr Pro Ser Ile Ile Gln Ala His Asn Leu Cys Phe Ser Thr
435 440 445

Leu Ser Leu Arg Ala Asp Ala Val Ala His Leu Glu Ala Gly Lys Asp
450 455 460

Tyr Leu Glu Ile Glu Val Gly Gly Arg Arg Leu Phe Phe Val Lys Ala
465 470 475 480

His Val Arg Glu Ser Leu Leu Ser Ile Leu Leu Arg Asp Trp Leu Ala
485 490 495

Met Arg Lys Gln Ile Arg Ser Arg Ile Pro Gln Ser Ser Pro Glu Glu
500 505 510

Ala Val Leu Leu Asp Lys Gln Gln Ala Ala Ile Lys Val Val Cys Asn
515 520 525

Ser Val Tyr Gly Phe Thr Gly Val Gln His Gly Leu Leu Pro Cys Leu
530 535 540

His Val Ala Ala Thr Val Thr Thr Ile Gly Arg Glu Met Leu Leu Ala
545 550 555 560

Thr Arg Glu Tyr Val His Ala Arg Trp Ala Ala Phe Glu Gln Leu Leu
565 570 575

Ala Asp Phe Pro Glu Ala Ala Asp Met Arg Ala Pro Gly Pro Tyr Ser
580 585 590

Met Arg Ile Ile Tyr Gly Asp Thr Asp Ser Ile Phe Val Leu Cys Arg
595 600 605

Gly Leu Thr Ala Ala Gly Leu Thr Ala Val Gly Asp Lys Met Ala Ser
610 615 620

His Ile Ser Arg Ala Leu Phe Leu Pro Pro Ile Lys Leu Glu Cys Glu
625 630 635 640

Lys Thr Phe Thr Lys Leu Leu Leu Ile Ala Lys Lys Lys Tyr Ile Gly
645 650 655

Val Ile Tyr Gly Gly Lys Met Leu Ile Lys Gly Val Asp Leu Val Arg
660 665 670

Lys Asn Asn Cys Ala Phe Ile Asn Arg Thr Ser Arg Ala Leu Val Asp
675 680 685

Leu Leu Phe Tyr Asp Asp Thr Val Ser Gly Ala Ala Ala Ala Leu Ala
690 695 700

Glu Arg Pro Ala Glu Glu Trp Leu Ala Arg Pro Leu Pro Glu Gly Leu
705 710 715 720

Gln Ala Phe Gly Ala Val Leu Val Asp Ala His Arg Arg Ile Thr Asp
725 730 735

Pro Glu Arg Asp Ile Gln Asp Phe Val Leu Thr Ala Glu Leu Ser Arg
740 745 750

His Pro Arg Ala Tyr Thr Asn Lys Arg Leu Ala His Leu Thr Val Tyr
755 760 765

Tyr Lys Leu Met Ala Arg Arg Ala Gln Val Pro Ser Ile Lys Asp Arg
770 775 780

Ile Pro Tyr Val Ile Val Ala Gln Thr Arg Glu Val Glu Glu Thr Val
785 790 795 800

Ala Arg Leu Ala Ala Leu Arg Glu Leu Asp Ala Ala Ala Pro Gly Asp
805 810 815

Glu Pro Ala Pro Pro Ala Ala Leu Pro Ser Pro Ala Lys Arg Pro Arg
820 825 830

Glu Thr Pro Ser Pro Ala Asp Pro Pro Gly Gly Ala Ser Lys Pro Arg
835 840 845

Lys Leu Leu Val Ser Glu Leu Ala Glu Asp Pro Ala Tyr Ala Ile Ala
850 855 860

His Gly Val Ala Leu Asn Thr Asp Tyr Tyr Phe Ser His Leu Leu Gly
865 870 875 880

Ala Ala Cys Val Thr Phe Lys Ala Leu Phe Gly Asn
885 890



17
896
PRT
Herpes simplex virus (type 2/strain 186)

17

Pro Ala Ile Arg Lys Tyr Glu Gly Gly Val Asp Ala Thr Thr Arg Phe
1 5 10 15

Ile Leu Asp Asn Pro Gly Phe Val Thr Phe Gly Trp Tyr Arg Leu Lys
20 25 30

Pro Gly Arg Gly Asn Ala Pro Ala Gln Pro Arg Pro Pro Thr Ala Phe
35 40 45

Gly Thr Ser Ser Asp Val Glu Phe Asn Cys Thr Ala Asp Asn Leu Ala
50 55 60

Val Glu Gly Ala Met Cys Asp Leu Pro Ala Tyr Lys Leu Met Cys Phe
65 70 75 80

Asp Ile Glu Cys Lys Ala Gly Gly Glu Asp Glu Leu Ala Phe Pro Val
85 90 95

Ala Glu Arg Pro Glu Asp Leu Val Ile Gln Ile Ser Cys Leu Leu Tyr
100 105 110

Asp Leu Ser Thr Thr Ala Leu Glu His Ile Leu Leu Phe Ser Leu Gly
115 120 125

Ser Cys Asp Leu Pro Glu Ser His Leu Ser Asp Leu Ala Ser Arg Gly
130 135 140

Leu Pro Ala Pro Val Val Leu Glu Phe Asp Ser Glu Phe Glu Met Leu
145 150 155 160

Leu Ala Phe Met Thr Phe Val Lys Gln Tyr Gly Pro Glu Phe Val Thr
165 170 175

Gly Tyr Asn Ile Ile Asn Phe Asp Trp Pro Phe Val Leu Thr Lys Leu
180 185 190

Thr Glu Ile Tyr Lys Val Pro Leu Asp Gly Tyr Gly Arg Met Asn Gly
195 200 205

Arg Gly Val Phe Arg Val Trp Asp Ile Gly Gln Ser His Phe Gln Lys
210 215 220

Arg Ser Lys Ile Lys Val Asn Gly Met Val Asn Ile Asp Met Tyr Gly
225 230 235 240

Ile Ile Thr Asp Lys Val Lys Leu Ser Ser Tyr Lys Leu Asn Ala Val
245 250 255

Ala Glu Ala Val Leu Lys Asp Lys Lys Lys Asp Leu Ser Tyr Arg Asp
260 265 270

Ile Pro Ala Tyr Tyr Ala Ser Gly Pro Ala Gln Arg Gly Val Ile Gly
275 280 285

Glu Tyr Cys Val Gln Asp Ser Leu Leu Val Gly Gln Leu Phe Phe Lys
290 295 300

Phe Leu Pro His Leu Glu Leu Ser Ala Val Ala Arg Leu Ala Gly Ile
305 310 315 320

Asn Ile Thr Arg Thr Ile Tyr Asp Gly Gln Gln Ile Arg Val Phe Thr
325 330 335

Cys Leu Leu Arg Leu Ala Gly Gln Lys Gly Phe Ile Leu Pro Asp Thr
340 345 350

Gln Gly Arg Phe Arg Gly Leu Asp Lys Glu Ala Pro Lys Arg Pro Ala
355 360 365

Val Pro Arg Gly Glu Gly Glu Arg Pro Gly Asp Gly Asn Gly Asp Glu
370 375 380

Asp Lys Asp Asp Asp Glu Asp Gly Asp Glu Asp Gly Asp Glu Arg Glu
385 390 395 400

Glu Val Ala Arg Glu Thr Gly Gly Arg His Val Gly Tyr Gln Gly Ala
405 410 415

Arg Val Leu Asp Pro Thr Ser Gly Phe His Val Asp Pro Val Val Val
420 425 430

Phe Asp Phe Ala Ser Leu Tyr Pro Ser Ile Ile Gln Ala His Asn Leu
435 440 445

Cys Phe Ser Thr Leu Ser Leu Arg Pro Glu Ala Val Ala His Leu Glu
450 455 460

Ala Asp Arg Asp Tyr Leu Glu Ile Glu Val Gly Gly Arg Arg Leu Phe
465 470 475 480

Phe Val Lys Ala His Val Arg Glu Ser Leu Leu Ser Ile Leu Leu Arg
485 490 495

Asp Trp Leu Ala Met Arg Lys Gln Ile Arg Ser Arg Ile Pro Gln Ser
500 505 510

Pro Pro Glu Glu Ala Val Leu Leu Asp Lys Gln Gln Ala Ala Ile Lys
515 520 525

Val Val Cys Asn Ser Val Tyr Gly Phe Thr Gly Val Gln His Gly Leu
530 535 540

Leu Pro Cys Leu His Val Ala Ala Thr Val Thr Thr Ile Gly Arg Glu
545 550 555 560

Met Leu Leu Ala Thr Arg Ala Tyr Val His Ala Arg Trp Ala Glu Phe
565 570 575

Asp Gln Leu Leu Ala Asp Phe Pro Glu Ala Ala Gly Met Arg Ala Pro
580 585 590

Gly Pro Tyr Ser Met Arg Ile Ile Tyr Gly Asp Thr Asp Ser Ile Phe
595 600 605

Val Leu Cys Arg Gly Leu Thr Gly Glu Ala Leu Val Ala Met Gly Asp
610 615 620

Lys Met Ala Ser His Ile Ser Arg Ala Leu Phe Leu Pro Pro Ile Lys
625 630 635 640

Leu Glu Cys Glu Lys Thr Phe Thr Lys Leu Leu Leu Ile Ala Lys Lys
645 650 655

Lys Tyr Ile Gly Val Ile Cys Gly Gly Lys Met Leu Ile Lys Gly Val
660 665 670

Asp Leu Val Arg Lys Asn Asn Cys Ala Phe Ile Asn Arg Thr Ser Arg
675 680 685

Ala Leu Val Asp Leu Leu Phe Tyr Asp Asp Thr Val Ser Gly Ala Ala
690 695 700

Ala Ala Leu Ala Glu Arg Pro Ala Glu Glu Trp Leu Ala Arg Pro Leu
705 710 715 720

Pro Glu Gly Leu Gln Ala Phe Gly Ala Val Leu Val Asp Ala His Arg
725 730 735

Arg Ile Thr Asp Pro Glu Arg Asp Ile Gln Asp Phe Val Leu Thr Ala
740 745 750

Glu Leu Ser Arg His Pro Arg Ala Tyr Thr Asn Lys Arg Leu Ala His
755 760 765

Leu Thr Val Tyr Tyr Lys Leu Met Ala Arg Arg Ala Gln Val Pro Ser
770 775 780

Ile Lys Asp Arg Ile Pro Tyr Val Ile Val Ala Gln Thr Arg Glu Val
785 790 795 800

Glu Glu Thr Val Ala Arg Leu Ala Ala Leu Arg Glu Leu Asp Ala Ala
805 810 815

Ala Pro Gly Asp Glu Pro Ala Pro Pro Ala Ala Leu Pro Ser Pro Ala
820 825 830

Lys Arg Pro Arg Glu Thr Pro Ser His Ala Asp Pro Pro Gly Gly Ala
835 840 845

Ser Lys Pro Arg Lys Leu Leu Val Ser Glu Leu Ala Glu Asp Pro Gly
850 855 860

Tyr Ala Ile Ala Arg Gly Val Pro Leu Asn Thr Asp Tyr Tyr Phe Ser
865 870 875 880

His Leu Leu Gly Ala Ala Cys Val Thr Phe Lys Ala Leu Phe Gly Asn
885 890 895



18
875
PRT
Equine herpesvirus type 1 (strain Ab4p)

18

Pro Glu Ile Thr Lys Phe Glu Gly Ser Val Asp Val Thr Thr Arg Leu
1 5 10 15

Leu Leu Asp Asn Glu Asn Phe Thr Ser Phe Gly Trp Tyr Arg Leu Arg
20 25 30

Pro Gly Thr His Gly Glu Arg Val Gln Leu Arg Pro Val Glu Arg His
35 40 45

Val Thr Ser Ser Asp Val Glu Ile Asn Cys Thr Pro Asp Asn Leu Glu
50 55 60

Pro Ile Pro Asp Glu Ala Ala Trp Pro Asp Tyr Lys Leu Met Cys Phe
65 70 75 80

Asp Ile Glu Cys Lys Ala Gly Thr Gly Asn Glu Met Ala Phe Pro Val
85 90 95

Ala Thr Asn Gln Glu Asp Leu Val Ile Gln Ile Ser Cys Leu Leu Tyr
100 105 110

Ser Leu Ala Thr Gln Asn His Glu His Thr Leu Leu Phe Ser Leu Gly
115 120 125

Ser Cys Asp Ile Ser Glu Glu Tyr Ser Phe Ala Cys Val Gln Arg Gly
130 135 140

Glu Pro Arg Pro Thr Val Leu Glu Phe Asp Ser Glu Tyr Glu Leu Leu
145 150 155 160

Val Ala Phe Leu Thr Phe Leu Lys Gln Tyr Ser Pro Glu Phe Ala Thr
165 170 175

Gly Tyr Asn Ile Val Asn Phe Asp Trp Ala Tyr Ile Val Asn Lys Val
180 185 190

Thr Ser Val Tyr Asn Ile Lys Leu Asp Gly Tyr Gly Lys Phe Asn Lys
195 200 205

Gly Gly Leu Phe Lys Val Trp Asp Ile Ala Thr Asn His Phe Gln Lys
210 215 220

Lys Ser Lys Val Lys Ile Asn Gly Leu Ile Ser Leu Asp Met Tyr Ser
225 230 235 240

Val Ala Thr Glu Lys Leu Lys Leu Pro Ser Tyr Lys Leu Asp Ala Val
245 250 255

Val Gly Asp Val Leu Gly Glu His Lys Ile Asp Leu Pro Tyr Lys Glu
260 265 270

Ile Pro Ser Tyr Tyr Ala Gly Gly Pro Asp Arg Arg Gly Val Ile Gly
275 280 285

Glu Tyr Cys Ile Gln Asp Ser Arg Leu Val Gly Lys Leu Phe Phe Lys
290 295 300

Tyr Leu Pro His Leu Glu Leu Ser Ala Val Ala Lys Leu Ala Arg Ile
305 310 315 320

Thr Leu Thr Arg Val Ile Phe Asp Gly Gln Gln Ile Arg Val Tyr Thr
325 330 335

Cys Leu Leu Lys Leu Ala Arg Glu Arg Asn Phe Ile Leu Pro Asp Asn
340 345 350

Arg Arg Arg Phe Asp Ser Gln Ala Asp Ala Ala Ser Glu Thr Ser Glu
355 360 365

Leu Ala Met Asp Ser Gln Ser His Ala Phe Asp Ser Thr Asp Glu Pro
370 375 380

Asp Gly Val Asp Gly Thr Pro Asp Ala Ala Gly Ser Gly Ala Thr Ser
385 390 395 400

Glu Asn Gly Gly Gly Lys Pro Gly Val Gly Arg Ala Val Gly Tyr Gln
405 410 415

Gly Ala Lys Val Leu Asp Pro Val Ser Gly Phe His Val Asp Pro Val
420 425 430

Val Val Phe Asp Phe Ala Ser Leu Tyr Pro Ser Ile Ile Gln Ala His
435 440 445

Asn Leu Cys Phe Thr Thr Leu Ala Leu Asp Glu Val Asp Leu Ala Gly
450 455 460

Leu Gln Pro Ser Val Asp Tyr Ser Thr Phe Glu Val Gly Asp Gln Lys
465 470 475 480

Leu Phe Phe Val His Ala His Ile Arg Glu Ser Leu Leu Gly Ile Leu
485 490 495

Leu Arg Asp Trp Leu Ala Met Arg Lys Ala Val Arg Ala Arg Ile Pro
500 505 510

Thr Ser Thr Pro Glu Glu Ala Val Leu Leu Asp Lys Gln Gln Ser Ala
515 520 525

Ile Lys Val Ile Cys Asn Ser Val Tyr Gly Phe Thr Gly Val Ala Asn
530 535 540

Gly Leu Leu Pro Cys Leu Arg Ile Ala Ala Thr Val Thr Thr Ile Gly
545 550 555 560

Arg Asp Met Leu Leu Lys Thr Arg Asp Tyr Val His Ser Arg Trp Ala
565 570 575

Thr Arg Glu Leu Leu Glu Asp Asn Phe Pro Gly Ala Ile Gly Phe Arg
580 585 590

Asn His Lys Pro Tyr Ser Val Arg Val Ile Tyr Gly Asp Thr Asp Ser
595 600 605

Val Phe Ile Lys Phe Val Gly Leu Thr Tyr Glu Gly Val Ser Glu Leu
610 615 620

Gly Asp Ala Met Ser Arg Gln Ile Ser Ala Asp Leu Phe Arg Ala Pro
625 630 635 640

Ile Lys Leu Glu Cys Glu Lys Thr Phe Gln Arg Leu Leu Leu Ile Thr
645 650 655

Lys Lys Lys Tyr Ile Gly Val Ile Asn Gly Gly Lys Met Leu Met Lys
660 665 670

Gly Val Asp Leu Val Arg Lys Asn Asn Cys Ser Phe Ile Asn Leu Tyr
675 680 685

Ala Arg His Leu Val Asp Leu Leu Leu Tyr Asp Glu Asp Val Ala Thr
690 695 700

Ala Ala Ala Glu Val Thr Asp Val Pro Pro Ala Glu Trp Val Gly Arg
705 710 715 720

Pro Leu Pro Ser Gly Phe Asp Lys Phe Gly Arg Val Leu Val Glu Ala
725 730 735

Tyr Asn Arg Ile Thr Ala Pro Asn Leu Asp Val Arg Glu Phe Val Met
740 745 750

Thr Ala Glu Leu Ser Arg Ser Pro Glu Ser Tyr Thr Asn Lys Arg Leu
755 760 765

Pro His Leu Thr Val Tyr Phe Lys Leu Ala Met Arg Asn Glu Glu Leu
770 775 780

Pro Ser Val Lys Glu Arg Ile Pro Tyr Val Ile Val Ala Gln Thr Glu
785 790 795 800

Ala Ala Glu Arg Glu Ala Gly Val Val Asn Ser Met Arg Gly Thr Ala
805 810 815

Gln Asn Pro Val Val Thr Lys Thr Ala Arg Pro Gln Pro Lys Arg Lys
820 825 830

Leu Leu Val Ser Asp Leu Ala Glu Asp Pro Thr Tyr Val Ser Glu Asn
835 840 845

Asp Val Pro Leu Asn Thr Asp Tyr Tyr Phe Ser His Leu Leu Gly Thr
850 855 860

Ile Ser Val Thr Phe Lys Ala Leu Phe Gly Asn
865 870 875



19
852
PRT
Varicella-zoster virus (strain Dumas)

19

Pro Glu Leu Lys Lys Tyr Glu Gly Arg Val Asp Ala Thr Thr Arg Phe
1 5 10 15

Leu Met Asp Asn Pro Gly Phe Val Ser Phe Gly Trp Tyr Gln Leu Lys
20 25 30

Pro Gly Val Asp Gly Glu Arg Val Arg Val Arg Pro Ala Ser Arg Gln
35 40 45

Leu Thr Leu Ser Asp Val Glu Ile Asp Cys Met Ser Asp Asn Leu Gln
50 55 60

Ala Ile Pro Asn Asp Asp Ser Trp Pro Asp Tyr Lys Leu Leu Cys Phe
65 70 75 80

Asp Ile Glu Cys Lys Ser Gly Gly Ser Asn Glu Leu Ala Phe Pro Asp
85 90 95

Ala Thr His Leu Glu Asp Leu Val Ile Gln Ile Ser Cys Leu Leu Tyr
100 105 110

Ser Ile Pro Arg Gln Ser Leu Glu His Ile Leu Leu Phe Ser Leu Gly
115 120 125

Ser Cys Asp Leu Pro Gln Arg Tyr Val Gln Glu Met Lys Asp Ala Gly
130 135 140

Leu Pro Glu Pro Thr Val Leu Glu Phe Asp Ser Glu Phe Glu Leu Leu
145 150 155 160

Ile Ala Phe Met Thr Leu Val Lys Gln Tyr Ala Pro Glu Phe Ala Thr
165 170 175

Gly Tyr Asn Ile Val Asn Phe Asp Trp Ala Phe Ile Met Glu Lys Leu
180 185 190

Asn Ser Ile Tyr Ser Leu Lys Leu Asp Gly Tyr Gly Ser Ile Asn Arg
195 200 205

Gly Gly Leu Phe Lys Ile Trp Asp Val Gly Lys Ser Gly Phe Gln Arg
210 215 220

Arg Ser Lys Val Lys Ile Asn Gly Leu Ile Ser Leu Asp Met Tyr Ala
225 230 235 240

Ile Ala Thr Glu Lys Leu Lys Leu Ser Ser Tyr Lys Leu Asp Ser Val
245 250 255

Ala Arg Glu Ala Leu Asn Glu Ser Lys Arg Asp Leu Pro Tyr Lys Asp
260 265 270

Ile Pro Gly Tyr Tyr Ala Ser Gly Pro Asn Thr Arg Gly Ile Ile Gly
275 280 285

Glu Tyr Cys Ile Gln Asp Ser Ala Leu Val Gly Lys Leu Phe Phe Lys
290 295 300

Tyr Leu Pro His Leu Glu Leu Ser Ala Val Ala Arg Leu Ala Arg Ile
305 310 315 320

Thr Leu Thr Lys Ala Ile Tyr Asp Gly Gln Gln Val Arg Ile Tyr Thr
325 330 335

Cys Leu Leu Gly Leu Ala Ser Ser Arg Gly Phe Ile Leu Pro Asp Gly
340 345 350

Gly Tyr Pro Ala Thr Phe Glu Tyr Lys Asp Val Ile Pro Asp Val Gly
355 360 365

Asp Val Glu Glu Glu Met Asp Glu Asp Glu Ser Val Ser Pro Thr Gly
370 375 380

Thr Ser Ser Gly Arg Asn Val Gly Tyr Lys Gly Ala Arg Val Phe Asp
385 390 395 400

Pro Asp Thr Gly Phe Tyr Ile Asp Pro Val Val Val Leu Asp Phe Ala
405 410 415

Ser Leu Tyr Pro Ser Ile Ile Gln Ala His Asn Leu Cys Phe Thr Thr
420 425 430

Leu Thr Leu Asn Phe Glu Thr Val Lys Arg Leu Asn Pro Ser Asp Tyr
435 440 445

Ala Thr Phe Thr Val Gly Gly Lys Arg Leu Phe Phe Val Arg Ser Asn
450 455 460

Val Arg Glu Ser Leu Leu Gly Val Leu Leu Lys Asp Trp Leu Ala Met
465 470 475 480

Arg Lys Ala Ile Arg Ala Arg Ile Pro Gly Ser Ser Ser Asp Glu Ala
485 490 495

Val Leu Leu Asp Lys Gln Gln Ala Ala Ile Lys Val Val Cys Asn Ser
500 505 510

Val Tyr Gly Phe Thr Gly Val Ala Gln Gly Phe Leu Pro Cys Leu Tyr
515 520 525

Val Ala Ala Thr Val Thr Thr Ile Gly Arg Gln Met Leu Leu Ser Thr
530 535 540

Arg Asp Tyr Ile His Asn Asn Trp Ala Ala Phe Glu Arg Phe Ile Thr
545 550 555 560

Ala Phe Pro Asp Ile Glu Ser Ser Val Leu Ser Gln Lys Ala Tyr Glu
565 570 575

Val Lys Val Ile Tyr Gly Asp Thr Asp Ser Val Phe Ile Arg Phe Lys
580 585 590

Gly Val Ser Val Glu Gly Ile Ala Lys Ile Gly Glu Lys Met Ala His
595 600 605

Ile Ile Ser Thr Ala Leu Phe Cys Pro Pro Ile Lys Leu Glu Cys Glu
610 615 620

Lys Thr Phe Ile Lys Leu Leu Leu Ile Thr Lys Lys Lys Tyr Ile Gly
625 630 635 640

Val Ile Tyr Gly Gly Lys Val Leu Met Lys Gly Val Asp Leu Val Arg
645 650 655

Lys Asn Asn Cys Gln Phe Ile Asn Asp Tyr Ala Arg Lys Leu Val Glu
660 665 670

Leu Leu Leu Tyr Asp Asp Thr Val Ser Arg Ala Ala Ala Glu Ala Ser
675 680 685

Cys Val Ser Ile Ala Glu Trp Asn Arg Arg Ala Met Pro Ser Gly Met
690 695 700

Ala Gly Phe Gly Arg Ile Ile Ala Asp Ala His Arg Gln Ile Thr Ser
705 710 715 720

Pro Lys Leu Asp Ile Asn Lys Phe Val Met Thr Ala Glu Leu Ser Arg
725 730 735

Pro Pro Ser Ala Tyr Ile Asn Arg Arg Leu Ala His Leu Thr Val Tyr
740 745 750

Tyr Lys Leu Val Met Arg Gln Gly Gln Ile Pro Asn Val Arg Glu Arg
755 760 765

Ile Pro Tyr Val Ile Val Ala Pro Thr Asp Glu Val Glu Ala Asp Ala
770 775 780

Lys Ser Val Ala Leu Leu Arg Gly Asp Pro Leu Gln Asn Thr Ala Gly
785 790 795 800

Lys Arg Cys Gly Glu Ala Lys Arg Lys Leu Ile Ile Ser Asp Leu Ala
805 810 815

Glu Asp Pro Ile His Val Thr Ser His Gly Leu Ser Leu Asn Ile Asp
820 825 830

Tyr Tyr Phe Ser His Leu Ile Gly Thr Ala Ser Val Thr Phe Lys Ala
835 840 845

Leu Phe Gly Asn
850



20
978
PRT
Human cytomegalovirus (strain AD169)

20

Gly Phe Pro Val Tyr Glu Val Arg Val Asp Pro Leu Thr Arg Leu Val
1 5 10 15

Ile Asp Arg Arg Ile Thr Thr Phe Gly Trp Cys Ser Val Asn Arg Tyr
20 25 30

Asp Trp Arg Gln Gln Gly Arg Ala Ser Thr Cys Asp Ile Glu Val Asp
35 40 45

Cys Asp Val Ser Asp Leu Val Ala Val Pro Asp Asp Ser Ser Trp Pro
50 55 60

Arg Tyr Arg Cys Leu Ser Phe Asp Ile Glu Cys Met Ser Gly Glu Gly
65 70 75 80

Gly Phe Pro Cys Ala Glu Lys Ser Asp Asp Ile Val Ile Gln Ile Ser
85 90 95

Cys Val Cys Tyr Glu Thr Gly Gly Asn Thr Ala Val Asp Gln Gly Ile
100 105 110

Pro Asn Gly Asn Asp Gly Arg Gly Cys Thr Ser Glu Gly Val Ile Phe
115 120 125

Gly His Ser Gly Leu His Leu Phe Thr Ile Gly Thr Cys Gly Gln Val
130 135 140

Gly Pro Asp Val Asp Val Tyr Glu Phe Pro Ser Glu Tyr Glu Leu Leu
145 150 155 160

Leu Gly Phe Met Leu Phe Phe Gln Arg Tyr Ala Pro Ala Phe Val Thr
165 170 175

Gly Tyr Asn Ile Asn Ser Phe Asp Leu Lys Tyr Ile Leu Thr Arg Leu
180 185 190

Glu Tyr Leu Tyr Lys Val Asp Ser Gln Arg Phe Cys Lys Leu Pro Thr
195 200 205

Ala Gln Gly Gly Arg Phe Phe Leu His Ser Pro Ala Val Gly Phe Lys
210 215 220

Arg Gln Tyr Ala Ala Ala Phe Pro Ser Ala Ser His Asn Asn Pro Ala
225 230 235 240

Ser Thr Ala Ala Thr Lys Val Tyr Ile Ala Gly Ser Val Val Ile Asp
245 250 255

Met Tyr Pro Val Cys Met Ala Lys Thr Asn Ser Pro Asn Tyr Lys Leu
260 265 270

Asn Thr Met Ala Glu Leu Tyr Leu Arg Gln Arg Lys Asp Asp Leu Ser
275 280 285

Tyr Lys Asp Ile Pro Arg Cys Phe Val Ala Asn Ala Glu Gly Arg Ala
290 295 300

Gln Val Gly Arg Tyr Cys Leu Gln Asp Ala Val Leu Val Arg Asp Leu
305 310 315 320

Phe Asn Thr Ile Asn Phe His Tyr Glu Ala Gly Ala Ile Ala Arg Leu
325 330 335

Ala Lys Ile Pro Leu Arg Arg Val Ile Phe Asp Gly Gln Gln Ile Arg
340 345 350

Ile Tyr Thr Ser Leu Leu Asp Glu Cys Ala Cys Arg Asp Phe Ile Leu
355 360 365

Pro Asn His Tyr Ser Lys Gly Thr Thr Val Pro Glu Thr Asn Ser Val
370 375 380

Ala Val Ser Pro Asn Ala Ala Ile Ile Ser Thr Ala Ala Val Pro Gly
385 390 395 400

Asp Ala Gly Ser Val Ala Ala Met Phe Gln Met Ser Pro Pro Leu Gln
405 410 415

Ser Ala Pro Ser Ser Gln Asp Gly Val Ser Pro Gly Ser Gly Ser Asn
420 425 430

Ser Ser Ser Ser Val Gly Val Phe Ser Val Gly Ser Gly Ser Ser Gly
435 440 445

Gly Val Gly Val Ser Asn Asp Asn His Gly Ala Gly Gly Thr Ala Ala
450 455 460

Val Ser Tyr Gln Gly Ala Thr Val Phe Glu Pro Glu Val Gly Tyr Tyr
465 470 475 480

Asn Asp Pro Val Ala Val Phe Asp Phe Ala Ser Leu Tyr Pro Ser Ile
485 490 495

Ile Met Ala His Asn Leu Cys Tyr Ser Thr Leu Leu Val Pro Gly Gly
500 505 510

Glu Tyr Pro Val Asp Pro Ala Asp Val Tyr Ser Val Thr Leu Glu Asn
515 520 525

Gly Val Thr His Arg Phe Val Arg Ala Ser Val Arg Val Ser Val Leu
530 535 540

Ser Glu Leu Leu Asn Lys Trp Val Ser Gln Arg Arg Ala Val Arg Glu
545 550 555 560

Cys Met Arg Glu Cys Gln Asp Pro Val Arg Arg Met Leu Leu Asp Lys
565 570 575

Glu Gln Met Ala Leu Lys Val Thr Cys Asn Ala Phe Tyr Gly Phe Thr
580 585 590

Gly Val Val Asn Gly Met Met Pro Cys Leu Pro Ile Ala Ala Ser Ile
595 600 605

Thr Arg Ile Gly Arg Asp Met Leu Glu Arg Thr Ala Arg Phe Ile Lys
610 615 620

Asp Asn Phe Ser Glu Pro Cys Phe Leu His Asn Phe Phe Asn Gln Glu
625 630 635 640

Asp Tyr Val Val Gly Thr Arg Glu Gly Asp Ser Glu Glu Ser Ser Ala
645 650 655

Leu Pro Glu Gly Leu Glu Thr Ser Ser Gly Gly Ser Asn Glu Arg Arg
660 665 670

Val Glu Ala Arg Val Ile Tyr Gly Asp Thr Asp Ser Val Phe Val Arg
675 680 685

Phe Arg Gly Leu Thr Pro Gln Ala Leu Val Ala Arg Gly Pro Ser Leu
690 695 700

Ala His Tyr Val Thr Ala Cys Leu Phe Val Glu Pro Val Lys Leu Glu
705 710 715 720

Phe Glu Lys Val Phe Val Ser Leu Met Met Ile Cys Lys Lys Arg Tyr
725 730 735

Ile Gly Lys Val Glu Gly Ala Ser Gly Leu Ser Met Lys Gly Val Asp
740 745 750

Leu Val Arg Lys Thr Ala Cys Glu Phe Val Lys Gly Val Thr Arg Asp
755 760 765

Val Leu Ser Leu Leu Phe Glu Asp Arg Glu Val Ser Glu Ala Ala Val
770 775 780

Arg Leu Ser Arg Leu Ser Leu Asp Glu Val Lys Lys Tyr Gly Val Pro
785 790 795 800

Arg Gly Phe Trp Arg Ile Leu Arg Arg Leu Val Gln Ala Arg Asp Asp
805 810 815

Leu Tyr Leu His Arg Val Arg Val Glu Asp Leu Val Leu Ser Ser Val
820 825 830

Leu Ser Lys Asp Ile Ser Leu Tyr Arg Gln Ser Asn Leu Pro His Ile
835 840 845

Ala Val Ile Lys Arg Leu Ala Ala Arg Ser Glu Glu Leu Pro Ser Val
850 855 860

Gly Asp Arg Val Phe Tyr Val Leu Thr Ala Pro Gly Val Arg Thr Ala
865 870 875 880

Pro Gln Gly Ser Ser Asp Asn Gly Asp Ser Val Thr Ala Gly Val Val
885 890 895

Ser Arg Ser Asp Ala Ile Asp Gly Thr Asp Asp Asp Ala Asp Gly Gly
900 905 910

Gly Val Glu Glu Ser Asn Arg Arg Gly Gly Glu Pro Ala Lys Lys Arg
915 920 925

Ala Arg Lys Pro Pro Ser Ala Val Cys Asn Tyr Glu Val Ala Glu Asp
930 935 940

Pro Ser Tyr Val Arg Glu His Gly Val Pro Ile His Ala Asp Lys Tyr
945 950 955 960

Phe Glu Gln Val Leu Lys Ala Val Thr Asn Val Leu Ser Pro Val Phe
965 970 975

Pro Gly



21
814
PRT
Murine cytomegalovirus (strain Smith)

21

Gly Arg Lys Val Tyr Glu Leu Gly Val Asp Pro Leu Ala Arg Phe Leu
1 5 10 15

Ile Asp Arg Lys Ile Pro Ser Phe Gly Trp Cys Leu Ala Arg Arg Tyr
20 25 30

Ser Val Arg Ala Ala Gly Tyr Val Ser Arg Ala Gln Leu Glu Ile Asp
35 40 45

Cys Asp Val Ala Asp Ile Leu Pro Ile Glu Glu Gln Ser Asn Trp Pro
50 55 60

Phe Tyr Arg Cys Leu Ser Phe Asp Ile Glu Cys Met Ser Gly Thr Gly
65 70 75 80

Ala Phe Pro Ala Ala Glu Asn Val Asp Asp Ile Ile Ile Gln Ile Ser
85 90 95

Cys Val Cys Phe Gly Val Gly Glu Met Val His His Ala Tyr Asp Val
100 105 110

His Ala Asp Leu Ser Thr Pro Ala Val Pro Glu Asn His Leu Phe Thr
115 120 125

Ile Gly Pro Cys Ala Pro Ile Pro Asp Val Lys Ile Tyr Thr Phe Pro
130 135 140

Ser Glu Tyr Glu Met Leu Arg Gly Phe Phe Ile Phe Leu Ser Trp Tyr
145 150 155 160

Ser Pro Glu Phe Ile Thr Gly Tyr Asn Ile Asn Gly Phe Asp Ile Lys
165 170 175

Tyr Ile Leu Thr Arg Ala Glu Lys Leu Tyr Lys Met Asp Val Gly Gln
180 185 190

Phe Thr Lys Leu Arg Arg Gly Gly Arg Met Phe Val Phe Ser Pro Glu
195 200 205

Lys Gly Lys Ala Gly Phe Gly Thr Ser Asn Thr Val Lys Val Phe Trp
210 215 220

Ser Gly Thr Val Val Leu Asp Met Tyr Pro Val Cys Thr Ala Lys Ala
225 230 235 240

Ser Ser Pro Asn Tyr Lys Leu Asp Thr Met Ala Glu Ile Tyr Leu Lys
245 250 255

Lys Lys Lys Asp Asp Leu Ser Tyr Lys Glu Ile Pro Val Gln Phe Ser
260 265 270

Ala Gly Asp Glu Gly Arg Ala Pro Gly Gly Lys Tyr Cys Leu Gln Asp
275 280 285

Ala Val Leu Val Arg Glu Leu Phe Glu Met Leu Ala Phe His Phe Glu
290 295 300

Ala Ala Ala Ile Ala Arg Leu Ala Arg Ile Pro Leu Arg Lys Val Ile
305 310 315 320

Phe Asp Gly Gln Gln Ile Arg Ile Tyr Thr Cys Leu Leu Glu Glu Cys
325 330 335

Ser Gly Arg Asp Met Ile Leu Pro Asn Met Pro Ser Leu Gly His Gly
340 345 350

Ala Ala Ala Ala Ile Glu Glu Ala Ala Ala Gly Gly Glu Gly Asp Glu
355 360 365

Thr Ser Glu Gly Glu Asn Ser Asn Asn Ser Arg Thr Val Gly Tyr Gln
370 375 380

Gly Ala Thr Val Leu Glu Pro Glu Cys Gly Phe His His Val Pro Val
385 390 395 400

Cys Val Phe Asp Phe Ala Ser Leu Tyr Pro Ser Ile Ile Met Ser Asn
405 410 415

Asn Leu Cys Tyr Ser Thr Leu Leu Val Glu Gly Ser Pro Glu Val Pro
420 425 430

Glu Lys Asp Val Leu Arg Val Glu Ile Gly Asp Gln Cys His Arg Phe
435 440 445

Val Arg Glu Asn Val His Arg Ser Leu Leu Ala Glu Leu Leu Val Arg
450 455 460

Trp Leu Thr Gln Arg Lys Leu Val Arg Glu Ala Met Lys Gln Cys Thr
465 470 475 480

Asn Glu Met Gln Arg Met Ile Met Asp Lys Gln Gln Leu Ala Leu Lys
485 490 495

Val Thr Cys Asn Ala Phe Tyr Gly Phe Thr Gly Val Ala Ala Gly Met
500 505 510

Leu Pro Cys Leu Pro Ile Ala Ala Ser Ile Thr Lys Ile Gly Arg Asp
515 520 525

Met Leu Leu Ala Thr Ala Gly His Ile Glu Asp Arg Cys Asn Arg Pro
530 535 540

Asp Phe Leu Arg Thr Val Leu Gly Leu Pro Pro Glu Ala Ile Asp Pro
545 550 555 560

Glu Ala Leu Arg Val Lys Ile Ile Tyr Gly Asp Thr Asp Ser Val Phe
565 570 575

Ala Ala Phe Tyr Gly Ile Asp Lys Glu Ala Leu Leu Lys Ala Val Gly
580 585 590

Ala Leu Ala Ala Asn Val Thr Asn Ala Leu Phe Lys Glu Pro Val Arg
595 600 605

Leu Glu Phe Glu Lys Met Phe Val Ser Leu Met Met Ile Cys Lys Lys
610 615 620

Arg Tyr Ile Gly Lys Val His Gly Ser Gln Asn Leu Ser Met Lys Gly
625 630 635 640

Val Asp Leu Val Arg Arg Thr Ala Cys Gly Phe Val Lys Ala Val Val
645 650 655

Ser Asp Val Leu His Met Val Phe Asn Asp Glu Thr Val Ser Glu Gly
660 665 670

Thr Met Lys Leu Ser Arg Met Thr Phe Asp Asp Leu Lys Lys Asn Gly
675 680 685

Ile Pro Cys Glu Phe Gly Pro Val Val Ser Arg Leu Cys Arg Ala Arg
690 695 700

Asp Asp Leu His Leu Lys Lys Val Pro Val Pro Glu Leu Thr Leu Ser
705 710 715 720

Ser Val Leu Ser Gln Glu Leu Ser Cys Tyr Lys Gln Lys Asn Leu Pro
725 730 735

His Leu Ala Val Ile Arg Arg Leu Ala Ala Arg Lys Glu Glu Leu Pro
740 745 750

Ala Val Gly Asp Arg Val Glu Tyr Val Leu Thr Leu Pro Asp Gly Cys
755 760 765

Lys Lys Asn Val Pro Asn Tyr Glu Ile Ala Glu Asp Pro Arg His Val
770 775 780

Val Glu Ala Lys Leu Ser Ile Asn Ala Glu Lys Tyr Tyr Glu Gln Val
785 790 795 800

Val Lys Ala Val Thr Asn Thr Leu Met Pro Val Phe Pro Arg
805 810



22
771
PRT
Herpes simplex virus type 6/strain Uganda-1102

22

Gly Phe Val Val Tyr Glu Ile Asp Val Asp Val Leu Thr Arg Phe Phe
1 5 10 15

Val Asp Asn Gly Phe Leu Ser Phe Gly Trp Tyr Asn Val Lys Lys Tyr
20 25 30

Ile Pro Gln Asp Met Gly Lys Gly Ser Asn Leu Glu Val Glu Ile Asn
35 40 45

Cys His Val Ser Asp Leu Val Ser Leu Glu Asp Val Asn Trp Pro Leu
50 55 60

Tyr Gly Cys Trp Ser Phe Asp Ile Glu Cys Leu Gly Gln Asn Gly Asn
65 70 75 80

Phe Pro Asp Ala Glu Asn Leu Gly Asp Ile Val Ile Gln Ile Ser Val
85 90 95

Ile Ser Phe Asp Thr Glu Gly Asp Arg Asp Glu Arg His Leu Phe Thr
100 105 110

Leu Gly Thr Cys Glu Lys Ile Asp Gly Val His Ile Tyr Glu Phe Ala
115 120 125

Ser Glu Phe Glu Leu Leu Leu Gly Phe Phe Ile Phe Leu Arg Ile Glu
130 135 140

Ser Pro Glu Phe Ile Thr Gly Tyr Asn Ile Asn Asn Phe Asp Leu Lys
145 150 155 160

Tyr Leu Cys Ile Arg Met Asp Lys Ile Tyr His Tyr Asp Ile Gly Cys
165 170 175

Phe Ser Lys Leu Lys Asn Gly Lys Ile Gly Ile Ser Val Pro His Glu
180 185 190

Gln Tyr Arg Lys Gly Phe Leu Gln Ala Gln Thr Lys Val Phe Thr Ser
195 200 205

Gly Val Leu Tyr Leu Asp Met Tyr Pro Val Tyr Ser Ser Lys Ile Thr
210 215 220

Ala Gln Asn Tyr Lys Leu Asp Thr Ile Ala Lys Ile Cys Leu Gln Gln
225 230 235 240

Glu Lys Glu Gln Leu Ser Tyr Lys Glu Ile Pro Lys Lys Phe Ile Ser
245 250 255

Gly Pro Ser Gly Arg Ala Val Val Gly Lys Tyr Cys Leu Gln Asp Ser
260 265 270

Val Leu Val Val Arg Leu Phe Lys Gln Ile Asn Tyr His Phe Glu Val
275 280 285

Ala Glu Val Ala Arg Leu Ala His Val Thr Ala Arg Cys Val Val Phe
290 295 300

Glu Gly Gln Gln Lys Lys Ile Phe Pro Cys Ile Leu Thr Glu Ala Lys
305 310 315 320

Arg Arg Asn Met Ile Leu Pro Ser Met Val Ser Ser His Asn Arg Gln
325 330 335

Gly Ile Gly Tyr Lys Gly Ala Thr Val Leu Glu Pro Lys Thr Gly Tyr
340 345 350

Tyr Ala Val Pro Thr Val Val Phe Asp Phe Gln Ser Leu Tyr Pro Ser
355 360 365

Ile Met Met Ala His Asn Leu Cys Tyr Ser Thr Leu Val Leu Asp Glu
370 375 380

Arg Gln Ile Ala Gly Leu Ser Glu Ser Asp Ile Leu Thr Val Lys Leu
385 390 395 400

Gly Asp Glu Thr His Arg Phe Val Lys Pro Cys Ile Arg Glu Ser Val
405 410 415

Leu Gly Ser Leu Leu Lys Asp Trp Leu Ala Lys Arg Arg Glu Val Lys
420 425 430

Ala Glu Met Gln Asn Cys Ser Asp Pro Met Met Lys Leu Leu Leu Asp
435 440 445

Lys Lys Gln Leu Ala Leu Lys Thr Thr Cys Asn Ser Val Tyr Gly Val
450 455 460

Thr Gly Ala Ala His Gly Leu Leu Pro Cys Val Ala Ile Ala Ala Ser
465 470 475 480

Val Thr Cys Leu Gly Arg Glu Met Leu Cys Ser Thr Val Asp Tyr Val
485 490 495

Asn Ser Lys Met Gln Ser Glu Gln Phe Phe Cys Glu Glu Phe Gly Leu
500 505 510

Thr Ser Ser Asp Phe Thr Gly Asp Leu Glu Val Glu Val Ile Tyr Gly
515 520 525

Asp Thr Asp Ser Ile Phe Met Ser Val Arg Asn Met Val Asn Gln Ser
530 535 540

Leu Arg Arg Ile Ala Pro Met Ile Ala Lys His Ile Thr Asp Arg Leu
545 550 555 560

Phe Lys Ser Pro Ile Lys Leu Glu Phe Glu Lys Ile Leu Cys Pro Leu
565 570 575

Ile Leu Ile Cys Lys Lys Arg Tyr Ile Gly Arg Gln Asp Asp Ser Leu
580 585 590

Leu Ile Phe Lys Gly Val Asp Leu Val Arg Lys Thr Ser Cys Asp Phe
595 600 605

Val Lys Gly Val Val Lys Asp Ile Val Asp Leu Leu Phe Phe Asp Glu
610 615 620

Glu Val Gln Thr Ala Ala Val Glu Phe Ser His Met Thr Gln Thr Gln
625 630 635 640

Leu Arg Glu Gln Gly Val Pro Val Gly Ile His Lys Ile Leu Arg Arg
645 650 655

Leu Cys Glu Ala Arg Glu Glu Leu Phe Gln Asn Arg Ala Asp Val Arg
660 665 670

His Leu Met Leu Ser Ser Val Leu Ser Lys Glu Met Ala Ala Tyr Lys
675 680 685

Gln Pro Asn Leu Ala His Leu Ser Val Ile Arg Arg Leu Ala Gln Arg
690 695 700

Lys Glu Glu Ile Pro Asn Val Gly Asp Arg Ile Met Tyr Val Leu Ile
705 710 715 720

Ala Pro Ser Ile Gly Asn Lys Gln Thr His Asn Tyr Glu Leu Ala Glu
725 730 735

Asp Pro Asn Tyr Val Ile Glu His Lys Ile Pro Ile His Ala Glu Lys
740 745 750

Tyr Phe Asp Gln Ile Ile Lys Ala Val Thr Asn Ala Ile Ser Pro Ile
755 760 765

Phe Pro Lys
770



23
757
PRT
Homo sapiens

23

Ser His Val Phe Gly Thr Asn Thr Ser Ser Leu Glu Leu Phe Leu Met
1 5 10 15

Asn Arg Lys Ile Lys Gly Pro Cys Trp Leu Glu Val Lys Lys Ser Thr
20 25 30

Ala Leu Asn Gln Pro Val Ser Trp Cys Lys Val Glu Ala Met Ala Leu
35 40 45

Lys Pro Asp Leu Val Asn Val Ile Lys Asp Val Ser Pro Pro Pro Leu
50 55 60

Val Val Met Ala Phe Ser Met Lys Thr Met Gln Asn Ala Lys Asn His
65 70 75 80

Gln Asn Glu Ile Ile Ala Met Ala Ala Leu Val His His Ser Phe Ala
85 90 95

Leu Asp Lys Ala Ala Pro Lys Pro Pro Phe Gln Ser His Phe Cys Val
100 105 110

Val Ser Lys Pro Lys Asp Cys Ile Phe Pro Tyr Ala Phe Lys Glu Val
115 120 125

Ile Glu Lys Lys Asn Val Lys Val Glu Val Ala Ala Thr Glu Arg Thr
130 135 140

Leu Leu Gly Phe Phe Leu Ala Lys Val His Lys Ile Asp Pro Asp Ile
145 150 155 160

Ile Val Gly His Asn Ile Tyr Gly Phe Glu Leu Glu Val Leu Leu Gln
165 170 175

Arg Ile Asn Val Cys Lys Ala Pro His Trp Ser Lys Ile Gly Arg Leu
180 185 190

Lys Arg Ser Asn Met Pro Lys Leu Gly Gly Arg Ser Gly Phe Gly Glu
195 200 205

Arg Asn Ala Thr Cys Gly Arg Met Ile Cys Asp Val Glu Ile Ser Ala
210 215 220

Lys Glu Leu Ile Arg Cys Lys Ser Tyr His Leu Ser Glu Leu Val Gln
225 230 235 240

Gln Ile Leu Lys Thr Glu Arg Val Val Ile Pro Met Glu Asn Ile Gln
245 250 255

Asn Met Tyr Ser Glu Ser Ser Gln Leu Leu Tyr Leu Leu Glu His Thr
260 265 270

Trp Lys Asp Ala Lys Phe Ile Leu Gln Ile Met Cys Glu Leu Asn Val
275 280 285

Leu Pro Leu Ala Leu Gln Ile Thr Asn Ile Ala Gly Asn Ile Met Ser
290 295 300

Arg Thr Leu Met Gly Gly Arg Ser Glu Arg Asn Glu Phe Leu Leu Leu
305 310 315 320

His Ala Phe Tyr Glu Asn Asn Tyr Ile Val Pro Asp Lys Gln Ile Phe
325 330 335

Arg Lys Pro Gln Gln Lys Leu Gly Asp Glu Asp Glu Glu Ile Asp Gly
340 345 350

Asp Thr Asn Lys Tyr Lys Lys Gly Arg Lys Lys Gly Ala Tyr Ala Gly
355 360 365

Gly Leu Val Leu Asp Pro Lys Val Gly Phe Tyr Asp Lys Phe Ile Leu
370 375 380

Leu Leu Asp Phe Asn Ser Leu Tyr Pro Ser Ile Ile Gln Glu Phe Asn
385 390 395 400

Ile Cys Phe Thr Thr Val Gln Arg Val Ala Ser Glu Ala Gln Lys Val
405 410 415

Thr Glu Asp Gly Glu Gln Glu Gln Ile Pro Glu Leu Pro Asp Pro Ser
420 425 430

Leu Glu Met Gly Ile Leu Pro Arg Glu Ile Arg Lys Leu Val Glu Arg
435 440 445

Arg Lys Gln Val Lys Gln Leu Met Lys Gln Gln Asp Leu Asn Pro Asp
450 455 460

Leu Ile Leu Gln Tyr Asp Ile Arg Gln Lys Ala Leu Lys Leu Thr Ala
465 470 475 480

Asn Ser Met Tyr Gly Cys Leu Gly Phe Ser Tyr Ser Arg Phe Tyr Ala
485 490 495

Lys Pro Leu Ala Ala Leu Val Thr Tyr Lys Gly Arg Glu Ile Leu Met
500 505 510

His Thr Lys Glu Met Val Gln Lys Met Asn Leu Glu Val Ile Tyr Gly
515 520 525

Asp Thr Asp Ser Ile Met Ile Asn Thr Asn Ser Thr Asn Leu Glu Glu
530 535 540

Val Phe Lys Leu Gly Asn Lys Val Lys Ser Glu Val Asn Lys Leu Tyr
545 550 555 560

Lys Leu Leu Glu Ile Asp Ile Asp Gly Val Phe Lys Ser Leu Leu Leu
565 570 575

Leu Lys Lys Lys Lys Tyr Ala Ala Leu Val Val Glu Pro Thr Ser Asp
580 585 590

Gly Asn Tyr Val Thr Lys Gln Glu Leu Lys Gly Leu Asp Ile Val Arg
595 600 605

Arg Asp Trp Cys Asp Leu Ala Lys Asp Thr Gly Asn Phe Val Ile Gly
610 615 620

Gln Ile Leu Ser Asp Gln Ser Arg Asp Thr Ile Val Glu Asn Ile Gln
625 630 635 640

Lys Arg Leu Ile Glu Ile Gly Glu Asn Val Leu Asn Gly Ser Val Pro
645 650 655

Val Ser Gln Phe Glu Ile Asn Lys Ala Leu Thr Lys Asp Pro Gln Asp
660 665 670

Tyr Pro Asp Lys Lys Ser Leu Pro His Val His Val Ala Leu Trp Ile
675 680 685

Asn Ser Gln Gly Gly Arg Lys Val Lys Ala Gly Asp Thr Val Ser Tyr
690 695 700

Val Ile Cys Gln Asp Gly Ser Asn Leu Thr Ala Ser Gln Arg Ala Tyr
705 710 715 720

Ala Pro Glu Gln Leu Gln Lys Gln Asp Asn Leu Thr Ile Asp Thr Gln
725 730 735

Tyr Tyr Leu Ala Gln Gln Ile His Pro Val Val Ala Arg Ile Cys Glu
740 745 750

Pro Ile Asp Gly Ile
755



24
757
PRT
Mus musculus

24

Ser His Val Phe Gly Thr Asn Thr Ser Ser Leu Glu Leu Phe Leu Met
1 5 10 15

Asn Arg Lys Ile Lys Gly Pro Cys Trp Leu Glu Val Lys Asn Pro Gln
20 25 30

Leu Leu Asn Gln Pro Ile Ser Trp Cys Lys Phe Glu Val Met Ala Leu
35 40 45

Lys Pro Asp Leu Val Asn Val Ile Lys Asp Val Ser Pro Pro Pro Leu
50 55 60

Val Val Met Ser Phe Ser Met Lys Thr Met Gln Asn Val Gln Asn His
65 70 75 80

Gln His Glu Ile Ile Ala Met Ala Ala Leu Val His His Ser Phe Ala
85 90 95

Leu Asp Lys Ala Pro Pro Glu Pro Pro Phe Gln Thr His Phe Cys Val
100 105 110

Val Ser Lys Pro Lys Asp Cys Ile Phe Pro Cys Asp Phe Lys Glu Val
115 120 125

Ile Ser Lys Lys Asn Met Lys Val Glu Ile Ala Ala Thr Glu Arg Thr
130 135 140

Leu Ile Gly Phe Phe Leu Ala Lys Val His Lys Ile Asp Pro Asp Ile
145 150 155 160

Leu Val Gly His Asn Ile Cys Ser Phe Glu Leu Glu Val Leu Leu Gln
165 170 175

Arg Ile Asn Glu Cys Lys Val Pro Tyr Trp Ser Lys Ile Gly Arg Leu
180 185 190

Arg Arg Ser Asn Met Pro Lys Leu Gly Ser Arg Ser Gly Phe Gly Glu
195 200 205

Arg Asn Ala Thr Cys Gly Arg Met Ile Cys Asp Val Glu Ile Ser Ala
210 215 220

Lys Glu Leu Ile His Cys Lys Ser Tyr His Leu Ser Glu Leu Val Gln
225 230 235 240

Gln Ile Leu Lys Thr Glu Arg Ile Val Ile Pro Thr Glu Asn Ile Arg
245 250 255

Asn Met Tyr Ser Glu Ser Ser Tyr Leu Leu Tyr Leu Leu Glu His Ile
260 265 270

Trp Lys Asp Ala Arg Phe Ile Leu Gln Ile Met Cys Glu Leu Asn Val
275 280 285

Leu Pro Leu Ala Leu Gln Ile Thr Asn Ile Ala Gly Asn Ile Met Ser
290 295 300

Arg Thr Leu Met Gly Gly Arg Ser Glu Arg Asn Glu Phe Leu Leu Leu
305 310 315 320

His Ala Phe Tyr Glu Asn Asn Tyr Ile Val Pro Asp Lys Gln Ile Phe
325 330 335

Arg Lys Pro Gln Gln Lys Leu Gly Asp Glu Asp Glu Glu Ile Asp Gly
340 345 350

Asp Thr Asn Lys Tyr Lys Lys Gly Arg Lys Lys Ala Thr Tyr Ala Gly
355 360 365

Gly Leu Val Leu Asp Pro Lys Val Gly Phe Tyr Asp Lys Phe Ile Leu
370 375 380

Leu Leu Asp Phe Asn Ser Leu Tyr Pro Ser Ile Ile Gln Glu Phe Asn
385 390 395 400

Ile Cys Phe Thr Thr Val Gln Arg Val Thr Ser Glu Val Gln Lys Ala
405 410 415

Thr Glu Asp Glu Glu Gln Glu Gln Ile Pro Glu Leu Pro Asp Pro Asn
420 425 430

Leu Glu Met Gly Ile Leu Pro Arg Glu Ile Arg Lys Leu Val Glu Arg
435 440 445

Arg Lys Gln Val Lys Gln Leu Met Lys Gln Gln Asp Leu Asn Pro Asp
450 455 460

Leu Val Leu Gln Tyr Asp Ile Arg Gln Lys Ala Leu Lys Leu Thr Ala
465 470 475 480

Asn Ser Met Tyr Gly Cys Leu Gly Phe Ser Tyr Ser Arg Phe Tyr Ala
485 490 495

Lys Pro Leu Ala Ala Leu Val Thr Tyr Lys Gly Arg Glu Ile Leu Met
500 505 510

His Thr Lys Asp Met Val Gln Lys Met Asn Leu Glu Val Ile Tyr Gly
515 520 525

Asp Thr Asp Ser Ile Met Ile Asn Thr Asn Ser Thr Asn Leu Glu Glu
530 535 540

Val Phe Lys Leu Gly Asn Lys Val Lys Ser Glu Val Asn Lys Leu Tyr
545 550 555 560

Lys Leu Leu Glu Ile Asp Ile Asp Ala Val Phe Lys Ser Leu Leu Leu
565 570 575

Leu Lys Lys Lys Lys Tyr Ala Ala Leu Val Val Glu Pro Thr Ser Asp
580 585 590

Gly Asn Tyr Ile Thr Lys Gln Glu Leu Lys Gly Leu Asp Ile Val Arg
595 600 605

Arg Asp Trp Cys Asp Leu Ala Lys Asp Thr Gly Asn Phe Val Ile Gly
610 615 620

Gln Ile Leu Ser Asp Gln Ser Arg Asp Thr Ile Val Glu Asn Ile Gln
625 630 635 640

Lys Arg Leu Ile Glu Ile Gly Glu Asn Val Leu Asn Gly Ser Val Pro
645 650 655

Val Ser Gln Phe Glu Ile Asn Lys Ala Leu Thr Lys Asp Pro Gln Asp
660 665 670

Tyr Pro Asp Arg Lys Ser Leu Pro His Val His Val Ala Leu Trp Ile
675 680 685

Asn Ser Gln Gly Gly Arg Lys Val Lys Ala Gly Asp Thr Val Ser Tyr
690 695 700

Val Ile Cys Gln Asp Gly Ser Asn Leu Thr Ala Thr Gln Arg Ala Tyr
705 710 715 720

Ala Pro Glu Gln Leu Gln Lys Leu Asp Asn Leu Ala Ile Asp Thr Gln
725 730 735

Tyr Tyr Leu Ala Gln Gln Ile His Pro Val Val Ala Arg Ile Cys Glu
740 745 750

Pro Ile Asp Gly Ile
755



25
748
PRT
Drosophila melanogaster

25

Ala His Ile Phe Gly Ala Thr Thr Asn Ala Leu Glu Arg Phe Leu Leu
1 5 10 15

Asp Arg Lys Ile Lys Gly Pro Cys Trp Leu Gln Val Thr Gly Phe Lys
20 25 30

Val Ser Pro Thr Pro Met Ser Trp Cys Asn Thr Glu Val Thr Leu Thr
35 40 45

Glu Pro Lys Asn Val Glu Leu Val Gln Asp Lys Gly Lys Pro Ala Pro
50 55 60

Pro Pro Pro Leu Thr Leu Leu Ser Leu Asn Val Arg Thr Ser Met Asn
65 70 75 80

Pro Lys Thr Ser Arg Asn Glu Ile Cys Met Ile Ser Met Leu Thr His
85 90 95

Asn Arg Phe His Ile Asp Arg Pro Ala Pro Gln Pro Ala Phe Asn Arg
100 105 110

His Met Cys Ala Leu Thr Arg Pro Ala Val Val Ser Trp Pro Leu Asp
115 120 125

Leu Asn Phe Glu Met Ala Lys Tyr Lys Ser Thr Thr Val His Lys His
130 135 140

Asp Ser Glu Arg Ala Leu Leu Ser Trp Phe Leu Ala Gln Tyr Gln Lys
145 150 155 160

Ile Asp Ala Asp Leu Ile Val Thr Phe Asp Ser Met Asp Cys Gln Leu
165 170 175

Asn Val Ile Thr Asp Gln Ile Val Ala Leu Lys Ile Pro Gln Trp Ser
180 185 190

Arg Met Gly Arg Leu Arg Leu Ser Gln Ser Phe Gly Lys Arg Leu Leu
195 200 205

Glu His Phe Val Gly Arg Met Val Cys Asp Val Lys Arg Ser Ala Glu
210 215 220

Glu Cys Ile Arg Ala Arg Ser Tyr Asp Leu Gln Thr Leu Cys Lys Gln
225 230 235 240

Val Leu Lys Leu Lys Glu Ser Glu Arg Met Glu Val Asn Ala Asp Asp
245 250 255

Leu Leu Glu Met Tyr Glu Lys Gly Glu Ser Ile Thr Lys Leu Ile Ser
260 265 270

Leu Thr Met Gln Asp Asn Ser Tyr Leu Leu Arg Leu Met Cys Glu Leu
275 280 285

Asn Ile Met Pro Leu Ala Leu Gln Ile Thr Asn Ile Cys Gly Asn Thr
290 295 300

Met Thr Arg Thr Leu Gln Gly Gly Arg Ser Glu Arg Asn Glu Phe Leu
305 310 315 320

Leu Leu His Ala Ser Thr Glu Lys Asn Tyr Ile Val Pro Asp Lys Lys
325 330 335

Pro Val Ser Lys Arg Ser Gly Ala Gly Asp Thr Asp Arg Thr Leu Ser
340 345 350

Gly Ala Asp Ala Thr Met Gln Thr Lys Lys Lys Ala Ala Tyr Ala Gly
355 360 365

Gly Leu Val Leu Glu Pro Met Arg Gly Leu Tyr Glu Lys Tyr Val Leu
370 375 380

Leu Met Asp Leu Asn Ser Leu Tyr Pro Ser Ile Ile Gln Glu Tyr Asn
385 390 395 400

Ile Cys Phe Asn Pro Val Gln Gln Pro Val Asp Ala Asp Glu Leu Pro
405 410 415

Thr Leu Pro Asp Ser Lys Thr Glu Pro Gly Ile Leu Pro Leu Gln Leu
420 425 430

Lys Arg Leu Val Glu Ser Arg Lys Glu Val Lys Lys Leu Met Ala Ala
435 440 445

Pro Asp Leu Ser Pro Glu Leu Gln Met Gln Tyr His Ile Arg Gln Met
450 455 460

Ala Leu Lys Leu Thr Ala Asn Ser Met Tyr Gly Cys Leu Gly Phe Ala
465 470 475 480

His Ser Arg Phe Phe Ala Gln His Leu Ala Ala Leu Val Thr His Lys
485 490 495

Gly Arg Asp Leu Thr Asn Thr Gln Gln Leu Val Gln Lys Met Asn Tyr
500 505 510

Asp Val Val Tyr Gly Asp Thr Asp Ser Leu Met Ile Asn Thr Asn Ile
515 520 525

Thr Asp Tyr Asp Gln Val Tyr Lys Ile Gly His Asn Ile Lys Gln Ser
530 535 540

Val Asn Lys Leu Tyr Lys Gln Leu Glu Leu Asp Ile Asp Gly Val Phe
545 550 555 560

Gly Cys Leu Leu Leu Leu Lys Lys Lys Lys Tyr Ala Ala Ile Lys Leu
565 570 575

Ser Lys Asp Ser Lys Gly Asn Leu Arg Arg Glu Gln Glu His Lys Gly
580 585 590

Leu Asp Ile Val Arg Arg Asp Trp Ser Gln Leu Ala Val Met Val Gly
595 600 605

Lys Ala Val Leu Asp Glu Val Leu Ser Glu Lys Pro Leu Glu Glu Lys
610 615 620

Leu Asp Ala Val His Ala Gln Leu Glu Lys Ile Lys Thr Gln Ile Ala
625 630 635 640

Glu Gly Val Val Pro Leu Pro Leu Phe Val Ile Thr Lys Gln Leu Thr
645 650 655

Arg Thr Pro Gln Asp Tyr Arg Asn Ser Ala Ser Leu Pro His Val Gln
660 665 670

Val Ala Leu Arg Met Asn Arg Glu Arg Asn Arg Arg Tyr Lys Lys Gly
675 680 685

Asp Met Val Asp Leu Cys Asp Cys Leu Asp Gly Thr Thr Asn Ala Ala
690 695 700

Met Gln Arg Ala Tyr His Leu Asp Glu Leu Lys Thr Ser Glu Asp Lys
705 710 715 720

Lys Leu Gln Leu Asp Thr Asn Tyr Tyr Leu Gly His Gln Ile His Pro
725 730 735

Val Val Thr Arg Met Val Glu Val Leu Glu Gly Thr
740 745



26
752
PRT
Schizosaccharomyces pombe

26

Ser His Val Phe Gly Thr Asn Thr Ala Leu Phe Glu Gln Phe Val Leu
1 5 10 15

Ser Arg Arg Val Met Gly Pro Cys Trp Leu Lys Ile Gln Gln Pro Asn
20 25 30

Phe Asp Ala Val Lys Asn Ala Ser Trp Cys Arg Val Glu Ile Gly Cys
35 40 45

Ser Ser Pro Gln Asn Ile Ser Val Ser Phe Glu Lys Asn Glu Ile Thr
50 55 60

Ser Lys Thr Pro Pro Met Thr Val Met Ser Leu Ala Phe Arg Thr Leu
65 70 75 80

Ile Asn Lys Glu Gln Asn Lys Gln Glu Val Val Met Ile Ser Ala Arg
85 90 95

Ile Phe Glu Asn Val Asp Ile Glu Lys Gly Leu Pro Ala Asn Asp Met
100 105 110

Pro Ser Tyr Ser Phe Ser Leu Ile Arg Pro Leu Lys Gln Ile Phe Pro
115 120 125

Asn Gly Phe Glu Lys Leu Ala Arg Gln His Lys Ser Ser Ile Phe Cys
130 135 140

Glu Arg Ser Glu Val Ser Leu Leu Asn Asn Phe Leu Asn Lys Val Arg
145 150 155 160

Thr Tyr Asp Pro Asp Val Tyr Phe Gly His Asp Phe Glu Met Cys Tyr
165 170 175

Ser Val Leu Leu Ser Arg Leu Lys Glu Arg Lys Ile His Asn Trp Ser
180 185 190

Ser Ile Gly Arg Leu Arg Arg Ser Glu Trp Pro Arg Ser Phe Asn Arg
195 200 205

Ser Ser Gln Gln Phe Val Glu Lys Gln Ile Ile Ala Gly Arg Leu Met
210 215 220

Cys Asp Leu Ser Asn Asp Phe Gly Arg Ser Met Ile Lys Ala Gln Ser
225 230 235 240

Trp Ser Leu Ser Glu Ile Val Leu Lys Glu Leu Asp Ile Lys Arg Gln
245 250 255

Asp Ile Asn Gln Glu Lys Ala Leu Gln Ser Trp Thr Asp Thr Ala His
260 265 270

Gly Leu Leu Asp Tyr Leu Val His Cys Glu Ile Asp Thr Phe Phe Ile
275 280 285

Ala Ala Val Ala Phe Lys Ile Gln Met Leu Gln Leu Ser Lys Asn Leu
290 295 300

Thr Asn Ile Ala Gly Asn Ser Trp Ala Arg Thr Leu Thr Gly Thr Arg
305 310 315 320

Ala Glu Arg Asn Glu Tyr Ile Leu Leu His Glu Phe Lys Lys Asn Gly
325 330 335

Tyr Ile Val Pro Asp Lys Gln Gln Ser Ile Arg Arg His Ala Glu Ala
340 345 350

Phe Gly Ala Glu Asp Gly Leu Gln Glu Glu Ser Leu Gly Lys Lys Lys
355 360 365

Asp Lys Tyr Lys Gly Gly Leu Val Phe Glu Pro Gln Lys Gly Leu Tyr
370 375 380

Glu Thr Cys Ile Leu Val Met Asp Phe Asn Ser Leu Tyr Pro Ser Ile
385 390 395 400

Ile Gln Glu Tyr Asn Ile Cys Phe Thr Thr Val Asp Arg Ser Pro Ser
405 410 415

Asn Ser Asp Ser Asp Asp Gln Ile Pro Asp Thr Pro Ser Ala Ser Ala
420 425 430

Asn Gln Gly Ile Phe Pro Arg Leu Ile Ala Asn Leu Val Glu Arg Arg
435 440 445

Arg Gln Ile Lys Gly Leu Leu Lys Asp Asn Ser Ala Thr Pro Thr Gln
450 455 460

Arg Leu Gln Trp Asp Ile Gln Gln Gln Ala Leu Lys Leu Thr Ala Asn
465 470 475 480

Ser Met Tyr Gly Cys Leu Gly Tyr Thr Lys Ser Arg Phe Tyr Ala Arg
485 490 495

Pro Leu Ala Val Leu Ile Thr Tyr Lys Gly Arg Glu Ala Leu Met Asn
500 505 510

Thr Lys Glu Leu Ala Asp Gln Met Gly Leu Gln Val Ile Tyr Gly Asp
515 520 525

Thr Asp Ser Val Met Leu Asn Thr Asn Val Thr Asp Lys Asn His Ala
530 535 540

Leu Arg Ile Gly Asn Glu Phe Lys Glu Lys Val Asn Glu Arg Tyr Ser
545 550 555 560

Lys Leu Glu Ile Asp Ile Asp Asn Val Tyr Gln Arg Met Leu Leu His
565 570 575

Ala Lys Lys Lys Tyr Ala Ala Leu Gln Leu Asp Ser Gln Gly Lys Pro
580 585 590

Asn Leu Asp Val Lys Gly Leu Asp Met Lys Arg Arg Glu Phe Cys Thr
595 600 605

Leu Ala Lys Glu Ala Ser Lys Phe Cys Leu Asp Gln Ile Leu Ser Gly
610 615 620

Glu Leu Thr Glu Thr Val Ile Glu Asn Ile His Ser Tyr Leu Met Asp
625 630 635 640

Phe Ser Glu Lys Met Arg Asn Gly Lys Phe Pro Ala Asn Lys Phe Ile
645 650 655

Ile Phe Asn Arg Leu Gly Lys Asn Pro Glu Asp Tyr Pro Asn Gly Lys
660 665 670

Thr Met Pro Phe Val Gln Val Ala Leu Lys Lys Lys Ala Arg Gly Glu
675 680 685

Asn Val Arg Val Gly Asp Val Ile Pro Phe Ile Ile Ala Gly Ser Asp
690 695 700

Ala Asp Gly His Pro Ala Asp Arg Ala Tyr Ser Pro Gln Glu Ile Met
705 710 715 720

Asn Thr Asn Ser Thr Leu Val Ile Asp Tyr Asn Tyr Tyr Leu Ser His
725 730 735

Gln Ile Leu Pro Pro Ile Glu Arg Val Ile Ala Pro Ile Glu Gly Thr
740 745 750



27
761
PRT
Saccharomyces cerevisiae

27

Tyr His Val Phe Gly Gly Asn Ser Asn Ile Phe Glu Ser Phe Val Ile
1 5 10 15

Gln Asn Arg Ile Met Gly Pro Cys Trp Leu Asp Ile Lys Gly Ala Asp
20 25 30

Phe Asn Ser Ile Arg Asn Ala Ser His Cys Ala Val Glu Val Ser Val
35 40 45

Asp Lys Pro Gln Asn Ile Thr Pro Thr Thr Thr Lys Thr Met Pro Asn
50 55 60

Leu Arg Cys Leu Ser Leu Ser Ile Gln Thr Leu Met Asn Pro Lys Glu
65 70 75 80

Asn Lys Gln Glu Ile Val Ser Ile Thr Leu Ser Ala Tyr Arg Asn Ile
85 90 95

Ser Leu Asp Ser Pro Ile Pro Glu Asn Ile Lys Pro Asp Asp Leu Cys
100 105 110

Thr Leu Val Arg Pro Pro Gln Ser Thr Ser Phe Pro Leu Gly Leu Ala
115 120 125

Ala Leu Ala Lys Gln Lys Leu Pro Gly Arg Val Arg Leu Phe Asn Asn
130 135 140

Glu Lys Ala Met Leu Ser Cys Phe Cys Ala Met Leu Lys Val Glu Asp
145 150 155 160

Pro Asp Val Ile Ile Gly His Arg Leu Gln Asn Val Tyr Leu Asp Val
165 170 175

Leu Ala His Arg Met His Asp Leu Asn Ile Pro Thr Phe Ser Ser Ile
180 185 190

Gly Arg Arg Leu Arg Arg Thr Trp Pro Glu Lys Phe Gly Arg Gly Asn
195 200 205

Ser Asn Met Asn His Phe Phe Ile Ser Asp Ile Cys Ser Gly Arg Leu
210 215 220

Ile Cys Asp Ile Ala Asn Glu Met Gly Gln Ser Leu Thr Pro Lys Cys
225 230 235 240

Gln Ser Trp Asp Leu Ser Glu Met Tyr Gln Val Thr Cys Glu Lys Glu
245 250 255

His Lys Pro Leu Asp Ile Asp Tyr Gln Asn Pro Gln Tyr Gln Asn Asp
260 265 270

Val Asn Ser Met Thr Met Ala Leu Gln Glu Asn Ile Thr Asn Cys Met
275 280 285

Ile Ser Ala Glu Val Ser Tyr Arg Ile Gln Leu Leu Thr Leu Thr Lys
290 295 300

Gln Leu Thr Asn Leu Ala Gly Asn Ala Trp Ala Gln Thr Leu Gly Gly
305 310 315 320

Thr Arg Ala Gly Arg Asn Glu Tyr Ile Leu Leu His Glu Phe Ser Arg
325 330 335

Asn Gly Phe Ile Val Pro Asp Lys Glu Gly Asn Arg Ser Arg Ala Gln
340 345 350

Lys Gln Arg Gln Asn Glu Glu Asn Ala Asp Ala Pro Val Asn Ser Lys
355 360 365

Lys Ala Lys Tyr Gln Gly Gly Leu Val Phe Glu Pro Glu Lys Gly Leu
370 375 380

His Lys Asn Tyr Val Leu Val Met Asp Phe Asn Ser Leu Tyr Pro Ser
385 390 395 400

Ile Ile Gln Glu Phe Asn Ile Cys Phe Thr Thr Val Asp Arg Asn Lys
405 410 415

Glu Asp Ile Asp Glu Leu Pro Ser Val Pro Pro Ser Glu Val Asp Gln
420 425 430

Gly Val Leu Pro Arg Leu Leu Ala Asn Leu Val Asp Arg Arg Arg Glu
435 440 445

Val Lys Lys Val Met Lys Thr Glu Thr Asp Pro His Lys Arg Val Gln
450 455 460

Cys Asp Ile Arg Gln Gln Ala Leu Lys Leu Thr Ala Asn Ser Met Tyr
465 470 475 480

Gly Cys Leu Gly Tyr Val Asn Ser Arg Phe Tyr Ala Lys Pro Leu Ala
485 490 495

Met Leu Val Thr Asn Lys Gly Arg Glu Ile Leu Met Asn Thr Arg Gln
500 505 510

Leu Ala Glu Ser Met Asn Leu Leu Val Val Tyr Gly Asp Thr Asp Ser
515 520 525

Val Met Ile Asp Thr Gly Cys Asp Asn Tyr Ala Asp Ala Ile Lys Ile
530 535 540

Gly Leu Gly Phe Lys Arg Leu Val Asn Glu Arg Tyr Arg Leu Leu Glu
545 550 555 560

Ile Asp Ile Asp Asn Val Phe Lys Lys Leu Leu Leu His Ala Lys Lys
565 570 575

Lys Tyr Ala Ala Leu Thr Val Asn Leu Asp Lys Asn Gly Asn Gly Thr
580 585 590

Thr Val Leu Glu Val Lys Gly Leu Asp Met Lys Arg Arg Glu Phe Cys
595 600 605

Pro Leu Ser Arg Asp Val Ser Ile His Val Leu Asn Thr Ile Leu Ser
610 615 620

Asp Lys Asp Pro Glu Glu Ala Leu Gln Glu Val Tyr Asp Tyr Leu Glu
625 630 635 640

Asp Ile Arg Ile Lys Val Glu Thr Asn Asn Ile Arg Ile Asp Lys Tyr
645 650 655

Lys Ile Asn Met Lys Leu Ser Lys Asp Pro Lys Ala Tyr Pro Gly Gly
660 665 670

Lys Asn Met Pro Ala Val Gln Val Ala Leu Arg Met Arg Lys Ala Gly
675 680 685

Arg Val Val Lys Ala Gly Ser Val Ile Thr Phe Val Ile Thr Lys Gln
690 695 700

Asp Glu Ile Asp Asn Ala Ala Asp Thr Pro Ala Leu Ser Val Ala Glu
705 710 715 720

Arg Ala His Ala Leu Asn Glu Val Met Ile Lys Ser Asn Asn Leu Ile
725 730 735

Pro Asp Pro Gln Tyr Tyr Leu Glu Lys Gln Ile Phe Ala Pro Val Glu
740 745 750

Arg Leu Leu Glu Arg Ile Asp Ser Phe
755 760



28
761
PRT
Trypanosoma brucei

28

Gln Val Val Val Gly Ala Ser Arg Ser Leu Leu Glu Leu Phe Leu Ile
1 5 10 15

Lys Lys Arg Leu Met Gly Pro Ser Tyr Leu Glu Ile Glu His Leu Val
20 25 30

Thr Ala Met Asp Arg Val Ser His Cys Lys Thr Glu Phe Leu Val Pro
35 40 45

Ser Pro Lys Asp Ile Lys Val Tyr Asn Ser Ser Lys Pro Pro Pro Pro
50 55 60

Phe Thr Val Ala Ser Ile Gln Leu His Ala Gln Leu Asp Ser Asp Gly
65 70 75 80

Val Lys Asn Glu Val Ile Ala Ala Ser Ile Ala Leu Tyr Gly Asp Val
85 90 95

Ser Ile Asp Gly Glu Arg Lys Pro Asn Ile Thr Glu Cys Phe Thr Gly
100 105 110

Val Arg Gln Leu Ser Pro Asp Ala Pro Leu Pro Leu Asp Leu Glu Thr
115 120 125

Tyr Cys Leu Ser Lys Arg Met Pro Gly Val His Arg Phe Ile Asn Glu
130 135 140

Arg Ala Leu Leu Thr Trp Phe Ala Glu Thr Leu Ala Ala Leu Asp Pro
145 150 155 160

Asp Ile Ile Val Gly His Asn Ile Ile Gly Tyr Thr Val Glu Thr Leu
165 170 175

Leu Asn Arg Tyr Gln Glu Leu Asn Ile Val Arg Trp Ser Thr Ile Gly
180 185 190

Arg Leu Asp Val Arg Arg Phe Pro Arg Ile Gln Gly Asn Asn Phe Asn
195 200 205

Leu Ala Ile Glu Lys Glu Ala Cys Val Gly Arg Leu Val Val Asp Thr
210 215 220

Tyr Leu Leu Ala Arg Glu Tyr Tyr Lys Ser Thr Asn Tyr Lys Leu Leu
225 230 235 240

Ser Leu Ser Thr Gln Met Glu Ile Lys Gly Ile Thr Asp Asn Arg Gly
245 250 255

His Phe Glu Pro Gly Ser Thr Val Leu Val Lys Asp Ser Met Met Ser
260 265 270

Ser Glu Ala Leu Cys Pro Ile Leu Leu Gln Leu Leu Asn Cys Ala Val
275 280 285

Leu Ser Phe Asn Val Ala Ser Phe Leu Asp Val Ile Pro Leu Thr Lys
290 295 300

Arg Leu Thr Leu Leu Ala Gly Asn Leu Trp Ser Arg Thr Leu Tyr Gly
305 310 315 320

Ala Arg Ser Glu Arg Ile Glu Tyr Leu Leu Leu His Ala Phe His Asn
325 330 335

Leu Lys Phe Val Thr Pro Asp Lys Lys Lys Arg Asp Leu Lys Arg Gly
340 345 350

Arg Glu Asp Asp Asp Asp Glu Gly Lys Arg Lys Thr Lys Tyr Gln Gly
355 360 365

Gly Met Val Leu Glu Pro Lys Ser Gly Leu Tyr Ser Glu Tyr Ile Leu
370 375 380

Leu Leu Asp Phe Asn Ser Leu Tyr Pro Ser Leu Ile Gln Glu Phe Asn
385 390 395 400

Val Cys Tyr Thr Thr Ile Asp Arg Asp Glu Asn Thr Val Ser Ala Glu
405 410 415

Val Pro Pro Pro Glu Ser Leu Ile Cys Leu Ser Cys Arg Ala Ala Gly
420 425 430

Leu Pro Ser Pro Cys Leu His Lys Cys Ile Leu Pro Lys Val Ile Arg
435 440 445

Gly Leu Val Asp Ser Arg Arg Glu Ile Lys Arg Met Met Lys Ser Glu
450 455 460

Lys Asp Pro Gly Asn Leu Ala Met Leu Glu Ile Arg Gln Leu Ala Leu
465 470 475 480

Lys Leu Thr Ala Asn Ser Met Tyr Gly Cys Leu Gly Phe Glu Tyr Ser
485 490 495

Arg Phe Tyr Ala Gln Pro Leu Ala Glu Leu Val Thr Arg Gln Gly Arg
500 505 510

Leu Ala Leu Gln Asn Thr Val Glu Leu Ile Pro Gln Ile Ser Pro Ser
515 520 525

Ile Arg Val Ile Tyr Gly Asp Thr Asp Ser Val Met Ile Gln Thr Gly
530 535 540

Ile Lys Asp Asp Ile Val Lys Val Arg Asn Leu Gly Phe Glu Ile Lys
545 550 555 560

Gly Lys Val Asn Gln Arg Tyr Gln Ser Leu Glu Leu Asp Ile Asp Gly
565 570 575

Val Phe Arg Ala Met Leu Leu Leu Arg Lys Lys Lys Tyr Ala Ala Leu
580 585 590

Ser Val Val Asp Trp Gln Gly Glu Gly Lys Val Tyr Lys Arg Glu Val
595 600 605

Lys Gly Leu Asp Met Val Arg Arg Asp Trp Cys Pro Leu Ser Gln His
610 615 620

Val Ser Asp Ala Val Leu Lys Arg Ile Leu Asn Ala Glu Gly Gly Glu
625 630 635 640

Asp Ile Leu Asp Phe Val Ile Lys Tyr Met Lys Gly Val Ala Gln Asp
645 650 655

Val Arg Ser Gly Asn Val Tyr Pro Leu Glu Glu Phe Val Ile Ser Lys
660 665 670

Ser Leu Thr Lys Glu Pro Glu Ser Tyr His Gly Thr Gly Tyr Pro His
675 680 685

Ala Val Val Ala Leu Arg Met Lys Gln Arg Lys Glu Gly Val Arg Val
690 695 700

Gly Asp Leu Ile Pro Tyr Val Ile Cys Glu Gly Asp Glu His Ile Asp
705 710 715 720

Asp Lys Ala Tyr His Ile Asp Glu Val Arg Arg Ser Asp Gly Leu Ser
725 730 735

Val Asp Val Glu Trp Tyr Leu Ser Ser Gln Leu Tyr Pro Pro Val Met
740 745 750

Arg Leu Cys Glu His Ile Gln Gly Phe
755 760



29
782
PRT
Autographa californica nucleopolynedrovirus

29

Asn Ala Ala Cys Leu Asp Lys Phe Leu His Asn Val Asn Arg Val His
1 5 10 15

Met Gln Thr Pro Phe Val Glu Gly Ala Tyr Met Arg Phe Lys Lys Thr
20 25 30

Gln Arg Cys Gln Asn Asn Tyr Val Gly Gly Ser Thr Thr Arg Met Phe
35 40 45

Asn Leu Gln His Phe Asn Glu Asp Phe Glu Leu Val Asp Glu Met Thr
50 55 60

Leu Thr Ser Gly Ile Met Pro Val Leu Ser Cys Tyr Asp Ile Glu Thr
65 70 75 80

His Ser Asp Gly His Asn Met Ser Lys Ala Ser Val Asp Cys Ile Met
85 90 95

Ser Ile Gly Phe Val Val Tyr Lys Asn Asp Glu Tyr Ala Lys Phe Cys
100 105 110

Phe Met Tyr His Lys Leu Pro Thr Gln Ile Pro Glu Thr Tyr Asp Asp
115 120 125

Asp Thr Tyr Val Val Met Phe Gln Asn Glu Ile Asp Met Ile Thr Ala
130 135 140

Phe Phe Asp Met Ile Lys Ile Thr Asn Pro Asp Val Ile Leu Asp Phe
145 150 155 160

Asn Gly Asp Val Phe Asp Leu Pro Tyr Ile Leu Gly Arg Leu Asn Lys
165 170 175

Thr Lys Met Leu Leu Lys Arg Tyr Asp Leu Pro Ala Ala Ala Pro Thr
180 185 190

Thr Lys Leu Phe Ile Asn Lys Leu Gly Asn Lys Val Asp Thr Tyr Tyr
195 200 205

Phe Asn Tyr Tyr Ile His Ile Asp Leu Tyr Lys Phe Phe Ser Ser Asp
210 215 220

Ser Asn Gln His Lys Val Glu Asn Phe Gln Leu Asn Thr Ile Ser Ser
225 230 235 240

Tyr Tyr Leu Gly Glu Asn Lys Ile Asp Leu Pro Trp Thr Glu Met Val
245 250 255

Lys Met Tyr Asn Thr Arg Arg Leu Asp Val Ile Ala Lys Tyr Asn Val
260 265 270

Gln Asp Cys Met Leu Pro Ile Lys Leu Phe Val Lys Leu Lys Met Ala
275 280 285

Asp Ser Val Tyr Ser Gln Cys Ile Leu His Arg Leu Cys Thr Asp Asp
290 295 300

Val Ile Cys Asn Ile Ser His Leu Ile Ser Val Ala Cys Phe Tyr Ala
305 310 315 320

Ala Ile Thr Asn Thr Arg Ile Asn Glu Ser Thr Gly Lys Glu Glu Pro
325 330 335

Asp Pro Tyr Phe Phe Asn Lys Asn Asp Leu Ser Ile Ile Ser Gly Gln
340 345 350

Phe Lys Ala Asp Lys Ala Ala Ala Gly Ile Ser Asn Leu Lys Arg Lys
355 360 365

Leu Ile Pro Leu Lys Asn Ile Pro Lys Asp Ala Ile Asn Leu Gly Pro
370 375 380

Ala Asn Gln Thr Val Lys Tyr Lys Gly Gly Lys Val Leu Lys Pro Arg
385 390 395 400

Ala Gly Ile Tyr Lys Asn Ala Phe Ser Leu Asp Phe Asn Ser Leu Tyr
405 410 415

Leu Thr Ile Met Ile Ala Ile Cys Ala Cys Leu Ser Asn Leu Ile Leu
420 425 430

Cys Glu Asp Gly Asn Val Tyr Leu Asn His Asn Ser Arg Ala Ile Val
435 440 445

Val Lys Leu Leu Leu Lys Leu Leu Ser Glu Arg Cys Lys Phe Lys Lys
450 455 460

Asn Arg Asp Asn Gln Ser Glu Ser Ala Phe Leu Tyr Asp Leu Tyr Asp
465 470 475 480

Gln Lys Gln Asn Ser Val Lys Arg Thr Ala Asn Ser Ile Tyr Gly Tyr
485 490 495

Tyr Gly Ile Phe Tyr Lys Val Leu Ala Asn Tyr Ile Thr Arg Val Gly
500 505 510

Arg Asn Gln Leu Arg Leu Ala Ile Ser Leu Ile Glu Gly Leu Ser Asn
515 520 525

Asp Pro Glu Ile Leu Glu Lys Phe Asn Leu Gly Ser Ile Thr Phe Lys
530 535 540

Val Val Tyr Gly Asp Thr Asp Ser Thr Phe Val Leu Pro Thr Phe Asn
545 550 555 560

Tyr Asn Glu Ile Ser Asn Glu Thr Asp Thr Leu Lys Gln Ile Cys Thr
565 570 575

His Val Glu Thr Arg Val Asn Asn Ser Phe Thr Asp Gly Tyr Lys Met
580 585 590

Ala Phe Glu Asn Leu Met Lys Val Leu Ile Leu Leu Lys Lys Lys Lys
595 600 605

Tyr Cys Tyr Leu Asn Ser Glu Asn Lys Ile Val Tyr Lys Gly Trp Leu
610 615 620

Val Lys Lys Asp Met Pro Val Phe Met Arg Ile Ala Phe Arg Thr Ala
625 630 635 640

Val Glu Gln Ile Leu Arg His Leu Asp Met Asp Lys Cys Leu Gln Ser
645 650 655

Leu Gln Thr Ser Phe Tyr Glu Tyr Tyr Asp Glu Phe Ala Lys Ser Lys
660 665 670

Ser Leu Thr Asp Tyr Ser Phe Ser Met Thr Tyr Asn Asp Asn Pro Gly
675 680 685

Lys Lys Arg Lys Ser Thr Asp Asp Asn Glu Gly Pro Ser Pro Lys Arg
690 695 700

Arg Val Ile Thr Val Ala Arg His Cys Arg Glu Ile Leu Val Asn Lys
705 710 715 720

Gly Thr Asp Phe Val Pro Gly Asn Gly Asp Arg Ile Pro Tyr Leu Leu
725 730 735

Ile Asp Ile Glu Gly Lys Val Thr Glu Lys Ala Tyr Pro Leu Arg Leu
740 745 750

Phe Asp Pro Val Lys Met Arg Ile Ser Trp Ile Lys His Met Gly Ile
755 760 765

Leu Cys Thr Phe Met Asn Glu Leu Leu Glu Ile Phe Gly Asp
770 775 780



30
797
PRT
Lymantria dispar multicapsid nuclear polyhedrosis

30

Asp Lys Asn Cys Leu Asp Gly Tyr Leu Ala Asp Val Asn Arg Val His
1 5 10 15

Met Gln Thr Ser Leu Leu Glu Gly Gln Tyr Val Arg Phe Lys Asn Ala
20 25 30

His Ala Cys Arg Asp Tyr Arg Leu Ser His Thr Ala Lys Asp Val His
35 40 45

Glu Phe Glu Ser Met Leu Glu Arg Val Gln Val Ser Ala Leu Ser His
50 55 60

Glu Ile Leu Pro Val Val Ala Cys Tyr Asp Ile Glu Thr His Ser Asp
65 70 75 80

Gly Gln Arg Phe Ser Ala Pro Asp Ala Asp Phe Ile Ile Ser Ile Ala
85 90 95

Val Val Val Arg Arg Asp Ala Ala Asp Thr Arg Ile Cys Leu Phe Tyr
100 105 110

Ser Pro Asp Asp Pro Val Asp Leu Ser Ser Ser Ser Ser Ser Pro Pro
115 120 125

Ala Ala Pro Asp Thr Ala Ala Val His Phe Arg Ala Glu Arg Asp Met
130 135 140

Ile Ala Ala Phe Phe Gln Leu Leu Pro Leu Leu Asn Ala Asp Val Val
145 150 155 160

Leu Asp Phe Asn Gly Asp Lys Phe Asp Leu Pro Phe Leu Thr Gly Arg
165 170 175

Ala Asn Lys Leu Cys Gly Pro Ala Glu Ala Ala Arg Ala Thr Lys Ile
180 185 190

Ala Arg Tyr Asp Leu Ser Pro Val Asn Val Val Thr Gln Gln Ser Tyr
195 200 205

Asp Lys Phe Ser Asn Lys Leu His Ser His Tyr Leu Thr Tyr Tyr Ile
210 215 220

His Ile Asp Leu Tyr Gln Phe Leu Ser Thr Asp Ser Glu His Asn Asp
225 230 235 240

Leu Glu Asn Phe Gln Leu Asn Thr Val Ala Glu His Tyr Leu Lys Lys
245 250 255

Ser Lys Val Asp Leu Pro Ile His Asp Met Leu Gln Met Tyr Gly Glu
260 265 270

Lys Arg Leu Ser Arg Ile Val Glu Tyr Asn Val Gln Asp Cys Val Leu
275 280 285

Pro Val Glu Leu Phe Leu Lys Leu Glu Ile Ala Asp Tyr Met Tyr Thr
290 295 300

Gln Cys Met Leu Leu Tyr Leu Cys Thr Asp Asp Leu Leu Arg Asn Ile
305 310 315 320

Ser His Lys Ile Thr Val Ala Tyr Phe His Leu Ala Leu Thr Asn Thr
325 330 335

Val Ala Arg Arg Pro Asp Pro Thr Pro Asp Pro Tyr Phe Phe Asn Lys
340 345 350

Tyr Asp Leu Ser Val Thr Ser Gly Ala Ser Ala Pro Ser Thr Ser Arg
355 360 365

Pro Ala Asn Ala Ile Asp Leu Ser Gln Leu Lys Arg Thr Pro Val Asp
370 375 380

Ala Ala Arg Ile Pro Pro Ser Ala Val Lys Leu Cys Ser Thr Arg Gln
385 390 395 400

Ser Cys Thr Tyr Lys Gly Gly Lys Val Leu Ser Pro Lys Pro Gly Phe
405 410 415

Asn Arg Trp Val Ala Thr Leu Asp Phe Asn Ala Leu Tyr Pro Thr Ile
420 425 430

Met Met Trp Glu Gly Val Cys Met Ser Ser Asn Val Phe Ile Ala Ser
435 440 445

Asp Gly Asn Val Tyr Leu Asp Lys Asn Val Asn Ala Val Asn Pro Lys
450 455 460

Leu Leu Lys Thr Leu Ser Glu Met Arg Val Arg Tyr Lys Gly Leu Arg
465 470 475 480

Asp Gln Cys Glu Tyr Asn Ser Phe Tyr Tyr Lys Leu Tyr Asp Lys Ile
485 490 495

Gln Asn Ala Leu Lys Arg Ile Ala Asn Ser Ile Tyr Gly Tyr Tyr Gly
500 505 510

Ile Phe Phe Lys Pro Leu Ala Asn Tyr Ile Thr Lys Met Gly Arg Gly
515 520 525

Lys Leu Lys Glu Val Val Gly Lys Val Glu Ala Met Ser Asp Asp Pro
530 535 540

Arg Ile Leu Arg Glu Phe Gly Leu Ser Lys Ile Asn Phe Ser Val Ile
545 550 555 560

Tyr Gly Asp Thr Asp Ser Cys Phe Ile Arg Val Leu Phe Asp Glu Ala
565 570 575

Glu Trp Arg Arg Thr Ala Ala Arg Pro Arg Ser Ala Pro Ser Cys Arg
580 585 590

Thr Thr Cys Ala Lys Arg Ser Thr Thr Leu Trp Cys Gly Tyr Lys Met
595 600 605

Ser Leu Glu Asn Ile Met Leu Ser Leu Ile Leu Leu Lys Lys Lys Lys
610 615 620

Tyr Cys Tyr Leu Asn Asn Glu Gln Arg Thr Lys Tyr Lys Gly Trp Leu
625 630 635 640

Ile Lys Arg Asp Met Pro Leu Phe Met Arg Lys Ala Phe Arg Ala Thr
645 650 655

Val Asp Ser Phe Ser Ala Ala Thr Arg Arg Val Arg Ala Arg Pro Ala
660 665 670

Arg Arg Glu Met Leu Arg Tyr Tyr Arg Glu Phe Gly Ala Pro Arg Glu
675 680 685

Asn Leu Val Asp Tyr Cys Phe Ser Met Ser Tyr Asn Glu Thr Ser Thr
690 695 700

Thr Ala Lys Arg Arg Lys Glu Glu Asp Pro Ala Arg Lys Pro Val Ile
705 710 715 720

Thr Ile Ala Lys His Cys Arg Glu Leu Leu Ala Asn Pro Gly Val Asp
725 730 735

Phe Leu Pro Gly Asn Gly Asp Arg Ile Gln Tyr Val Leu Val Asp Val
740 745 750

Lys Glu Lys Ile Thr Gln Lys Ala Phe Pro Leu Lys Leu Phe Asp Pro
755 760 765

Asp Ser Pro Thr Leu Gln Ile Ser Trp Leu Lys His Met Asn Ile Leu
770 775 780

Cys Thr Phe Met Asn Glu Leu Ile Gln Val Phe Gly Asn
785 790 795



31
745
PRT
Saccharomyces cerevisiae

31

Asn Lys Val Pro Ser Met Gly Asn Lys Lys Thr Glu Ser Gln Ile Ser
1 5 10 15

Met His Thr Pro His Ser Lys Phe Leu Tyr Lys Phe Ala Ser Asp Val
20 25 30

Ser Gly Lys Gln Lys Arg Lys Lys Ser Ser Val His Asp Ser Leu Thr
35 40 45

His Leu Thr Leu Glu Ile His Ala Asn Thr Arg Ser Asp Lys Ile Pro
50 55 60

Asp Pro Ala Ile Asp Glu Val Ser Met Ile Ile Trp Cys Leu Glu Glu
65 70 75 80

Glu Thr Phe Pro Leu Asp Leu Asp Ile Ala Tyr Glu Gly Ile Met Ile
85 90 95

Val His Lys Ala Ser Glu Asp Ser Thr Phe Pro Thr Lys Ile Gln His
100 105 110

Cys Ile Asn Glu Ile Pro Val Met Phe Tyr Glu Ser Glu Phe Glu Met
115 120 125

Phe Glu Ala Leu Thr Asp Leu Val Leu Leu Leu Asp Pro Asp Ile Leu
130 135 140

Ser Gly Phe Glu Ile His Asn Phe Ser Trp Gly Tyr Ile Ile Glu Arg
145 150 155 160

Cys Gln Lys Ile His Gln Phe Asp Ile Val Arg Glu Leu Ala Arg Val
165 170 175

Lys Cys Gln Ile Lys Thr Lys Leu Ser Asp Thr Trp Gly Tyr Ala His
180 185 190

Ser Ser Gly Ile Met Ile Thr Gly Arg His Met Ile Asn Ile Trp Arg
195 200 205

Ala Leu Arg Ser Asp Val Asn Leu Thr Gln Tyr Thr Ile Glu Ser Ala
210 215 220

Ala Phe Asn Ile Leu His Lys Arg Leu Pro His Phe Ser Phe Glu Ser
225 230 235 240

Leu Thr Asn Met Trp Asn Ala Lys Lys Ser Thr Thr Glu Leu Lys Thr
245 250 255

Val Leu Asn Tyr Trp Leu Ser Arg Ala Gln Ile Asn Ile Gln Leu Leu
260 265 270

Arg Lys Gln Asp Tyr Ile Ala Arg Asn Ile Glu Gln Ala Arg Leu Ile
275 280 285

Gly Ile Asp Phe His Ser Val Tyr Tyr Arg Gly Ser Gln Phe Lys Val
290 295 300

Glu Ser Phe Leu Ile Arg Ile Cys Lys Ser Glu Ser Phe Ile Leu Leu
305 310 315 320

Ser Pro Gly Lys Lys Asp Val Arg Lys Gln Lys Ala Leu Glu Cys Val
325 330 335

Pro Leu Val Met Glu Pro Glu Ser Ala Phe Tyr Lys Ser Pro Leu Ile
340 345 350

Val Leu Asp Phe Gln Ser Leu Tyr Pro Ser Ile Met Ile Gly Tyr Asn
355 360 365

Tyr Cys Tyr Ser Thr Met Ile Gly Arg Val Arg Glu Ile Asn Leu Thr
370 375 380

Glu Asn Asn Leu Gly Val Ser Lys Phe Ser Leu Pro Arg Asn Ile Leu
385 390 395 400

Ala Leu Leu Lys Asn Asp Val Thr Ile Ala Pro Asn Gly Val Val Tyr
405 410 415

Ala Lys Thr Ser Val Arg Lys Ser Thr Leu Ser Lys Met Leu Thr Asp
420 425 430

Ile Leu Asp Val Arg Val Met Ile Lys Lys Thr Met Asn Glu Ile Gly
435 440 445

Asp Asp Asn Thr Thr Leu Lys Arg Leu Leu Asn Asn Lys Gln Leu Ala
450 455 460

Leu Lys Leu Leu Ala Asn Val Thr Tyr Gly Tyr Thr Ser Ala Ser Phe
465 470 475 480

Ser Gly Arg Met Pro Cys Ser Asp Leu Ala Asp Ser Ile Val Gln Thr
485 490 495

Gly Arg Glu Thr Leu Glu Lys Ala Ile Asp Ile Ile Glu Lys Asp Glu
500 505 510

Thr Trp Asn Ala Lys Val Val Tyr Gly Asp Thr Asp Ser Leu Phe Val
515 520 525

Tyr Leu Pro Gly Lys Thr Ala Ile Glu Ala Phe Ser Ile Gly His Ala
530 535 540

Met Ala Glu Arg Val Thr Gln Asn Asn Pro Lys Pro Ile Phe Leu Lys
545 550 555 560

Phe Glu Lys Val Tyr His Pro Ser Ile Leu Ile Ser Lys Lys Arg Tyr
565 570 575

Val Gly Phe Ser Tyr Glu Ser Pro Ser Gln Thr Leu Pro Ile Phe Asp
580 585 590

Ala Lys Gly Ile Glu Thr Val Arg Arg Asp Gly Ile Pro Ala Gln Gln
595 600 605

Lys Ile Ile Glu Lys Cys Ile Arg Leu Leu Phe Gln Thr Lys Asp Leu
610 615 620

Ser Lys Ile Lys Lys Tyr Leu Gln Asn Glu Phe Phe Lys Ile Gln Ile
625 630 635 640

Gly Lys Val Ser Ala Gln Asp Phe Cys Phe Ala Lys Glu Val Lys Leu
645 650 655

Gly Ala Tyr Lys Ser Glu Lys Thr Ala Pro Ala Gly Ala Val Val Val
660 665 670

Lys Arg Arg Ile Asn Glu Asp His Arg Ala Glu Pro Gln Tyr Lys Glu
675 680 685

Arg Ile Pro Tyr Leu Val Val Lys Gly Lys Gln Gly Gln Leu Leu Arg
690 695 700

Glu Arg Cys Val Ser Pro Glu Glu Phe Leu Glu Gly Glu Asn Leu Glu
705 710 715 720

Leu Asp Ser Glu Tyr Tyr Ile Asn Lys Ile Leu Ile Pro Pro Leu Asp
725 730 735

Arg Leu Phe Asn Leu Ile Gly Ile Asn
740 745



32
727
PRT
Pyrococcus woesei

32

Phe Lys Ile Glu His Asp Arg Thr Phe Arg Pro Tyr Ile Tyr Ala Leu
1 5 10 15

Leu Arg Asp Asp Ser Lys Ile Glu Glu Val Lys Lys Ile Thr Gly Glu
20 25 30

Arg His Gly Lys Ile Val Arg Ile Val Asp Val Glu Lys Val Glu Lys
35 40 45

Lys Phe Leu Gly Lys Pro Ile Thr Val Trp Lys Leu Tyr Leu Glu His
50 55 60

Pro Gln Asp Val Pro Thr Ile Arg Glu Lys Val Arg Glu His Pro Ala
65 70 75 80

Val Val Asp Ile Phe Glu Tyr Asp Ile Pro Phe Ala Lys Arg Tyr Leu
85 90 95

Ile Asp Lys Gly Leu Ile Pro Met Glu Gly Glu Glu Glu Leu Lys Ile
100 105 110

Leu Ala Phe Asp Ile Glu Thr Leu Tyr His Glu Gly Glu Glu Phe Gly
115 120 125

Lys Gly Pro Ile Ile Met Ile Ser Tyr Ala Asp Glu Asn Glu Ala Lys
130 135 140

Val Ile Thr Trp Lys Asn Ile Asp Leu Pro Tyr Val Glu Val Val Ser
145 150 155 160

Ser Glu Arg Glu Met Ile Lys Arg Phe Leu Arg Ile Ile Arg Glu Lys
165 170 175

Asp Pro Asp Ile Ile Val Thr Tyr Asn Gly Asp Ser Phe Asp Phe Pro
180 185 190

Tyr Leu Ala Lys Arg Ala Glu Lys Leu Gly Ile Lys Leu Thr Ile Gly
195 200 205

Arg Asp Gly Ser Glu Pro Lys Met Gln Arg Ile Gly Asp Met Thr Ala
210 215 220

Val Glu Val Lys Gly Arg Ile His Phe Asp Leu Tyr His Val Ile Thr
225 230 235 240

Arg Thr Ile Asn Leu Pro Thr Tyr Thr Leu Glu Ala Val Tyr Glu Ala
245 250 255

Ile Phe Gly Lys Pro Lys Glu Lys Val Tyr Ala Asp Glu Ile Ala Lys
260 265 270

Ala Trp Glu Ser Gly Glu Asn Leu Glu Arg Val Ala Lys Tyr Ser Met
275 280 285

Glu Asp Ala Lys Ala Thr Tyr Glu Leu Gly Lys Glu Phe Leu Pro Met
290 295 300

Glu Ile Gln Leu Ser Arg Leu Val Gly Gln Pro Leu Trp Asp Val Ser
305 310 315 320

Arg Ser Ser Thr Gly Asn Leu Val Glu Trp Phe Leu Leu Arg Lys Ala
325 330 335

Tyr Glu Arg Asn Glu Val Ala Pro Asn Lys Pro Ser Glu Glu Glu Tyr
340 345 350

Gln Arg Arg Leu Arg Glu Ser Tyr Thr Gly Gly Phe Val Lys Glu Pro
355 360 365

Glu Lys Gly Leu Trp Glu Asn Ile Val Tyr Leu Asp Phe Arg Ala Leu
370 375 380

Tyr Pro Ser Ile Ile Ile Thr His Asn Val Ser Pro Asp Thr Leu Asn
385 390 395 400

Leu Glu Gly Cys Lys Asn Tyr Asp Ile Ala Pro Gln Val Gly His Lys
405 410 415

Phe Cys Lys Asp Ile Pro Gly Phe Ile Pro Ser Leu Leu Gly His Leu
420 425 430

Leu Glu Glu Arg Gln Lys Ile Lys Thr Lys Met Lys Glu Thr Gln Asp
435 440 445

Pro Ile Glu Lys Ile Leu Leu Asp Tyr Arg Gln Lys Ala Ile Lys Leu
450 455 460

Leu Ala Asn Ser Phe Tyr Gly Tyr Tyr Gly Tyr Ala Lys Ala Arg Trp
465 470 475 480

Tyr Cys Lys Glu Cys Ala Glu Ser Val Thr Ala Trp Gly Arg Lys Tyr
485 490 495

Ile Glu Leu Val Trp Lys Glu Leu Glu Glu Lys Phe Gly Phe Lys Val
500 505 510

Leu Tyr Ile Asp Thr Asp Gly Leu Tyr Ala Thr Ile Pro Gly Gly Glu
515 520 525

Ser Glu Glu Ile Lys Lys Lys Ala Leu Glu Phe Val Lys Tyr Ile Asn
530 535 540

Ser Lys Leu Pro Gly Leu Leu Glu Leu Glu Tyr Glu Gly Phe Tyr Lys
545 550 555 560

Arg Gly Phe Phe Val Thr Lys Lys Arg Tyr Ala Val Ile Asp Glu Glu
565 570 575

Gly Lys Val Ile Thr Arg Gly Leu Glu Ile Val Arg Arg Asp Trp Ser
580 585 590

Glu Ile Ala Lys Glu Thr Gln Ala Arg Val Leu Glu Thr Ile Leu Lys
595 600 605

His Gly Asp Val Glu Glu Ala Val Arg Ile Val Lys Glu Val Ile Gln
610 615 620

Lys Leu Ala Asn Tyr Glu Ile Pro Pro Glu Lys Leu Ala Ile Tyr Glu
625 630 635 640

Gln Ile Thr Arg Pro Leu His Glu Tyr Lys Ala Ile Gly Pro His Val
645 650 655

Ala Val Ala Lys Lys Leu Ala Ala Lys Gly Val Lys Ile Lys Pro Gly
660 665 670

Met Val Ile Gly Tyr Ile Val Leu Arg Gly Asp Gly Pro Ile Ser Asn
675 680 685

Arg Ala Ile Leu Ala Glu Glu Tyr Asp Pro Lys Lys His Lys Tyr Asp
690 695 700

Ala Glu Tyr Tyr Ile Glu Asn Gln Val Leu Pro Ala Val Leu Arg Ile
705 710 715 720

Leu Glu Gly Phe Gly Tyr Arg
725



33
702
PRT
Sulfolobus solfataricus

33

Phe Asn Asn Tyr Met Tyr Asp Ile Gly Leu Ile Pro Gly Met Pro Tyr
1 5 10 15

Val Val Lys Asn Gly Lys Leu Glu Ser Val Tyr Leu Ser Leu Asp Glu
20 25 30

Lys Asp Val Glu Glu Ile Lys Lys Ala Phe Ala Asp Ser Asp Glu Met
35 40 45

Thr Arg Gln Met Ala Val Asp Trp Leu Pro Ile Phe Glu Thr Glu Ile
50 55 60

Pro Lys Ile Lys Arg Val Ala Ile Asp Ile Glu Val Tyr Thr Pro Val
65 70 75 80

Lys Gly Arg Ile Pro Asp Ser Gln Lys Ala Glu Phe Pro Ile Ile Ser
85 90 95

Ile Ala Leu Ala Gly Ser Asp Gly Leu Lys Lys Val Leu Val Leu Asn
100 105 110

Arg Asn Asp Val Asn Glu Gly Ser Val Lys Leu Asp Gly Ile Ser Val
115 120 125

Glu Arg Phe Asn Thr Glu Tyr Glu Leu Leu Gly Arg Phe Phe Asp Ile
130 135 140

Leu Leu Glu Tyr Pro Ile Val Leu Thr Phe Asn Gly Asp Asp Phe Asp
145 150 155 160

Leu Pro Tyr Ile Tyr Phe Arg Ala Leu Lys Leu Gly Tyr Phe Pro Glu
165 170 175

Glu Ile Pro Ile Asp Val Ala Gly Lys Asp Glu Ala Lys Tyr Leu Ala
180 185 190

Gly Leu His Ile Asp Leu Tyr Lys Phe Phe Phe Asn Lys Ala Val Arg
195 200 205

Asn Tyr Ala Phe Glu Gly Lys Tyr Asn Glu Tyr Asn Leu Asp Ala Val
210 215 220

Ala Lys Ala Leu Leu Gly Thr Ser Lys Val Lys Val Asp Thr Leu Ile
225 230 235 240

Ser Phe Leu Asp Val Glu Lys Leu Ile Glu Tyr Asn Phe Arg Asp Ala
245 250 255

Glu Ile Thr Leu Gln Leu Thr Thr Phe Asn Asn Asp Leu Thr Met Lys
260 265 270

Leu Ile Val Leu Phe Ser Arg Ile Ser Arg Leu Gly Ile Glu Glu Leu
275 280 285

Thr Arg Thr Glu Ile Ser Thr Trp Val Lys Asn Leu Tyr Tyr Trp Glu
290 295 300

His Arg Lys Arg Asn Trp Leu Ile Pro Leu Lys Glu Glu Ile Leu Ala
305 310 315 320

Lys Ser Ser Asn Ile Arg Thr Ser Ala Leu Ile Lys Gly Lys Gly Tyr
325 330 335

Lys Gly Ala Val Val Ile Asp Pro Pro Ala Gly Ile Phe Phe Asn Ile
340 345 350

Thr Val Leu Asp Phe Ala Ser Leu Tyr Pro Ser Ile Ile Arg Thr Trp
355 360 365

Asn Leu Ser Tyr Glu Thr Val Asp Ile Gln Gln Cys Lys Lys Pro Tyr
370 375 380

Glu Val Lys Asp Glu Thr Gly Glu Val Leu His Ile Val Cys Met Asp
385 390 395 400

Arg Pro Gly Ile Thr Ala Val Ile Thr Gly Leu Leu Arg Asp Phe Arg
405 410 415

Val Lys Ile Tyr Lys Lys Lys Ala Lys Asn Pro Asn Asn Ser Glu Glu
420 425 430

Gln Lys Leu Leu Tyr Asp Val Val Gln Arg Ala Met Lys Val Phe Ile
435 440 445

Asn Ala Thr Tyr Gly Val Phe Gly Ala Glu Thr Phe Pro Leu Tyr Ala
450 455 460

Pro Arg Val Ala Glu Ser Val Thr Ala Leu Gly Arg Tyr Val Ile Thr
465 470 475 480

Ser Thr Val Lys Lys Ala Arg Glu Glu Gly Leu Thr Val Leu Tyr Gly
485 490 495

Asp Thr Asp Ser Leu Phe Leu Leu Asn Pro Pro Lys Asn Ser Leu Glu
500 505 510

Asn Ile Ile Lys Trp Val Lys Thr Thr Phe Asn Leu Asp Leu Glu Val
515 520 525

Asp Lys Thr Tyr Lys Phe Val Ala Phe Ser Gly Leu Lys Lys Asn Tyr
530 535 540

Phe Gly Val Tyr Gln Asp Gly Lys Val Asp Ile Lys Gly Met Leu Val
545 550 555 560

Lys Lys Arg Asn Thr Pro Glu Phe Val Lys Lys Val Phe Asn Glu Val
565 570 575

Lys Glu Leu Met Ile Ser Ile Asn Ser Pro Asn Asp Val Lys Glu Ile
580 585 590

Lys Arg Lys Ile Val Asp Val Val Lys Gly Ser Tyr Glu Lys Leu Lys
595 600 605

Asn Lys Gly Tyr Asn Leu Asp Glu Leu Ala Phe Lys Val Met Leu Ser
610 615 620

Lys Pro Leu Asp Ala Tyr Lys Lys Asn Thr Pro Gln His Val Lys Ala
625 630 635 640

Ala Leu Gln Leu Arg Pro Phe Gly Val Asn Val Leu Pro Arg Asp Ile
645 650 655

Ile Tyr Tyr Val Lys Val Arg Ser Lys Asp Gly Val Lys Pro Val Gln
660 665 670

Leu Ala Lys Val Thr Glu Ile Asp Ala Glu Lys Tyr Leu Glu Ala Leu
675 680 685

Arg Ser Thr Phe Glu Gln Ile Leu Arg Ala Phe Gly Val Ser
690 695 700



34
719
PRT
Escherichia coli

34

Ala Gln His Ile Leu Gln Gly Glu Gln Gly Phe Arg Leu Thr Pro Leu
1 5 10 15

Ala Leu Lys Asp Phe His Arg Gln Pro Val Tyr Gly Leu Tyr Cys Arg
20 25 30

Ala His Arg Gln Leu Met Asn Tyr Glu Lys Arg Leu Arg Glu Gly Gly
35 40 45

Val Thr Val Tyr Glu Ala Asp Val Arg Pro Pro Glu Arg Tyr Leu Met
50 55 60

Glu Arg Phe Ile Thr Ser Pro Val Trp Val Glu Gly Asp Met His Asn
65 70 75 80

Gly Thr Ile Val Asn Ala Arg Leu Lys Pro His Pro Asp Tyr Arg Pro
85 90 95

Pro Leu Lys Trp Val Ser Ile Asp Ile Glu Thr Thr Arg His Gly Glu
100 105 110

Leu Tyr Cys Ile Gly Leu Glu Gly Cys Gly Gln Arg Ile Val Tyr Met
115 120 125

Leu Gly Pro Glu Asn Gly Asp Ala Ser Ser Leu Asp Phe Glu Leu Glu
130 135 140

Tyr Val Ala Ser Arg Pro Gln Leu Leu Glu Lys Leu Asn Ala Trp Phe
145 150 155 160

Ala Asn Tyr Asp Pro Asp Val Ile Ile Gly Trp Asn Val Val Gln Phe
165 170 175

Asp Leu Arg Met Leu Gln Lys His Ala Glu Arg Tyr Arg Leu Pro Leu
180 185 190

Arg Leu Gly Arg Asp Asn Ser Glu Leu Glu Trp Arg Glu His Gly Phe
195 200 205

Lys Asn Gly Val Phe Phe Ala Gln Ala Lys Gly Arg Leu Ile Ile Asp
210 215 220

Gly Ile Glu Ala Leu Lys Ser Ala Phe Trp Asn Phe Ser Ser Phe Ser
225 230 235 240

Leu Glu Thr Val Ala Gln Glu Leu Leu Gly Glu Gly Lys Ser Ile Asp
245 250 255

Asn Pro Trp Asp Arg Met Asp Glu Ile Asp Arg Arg Phe Ala Glu Asp
260 265 270

Lys Pro Ala Leu Ala Thr Tyr Asn Leu Lys Asp Cys Glu Leu Val Thr
275 280 285

Gln Ile Phe His Lys Thr Glu Ile Met Pro Phe Leu Leu Glu Arg Ala
290 295 300

Thr Val Asn Gly Leu Pro Val Asp Arg His Gly Gly Ser Val Ala Ala
305 310 315 320

Phe Gly His Leu Tyr Phe Pro Arg Met His Arg Ala Gly Tyr Val Ala
325 330 335

Pro Asn Leu Gly Glu Val Pro Pro His Ala Ser Pro Gly Gly Tyr Val
340 345 350

Met Asp Ser Arg Pro Gly Leu Tyr Asp Ser Val Leu Val Leu Asp Tyr
355 360 365

Lys Ser Leu Tyr Pro Ser Ile Ile Arg Thr Phe Leu Ile Asp Pro Val
370 375 380

Gly Leu Val Glu Gly Met Ala Gln Pro Asp Pro Glu His Ser Thr Glu
385 390 395 400

Gly Phe Leu Asp Ala Trp Phe Ser Arg Glu Lys His Cys Leu Pro Glu
405 410 415

Ile Val Thr Asn Ile Trp His Gly Arg Asp Glu Ala Lys Arg Gln Gly
420 425 430

Asn Lys Pro Leu Ser Gln Ala Leu Lys Ile Ile Met Asn Ala Phe Tyr
435 440 445

Gly Val Leu Gly Thr Thr Ala Cys Arg Phe Phe Asp Pro Arg Leu Ala
450 455 460

Ser Ser Ile Thr Met Arg Gly His Gln Ile Met Arg Gln Thr Lys Ala
465 470 475 480

Leu Ile Glu Ala Gln Gly Tyr Asp Val Ile Tyr Gly Asp Thr Asp Ser
485 490 495

Thr Phe Val Trp Leu Lys Gly Ala His Ser Glu Glu Glu Ala Ala Lys
500 505 510

Ile Gly Arg Ala Leu Val Gln His Val Asn Ala Trp Trp Ala Glu Thr
515 520 525

Leu Gln Lys Gln Arg Leu Thr Ser Ala Leu Glu Leu Glu Tyr Glu Thr
530 535 540

His Phe Cys Arg Phe Leu Met Pro Thr Ile Arg Gly Ala Asp Thr Gly
545 550 555 560

Ser Lys Lys Arg Tyr Ala Gly Leu Ile Gln Glu Gly Asp Lys Gln Arg
565 570 575

Met Val Phe Lys Gly Leu Glu Thr Val Arg Thr Asp Trp Thr Pro Leu
580 585 590

Ala Gln Gln Phe Gln Gln Glu Leu Tyr Leu Arg Ile Phe Arg Asn Glu
595 600 605

Pro Tyr Gln Glu Tyr Val Arg Glu Thr Ile Asp Lys Leu Met Ala Gly
610 615 620

Glu Leu Asp Ala Arg Leu Val Tyr Arg Lys Arg Leu Arg Arg Pro Leu
625 630 635 640

Ser Glu Tyr Gln Arg Asn Val Pro Pro His Val Arg Ala Ala Arg Leu
645 650 655

Ala Asp Glu Glu Asn Gln Lys Arg Gly Arg Pro Leu Gln Tyr Gln Asn
660 665 670

Arg Gly Thr Ile Lys Tyr Val Trp Thr Thr Asn Gly Pro Glu Pro Leu
675 680 685

Asp Tyr Gln Arg Ser Pro Leu Asp Tyr Glu His Tyr Leu Thr Arg Gln
690 695 700

Leu Gln Pro Val Ala Glu Gly Ile Leu Pro Phe Ile Glu Asp Asn
705 710 715



35
773
PRT
Desilforococcus strain Tok

35

Met Ile Leu Asp Ala Asp Tyr Ile Thr Glu Asp Gly Lys Pro Val Ile
1 5 10 15

Arg Val Phe Lys Lys Glu Lys Gly Glu Phe Lys Ile Asp Tyr Asp Arg
20 25 30

Asp Phe Glu Pro Tyr Ile Tyr Ala Leu Leu Lys Asp Asp Ser Ala Ile
35 40 45

Glu Asp Ile Lys Lys Ile Thr Ala Glu Arg His Gly Thr Thr Val Arg
50 55 60

Val Thr Arg Ala Glu Arg Val Lys Lys Lys Phe Leu Gly Arg Pro Val
65 70 75 80

Glu Val Trp Lys Leu Tyr Phe Thr His Pro Gln Asp Val Pro Ala Ile
85 90 95

Arg Asp Lys Ile Arg Glu His Pro Ala Val Val Asp Ile Tyr Glu Tyr
100 105 110

Asp Ile Pro Phe Ala Lys Arg Tyr Leu Ile Asp Arg Gly Leu Ile Pro
115 120 125

Met Glu Gly Asp Glu Glu Leu Arg Met Leu Ala Phe Asp Ile Glu Thr
130 135 140

Leu Tyr His Glu Gly Glu Glu Phe Gly Glu Gly Pro Ile Leu Met Ile
145 150 155 160

Ser Tyr Ala Asp Glu Glu Gly Ala Arg Val Ile Thr Trp Lys Asn Ile
165 170 175

Asp Leu Pro Tyr Val Glu Ser Val Ser Thr Glu Lys Glu Met Ile Lys
180 185 190

Arg Phe Leu Lys Val Ile Gln Glu Lys Asp Pro Asp Val Leu Ile Thr
195 200 205

Tyr Asn Gly Asp Asn Phe Asp Phe Ala Tyr Leu Lys Lys Arg Ser Glu
210 215 220

Met Leu Gly Val Lys Phe Ile Leu Gly Arg Asp Gly Ser Glu Pro Lys
225 230 235 240

Ile Gln Arg Met Gly Asp Arg Phe Ala Val Glu Val Lys Gly Arg Ile
245 250 255

His Phe Asp Leu Tyr Pro Val Ile Arg Arg Thr Ile Asn Leu Pro Thr
260 265 270

Tyr Thr Leu Glu Thr Val Tyr Glu Pro Val Phe Gly Gln Pro Lys Glu
275 280 285

Lys Val Tyr Ala Glu Glu Ile Ala Arg Ala Trp Glu Ser Gly Glu Gly
290 295 300

Leu Glu Arg Val Ala Arg Tyr Ser Met Glu Asp Ala Lys Ala Thr Tyr
305 310 315 320

Glu Leu Gly Lys Glu Phe Phe Pro Met Glu Ala Gln Leu Ser Arg Leu
325 330 335

Val Gly Gln Ser Leu Trp Asp Val Ser Arg Ser Ser Thr Gly Asn Leu
340 345 350

Val Glu Trp Phe Leu Leu Arg Lys Ala Tyr Glu Arg Asn Asp Val Ala
355 360 365

Pro Asn Lys Pro Asp Glu Arg Glu Leu Ala Arg Arg Thr Glu Ser Tyr
370 375 380

Ala Gly Gly Tyr Val Lys Glu Pro Glu Lys Gly Leu Trp Glu Asn Ile
385 390 395 400

Val Tyr Leu Asp Tyr Lys Ser Leu Tyr Pro Ser Ile Ile Ile Thr His
405 410 415

Asn Val Ser Pro Asp Thr Leu Asn Arg Glu Gly Cys Arg Glu Tyr Asp
420 425 430

Val Ala Pro Gln Val Gly His Arg Phe Cys Lys Asp Phe Pro Gly Phe
435 440 445

Ile Pro Ser Leu Leu Gly Asp Leu Leu Glu Glu Arg Gln Lys Val Lys
450 455 460

Lys Lys Met Lys Ala Thr Val Asp Pro Ile Glu Arg Lys Leu Leu Asp
465 470 475 480

Tyr Arg Gln Arg Ala Ile Lys Ile Leu Ala Asn Ser Tyr Tyr Gly Tyr
485 490 495

Tyr Ala Tyr Ala Asn Ala Arg Trp Tyr Cys Arg Glu Cys Ala Glu Ser
500 505 510

Val Thr Ala Trp Gly Arg Gln Tyr Ile Glu Thr Thr Met Arg Glu Ile
515 520 525

Glu Glu Lys Phe Gly Phe Lys Val Leu Tyr Ala Asp Thr Asp Gly Phe
530 535 540

Phe Ala Thr Ile Pro Gly Ala Asp Ala Glu Thr Val Lys Asn Lys Ala
545 550 555 560

Lys Glu Phe Leu Asn Tyr Ile Asn Pro Arg Leu Pro Gly Leu Leu Glu
565 570 575

Leu Glu Tyr Glu Gly Phe Tyr Arg Arg Gly Phe Phe Val Thr Lys Lys
580 585 590

Lys Tyr Ala Val Ile Asp Glu Glu Asp Lys Ile Thr Thr Arg Gly Leu
595 600 605

Glu Ile Val Arg Arg Asp Trp Ser Glu Ile Ala Lys Glu Thr Gln Ala
610 615 620

Arg Val Leu Glu Ala Ile Leu Lys His Gly Asp Val Glu Glu Ala Val
625 630 635 640

Arg Ile Val Lys Glu Val Thr Glu Lys Leu Ser Arg His Glu Val Pro
645 650 655

Pro Glu Lys Leu Val Ile Tyr Glu Gln Ile Thr Arg Asp Leu Arg Ser
660 665 670

Tyr Arg Ala Thr Gly Pro His Val Ala Val Ala Lys Arg Leu Ala Ala
675 680 685

Arg Gly Ile Lys Ile Arg Pro Gly Thr Val Ile Ser Tyr Ile Val Leu
690 695 700

Lys Gly Pro Gly Arg Val Gly Asp Arg Ala Ile Pro Phe Asp Glu Phe
705 710 715 720

Asp Pro Ala Lys His Arg Tyr Asp Ala Glu Tyr Tyr Ile Glu Asn Gln
725 730 735

Val Leu Pro Ala Val Glu Arg Ile Leu Arg Ala Phe Gly Tyr Arg Lys
740 745 750

Glu Asp Leu Arg Tyr Gln Lys Thr Lys Gln Ala Gly Leu Gly Ala Trp
755 760 765

Leu Lys Pro Lys Thr
770



36
871
PRT
Bacteriophage RM378

36

Met Lys Ile Thr Leu Ser Ala Ser Val Tyr Pro Arg Ser Met Lys Ile
1 5 10 15

Tyr Gly Val Glu Leu Ile Glu Gly Lys Lys His Leu Phe Gln Ser Pro
20 25 30

Val Pro Pro His Leu Lys Arg Ile Ala Gln Gln Asn Arg Gly Lys Ile
35 40 45

Glu Ala Glu Ala Ile Ser Tyr Tyr Ile Arg Glu Gln Lys Ser His Ile
50 55 60

Thr Pro Glu Ala Leu Ser Gln Cys Val Phe Ile Asp Ile Glu Thr Ile
65 70 75 80

Ser Pro Lys Lys Ser Phe Pro Asp Pro Trp Arg Asp Pro Val Tyr Ser
85 90 95

Ile Ser Ile Lys Pro Tyr Gly Lys Pro Val Val Val Val Leu Leu Leu
100 105 110

Ile Thr Asn Pro Glu Ala His Ile Asp Asn Phe Asn Lys Phe Thr Thr
115 120 125

Ser Val Gly Asp Asn Thr Phe Glu Ile His Tyr Arg Thr Phe Leu Ser
130 135 140

Glu Lys Arg Leu Leu Glu Tyr Phe Trp Asn Val Leu Lys Pro Lys Phe
145 150 155 160

Thr Phe Met Leu Ala Trp Asn Gly Tyr Gln Phe Asp Tyr Pro Tyr Leu
165 170 175

Leu Ile Arg Ser His Ile His Glu Val Asn Val Ile Ser Asp Lys Leu
180 185 190

Leu Pro Asp Trp Lys Leu Val Arg Lys Ile Ser Asp Arg Asn Leu Pro
195 200 205

Phe Tyr Phe Asn Pro Arg Thr Pro Val Glu Phe Val Phe Phe Asp Tyr
210 215 220

Met Arg Leu Tyr Arg Ser Phe Val Ala Tyr Lys Glu Leu Glu Ser Tyr
225 230 235 240

Arg Leu Asp Tyr Ile Ala Arg Glu Glu Ile Gly Glu Gly Lys Val Asp
245 250 255

Phe Asp Val Arg Phe Tyr His Glu Ile Pro Val Tyr Pro Asp Lys Lys
260 265 270

Leu Val Glu Tyr Asn Ala Val Asp Ala Ile Leu Met Glu Glu Ile Glu
275 280 285

Asn Lys Asn His Ile Leu Pro Thr Leu Phe Glu Ile Ala Arg Leu Ser
290 295 300

Asn Leu Thr Pro Ala Leu Ala Leu Asn Ala Ser Asn Ile Leu Ile Gly
305 310 315 320

Asn Val Thr Gly Lys Leu Gly Val Lys Phe Val Asp Tyr Ile Lys Lys
325 330 335

Ile Asp Thr Ile Asn Thr Met Phe Lys Lys Ile Pro Glu Met Asn Ile
340 345 350

Asn Lys Tyr Arg Tyr Arg Gly Ala Tyr Ile Glu Leu Thr Asn Pro Asp
355 360 365

Ile Tyr Phe Asn Val Phe Asp Leu Asp Phe Thr Ser Leu Tyr Pro Ser
370 375 380

Val Ile Ser Lys Phe Asn Ile Asp Pro Ala Thr Phe Val Thr Glu Phe
385 390 395 400

Tyr Gly Cys Met Arg Val Glu Asn Lys Val Ile Pro Val Asp Gln Glu
405 410 415

Glu Pro Glu Phe Gly Phe Pro Leu Tyr Ile Phe Asp Ser Gly Met Asn
420 425 430

Pro Ser Tyr Arg Ser Glu Pro Leu Phe Val Ile Asn Ser Phe Glu Glu
435 440 445

Leu Arg Gln Phe Leu Lys Ser Arg Asn Ile Ile Met Val Pro Asn Pro
450 455 460

Ser Gly Ile Cys Trp Phe Tyr Arg Lys Glu Pro Val Gly Val Leu Pro
465 470 475 480

Ser Ile Ile Arg Glu Ile Phe Thr Arg Arg Lys Glu Glu Arg Lys Leu
485 490 495

Phe Lys Glu Thr Gly Asn Met Glu His His Phe Arg Gln Trp Ala Leu
500 505 510

Lys Ile Met Met Asn Ser Met Tyr Gly Ile Phe Gly Asn Arg Ser Val
515 520 525

Tyr Met Gly Cys Leu Pro Ile Ala Glu Ser Val Thr Ala Ala Gly Arg
530 535 540

Met Ser Ile Arg Ser Val Ile Ser Gln Ile Arg Asp Arg Phe Ile Tyr
545 550 555 560

Ser His Thr Asp Ser Ile Phe Val Lys Ala Phe Thr Asp Asp Pro Val
565 570 575

Ala Glu Ala Gly Glu Leu Gln Glu His Leu Asn Ser Phe Ile Asn Asp
580 585 590

Tyr Met Glu Asn Asn Phe Asn Ala Arg Glu Asp Phe Lys Leu Glu Leu
595 600 605

Lys Gln Glu Phe Val Phe Lys Ser Ile Leu Ile Lys Glu Ile Asn Arg
610 615 620

Tyr Phe Ala Val Thr Val Asp Gly Lys Glu Glu Met Lys Gly Ile Glu
625 630 635 640

Val Ile Asn Ser Ser Val Pro Glu Ile Val Lys Lys Tyr Phe Arg Gly
645 650 655

Tyr Leu Lys Tyr Ile Ser Gln Pro Asp Ile Asp Val Ile Ser Ala Thr
660 665 670

Ile Ala Phe Tyr Asn Asn Phe Val Ser Gln Lys Asn Phe Trp Ser Ile
675 680 685

Glu Asp Leu Tyr His Lys Met Lys Ile Ser Ser Ser Asp Ser Ala Glu
690 695 700

Arg Tyr Val Glu Tyr Val Glu Glu Val Met Lys Met Lys Lys Glu Asn
705 710 715 720

Val Pro Ile Ser Glu Ile Phe Ile Lys Met Tyr Asp His Thr Leu Pro
725 730 735

Ile His Tyr Lys Gly Ala Leu Phe Ala Ser Ile Ile Gly Cys Lys Pro
740 745 750

Pro Gln Met Gly Asp Lys Ile Tyr Trp Phe Tyr Cys Thr Met Leu Asp
755 760 765

Pro Ser Arg Thr Asn Leu Pro Leu Ser Leu Glu Glu Val Asn Pro Glu
770 775 780

His Gly Ser Gly Val Trp Asp Ile Leu Lys Ala Gly Lys Lys Thr His
785 790 795 800

Ile Asn Arg Leu Arg Asn Ile His Ala Leu Ser Ile Arg Glu Asp Asp
805 810 815

Glu Glu Gly Leu Glu Ile Val Lys Lys Tyr Ile Asp Arg Asp Lys Tyr
820 825 830

Cys Gln Ile Ile Ser Glu Lys Thr Ile Asp Leu Leu Lys Ser Leu Gly
835 840 845

Tyr Val Glu Asn Thr Thr Lys Ile Lys Thr Val Glu Asp Leu Ile Arg
850 855 860

Phe Leu Val Glu Ser Glu Asn
865 870



37
898
PRT
Bacteriophage RB69

37

Met Lys Glu Phe Tyr Leu Thr Val Glu Gln Ile Gly Asp Ser Ile Phe
1 5 10 15

Glu Arg Tyr Ile Asp Ser Asn Gly Arg Glu Arg Thr Arg Glu Val Glu
20 25 30

Tyr Lys Pro Ser Leu Phe Ala His Cys Pro Glu Ser Gln Ala Thr Lys
35 40 45

Tyr Phe Asp Ile Tyr Gly Lys Pro Cys Thr Arg Lys Leu Phe Ala Asn
50 55 60

Met Arg Asp Ala Ser Gln Trp Ile Lys Arg Met Glu Asp Ile Gly Leu
65 70 75 80

Glu Ala Leu Gly Met Asp Asp Phe Lys Leu Ala Tyr Leu Ser Asp Thr
85 90 95

Tyr Asn Tyr Glu Ile Lys Tyr Asp His Thr Lys Ile Arg Val Ala Asn
100 105 110

Phe Asp Ile Glu Val Thr Ser Pro Asp Gly Phe Pro Glu Pro Ser Gln
115 120 125

Ala Lys His Pro Ile Asp Ala Ile Thr His Tyr Asp Ser Ile Asp Asp
130 135 140

Arg Phe Tyr Val Phe Asp Leu Leu Asn Ser Pro Tyr Gly Asn Val Glu
145 150 155 160

Glu Trp Ser Ile Glu Ile Ala Ala Lys Leu Gln Glu Gln Gly Gly Asp
165 170 175

Glu Val Pro Ser Glu Ile Ile Asp Lys Ile Ile Tyr Met Pro Phe Asp
180 185 190

Asn Glu Lys Glu Leu Leu Met Glu Tyr Leu Asn Phe Trp Gln Gln Lys
195 200 205

Thr Pro Val Ile Leu Thr Gly Trp Asn Val Glu Ser Phe Asp Ile Pro
210 215 220

Tyr Val Tyr Asn Arg Ile Lys Asn Ile Phe Gly Glu Ser Thr Ala Lys
225 230 235 240

Arg Leu Ser Pro His Arg Lys Thr Arg Val Lys Val Ile Glu Asn Met
245 250 255

Tyr Gly Ser Arg Glu Ile Ile Thr Leu Phe Gly Ile Ser Val Leu Asp
260 265 270

Tyr Ile Asp Leu Tyr Lys Lys Phe Ser Phe Thr Asn Gln Pro Ser Tyr
275 280 285

Ser Leu Asp Tyr Ile Ser Glu Phe Glu Leu Asn Val Gly Lys Leu Lys
290 295 300

Tyr Asp Gly Pro Ile Ser Lys Leu Arg Glu Ser Asn His Gln Arg Tyr
305 310 315 320

Ile Ser Tyr Asn Ile Ile Asp Val Tyr Arg Val Leu Gln Ile Asp Ala
325 330 335

Lys Arg Gln Phe Ile Asn Leu Ser Leu Asp Met Gly Tyr Tyr Ala Lys
340 345 350

Ile Gln Ile Gln Ser Val Phe Ser Pro Ile Lys Thr Trp Asp Ala Ile
355 360 365

Ile Phe Asn Ser Leu Lys Glu Gln Asn Lys Val Ile Pro Gln Gly Arg
370 375 380

Ser His Pro Val Gln Pro Tyr Pro Gly Ala Phe Val Lys Glu Pro Ile
385 390 395 400

Pro Asn Arg Tyr Lys Tyr Val Met Ser Phe Asp Leu Thr Ser Leu Tyr
405 410 415

Pro Ser Ile Ile Arg Gln Val Asn Ile Ser Pro Glu Thr Ile Ala Gly
420 425 430

Thr Phe Lys Val Ala Pro Leu His Asp Tyr Ile Asn Ala Val Ala Glu
435 440 445

Arg Pro Ser Asp Val Tyr Ser Cys Ser Pro Asn Gly Met Met Tyr Tyr
450 455 460

Lys Asp Arg Asp Gly Val Val Pro Thr Glu Ile Thr Lys Val Phe Asn
465 470 475 480

Gln Arg Lys Glu His Lys Gly Tyr Met Leu Ala Ala Gln Arg Asn Gly
485 490 495

Glu Ile Ile Lys Glu Ala Leu His Asn Pro Asn Leu Ser Val Asp Glu
500 505 510

Pro Leu Asp Val Asp Tyr Arg Phe Asp Phe Ser Asp Glu Ile Lys Glu
515 520 525

Lys Ile Lys Lys Leu Ser Ala Lys Ser Leu Asn Glu Met Leu Phe Arg
530 535 540

Ala Gln Arg Thr Glu Val Ala Gly Met Thr Ala Gln Ile Asn Arg Lys
545 550 555 560

Leu Leu Ile Asn Ser Leu Tyr Gly Ala Leu Gly Asn Val Trp Phe Arg
565 570 575

Tyr Tyr Asp Leu Arg Asn Ala Thr Ala Ile Thr Thr Phe Gly Gln Met
580 585 590

Ala Leu Gln Trp Ile Glu Arg Lys Val Asn Glu Tyr Leu Asn Glu Val
595 600 605

Cys Gly Thr Glu Gly Glu Ala Phe Val Leu Tyr Gly Asp Thr Asp Ser
610 615 620

Ile Tyr Val Ser Ala Asp Lys Ile Ile Asp Lys Val Gly Glu Ser Lys
625 630 635 640

Phe Arg Asp Thr Asn His Trp Val Asp Phe Leu Asp Lys Phe Ala Arg
645 650 655

Glu Arg Met Glu Pro Ala Ile Asp Arg Gly Phe Arg Glu Met Cys Glu
660 665 670

Tyr Met Asn Asn Lys Gln His Leu Met Phe Met Asp Arg Glu Ala Ile
675 680 685

Ala Gly Pro Pro Leu Gly Ser Lys Gly Ile Gly Gly Phe Trp Thr Gly
690 695 700

Lys Lys Arg Tyr Ala Leu Asn Val Trp Asp Met Glu Gly Thr Arg Tyr
705 710 715 720

Ala Glu Pro Lys Leu Lys Ile Met Gly Leu Glu Thr Gln Lys Ser Ser
725 730 735

Thr Pro Lys Ala Val Gln Lys Ala Leu Lys Glu Cys Ile Arg Arg Met
740 745 750

Leu Gln Glu Gly Glu Glu Ser Leu Gln Glu Tyr Phe Lys Glu Phe Glu
755 760 765

Lys Glu Phe Arg Gln Leu Asn Tyr Ile Ser Ile Ala Ser Val Ser Ser
770 775 780

Ala Asn Asn Ile Ala Lys Tyr Asp Val Gly Gly Phe Pro Gly Pro Lys
785 790 795 800

Cys Pro Phe His Ile Arg Gly Ile Leu Thr Tyr Asn Arg Ala Ile Lys
805 810 815

Gly Asn Ile Asp Ala Pro Gln Val Val Glu Gly Glu Lys Val Tyr Val
820 825 830

Leu Pro Leu Arg Glu Gly Asn Pro Phe Gly Asp Lys Cys Ile Ala Trp
835 840 845

Pro Ser Gly Thr Glu Ile Thr Asp Leu Ile Lys Asp Asp Val Leu His
850 855 860

Trp Met Asp Tyr Thr Val Leu Leu Glu Lys Thr Phe Ile Lys Pro Leu
865 870 875 880

Glu Gly Phe Thr Ser Ala Ala Lys Leu Asp Tyr Glu Lys Lys Ala Ser
885 890 895

Leu Phe



38
394
PRT
Autographa californica nucleopolynedrovirus

38

Met Leu His Val Ser Arg Leu Leu Ala Asn Gly Gly Val Lys Asn Leu
1 5 10 15

Cys Asp Lys Phe Lys Val Lys Ile Lys Asn Tyr Thr Glu His Asp Leu
20 25 30

Met Val Leu Asn Tyr Glu Ser Phe Glu Arg Asp Arg Asp His Pro Val
35 40 45

Val Val Glu Cys Arg Gly Leu Ile Leu Asn Ser Arg Thr Tyr Ala Val
50 55 60

Val Ser Arg Ser Phe Asp Arg Phe Phe Asn Phe Gln Glu Leu Leu Gln
65 70 75 80

Asn Ile Gly Gly Glu Asp Ala His His Lys Leu Phe Gln Ser Lys Glu
85 90 95

Asn Phe Lys Phe Tyr Glu Lys Ile Asp Gly Ser Leu Ile Lys Ile Tyr
100 105 110

Lys Tyr Asn Gly Glu Trp His Ala Ser Thr Arg Gly Ser Ala Phe Ala
115 120 125

Glu Asn Leu Cys Val Ser Asp Val Thr Phe Lys Arg Leu Val Leu Gln
130 135 140

Ala Leu Gln Leu Asp Glu Ala His Asn Gln Phe Gln Ala Leu Cys Asn
145 150 155 160

Glu Tyr Leu Asp Cys Ala Ser Thr His Met Phe Glu Leu Thr Ser Lys
165 170 175

His Asn Arg Ile Val Thr Val Tyr Asp Glu Gln Pro Thr Leu Trp Tyr
180 185 190

Leu Ala Ser Arg Asn Asn Glu Thr Gly Asp Tyr Phe Tyr Cys Ser Asn
195 200 205

Leu Pro Phe Cys Lys Tyr Pro Lys Cys Tyr Glu Phe Thr Ser Val Gln
210 215 220

Glu Cys Val Glu His Ala Ala Gln Leu Lys Asn Leu Glu Glu Gly Phe
225 230 235 240

Val Val Tyr Asp Lys Asn Asn Ala Pro Leu Cys Lys Ile Lys Ser Asp
245 250 255

Val Tyr Leu Asn Met His Lys Asn Gln Ser Arg Ala Glu Asn Pro Thr
260 265 270

Lys Leu Ala Gln Leu Val Ile Asn Gly Glu His Asp Asp Phe Leu Ala
275 280 285

Leu Phe Pro His Leu Lys Ser Val Ile Lys Pro Tyr Val Asp Ala Arg
290 295 300

Asn Thr Phe Thr Asn Glu Ser Thr Ile Asn Ile Met Val Ser Gly Leu
305 310 315 320

Thr Leu Asn Gln Gln Arg Phe Asn Glu Leu Val Gln Thr Leu Pro Trp
325 330 335

Lys Cys Leu Ala Tyr Arg Cys Arg Lys Ala Gln Thr Ile Asp Val Glu
340 345 350

Ser Glu Phe Leu Lys Leu Thr Glu Pro Glu Lys Ile Lys Met Ile Lys
355 360 365

Asn Ile Ile Lys Phe Val Ser Thr Lys Gln Ala Leu Asn Asn Lys Leu
370 375 380

Ala Pro Thr Ile Lys Leu Pro Ser Ser Lys
385 390



39
374
PRT
Bacteriophage T4

39

Met Gln Glu Leu Phe Asn Asn Leu Met Glu Leu Cys Lys Asp Ser Gln
1 5 10 15

Arg Lys Phe Phe Tyr Ser Asp Asp Val Ser Ala Ser Gly Arg Thr Tyr
20 25 30

Arg Ile Phe Ser Tyr Asn Tyr Ala Ser Tyr Ser Asp Trp Leu Leu Pro
35 40 45

Asp Ala Leu Glu Cys Arg Gly Ile Met Phe Glu Met Asp Gly Glu Lys
50 55 60

Pro Val Arg Ile Ala Ser Arg Pro Met Glu Lys Phe Phe Asn Leu Asn
65 70 75 80

Glu Asn Pro Phe Thr Met Asn Ile Asp Leu Asn Asp Val Asp Tyr Ile
85 90 95

Leu Thr Lys Glu Asp Gly Ser Leu Val Ser Thr Tyr Leu Asp Gly Asp
100 105 110

Glu Ile Leu Phe Lys Ser Lys Gly Ser Ile Lys Ser Glu Gln Ala Leu
115 120 125

Met Ala Asn Gly Ile Leu Met Asn Ile Asn His His Arg Leu Arg Asp
130 135 140

Arg Leu Lys Glu Leu Ala Glu Asp Gly Phe Thr Ala Asn Phe Glu Phe
145 150 155 160

Val Ala Pro Thr Asn Arg Ile Val Leu Ala Tyr Gln Glu Met Lys Ile
165 170 175

Ile Leu Leu Asn Val Arg Glu Asn Glu Thr Gly Glu Tyr Ile Ser Tyr
180 185 190

Asp Asp Ile Tyr Lys Asp Ala Thr Leu Arg Pro Tyr Leu Val Glu Arg
195 200 205

Tyr Glu Ile Asp Ser Pro Lys Trp Ile Glu Glu Ala Lys Asn Ala Glu
210 215 220

Asn Ile Glu Gly Tyr Val Ala Val Met Lys Asp Gly Ser His Phe Lys
225 230 235 240

Ile Lys Ser Asp Trp Tyr Val Ser Leu His Ser Thr Lys Ser Ser Leu
245 250 255

Asp Asn Pro Glu Lys Leu Phe Lys Thr Ile Ile Asp Gly Ala Ser Asp
260 265 270

Asp Leu Lys Ala Met Tyr Ala Asp Asp Glu Tyr Ser Tyr Arg Lys Ile
275 280 285

Glu Ala Phe Glu Thr Thr Tyr Leu Lys Tyr Leu Asp Arg Ala Leu Phe
290 295 300

Leu Val Leu Asp Cys His Asn Lys His Cys Gly Lys Asp Arg Lys Thr
305 310 315 320

Tyr Ala Met Glu Ala Gln Gly Val Ala Lys Gly Ala Gly Met Asp His
325 330 335

Leu Phe Gly Ile Ile Met Ser Leu Tyr Gln Gly Tyr Asp Ser Gln Glu
340 345 350

Lys Val Met Cys Glu Ile Glu Gln Asn Phe Leu Lys Asn Tyr Lys Lys
355 360 365

Phe Ile Pro Glu Gly Tyr
370



40
437
PRT
Bacteriophage RM378

40

Met Ser Met Asn Val Lys Tyr Pro Val Glu Tyr Leu Ile Glu His Leu
1 5 10 15

Asn Ser Phe Glu Ser Pro Glu Val Ala Val Glu Ser Leu Arg Lys Glu
20 25 30

Gly Ile Met Cys Lys Asn Arg Gly Asp Leu Tyr Met Phe Lys Tyr His
35 40 45

Leu Gly Cys Lys Phe Asp Lys Ile Tyr His Leu Ala Cys Arg Gly Ala
50 55 60

Ile Leu Arg Lys Thr Asp Ser Gly Trp Lys Val Leu Ser Tyr Pro Phe
65 70 75 80

Asp Lys Phe Phe Asn Trp Gly Glu Glu Leu Gln Pro Glu Ile Val Asn
85 90 95

Tyr Tyr Gln Thr Leu Arg Tyr Ala Ser Pro Leu Asn Glu Lys Arg Lys
100 105 110

Ala Gly Phe Met Phe Lys Leu Pro Met Lys Leu Val Glu Lys Leu Asp
115 120 125

Gly Thr Cys Val Val Leu Tyr Tyr Asp Glu Gly Trp Lys Ile His Thr
130 135 140

Leu Gly Ser Ile Asp Ala Asn Gly Ser Ile Val Lys Asn Gly Met Val
145 150 155 160

Thr Thr His Met Asp Lys Thr Tyr Arg Glu Leu Phe Trp Glu Thr Phe
165 170 175

Glu Lys Lys Tyr Pro Pro Tyr Leu Leu Tyr His Leu Asn Ser Ser Tyr
180 185 190

Cys Tyr Ile Phe Glu Met Val His Pro Asp Ala Arg Val Val Val Pro
195 200 205

Tyr Glu Glu Pro Asn Ile Ile Leu Ile Gly Val Arg Ser Val Asp Pro
210 215 220

Glu Lys Gly Tyr Phe Glu Val Gly Pro Ser Glu Glu Ala Val Arg Ile
225 230 235 240

Phe Asn Glu Ser Gly Gly Lys Ile Asn Leu Lys Leu Pro Ala Val Leu
245 250 255

Ser Gln Glu Gln Asn Tyr Thr Leu Phe Arg Ala Asn Arg Leu Gln Glu
260 265 270

Leu Phe Glu Glu Val Thr Pro Leu Phe Lys Ser Leu Arg Asp Gly Tyr
275 280 285

Glu Val Val Tyr Glu Gly Phe Val Ala Val Gln Glu Ile Ala Pro Arg
290 295 300

Val Tyr Tyr Arg Thr Lys Ile Lys His Pro Val Tyr Leu Glu Leu His
305 310 315 320

Arg Ile Lys Thr Thr Ile Thr Pro Glu Lys Leu Ala Asp Leu Phe Leu
325 330 335

Glu Asn Lys Leu Asp Asp Phe Val Leu Thr Pro Asp Glu Gln Glu Thr
340 345 350

Val Met Lys Leu Lys Glu Ile Tyr Thr Asp Met Arg Asn Gln Leu Glu
355 360 365

Ser Ser Phe Asp Thr Ile Tyr Lys Glu Ile Ser Glu Gln Val Ser Pro
370 375 380

Glu Glu Asn Pro Gly Glu Phe Arg Lys Arg Phe Ala Leu Arg Leu Met
385 390 395 400

Asp Tyr His Asp Lys Ser Trp Phe Phe Ala Arg Leu Asp Gly Asp Glu
405 410 415

Glu Lys Met Gln Lys Ser Glu Lys Lys Leu Leu Thr Glu Arg Ile Glu
420 425 430

Lys Gly Leu Phe Lys
435



41
300
PRT
Escherichia coli

41

Met Val Gln Ile Pro Gln Asn Pro Leu Ile Leu Val Asp Gly Ser Ser
1 5 10 15

Tyr Leu Tyr Arg Ala Tyr His Ala Phe Pro Pro Leu Thr Asn Ser Ala
20 25 30

Gly Glu Pro Thr Gly Ala Met Tyr Gly Val Leu Asn Met Leu Arg Ser
35 40 45

Leu Ile Met Gln Tyr Lys Pro Thr His Ala Ala Val Val Phe Asp Ala
50 55 60

Lys Gly Lys Thr Phe Arg Asp Glu Leu Phe Glu His Tyr Lys Ser His
65 70 75 80

Arg Pro Pro Met Pro Asp Asp Leu Arg Ala Gln Ile Glu Pro Leu His
85 90 95

Ala Met Val Lys Ala Met Gly Leu Pro Leu Leu Ala Val Ser Gly Val
100 105 110

Glu Ala Asp Asp Val Ile Gly Thr Leu Ala Arg Glu Ala Glu Lys Ala
115 120 125

Gly Arg Pro Val Leu Ile Ser Thr Gly Asp Lys Asp Met Ala Gln Leu
130 135 140

Val Thr Pro Asn Ile Thr Leu Ile Asn Thr Met Thr Asn Thr Ile Leu
145 150 155 160

Gly Pro Glu Glu Val Val Asn Lys Tyr Gly Val Pro Pro Glu Leu Ile
165 170 175

Ile Asp Phe Leu Ala Leu Met Gly Asp Ser Ser Asp Asn Ile Pro Gly
180 185 190

Val Pro Gly Val Gly Glu Lys Thr Ala Gln Ala Leu Leu Gln Gly Leu
195 200 205

Gly Gly Leu Asp Thr Leu Tyr Ala Glu Pro Glu Lys Ile Ala Gly Leu
210 215 220

Ser Phe Arg Gly Ala Lys Thr Met Ala Ala Lys Leu Glu Gln Asn Lys
225 230 235 240

Glu Val Ala Tyr Leu Ser Tyr Gln Leu Ala Thr Ile Lys Thr Asp Val
245 250 255

Glu Leu Glu Leu Thr Cys Glu Gln Leu Glu Val Gln Gln Pro Ala Ala
260 265 270

Glu Glu Leu Leu Gly Leu Phe Lys Lys Tyr Glu Phe Lys Arg Trp Thr
275 280 285

Ala Asp Val Glu Ala Gly Lys Trp Leu Gln Ala Lys
290 295 300



42
300
PRT
Thermus aquaticaus

42

Met Arg Gly Met Leu Pro Leu Phe Glu Pro Lys Gly Arg Val Leu Leu
1 5 10 15

Val Asp Gly His His Leu Ala Tyr Arg Thr Phe His Ala Leu Lys Gly
20 25 30

Leu Thr Thr Ser Arg Gly Glu Pro Val Gln Ala Val Tyr Gly Phe Ala
35 40 45

Lys Ser Leu Leu Lys Ala Leu Lys Glu Asp Gly Asp Ala Val Ile Val
50 55 60

Val Phe Asp Ala Lys Ala Pro Ser Phe Arg His Glu Ala Tyr Gly Gly
65 70 75 80

Tyr Lys Ala Gly Arg Ala Pro Thr Pro Glu Asp Phe Pro Arg Gln Leu
85 90 95

Ala Leu Ile Lys Glu Leu Val Asp Leu Leu Gly Leu Ala Arg Leu Glu
100 105 110

Val Pro Gly Tyr Glu Ala Asp Asp Val Leu Ala Ser Leu Ala Lys Lys
115 120 125

Ala Glu Lys Glu Gly Tyr Glu Val Arg Ile Leu Thr Ala Asp Lys Asp
130 135 140

Leu Tyr Gln Leu Leu Ser Asp Arg Ile His Val Leu His Pro Glu Gly
145 150 155 160

Tyr Leu Ile Thr Pro Ala Trp Leu Trp Glu Lys Tyr Gly Leu Arg Pro
165 170 175

Asp Gln Trp Ala Asp Tyr Arg Ala Leu Thr Gly Asp Glu Ser Asp Asn
180 185 190

Leu Pro Gly Val Lys Gly Ile Gly Glu Lys Thr Ala Arg Lys Leu Leu
195 200 205

Glu Glu Trp Gly Ser Leu Glu Ala Leu Leu Lys Asn Leu Asp Arg Leu
210 215 220

Lys Pro Ala Ile Arg Glu Lys Ile Leu Ala His Met Asp Asp Leu Lys
225 230 235 240

Leu Ser Trp Asp Leu Ala Lys Val Arg Thr Asp Leu Pro Leu Glu Val
245 250 255

Asp Phe Ala Lys Arg Arg Glu Pro Asp Arg Glu Arg Leu Arg Ala Phe
260 265 270

Leu Glu Arg Leu Glu Phe Gly Ser Leu Leu His Glu Phe Gly Leu Leu
275 280 285

Glu Ser Pro Lys Ala Leu Glu Glu Ala Pro Trp Pro
290 295 300



43
318
PRT
Bacteriophage RM378

43

Met Lys Arg Leu Arg Asn Met Val Asn Leu Ile Asp Leu Lys Asn Gln
1 5 10 15

Tyr Tyr Ala Tyr Ser Phe Lys Phe Phe Asp Ser Tyr Gln Ile Ser Trp
20 25 30

Asp Asn Tyr Pro His Leu Lys Glu Phe Val Ile Glu Asn Tyr Pro Gly
35 40 45

Thr Tyr Phe Ser Cys Tyr Ala Pro Gly Ile Leu Tyr Lys Leu Phe Leu
50 55 60

Lys Trp Lys Arg Gly Met Ile Ile Asp Asp Tyr Asp Arg His Pro Leu
65 70 75 80

Arg Lys Lys Leu Leu Pro Gln Tyr Lys Glu His Arg Tyr Glu Tyr Ile
85 90 95

Glu Gly Lys Tyr Gly Val Val Pro Phe Pro Gly Phe Leu Lys Tyr Leu
100 105 110

Lys Phe His Phe Glu Asp Leu Arg Phe Lys Met Arg Asp Leu Gly Ile
115 120 125

Thr Asp Phe Lys Tyr Ala Leu Ala Ile Ser Leu Phe Tyr Asn Arg Val
130 135 140

Met Leu Arg Asp Phe Leu Lys Asn Phe Thr Cys Tyr Tyr Ile Ala Glu
145 150 155 160

Tyr Glu Ala Asp Asp Val Ile Ala His Leu Ala Arg Glu Ile Ala Arg
165 170 175

Ser Asn Ile Asp Val Asn Ile Val Ser Thr Asp Lys Asp Tyr Tyr Gln
180 185 190

Leu Trp Asp Glu Glu Asp Ile Arg Glu Arg Val Tyr Ile Asn Ser Leu
195 200 205

Ser Cys Ser Asp Val Lys Thr Pro Arg Tyr Gly Phe Leu Thr Ile Lys
210 215 220

Ala Leu Leu Gly Asp Lys Ser Asp Asn Ile Pro Lys Ser Leu Glu Lys
225 230 235 240

Gly Lys Gly Glu Lys Tyr Leu Glu Lys Lys Gly Phe Ala Glu Glu Asp
245 250 255

Tyr Asp Lys Glu Leu Phe Glu Asn Asn Leu Lys Val Ile Arg Phe Gly
260 265 270

Asp Glu Tyr Leu Gly Glu Arg Asp Lys Ser Phe Ile Glu Asn Phe Ser
275 280 285

Thr Gly Asp Thr Leu Trp Asn Phe Tyr Glu Phe Phe Tyr Tyr Asp Pro
290 295 300

Leu His Glu Leu Phe Leu Arg Asn Ile Arg Lys Arg Arg Leu
305 310 315



44
305
PRT
Bacteriophage T4

44

Met Asp Leu Glu Met Met Leu Asp Glu Asp Tyr Lys Glu Gly Ile Cys
1 5 10 15

Leu Ile Asp Phe Ser Gln Ile Ala Leu Ser Thr Ala Leu Val Asn Phe
20 25 30

Pro Asp Lys Glu Lys Ile Asn Leu Ser Met Val Arg His Leu Ile Leu
35 40 45

Asn Ser Ile Lys Phe Asn Val Lys Lys Ala Lys Thr Leu Gly Tyr Thr
50 55 60

Lys Ile Val Leu Cys Ile Asp Asn Ala Lys Ser Gly Tyr Trp Arg Arg
65 70 75 80

Asp Phe Ala Tyr Tyr Tyr Lys Lys Asn Arg Gly Lys Ala Arg Glu Glu
85 90 95

Ser Thr Trp Asp Trp Glu Gly Tyr Phe Glu Ser Ser His Lys Val Ile
100 105 110

Asp Glu Leu Lys Ala Tyr Met Pro Tyr Ile Val Met Asp Ile Asp Lys
115 120 125

Tyr Glu Ala Asp Asp His Ile Ala Val Leu Val Lys Lys Phe Ser Leu
130 135 140

Glu Gly His Lys Ile Leu Ile Ile Ser Ser Asp Gly Asp Phe Thr Gln
145 150 155 160

Leu His Lys Tyr Pro Asn Val Lys Gln Trp Ser Pro Met His Lys Lys
165 170 175

Trp Val Lys Ile Lys Ser Gly Ser Ala Glu Ile Asp Cys Met Thr Lys
180 185 190

Ile Leu Lys Gly Asp Lys Lys Asp Asn Val Ala Ser Val Lys Val Arg
195 200 205

Ser Asp Phe Trp Phe Thr Arg Val Glu Gly Glu Arg Thr Pro Ser Met
210 215 220

Lys Thr Ser Ile Val Glu Ala Ile Ala Asn Asp Arg Glu Gln Ala Lys
225 230 235 240

Val Leu Leu Thr Glu Ser Glu Tyr Asn Arg Tyr Lys Glu Asn Leu Val
245 250 255

Leu Ile Asp Phe Asp Tyr Ile Pro Asp Asn Ile Ala Ser Asn Ile Val
260 265 270

Asn Tyr Tyr Asn Ser Tyr Lys Leu Pro Pro Arg Gly Lys Ile Tyr Ser
275 280 285

Tyr Phe Val Lys Ala Gly Leu Ser Lys Leu Thr Asn Ser Ile Asn Glu
290 295 300

Phe
305



45
300
PRT
Bacteriophage T7

45

Met Ala Leu Leu Asp Leu Lys Gln Phe Tyr Glu Leu Arg Glu Gly Cys
1 5 10 15

Asp Asp Lys Gly Ile Leu Val Met Asp Gly Asp Trp Leu Val Phe Gln
20 25 30

Ala Met Ser Ala Ala Glu Phe Asp Ala Ser Trp Glu Glu Glu Ile Trp
35 40 45

His Arg Cys Cys Asp His Ala Lys Ala Arg Gln Ile Leu Glu Asp Ser
50 55 60

Ile Lys Ser Tyr Glu Thr Arg Lys Lys Ala Trp Ala Gly Ala Pro Ile
65 70 75 80

Val Leu Ala Phe Thr Asp Ser Val Asn Trp Arg Lys Glu Leu Val Asp
85 90 95

Pro Asn Tyr Lys Ala Asn Arg Lys Ala Val Lys Lys Pro Val Gly Tyr
100 105 110

Phe Glu Phe Leu Asp Ala Leu Phe Glu Arg Glu Glu Phe Tyr Cys Ile
115 120 125

Arg Glu Pro Met Leu Glu Gly Asp Asp Val Met Gly Val Ile Ala Ser
130 135 140

Asn Pro Ser Ala Phe Gly Ala Arg Lys Ala Val Ile Ile Ser Cys Asp
145 150 155 160

Lys Asp Phe Lys Thr Ile Pro Asn Cys Asp Phe Leu Trp Cys Thr Thr
165 170 175

Gly Asn Ile Leu Thr Gln Thr Glu Glu Ser Ala Asp Trp Trp His Leu
180 185 190

Phe Gln Thr Ile Lys Gly Asp Ile Thr Asp Gly Tyr Ser Gly Ile Ala
195 200 205

Gly Trp Gly Asp Thr Ala Glu Asp Phe Leu Asn Asn Pro Phe Ile Thr
210 215 220

Glu Pro Lys Thr Ser Val Leu Lys Ser Gly Lys Asn Lys Gly Gln Glu
225 230 235 240

Val Thr Lys Trp Val Lys Arg Asp Pro Glu Pro His Glu Thr Leu Trp
245 250 255

Asp Cys Ile Lys Ser Ile Gly Ala Lys Ala Gly Met Thr Glu Glu Asp
260 265 270

Ile Ile Lys Gln Gly Gln Met Ala Arg Ile Leu Arg Phe Asn Glu Tyr
275 280 285

Asn Phe Ile Asp Lys Glu Ile Tyr Leu Trp Arg Pro
290 295 300



46
287
PRT
Escherichia coli

46

Val Leu Asp Ala Thr Val Ala Arg Ile Glu Gln Leu Phe Gln Gln Pro
1 5 10 15

His Asp Gly Val Thr Gly Val Asn Thr Gly Tyr Asp Asp Leu Asn Lys
20 25 30

Lys Thr Ala Gly Leu Gln Pro Ser Asp Leu Ile Ile Val Ala Ala Arg
35 40 45

Pro Ser Met Gly Lys Thr Thr Phe Ala Met Asn Leu Val Glu Asn Ala
50 55 60

Ala Met Leu Gln Asp Lys Pro Val Leu Ile Phe Ser Leu Glu Met Pro
65 70 75 80

Ser Glu Gln Ile Met Met Arg Ser Leu Ala Ser Leu Ser Arg Val Asp
85 90 95

Gln Thr Lys Ile Arg Thr Gly Gln Leu Asp Asp Glu Asp Trp Ala Arg
100 105 110

Ile Ser Gly Thr Met Gly Ile Leu Leu Glu Lys Arg Asn Ile Tyr Ile
115 120 125

Asp Asp Ser Ser Gly Leu Thr Pro Thr Glu Val Arg Ser Arg Ala Arg
130 135 140

Arg Ile Ala Arg Glu His Gly Gly Ile Gly Leu Ile Met Ile Asp Tyr
145 150 155 160

Leu Gln Leu Met Arg Val Pro Ala Leu Ser Asp Asn Arg Thr Leu Glu
165 170 175

Ile Ala Glu Ile Ser Arg Ser Leu Lys Ala Leu Ala Lys Glu Leu Asn
180 185 190

Val Pro Val Val Ala Leu Ser Gln Leu Asn Arg Ser Leu Glu Gln Arg
195 200 205

Ala Asp Lys Arg Pro Val Asn Ser Asp Leu Arg Glu Ser Gly Ser Ile
210 215 220

Glu Gln Asp Ala Asp Leu Ile Met Phe Ile Tyr Arg Asp Glu Val Tyr
225 230 235 240

His Glu Asn Ser Asp Leu Lys Gly Ile Ala Glu Ile Ile Ile Gly Lys
245 250 255

Gln Arg Asn Gly Pro Ile Gly Thr Val Arg Leu Thr Phe Asn Gly Gln
260 265 270

Trp Ser Arg Phe Asp Asn Tyr Ala Gly Pro Gln Tyr Asp Asp Glu
275 280 285



47
291
PRT
Haemophilus influenza

47

Val Leu Glu Ser Thr Ile Glu Lys Ile Asp Ile Leu Ser Lys Leu Glu
1 5 10 15

Asn His Ser Gly Val Thr Gly Val Thr Thr Gly Phe Thr Asp Leu Asp
20 25 30

Lys Lys Thr Ala Gly Leu Gln Pro Ser Asp Leu Ile Ile Val Ala Ala
35 40 45

Arg Pro Ser Met Gly Lys Thr Thr Phe Ala Met Asn Leu Cys Glu Asn
50 55 60

Ala Ala Met Ala Ser Glu Lys Pro Val Leu Val Phe Ser Leu Glu Met
65 70 75 80

Pro Ala Glu Gln Ile Met Met Arg Met Ile Ala Ser Leu Ala Arg Val
85 90 95

Asp Gln Thr Lys Ile Arg Thr Gly Gln Asn Leu Asp Glu Ile Glu Trp
100 105 110

Asn Lys Ile Ala Ser Val Val Gly Met Phe Lys Gln Lys Asn Asn Leu
115 120 125

Phe Ile Asp Asp Ser Ser Gly Leu Thr Pro Thr Asp Val Arg Ser Arg
130 135 140

Ala Arg Arg Val Tyr Arg Glu Asn Gly Gly Leu Ser Met Ile Met Val
145 150 155 160

Asp Tyr Leu Gln Leu Met Arg Ala Pro Ala Phe Ser Asp Asn Arg Thr
165 170 175

Leu Glu Ile Ala Glu Ile Ser Arg Ser Leu Lys Ala Leu Ala Lys Glu
180 185 190

Leu Gln Val Pro Val Val Ala Leu Ser Gln Leu Asn Arg Thr Leu Glu
195 200 205

Gln Arg Gly Asp Lys Arg Pro Val Asn Ser Asp Leu Arg Glu Ser Gly
210 215 220

Ser Ile Glu Gln Asp Ala Asp Leu Ile Met Phe Ile Tyr Arg Asp Glu
225 230 235 240

Val Tyr Asn Asp Asn Ser Glu Asp Lys Gly Val Ala Glu Ile Ile Ile
245 250 255

Gly Lys Gln Arg Asn Gly Pro Ile Gly Arg Val Arg Leu Lys Phe Asn
260 265 270

Gly Gln Phe Ser Arg Phe Asp Asn Leu Ala Glu Gln Arg Glu Tyr Arg
275 280 285

Asp Asp Tyr
290



48
287
PRT
Chlamydomonas trachomatis

48

Ala Leu Gln Glu Arg Gln Glu Ala Phe Gln Ala Ser Ala His Asp Ser
1 5 10 15

Ser Ser Pro Met Leu Ser Gly Phe Pro Thr His Phe Leu Asp Leu Asp
20 25 30

Lys Met Ile Ser Gly Phe Ser Pro Ser Asn Leu Ile Ile Leu Ala Ala
35 40 45

Arg Pro Ala Met Gly Lys Thr Ala Leu Ala Leu Asn Ile Val Glu Asn
50 55 60

Phe Cys Phe Asp Ser Arg Leu Pro Val Gly Ile Phe Ser Leu Glu Met
65 70 75 80

Thr Val Asp Gln Leu Ile His Arg Ile Ile Cys Ser Arg Ser Glu Val
85 90 95

Glu Ala Lys Lys Ile Ser Val Gly Asp Ile Ser Gly Arg Asp Phe Gln
100 105 110

Arg Val Val Ser Val Val Arg Glu Met Glu Glu His Thr Leu Leu Ile
115 120 125

Asp Asp Tyr Pro Gly Leu Lys Ile Thr Asp Leu Arg Ala Arg Ala Arg
130 135 140

Arg Met Lys Glu Ser Tyr Asp Ile Gln Phe Leu Val Ile Asp Tyr Leu
145 150 155 160

Gln Leu Ile Ser Ser Ser Gly Asn Leu Arg Asn Ser Asp Ser Arg Asn
165 170 175

Gln Glu Ile Ser Glu Ile Ser Arg Met Leu Lys Asn Leu Ala Arg Glu
180 185 190

Leu Asn Ile Pro Ile Leu Cys Leu Ser Gln Leu Ser Arg Lys Val Glu
195 200 205

Asp Arg Ala Asn His Arg Pro Leu Met Ser Asp Leu Arg Glu Ser Gly
210 215 220

Ser Ile Glu Gln Asp Ala Asp Gln Ile Met Phe Leu Leu Arg Arg Glu
225 230 235 240

Tyr Tyr Asp Pro Asn Asp Lys Pro Gly Thr Ala Glu Leu Ile Val Ala
245 250 255

Lys Asn Arg His Gly Ser Ile Gly Ser Val Gln Leu Val Phe Glu Lys
260 265 270

Asp Phe Ala Arg Phe Arg Asn Tyr Ala Gly Cys Glu Phe Pro Gly
275 280 285



49
290
PRT
Bacillus stearothermophilus

49

Ile Leu Val Gln Thr Tyr Asp Asn Ile Glu Met Leu His Asn Arg Asp
1 5 10 15

Gly Glu Ile Thr Gly Ile Pro Thr Gly Phe Thr Glu Leu Asp Arg Met
20 25 30

Thr Ser Gly Phe Gln Arg Ser Asp Leu Ile Ile Val Ala Ala Arg Pro
35 40 45

Ser Val Gly Lys Thr Ala Phe Ala Leu Asn Ile Ala Gln Asn Val Ala
50 55 60

Thr Lys Thr Asn Glu Asn Val Ala Ile Phe Ser Leu Glu Met Ser Ala
65 70 75 80

Gln Gln Leu Val Met Arg Met Leu Cys Ala Glu Gly Asn Ile Asn Ala
85 90 95

Gln Asn Leu Arg Thr Gly Lys Leu Thr Pro Glu Asp Trp Gly Lys Leu
100 105 110

Thr Met Ala Met Gly Ser Leu Ser Asn Ala Gly Ile Tyr Ile Asp Asp
115 120 125

Thr Pro Ser Ile Arg Val Ser Asp Ile Arg Ala Lys Cys Arg Arg Leu
130 135 140

Lys Gln Glu Ser Gly Leu Gly Met Ile Val Ile Asp Tyr Leu Gln Leu
145 150 155 160

Ile Gln Gly Ser Gly Arg Ser Lys Glu Asn Arg Gln Gln Glu Val Ser
165 170 175

Glu Ile Ser Arg Ser Leu Lys Ala Leu Ala Arg Glu Leu Glu Val Pro
180 185 190

Val Ile Ala Leu Ser Gln Leu Ser Arg Ser Val Glu Gln Arg Gln Asp
195 200 205

Lys Arg Pro Met Met Ser Asp Ile Arg Glu Ser Gly Ser Ile Glu Gln
210 215 220

Asp Ala Asp Ile Val Ala Phe Leu Tyr Arg Asp Asp Tyr Tyr Asn Lys
225 230 235 240

Asp Ser Glu Asn Lys Asn Ile Ile Glu Ile Ile Ile Ala Lys Gln Arg
245 250 255

Asn Gly Pro Val Gly Thr Val Gln Leu Ala Phe Ile Lys Glu Tyr Asn
260 265 270

Lys Phe Val Asn Leu Glu Arg Arg Phe Asp Glu Ala Gln Ile Pro Pro
275 280 285

Gly Ala
290



50
332
PRT
Halobacter pylori

50

Val Leu Glu Ser Ala Met Asp Leu Ile Thr Glu Asn Gln Arg Lys Gly
1 5 10 15

Ser Leu Glu Val Thr Gly Ile Pro Thr Gly Phe Val Gln Leu Asp Asn
20 25 30

Tyr Thr Ser Gly Phe Asn Lys Gly Ser Leu Val Ile Ile Gly Ala Arg
35 40 45

Pro Ser Met Gly Lys Thr Ser Leu Met Met Asn Met Val Leu Ser Ala
50 55 60

Leu Asn Asp Asp Arg Gly Val Ala Val Phe Ser Leu Glu Met Ser Ala
65 70 75 80

Glu Gln Leu Ala Leu Arg Ala Leu Ser Asp Leu Thr Ser Ile Asn Met
85 90 95

His Asp Leu Glu Ser Gly Arg Leu Asp Asp Asp Gln Trp Glu Asn Leu
100 105 110

Ala Lys Cys Phe Asp His Leu Ser Gln Lys Lys Leu Phe Phe Tyr Asp
115 120 125

Lys Ser Tyr Val Arg Ile Glu Gln Ile Arg Leu Gln Leu Arg Lys Leu
130 135 140

Lys Ser Gln His Lys Glu Leu Gly Ile Ala Phe Ile Asp Tyr Leu Gln
145 150 155 160

Leu Met Ser Gly Ser Lys Ala Thr Lys Glu Arg His Glu Gln Ile Ala
165 170 175

Glu Ile Ser Arg Glu Leu Lys Thr Leu Ala Arg Glu Leu Glu Ile Pro
180 185 190

Ile Ile Ala Leu Val Gln Leu Asn Arg Ser Leu Glu Asn Arg Asp Asp
195 200 205

Lys Arg Pro Ile Leu Ser Asp Ile Lys Asp Ser Gly Gly Ile Glu Gln
210 215 220

Asp Ala Asp Ile Val Leu Phe Leu Tyr Arg Gly Tyr Ile Tyr Gln Met
225 230 235 240

Arg Ala Glu Asp Asn Lys Ile Asp Lys Leu Lys Lys Glu Gly Lys Ile
245 250 255

Glu Glu Ala Gln Glu Leu Tyr Leu Lys Val Asn Glu Glu Arg Arg Ile
260 265 270

His Lys Gln Asn Gly Ser Ile Glu Glu Ala Glu Ile Ile Val Ala Lys
275 280 285

Asn Arg Asn Gly Ala Thr Gly Thr Val Tyr Thr Arg Phe Asn Ala Pro
290 295 300

Phe Thr Arg Tyr Glu Asp Met Pro Ile Asp Ser His Leu Glu Glu Gly
305 310 315 320

Gln Glu Thr Lys Val Asp Tyr Asp Ile Val Thr Thr
325 330



51
295
PRT
Mycolplasma genitalium

51

Glu Ile Ala Asn Gln Glu Glu Ala Leu Ile Lys Lys Val His Arg Gly
1 5 10 15

Glu Leu Ile Ile Ser Gly Leu Ser Ser Gly Phe Leu Lys Leu Asp Gln
20 25 30

Leu Thr Ser Gly Trp Lys Pro Gly Glu Leu Ile Val Ile Ala Ala Arg
35 40 45

Pro Gly Arg Gly Lys Thr Ala Leu Leu Ile Asn Phe Met Ala Ser Ala
50 55 60

Ala Lys Gln Ile Asp Pro Lys Thr Asp Val Val Leu Phe Phe Ser Leu
65 70 75 80

Glu Met Arg Asn Arg Glu Ile Tyr Gln Arg His Leu Met His Glu Ser
85 90 95

Gln Thr Ser Tyr Thr Leu Thr Asn Arg Gln Arg Ile Asn Asn Val Phe
100 105 110

Glu Glu Leu Met Glu Ala Ser Ser Arg Ile Lys Asn Leu Pro Ile Lys
115 120 125

Leu Phe Asp Tyr Ser Ser Leu Thr Leu Gln Glu Ile Arg Asn Gln Ile
130 135 140

Thr Glu Val Ser Lys Thr Ser Asn Val Arg Leu Val Ile Ile Asp Tyr
145 150 155 160

Leu Gln Leu Val Asn Ala Leu Lys Asn Asn Tyr Gly Leu Thr Arg Gln
165 170 175

Gln Glu Val Thr Met Ile Ser Gln Ser Leu Lys Ala Phe Ala Lys Glu
180 185 190

Phe Asn Thr Pro Ile Ile Ala Ala Ala Gln Leu Ser Arg Arg Ile Glu
195 200 205

Glu Arg Lys Asp Ser Arg Pro Ile Leu Ser Asp Leu Arg Glu Ser Gly
210 215 220

Ser Ile Glu Gln Asp Ala Asp Met Val Leu Phe Ile His Arg Thr Asn
225 230 235 240

Asp Asp Lys Lys Glu Gln Glu Glu Glu Asn Thr Asn Leu Phe Glu Val
245 250 255

Glu Leu Ile Leu Glu Lys Asn Arg Asn Gly Pro Asn Gly Lys Val Lys
260 265 270

Leu Asn Phe Arg Ser Asp Thr Ser Ser Phe Ile Ser Gln Tyr Ser Pro
275 280 285

Ser Phe Asp Asp Gln Tyr Ser
290 295



52
283
PRT
Borrelia burgdorferi

52

Ile Ala Glu Arg Val His Asn Glu Ile Tyr Glu Arg Ser Met Lys Lys
1 5 10 15

Lys Glu Ala Asn Phe Gly Ile Pro Ser Gly Phe Arg Lys Val Asp Ser
20 25 30

Leu Ile Gly Gly Phe Arg Asn Ser Asp Phe Ile Ile Val Gly Ala Arg
35 40 45

Pro Ser Ile Gly Lys Thr Ala Phe Ala Leu Asn Ile Ala Ser Tyr Ile
50 55 60

Ala Leu Arg Lys Glu Glu Lys Lys Lys Val Gly Phe Phe Ser Leu Glu
65 70 75 80

Met Thr Ala Asp Ala Leu Ile Lys Arg Ile Ile Ser Ser Gln Ser Cys
85 90 95

Ile Asp Ser Phe Lys Val Gln Asn Ser Ile Leu Ser Gly Gln Glu Ile
100 105 110

Lys Ser Leu Asn Asp Ile Ile Asn Glu Ile Ser Asp Ser Glu Leu Tyr
115 120 125

Ile Glu Asp Thr Pro Asn Ile Ser Leu Leu Thr Leu Ala Thr Gln Ala
130 135 140

Arg Lys Leu Lys Arg Phe Tyr Gly Ile Asp Ile Ile Phe Val Asp Tyr
145 150 155 160

Ile Ser Leu Ile Ser Phe Glu Thr Lys Asn Leu Pro Arg His Glu Gln
165 170 175

Val Ala Ser Ile Ser Lys Ser Leu Lys Glu Leu Ala Arg Glu Leu Glu
180 185 190

Ile Pro Ile Val Ala Leu Ser Gln Leu Thr Arg Asp Thr Glu Gly Arg
195 200 205

Glu Pro Asn Leu Ala Ser Leu Arg Glu Ser Gly Ala Leu Glu Gln Asp
210 215 220

Ala Asp Ile Val Ile Leu Leu His Arg Asp Lys Asp Phe Lys Phe Glu
225 230 235 240

Ser Ser Ala Glu Ile Glu Pro Ile Glu Thr Lys Val Ile Val Ala Lys
245 250 255

His Arg Asn Gly Pro Thr Gly Arg Ala Asp Ile Leu Phe Leu Pro His
260 265 270

Ile Thr Lys Phe Val Asn Lys Asp His Gln Tyr
275 280



53
327
PRT
Bacteriophage T4

53

Tyr Val Gly His Asp Trp Met Asp Asp Tyr Glu Ala Arg Trp Leu Ser
1 5 10 15

Tyr Met Asn Lys Ala Arg Lys Val Pro Phe Lys Leu Arg Ile Leu Asn
20 25 30

Lys Ile Thr Lys Gly Gly Ala Glu Thr Gly Thr Leu Asn Val Leu Met
35 40 45

Ala Gly Val Asn Val Gly Lys Ser Leu Gly Leu Cys Ser Leu Ala Ala
50 55 60

Asp Tyr Leu Gln Leu Gly His Asn Val Leu Tyr Ile Ser Met Glu Met
65 70 75 80

Ala Glu Glu Val Cys Ala Lys Arg Ile Asp Ala Asn Met Leu Asp Val
85 90 95

Ser Leu Asp Asp Ile Asp Asp Gly His Ile Ser Tyr Ala Glu Tyr Lys
100 105 110

Gly Lys Met Glu Lys Trp Arg Glu Lys Ser Thr Leu Gly Arg Leu Ile
115 120 125

Val Lys Gln Tyr Pro Thr Gly Gly Ala Asp Ala Asn Thr Phe Arg Ser
130 135 140

Leu Leu Asn Glu Leu Lys Leu Lys Lys Asn Phe Val Pro Thr Ile Ile
145 150 155 160

Ile Val Asp Tyr Leu Gly Ile Cys Lys Ser Cys Arg Ile Arg Val Tyr
165 170 175

Ser Glu Asn Ser Tyr Thr Thr Val Lys Ala Ile Ala Glu Glu Leu Arg
180 185 190

Ala Leu Ala Val Glu Thr Glu Thr Val Leu Trp Thr Ala Ala Gln Val
195 200 205

Gly Lys Gln Ala Trp Asp Ser Ser Asp Val Asn Met Ser Asp Ile Ala
210 215 220

Glu Ser Ala Gly Leu Pro Ala Thr Ala Asp Phe Met Leu Ala Val Ile
225 230 235 240

Glu Thr Glu Glu Leu Ala Ala Ala Glu Gln Gln Leu Ile Lys Gln Ile
245 250 255

Lys Ser Arg Tyr Gly Asp Lys Asn Lys Trp Asn Lys Phe Leu Met Gly
260 265 270

Val Gln Lys Gly Asn Gln Lys Trp Val Glu Ile Glu Gln Asp Ser Thr
275 280 285

Pro Thr Glu Val Asn Glu Val Ala Gly Ser Gln Gln Ile Gln Ala Glu
290 295 300

Gln Asn Arg Tyr Gln Arg Asn Glu Ser Thr Arg Ala Gln Leu Asp Ala
305 310 315 320

Leu Ala Asn Glu Leu Lys Phe
325



54
302
PRT
Bacteriophage T7

54

Val Val Ser Ala Leu Ser Leu Arg Glu Arg Ile Arg Glu His Leu Ser
1 5 10 15

Ser Glu Glu Ser Val Gly Leu Leu Phe Ser Gly Cys Thr Gly Ile Asn
20 25 30

Asp Lys Thr Leu Gly Ala Arg Gly Gly Glu Val Ile Met Val Thr Ser
35 40 45

Gly Ser Gly Met Gly Lys Ser Thr Phe Val Arg Gln Gln Ala Leu Gln
50 55 60

Trp Gly Thr Ala Met Gly Lys Lys Val Gly Leu Ala Met Leu Glu Glu
65 70 75 80

Ser Val Glu Glu Thr Ala Glu Asp Leu Ile Gly Leu His Asn Arg Val
85 90 95

Arg Leu Arg Gln Ser Asp Ser Leu Lys Arg Glu Ile Ile Glu Asn Gly
100 105 110

Lys Phe Asp Gln Trp Phe Asp Glu Leu Phe Gly Asn Asp Thr Phe His
115 120 125

Leu Tyr Asp Ser Phe Ala Glu Ala Glu Thr Asp Arg Leu Leu Ala Lys
130 135 140

Leu Ala Tyr Met Arg Ser Gly Leu Gly Cys Asp Val Ile Ile Leu Asp
145 150 155 160

His Ile Ser Ile Val Val Ser Ala Ser Gly Glu Ser Asp Glu Arg Lys
165 170 175

Met Ile Asp Asn Leu Met Thr Lys Leu Lys Gly Phe Ala Lys Ser Thr
180 185 190

Gly Val Val Leu Val Val Ile Cys His Leu Lys Asn Pro Asp Lys Gly
195 200 205

Lys Ala His Glu Glu Gly Arg Pro Val Ser Ile Thr Asp Leu Arg Gly
210 215 220

Ser Gly Ala Leu Arg Gln Leu Ser Asp Thr Ile Ile Ala Leu Glu Arg
225 230 235 240

Asn Gln Gln Gly Asp Met Pro Asn Leu Val Leu Val Arg Ile Leu Lys
245 250 255

Cys Arg Phe Thr Gly Asp Thr Gly Ile Ala Gly Tyr Met Glu Tyr Asn
260 265 270

Lys Glu Thr Gly Trp Leu Glu Pro Ser Ser Tyr Ser Gly Glu Glu Glu
275 280 285

Ser His Ser Glu Ser Thr Asp Trp Ser Asn Asp Thr Asp Phe
290 295 300



55
270
PRT
Bacteriophage RM378

55

Val Ser Leu Val Glu Glu Phe Asp Leu Ala Thr Ser Glu Phe Asn Glu
1 5 10 15

Leu Phe Val Lys Glu Glu Arg Ile Pro Thr Pro Trp Glu Ser Val Asn
20 25 30

Lys Asn Met Ala Gly Gly Leu Gly Arg Gly Glu Leu Gly Ile Val Met
35 40 45

Leu Pro Ser Gly Trp Gly Lys Ser Trp Phe Leu Val Ser Leu Gly Leu
50 55 60

His Ala Phe Arg Thr Gly Lys Arg Val Ile Tyr Phe Thr Leu Glu Leu
65 70 75 80

Asp Gln Lys Tyr Val Met Lys Arg Phe Leu Lys Met Phe Ala Pro Tyr
85 90 95

Cys Lys Gly Arg Ala Ser Ser Tyr Arg Asp Val Tyr Gln Ile Met Lys
100 105 110

Glu Leu Met Phe Ser Gln Asp Asn Leu Leu Lys Ile Val Phe Cys Asn
115 120 125

Ala Met Glu Asp Ile Glu His Tyr Ile Ala Leu Tyr Asn Pro Asp Val
130 135 140

Val Leu Ile Asp Tyr Ala Asp Leu Ile Tyr Asp Val Glu Thr Asp Lys
145 150 155 160

Glu Lys Asn Tyr Leu Leu Leu Gln Lys Ile Tyr Arg Lys Leu Arg Leu
165 170 175

Ile Ala Lys Val Tyr Asn Thr Ala Val Trp Ser Ala Ser Gln Leu Asn
180 185 190

Arg Gly Ser Leu Ser Lys Gln Ala Asp Val Asp Phe Ile Glu Lys Tyr
195 200 205

Ile Ala Asp Ser Phe Ala Lys Val Val Glu Ile Asp Phe Gly Met Ala
210 215 220

Phe Ile Pro Asp Ser Glu Asn Ser Thr Pro Asp Ile His Val Gly Phe
225 230 235 240

Gly Lys Ile Phe Lys Asn Arg Met Gly Ala Val Arg Lys Leu Glu Tyr
245 250 255

Thr Ile Asn Phe Glu Asn Tyr Thr Val Asp Val Ala Val Lys
260 265 270



56
1197
DNA
Bacteriophage RM378

CDS
(112)...(1158)


56

attttctgtt ttttcacagg caagtattcg acatgctcga aacccgcgaa gcttattatc 60

agttgcttca atcgttaaac gatttcctcg aagaagacct gaaggagaat t atg aag 117
Met Lys
1

atc acg cta agc gca agc gta tac ccc cga tcg atg aaa att tac gga 165
Ile Thr Leu Ser Ala Ser Val Tyr Pro Arg Ser Met Lys Ile Tyr Gly
5 10 15

gtg gag cta atc gag ggg aaa aaa cac tta ttt caa tca ccc gta ccc 213
Val Glu Leu Ile Glu Gly Lys Lys His Leu Phe Gln Ser Pro Val Pro
20 25 30

cca cat ttg aag cgc atc gct cag cag aat cga ggg aag att gag gct 261
Pro His Leu Lys Arg Ile Ala Gln Gln Asn Arg Gly Lys Ile Glu Ala
35 40 45 50

gag gct ata tcc tat tac atc aga gaa caa aaa agc cac atc acg ccg 309
Glu Ala Ile Ser Tyr Tyr Ile Arg Glu Gln Lys Ser His Ile Thr Pro
55 60 65

gaa gct ttg tct cag tgc gtc ttt atc gat att gag acg att tcc ccg 357
Glu Ala Leu Ser Gln Cys Val Phe Ile Asp Ile Glu Thr Ile Ser Pro
70 75 80

aaa aaa agc ttt ccc gac ccg tgg aga gac cca gtt tat tcc att tcc 405
Lys Lys Ser Phe Pro Asp Pro Trp Arg Asp Pro Val Tyr Ser Ile Ser
85 90 95

atc aaa ccg tat gga aaa ccg gtg gtg gta gtg ctt ctc ctt atc acc 453
Ile Lys Pro Tyr Gly Lys Pro Val Val Val Val Leu Leu Leu Ile Thr
100 105 110

aac ccg gag gct cat atc gat aac ttt aac aaa ttt acc acc agc gta 501
Asn Pro Glu Ala His Ile Asp Asn Phe Asn Lys Phe Thr Thr Ser Val
115 120 125 130

ggg gat aac aca ttt gaa att cat tac aga aca ttc ctt tcg gaa aaa 549
Gly Asp Asn Thr Phe Glu Ile His Tyr Arg Thr Phe Leu Ser Glu Lys
135 140 145

aga ttg ctc gag tat ttc tgg aat gtg ctg aaa cca aaa ttt act ttc 597
Arg Leu Leu Glu Tyr Phe Trp Asn Val Leu Lys Pro Lys Phe Thr Phe
150 155 160

atg ctc gca tgg aac ggt tat cag ttc gat tat ccc tac ctg ctc att 645
Met Leu Ala Trp Asn Gly Tyr Gln Phe Asp Tyr Pro Tyr Leu Leu Ile
165 170 175

cgt agt cat atc cat gag gtg aat gtc att agt gat aag ttg ctt ccg 693
Arg Ser His Ile His Glu Val Asn Val Ile Ser Asp Lys Leu Leu Pro
180 185 190

gac tgg aag ctg gtg cgg aaa att tcc gat cga aac cta cca ttc tat 741
Asp Trp Lys Leu Val Arg Lys Ile Ser Asp Arg Asn Leu Pro Phe Tyr
195 200 205 210

ttc aat ccc cgt acc cct gta gaa ttt gtg ttt ttt gat tac atg cgg 789
Phe Asn Pro Arg Thr Pro Val Glu Phe Val Phe Phe Asp Tyr Met Arg
215 220 225

ctt tat cgc tcc ttt gtg gca tac aaa gag ttg gag tcc tac cgg ctc 837
Leu Tyr Arg Ser Phe Val Ala Tyr Lys Glu Leu Glu Ser Tyr Arg Leu
230 235 240

gac tat att gcg cga gag gaa ata gga gaa ggt aag gtg gat ttc gac 885
Asp Tyr Ile Ala Arg Glu Glu Ile Gly Glu Gly Lys Val Asp Phe Asp
245 250 255

gta aga ttc tat cat gag att cct gtc tac ccg gat aaa aag ttg gtg 933
Val Arg Phe Tyr His Glu Ile Pro Val Tyr Pro Asp Lys Lys Leu Val
260 265 270

gaa tac aac gcc gta gac gcc att ttg atg gaa gaa atc gaa aat aaa 981
Glu Tyr Asn Ala Val Asp Ala Ile Leu Met Glu Glu Ile Glu Asn Lys
275 280 285 290

aac cat att ctc ccg acg ctg ttt gaa att gca aga ctt tca aat ctg 1029
Asn His Ile Leu Pro Thr Leu Phe Glu Ile Ala Arg Leu Ser Asn Leu
295 300 305

act ccc gca ctg gca ttg aac gct tcc aat att ctt atc gga aat gtt 1077
Thr Pro Ala Leu Ala Leu Asn Ala Ser Asn Ile Leu Ile Gly Asn Val
310 315 320

aca gga aaa ctt ggt gtc aaa ttc gtt gat tac atc aag aaa atc gac 1125
Thr Gly Lys Leu Gly Val Lys Phe Val Asp Tyr Ile Lys Lys Ile Asp
325 330 335

acc att aat aca atg ttc aaa aaa ata cct gag taaactatga atatgcagac 1178
Thr Ile Asn Thr Met Phe Lys Lys Ile Pro Glu
340 345

cattgacgaa acgctttat 1197



57
349
PRT
Bacteriophage RM378

57

Met Lys Ile Thr Leu Ser Ala Ser Val Tyr Pro Arg Ser Met Lys Ile
1 5 10 15

Tyr Gly Val Glu Leu Ile Glu Gly Lys Lys His Leu Phe Gln Ser Pro
20 25 30

Val Pro Pro His Leu Lys Arg Ile Ala Gln Gln Asn Arg Gly Lys Ile
35 40 45

Glu Ala Glu Ala Ile Ser Tyr Tyr Ile Arg Glu Gln Lys Ser His Ile
50 55 60

Thr Pro Glu Ala Leu Ser Gln Cys Val Phe Ile Asp Ile Glu Thr Ile
65 70 75 80

Ser Pro Lys Lys Ser Phe Pro Asp Pro Trp Arg Asp Pro Val Tyr Ser
85 90 95

Ile Ser Ile Lys Pro Tyr Gly Lys Pro Val Val Val Val Leu Leu Leu
100 105 110

Ile Thr Asn Pro Glu Ala His Ile Asp Asn Phe Asn Lys Phe Thr Thr
115 120 125

Ser Val Gly Asp Asn Thr Phe Glu Ile His Tyr Arg Thr Phe Leu Ser
130 135 140

Glu Lys Arg Leu Leu Glu Tyr Phe Trp Asn Val Leu Lys Pro Lys Phe
145 150 155 160

Thr Phe Met Leu Ala Trp Asn Gly Tyr Gln Phe Asp Tyr Pro Tyr Leu
165 170 175

Leu Ile Arg Ser His Ile His Glu Val Asn Val Ile Ser Asp Lys Leu
180 185 190

Leu Pro Asp Trp Lys Leu Val Arg Lys Ile Ser Asp Arg Asn Leu Pro
195 200 205

Phe Tyr Phe Asn Pro Arg Thr Pro Val Glu Phe Val Phe Phe Asp Tyr
210 215 220

Met Arg Leu Tyr Arg Ser Phe Val Ala Tyr Lys Glu Leu Glu Ser Tyr
225 230 235 240

Arg Leu Asp Tyr Ile Ala Arg Glu Glu Ile Gly Glu Gly Lys Val Asp
245 250 255

Phe Asp Val Arg Phe Tyr His Glu Ile Pro Val Tyr Pro Asp Lys Lys
260 265 270

Leu Val Glu Tyr Asn Ala Val Asp Ala Ile Leu Met Glu Glu Ile Glu
275 280 285

Asn Lys Asn His Ile Leu Pro Thr Leu Phe Glu Ile Ala Arg Leu Ser
290 295 300

Asn Leu Thr Pro Ala Leu Ala Leu Asn Ala Ser Asn Ile Leu Ile Gly
305 310 315 320

Asn Val Thr Gly Lys Leu Gly Val Lys Phe Val Asp Tyr Ile Lys Lys
325 330 335

Ile Asp Thr Ile Asn Thr Met Phe Lys Lys Ile Pro Glu
340 345



58
1764
DNA
Bacteriophage RM378

CDS
(142)...(1707)


58

ctatacggat gaagttttga gaattattga tctttctcca ctcgatggcg tattatacaa 60

atgtgattta aaagacacct accttatcga ggtgaaagat acccattttg atcccgcaat 120

gtaaaacaaa cgtattctgc t atg aac atc aac aag tat cgt tat cgc ggt 171
Met Asn Ile Asn Lys Tyr Arg Tyr Arg Gly
1 5 10

gct tac att gaa ctt acc aac ccc gat att tac ttc aac gta ttc gat 219
Ala Tyr Ile Glu Leu Thr Asn Pro Asp Ile Tyr Phe Asn Val Phe Asp
15 20 25

ctt gat ttt aca tcg ctg tac ccc tct gta atc agc aaa ttc aat atc 267
Leu Asp Phe Thr Ser Leu Tyr Pro Ser Val Ile Ser Lys Phe Asn Ile
30 35 40

gat ccc gct acg ttc gta acg gag ttt tac ggg tgt atg cgg gtg gag 315
Asp Pro Ala Thr Phe Val Thr Glu Phe Tyr Gly Cys Met Arg Val Glu
45 50 55

aac aaa gtg att ccg gta gat cag gaa gaa ccg gaa ttc ggg ttt ccc 363
Asn Lys Val Ile Pro Val Asp Gln Glu Glu Pro Glu Phe Gly Phe Pro
60 65 70

ctc tac atc ttc gat tca ggg atg aac cct tct tac cgg agt gaa ccc 411
Leu Tyr Ile Phe Asp Ser Gly Met Asn Pro Ser Tyr Arg Ser Glu Pro
75 80 85 90

ctc ttt gtc atc aac agc ttt gag gaa ctc cgg caa ttt tta aaa agt 459
Leu Phe Val Ile Asn Ser Phe Glu Glu Leu Arg Gln Phe Leu Lys Ser
95 100 105

cga aat atc att atg gtg ccc aac ccg tcg ggt atc tgc tgg ttt tac 507
Arg Asn Ile Ile Met Val Pro Asn Pro Ser Gly Ile Cys Trp Phe Tyr
110 115 120

agg aaa gag ccg gtt ggc gtg ctt cct tct atc att cgg gag att ttc 555
Arg Lys Glu Pro Val Gly Val Leu Pro Ser Ile Ile Arg Glu Ile Phe
125 130 135

acc cga cgt aag gaa gaa cgt aag ctt ttc aaa gaa act ggc aac atg 603
Thr Arg Arg Lys Glu Glu Arg Lys Leu Phe Lys Glu Thr Gly Asn Met
140 145 150

gaa cac cat ttc cgt caa tgg gca ctt aaa att atg atg aac tcc atg 651
Glu His His Phe Arg Gln Trp Ala Leu Lys Ile Met Met Asn Ser Met
155 160 165 170

tac ggt atc ttc gga aac cgt tcg gtg tac atg ggg tgc ctt ccc att 699
Tyr Gly Ile Phe Gly Asn Arg Ser Val Tyr Met Gly Cys Leu Pro Ile
175 180 185

gcg gaa agt gta acc gcc gcc ggg cgc atg tct att cgc tcc gtg att 747
Ala Glu Ser Val Thr Ala Ala Gly Arg Met Ser Ile Arg Ser Val Ile
190 195 200

tct cag att cgc gat cgc ttc att tat tcg cat acc gac tcc att ttc 795
Ser Gln Ile Arg Asp Arg Phe Ile Tyr Ser His Thr Asp Ser Ile Phe
205 210 215

gtc aaa gct ttt acg gat gat ccg gtg gcg gaa gcc ggt gag ctt caa 843
Val Lys Ala Phe Thr Asp Asp Pro Val Ala Glu Ala Gly Glu Leu Gln
220 225 230

gaa cat ctc aac tct ttt atc aat gac tat atg gaa aat aac ttt aat 891
Glu His Leu Asn Ser Phe Ile Asn Asp Tyr Met Glu Asn Asn Phe Asn
235 240 245 250

gca aga gaa gat ttc aag ctg gag tta aag cag gag ttc gtg ttc aaa 939
Ala Arg Glu Asp Phe Lys Leu Glu Leu Lys Gln Glu Phe Val Phe Lys
255 260 265

tcc att ctt atc aaa gaa atc aac cgc tac ttt gcg gtt act gta gac 987
Ser Ile Leu Ile Lys Glu Ile Asn Arg Tyr Phe Ala Val Thr Val Asp
270 275 280

ggt aaa gaa gag atg aag gga atc gaa gtg atc aac tct tcg gtg cct 1035
Gly Lys Glu Glu Met Lys Gly Ile Glu Val Ile Asn Ser Ser Val Pro
285 290 295

gaa att gtc aag aag tat ttc agg ggt tac ctg aag tat atc agc caa 1083
Glu Ile Val Lys Lys Tyr Phe Arg Gly Tyr Leu Lys Tyr Ile Ser Gln
300 305 310

ccc gac atc gat gtc att tcc gcc acc ata gcg ttc tac aat aac ttt 1131
Pro Asp Ile Asp Val Ile Ser Ala Thr Ile Ala Phe Tyr Asn Asn Phe
315 320 325 330

gtg tct caa aag aat ttc tgg tct att gaa gat ctc tat cac aaa atg 1179
Val Ser Gln Lys Asn Phe Trp Ser Ile Glu Asp Leu Tyr His Lys Met
335 340 345

aaa ata tct tcg tct gac agc gcc gaa aga tat gtg gag tat gta gag 1227
Lys Ile Ser Ser Ser Asp Ser Ala Glu Arg Tyr Val Glu Tyr Val Glu
350 355 360

gaa gtt atg aag atg aaa aag gag aat gtc cca atc tct gag ata ttc 1275
Glu Val Met Lys Met Lys Lys Glu Asn Val Pro Ile Ser Glu Ile Phe
365 370 375

ata aaa atg tat gac cat aca ctt ccc att cat tat aag gga gcg ctt 1323
Ile Lys Met Tyr Asp His Thr Leu Pro Ile His Tyr Lys Gly Ala Leu
380 385 390

ttc gct tcc att ata gga tgc aaa ccc ccg caa atg gga gac aag atc 1371
Phe Ala Ser Ile Ile Gly Cys Lys Pro Pro Gln Met Gly Asp Lys Ile
395 400 405 410

tac tgg ttc tac tgc acc atg ctg gat cct tcc aga acc aat ctc ccg 1419
Tyr Trp Phe Tyr Cys Thr Met Leu Asp Pro Ser Arg Thr Asn Leu Pro
415 420 425

ctt tct ctg gaa gaa gtt aac ccc gaa cat ggg agc ggc gtg tgg gat 1467
Leu Ser Leu Glu Glu Val Asn Pro Glu His Gly Ser Gly Val Trp Asp
430 435 440

att ctg aaa gcg gga aag aaa acg cat atc aac agg ctc cgc aat atc 1515
Ile Leu Lys Ala Gly Lys Lys Thr His Ile Asn Arg Leu Arg Asn Ile
445 450 455

cac gca ctt agc ata cgt gag gat gat gag gag ggt ctt gaa atc gtt 1563
His Ala Leu Ser Ile Arg Glu Asp Asp Glu Glu Gly Leu Glu Ile Val
460 465 470

aaa aaa tac ata gat aga gac aaa tac tgt cag atc att tca gag aaa 1611
Lys Lys Tyr Ile Asp Arg Asp Lys Tyr Cys Gln Ile Ile Ser Glu Lys
475 480 485 490

aca att gat ctg ctg aaa agt ctc ggg tat gtt gaa aat act aca aag 1659
Thr Ile Asp Leu Leu Lys Ser Leu Gly Tyr Val Glu Asn Thr Thr Lys
495 500 505

ata aaa acc gtt gag gat ctt att cgt ttt ctt gta gag agt gaa aac 1707
Ile Lys Thr Val Glu Asp Leu Ile Arg Phe Leu Val Glu Ser Glu Asn
510 515 520

taaacccatt agcgccatga ttctcaaatt cgacactgaa ggcattgttc gtatcct 1764



59
522
PRT
Bacteriophage RM378

59

Met Asn Ile Asn Lys Tyr Arg Tyr Arg Gly Ala Tyr Ile Glu Leu Thr
1 5 10 15

Asn Pro Asp Ile Tyr Phe Asn Val Phe Asp Leu Asp Phe Thr Ser Leu
20 25 30

Tyr Pro Ser Val Ile Ser Lys Phe Asn Ile Asp Pro Ala Thr Phe Val
35 40 45

Thr Glu Phe Tyr Gly Cys Met Arg Val Glu Asn Lys Val Ile Pro Val
50 55 60

Asp Gln Glu Glu Pro Glu Phe Gly Phe Pro Leu Tyr Ile Phe Asp Ser
65 70 75 80

Gly Met Asn Pro Ser Tyr Arg Ser Glu Pro Leu Phe Val Ile Asn Ser
85 90 95

Phe Glu Glu Leu Arg Gln Phe Leu Lys Ser Arg Asn Ile Ile Met Val
100 105 110

Pro Asn Pro Ser Gly Ile Cys Trp Phe Tyr Arg Lys Glu Pro Val Gly
115 120 125

Val Leu Pro Ser Ile Ile Arg Glu Ile Phe Thr Arg Arg Lys Glu Glu
130 135 140

Arg Lys Leu Phe Lys Glu Thr Gly Asn Met Glu His His Phe Arg Gln
145 150 155 160

Trp Ala Leu Lys Ile Met Met Asn Ser Met Tyr Gly Ile Phe Gly Asn
165 170 175

Arg Ser Val Tyr Met Gly Cys Leu Pro Ile Ala Glu Ser Val Thr Ala
180 185 190

Ala Gly Arg Met Ser Ile Arg Ser Val Ile Ser Gln Ile Arg Asp Arg
195 200 205

Phe Ile Tyr Ser His Thr Asp Ser Ile Phe Val Lys Ala Phe Thr Asp
210 215 220

Asp Pro Val Ala Glu Ala Gly Glu Leu Gln Glu His Leu Asn Ser Phe
225 230 235 240

Ile Asn Asp Tyr Met Glu Asn Asn Phe Asn Ala Arg Glu Asp Phe Lys
245 250 255

Leu Glu Leu Lys Gln Glu Phe Val Phe Lys Ser Ile Leu Ile Lys Glu
260 265 270

Ile Asn Arg Tyr Phe Ala Val Thr Val Asp Gly Lys Glu Glu Met Lys
275 280 285

Gly Ile Glu Val Ile Asn Ser Ser Val Pro Glu Ile Val Lys Lys Tyr
290 295 300

Phe Arg Gly Tyr Leu Lys Tyr Ile Ser Gln Pro Asp Ile Asp Val Ile
305 310 315 320

Ser Ala Thr Ile Ala Phe Tyr Asn Asn Phe Val Ser Gln Lys Asn Phe
325 330 335

Trp Ser Ile Glu Asp Leu Tyr His Lys Met Lys Ile Ser Ser Ser Asp
340 345 350

Ser Ala Glu Arg Tyr Val Glu Tyr Val Glu Glu Val Met Lys Met Lys
355 360 365

Lys Glu Asn Val Pro Ile Ser Glu Ile Phe Ile Lys Met Tyr Asp His
370 375 380

Thr Leu Pro Ile His Tyr Lys Gly Ala Leu Phe Ala Ser Ile Ile Gly
385 390 395 400

Cys Lys Pro Pro Gln Met Gly Asp Lys Ile Tyr Trp Phe Tyr Cys Thr
405 410 415

Met Leu Asp Pro Ser Arg Thr Asn Leu Pro Leu Ser Leu Glu Glu Val
420 425 430

Asn Pro Glu His Gly Ser Gly Val Trp Asp Ile Leu Lys Ala Gly Lys
435 440 445

Lys Thr His Ile Asn Arg Leu Arg Asn Ile His Ala Leu Ser Ile Arg
450 455 460

Glu Asp Asp Glu Glu Gly Leu Glu Ile Val Lys Lys Tyr Ile Asp Arg
465 470 475 480

Asp Lys Tyr Cys Gln Ile Ile Ser Glu Lys Thr Ile Asp Leu Leu Lys
485 490 495

Ser Leu Gly Tyr Val Glu Asn Thr Thr Lys Ile Lys Thr Val Glu Asp
500 505 510

Leu Ile Arg Phe Leu Val Glu Ser Glu Asn
515 520



60
1619
DNA
Bacteriophage RM378

60

ccggtttgat acccgtattg gtcatttcct tgtggaaacc ccggttgaaa agtggagtaa 60

caaaatgttg cgcgtagctg aaaaacttgt aaccaattcc cgtaaacaga tttacgaagg 120

aggtgtgtga ttgctacggt ttcctatccg gaaactatga agttgtagac gaactccctg 180

atcaaccgac gcttccgaaa actcaaaaca agacttatag tacgctatgg aatcgatgaa 240

cgtaaaatac ccggttgagt accttatcga acacctgaac tcttttgagt ctccggaagt 300

agccgtcgaa tcccttcgca aggaggggat tatgtgcaaa aaccggggtg atctatacat 360

gttcaaatat caccttggtt gtaagtttga taagatatat caccttgcct gtcgcggggc 420

gattctccgc aaaacggata gtggttggaa agttctgtct tatccctttg acaaattttt 480

caactggggg gaagaactcc agccggaaat cgtaaactat tatcagacgc ttcgttacgc 540

gtctcccctg aatgaaaagc gcaaagccgg tttcatgttc aaacttccca tgaaactggt 600

tgaaaagctg gatggtactt gtgtggtttt atattatgat gaagggtgga aaattcacac 660

tcttgggagt attgacgcaa atggatccat tgtcaaaaac ggaatggtta ccactcatat 720

ggataaaaca tatcgagaat tgttctggga aacctttgaa aagaaatatc cgccttacct 780

tctctatcat ttgaactcct catactgtta catatttgaa atggttcatc cggacgcgcg 840

agtggtggtt ccttatgagg agccaaatat cattctgatc ggtgtgcgtt cggtggatcc 900

ggagaaggga tatttcgagg tgggtccctc cgaagaagcc gtacgcattt tcaacgaaag 960

tggcggaaaa ataaatctta agctaccggc tgttctgtct caagagcaaa actatactct 1020

ttttcgtgcc aatcgccttc aggaactatt tgaggaagtt acaccgcttt tcaaaagcct 1080

gagagacggt tatgaggtgg tatatgaagg atttgtagcc gtacaggaaa ttgccccgcg 1140

tgtttattac cgcacaaaga tcaagcaccc ggtatatctg gagctccacc ggattaaaac 1200

tacaatcact cctgagaagc tcgccgatct ttttcttgaa aacaaacttg atgattttgt 1260

acttaccccg gatgaacagg aaaccgtgat gaaactcaaa gaaatttata ccgatatgcg 1320

aaatcagctt gagtcatctt ttgatacgat ttataaagag atttccgaac aggtttctcc 1380

ggaagaaaac cccggagagt ttcgcaaaag gttcgctctt cgacttatgg attatcatga 1440

taaaagttgg ttttttgccc gccttgacgg cgacgaagag aaaatgcaaa agtcggaaaa 1500

gaagcttcta acggagagaa ttgaaaaggg gttatttaaa taaaaatgat aaaaaagcgt 1560

aatcctcttt tctggggaag acgggaactc aatcttcttc agcattttgc ccttgaagc 1619



61
1440
DNA
Bacteriophage RM378

61

gcttcgtcaa aactcacgtc tatagtatct atgtcgtagg gttcgaggtt ggaggcaatc 60

aggttgaaca gttcatcata atcataattc tcgaaaagaa tgttgcgaat accgatccct 120

ctttctggat cgtagggata ttcccccggc tcgatgaaaa gcaggagttt tatcttatcg 180

atcaggagtt ttaccgggtc atcaggaaat ctgaaattcg gtgcagtgtc gttcagatag 240

aacatttcat ttttgtttaa ataaatcctc gaggaatctt caaataaaga ggggcgttaa 300

tggatgaaaa gactgaggaa tatggtcaat cttatcgatc tcaaaaatca gtattatgct 360

tactctttca agtttttcga ctcctatcag atcagctggg ataattaccc gcatcttaaa 420

gagttcgtca ttgaaaacta tcccggcact tatttttcat gctacgctcc ggggattctg 480

tacaagcttt tcctcaaatg gaagcggggt atgatcattg acgactatga ccgacacccg 540

ctccgaaaga agttacttcc tcagtacaaa gagcaccgct atgaatacat tgagggaaaa 600

tacggtgtgg ttcctttccc cgggtttctg aaatatctga agttccactt tgaggacttg 660

cggtttaaaa tgcgcgatct tggaatcacc gatttcaaat atgcacttgc catttctctt 720

ttttacaacc gggtaatgct cagagatttt ctgaaaaact ttacctgtta ttacattgcc 780

gaatatgaag ctgacgatgt aatcgcacat ctggcgcgtg agattgcacg aagcaatatc 840

gacgtaaaca tcgtctcaac ggataaagat tattaccagc tatgggatga agaggatata 900

agagaaaggg tttatatcaa ttctctttca tgtagtgatg tgaagacacc ccgctacgga 960

tttcttacca ttaaagcact tcttggagac aaaagcgata acattcccaa atctctggaa 1020

aaaggaaaag gcgaaaagta tcttgaaaag aaaggatttg cggaggaaga ttacgataag 1080

gaactattcg agaataatct gaaggtgatc aggtttggag acgaatatct tggagaaagg 1140

gataaaagct ttatagaaaa tttttctacg ggggatactc tgtggaactt ttatgaattt 1200

ttttactatg accctttgca tgaacttttc ctcagaaata taagaaagag gagactatga 1260

aagtactcgc atttaccgat gcacctacgt ttcccacggg ggtgggtcat cagcttcaca 1320

acattatcaa ttacgggttt gacgcaaccg atcgctgggt tgtggtgcac ccgccccggt 1380

cgccaagggc tggagagact aaaaacgtcg ttattggaaa cactccagtc aagcttatca 1440



62
1508
DNA
Bacteriophage RM378

62

acttcccaaa tgctatgtgg aggtggatga tagaaagcgt attgttaatg aagaggcggt 60

caagtctttt ctccataagc atgttaccga actgctgaag aattatcagt aacccaaacc 120

taaacccgaa aaatatatgg aaacgattgt aatttcccaa aacaatacga cggagatgac 180

ggaacccccc cagaacattt ccgattcggt taaaagcggg tttatctatc ttatcgaaaa 240

gtctcatttc cttgaaaaga aaaacttcct taaaatcata tcgaacatgg acccccgccg 300

catttccaat ccggaggtgc gcgtggtggc ggagtacata tatgattatt tcaaaagtca 360

tagtaatttc ccttctaaaa gaaatctttg ccatcacttt gagtggagcg aagatctgga 420

aggagacccc gccgattatc agcgtatcat tcagtatctc aaatcttctt acattcgatc 480

ctctataaca aaaacgcttt catatcttga gaaggatgac ctttccgcgt tgaaagaaat 540

tgtcagagcc attcgggtgg tggaggatag tggggtgtcg ctggtggagg aattcgatct 600

tgcaaccagc gagtttaatg aactttttgt taaagaagaa cgcattccca ccccctggga 660

gagtgtaaac aaaaatatgg cgggcggtct tggtcgggga gagcttggaa tcgttatgct 720

tccttcgggg tggggtaagt catggttcct tgtttcactt ggtcttcatg cctttcgaac 780

gggtaagcgc gtgatttatt tcactctgga gcttgaccaa aaatatgtga tgaagcggtt 840

tttaaagatg tttgcacctt attgcaaagg acgcgcttct tcctatcgcg acgtttatca 900

aataatgaaa gagcttatgt tttctcagga taatcttttg ragattgttt tctgtaatgc 960

gatggaagat attgagcact atattgcgct gtataacccc gacgttgtgc tgattgacta 1020

tgccgatctt atttatgatg tggaaaccga caaagagaaa aattatctgc ttttgcaaaa 1080

aatttatagg aaacttcgtc tcattgcaaa ggtatataat acagcagtat ggagcgcctc 1140

tcagcttaat cgcggttccc tttcaaagca agccgacgtc gatttcattg agaaatacat 1200

tgccgattca tttgcaaaag ttkttgaaat cgacttcggg atggcgttta ttccggatag 1260

cgagaactca acccccgata ttcacgtcgg attcggtaaa atcttcaaaa accgtatggg 1320

tgcggtaaga aagctggaat atacaattaa ctttgaaaac tatacggtag acgttgctgt 1380

taaatgacac aagttaagac aaaagggctt aaagacatca gaataggtag aaaggagggt 1440

aagttcacac atgtaaatac aacaaagaaa ggaaagaata agaaatattt cagggcggaa 1500

catgaacg 1508



63
8
PRT
Artificial Sequence

Peptide


63

Asp Xaa Xaa Ser Leu Tyr Pro Ser
1 5



64
33
DNA
Artificial Sequence

Nucleic acid


64

cacgagctca tgaagatcac gctaagcgca agc 33



65
33
DNA
Artificial Sequence

Nucleic acid


65

acaggtacct tactcaggta tttttttgaa cat 33



66
33
DNA
Artificial Sequence

Nucleic acid


66

cacgagctca tgaacatcaa caagtatcgt tat 33



67
30
DNA
Artificial Sequence

Nucleic acid


67

acaggtacct tagttttcac tctctacaag 30



68
28
DNA
Artificial Sequence

Nucleic acid


68

gggaattctt atgaacgtaa aatacccg 28



69
28
DNA
Artificial Sequence

Nucleic acid


69

ggagatctta tttaaataac cccttttc 28



70
30
DNA
Artificial Sequence

Nucleic acid


70

gggaattctt atgaaaagac tgaggaatat 30



71
26
DNA
Artificial Sequence

Nucleic acid


71

ggagatctca tagtctcctc tttctt 26



72
31
DNA
Artificial Sequence

Nucleic acid


72

gggcaattgt tatggaaacg attgtaattt c 31



73
26
DNA
Artificial Sequence

Nucleic acid


73

cgggatcctc atttaacagc aacgtc 26