Patent Publication Number: US-2004053274-A1

Title: Gene cluster of vicenistatin biosynthesis, a vicenisamine glycosyltransferase polypeptide, and a gene encoding the polypeptide

Description:
BACKGROUND OF THE INVENTION  
       [0001] 1. Field of the Invention  
       [0002] This invention relates to an enzyme cluster of vicenistatin biosynthesis enzyme, and a gene cluster of vicenistatin biosynthesis enzyme encoding the enzyme cluster. Particularly, this invention relates to VinC enzyme, which is a glycosyltransferase catalyzing the reaction to produce vicenistatin using dTDP-vicenisamine as a substrate, and to vinC gene encoding the enzyme.  
       [0003] 2. Prior Art  
       [0004] Enthusiastic investigation on genes encoding biosynthesis of polyketide compounds has been performed worldwide, and attempts to create new polyketides have been also performed by deletion or insertion of the gene. Under such situation, to obtain novel polyketide compounds, not only simple polyketides but also complex polyketides have attracted attention of researches as novel genetic resources, and wide-range investigation has been performed.  
       [0005] Vicenistatin is an anticancer antibiotic produced by Streptomyces sp. HC-34 strain of actinomycetes. From a study on experimental human cancer research using nude mice which received transplantation of human cancer cells, it has been known that vicenistatin can markedly inhibit growth of human intestinal cancer cells. As to its chemical structure, plane structure of vicenistatin and absolute conformation on vicenisamine (sugar moiety of vicenistatin) were firstly elucidated. Then, the absolute configuration of the aglycon was determined. The actinomycetes species capable of producing vicenistatin was identified as  Streptomyces halstedii  HC-34.  
       [0006] As to the biosynthetic pathway of vicenistatin, it was elucidated that it consists of the following steps. Firstly, glutamate as a starting material undergoes a series of reactions including mutase reaction to produce a polyketide starter unit. Then, propionate and acetate are introduced as precursors to evoke a normal polyketide elongation reaction to produce a characteristic 20-membered cyclic aglycon portion. It was clarified that vicenisamine was derived from glucose via conversion of functional groups similar to reaction involved in production of other aminosugars, and N-methyl groups derived from methionine was incorporated for biosynthesis of vicenisamine.  
       [0007] To create a novel compound by further modification on the molecular structure through biosynthetic engineering, attempts have been made for identification of genes responsible for biosynthesis of vicenistatin. A number of novel lactam polyketide antibiotics were discovered by researches mainly achieved in Japan, and some studies were reported on biosynthetic precursors. However, no study has been made on the genes and enzymes involved in the biosynthesis of those compounds.  
       SUMMARY OF THE INVENTION  
       [0008] Vicenistatin has a structure comprising unique 20-membered lactam glycoside and it is a noteworthy anti biotic because of its strong inhibitory effect on growth of human solid cancer cells transplanted into experimental models. However, vicenistatin is not put into practical use yet because of its limited solubility and moderate toxicity. However, if these disadvantages will be conquered in the future by researches on chemical or biosynthetic engineering, it will provide a useful medicine. Therefore, for the purpose to achieve development of novel useful substances by biosynthetic engineering, elucidation and modification on the system involved in biosynthesis of the unique chemical structure are required. Thus, the object of this invention is to obtain genes involved in biosynthesis of vicenistatin, which is the principle genes in the biosynthetic system, and to elucidate functions of the genes.  
       [0009] Vicenistatin is a glycoside containing an aminosugar. There is no known compound containing sugar moiety identical to vicenisamine, but it was assumed that some similar genes responsible for biosynthesis of similar aminosugars might be involved in biosynthesis of vicenistatin. It is known that the aglycon portion is a polyketide derived from acetate/propionate as its precursor. From this knowledge, it was predicted that genes similar to those responsible for biosynthesis of polyketide synthases (PKS) were involved in biosynthesis of the aglycon portion. However, it was also known that the polyketide starter unit comprises unique amino acids derived from glutamate, therefore, it was predicted that certain novel genes different from those conventionally known might be involved in biosynthesis of this polyketides.  
       [0010] In this invention, an attempt was made to identify genes responsible for biosynthesis of vicenistatin, using knowledge on ketosynthases (KS), which is indispensable for biosynthesis of polyketides and having high homology with synthases of various polyketides, as well as analogies of aminosugars and singular starter unit, using techniques of PCR and hybridization. As a result, the genes encoding cluster of enzymes indispensable to produce the ultimate structure of vicenistatin were identified and base sequences of the genes were sequenced. This knowledge provides a great possibility for modification of vicenistatin biosynthesis through biosynthetic engineering, by methods such as modification, deletion or duplication in the base sequence of the biosynthetic genes, or insertion of some exogenous genes, etc.  
       [0011] The first aspect of this invention is to provide a gene cluster comprising a base sequence represented by base Nos. 1-64492 shown in the SEQ ID No. 1 in the sequence listing.  
       [0012] The second aspect of this invention is to provide a polypeptide comprising an amino acid sequence represented by amino acid Nos. 1-419 shown in the SEQ ID No. 4 in the sequence listing. A polypeptide comprising an amino acid sequence in which a part of the amino acid sequence is deleted or another amino acid sequence is added to the amino acid sequence, or a part of the amino acid sequence is substituted with another amino acid sequence, and exhibiting enzymatic activity as a glycosyltransferase, is also included within the scope of this invention. Furthermore, a gene encoding the polypeptide is also included within the scope of this invention.  
       [0013] The third aspect of this invention is to provide a gene comprising a base sequence represented by base Nos. 2790-4049 shown in the SEQ ID No. 1 in the sequence listing. A gene comprising a base sequence in which a part of the base sequence is deleted or another base sequence is added to the base sequence, or a part of the base sequence is substituted with another base sequence, and encoding a polypeptide exhibiting enzymatic activity as a glycosyltransferase, is also included within the scope of this invention.  
       [0014] The fourth aspect of this invention is to provide a method for production of vicenistatin by catalytic reaction of the glycosyltransferase comprising the polypeptide as described above, using dTDP-vicenisamine as a starting material. 
     
    
    
     BRIEF DESCRIPTION OF THE DRAWINGS  
     [0015]FIG. 1 is a schematic figure showing gene mapping of the gene obtained in this study.  
     [0016]FIG. 2 is a figure showing results of homology analysis performed on the respective open reading frames (ORFs).  
     [0017]FIG. 3 is a figure showing the biosynthetic pathway of vicenistatin agylcon.  
     [0018]FIG. 4 is a figure showing the biosynthetic pathway of vicenistatin.  
     [0019]FIG. 5 is a figure showing the synthetic pathway of the substrates (dTDP-vicenisamine, dTDP-mycarose, and dTDP-2-deoxyglucose) used for the enzyme reaction. 
    
    
     DETAILED DESCRIPTION OF THE INVENTION  
     [0020] A cosmid library comprising DNA insert fragments of about 40 kbp were constructed according to the conventional method, from the genome of  Streptomyces halstedii  sp. HC-34, which is a vecenistatin (an antibiotic) producing bacteria. From knowledge on biosynthesis of aminosugar, it was assumed that both of dTDP-glucose-4,6-dehydratase and dTDP-4-keto-6-deoxyglucose-2,3-dehydratase were involved in biosynthesis of vicenisamine, which is a sugar component of vecenistatin. Therefore, the known base sequences of the enzymes were used to design probes and investigations were performed using PCR and other approaches. Consequently, two kinds of cosmids were isolated.  
     [0021] Subsequently, the two kinds of cosmids were sequenced. In general, genes involved in biosynthesis of antibiotics form a cluster and exist in forms of one mass. In view of this knowledge, the inventors searched for which is the gene encoding the enzyme concerned here. In this case, the previously reported knowledge on the mechanism of biosynthesis of antibiotics was effective. Particularly, in view of the knowledge on the sequence conserved among genes encoding ketosynthase (KS) involved in polyketide biosynthesis, the inventors limited candidate genes responsible for vicenistatin biosynthesis enzyme to cosmids K1B10 and K1D11. They analyzed on base sequence of the genes existing adjacent to these cosmids, and functions of respective open reading frames (ORFs) were predicted from homology search from existing databases.  
     [0022] Again, the previous observation was-effective, that is, it was known that the starter unit of the lactam portion of vicenistatin was derived from glutamate and the starter unit was formed via a mutase reaction. Based on this knowledge, the inventors found ORFs having high homology with known glutamate mutase. Moreover, they confirmed that putative function of respective modules in the ORFs highly correlated with the biosynthetic pathway of vicenistatin. The entire cluster and the respective open reading frames of the sugar portion and the lactam portion were named to be vin gene, in connection with the name of vicenistatin.  
     [0023] Furthermore, to confirm the function of the vin gene cluster, the inventors expressed glycosyltransferase gene (vinC) in  E. coli,  and the glycosyltransferase was used for the reaction between chemically synthesized dTDP-vicenisamine and the aglycon chemically derived from vicenistatin. As a result, it was confirmed that this vinC efficiently catalyzed this reaction as a transferase. Therefore, it was confirmed that the vin gene cluster was responsible for vicenistatin biosynthesis. Hitherto, the gene identified to be a biosynthetic gene of macrocyclic lactam antibiotic was limited to only rifamycin, which is a member of ansamycin group antibiotics. Rifamycin is different from vicenistatin in various aspects including its chemical structure and biological activity, therefore, the gene cluster of this invention will serve as a valuable resource for further creation of novel substances, using techniques of biosynthetic engineering.  
     [0024] As to vinC gene which function was identified in this invention, the VinC protein was produced in a large scale in  E. coli,  by the technique of electrophoresis. In addition, to confirm its function, glycosyltransferase reaction was performed between chemically synthesized dTDP-vicenisamine and the vicenistatin aglycon. Moreover, it was detected that the VinC enzyme can catalyze transferase reaction of chemically synthesized dTDP-mycarose or dTDP-2-deoxyglucose with the vicenistatin aglycon. From this result, it was suggested that use of the enzyme of this invention would enable synthesis of a novel polyketide glycosides hitherto unknown. According to this invention, genes responsible for biosynthesis of vicenistatin (an anticancer antibiotic) were identified. Among these enzymes, particularly, the function of VinC was confirmed as a glycosyltransferase.  
     [0025] The base sequence described in SEQ ID No.1 in the sequence listing represents the gene corresponding to the entire region of the gene cluster of vicenistatin biosynthesis enzyme, obtained by analysis of the base sequence of the region of cosmid K1B10 and the regions adjacent to it. Genes involved in biosynthesis of vicenistatin form a cluster and the genes described in SEQ ID No.1 in the sequence listing encode various enzymes involved in vicenistatin biosynthesis, not only the glycosyltransferase.  
     [0026] That is, in the gene described in SEQ ID No.1 in the sequence listing, the portion corresponding to base Nos. 2790-4049 encodes a glycosyltransferase, serving for biosynthesis of vicenistatin using vicenisamine as a substrate. The transferase of vicenisamine is a polypeptide represented by an amino acid sequence as listed in the SEQ ID No.4 in the sequence listing.  
     [0027] The polypeptide consisting of an amino acid sequence in which a part of said polypeptide represented by amino acid sequence shown in SEQ ID NO: 4 in the sequence listing is deleted, substituted or added with another amino acid sequence means a polypeptide in which ten or less, preferably five or less, and more preferably two or less amino acids of the sequence is deleted, substituted or added to the amino acid sequence represented by SEQ ID NO: 4 in the sequence listing. Moreover, such polypeptide exhibits homology 90% or more, preferably 95% or more and still preferably 99% or more with the amino acid sequence represented by in SEQ ID NO: 4 in the sequence listing. Such polypeptide is also within the scope of this invention so far as it exhibits enzymatic activity as a glycosyltransferase, that is, catalyzing synthesis of vicenistatin using vicenisamine as a substrate.  
     [0028] According to technique of gene recombination, artificial modification can be achieved at a specific site of basic DNA, without alteration or with improvement of basic characteristic of said DNA. Concerning a gene having native sequence provided according to this invention or modified sequence different from said native sequence, it is also possible to perform artificial modification such as insertion, deletion or substitution to obtain gene of equivalent or improved characteristic compared with said native gene. Moreover, a gene with such mutation is also included in the scope of this invention.  
     [0029] That is, the gene, consisting of a base sequence in which a part of said gene represented by base Nos. 2790-4049 in the SEQ ID No.1 in the sequence listing is deleted, substituted or added with another base sequence means a gene in which ten or less, preferably five or less, and more preferably two or less bases of the sequence is deleted, substituted or added to the base sequence base Nos. 2790-4049 shown in the SEQ ID No.1 in the sequence listing. Moreover, such gene exhibits homology 90% or more, preferably 95% or more and still preferably 99% or more with the base sequence represented by base Nos. 2790-4049 shown in the SEQ ID No. 1 in the sequence listing. Such gene is also within the scope of this invention so far as it encodes a polypeptide exhibiting enzymatic activity as a glycosyltransferase, that is, catalyzing synthesis of vicenistatin using vicenisamine as a substrate. In addition, such gene hybridizes with the base sequence represented by base Nos. 2790-4049 shown in the SEQ ID No.1 in the sequence listing under stringent conditions.  
     [0030] The condition for hybridization can be selected by those skilled in the art ad libitum. That is, hybridization can be performed by the following procedure. DNA molecules or RNA molecules to be tested are transferred onto a membrane, then the membrane is hybridized with a labeled probe in a proper hybridization buffer. The hybridization buffer may comprise, for example, 5×SSC, 5% (weight %) dextran sulfate, {fraction (1/20)} volume of blocking reagent and 2 to 7×SSC, however, other various formulation can be also used for the hybridization buffer. The blocking reagent for nucleic acid hybridization may comprise, for example, a buffer (pH 7.5) containing 0.1M maleic acid and 0.15M sodium chloride, and commercially available blocking reagent for hybridization may be dissolved into the buffer at the concentration of 10%. The 20×SSC solution may comprise 3M sodium chloride and 0.3M citrate, and the SSC solution may be preferably utilized at the concentration of 3 to 6×SSC, more preferably at the concentration of 4 to 5×SSC.  
     [0031] The temperature for hybridization may preferably be 40 to 80° C., more preferably be 50 to 70° C., further more preferably be 55 to 65° C. Incubation may be performed from several hours to overnight, then washed by a washing buffer. The temperature for washing may preferably be room temperature, more preferably it may be the temperature used for hybridization. The formulation for the washing buffer may preferably comprise 6×SSC and 0.1% (weight %) SDS, more preferably may comprise 4×SSC and 0.1% (weight %) SDS, further preferably may comprise 2×SSC and 0.1% (weight %) SDS, more further preferably may comprise 1×SSC and 0.1% (weight %) SDS, most preferably may comprise 0.1×SSC and 0.1% (weight %) SDS. The membrane may be washed by such washing buffer, then DNA molecule or RNA molecule may be distinguished by the hybridization with the labeled probe.  
     [0032] It is known that the gene cluster shown in the sequence ID No. 1 of the sequence listing includes plural ORFs, except for that of the glycosyltransferase, and predicted amino acid sequences encoded by the ORFs are also obtained. Moreover, the functions of the enzymes defined by these amino acid sequences can be predicted based on the results of homology search with amino acid sequences derived from various enzymes.  
     [0033] In the SEQ ID No. 1 in the sequence listing, bases Nos. 695-1762 represents an ORF and the gene corresponding to the ORF (vinA) encodes a protein consisting of 355 amino acids. The sequence shown in SEQ ID No. 2 in the sequence listing represents predicted amino acid sequence encoded by the vinA gene. As will be detailed later, that protein is assumed to be dTDP-glucose synthase.  
     [0034] In the SEQ ID No. 1 in the sequence listing, bases Nos. 1759-2730 represents an ORF and the gene corresponding to the ORF (vinB) encodes a protein consisting of 323 amino acids. The sequence shown in SEQ ID No. 3 in the sequence listing represents predicted amino acid sequence encoded by the vinB gene. As will be detailed later, that protein is assumed to be dTDP-glucose 4,6-dehydratase.  
     [0035] In the SEQ ID No. 1 in the sequence listing, bases Nos. 4412-11194 represents an ORF and the gene corresponding to the ORF (vinP2) encodes a protein consisting of 2260 amino acids. The sequence shown in SEQ ID No. 5 in the sequence listing represents predicted amino acid sequence encoded by the vinP2 gene. As will be detailed later, that protein is assumed to be polyketide synthase module.  
     [0036] In the SEQ ID No. 1 in the sequence listing, bases Nos. 11260-21348 represents an ORF and the gene corresponding to the ORF (vinP3) encodes a protein consisting of 3362 amino acids. The sequence shown in SEQ ID No. 6 in the sequence listing represents predicted amino acid sequence encoded by the vinP3 gene. As will be detailed later, that protein is assumed to be polyketide synthase module.  
     [0037] In the SEQ ID No. 1 in the sequence listing, bases Nos. 21411-32837 represents an ORF and the gene corresponding to the ORF (vinP4) encodes a protein consisting of 3808 amino acids. The sequence shown in SEQ ID No. 7 in the sequence listing represents predicted amino acid sequence encoded by the vinP4 gene. As will be detailed later, that protein is assumed to be polyketide synthase module.  
     [0038] In the SEQ ID No. 1 in the sequence listing, bases Nos. 33262-33972 (complementary strand) represents an ORF and the gene corresponding to the ORF (vinG) encodes a protein consisting of 236 amino acids. The sequence shown in SEQ ID No. 8 in the sequence listing represents predicted amino acid sequence encoded by the vinG gene. As will be detailed later, that protein is assumed to be N-methyltransferase, that is, an enzyme closely related to dTDP-N-dimethyldesosamine-N-methyltransferase.  
     [0039] In the SEQ ID No. 1 in the sequence listing, bases Nos. 33980-35173 (complementary strand) represents an ORF and the gene corresponding to the ORF (vinF) encodes a protein consisting of 397 amino acids. The sequence shown in SEQ ID No. 9 in the sequence listing represents predicted amino acid sequence encoded by the vinF gene. As will be detailed later, that protein is assumed to be dTDP-hexose-aminotransferase.  
     [0040] In the SEQ ID No. 1 in the sequence listing, bases Nos. 35320-36801 represents an ORF and the gene corresponding to the ORF (vinD) encodes a protein consisting of 493 amino acids. The sequence shown in SEQ ID No. 10 in the sequence listing represents predicted amino acid sequence encoded by the vinD gene. As will be detailed later, that protein is assumed to be dTDP-4-keto-6-deoxyglucose-2,3-dehydratase.  
     [0041] In the SEQ ID No. 1 in the sequence listing, bases Nos. 36849-37841 represents an ORF and the gene corresponding to the ORF (vinE) encodes a protein consisting of 330 amino acids. The sequence shown in SEQ ID No. 11 in the sequence listing represents predicted amino acid sequence encoded by the vinE gene. As will be detailed later, that protein is assumed to be dTDP-4-keto-6-deoxyhexose-2,3-reductase.  
     [0042] In the SEQ ID No. 1 in the sequence listing, bases Nos. 38022-38498 represents an ORF and the gene corresponding to the ORF (vinH) encodes a protein consisting of 158 amino acids. The sequence shown in SEQ ID No. 12 in the sequence listing represents predicted amino acid sequence encoded by the vinH gene. As will be detailed later, that protein is assumed to be S-subunit of glutamate mutase.  
     [0043] In the SEQ ID No. 1 in the sequence listing, bases Nos. 38495-39904 represents an ORF and the gene corresponding to the ORF (vinI) encodes a protein consisting of 469 amino acids. The sequence shown in SEQ ID No. 13 in the sequence listing represents predicted amino acid sequence encoded by the vinI gene. As will be detailed later, that protein is assumed to be E-subunit of glutamate mutase.  
     [0044] In the SEQ ID No. 1 in the sequence listing, bases Nos. 39990-40889 represents an ORF and the gene corresponding to the ORF (vinJ) encodes a protein consisting of 299 amino acids. The sequence shown in SEQ ID No. 14 in the sequence listing represents predicted amino acid sequence encoded by the vinJ gene. As will be detailed later, that protein is assumed to be proline iminopeptidase.  
     [0045] In the SEQ ID No. 1 in the sequence listing, bases Nos. 40886-41869 represents an ORF and the gene corresponding to the ORF (vinK) encodes a protein consisting of 327 amino acids. The sequence shown in SEQ ID No. 15 in the sequence listing represents predicted amino acid sequence encoded by the vinK gene. As will be detailed later, that protein is assumed to be acyl CoA-ACP transacylase closely related to malonyl CoA-ACP transacylase.  
     [0046] In the SEQ ID No. 1 in the sequence listing, bases Nos. 41987-42235 represents an ORF and the gene corresponding to the ORF (vinL) encodes a protein consisting of 82 amino acids. The sequence shown in SEQ ID No. 16 in the sequence listing represents predicted amino acid sequence encoded by the vinL gene. As will be detailed later, that protein is assumed to be acyl carrier protein.  
     [0047] In the SEQ ID No. 1 in the sequence listing, bases Nos. 42289-43863 represents an ORF and the gene corresponding to the ORF (vinM) encodes a protein consisting of 524 amino acids. The sequence shown in SEQ ID No. 17 in the sequence listing represents predicted amino acid sequence encoded by the vinM gene. As will be detailed later, that protein is assumed to be non-ribosomal type peptide synthase.  
     [0048] In the SEQ ID No. 1 in the sequence listing, bases Nos. 44156-45592 represents an ORF and the gene corresponding to the ORF (vinN) encodes a protein consisting of 478 amino acids. The sequence shown in SEQ ID No. 18 in the sequence listing represents predicted amino acid sequence encoded by the vinN gene. As will be detailed later, that protein is assumed to be long chain fatty acid-CoA ligase.  
     [0049] In the SEQ ID No. 1 in the sequence listing, bases Nos. 45589-46833 represents an ORF and the gene corresponding to the ORF (vinO) encodes a protein consisting of 414 amino acids. The sequence shown in SEQ ID No. 19 in the sequence listing represents predicted amino acid sequence encoded by the vinO gene. As will be detailed later, that protein is assumed to be PLP-dependent decarboxylase.  
     [0050] In the SEQ ID No. 1 in the sequence listing, bases Nos. 46982-64492 represents an ORF and the gene corresponding to the ORF (vinP1) encodes a protein consisting of 5836 amino acids. The sequence shown in SEQ ID No. 20 in the sequence listing represents predicted amino acid sequence encoded by the vinP1 gene. As will be detailed later, that protein is assumed to be polyketide synthase module.  
     [0051] The vin gene cluster is consisted of these genes and the proteins encoded by the gene cluster are involved in vicenistatin biosynthesis. Information on this gene cluster is useful for efficient production of vicenistatin, as well as for tools available for development of novel antibiotics. Therefore, this invention provides a great opportunity for development of novel useful substances.  
     EXAMPLES  
     Example 1  
     Screening of 4,6-dehydratase Gene  
     [0052] Deoxysugars are ubiquitously present in bacterial systems as a constituent of the cell wall or of secondary metabolites. Indeed, deoxysugars are present in many kinds of antibiotics such as macrolides and anthracylines. List of known deoxysugars include, for example, mycarose and desosamine contained in erythromycin, daunosamine contained in daunorubicin, mikamynose contained in tyrosine, and vancosamine contained in vancomycin, etc. Many deoxysugars play an important role in exerting the activity of those antibiotics.  
     [0053] Recently, many studies have been made on biosynthesis of 2,6-deoxysugars, and the biosynthesis of various deoxysugars is generally believed to proceed as follows: glucose-1-phosphate is metabolized to NDP-glucose by NDP-glucose synthase; the latter is then deoxygenated at C-6 by NDP-glucose-4,6-dehydratase to yield NDP-4-keto-6-deoxy glucose; and it is further deoxygenated at C-2 by NDP-4-keto-6-deoxy glucose 2,3-dehydratase. This sequence is the common pathway of 2,6-deoxysugar biosynthesis, and various 2,6-deoxysugars are assumed to be biosynthesized as the result of further modification.  
     [0054] Many genes involved in biosynthesis of various deoxysugars have been cloned. In biosynthetic pathway of 2,6-deoxysugars, it was demonstrated that the genes coding for 4,6-dehydratase and 2,3-dehydratase revealed to exhibit high homology with respective congeners. Thus they serve as a powerful tool for cloning of genes involved in the production of the secondary metabolite products.  
     [0055] Based on a study using labeled precursors, it was confirmed that vicenisamine was derived from glucose. Therefore, it was predicted that vicenisamine would also take the same biosynthetic pathway similar to other 2,6-deoxysugars. Thus, the inventors presumed that a gene responsible for biosynthesis of vicenistatin would be cloned by utilizing a gene responsible for biosynthesis of deoxysugar as a probe. Thus, the inventors utilized a gene coding for 4,6-dehyratase as a probe for screening on a genomic library, because the 4,6-dehyratase gene exhibited high homology among corresponding genes.  
     [0056] (Design of Primers)  
     [0057] Gene coding for 4,6-dehydratase exhibited very high homology among corresponding genes. In the base sequences of 4,6-dehydratase, the regions of 46DH-1 and 46DH-2 were known to be conserved in their sequences. It was expected that if sense and anti-sense primers were designed based on the base sequences of 46DH-1 and 46DH-2 and the two primers were used in PCR, a DNA fragment of 530 bp would be amplified.  
     [0058] 46DH-1: 5′-ACSGGYCSBGCCGCHTTCATCGG-3′ 
     [0059] 46DH-2: 5′-GRWRCTGRTRSGGCCGTAGTTGTT-3′ 
     [0060] (where S represents C or G; Y represents C or T; B represents C, G or T; H represents A, C or T; R represents A or G; and W represents A or T.)  
     [0061] (PCR Using Genomic DNA as a Template)  
     [0062] To perform screening on genomic library directed to isolation of clones containing a gene coding for 4,6-dehydratase, it is necessary to confirm whether 4,6-dehydratase gene is specifically amplified using the designed primers. At first, PCR was conducted using a genome of  Streptomyces halstedii  HC34 ( S. halstedii ) as a template, for this purpose. PCR condition consisted of 30 cycles with a cycle of 94° C. for 7 minutes, 94° C. for 30 seconds, 52° C. for 30 seconds, and 72° C. for 60 seconds, which was lastly followed by 72° C. for 7 minutes. As a result of the PCR, a DNA fragment having an expected size (about 530 bp) was obtained.  
     [0063] (Sequencing of the PCR Product)  
     [0064] The DNA fragment obtained by PCR was subcloned into a pT7Blue T vector, which was then introduced into  E. coli.  Plasmids were isolated on the obtained transformants and the sequences were confirmed to obtain three sequences of 46DH-A, 46DH-B and 46DH-C. The inventors performed homology search on the databases, and found that these sequences commonly exhibited high homology with known 4,6-dehydratase genes. From this, it was confirmed that the designed primers enabled the specific amplification of the gene encoding 4,6-dehydratase and that they could be used for screening of genomic library in the search of the target gene. It was predicted that any one of the three sequences was obtained by amplifying a gene involved in biosynthesis of vicenistatin. Next, a genomic library was screened using 46DH-1 and 46DH-2 as primers.  
     [0065] (Screening of the Genomic Library)  
     [0066] A genomic library derived from  S. halstedii  HC34 was constructed as follows. A genomic library is a population of DNA clones obtained by cutting the chromosomal DNA of a living organism into fragments having an appropriate length, and subcloning of these fragments into a vector. Each DNA fragment comprises a part of the genome chosen at random. To prepare a genomic library of  S. halstedii  HC34, the genome of  S. halstedii  HC34 was randomly digested with Sau3AI, and DNA fragments having a length of approximately 40 kbp were subcloned into a cosmid vector pOJ446, which gave a total population of 6048 clones. They were subdivided into 63 pools of 96 clones and they were stored as the divided 63 pools, otherwise the target gene has to be cloned from enormous amount of 6048 clones.  
     [0067] (Primary Screening)  
     [0068] Primary screening by PCR was conducted on the 63 pools in order to screen pools containing a gene encoding 4,6-dehydratase. Using a library fraction contained in each pool as a template, PCR was conducted with 46DH-1 and 46DH-2 as primers, and pools exhibiting amplification of DNA fragment of the purpose having a size of 530 bp were selected as a positive candidate. Thus, 30 pools were found to be positive.  
     [0069] In the same manner, PCR primers of 23DH-1 and 23DH-2 were designed from dTDP-4-keto-6-deoxyglucose 2,3-dehydratase gene, which was known to have high homology among cognate genes, and PCR based on the primers was conducted using the genome as a template. As a consequence, two kinds of base sequences (23DH-A and 23DH-B) were confirmed and both of which exhibited high homology with known 2,3-dehydratase genes. When the library was screened using these primers, 17 positive clones were obtained. The sequences of 23DH-1 and 23DH-2 are as shown below.  
                                          23DH-1:   5′-AGGCCACCCGSAGCAACTACAC-3′                           23DH-2:   5′-GAASCGSCCGCCCTCCTCSGA-3′          
 
     [0070] In general, genes involved in biosynthesis of secondary metabolites in microorganisms tends to form a cluster. Therefore, it was expected that the genes encoding 4,6-dehydratase and 2,3-dehydratase, both of which are involved in the synthesis of vicenistatin, would exist close to each other, and thus the two genes of the purpose might exist in a same cosmid. Therefore, nine pools containing the two genes were selected as positive candidates.  
     [0071] (Secondary Screening)  
     [0072] PCR for the secondary screening proceeded in the same manner as in the first screening. In the secondary screening, those containing two genes of 4,6-dehydratase gene and 2,3-dehydratase gene were selected as positive. As a consequence, two cosmid clones (K1B10 and K1D11) were isolated.  
     [0073] (Classification of Positive Clones)  
     [0074] As described above, the two cosmids of K1B10 and K1D11 contained 4,6-dehydratase gene and 2,3-dehydratase gene. Based on sequence result of the PCR products, it was demonstrated that there are three kinds of genes (46DH-A, 46DH-B and 46DH-C) and two kinds of genes (23DH-A and 23DH-B) coding for 4,6-dehydratase and 2,3-dehydratase respectively, existing on the genome. Thus, the inventors confirmed on what kind of 4,6-dehydratase and 2,3-dehydratase correspond to those contained in the K1B10 and the K1D11, respectively. For this purpose, the inventors performed PCR using each cosmid as a template, PCR products were subcloned into an appropriate vector, then the clones were sequenced. As a result, they found that 4,6-dehydratase gene and 2,3-dehydratase gene contained in the K1B10 correspond to 46DH-A and 23DH-A, respectively. In the same manner it was revealed that 4,6-dehydratase gene and 2,3-dehydratase gene contained in the K1D11 correspond to 46DH-B and 23DH-B, respectively.  
     [0075] From this, it was suggested that the two cosmids represented different portions of the genome. It had been known that there were two kinds of genes coding for 2,3-dehydratase in the genome, and cosmids containing respective 2,3-dehydratase genes were cloned. Therefore, it was expected that genes responsible for vicenistatin biosynthesis were likely to exist either in the cosmid K1B10 or in the cosmid K1D11. Thus, the inventors proceeded to the analysis of the two cosmids.  
     [0076] (Estimation on the Genes Contained in the Positive Clones)  
     [0077] The two cosmids contained different kinds of genes coding for 4,6-dehydratase and 2,3-dehydratase, thus, it was assumed that the genes were involved in the biosynthesis of two different 2,6-deoxysugars. It was suggested that one of the 2,6-deoxysugars was vicenisamine, and that regions adjacent to 4,6-dehydratase gene and 2,3-dehydratase gene in the cosmids K1B10 and K1D11 might contain other genes coding for the enzymes involved in biosynthesis of vicenisamine. The inventors tried to confirm which one of the two cosmids contained genes encoding for enzyme catalyzing biosynthesis of the deoxysugar and involved in biosynthetic system of vicenistatin.  
     [0078] Each cosmid had been prepared to have an insert size of about 40 kbp. Thus, it was not easy to sequence the total insert at one time. Therefore, an attempt was made to estimate what gene is contained in each of the cosmid. For this purpose, the cosmid was digested with restriction enzymes, and the resulting DNA fragments were subcloned into an appropriate vector, then the clones were sequenced.  
     [0079] Firstly, the cosmid K1B10 was cleaved with BamHI, BglII and EcoRI, the resulting DNA fragments were subcloned. The cosmid K1B10 was found to contain base sequences having high homologies with those coding for NDP-glucose 4,6-dehydratase, NDP-4-keto-6-deoxyglucose 2,3-dehydratase, NDP-hexose aminotransferase, and NDP-aminohexose-N-methyltransferase. The cosmid also contained sequences having high homologies with those for PKS (polyketide synthase) module I and glutamate mutase. On the other hand, the cosmid K1D10 was found to contain base sequences having high homologies with those for PKS module I and gycosyltransferase. It further contained a sequence having high homology with that for cytochrome P450.  
     [0080] Comparison of the genes contained in the two cosmids revealed that the cosmid K1B10 contained the genes coding for aminotransferase and for methyltransferase, both of which were considered to be involved in the biosynthesis of vicenisamine, as well as the gene for glutamate mutase which was predicted to be involved in biosynthesis of vicenistatin starter. From this it was suggested that genes existing in the region adjacent to the cosmid K1B10 were involved in the biosynthesis of vicenistatin.  
     Example 2  
     Sequencing of Gene Cluster  
     [0081] Then, regions in and adjacent to the cosmid K1B10 were sequenced to obtain the entire sequence involved in biosynthesis of vicenistatin. Cosmid clones adjacent to the cosmid K1B10 were obtained, and the clones were sequenced. The base sequence data obtained were translated into amino acid sequences, and their functions of the respective genes were estimated by performing homology search based on public database (BLAST).  
     [0082] (Sequencing of the Cosmid)  
     [0083] A DNA sequencer reveals, at each run, the sequence of a DNA fragment having a length of about 600 to 700 bp at maximum. The cosmids derived from genomic library of  S. halstedii  HC34 was produced to contain the insert having length of about 40 kbp. In order to sequence the insert having such a large size, it was necessary to cut the cosmid DNA into fragments having an appropriate size, and to subclone the fragments into an appropriate vector. If the cosmid DNA was cut into small fragments having a length of about 500 bp, the base sequence of the both chains could be sequenced. However, in such case, identification of the restriction sites would be very difficult and ligation of respective fragments would become an excessive work. To cope with this, each insert of 40 kbp was cleaved with an appropriately chosen restriction enzyme into fragments of about 2 to 10 kbp; the fragments were subcloned into a vector; the clones were sequenced; and the thus obtained sequences were ligated properly.  
     [0084] An EZ::TN&lt;KAN-2&gt; insertion kit enables random insertion of a transposon into a plasmid. By using primers specific to both ends of a transposon, sequence can be determined on the regions adjacent to the inserted transposon.  
     [0085] Then under the presence of both of template plasmid DNA and transposon, the transposon is inserted in by transposase, and  E. coli  is transformed by the plasmid DNA. Since kanamycin-resistance gene is encoded on the transposon, it is assumed that the transformants containing template plasmid containing the inserted transposon may exhibit resistance to kanamycin. Therefore, transformants of the purpose can be selected based on the kanamycin-resistance. The transformants containing the plasmid are cultivated, and the sequence was determined using the purified plasmid as a template. This method is appropriate for analyzing a DNA fragment having a length of about 2 to 10 kbp. Thus, the inventors confirmed overall sequences of the respective fragments obtained by restriction enzyme treatment of K1B10, and ligated these fragments.  
     [0086] (Acquisition of Cosmids Adjacent to K1B10)  
     [0087] The sequence data of the K1B10 revealed that both ends of its insert contained base sequences having high homologies with TDP-glucose synthase and glutamate mutase. These enzymes were likely to be involved in biosynthesis of vicenistatin, and it was expected that gene cluster involved in vicenistatin biosynthesis would be extended to outside of this region.  
     [0088] Thus, an attempt was made to obtain other cosmid clones having regions adjacent to the K1B10. Firstly, an attempt was made to obtain cosmids containing left region of the K1B10. Therefore, based on the base sequence of K1B10C1 existing left end of the K1B10C1 insert, specific PCR primers (K1B10-leftF, K1B10-leftR) were designed, and genomic library was screened again by PCR using these primers. Primary and secondary screenings were performed as above to obtain cosmid Y3D4. Furthermore, in the same manner with the left end, PCR primers designed for the right end of the cosmid K1B10 based on the base sequence of K1B10AS (K1B1O-rightF, K1B10-rightR), and they were used for screening and cosmid K7G3 was obtained. Further primers were designed based on the K7G3 and screened, and cosmid L6D5 was obtained.  
     Example 3  
     Homology Analysis of ORFs  
     [0089] Base sequence was determined on the approximately 60 bp region existing adjacent to the cosmid K1B10. When a base sequence is translated into amino acid sequence, six different frames can be given in total, that is, three frames for the forward direction and three frames for the reverse direction, respectively. In general, a prokaryote has a region of about 5 bp with abundant A (adenine) and G (guanine), existing about 10 bp upstream from the start codon, and this region is called Shine-Dalgarno (SD) sequence. It is known that ribosome binds to this region to initiate translation. Therefore, based on this knowledge, the inventors analyzed on ORFs encoding for amino acid sequences.  
     [0090] However, as to actinomycetes, it is known that the SD sequence does not necessarily exist in the organisms. Therefore, an alternative method is known, that is, the frame can be analyzed by calculating GC content in the frame. The chromosomal DNA of actynomycetes usually exhibits high GC content of 70% or more in the average. However, contents of amino acids corresponding to codons comprising only GC, namely arginine, glycine, proline and alanine, are not significantly higher compared with those of other prokaryotes. The third base of a triplet codon is not practically important to determine amino acid encoded by the codon, and GC content in the third base of the triplet codon is extremely high (90% or higher), while GC content for the second base is very low (about 50%) and that for the first base is about 70%. Moreover, as to region not translated to corresponding amino acid, such as promoter, GC content in the region is about 50%. For example, GC content is analyzed on the 5 kbp region existing left end of the K1B10 using a computer program of Frame Plot. As a result, four ORFs (orfA, orfB, orfC and orfP2) were revealed to exist in the region.  
     [0091] In the same manner, frame analysis was performed on the all regions to confirm existence of 18 ORFs. FIG. 1 shows a gene mapping obtained in the present experiment. Homology search was performed for the respective ORFs by public databases (BLAST), based on its putative amino acid sequence. Proteins revealed the highest homologies were listed in FIG. 2.  
     [0092] (Homology Analysis of orfA)  
     [0093] The orfA consisted of 1068 bp, and was estimated to represent a protein comprising 355 aa (amino acids, that is, the number of amino acid residues) having a molecular weight of about 38 kDa. The orfA corresponds with the vinA gene described above. As a result of the search through databases (BLAST), the protein encoded by the orfA exhibited 69% homology with MtmD (protein ID T48866: glucose-1-phosphate thymidylyl transferase), which is contained in gene cluster of  S. argillaceus,  and involved in biosynthesis of mithramycin. Moreover, the protein encoded by the orfA exhibited 67% homology with StrD (protein ID A26984: glucose-1-phosphate thymidylyl transferase) of  S. griseus  which is involved in biosynthesis of streptomycin. Besides, it exhibited high homologies with dTDP-glucose synthases of various secondary metabolites.  
     [0094] (Homology Analysis of orfB)  
     [0095] The orfB consisted of 972 bp, and was estimated to represent a protein comprising 323 aa having a molecular weight of about 36 kDa. The orfB corresponds with the vinB gene described above. As a result of database search, the protein encoded by the orfB exhibited high homology with dTDP-glucose-4,6-dehydratase of various Streptomyces species. This enzyme is involved in deoxygenation of a sugar at C-6.  
     [0096] The orfC consisted of 1260 bp, and was estimated to represent a protein comprising 419 aa having a molecular weight of about 46 kDa. The orfC corresponds with the vinC gene described above. As a result of database search, the protein encoded by the orfC exhibited high homology with various glycosyltransferases.  
     [0097] All of the proteins exhibited high homology with the orfC are glycosyltransferase of 2,6-deoxysugars involved in biosynthesis of antibiotics. It is known that these enzymes contain conserved amino acid sequences of DXD and LPXCXXhhHHGGXGXXXhAhbXGhPQbbP (where X represents an arbitrary amino acid residue and h represents a hydrophobic amino acid residue). The protein encoded by the orfC also contained these sequences, and from this it was estimated that the protein would be a glycosyltransferase of 2,6-deoxysugars. Furthermore, as the protein had high homology with glycosyltransferase of aminosugars (particularly among 2,6-deoxysugars), it was suggested that the protein serves as glycosyltransferase in the biosynthesis of vicenistatin.  
     [0098] (Homology Analysis of orfD)  
     [0099] The orfD consisted of 1482 bp, and was estimated to represent a protein comprising 493 aa having molecular weight of about 55 kDa. The orfD corresponds with the vinD gene described above. As a result of database search, the protein encoded by the orfD exhibited high homology with known dTDP-4-keto-6-deoxyglucose 2,3-dehydratase. For example, the protein exhibited 61% homology with SnogH (protein ID CAA12009: estimated 2,3-dehydratase) derived from  S. nogalater ).  
     [0100] (Homology Analysis of orfE)  
     [0101] The orfE consisted of 993 bp, and was estimated to represent a protein comprising 330 aa having molecular weight of about 36 kDa. The orfE corresponds with the vinE gene described above. As a result of database search, the protein encoded by the orfE exhibited high homology with known dTDP-4-keto-6-deoxyhexose 2,3-reductase, i.e. it exhibited 60% homology with TylCVI (protein ID AAD41821,  S. fradiae ). This enzyme is involved in reduction of sugar at C-3 position, and is believed to be also involved in the reduction of sugar at C-3 position in vicenistatin biosynthesis.  
     [0102] (Homology Analysis of orfF)  
     [0103] The orfF consisted of 1194 bp, and was estimated to represent a protein comprising 397 aa having molecular weight of about 43 kDa. The orfF corresponds with the vinF gene described above. As a result of database search, the protein encoded by the orfF exhibited high homology with aminotransferases involved in biosynthesis of various aminosugars. For example, the protein exhibited 48% homology with EryCIV (protein ID CAA72084) aminotransferase involved in biosynthesis of desosamine, which is an aminosugar constituting erythromycin produced by  Saccharopolyspora erythraea,  and exhibited 37% homology with VioA (protein ID AAD44154) involved in biosynthesis of 4-amino-2,6-dideoxyglucose produced by  E. coli.  From these facts it was estimated that the orfF is an enzyme participating in amino group introduction in vicenistatin biosynthesis.  
     [0104] (Homology Analysis of orfG)  
     [0105] The orfG consisted of 711 bp, and was estimated to represent a protein comprising 236 aa having molecular weight of about 26 kDa. The orfG corresponds with the vinG gene described above. As a result of database search, the protein encoded by the orfG exhibited 45% homology with methyltransferases utilizing S-adenosylmethionine as the methyl group donor, e.g., the protein exhibited 45% homology with methyltransferase AknX2 (protein ID AAF73460) from  S. gallilaeus,  and the protein exhibited 44% homology with methyltransferase EryCVI (protein ID CAA72082), which is involved in biosynthesis of desosamine and derived from  Saccharopolyspora erythraea.  From a study using labeled methionine, it is known that the N-methyl group of vicenisamine is derived from S-adenosylmethionine. From these observations, it was estimated that the protein encoded by the orfG is methyltransferase involved in vicenisamine biosynthesis.  
     [0106] (Homology Analysis of orfH and orfI)  
     [0107] The orfH consisted of 477 bp, and was estimated to represent a protein comprising 158 aa having molecular weight of about 17 kDa. The orfI consisted of 1410 bp, and was estimated to represent a protein comprising 469 aa having molecular weight of about 50 kDa. The orfH corresponds with the vinH gene described above while the orfI corresponds with the vinI gene described above. As a result of databases search, the protein encoded by the orfH exhibited high homology with S-subunit of glutamate mutase, while the protein encoded by the orfI exhibited high homology with E-subunit of glutamate mutase. Glutaminate mutase is a unique enzyme in that it isomerises glutamate into 3-methylaspartate utilizing vitamin B12 (adenosylcobalamin) as a coenzyme.  
     [0108] X-ray crystallographic analysis on site-directed mutated enzymes was performed on GlmE, S (accession number, X80997) of  Clostridium cochlearium.  The study revealed that His16 of the S-subunit serves as a binding site for the coenzyme, and that Glu171 of the E-subunit serves to recognize the amino group of glutamic acid. In addition, these amino acids are preserved in the protein encoded by the orfI. It has been known that glutamate and 3-methylaspartate are produced as intermediates in vicenistatin biosynthesis, as described above. This suggests that the proteins encoded by the orfH and orfI may catalyze the aforementioned reaction.  
     [0109] (Homology Analysis of orfJ) The orfJ consisted of 900 bp, and was estimated to represent a protein comprising 299 aa having molecular weight of about 34 kDa. The orfJ corresponds with the vinJ gene described above. As a result of database search, the protein encoded by the orfJ exhibited 54% homology with proline iminopeptidase from  Mesorhizobium loti.  Besides, it exhibited high homology with proline iminopeptidase from various microorganisms. Contribution of orfJ in vicenistatin biosynthesis could not be predicted only from the homology analysis. However, generally in microorganisms, genes coding for microbial secondary metabolites form a cluster, and thus it seemed possible that this protein might be involved in the biosynthesis of vicenistatin in some way. Gene disruption experiment of the orfJ will be requisite to elucidate the function of this protein in vicenistatin biosynthesis.  
     [0110] (Homology analysis of orfK)  
     [0111] The orfK consisted of 984 bp, and was estimated to represent a protein comprising 327 aa having molecular weight of about 36 kDa. The orfK corresponds with the vinK gene described above. As a result of database search, the protein encoded by orfK exhibited homology with acyl CoA-ACP (acyl carrier protein) transacylase of type-II fatty acid synthases derive from various species. When an amino acid serving as a starter unit in the biosynthesis of vicenistatin is incorporated into a polyketide synthase (PKS), this enzyme is considered to catalyze conversion of the CoA derivatives of amino acids into the corresponding ACP derivatives.  
     [0112] (Homology Analysis of orfL)  
     [0113] The orfL consisted of 249 bp, and was estimated to represent a protein comprising 82 aa having molecular weight of about 9.6 kDa. The orfL corresponds with the vinL gene described above. As a result of databases search, the protein encoded by the orfL exhibited homology with known ACP. This protein is considered to serve as an ACP to which a glutamate derivative binds, when the derivative is captured by PKS.  
     [0114] (Homology Analysis of orfM)  
     [0115] The orfM consisted of 1575 bp, and was estimated to represent a protein comprising 524 aa having molecular weight of about 56 kDa. The orfM corresponds with the vinM gene described above. As a result of database search, the protein encoded by orfM exhibited homology with adenylation domain A (A domain) of type I non-ribosomal peptide synthetase. It was considered that the protein could be involved in activation of amino acids in vicenistatin biosynthesis, that is, in isomerization of the amino acid at biosynthesis of the starter unit or in the formation of macrolactam. If the function of this enzyme is elucidated through further study utilizing gene disruption experiments and overexpression of the enzyme, it will provide interesting results.  
     [0116] (Homology Analysis of orfN)  
     [0117] The orfN consisted of 1437 bp, and was estimated to represent a protein comprising 478 aa having a molecular weight of about 52 kDa. The orfN corresponds with the vinN gene described above. As a result of database search, the protein encoded by the orfN was found to have homology with some CoA ligases, i.e., it exhibited 33% homology with estimated long chain fatty acid CoA ligase from  Sinorhizobium meliloti,  that is, SMb20650 (protein ID CAC49758). On the basis of a study using a labeled starter unit, it is believed that when 3-methylaspartic acid is captured by PKS, it undergoes decarboxylation and isomerization. The capture by PKS may involve the following steps: 3-methylaspartic acid is converted by CoA ligase into a CoA derivative which is then converted into an ACP derivative by the protein encoded by the orfK; and the ACP derivative is captured by PKS.  
     [0118] (Homology Analysis of orfO)  
     [0119] The orfO consisted of 1245 bp, and was estimated to represent a protein comprising 414 aa. The orfO corresponds with the vinO gene described above. As a result of database search, the protein encoded by the orfO was found to have a homology with decarboxylase utilized as a coenzyme pyridoxal-5′-phosphate, PLP. It had a highest homology (identity 31%, positive 51%) with BtrK (protein ID BAB18473,  Bacillus circulans ), which had been suggested to be involved in the biosynthesis of butirosin. Besides, the protein exhibited homology with diaminopimelate decarboxylase and ornithine decarboxylase, which had been believed to be involved in the primary metabolism. It was estimated from the level of homology that the protein encoded by the orfO is decarboxylase involved in the biosynthesis of secondary metabolites, but is rather different from decarboxylase involved in the primary metabolites. From the above results, it is suggested that the protein encoded by orfO may catalyze the expected decarboxylation of a starter unit in vicenistatin biosynthesis.  
     [0120] (Homology Analysis of orfs P1, P2, P3 and P4)  
     [0121] As a result homology analysis by database search, the proteins encoded by orfs P1, P2, P3 and P4 exhibited homology with type I PKSs. The orfs P1, P2, P3 and P4 correspond to previously described vinP1, vinP2, vinP3 and vinP4 genes, respectively. The amino acid sequences of the proteins were compared with other PKSs, and it was estimated that the orfP1 is comprised from three modules, orfP2 one module, orfP3 two modules, and orfP4 two modules.  
     [0122] Among functional domains of PKS, it is known that sequence analysis of AT domain enables to determine whether the extension unit is acetate or propionate. In malonyltransferase (MT) utilizing acetate as the extension unit, two motifs of XYAQXXXXXXQXAL and GHSI (where X represents an arbitrarily chosen amino acid residue) are preserved adjacent to its active site. On the other hand, in methylmalonyltransferase (MMT) utilizing propionate as the extension unit, two motifs of VDVVQXXXXXXMXSLA and GHSQ exist adjacent to the active site. The AT domains of the modules contained in the orfP1 included MT, MT and MMT, that in the orfP2 included MMT, those in the orfP3 included MT and MMT, and those in the orfP4 included MT and MT, in this order.  
     [0123] Assuming that the orfs P1, P2, P3 and P4 are extended in the order to exert their enzymatic action, the sequential order of the functional domain in the respective modules coincides with carbon backbone constituting aglycon of vicenistatin. Ultimately, the polyketide may be released from the enzyme by thioesterase (TE) domain existing on the OrfP4 to be converted into a ring (FIG. 3). This strongly suggests that the PKS genes concerned here are those responsible for the biosynthesis of vicenistatin. FIG. 4 summarizes the reactions catalyzed by the enzymes encoded by respective vin genes.  
     [0124] The base sequence analysis suggested that the proteins represented by orfs A, B, D, E, F and G are involved in the biosynthesis of vicenisamine, and that orfC encodes glycosyltransferase for deoxysugars. In addition, it suggested that the proteins represented by orfs H, I, K, L, N, O, P1, P2, P3, and P4 are involved in the biosynthesis of aglycon of vicenistatin. It was expected that these enzymes serve in this sequential order for biosynthesis of vicenistatin. Based on these observations, it was strongly suggested that the genes obtained through the above study should be responsible for the biosynthesis of vicenistatin. The predicted pathway of vicenistatin biosynthesis is summarized in the scheme shown in FIG. 4.  
     [0125] The proteins represented by 18 ORFs identified in this study did not include that possibly serving as isomerase for 3-methylaspartate, but any one enzyme bearing the activity may serve as an isomerase. Alternatively, the proteins represented by the Orf M and Orf J whose function could not be identified in this study might be involved in this function. Otherwise, the ORF concerned for this reaction might exist outside of the region analysed in this study.  
     Example 4  
     Expression of vinC by Recombinant  E. coli    
     [0126] VinC was amplified from the cosmid K1B10 by PCR using two oligonucleotids (oligo EXPRESS SELECT), that is, vinC-N term (5′-AAGGTACCATATGCGCGTCCTGATGA-3′) and vinC-C term (5′-CCCGGATCCGCTGGGCGGAGTGCTAC-3′). The NdeI and BamHI sites inserted into the oligonucleotides are underlined. The used DNA polymerase was Takara Ex-Taq (Takara). The PCR conditions consisted of 30 cycles with a cycle of 95° C. for 7 minutes, 95° C. 30 for seconds, 56° C. for 30 seconds, and 72° C. for 90 seconds, followed by 72° C. for 7 minutes.  
     [0127] The PCR product was cloned into pT7Blue T vector; the sequence of the clones was confirmed and clones containing proper sequence were selected. VinC was cloned using NdeI and BamHI sites and cloned into pET30b(+) to produce pET-vinC. The obtained pET-vinC was used to transform  E. coli  BL21 (DE3), to produce recombinant  E. coli  cells for expression of vinC. The recombinant E. coli cells thus obtained were designated as BL21(DE3)/pETvinC. The procedures for conventional gene manipulation was performed in accordance with the description of “Molecular Cloning” written by Joseph Sambrook and David W. Russell, Cold Spring Harbor Laboratory Press.  
     Example 5  
     Confirmation on Enzymatic Activity of the Recombinant VinC  
     [0128] A cell-free extract was prepared from the cells of  E. coli  obtained as described for VinC expression and it was used as a crude enzyme solution. Then glycosyltransferase activity of the enzyme solution was confirmed using dTDP-vicenisamine as a substrate. The method to produce starting materials used in the enzyme reaction, and the result of the enzymatic activity will be described below. FIG. 5 shows the scheme for synthesis of dTDP-vicenisamine, dTDP-2-mycarose, and dTDP-2-deoxyglucose, used as substrates of the enzymatic reactions.  
     [0129] (Preparation of dTDP-Na Salt)  
     [0130] Sodium salt of dTDP (100 mg) was dissolved in cold water, and the solution was passed through a column filled with H +  type DOWEX AG-50 X8. Into the fraction containing the target substance having pH of 1 to 2, an aqueous solution of 4% tetrabutylammonium hydroxide (Bu 4 N—OH) was added until the pH reached to 5 to 6. The solution was freeze-dried and a white crystalline substance was obtained.  
     [0131] (Synthesis of dTDP-vicenisamine)  
     [0132] The synthesized compound (1) (41.5 mg, 1.41×10 −4  mol) was dissolved into 2 ml of CH 2 Cl 2 , and the solution was transferred into a bath containing acetone-dry ice and kept at −10° C. Into the solution, Et 3 N (0.392 ml, 2.81×10 −3  mol, 20 mol eq.) was added, and then TMS-Cl (0.213 ml, 1.68×10 −3  mol, 12 mol eq.) was added. After stirring for 30 min, 0.4 ml of Et 3 N and 0.2 ml of TMS-Cl were added. After another 30 min stirring, 0.2 ml of Et 3 N and 0.1 ml of TMS-Cl were further added to the mixture. After stirring for 1.8 hour, the solution was concentrated with an evaporator.  
     [0133] To the residue, a solution of pentane/ethyl acetate (EA)=4 was added; the resulting solution was filtered and concentrated; and benzene was added to the solution followed by azeotropic evaporation, to give a solid. Then 1.2 ml of CH 2 Cl 2  was added to the solid and it was kept at −78° C., to which was added TMS-I (0.026 ml, 1.83× −4  mol, 1.3 mol eq.). Forty-five minutes later, the resultant was added to a mixture containing dTDP-Bu 4 N salt and 20 μl of diisopropylethylamine (DIEA) dissolved in 1.5 ml of CH 2 Cl 2 .  
     [0134] The solution was stirred for 1.5 hour, and then its temperature was gradually raised. After 1.3 hour, 120 μl of tetrabutylammonium fluoride (TBAF) was added to the solution. After 55 min of stirring, the solution was concentrated, and the concentrate was purified by reverse phase silica gel chromatography (water:methanol=1:1-&gt;1:5) to yield 103 mg of partially-purified sample. A solution of water:methanol=1:1 (7 ml in total) was added to the sample. To the solution, it was added with 11.3 mg of Pd/C, and the whole was subjected to hydrogenolysis in hydrogen atmosphere. After the reaction was completed, the mixture was filtered and concentrated. The concentrate was purified with a DEAE Sephadex column A-25 equillibated with 30 ml of NH 4 HCO 3  solution to yield 13.2 mg (two steps, 16%) of dTDP-vicenisamine diammonium salt (compound (3)) in the form of white powder.  
     [0135] MS data: [C 17 H 29 N 3 O 3 P 2 -H]-, and calculated MW: 544.11, measured MW: 544.2 (base peak)  
     [0136] Synthesis of ADP-vicenisamine and UDP-vicenisamine was performed by the process according to the procedure described above.  
     [0137] (Synthesis of dTDP-mycarose)  
     [0138] The compound (4) (46.4 mg, 2.86×10 −4  mol) was added to 1 ml of pyridine, and the mixture was kept at 0° C., to which was added TMS-Cl (0.8 ml, 22 mol eq). After 11.5 hours, 7 ml of pentane was added, and cold water was added and then separated. It was washed until the residual pyridine becomes less than detection limit by TLC. The supernatant was concentrated, and the residue was used for further operation. The crude product (compound (5)) was dissolved in 1 ml of CH 2 Cl 2 , and the solution was kept at −78° C. Then, TMS-I (0.0529 ml, 1.3 mol eq.) was added thereto, and 45 minutes later, a mixture solution of dTDP-Bu 4 N salt and 40 μl of DIEA dissolved in CH 2 Cl 2  was added to it. After stirring for three hours, 480 μl of TBAF was added thereto, and the mixture was concentrated 40 minutes later. The concentrate was purified via DEAE-Sephadex as above to yield 21.5 mg of dTDP-mycarose (compound (6)).  
     [0139] (Synthesis of dTDP Derivative of 2-deoxyglucose)  
     [0140] 2-Deoxyglucose (7)(31.3 mg, 1.91×10 −4  mol) was dissolved into 1 ml of pyridine, to which was added TMS-Cl (0.5 ml, 3.94×10 −3  mol, 20 mol eq.) at room temperature. After 1.5 hour, 5 ml of pentane was added, then cold water was added and separated. The supernatant was concentrated, and the concentrate was subjected to azeotropic treatment with benzene to afford a TMS derivative (compound (8)).  
     [0141] To this crude product was added 1 ml of CH 2 Cl 2 , and the mixture was cooled to −78° C. Then, TMS-I (0.3 ml, 2.48×10 −4 , 1.3 mol eq.) was added. Forty minutes later, a mixture (which was obtained by dissolving dTDP-Bu 4 N salt and 40 μl of DIEA in CH 2 Cl 2 ) was added. The temperature of the solution was gradually raised, and after stirring for 3.4 hours, 0.1 ml of TBAF was added to the solution. After additional stirring for fifty minutes, the solution was concentrated, and the concentrate was purified by DEAE Sephadex A-25 column.  
     [0142] (Enzyme Reaction)  
     [0143] The above-mentioned recombinant  E. coli  BL21(DE3)/pETvinC was used for pre-culture on 4 ml of LB medium containing kanamycin. Then, a mixture comprising 100 ml of LB medium, 30 μg/ml of kanamycin and 1 ml of the pre-culture was prepared and was incubated for two hours at 37° C. under shaking with 220 rpm. The cultivation continued until OD600 reached to about 0.6. IPTG was added to the culture until the concentration reached to 0.2 mM. The culture was further incubated at 37° C. for about three hours under shaking with 180 rpm. About 400 mg of the recombinant  E. coli  cells were collected, and a buffer (comprising 50 mM tris-HCl, pH 7.5; 1 mM, MnCl 2 ; 1 mM, MgCl 2 ) was added to the cell pellet, at such a volume corresponding to 10 times as much as that of the cell pellet (4 ml of buffer to 400 mg of cell pellet). The cell suspension was sonicated 10 times for two minutes to disrupt the cells. The resultant solution was centrifuged at 12,000 rpm for 30 minutes. The supernatant (cell-free extract) was collected and used as a crude enzyme solution.  
     [0144] A 14 μl of dTDP-vicenisamine dissolved in distilled water (3.3 mg/700 μl) and 3.6 μl of aglycon (saturated solution in DMSO) were transferred into an Eppendorf tube in an ice bath, and 100 μl of the crude enzyme solution was added thereto, and the mixture was stirred to allow the enzyme reaction to proceed. Twenty-four hours later, distilled EA and 2N NaOH were added to adjust pH of the solution at pH10 or higher. Then, the solution was extracted with ethyl acetate. The extracted supernatant was concentrated with an evaporator, and 30 μl of methanol was added thereto. In the same manner, dTDP-mycarose and dTDP-2-deoxyglucose were allowed to react separately with the aglycon.  
     [0145] The reaction product was detected with an LC-MS equipment (LCQ type, Finnigan) connected with a HPLC system equipping ODS column (Mightysil RP-18 GP, Kanto Kagaku). The reaction product was detected by UV 254 nm, and its structure was simultaneously analyzed by mass spectrometry. As a result, it was confirmed that the reaction between dTDP-vicenisamine and the aglycon in the presence of the enzyme underwent glycosyl transfer reaction to produce vicenistatin.  
     [0146] Mass spectral data: [M+H] + ; calculated MW: 501.36; measured MW: 501.2  
     [0147] In the same manner, glycosyl transfer reaction between dTDP-mycarose and vicenistatin aglycon was also confirmed.  
     [0148] Mass spectral data: [M+H] + ; calculated MW: 502.35; measured MW: 502.3  
     [0149] Moreover, glycosyl transfer reaction between dTDP-2-deoxyglucose and vicenistatin aglycon was also confirmed.  
     [0150] Mass spectral data: [M+H] + ; calculated MW: 504.32; measured MW: 504.1  
     [0151] These results suggested that the recombinant VinC enzyme produced by the recombinant  E. coli  exhibited enzymatic activity as a glycosyltransferase. Therefore, it was confirmed that the VinC enzyme derived from the vicenistatin biosynthetic gene cluster plays a role as a glycosyltransferase.  
     [0152] This invention provides base sequence of the vin gene cluster, which is a cluster of genes encoding an enzyme complex catalyzing biosynthesis of vicenistatin. This invention further provides a transferase (VinC enzyme), which catalyzes synthesis of vicenistatin using dTDP-vicenisamine as a substrate, as well as a gene (vinC gene) encoding the enzyme. The VinC enzyme is useful for enzymatic synthesis of vicenistatin, which is a valuable compound. It is further suggested that use of the VinC enzyme may be useful for synthesis of novel polyketide glycosides.  
    
     
       
         1 
         
           
             26  
           
           
             1  
             64492  
             DNA  
             Streptomyces halstedii sp.HC-34  
           
            1 

agatctggtg aatccgatgg gcctcgggct gccggagcgt gcgggactcc agctcgctct     60 

cgcccggcag taatgcgtcc actgtgacga tttcagcgat atgcgcggct tgatcggcgg    120 

gcaggggcac gctccggaag agctgatcca ccacgccgag ttgtagctca cgctctgcct    180 

tggccccggt cgccgcgaga tgcagcgcgc ccgagtcgag agcgtggtgt gacagtgcct    240 

ccaggagggc agtcttgccg gaggctatgg cgccactgat cagtacggct ctcccgtgcc    300 

cccgggtggc gtcacccagc aaccctccca aggcgtgcag ttcctcgtcg cgttccacga    360 

acaccatcgt cgcaaccctc tccccgttca gatgtcgcgt acgtacgtat gaatatatcg    420 

catgccactt gccgggtgaa tataaatttt actttactta cggattactt gcgctctgtc    480 

gtgtcgtcat ggcaagggcg ctcacccttc aacgtaggtg ctacgggccg acataggggc    540 

cgccccgggc cgattagggg ttatcccggc cggggccccc gagtaaaaat gctgtcgccg    600 

gaccgcggaa aaattcacgg cggcgacgcg acccccaacg gcgtgtcccc gctcctgcgg    660 

gtatctctcc agccggctag acctaggggg ttgggtgaaa gcgctcgttt tgtctggcgg    720 

atccggtaca cggctccgac cgatcacaca cacatcagcc aaacaactgg tgcccgttgc    780 

gaacaagccc atcctgttct acgtcctgga gtcgatcgcc gaagcgggca tcaccgacgt    840 

tggcatcgtt gtcggacaca ccgctccgga ggtccaggac gcggtcggtg acggctccgc    900 

cttcggggtg gacgtcacct acatcgccca ggacgagccg ctcggcctcg cccacgcggt    960 

ccgcatctcc cgcgactacc tcggtgatga cgactttgtc atgttcctcg gtgacaactt   1020 

catcatcgac ggcgtcaccg gacttgtcga ccgcttccgt gatgagcgcc ccgacgcgca   1080 

gatcctgctg acccgggtcc ccgacccccg ggccttcggc gtcgccgtcc tcgacgaaca   1140 

gggccgcgtc atcggcctgg aggagaagcc agaacacccc cgcagcgatc tggcgctcgc   1200 

cggcgtctac ttcttcaccc ccctcatcca cgaggccgtc tgggccgtca aaccctcctg   1260 

gcgcggcgaa ctggagatca ctgactccat ccagcacctc atcgacaccg gagccgacgt   1320 

ccgctcccac atcatcgacg ggtactggaa ggacaccggg aacgtcgtcg acatcctgga   1380 

ggtcaaccgc atcatcctgg agagcgtcga gaccgccatc gacggcgacg tcgacgcgga   1440 

ctccgagatc atcggccggg tcgtcatcga gaagggcgcc accgtcaagg gctcgcggat   1500 

cgtgggcccc gccctcatcg ccaccggaac cgagatccgc gactcctacg tcggaccctt   1560 

cacctccgtc gccgagaact gtcgcatcca cgacagcgaa ctggagttct ccatcatgat   1620 

gcgggactcg tccctcaccg gcatccgccg catcgaggcg tcgctcatcg gccgccatgt   1680 

ccacggcacc gccgtacccc gcgtacccaa cgcccaccgg ctcgtcctcg gcgaccacag   1740 

caccttccag atcagctcat gagcacccga ctgctcgtca cgggcgccgc cggattcatc   1800 

ggatcggcct acgtccgcgg actcctcacc gaccagcccg acctgcgggt caccgtcctc   1860 

gacagcctca cctacgcggg caaccgggcc aacctcgacc tgacacaccc ctccctcgac   1920 

ctcgtcgagg gtgacatctg cgacaccgag ctcgtggacc gcctcaccgc cgaagccgac   1980 

cagatcgtcc acttcgccgc cgagagccac gtcgaccggt ccatcaccgg ctccgccgag   2040 

ttcatccgca ccaacgtcct cggcacccac accctcctcg acgccgcgct ccgccacggc   2100 

atcgaccggt tcgtccacat ctccacggac gaggtctacg gatcgatcga gaagggctcc   2160 

tggccggaga ccgacccgct gcgccccaac tccccctact cggcgtccaa ggcatccagc   2220 

gacctcctgg cgctcgccta ccaccggacc cacgggctcg acgtacgggt cacccgttgc   2280 

tccaacaact atggccccta ccagcatccc gagaaggtca tcccgctctt cgtcaccaac   2340 

ctcctcgacg gcaagcgggt acccctgtac ggggacggcc agaacgtccg cgactggctg   2400 

cacgtcgagg accactgcgc cgccatcgaa tgcgtccgca cccgcggtgg cgccggggag   2460 

atctacaaca tcggcggcgg caccgaactg agcaaccggg aactcaccgg cctgctcctg   2520 

gaggcgtgcg gggcggactg ggacagcgtg gagtacgtca ccgaccgcaa gggccacgac   2580 

ctgcgctact ccgtcgactg gtccaaggtc gccgacctcg gctacacccc cgcccacgac   2640 

ttccgtgccg ggctcgcgga gaccgtcgac tggtaccgct ccaaccgcac ctggtgggaa   2700 

ccggcgaagt acggccacag ccccgcctga ccggccctac cgccggccga cactcccaca   2760 

cccgcacctt cgctcggaga agaaacccca tgcgcgtcct gatgacggtg ttcgccaacc   2820 

gctcccacct ctacaacatg gtgcccctcg cctgggccct gaccaccgcg ggccacgagg   2880 

tccacatcgc cagccacccc gacaacgtgc aggcgatcag cgacagcggc ctcaccgccg   2940 

tacccgtcgg caacgacctc aacatcatgg cgctggcgca gtccaccccg cgcgaggaga   3000 

tggtcaacgg cggcgcgctc accctcaacg agacccggcc cgagaagctg acctggcagt   3060 

acatccacga cgtgttcgcg cagtactccc agatatacga gtacatggcg gactcgacca   3120 

tgaccgccga cctggtcgcc cacgcccgcc agtggcagcc cgacctcgtc atctgggacg   3180 

ccctcaccta cgccggcccc atcgccgccg aagccgtcgg cgcaccgcac gtccggatgc   3240 

tcttcggcct cgaccagtgg ggccggatgc gcgaccactt caaccggctc accggggaac   3300 

gcgccgccga cgaccgccac gacccgctcg ccgactggct cgcaaccaag ggcgagccgc   3360 

acggagtggc cttcaccgaa tccctcgtca ccggcacgac caccctcgcg gtcgccccgc   3420 

cgtggatgtc gttccccagc gagcagcccg ccctctccat gcggcacctc cccttcaacg   3480 

ggcccgccgt gctccccgac tggctccgcg aggcccccag caggccgcgc gtctgcctca   3540 

ccctcgggct gaccctgcgt gaactcgccg acgacaacgt caccctcgcc gacttcgtca   3600 

acgccgtcgc cgacatcgac gccgacgtcg tggcgacctt ctccgcggaa caggtcgccg   3660 

agatcggcga cctgcccgac aacgtccgcg cggtggactt cgtaccccta cacgccctgc   3720 

tgccgagctg cgccgcgatc gtccaccacg gcggcggcgg cacccgcacc aacgccatcc   3780 

ggtacggggt gccccagctg atcgtcccca actggctctg ggacgagggg tatgtggccg   3840 

agcgcttcgc cgagcgtggc gcggcactcg tcaccgaggt ccccgacctc acccccgacc   3900 

ggctgcgcga ccagctccgc aggctcatcg ccgagccgtc cttcaaggcg gcggcggagc   3960 

agatccagaa ggagtacgac gcgctgccca gcctcaccga gaccgtcggt gagctggtgc   4020 

gcgtcgcgga gcgcgggcgc tccctgtagc actccgccca gcggtacggg gggccgctgg   4080 

gcggcccgcc gtaccgaggg cgtgacccgt atcgattcgg ccatccttgg cgcggcagac   4140 

ccctgccggt ccgctccggg caaccccgag acggggatgg tcctctaagg gggcgtaggg   4200 

gttggcggcc cccacccctg cccccgtagc gtgggaatcg ttcaggctcg ctggcgattg   4260 

tccaatcaaa tagttaagcc cgtagattcc atcgagcctt ttcgagaact gcgggttcgc   4320 

tttgtcgtgc tctccgcacc cgaatcatcg ggtgcccagc agagttccga cagccgctca   4380 

ttcaaccgaa cccgtttcac gaggtgatgg cgtggagaac gaaaagaaac ttctcgatta   4440 

cctcaagcgg gctaccacgg acctacgtga agcacgccgc cgcctccgcg agatggagga   4500 

aaaggaccag gagcccatcg ccatcgtcgg catcggctgc cgctttcccc gcggtgtcga   4560 

gtcggcggag cagctctggg acctcgtcgc cgatggcggc gaggcgctca ccccgttccc   4620 

cgaggaccgg ggctgggaca ccgacagcct gtaccacccc gacccggagc acctgggcac   4680 

cagctacacc aacgtcgggg ccttcctgca cgacgccgcc gagttcgacc ccggcttctt   4740 

cgggatctcg ccgcgcgagg ccctcgccat ggacccgcag cagcgactgc tgcttgagac   4800 

gtcctgggag gccatggagc gggcgggcat cgacccggcc ggcctgcgcg gcagccgcac   4860 

cggtgtcttc acgggtctga tgtacttcga ctacgggtcc cgggtgcact ccgcccccga   4920 

ggacatcgag ggctacctcg gcaacggcag cgcgggcagc atcgcgtccg gccgggtcgc   4980 

ctacaccttc ggcttcgagg gccccgccgt cacactcgac accgcctgct cgtcgtccct   5040 

ggtcgccatc cacctcgccg cgcagtccct gcgcaagggc gagtgcaccc tggcgctggc   5100 

cggtggcgcg tcggtgatgt cgacgccgga catcttcgtt gacttcagcc gccagcgggg   5160 

tctgtccgcc gacggccggt gcaaggcgtt ctcgtccgac gcggacggta cgggctgggg   5220 

cgagggcgtc ggtgtcctgc tgctggagcg gttgtcggac gcgcggaaga acgggcaccg   5280 

gatcctgggc ctggtacgcg gctccgccgt caaccaggac ggcgccagca gcggtctgac   5340 

ggcgccgaac ggtccttcgc agcagcgggt gatccgccag gcgctggcca acgccggtct   5400 

gtcggccgcc gaggtggacg cggtcgaggc gcacggtacg ggtacgaagc tgggtgaccc   5460 

gatcgaggcg caggcgctgc tggcgaccta cggccaggag cgggaagagg gccggccgct   5520 

ctggctcggt tcgatcaagt cgaatgtggg tcacacgcag gctgccgcgg gtgtcgccgg   5580 

tgtgatcaag atggtgctcg cgatgcgggc cggtgtgctg ccgaagacgc tgcatgtgtc   5640 

ggagccgtcg ccgcacgtgg actggtccgc cggcgcggtg gaactgctga cggagacgcg   5700 

cgactggccg gagaccggcc gtccgcgccg cgccggtgtg tcgtcgttcg gtatcagtgg   5760 

cacgaacgcg cacgtcatcg tggagcaggc gcccatggac gaggcgatgg acgaggtggc   5820 

cggcgagcgg gagacccctg ccgcggggtc ggaccggacc gtcccgtggg tcatatcggc   5880 

gaagtccgcc gacgcgctcc gcgcacaggc cggacggctg agcaccttcc tcgccgggac   5940 

cgagggaact ctgactactg gtatttcttc cgaaacttct gtggccgctg tttcagcgga   6000 

tgcgtccgcg gttggttggt cgttggtgcg gggtcgttcg gtgttcgcgc atcgggcggt   6060 

tgtggtgggt ggtgagtggg acgcgctgct ggcgagtatc ggtgaactgg ccgatggcgc   6120 

cgaggatggt tccggtgctg cctctggttc tgttgtgtcg ggtgtggcgg atgtgtcggg   6180 

gcgtcgggtg tttgtgttcc cggggcaggg ttcgcagtgg gttggtatgg cgcaggggtt   6240 

gttggattcg tcggtgatgt tcacggagcg gatgacggag tgtgctgcgg cgttggatcc   6300 

gttggtggag tggtcgttgt tggatgtggt gcggggtgtg gagggtgcgg cgtcgttgga   6360 

gcgggtggat gtggtgcagc cggtgttgtg ggcggtgatg gtgtcgttgg cgtcggtgtg   6420 

gcgttcggtg ggtgtggtgc cggatgcggt ggtgggtcat tcgcagggtg agatcgcggc   6480 

tgctgtggtg ggtggttggt tgtcgttggt ggatggtgcg cgggtggtgg cgttgcggtc   6540 

gttggcgatt cgtgaggtgt tggcgggtgg tggtggcatg gtcgcggtcc aggctgcgga   6600 

ggatgaggtt gctgggtggc ttgagggtgt ggagggggtg gggattgctg cggtgaatgg   6660 

tccgcgttcg gtggtgatct cgggtacgcg tgcgggtttg gatgcgtgtg tggagttgtg   6720 

gtctgggcgg gggacgtggg tgaagcgggt tccggtggac tatgcctcgc attcggctga   6780 

ggtggagcgg gtgcgtgagc gggtgctggc ggatctggcg agtgtgacgg gtttgtcggg   6840 

gtcggtgccg atgttgtcga cgatgacggg tgactggatt gttgagggtc aggttggggc   6900 

cgggtattgg gtggagaatc tgcgtcgtcc ggtgttgttc gcggacgcga cgaggcggtt   6960 

ggcgtcggag ggtttcggcg cgttcgttga ggtgagtgcg catccggtcc tggtcatggg   7020 

catcgaggag acgatcgagg cgctgaggtc gggtgccgcc gatggtgcga agtccggtgc   7080 

tggtgaggag agttcctccg ctgtggtggc ggtggggacg ttgcgtcgtg gtgagggtgg   7140 

ttgggatcag ttcctgcgtt ccctcgcggg gctcttcgtc cggggtgcgg tgacaccgga   7200 

ttgggagtcg ttgttgggtg gtgtgcgtcc tcgggttgat ttgccgacgt atgcgttcca   7260 

gcgtgagcgg ttgtggctgg atgcgggtgt ggtggcgggg gatgtgtcgg ggttgggtca   7320 

ggtggtggtg ggtcatccgt tgttgggtgc tggtgtgggt gttgctggtg agggtggggg   7380 

tgtgttgttt acgggtcgtt tggggttggg ttcgcatccg tggctgggtg atcatgcggt   7440 

gtcgggtgtg gtgttgttgc cgggggctgc gtttgtggag ttggtggtgc gtgcgggtga   7500 

tgaggtgggg tgtggtcggt tggaggagtt gacgttggcg gctccgttgg tggtgccgga   7560 

gcgtggttcg gtgcggattc aggtggtggt gggtgctggt gatgggtcgg gtgcgcgttc   7620 

ggtgggtgtg tggtcgtcgg tgggggatga gggtgtgggt ggggagtggg tgtgtcatgc   7680 

gtcgggtttg ttgacggctg atgtgggtgt ggcgccggtg ttgggtggtg tgtggccgcc   7740 

ggtgggtggt gtggcggtgg atgtgtcggg tgtgtatgag gggttggcgt tggaggggta   7800 

tgagtatggg tcggtgtttc gggggttgag gtcggtgtgg cgtcgtgggg atgaggtttt   7860 

tgctgaggtg gcgttgggtg agggtgtggg ggtggagggg tttggtttgc atccggcgtt   7920 

gttggatgcg gcgttgcagg ctgctgggtt tggttcgttt gtgccggagt ccgaggcagg   7980 

gtctgaggcg ggttcgggtg gggtgcggtt gccgttctcg tggtcgggtg tgtcgttgtt   8040 

tgcgtcgggt gcttcggtgg ggcgggtgcg gttgtggccg gtgggtgggg atggttttgg   8100 

tgtggagttg tttgatgggg tggggatgcc ggtggcgcgg gtggatgcgt tggtgacgcg   8160 

ggagattagt gcgggtcagt tgggtgcggc tgctggtgcc gggtcgttgg tgggtgggga   8220 

gtcgttgttc cgggtggagt gggctcctgt gtcgggtgtt gcaccggctt ctgctggtgt   8280 

gggtggttgt gtggtggtgg gtgcggggag tgtgttgtct ggttttgggg aggtggttcc   8340 

ggatctggcg gcggtttccg cgggttctgc ggctgtgccg gggtgggtgt tggtggatgt   8400 

ggatgcgtgg ttgggtgcgg atctggcggt gggtgtggtg tcgggtgagg gtgttccggt   8460 

ggtggcgcgt ggtgtggtgg cgcgggtgtt ggggttggtg cgggagtggt tgggggatga   8520 

gcggtgggtg tcgtcgcggt tggtgtgggt gacgcgtggt gcggtgggtg ctcgggtgtt   8580 

ggatgaggtg tcgggtgtgg tgtcgtcggg gttgtggggg ttggtgcggg ctgctcagtc   8640 

ggagcatccg gaccggttcg cgcttcttga tctggacagt gccaccgccg tggatgccgt   8700 

tcgtgatggt gtgttggggt tgttggctgc tggtgagccg cagttggtgg tgcgtgaggg   8760 

tgaggtgctg gccgcacggc tgacccccgc ccacaccacc gacgccctga tccccctcgc   8820 

cgaccacgcc ccgtggcgcc tcgccaagga ccccggtggc agccttgacg cgctgacggt   8880 

cgtcccggcc cccgacgtac tggagccgct caccgaggga caggtccgca tcgcggtccg   8940 

cgccgccggg gtgaacttcc gtgacgtact catggcactc ggcatggtcc ccgcccgggg   9000 

tacccagctc ggtggcgagg ccgccggcgt cgtgaccgct gtcggccctg gagtcaccgg   9060 

gatcgccgtc ggcgaccgcg tgatgggcgt cttcgacggc ccgttcggcc cggtggccgt   9120 

cgcggatcgg cgcatggtct cccgtatccc cgatgcctgg tcgtacaccg aggccgcgac   9180 

gatcccgctg gtgtacctca ccgcgtacta cggactggtg gacctcgccg ctctccagca   9240 

gggacagcgc atcctggtgc acgccgccac cggtggcgtg ggcatggcag cggtccagct   9300 

cgcccgccac ttcggcgccg aggtgtacgg cacggccagc cccggcaagt gggacaccct   9360 

gcgcgcgatg ggattcgacg aggcgcatat ggcctcctcg cggtccctcg acttcgagga   9420 

ccacttctgg cagacgacgg gtggcgaagg cttcgacgtc gtactcaact ccctcgcgca   9480 

ggagtacgtg gatgcttcac tgcggctcca gccgcgcggc ggccgattcc tggagatggg   9540 

taagaccgat atccgggacg ccgatgaggt cgcggcggca cacgagggag tgcgctatga   9600 

ggcgtacgac ctcaccgtct tcaccagcgt cgacggaccg ggcgcgatcc ccgagcgcat   9660 

tcaggagatg ctctccgaac tgcttgcgct gttcgacaag ggagtcctca ccccgctgcc   9720 

cgtcaccacc tgggacgtcc gccgcgcgtc cgccgcgctg cggcacatgt cgcaggcccg   9780 

gcacaccggc aagatcgcgc tgacggtgcc gcgcccgctc gaccaggacg gcacggtcct   9840 

cgtcaccggt ggcaccggtg tcctgggcag tctcctggcc cgtcatctgg tgaccgagca   9900 

cggggtacgg aatctgctgc tggtgagccg tcggggcggc gacgcccccg gcgccgccga   9960 

actggtcgcc gagctgacgg cagccggtgc cgaggtgagc gtcgtcgcct gtgacaccgc  10020 

cgaccgggca gcgttggaga agctcctcgc gtccgtgccg ggtgacgccc cgctgacggg  10080 

cgtcttccac acggcgggcg tgctggacga cggaatcgtc gaggcgatga ccccggagcg  10140 

ggtggacgcc gtgatgcgcc ccaaggtgga cgcggcctgg catctgcacg agctgaccga  10200 

gggacttgat ctcgcggcct tcgtgctcta ctcctccgca gccggtgtct ccggtgacgc  10260 

gggccagtcc aactacgccg ccgccaatgt cttcctcgac gccctcgcac agcggcggcg  10320 

ggctgccggg ctgcccggcc agtccctcgc ctggggcctg tgggacgacc ggagcgagat  10380 

gaccggtcac ctcggcgacg ccgagatcgc ccggatgacc gaggccggtg tcctcggctt  10440 

caccgccgcc gacggcctgg ccgcgctgga ccgcgcggcg atgtacgacg acgccgtgct  10500 

ggtgccgatg aagctggaca cggcgaccct gggcgcgggc tcgtcgcccg taccgcatct  10560 

cttccgcggt ctggtgcgga cccccgtcgt acgccgggcc gtcgccggga acaccggcgg  10620 

ggacagcggc ggcggacttg agcagcggct cgccgctctc accgcggccg agcgcaccga  10680 

gaccgtgctg gaactcgtac gggagcgcgt cgccgcggtc ctcggacatg ccagcgccga  10740 

cgccatcgat cccgcccggg cgttcaagga gatcgggttc gactcgctca cggctgtcga  10800 

actgcggaac aggctgaacg cggccaccgg actgcggctg cccgccacac tggtcttcga  10860 

ctatccgacg cccacggtgc tctcgcagta cctcctggcg gagctggcac ccggcttgcc  10920 

ggccgaggac ccggtcggga cccggctgct ggagcagatc gcccgtatcg aagcggtcct  10980 

ctccgaggtc tcggaggtca cggacgagac ctcctccctc tccgacatgg acgccgatgc  11040 

ccgatcgggc atcaccgcac gcctcaacga catcctgacc gcatggaaca gggcccagcg  11100 

cgcgccgggt cacgacgcgg tcgcggcgga actggacgac gccagcgacg acgaaatctt  11160 

cgatttcatc gacagcacct tcggcaagtc ctgactcatc cccgctgacc caccgacgcc  11220 

aaccccgcgt ttccgcatac ctggacgggt gaaccactca tggccaacga agccaagctc  11280 

cgcgaatacc tcaagcgcgt caccaccgat ctgcacgaga ccaatgagcg cttgcgcgag  11340 

gtcgagggca gggcgaacga accgatcgcg atcgtgggta tgagctgccg cttccccggg  11400 

ggtgtcgagt ccccggagca gttgtgggag ctgttccgta cgggtacgga cgccatcggt  11460 

gagttccccg aaggacgcgg ctgggacgtc gaggggctct accacccgga ccccgaccac  11520 

gcgggcacca gctacacgcg tgaaggcggc ttcgtccacg gcgccgagcg cttcgacccg  11580 

agcctcttcg gcatctcgcc gcgcgaggcc gtgtcgatgg acccgcagca gcggctgctc  11640 

cttgagacct cgtgggaggc cctggaggcg agcggactcg acccgctccg cctcaagggc  11700 

agccgcaccg gtgtcttcgt cggtgtcatg tcctcggact acggcattca gaagggctcg  11760 

gcgcccgacg gtgtcgaggg cttcctgagc accggtacgc actccagcat cgtctccggc  11820 

cgggtctcgt acgtcctggg tctggagggt ccggcggtct cggtcgacac cgcttgctcg  11880 

tcctcgctcg tcgccctgca ctccgccgcg cacgccctgc gccagggtga gtgctccctc  11940 

gccctggcgg gcggcgtgac gatcatgtcg acgccggaac gtttcgtcga gttcagccga  12000 

cagcgggccc tgtccgccga cggccgctgc aaggcgttct cggcgagcgc cgacggcacc  12060 

ggctggtccg agggtgtcgg catgttggtc ctggagcggc tctccgacgc gcggaagaac  12120 

gggcaccggg tgcttgcggt catccgtggt tcggcgttga accaggatgg tgcgagcaat  12180 

ggtctgacgg cgccgaacgg tccgtcccag cagcgggtga ttcgtcaggc gctggcgagt  12240 

gccggtctga cggcggccga ggtggacgct gtcgaggcgc atggcaccgg caccacgctc  12300 

ggtgacccca ttgaggcgca ggcactgctg gcgacctacg gcaaggagcg cgaggacggt  12360 

cgtccgctgc tgctgggttc ctccaagtcg aacctcggcc acacccaggc cgcggccggt  12420 

gttgccggtg tgatcaagat ggtgctcgcg atgcgggccg gtgtgctgcc gaagacgctg  12480 

catgtgtcgg agccgtcgcc gcacgtggac tggtccgccg gcgcggtgga gctactcacg  12540 

gaggcccggg agtggccgga gaccggccgt ccgcgccgcg ccggtgtgtc gtcgttcggg  12600 

ttcagtggca cgaacgcgca cgtgatcatc gaggaggcgt cggagttcga gccgagcgcc  12660 

gtggagccgc tggccgggtc gggcgtgact ccgccgtggg tgctgtcggc gcggtcggcc  12720 

gacgcgttgc gggggcaggc ggagcggctg ctgtcgttcg tctctgccgc cggtgatgtg  12780 

tcggtggtgg atgtggcgta ctcgctgggt gtgtcgcgtg cgggtcttga gcatcgtggt  12840 

gtggtggtgg gggagtcgcg tgcggagttg ctcgcggctc tggagtcgtt ggcgtccggg  12900 

gttgagtcgc cgggtgtggt gacgggtcgg gtcgctgagg gtcggttggc gttcttgttc  12960 

acggggcagg gtgcgcagcg ggttggtatg gggcgtgagc tggctgctgc gttcccgttg  13020 

tttgcggcgt ctcttgagga gacgtgtggc ttgttggagc gtgccggggt tgcggtgcgt  13080 

gaggtgctgt tcgccgagga gggttcggcc gaggccgccc tgctgacgcg gacggtgtat  13140 

gcgcaggcgg cgttgtttgc ggtggaggtg gcgctgttcc ggttggtgga gtcgttcggt  13200 

gtggtgccgg actttgtcgc tgggcattcg gtgggtgaga tcgctgccgc gcatgtcgcg  13260 

ggggtgttct cgcttgagga tgcggtgtct ctggtggcgg ctcgtggtcg gttgatggat  13320 

gcgctgccgg agggtggggc gatggtggcg gtgcaggcca ccgaggagga tgtgctcgct  13380 

ctgttggagg gggtggagga tgcctccatc gcggcgatca atggccccga cgccgtggtg  13440 

gtctccggca ccgaggccgg tgtcgcccgc gtagtggatg tactccggga gcggggtgcg  13500 

aagaccaagc ggctcgtggt gagtcatgcc ttccactcgc cgctgatgga gccgatgttg  13560 

gctgagttcg ccaccgtcgt ggaggggttg tcgttcgcgg ctcccaccat tccggtggtg  13620 

tcgaatgtgt cgggtgcggt ggcggatgcc gagttgtcgt cgccgggtta ctgggtgcgg  13680 

catgtgcgtg aggcggttcg tttcggtgcc ggggtggaga ccctgctcgg cgctggtgtg  13740 

tcgtcgttcc tggagatcgg tccggacggt gtgctgagcg ggatggcccg cacgtccgtg  13800 

cctgagggtg cggatgtgga gtgcgcgccg ctgatgcgcc ggggccgtgg tgaggtgcgg  13860 

gagttcctca ccggcctctc ccggatggtc gtacggggag tcccggtcga ctggcagtcg  13920 

ctggtcgagg gcggtcgcct ggccggactg ccgacgtacg ccttccagcg tgagcggttc  13980 

tggctggacg ttccttccgc tgtcggtgat gtggccaccg ccggacttgc gccctcgggc  14040 

caccccctgc tcggtgcggt catgcgacgc gccgatgtcg atggtgtcgt gttcacgggc  14100 

cgctggtcac tgcgcagtca tccgtggctg ggtgagcacc gggtcgggtc ttcggtggtg  14160 

ttcccgggga ccgggttcgt cgagctgctg atgcgcgcgg gcgacgaggt cggttgcggc  14220 

cggatcgagg agttgaacca ggagactccg ctcgtcgtcc ccgagcgcgg agcgctccag  14280 

ctccaggtgg tcgtgggcgc gcccgaggag accggcctcc gtggtgtcgg cgtgtactcg  14340 

cgcgcggagg acgccgatgc ggatgtgccg tggacccggc acgccagtgg tctgctgagc  14400 

ccggccgtgg tgccggccga cttcgagctg acgcagtggc cgccggccgg tgcggaggcc  14460 

ctcaatgtcg aggacacgta ccagcgactc gctgatgccg gactggtcta cggcgagcgg  14520 

ttccagggcc tcaagtcggg ctggatcaag ggtgaggaca tctacgccga gatcgcgctg  14580 

cccgagcacg ccgtcgccga ggcggccgag tacacgctgc acccggcggc gctggacgct  14640 

gcccttcagg cgagcggtct gaacgatccg cccgaggtgc aggcgacggc ctatgtcccc  14700 

ttctcgtggt cgggggtgtc gttgtttgct tcgggtgctt cggtgttgcg ggtgtgtgtg  14760 

cgtcatgtgg cgcgggatcg ggtgtcgttg ttggtggctg atggtgtggg tgtgccggtt  14820 

gcggtggtgg agtcgttggt gttgcgggcg atttctgctg gtgcggtggc ggttgctggg  14880 

gtgggttcgg gtgtgggtgg tgggttgttt gaggtggtgt ggtctccggt tgttggtgtg  14940 

aggggtgtgg atgtgtcggg tgtggtggtg ttggaggctg gtgtgggtgt tggtggggat  15000 

ggggtttcgg tggtgggtgg tgtgttggag ggtttgcagg gtgtgttggg tgggggttct  15060 

ggttctcgtg tggtggtggt gacgcggggt gcggttggtt ctggtggtgt ggtggatgtg  15120 

tcgggtgcgg gtgtgtgggg gttggtgcgg tcggttcagg ctgagcatcc gggtcggttg  15180 

gtgttggtgg atgtgggtgt tgagggtgat gtgggtgtgg gtgtggggtt ggctttgggt  15240 

tcgggtgagg agcaggtggt ggtgcgtggg ggtgaggtgt ttgttcctcg tttggcgcgg  15300 

gtgggtgctg tggcggcgga tgcgggtgtt gatggtgctg agatcgcggg tggtttgggt  15360 

gatggtgtgg tgttggtgac gggtggtacg ggtgggttgg gtgcgttggt ggcgcggcat  15420 

gtggtggtgg agcgtggggt gcgtcgtttg gtgttggtgt cgcgtcgtgg gttgggtgct  15480 

ccgggtgcgg tggggttggt ggctgagttg gagggtttgg gtgctgtggt ggaggtggtg  15540 

gcgtgtgatg tgagtgatcg tgtggcgttg gcgggtgtgg tggggggtat tgggtcggat  15600 

ctttcggctg tggtgcatac ggcgggtgtg gtggatgacg gtgtggtgga gtcgatgtcg  15660 

gtgggtcggg tggcgtcggt gtttggtccg aaggcggatg ctgcgtggtt tttgcatgag  15720 

ttgacgcgtg acatggggct gtcggcgttt gtgttgttct cgtcgatggc ggggacggtg  15780 

ggtggtggtg gtcagagcaa ctatgcggcg gcgaatgctt atttggatgg tttggcggag  15840 

tatcggcgtg ggttggggct ggcggcgaca tctctagcct ggggactctg ggaagagtcg  15900 

acgggcatgg gcagccgcct caccgacgcc gacctggaca ggatgagccg ctcgggcatc  15960 

cgtacgctct cgatcgagga cgggctggcg ctcttcgacg cggccctcgc cgccgaccgg  16020 

ccgacagtca tgccggccca cttcgacatc cccgccctgc ggggacaggg cgaatccctc  16080 

gcgccggtct tccgcaccct ggccggcccc ccggcccgcc gctcggcggc cgtcaccccc  16140 

cgtgacatcg cggcggcgac cgagagcagc ctcaccgacc ggctcgccgg tctggacgcg  16200 

gaaggacgcc gggcgctggt gctcggtgtg gttcgtgcgc aggtcgcgca ggtgctggcc  16260 

tacgcctcac cggatctcgt ggagccggag cgcgccttcc aggacctcgg cttcgactcg  16320 

ctgaccgccg tcgaactgcg caacggcctc acggccatcg cgggagtccg cctcccggcg  16380 

acgctcgtct tcgactaccc ctcgaccgac atcctcaccg acttcctcct cgccgaactc  16440 

tccgacgaga ttccggcggc ggtggcgacc ctgccggcga tgggccatgt cgtcgacgac  16500 

gacccgatcg ccgtcatcgg catgggctgc cgctaccccg gcggggtcga gtcccccgag  16560 

gaactgtgga agctcatggc ggagggccgg gacgccatct ccgagttccc gaccgaccgc  16620 

gggtgggacc tcgatgccat ctaccacccc gacccgatgc acacgggcac cagctacacc  16680 

cgcgagggtg gcttcatcca caacgcgggc gacttcgacg ccgccttctt cgggatctcg  16740 

ccgcgcgagg cgatggagac cgacccccag cagcgactgc tccttgagac gtcctgggag  16800 

gcgttcgagc aggccgggat cgtccccacc gatctcaagg gcactcagac cggtgtcttc  16860 

gccggtgtca tgtaccacga ctacgcgggc aacatcggct ccggcagcat cgtcacgggc  16920 

cgcgtcgcgt acaccctggg cctggagggt ccggcagtct ccatcgacac cgcctgctcg  16980 

tcgtccctgg tcgccatcca cctcgccgcg cagtccctgc gtcagggcga gtgctccatg  17040 

gccatcgccg gaggtgtcgc cgtcatggcg acgccggagt cgttcatcga attcagccgc  17100 

cagcgcgcgc tctcccagaa cggccgctgc cgcgccttct cctcggacgc ggacggtacg  17160 

gcctggggcg agggtgtcgg tgtcctgatc ctggagcggt tgtcggacgc gcggaagaac  17220 

gggcacgagg tactcgcggt catccgtggt tcggcgttga accaggatgg tgcgagcaat  17280 

ggtctgacgg cgccgaacgg tccgtcccag cagcgggtga tccgccaggc gctggcgaac  17340 

tcgggtctgt cggccgccga ggtggacgcg gtcgaggcgc acggcaccgg taccacgctc  17400 

ggtgacccga tcgaggcgca ggcactgctg gcgacctacg gcaaggagcg ggacgcggac  17460 

cagcccctct ggctcggttc gtccaagtcg aacttcggtc acaccaaggc cgccgccggt  17520 

gtcgccggtg tgatcaagat ggtgatggcc atcaggaacg gtgtgctgcc gaagacgctg  17580 

catgtcaccg agccgtcgcc gcacgtggat tggtctgctg gtgcggtgga gctgttggcg  17640 

gaggctcggg agtggcctga gacgggtcgt ccgcgccgcg ccggtgtgtc gtccttcggt  17700 

atcagtggga cgaacgcgca cgtgatcgtg gagcaggccc ccaccgacca ggccgctacc  17760 

aagccgaagg ctgccgacgc ggtcccgggc ctgcccgttc cgtgggtggt gtctgcgaag  17820 

aacccggagg cgttgcgggc gcaggcgggt cggttggggt cgttcttggg tgagaccggt  17880 

gttgttgatg tgccggcggt gggttggtcg ttggtgcggg gtcgttcggt gttcgcgcat  17940 

cgggcggttg tggtgggtgg tgagtgggac gcgctgctgg cgagtatcgg tgaactggcc  18000 

gatggcgccg aggatggttc cggtgctgcc tctggttctg ttgtgtcggg tgtggcggat  18060 

gtgtcggggc gtcgggtgtt tgtgttcccg gggcagggtt cgcagtgggt tggtatggcg  18120 

caggggttgt tggattcgtc ggtggtgttc acggagcgga tgacggagtg tgctgcggcg  18180 

ttggatccgt tggtggagtg gtcgttgttg gatgtggtgc ggggtgtgga gggtgcggcg  18240 

tcgttggagc gggtggatgt ggtgcagccg gtgttgtggg cggtgatggt gtcgttggcg  18300 

tcggtgtggc gttcggtggg tgtggtgccg gatgcggtgg tgggtcattc gcagggtgag  18360 

atcgcggctg ctgtggtggg tggttggttg tcgttggtgg atggtgcgcg ggtggtggcg  18420 

ttgcggtcgt tggcgattcg tgaggtgttg gcgggtggtg gtggcatggt cgcggtccag  18480 

gctgcggagg atgaggttgc tgggtggctt gagggtgtgg agggggtggg gattgctgcg  18540 

gtgaatggtc cgcgttcggt ggtgatctcg ggtacgcgtg cgggtttgga tgcgtgtgtg  18600 

gagttgtggt ctgggcgggg gacgtgggtg aagcgggttc cggtggacta tgcctcgcat  18660 

tcggctgagg tggagcgggt gcgtgagcgg gtgctggcgg atctggcgag tgtgacgggt  18720 

ttgtcggggt cggtgccgat gttgtcgacg atgacgggtg actggattgt tgagggtcag  18780 

gttggggccg ggtattgggt ggagaatctg cgtcgtccgg tgttgttcgc ggacgcgacg  18840 

aggcggttgg cgtcggaggg tttcggcgcg ttcgttgagg tgagtgcgca tccggtcctg  18900 

gtcatgggca tcgaggagac cttggaggcc catcacaccg ccacgaccga cgacgacacc  18960 

accacccgaa cccccgtggt caccgtcggc acgttgcgtc gtggtgaggg tggttgggat  19020 

cagttcctgc gctccctcgc ggggctcttc gtccggggtg cggtgacacc ggattgggag  19080 

tcgttgctgg gcggtacgcg tccccgggtc gacctcccga cctacgcctt ccagcgtcgg  19140 

cgcttctgga tcgagagcgt caggaaggaa gcggtgacac tcgccgccga cccggtcgac  19200 

gccgcgttct gggaggccgt cgagagcgcc gacctggcga agctcgccga cagcctgcgc  19260 

atcgagaccg acgtactcga aggcgtactc cccgcgctca cctcctggcg gacacgcagc  19320 

cgtgagcagt cgctcgtcga cggctggcgc taccgcgagg agtggaagcc ggtgcccgca  19380 

ccgaccccga acagcgccac cggcacctgg accgtgctgg tcccggccac ccaccagggc  19440 

gacgccaccg tgaccggtgt gctggacggc ctgcgccgtg gcggcgccga catccgggtg  19500 

ctcgaggtca ccgccaccga ccgcgaggcc ctggccgagc agctccgcgc cgaactcgcc  19560 

cagagcgagc cccggctcat cctctccctg ctggcactgg acgaccgcgc ccacccccgt  19620 

caccccgagc tgaccgaggg catcaccgcc accatcgctc tcgtccaggc gctggacgac  19680 

tgcggcgcca ccgcccggct ctggtgcgcc acctcgctgg ccgtcgcggt caccgaatcg  19740 

gccgaggtgc tcaaccccgt acagacgacc gcctggggca tgggcgcgtc cttcgcgctc  19800 

gaccaccccg agacctgggg cggactggtc gacctcccgg ccgacatcga cacccgtacc  19860 

gcggacatcc tctgctcggt cctggcgtcg gacctccagg aagaccagat cgccctgcgt  19920 

acggccggcc tcttcgcccg ccgtatggtc cgggcccgcc tcgacgaatc cgccgtggcg  19980 

acagagcagc cgtggcggcc caacggcacc gtcctggtca ccggaggcac cggcgggatc  20040 

ggctcgcacg tggcgcgctg gctggcggcc gccggtgcgg agcacctcgt actcaccagc  20100 

cgtcgcggtg ccgaggcgcc cggcgccgcc gaactcgaag ccgagctggc cctgctgggt  20160 

gccaaggtga ccctcgccgc ctgtgacatg ggagaccgcg agtccgtacg ggaactcgtc  20220 

gccgccctcc ccgacgccgc accgctcacg gccgtcttcc acctggccgg cgcactcccg  20280 

gacggcgagc gccgactctc ggcgacgacg ttcgaggact tctcccggat gacccgggcg  20340 

aagatcggtg gagccgttca cctggacgag ctgctcgcgg accgcgagct cgcggccttc  20400 

gtgaccttct cctccggctc ggcgatctgg ggcaacgcca accaggcggc gtacggcgcg  20460 

tccaacgcgt tcctcgacgg cctcgtccac aaccggcggg cacgtgggct cgccgggacg  20520 

tcgatcgcgt gggggctctg gggcggtgac ggcacggaca ccgagaccga cgagcagctc  20580 

agccgcatcg gtgtcaggtc gatggaccct cggctggccc ttgaggtcct ccggcaggcc  20640 

ctcgaccagg acaccagcca tctgatcgcc accgacatcg actggcagcg cttcgccccg  20700 

gtgttcacca tcgcccggcc gcgcccgctg ctggacggaa tcgccgaggt cagggccgtc  20760 

ctgtcggcgg acaccgccga ggtcgggccg gccgacgatg acaccccgaa ggagaccgtc  20820 

gtcacccggc tcgccggcct cagccccgcc gagcgtgacc acgccctgct ggagctcgta  20880 

cggacacagg tggccgcggt gctccgctac tcggacacct cggacgtcga gcaggaccag  20940 

tccttcaagg acctcggctt cgactccgtc accgcggtcg aactgcggaa caagctcaca  21000 

cgcggcgtcc gcgctgcggc tgcccgccac ggcgtcttcg actacgccac cccggtcgcc  21060 

ctcgcggccc atctgcggtc ggagctgttc acggacgacg ccgcggcgtc gggagaggtg  21120 

ccgctgctgg cggagctcga ccggatcgag gcggcggtga cctcgctccc gtcggccgac  21180 

atcgagcgga tgcacctcac ctccaggctt cagagcctgg tgaccaagtt gaacgacatc  21240 

gtcggcgcgg gagctcccct ggaagcggag gccatcgcgg acaagctcga aacggccact  21300 

gccgatgaca tcttcgcgtt catcgacaag gacctcggtc tgaactgacc ggcacgtccc  21360 

cgcctccccg cgctcccgct ccctcgcaca aagattggtg tgtcaccgga atgtcgaacg  21420 

aagagaagct cctcgactac ctcaagcggg tcaccgccga tctccacgcg acccggcagc  21480 

ggctgcgtga ggcggagtcc gatgagcagg agccgatcgc ggtcgtcgcg atgggctgcc  21540 

gctacccggg ggacgtccgt acccccgagg acctgtggca gctcgtcgcg acgggcggtg  21600 

acgccgtcac cgaattcccc gccgaccggg gctgggactt cgacacactc ctcggcggcg  21660 

atgcgggcgc atccgggagc acctatgtgg cccgcggcgg gttcgtccac gacgcggccg  21720 

acttcgatgc ggacttcttc ggcatctcgc cgcgcgaggc gctggcgatg gacccgcagc  21780 

agcggctgct gctggaactc gcctgggaga ccagcgagcg ggccggcatc gacccgcaca  21840 

gcctgcgggg tgcctccgtc ggcgtcttcg ccggcaccaa cggtcaggac tacgccgacc  21900 

tgatggaccg ggcgccggag gacaccgagg catacctctc caccggtagc gtcgcggccg  21960 

tcgtctccgg ccgggtctcg tacgcgctgg gtctggaggg cccttcggtc tcggtcgaca  22020 

ccgcctgctc ctcctcgctc gtcgcgctgc acctcgcctg ccaggcactc cggcagaagg  22080 

agtgctccat ggccttcgcg ggtggcgtca cgatcatgtc gacgcccggg ccgttcatcg  22140 

ccttcagcag gcagagcggt ctcgcgtcgg acggccggtg caaggcgttc tccgacgaca  22200 

cggacggtac ggggtggggt gagggcgcgg gcctcctgct gctggagcgg ctctcggacg  22260 

cgcgcaggaa cgggcatcag gtgctcgccg tggtgcgggg ctcggcgttg aaccaggatg  22320 

gtgcgagcaa tggtctgacg gcgccgaacg gtccgtccca gcagcgggtg atccgccagg  22380 

cgctggccaa cgccggtctg acggcggccg aggtggacgc ggtcgaggcg cacggcaccg  22440 

gtacgaccct cggtgacccg atcgaggcgc aggccatcct cgccacgtat gggcagagcc  22500 

gcgagcagga ccagccgctc tggctcggct ccatcaagtc gaacatcggt catacccagg  22560 

ccgcggccgg ggtcagcggt gtgatcaaga tggtgatggc catccagaac ggcgtgctgc  22620 

cgaagacgct gcatgtgtcg gagccgtcgt ccgttgtgga ttggtccgct ggtgcggtgg  22680 

agctactcac ggaggctcgg gagtggccgg agaccggtcg tccgcgccgt gccggtgtgt  22740 

cgtcgttcgg tgtgagcggt acgaacgccc acatcatcat ggagcaggcg cccgtgcctg  22800 

aggcagagtc ggagccggac ggcgaagcac ccgccgcggt gtccgggctg ccggttcctt  22860 

gggtggtctc cgggaagacc gccgacgcgt tgcgggcgca ggccgagcgg ctgctgtcgt  22920 

tcgtctccgc cgacgcggat gtctccgtgg tggatgtggc gtactcgctg ggtgtgtcgc  22980 

gtgcgggtct tgagcatcgt ggtgtggtgg tgggggagtc gcgtgcggag ttgctcgcgg  23040 

ctctggagtc gttggcgtcc ggggttgagt cgccgggtgt ggtgacgggt cgggtcgccg  23100 

agggtcggtt ggcgttcttg ttcacggggc agggtgcgca gcgggttggt atggggcgtg  23160 

agctggctgc tgcgttcccg gtgtttgcgg cgtctcttga ggagacgtgt ggcttgttgg  23220 

agcgtgccgg ggttgcggtg cgtgaggtgc tgttcgccga ggagggttcg gccgaggccg  23280 

ccctgctgac gcggacggtg tatgcgcagg cggcgttgtt tgcggtggag gtggcgctgt  23340 

tccggttggt ggagtcgttc ggtgtggtgc cggactttgt cgctgggcat tcggtgggtg  23400 

agatcgctgc cgcgcatgtc gcgggggtgt tctcgcttga ggatgcggtg tctctggtgg  23460 

cggctcgtgg tcggttgatg gatgcgctgc cggagggtgg ggcgatggtg gcggtgcagg  23520 

ccaccgagga ggatgtgctc gctctgttgg agggggtgga ggatgcctcc atcgcggcga  23580 

tcaatggccc cgacgccgtg gtggtctccg gcaccgaggc cggtgtcgcc cgcgtagtgg  23640 

acgtactccg ggagcggggt gcgaagacca agcggctcga cgtcagccac gccttccact  23700 

cgccgctgat ggagccgatg ttggctgagt tcgccaccgt cgtggagggg ttgtcgttcg  23760 

cggctcccac cattccggtg gtgtcgaatg tgtcgggtgc ggtggcggat gccgagttgt  23820 

cgtcgccggg ttactgggtg cggcatgtgc gtgaggcggt tcgtttcggt gccggggtgg  23880 

agaccctgct cggcgctggt gtgtcgtcgt tcctggagat cggtccggac ggtgtgctga  23940 

gcgggatggc ccgtgggtcg atctccgacg gcgccgacgt tggctgtgtc cccgtgatgc  24000 

gccggggccg gggtgaggtg cgggagttcc tcaccggcct ctcccggatc gccgtacggg  24060 

gagtccccgt gagctggggt ccgctgctgg cgggtggtcg gcgggtcgag ctgccgacgt  24120 

acgccttcca gcgtcgccgg ttctggctgg aggcggggca ctccgtcacg gacgcttcgg  24180 

gtctgggcca gacggctgcc gggcatccgc tgatcggtgc tgtggtgagt ctggccggtg  24240 

gtgacggtgc cgtgctgacc ggtcgggtgt cgttgaacac gcatccctgg ctgggcgacc  24300 

accgggtcgc gtcttcggtg gtgttcccgg ggaccgggtt cgtcgagctg ctgatgcgcg  24360 

cgggcgacga ggtcggctgc ggccggctgg aggagctgaa ccaggaggca ccgctcgtcg  24420 

tacccgaccg gggcgccgtc cagatccagg tgaccgtgga ggcccccaat gctgtgggag  24480 

agcgaccggt cgcggtttac tcgcggctgg aggacacgga tacggacgcc ccgtggaccc  24540 

ggcacgccag tggtctgctg agcccaacca ccgcttcggc ggacttcgac ttcacggcat  24600 

ggccgccggc cggtgcggac cccctctccg tcgacggaat gtatgaccgc ccggactcgg  24660 

gcctggtcta cggtcccctg ttccaggggc tgacggccgc ctggcgcaag ggcgatgagg  24720 

tgtacgcgga gatcgagctg cccgaggggg cggcggtcga cgccgcccgc ttcgggatgc  24780 

accccgccct cctcgacgcc gccctccacg ccctcgggtt ctcggcctcc tacgaggacc  24840 

aggaggagga cggcaccgtg gcccggctgc ccttctcgtg gtcgggggtg tcgttgtttg  24900 

cttcgggtgc ttcggtgttg cgggtgtgtg tgcgtcatgt ggcgcgggat cgggtgtcgt  24960 

tgttggtggc tgatggtgtg ggtgtgccgg ttgcggtggt ggagtcgttg gtgttgcggg  25020 

cgatttctgc tggtgcggtg gcggttgctg gggtgggttc gggtgtgggt ggtgggttgt  25080 

ttgaggtggt gtggtctccg gttgttggtg tgaggggtgt ggatgtgtcg ggtgtggtgg  25140 

tgttggaggc tggtgtgggt gttggtgggg atggggtttc ggtggtgggt ggtgtgttgg  25200 

agggtttgca gggtgtgttg ggtgggggtt ctggttctcg tgtggtggtg gtgacgcggg  25260 

gtgcggttgg ttctggtggt gtggtggatg tgtcgggtgc gggtgtgtgg gggttggtgc  25320 

ggtcggttca ggccgagcat ccgggtcggt tggtgttggt ggatgtgggt gttgagggtg  25380 

atgtgggtgt gggtgtgggg ttggctttgg gttcgggtga ggagcaggtg gtggtgcgtg  25440 

ggggtgaggt gtttgttcct cgtttggcgc gggtgagtgt tgtggcggcg gatgtggtgc  25500 

cggatgcggg tgttgatggt gccgatatca ggggtggttt gggtgatggt gtggtgttgg  25560 

tgacgggtgg tacgggtggg ttgggtgcgt tggtggcgcg gcatgtggtg gtggagcgtg  25620 

gggtgcgtcg tttggtgttg gtgtcgcgtc gtgggttggg tgctccgggt gcggtggggt  25680 

tggtggctga gcttgagagc ttgggtgctg tggtggaggt ggtggcgtgt gatgtgagtg  25740 

atcgtgtggc gttggcgggt gtggtggggg gtattgggtc ggatctttcg gctgtggtgc  25800 

atacggcggg tgtggtggat gacggtgtgg tggagtcgat gtcggtgggt cgggtggcgt  25860 

cggtgtttgg tccgaaggcg gatgctgcgt ggtttttgca tgagttgacg cgtgacatgg  25920 

ggctgtcggc gtttgtgttg ttctcgtcga tggcggggac ggtgggtggt ggtggtcaga  25980 

gcaactatgc ggcggcgaat gcttatttgg atggtttggc ggagtatcgg cgtgggttgg  26040 

ggctggcggc gacatccctg gcctggggac tctgggaaga caccgcgaac ggcggtatga  26100 

cgggccacct ggccgaagcc gaccgtacgc ggatggcacg cgggggagtc ttccctctgg  26160 

cgctggacga ggggctcgca ctcttcgacg ccgccctcgc caccggaaag gcgacactcg  26220 

tccccgtcca tctggacacc accgcgctgc gcgcacacgc tgacgaactg cccgccctct  26280 

tccgtgacct cgtccgcgcg ccgaagcggc gcacggcggc ggaaggccgt gcggcggact  26340 

ccgccgacga cctcgcgggc cgcctcgccg gcctggccgc cgaggcgcgc cggccgttgg  26400 

tgctcggtgt ggttcgtgcg caggtcgcgc aggtgctggg gtacgcctcg gcggatctcg  26460 

tggagccgga gcgcgcgttc caggacctcg gcttcgattc gctgacggcc gtcgaactgc  26520 

gcaacggcct cacggccgtc gcgggggtcc gcctcccggc gacgctcgtc ttcgactatc  26580 

cctcgaccga catcctcacc gacttcctcc tcgccgaact ctccggcaag gtcgccgtgg  26640 

ccgcgcccct cgcgccgctc gccaccaccg ggccggtgca cgacgacccg atcgtcgtca  26700 

tcggcatggg ctgccgctac ccaggcgggg tccgctcgcc ggaggacctg tggcggctgg  26760 

tcgccgatgg ccgggatgcg atatcggagt tcccgaccga ccgcggctgg gacctcgacg  26820 

cgctgtacca cccggacccg gaccacgccg ggaccagcta cacccgcgag ggcgggttcc  26880 

tgcacgacgc ggccgatttc gacgcggact tcttcgggat ctcgccgcgt gaggccatcg  26940 

tcatggaccc gcagcagcgg ctgctccttg agacgtcctg ggaggcgttc gagcaggccg  27000 

gcatcgtgcc cgccgacctc aagggcaccc agaccggcgt cttcgccgga gtgatgtacc  27060 

acgactacgg cacccgaatc gtcgacattc ccgagggggc cgaaggctat ctgggcaccg  27120 

gcatctccgg cagcgtcgtc tccggccggg tcgcgtacac cctgggtctg gagggcccgg  27180 

cggtcacgat cgacaccgcc tgctcctcct cgctcgtcgc cctgcattcc gccgcgcacg  27240 

ccctgcgcca gggtgagtgc tccatggcca tcgccggtgg tgtcaccgtc atggcgggcc  27300 

ccgacacctt catcgacttc agcaggcagc gcggtctggc cacgaacggt cgctgcaagg  27360 

cgttctcggc ggacgccgac ggcaccggct ggggcgaggg cgtcggcgtc ctggtcctgg  27420 

agcggttgtc ggacgcgcgg aagaacgggc acgaggtact cgcggtcatc cgtggttcgg  27480 

cgctgaacca ggacggtgcg agtaacggtc tgacggcgcc gaacggtcct tcgcagcagc  27540 

gggtgatccg ccaggcactg gccagcgccg gtctgacgac gtcggacgtc gacgcggtcg  27600 

aggcgcacgg caccggcacc acgctcggtg acccgatcga ggcccaggcg gtgctggcca  27660 

cctacggcca ggatcgcgcc gcggaccagc cgctctggct cggctcggcc aagtcgaact  27720 

tcggtcacac gcaggccgcg gccggtgtcg ccggtgtgat caagatggtg atggccatcc  27780 

ggaacggcgt gctgccgaag acgctgcatg tgtcggagcc ttcgacacat gtggactggt  27840 

ccgccggcgc cgtggagctg ctggcggagg cccgggagtg gccggagacc ggtcgtccgc  27900 

gccgcgccgg tgtgtcgtcg ttcggtgtga gcggtacgaa cgcgcacgtc atcgtcgagc  27960 

aggcccccac cgaggagcag gcccccgcgg acgcgcctgc cccgacggac gcgcccgccg  28020 

gcactccggt gccctggatc gtctccggtc ggaccgccga ctcactgcgc gaccaggccc  28080 

gccgtctgct ggagcacctc gaccggaacg gcgacctcga cccgcaggac gtcgcgcggg  28140 

ccctcctcac cacccgtacc cgcttccacc accgtgccgc cgttgtggcg accgagcgac  28200 

aggacatcgt cgcggcgctc gaagcactcg ccgacggccg gcccgtgagc ggtctggttc  28260 

aggggacggc caccaccatg gcgaagtccg cgttcctgtt cacggggcag ggtgcgcagc  28320 

gggtcggcat gggtcgggaa ctcgcggccg aattcccggt gtttgcggcg tctcttgagc  28380 

agacgtgtgg tctgttggag cgtgccgggg ttgcggtgcg tgaggtgttg ttcgccgagg  28440 

agggttcggc cgaggccgcc ctgctgacgc ggacggtgta tgcgcaggct gcgttgttcg  28500 

ccgtcgaggt ggcgctgttc cggttggtgg agtcgttcgg tgtggtgccg gactttgtcg  28560 

ctgggcattc ggtgggtgag atcgctgccg cgcatgtcgc gggggtgttc tcgcttgagg  28620 

atgcggtgtc cctggtggcg gctcgtggtc ggttgatgga tgcgctgccg gagggtgggg  28680 

cgatggtggc ggtgcaggcc accgaggagg atgtgcttgc cctcctggag ggggtggagg  28740 

acgcctccat cgccgcgatc aacggccccg acgccgtggt cgtctccggc accgagaccg  28800 

gtgtcgcccg cgtagtggac gtactccggg agcggggcgc gaagaccaag cggctcgacg  28860 

tcagccacgc cttccactca ccgctgatgg agccgatgct cgccgacttc gcacgggtgg  28920 

tcgcgggtct gtcctatgag gaccctgcga tcccggtcgt gtcgaatgtg tcggggtcga  28980 

tggcggacgg tgagctgtcg acgccgggat actgggtgcg gcatgttcgt gaggcggttc  29040 

gtttcggtgc cggggtggag accctgctcg gcgctggtgt gtcgtcgttc ctggagatcg  29100 

gccccgatgg tgtgctgagc gggatggccc gtacgtccgt acctgagggt gcggatgtgg  29160 

agtgcgcgcc gctgatgcgc cgagaccgcg ccgaggtacg ggagttcctc accggcctct  29220 

cccgtctcgc cgtacgcggt gtcccggtga gctggtcccc cctcgtggcg gggggccggc  29280 

gggtcgagct gccgacgtac gccttccagc gtcgccggtt ctggctcgac gccggacact  29340 

cggtcacgga cgcttcgggt ctgggccaga cggccgccgg gcatccgctg atcggtgccg  29400 

tggtgggtct ggccggtggc gatggtgtcg tcctgaccgg tcgggtgtcg ttgcacaccc  29460 

acccctggtt ggcggatcac caggtcgcgg gggtgacgct gcttccgggt acgggctttg  29520 

tggagctggc ggtccgtgcc ggtgacgagg tcggctgtgg ccggctggag gaactgaccc  29580 

tggaggcccc gctggtcgtg cccgaccggg gcgccgtcca gctccaggtc gtcgtcggcg  29640 

ggctggagga atccggcgtc cgtaccgtca gcgtctactc ccgagccgag gacaccgaca  29700 

accccgacac cccctggacc cggcacgcca gtggtgccct cggcacggcg gccgacccgg  29760 

ccgacttcga cctcaccgcc tggccgccgg ccggaaccga ggccgtcgag atcggggact  29820 

tctacggcga actggccgcc acacccgacg gtctggtcta cggtccgctg ttccaggggc  29880 

tgacggccgc ctggcgcaag ggcgatgagg tgtacgcgga gatcgagctg cccgagggcg  29940 

cggcggtcga cgccgcccgc ttcgggatgc accccgccct cctcgacgcc gccctccacg  30000 

ccgtcggact ctcgaacgac gccgacgccg acgccgacgc gggcacggca caggaggacg  30060 

gcaccgtggc ccggctcccc ttcgcctggt ccggtgtgac gctccaccgc tccggcgcga  30120 

cccggctgcg gctctccgta cggcccaccg gaggcgacag ctaccacctg cggatcgccg  30180 

acgcggtcgg cgcgcccgtc gcgaccgtcg gggaactgct gctgcgcggt atcagcgccg  30240 

agcagctcgc gcgggccggc accgaccgcc cggacgcgct cttccggctg gagtgggagg  30300 

cgctgcgcgg cgacggggcg accaccgcgg gggagtgggc gctgctcgga ggggacccgt  30360 

acggtctcgc tccggcccgt gccgtcccgt acggcgatct cgacgccctg gcggccgagg  30420 

ccgagggcgg cacgccgccc gaggtcgtcc tgctgcccct gacagtgccc gccggcgaag  30480 

agccggacgc gggcgagcgg gccgcgcacc gggcgctgcg cgcggtgcgg tcctggctcg  30540 

ccgacgaccg gttcgcggct gcgaccctcg tcctgatgac caggggcgcg ctggcggcga  30600 

cccccggcga tgaggtcacc gatgtggcgg gcgccgaggt ctggggcctc gtacggtcgg  30660 

cgcagaccga gcaccccggc cggttcgtcc tggtcgactc ggacggttcc gaggcgtccg  30720 

cgcgggcgct cccggccgcc gtggcgagcg gtgagccaca gctcgcactg cgcgcgggta  30780 

ccgtcaacgc ggcccggctg ggccgcgtgg agcgggccgg ggcggaggcc gtggccacgt  30840 

tcgatcccga gcggaccgtc ctgatcaccg ggggtacggg cgcgctcgcc ggccaactcg  30900 

cccggcatct cgcccgtgcg tacggcgtcc ggcatctgct gctcgccggg cggcgcggcc  30960 

cgagcgcccc ccacgcggcg gagctggtcg ccgagctggc cgaactgggc gccctggccg  31020 

aggtcgtggc ctgcgatgtg gccgaccgtg aggcgctgac cgccctgctg gccgcggtcc  31080 

ccgccgaccg gccgctgggt gccgtcgtgc acacggcggg ggtcctggac gacgggctcg  31140 

tggagtccct cacgcccgag cggctcgacg cggtgctcca cccgaaggcg accgcggccc  31200 

tcctgctcga cgaactgacc cgtgacgccg acctgacggc gttcgtgctc ttctcctccg  31260 

ccgcgggcac cctcggcagc cccggtcagg ccaactacgc ggcggccaac gccggtctcg  31320 

acgcgctcgc cgtccggcga cgcggccagg ggctgcccgg tctgtcgctc ggctggggcc  31380 

tgtggcaggc ggacggcggt atgggcggcg cgctcagcgg cggcgaccag gcgcgtatcg  31440 

cccgtggtgg tgtcgccgcg ctcacgaccg accacggtct ggcgctcttc gacaccgcct  31500 

gcgccggtcc ggacgccgtc gtactgccga tgctgctgga cctgcgaccg caggacgacg  31560 

taccgcatct gctgcggtcc ctggtgagcg cgcgccgcaa gggcgcgtcg gcgggagccc  31620 

gccacgaggg tccggccgag ctgcggcgca ggctcgccgc cgcgacgccc gacgagcggt  31680 

acgaacacct cctcggcctg gtccgctcgt gcaccgccgt ggtgctgggg caccggggcc  31740 

cgcaggacgt cgatcccggg gtcgggttcc tggagtccgg tttcgactcg ctgaccgcga  31800 

tggagctgcg caaccagctc aacgaggcca ccggtctgcg gctcgcggcc accgtcgtct  31860 

tcgaccacac cacccccgca gatctggcgc ggcacctggt cgacggagtg gccgacacgg  31920 

tcgccgccgc accgggccag cagccggcgc cgcggtcgga cgacgacgcg gacaccctga  31980 

gcgggctgtt ccgtacggcg gtacgggccg gtcaggtgac gaagggcgtc gatctgctac  32040 

gggccgtggc cgagctgcgc ccggccttcc acagcgccga cgaactgggc gacgatctgc  32100 

cggtgccggt acggctcgcc cagggcccga gtgccgcgcg gctgttctgc ttcgcctcgc  32160 

cgatggcgat gggcggcacg caccagtacg ccaggctggc ggcgcacttc cggggcgtac  32220 

gcgaggtctc ggcgctcccc atgcccggat tcgcgacggg agacctgctg ccggcgacgg  32280 

ccgaagccgt cgtggaggtc ttcggccgga gcctcctgcg ggcggccggg gacgagccgt  32340 

tcgtcctcct cggctactcg gctggcggtg tcttcgccca cgcggtggcc gcctggctgg  32400 

agtccgaagg gtgcgcgcca gccgccgtgg tgctgctgga cagctaccgc gcggacggtg  32460 

gcaccagcat ggacggcgac ttctgggtga gcatggtgga gggcctgttc tcgcgggaag  32520 

aggtcttcgg acggttcacc agcgcccgac tgtcggcgat gggccggtac gcgcggctcg  32580 

tcggcgaggt caagacgggt gaggtgaagg cgccggtgct cttcgtccgc ccggagcggt  32640 

cgctgagcgc gagcgccgac gcgggcggag tcgggggcgg ggacgccggg gccgctgccg  32700 

ccacggatga ctggcgggcc tcgtgggaca cggccgagac ggtgctggag gtggcgggcg  32760 

accacttcga catcatcgag agccaggccg ccgcgaccgc cgacgccgtg gagggatggc  32820 

tcgcggaccg ggtctgaccc gtctccccat cagccggtcg agcgccggag gacatcgctg  32880 

agggccgacc ccgcacaggg gccggccctc ggccgtaggt acgggtggga cgcgtacccg  32940 

ccgtccgcat cgcgtgcctt gctcgtaccg cgacctgctc gtaccgcgac ctgctcgtac  33000 

cgtgacccct gcctgtacgc gccctgcccg cactgcgatc ctgcccgcac tgcgatcctg  33060 

cccgcactgc gatcctgccc gtacgcgccg tgcccgtacg ccccctgccc ataccgcact  33120 

tgtccgtacg cgccccgcct cccgtacgag cgcgcgcggg aacagcattc ccgtacgacg  33180 

tcaggggcgg tgcggcgagg atcccggccc ggaagccgtt gtccttgccg caccgcccct  33240 

gacggtgcgg agcgcgtcag cctatggctg tcgcaccccc acgaagacac cgcggtcgac  33300 

atacccgtcg ggcaggtact ccaccgagca cccggccgcg cggaacgcct cctcgtactc  33360 

gtccttggag aacagcgaca gctcctgttc gtccacgaag tgccgtacgg gatcgtcgcc  33420 

gctcgtcacc aggtagtgca tctccacatg gctgcgcccg gcccgggtgg tccagcggcc  33480 

catgcggacc accttgccgc cctcgttctc gaagctcgcc tccaccagat cgccgccgtt  33540 

ccaactgtcc cgcagaatcc acggctcgat gatcagcacc ccgccgggac gcagatggtg  33600 

ggccatgttc ttcagggcgg cgaacagacc gtccagggtc tccagatagc cgacggagct  33660 

gtacatcgaa cagatcacgt cgaagctccg gtcgagcccg aaggtgcgca tatcgccctc  33720 

gtggaccggc acccccggca gcttggcctc ggcgacccgg accatcggcg ccgacaggtc  33780 

cacaccggtg acggcgaaat cgtccctcag cagcgcgagg tgctcgccgg tgccacagcc  33840 

cacatcgagc agatcggccg ctccggggtt gcgttcgagc gccagctcgc ggatgcgggc  33900 

ggcctcaccg gcgtagtcct tgtgccgccg atagatgtcg tcatagacgc gcgcgaagtc  33960 

ctcttcgtac atgaaggagt cacctggccg gggttcgggc actgacacag cgccggatga  34020 

tgtcgcagac ctgatcgatc tccgacggcc cgacggtggt acccgtcggg agggcgagca  34080 

cgcgctcggc cagtgcctcc gcgtgcggca gagggtgtgg cgcgtgccgg gcggggtcgc  34140 

tcagataggg ctccacctga tggcaactgg ggtggaagta gcggcgcgag aggacgttct  34200 

gggcgatgag ggcggtgtgc acctcgtcgc ggtggatacc cgccactgcg gcgtcgatct  34260 

cgatcaccag atactggtgg ttggcgcgct cgccctcggc ctgaccgcgt acccagacac  34320 

cgggcagccc gtccaggccc ttctcgtagc ggccgtggtt gatccggttg gcctccatga  34380 

ggctgtccat cacctccagc gaggtgagac ccatggccgc cgctgcttcg ttcatcttgg  34440 

cgttggtccc gccggagcgg atctcaccgg cgctggtgat gccgaagttg cgcagctcgc  34500 

ggcagcgctc ggcgaactcg gcgtcccggg tgacgatcgc gccgccctcg aagctgttga  34560 

cgaacttggt cgcgtggaag ctgtacacct ccgccgtgcc gaagccgccg acggggcggc  34620 

ccttgtaggt gcagccgatg gcgtgcgcgg agtcgaacag cagcggcagt ccgtgccggc  34680 

cggcgatctc ctccagctcg tccacctcgc aggggcggcc gaagacgtgc acgcccatga  34740 

tgccgcgggt gcgcgggccg atcagcgcct cgaccttggt ccagtcgatg tttccggtcg  34800 

tctcgtcggc gtcgcagaag acggggacga ttccgatcca gtccagtgcc gccgcggtgg  34860 

ccacccaggt gaaggccggg acgatgacct cgtcgccacc ccggattccc gcggccttcg  34920 

ccgccacctg gagcccgatc gtggcgttgc acaccgcgac gcagtggtcg acaccggcga  34980 

cctcggcgag tctctcctcg aattctcgga ccagcggacc attggtgaga tagagccggt  35040 

cgagtgctcc ctccagtctc tccgtcaggc gggcacgact gcctatattg ggtcgcccga  35100 

catgcaacgg ctcgcggaac acaggggaat cagtcacctg ttcatcgttc cgttcacccg  35160 

cccctagcct caacctgcgg gcatgggcgc gccccagtag gggccgccgc cagcccctaa  35220 

ccacccccct atgcggtccc actgctgctg acgcggcggc ctccgcggca ctagcgtcgg  35280 

cgccgtctgc cactgagttc accatggcca gccgccccaa tggagatttc catgaccgag  35340 

acgctgtcga ctcttccgcc cacccacacc ggcgacgagt cgctcgcggt ccgtatcgcc  35400 

aagtcggtga gtgtcgtcga cgacggggcg ctgcacagcc tcgacgaatt ccacgactgg  35460 

ttcaccgcca gagggcagcg gaccgcacat gtcgagagag tgccgctcga cgaactcact  35520 

ggttggagct ccgatcccgt gaccgggaac atcgggcacg acagtgggaa gttcttcagt  35580 

gtgcaggggc tctccgtcga actgcccggt gcgccggtgc ccgcctgggc gcagcccatc  35640 

atcaatcagc ccgagatcgg gatcctgggg attctgatca aggaattcaa cggtgttctg  35700 

cactgtctga tgcaggcgaa gctggagccg gggaaccgca acggcctcca gctctccccg  35760 

acggtgcagg cgacccggag caactacacc cgggtgcacc agggcaaccc cgtcccgtac  35820 

gtgggctact tccaggacac ctcggcgaac cgggtgatca ccgacgcgct ccagtccgaa  35880 

cagggctcgt ggttctacca gaagcgcaac cggaacatgg tcgtcgagac cgaggcggag  35940 

atcgagcagc acgaggcgtt catgtggctg accatcggtc agctgcaccg cctccttgcg  36000 

atcgacgacc tgatcaacat ggacacccgt acggtgctgt cgtgtctgcc cttctccggt  36060 

gcgcagctcg ccgagcagct cccgggcacc ggcggcgatc tgcggatgcc gatcctgcgc  36120 

tcgtgcagcg aggaccaggg cagtctgcac accaccgggg acctgctgag ctggatcact  36180 

gacgcccgta cccgcaacga ggtgcgcacc cggctgacgc cgctgcgcga cgtggcgggc  36240 

tggcggcgca ccccggacgc gatcacgcac gacacgggtc ggttcttcga cgtgatggcc  36300 

gtgcgcatcg agaccgacgg ggaccgcgag gtccgccagt ggacccagcc gatgatcgcg  36360 

ccggccggga tcggcatcgt ggcgttcctg gtcaagcgga tcgacggggt gctgcacgtg  36420 

ctggcgcacg cccgggtcga gccgggctat ctcgatgtcg tggagctgtc gcccacggtc  36480 

atgtgcacgc ccggcaacta cgagggcctg cccgccgccg cccggccgcc gttcctcggc  36540 

gaggtgctct cggcccgtcc cgagcaggtc cgcttcgaga cgatcctctc cgaggagggc  36600 

ggccggttct accacgcgca gaaccggtac atcatcgtcg agtccgatat cgacgtggcg  36660 

ccggaactgg cctcggagta ccgctggatg gcgctccacc agatggtcgg cctgctgcgg  36720 

cacagccact acgtcaacgt ccaggcccgc agtctgatcg cgtgtctgca cagcctctcg  36780 

ggggcgcagg ggcggaactg acccgcgccc tccccggatc tcctcccgct ctccccggcc  36840 

ctgaaagggt gacgatgctc taccggcagc tcggacgtac ggcactgaag gtcagcccgc  36900 

tctgtctggg caccctcaac ctcggcgtcc gtaccacccg tgacgaggcg ttcgccctca  36960 

tggacgaggc cctggagcag ggcatcaact tcttcgacac cgccaaccag tacggctggc  37020 

aggtccacaa gggcctgacg gaggagatca tcggagagtg gttcgcacag ggcggcggcc  37080 

ggcgcgagcg cgtggtcctg ggcaccaagg tctgcaaccc gatgagcgat ctgcccaacg  37140 

accaggggct gtcggcgcgg cacatcatcg cctcctgcga ggactcgcta cggcggctgc  37200 

gcaccgactg gatcgatgtc taccagctcc acaacatcga cccgacggcg tcctgggacg  37260 

aggtgtggca ggccatggag accctggtgc accagggcaa gatccgttac gtggggtcgt  37320 

ccaacttcgc gggctggcat ctggccgacg cgcaggccgc ggcggcccgc cgtaacttcc  37380 

tcggactcgt gtcggagcag tgctgctaca acctggcgac ccggtacgtg gagatggagg  37440 

tcgtccccgc cgcgcgggcg cacggcatcg gagtgctggc ctggtcgccg ctgcacggcg  37500 

gtctgctgag cggggcgctg cgcaagctgg acgaggggac ggcggtgaag acggcccagg  37560 

gccgtgcgca gatcgcgctg cggaccatgc gggacaccgt cgagcagtac gagaagctgt  37620 

gcgagagcat ctccgccgac ccgtcccagg ttgccctggc ctggctgctg tcccggccgg  37680 

gtctcacggc cgccgtcatc ggcccgcgca ccaccgggca cctggcgagc gcgctggaga  37740 

ccctggacat gacgctgccc gaggacatcc tggcgccgct ggacgaactc ttcccgccga  37800 

tcggcaacgg tcagccggcg ccggccacct ggctcgcctg acgggcggga cgacttcccc  37860 

ggccggtcac ccacgagcgt gtcaccggcc ggggggcacc agcggtcggg agccctgaca  37920 

acgggcaccg ccactggtgc cggacccgaa caacgaccgc gtcccggccg ttcccacccc  37980 

tgacacggag cagtccccac atgccgcctc atgtccgccc gatgcccgac atcacatccg  38040 

aacggctccc ggaccaggac caccacctgc ccgccgagcg tgcccggccc gtgctgatca  38100 

gcagcgtcgc ctccgactcg cacacctgga acctggtctt cctccaactg ctgatcgagg  38160 

agctgggaca cgaggtcatc aacctcggtc cctgcgtgcc cgacgaactg ctcatcgccg  38220 

agtgccgtga ccgccgcccc ggcctcgtcg tcatcagcac cgtcaacggc cacggctacc  38280 

aggacgggct acgggtgatc gggaaactgc gcgcctgcga ggacctcgcg aacatccccg  38340 

tcgtcatcgg cgggaagctc ggcgtctcgg gcccgggtca gtcgtacgcg gccgagttgg  38400 

ccggcgccgg gttcgacgcg gtgttccccg acggggcgga ggccgtgtcc tccttcacca  38460 

gatacgtcga gaagctcccg cagcgagtag tgtcttgacc ggattcggcg cctacgtccg  38520 

ctccgtccac cggcgcggcg aactcgtcgt ccagccgcgg atgggattca gcggtacggt  38580 

cgagatgcgc gccggtctcg ccgcgacccg ggcggcggac gcggccacgg tcggcaccat  38640 

caccctggac agctacaccc gggtcgggga actcgccgca gccgaggagg cactccgctc  38700 

cggcatcgcc ctcaacggct accccatcgt cacctacgac gaatccacca cccgtgaact  38760 

cctcgccggg atcgcgggtg aggacttccc cgttcagatc cggcacgggt cggcgacccc  38820 

cctgcacatc ttcggcgcgc tgacccgcgc gggcctggac gccaccgagg gcggccccgt  38880 

ctcctactgc ctgccctacg gccggattcc gctggaacag tcggtgacca actggacccg  38940 

ctgctgcgag gagttcgccc ggctgcgcgg gctgggccgt gaaccgcatc tggagacctt  39000 

cggcggctgc atgctcgggc agctctgccc gcccagccag ctcgtcgcca tcagcatgct  39060 

cgaagcgctc ttcttccacc agcacggcat tcgcagcatc tccctcagct acgcccagca  39120 

gacccatcag ggacaggacg aggaagccgt gctggcgctg cgccggctcc accgcgaact  39180 

gctgcccgat gccgactgcc acatcgtcat ctacgcctat atgggggtct atccgaccac  39240 

ccccgagggg gcccacgcac tgctgggccg ggccgccgaa ctcgccgtcg ccaccggggc  39300 

cgagcggctc atcgtcaaga ccgcggccga ggcccaccgc atccccacca tcggggagaa  39360 

cgtggcggcc ctggagcacg cggccaccgt gtcccgcgcc gcccgccggg ccaccgcgct  39420 

cccggccggt cactccgctg cgcccgctgc caccgacccc accgccgcgc tcacggcccg  39480 

acccggtacg tacgcggacg gatccgccgc gctcacagcg ggccccggcg ccgcgcggga  39540 

cggctccacc gactccgccg tctacgcgga ggcccgcgcc ctcatcgaag ccgtcatgaa  39600 

ctgcggaccg gatgtcggca ccgcactgtt ccgcgctttc aagaggggat acctggacat  39660 

cccctactgc ctccaccccg acaacatggg ccgcagccgg agttacatcg acgacaccgg  39720 

gcggctgcaa tgggcggaga ccggaatgct gcccctgggg aatgccagaa aaagcggaac  39780 

aggccgctcg gtatcgtcaa ccgatctgat atcggccctt tccttcgtgc agcggaccta  39840 

tgaccaactg gcatttccgg aatcccggga gccgctccgg ataccccggc agcagcgccc  39900 

ctaggggtgg ctagggggcg gataggggac ggctggagcg gcgctctccc ctagcatgag  39960 

cgacgtaatc gaaccgtgag gtggtgtgaa tgtccaagcc cccgagtgcc aaggggactg  40020 

tgccgttcgg tcaataccgg acgtggtatc gggtaacggg cgatctgcat tccggtaaac  40080 

caccggtggt gctgttgcac ggtggtcccg gctccaccca cgactacctg ctggccatga  40140 

cctccctcac cgaagccggc tggcccgtcg tccactacga ccagctcggc aacggcggat  40200 

ccacccacct ccccgagaag ggcgaggact tctggaccgt ccagctcttc gaggacgaac  40260 

tggacaacct cctcaaccag ctcggcatag ccggcgacta cgtgctcttc ggccagtcct  40320 

ggggcgggat gctcggctcg gtgcacgccg cccgccgccc cgccggactg cgcggcctcg  40380 

tcgtcgccaa cgcacccgcc tccatgaaga tctggctcca ggagatggcg cggctgcgcg  40440 

cactgctccc gcccgacgtg caggagaccc tcctcaagca cgaggcggcg cggaccacgg  40500 

acaccgagga gtacttccac gccatgcggg ccttctacga ccggcacgtc tgccggatcg  40560 

tgccctggcc ccgggacttc gccgccacct tcatggagat ctacaacgac ccgacggtct  40620 

acacgaccat gaacgggccg aacgagttcc atgtgatcgg caccctgcgc gactggtccg  40680 

tcgaggactg cctgcccgac atccaggtgc ccaccatggt cctcatcggc cgtcatgacg  40740 

aggccacccc cgcgaccgtc aagcccttcc tcgacctcgt gcccgacgtc cggtacgagg  40800 

tgctggagaa ctccagccac gtaccgcacc tggaggagcc cgagcggttc cacgaggtga  40860 

tgatcgacta cctcgaaagc ctggtgtgaa cgcgaccgtg gagacgacac agcacgacgt  40920 

cgaggggacc ggcgcggccg gcgcgaccgc gatgctcttc cccgggatgg gacccgccgc  40980 

gttctccgac gtcggccggt tcatggtgac caaccggtac accagggaac tcctcgcgga  41040 

ggccgacgac accctcggct actccctcgt cgaccggttc cggcaggccg agggcgacta  41100 

ctccgagtac gcccagatcg ccttcctggt caactgcgtc gccctcgccc gctgggccga  41160 

gcagaccatg gacctcaccc cccggatctg cgccggagcc agcttcggcg agaagtccgt  41220 

cgccgcctac agcggcgccc tcaccttcgc cgacgccgtc cggatgaccg ccggcctcgc  41280 

ccgctgtatg gacgagtact tccgtacgga gcacctcggg gtcgtcaccc actccttcgt  41340 

ccgcgcccct cgggagcggc tcgacgagat cctcgccgaa ctcgacgagc gcggcgaatg  41400 

gcacgagatc tcctgccaca tcgaccacga cttcttcatg ctcaccctcc atgaacgcaa  41460 

cagtgtctgg ctggagggcc ggctccggtc ggtgggcgcc atgccgctgt acgccatgcg  41520 

gcccccgatg cacgccgccg ccttcggcgg gctgcgcgac aaggccgagg aggaggtcat  41580 

cgcccccctc accttccacg acccgaccct gcccgtcgtc gccgaccagg acggcaaggt  41640 

gctgaccacc ggcgacgagg tgcgcaccat gctcctggag agcttcgtcc gcccgctgcg  41700 

ctggcccgac gtcatctcct cgctccagga ccagggcgtc acccgcgtct gtgtcgcggg  41760 

ccccgacagc ctcttcgggc gggtcggcac caccacccgc gccttcgagg tcatcgcggc  41820 

gaccccgcgg ctcgccctcc agccccgcgc gcgcaccacc tcgcgctgac cccgatcggg  41880 

gttccgcccg cccaccacgg cggcgggacc ccgggggtcc ccgcaccacg gccgcccggc  41940 

caccaccacc gtccgccccc ctgccggggg ccgaagggag cctcccatgt gggacgccca  42000 

gttcgagaac ctcctccgcc gctacctccc gttcctctcc gccgaccagc cgctggagca  42060 

ggacatcaac ctgcgtgaca tcggcctcga ctcgctcggc accgtcgagc tgctctccga  42120 

gctggagaac acctacgacg tccacttcca ggacgaggcg ctcaccaagg agaccttcga  42180 

gacccccggc gtgctctgga agaccctctc ccagatggtc gagccgcgcc actgaccacc  42240 

cggcccggcg cacaacccgg gccgccagcc cggcccgacg gaggaccgat gcacgccgcc  42300 

gaccacgccc tgcacgcccg cttcctgcgc gggctcgcct gcgcgcccga ccggcccgcc  42360 

gtacggttcg gcgggcggac cctgacgtac gcgcaggccc accgcaccgc cctgacctgg  42420 

gcgggttccc tgctgcgcgc cacgccggag cccccggccg ccgtcggtgt cctcgccgac  42480 

aagggcatcc ccgcctatct gggcatcctg accgcgctct acgccggcgc cgccgtcgtg  42540 

ccgctgcggc cggacttccc cgcggcccgt accgccgaga tgatgcgggc cgcgggggtc  42600 

accgccgtca tagccgacgg tcgtggccgg cggctgctcc ccgaactgct cgccgaccgc  42660 

cgggacaccg ccgtcctggc cgccgacgag gaaggcgccc ccgccgacga gagccccgcc  42720 

gacgggagcg ccccgggccg ccgtgtcgcg atcgacgagg ggtacgcgct caccgcgccc  42780 

cgggacgtcg tcccggacga caccgcgtac gtcctcttca cctccggctc caccgggcgg  42840 

cccaagggcg tgccgctcag ccacggcaac atcgcccact acttcgaggt cctcgacgcc  42900 

cgctacgact tcaccgcgga cgacgtcttc acccagacct tcgacctcaa cttcgactgc  42960 

tcgctcttcg acctgttctg cgcctggggc gccggcgcga gcgtcatcca gatcccgccc  43020 

caggcatacc gggacctgcc gtcccacctc gccgaacagg gcgtcaccgt ctggttctcc  43080 

accccgagca gcatcgcgct ggtgcgccgg ctcggcggtc tggcacccgg ctcactgccc  43140 

accctgcgct ggagcttctt cgcgggcgag gcactcaagt gcgccgacac ggaggactgg  43200 

cagcgcgccg cgcccgcctc cttcgtggag aacctgtacg gccccaccga actcaccgtc  43260 

accgtcaccg cccaccgctg gtccccggag gtctccccgg tcgtcggcgc caacggcgtc  43320 

gtccccatcg gccccctcca caagggcctg gaccacgtcc tgatcgacgc cggtggactg  43380 

ccccaccccg acaccgggga actctgcgtc accggacccc agatggcggg ccgctacctc  43440 

gaccccgccg acgaccacgg ccgcttcctc gaccacgacg ggcgccgctg gtaccgcacc  43500 

ggggaccggg tccgactggc ccccggcggg gaactcgtct acctcggccg gatggacgcc  43560 

caggtccaga tccagggctg gcgggtggag ctcgccgagg tcgatcacgc cctccagggg  43620 

tgcgagggcg tcggcgaggc cgtcaccgtc ggcgccgcca ccgacgcggg caccgagctg  43680 

gtcgtcttct acacggcccc cgccccggtg ccgcccgtcc gcttcgccgc cgtgctgcgc  43740 

gccaccctgc ccgacggtgt cgtaccacgg cactaccgcc atgtcgccga actgccgttg  43800 

aattccaacc gcaagatcga ccggcgagca ctgaccgcac gtgccgagga actcctcggc  43860 

tgagcacgtc cgagcggccg ggcaaccccc cggccgctca ctcattgccg caccccttac  43920 

agcgacaggc ccctaggggc cgctaggggt atgtcggccg gcccgcaccg ggctagcctc  43980 

actattgaca gacgtattcg ggggagttcg ccgtgtgtat tcaccagaca ggagagcggc  44040 

gttgaacagc gtggccaaca tggtgtccga caatgccgat aaggatctcc gctacggcgg  44100 

actcgtccac gatctcctgg cagactcagg aaaagcgaca ccgaattccg atgccatgga  44160 

agacgcattc ggaacctgga cctatcaaga gctgctgaac catagtcagg cattcagcgc  44220 

ctggctggac ggaaagggcg tcgcccgcgg cgaacgcatc gtcgtccagc tcccgaacat  44280 

ccgccagacg gtcgccgtgt tctacggagc ctgccgccgc ggcgtcgtgt tcgtcccgct  44340 

caacccgggc atgaagccct tccacctgcg gtccgtcatc gccgacgccg acccgcgcct  44400 

ggtcatcgcc gaggacgaga ccgcggccga ccggctgcgt gacgtcaccg acctgccggt  44460 

gtactccatc gactccctct gggcggatgt cgagcggctg cgcgacgcgg gcgccggagc  44520 

cgaggccgtc gaggtctccc cggaggatct ggccgtcctc atctacacct ccggctccac  44580 

cgcggccccc aaggcggtcg cctgccccca ccagcagatc gtgttcgccg cctcctcgat  44640 

caacgccgta ctcggctacc acgccgaaga catcgtcttc tgccggatgt cggtctcctg  44700 

ggacttcggt ctctacaagg tgctgatctc caccctcacc ggcgccaagc tcgtcctcgc  44760 

gggcggtgag cccgacatcg cgctcgtcaa gtccctccgc gagagcggcg ccacgatgat  44820 

gcccatcgtg ccgtccctgg cgagcatgct caccaccctc atccggcgcg accccgaggg  44880 

cgccccgacg ctgcggatgt tcaccaacag cgccgccgcg ctgccccagg tcaccatcga  44940 

cgccctgcgc tccgcgttcc ccggcgccca ggtcgtgcgc atgtacggcc agaccgagtg  45000 

caagcgcatc tcgatcatgc cgccgcatct ggagcacgag cgacccgact ccgtcggtct  45060 

gccgctgccc ggcaccacca tcgagatcct ggacgaggac ggcaccctcc tgccgcccgg  45120 

tgagcccggc gagatcaccg tcaccggacc ccatgtcatg gccggctact ggcgcgcgcc  45180 

cgagatcacc gcccgcgcct accgccgcga cgagaccacc ggcgcgatgc gcctgcacac  45240 

cggcgactac ggccacctcg acgaggacgg attcctctac ttcggcggcc ggcgcgacga  45300 

catgttcaag cgcaagggca cccggatgag caccgtcgag atcgaggccg cggccctcga  45360 

catccccggc gtcaccgccg ccgtggcgct gcccccgacc gccacccggg acctggccct  45420 

gtgtgtcgcg tccgacctcg aaccccatga cgtcctccgc agcctcgcgg agcggctcga  45480 

accggcgaag gtccccgcga cctgccgtat cgtcaacgac ttcccgctca ccctgaacgg  45540 

caagtccgag cgcaagcagc tcgcacgcct gctcgacggg agcgacaagt gaaccagtac  45600 

gaagaactcg ccgaccagta cggcaccccg ctctacgtct acgacctcga ccgcgtcgcc  45660 

gaggcccggc acgatctgcg cacctcactg cccgacgagg tcgagatcta ctacgccctc  45720 

aaggccaacc cccacccgca ggtcgccggc gccctgcgca gcggcgaggg ccgcgagtgc  45780 

cgcgccgaga tcagctccgt cggcgagctg gccgccgccc tcaccgccgg cttccgtgcc  45840 

tccgagatcc tctacaccgg ccccggcaag accgacggcg aactggacga agcgatcggc  45900 

aagggcgtca agaccttctg cgtcgaatcg ctgaccgacc tccagcacgt cggcgccgtc  45960 

gccctgcgac acggcgtcgt cgccgactgc ctgctgcgca tcaacagcgc caccgccagc  46020 

gccaccacca gcatccggat gaccggaacc ccctcacagt tcggcatcga cagcgagacc  46080 

ctcgtcgacg ccatgcccga actgcgcgcc gtacccggca cccggatcac gggcctgcac  46140 

ttcttccccc tcagcaacgc gagggacgag gccagcctca tcggcgagtt ccgccacacc  46200 

atcgcctacg cggccggcct cgccgaggag accggtctca ccctggaatt cctcgacatc  46260 

ggcggcggct tcgcccaccc ctacggcgcg cccggcgagc gccccgtcta ccgcgaactc  46320 

cgcaccgagc tggccgccgc cctcgacgag cacttcccgc actggcgcga gggcgccccg  46380 

cgcatcgcgg tggagaccgg ccgctaccag accagcggcg ccggaaccct gctcacccgg  46440 

gtcgtcaaca tcaaggtcag ccggggccgg aagttcgtcg tcatcgacgc cgggatcaac  46500 

accttcggcg gtatgtccgg cctcggccgg ctgctgccgg tcgccgtcga acccgagtac  46560 

accggctccg ccgaagccac cgaactcacc gatgtcgcca gcctcgccgg ccccctctgc  46620 

acccccggtg acatcctcgg ccgcgagatc cgcctgcccg aactggcccc cggcgacctc  46680 

gtgaccatcc ccaacgcggg cgcgtacggc gtcaccgcga gcctgctgat gttcctcggc  46740 

aggcccgcgc cggtcgaggt cgtcctgaag ggcggcaagg tcgtctccgc gtcccgactg  46800 

gagcaccacc gcactccggc gacccccgga taaccacggc cgaccacccg ccgcgccccc  46860 

ggtgacctcc gggggcggcc ggtaccgagc cccctgcgca ccacatccgg gaacgcccgc  46920 

cacgggcgtt cccgcctttt cccgcgccgt cgccaccgag cccgcgcgcg ccgcaccacg  46980 

tatgtcgccc gccttagcga ggagtaagcg aatgagcgag tccgagaacc ccgtttccgc  47040 

caccacagcc ggtgcggatg aaaccccgga cacgcgtacg gcgctggctc ggcggctggc  47100 

gggactgtcc cccgccgagc aggagcagca cctcgtcgac atggtgcacc ggcacacggt  47160 

cgccgcgctc caggccgtcg ccccgctcac tccggaccag gtcgatgtgc agcgcccgtt  47220 

cctggaactc ggcttcgact ccctcgccgc cgtggacctg cacaagcggc tcaccggcga  47280 

gaccggcctc gaactgccgg tgaccgtcgc cttcgacttc cccacccccg tactcgtcgc  47340 

cgaggagatc cgccggatcg ccttcggcat ccggcccgcc ccgctcgcgc ccgtcgtcgc  47400 

caccggcaac ctggacgacg accccatcgc gatcatcggc atcggctgcc gtttccccgg  47460 

cggcatcaac tccgccgagg aactgtggca gctcgtcatg gacgaggccg aggtgctctc  47520 

cggattcccc accaaccgtg gctgggacgt cgagggcatc tacgaccccg acccgggcaa  47580 

gcccggcaag agctacgtcc gcgaaggagg cttcctccag gacgcgggcg acttcgacgc  47640 

ggacttcttc gggatctcgc cgcgcgaggc cctcgccatg gacccgcagc agcggctcgt  47700 

cctggagacc gcctgggagg cgttcgaacg cgcgggcatc gaccccggct ccctccacgg  47760 

cagcaaggcc ggtgtcttca tcggcgccga ggtccatgag tacggtacgc gcgtccatga  47820 

agcccccgaa gggctcgacg gctacctcat gaccggcaac gcgcccagcg tcgcctccgg  47880 

ccggatcgcc tacagcctcg ggctcgaagg ccccgccgtc accatcgaca ccgcctgctc  47940 

gggctccctc gtcgccctgc acctcgccgc gcactcgctg cgccagggcg agtcctcgct  48000 

cgccatcgcc ggcggtgtga ccgtcatggg caaccccggc atgttcgccg ccttcagccg  48060 

gcagcgcggt ctcgccgccg acggccgctg caagcccttc gccgccgccg ccgacggcac  48120 

cggcttctcc gagggcgtcg gcgtcttcgt cgttgagcgc ctcgccgacg cccgccgcaa  48180 

cggccacccc gtgctgggca tcgtcaaggg ctccgccatc aaccaggacg gcgccagcaa  48240 

cggactgacc gccccgaacg gcccctcgca gcagcgcctc atcctccagg ccctcgccaa  48300 

cgccggtctg aagccggcgg acgtcgacac catggaggcc cacggcaccg gcaccaagct  48360 

gggtgacccg atcgaggccc aggccatcct ggcgacctac gggcaggagc gcgaagaggg  48420 

caggccgctc tggctcggct ccatcaagtc caacctcggc cacacccagg ccgcgggcgg  48480 

cgccgccagc ctcatcaaga tgctgatggg gatgcgccac ggcaagctgc cgcgcagcct  48540 

ccacatcgac gcgcccaccc cgcacgtcga ctggacgacc ggtgacgtcg cgctgctcac  48600 

cgagacccgc gactgggacg cccccgaccg cccccggcgc gccggtgtct ccgccttcgg  48660 

catcagcggc accaacgcgc acgtgatcat cgaggaggcg ccggagttcg agccgagcgc  48720 

cgtggagccg gtggccgggt cgggggtgac accgccgtgg gtgctgtcgg cccggtcggc  48780 

cgacgcgttg cgggggcagg ccgagcggct gctgtcgttc gtctccaccg acgccgatgt  48840 

ctccgtggtg gatgtggcgt actcactcgg tgtgtcgcgt gcgggcctgg aacaccgcgg  48900 

tgtggtgctg ggggagtcgc gcgaggaact gatcgcggct ctggagtcgc tggcgtccgg  48960 

tgccgaggcg ccgggtgtgg tgacgggtcg ggtcgccgag ggccggttgg cgttcctgtt  49020 

caccggccag ggtgcgcagc gcgtcggtat gggccgggaa ctcgccgccg aattccccgt  49080 

gttcgccgct tccctggaag agacctgcga cctgctggac gtgggcctgg aggaccagga  49140 

ccactcactg cgcgaggtgc tgttcgccga ggagggctcg gccgaggccg ccctgctgac  49200 

gcggacggtg tacgcccagg ccgcgttgtt cgcggtggag gtggcgctgt tccggctggt  49260 

ggagtcgttc ggtgtggtgc cggacttcgt cgccggtcac tcggtgggtg agatcgccgc  49320 

cgcacacgtc gcgggcgtgt tctcgctgga agacgccacc atgctcgtcg ccgcccgggg  49380 

ccggctgatg gacgccctgc cggagggcgg gacgatggtg gcggtgcagg ccaccgagga  49440 

ggatgtgctc gccctgctgg agggggtgga ggacgcctcc atcgccgcga tcaacggccc  49500 

cgacgccgtg gtcgtctccg gcaccgagac cggtgtcgcc cgggtggtcg acgtactccg  49560 

ggaccggggc gcgaagacca agcggctcga cgtcagccac gccttccact caccgctcat  49620 

ggagccgatg ctcaccgagt tccgccgggt ggccgaggtc ctcgaatacc aggcaccgcg  49680 

gatcgccgtg gtgtcgaacg tgtccggatc ggtcgccggc accgaactgg ccacgcccga  49740 

gtactgggtc acccacgtcc gcgaggccgt ccgcttcagc gccggcgtcc ggaccctgct  49800 

cggcgccggc gtctcctcct tcctggagat cggtccggac ggtgtgctca gcgggatggc  49860 

ccgtgggtcg gtctccgacg gcgccgacgt tggctgtgtc cccgtgatgc gccggggccg  49920 

gggtgaggtg cgggagttcc tgaccggcct ctcccggatc gccgtacgcg gagtcccggt  49980 

cacctgggag ccgctgatcg aaggcgcccg ccgcgtcgag ctgcccacct acgccttcca  50040 

gcgccgctgg ttctggctgg aggccggccg ctcgaccacg gacgccctgg gcctgggcca  50100 

gaccgccgcg gagcacccct tggtgggtgc cgtggtgggt ctggccggtg gtgatggtgt  50160 

cgtcctgacc ggtcgggtgt cgttgcacac ccacccctgg ttggcggatc accaggtcgc  50220 

cggggtgacg ctgctgccgg gtacgggctt cgtggagctg gcggtccgtg ccggtgacga  50280 

ggtcggctgt ggccggttgg aggaactgac gctggaggca ccgctcgtcg tgcccgaccg  50340 

gggcgccgtc cagctccagg tcgtcgtcgg cgcactggag gagtccgacg tccgcaccgt  50400 

cagcgtctac tcccgcgccg aggaggacga cgtctggacc cgccacgcca ccggattcgt  50460 

cggcgccgcc gtcgacggcg gactgaacct ggaggcatgg cccccgccgg gcgcccgggc  50520 

ggtggacgtc agcgacgtct acgccggact ggccgaccag ggctacggat acggtcccgt  50580 

cttccagggc ctccggtcgg tgtggcgcgg cgacggcgag gtgttcgccg aggtcgtgtt  50640 

gccggaaggt gcacaggcgg acgcctccgc attcgggctg caccccgccc tgctggacgc  50700 

cgcactgcac gccaccgact acctcgaccc ggagtccgcc gtcgagggca cgcatctgcc  50760 

gttcgcctgg accggtgtct cgctgcacgc caccggtgcg tccgaactgc gggtacggat  50820 

caccgccacc ggcaacgacg gatacgcgct cgacctcgcc gacaccaccg gccgccccgt  50880 

cgccaccgtc cagtcgctcg tgctgcgccc ggtcaccgag gagcagctcc gcagcgccca  50940 

gggcggcaac ggccccgaca gcctgttccg ggtggaatgg gcccccgtca ccgccgacct  51000 

caccgcatcc ggcgccggct gggccgtgct cggcgccggt gctcccgaac tcgccgccgc  51060 

cctcaccgcg gccggcaccc cgggcaccgc ctaccacggc acggccgagc tgagcgccgc  51120 

cgtcgacggt ggcaccaccc ccgatgtcgt cgccgtccag ttgccgtcgg ccggcgccgc  51180 

cgacgccgac ctcccggacg cagtccgcgc caccctgaac accgcgctgg agttcgtcca  51240 

gaactggctg gccgacgagc gtctcgccga gaccaggctc gtggtcgtca cccgcgacgc  51300 

cgtcaccgtc gacaccgccg cgggcggccc cgacctgacc gtcgcccccg tctggggact  51360 

gatccgctcc gcgcaggccg agaaccccgg ccgcatcctg ctcgccgaca tcgacggcac  51420 

cgaccagtcc cgtaccgccc tggccgcgat caccgccgcc gacgaacccg aactcgcctt  51480 

ccgcaacggc aacgcgtacg ccccccggct ggtcaggtcc gtcagcgagg gcggcctcgt  51540 

cccgccgtcg gacgccgcga gctggcgcct ggacgtgctg agccagggca ccctggagaa  51600 

cctcgccctc atccccagcg acgccgacga gcggaccctc gccccgggcg aggtccggat  51660 

cgccgtccgt gccgcgggag tcaacttccg tgacgtcctg gtggcgctcg ggatgtaccc  51720 

gaccaaggcg gacatcggtg gtgaggccgc cggtctcgta ctcgaagtcg gccccggtgt  51780 

caccgacttc acccccggcg accgggtgat gggtctcttc gacaccgcct tcggtccgca  51840 

cgcgatcacc gaccaccgca ccctggtgcc gatgcccacc ggctggacct acgcgcaggc  51900 

cgccacggcc ccgttggtct tcgccaccgc gtactacggc ctcgtggacc tcgccgaact  51960 

gcgctccggc gaatcggcgc tcatccacgc cgcggccggc ggcgtcggca tggcggccgt  52020 

ccagatcgcc cgccacctgg gcgccgaggt gtacggcacg gccagccccg gcaagtggaa  52080 

cgcgctgcgc gccgccggac tcgacgacaa ccacatcgcg tcgtcccgtg acaccacgtt  52140 

cgagcagaag ttcctcgcga actccggtgg ccgtggcgtc gatgtcgtcc tggacgccct  52200 

caccggcgaa ttcatcgacg cgtcactccg gctgctgccg cgcggtggac gcttcgccga  52260 

gatgggcaag accgatgtgc gcgacccgga gcgggtcgcg gccgagtacc ccggagtgcg  52320 

ctaccgggcc ttcgacctct tcgaggcgga cctcgaccgg ctccgcgaga tcctgcgcga  52380 

gctgctcgcc ctcttcgaga gcggtgcgct gcggccgctg ccggtgcgtg catgggacat  52440 

ccgcaagtcc aaggacgcct tccgccatat cgcccaggcc cggcacatcg gcaaggtcgc  52500 

cctcaccatg cccacgggtg gtttgggtga tggtgtggtg ttggtgacgg gtggtacggg  52560 

tgggttgggt gcgttggtgg cgcggcatgt ggtggtggtg catggggtgc gtcgtttggt  52620 

gttggtgtcg cgtcgtgggt tgggtgctcc gggtgcggtg gggttggtgg ctgagttgga  52680 

gggtttgggt gctgtggtgg aggtggtggc gtgtgatgtg agtgatcgtg tggcgttggc  52740 

gggtgtggtg gggggtattg ggtcggatct gtcggctgtg gtgcatacgg cgggtgtggt  52800 

ggatgacggt gtggtgggtt cgttgtcggt ggggcggttg tcgtcggtgt tgggtccgaa  52860 

ggcggatgcg gcgtggtatt tgcatgagtt gacggtgggg ttggatctgt cggcgtttgt  52920 

gttgttctcg tcggttgctg gtgtggtgga tggtgcgggt caggggaatt atgcggcggc  52980 

gaatgtgttt ttggatgggt tggctgtggt gcggcgtggt ttggggttgc cgggtacgtc  53040 

ggtggcgtgg gggttgtggg agggggctgg tatgggtgcg gtgttgggtg aggctgatgt  53100 

gttgcggatg agtcgttcgg gtgtgttggg gttgtcggtg ggtgaggggt tggggttgtt  53160 

tgatgtggcg ttgggtgagg atgtggcggc gttggtgccg gtgcggttgg atttgggggc  53220 

tttgcgttcg cgggttgatg gggtgcctgc ggtgttccgg tcgttggtgc gggtgccggt  53280 

gcgtcgttcg gtgggtgtgg gtgtttcggg tggtggtgag gtgtcgttgg agcggcgttt  53340 

ggtggtgttg gatgcgggtg agcgtgagcg ggtgttgttg gagttggtgc ggtcgcatgt  53400 

ggcggctgtg ttgggttatg agggtgcggg gtcgattgag ccgggtcgtg cgttcagtga  53460 

tatcgggttc gattcgttgt cggcggttga gctgcggaat cgtttgaatg gtgagacggg  53520 

gctgcggctg ccggcgacgc tgatcttcga ttaccccacc cctcaagccc tcgccgaata  53580 

cgtcatcgtc gccctgctcg gcgaggaggc ggccaacgcc cccgccctgc cgcccaccga  53640 

ggcccccacc gtcaccggaa ccgatgacga ccccgtggtc atcgtcggca tgggctgccg  53700 

cttccccggc gacgtccgta cccccgagga cctgtggcga ctggtctcca acggcagcga  53760 

cgccgtgacc cccttccccg acaaccgcgc ctgggacatc gaaggcatct acgacccgct  53820 

gcccggcgtg tccgggaaga cgtacgcccg cgagggcggc ttcctgcacg acgcggccga  53880 

gttcgacccc gagttcttcg ggatctcgcc gcgtgaggcc ctcgccatgg acccccagca  53940 

gcgactgctc cttgagacgt cctgggaggc catcgagcgg gcgggcatcg acccgaacag  54000 

cctgcgcgga acccagaccg gcgtcttcgc cggagtcatg cagaccgact acggcaacgg  54060 

cggcgcccgg ctcgccgagg acgtcgaggg ctacatcgcc aacggcacgc tcggcagcat  54120 

cgtctccggc cgggtctcct acgccctggg tctggagggc ccggcggtca cgatcgacac  54180 

cgcctgctcc tcctccctcg ttgccatgca ctgggcggcc cacgccctgc ggcagggcga  54240 

gtgctcgctc gccctggccg gcggcgtgac cgtcatgtcg acgccggaga ccttcgtcga  54300 

cttcagcctt cagcgcggcc tcgctcccaa cggtcggtgc aaggcgttct cggcggacgc  54360 

cgacggcacc ggctggggcg agggcgtcgg cgtcctggtc cttgagcggt tgtcggacgc  54420 

ccgccggaac gggcatcagg tactcgcggt catccgtggt tccgcgctga accaggacgg  54480 

tgcgagcaac ggcctgacgg ctccgaatgg tccctcgcag cagcgggtga tccgccaggc  54540 

cctcgtgagc gccggtctga ccacgtcgga cgtcgacgcg gtcgaggcgc acggcaccgg  54600 

caccacgctc ggtgacccga tcgaggccca ggcgctgctg gccacctacg gccaggagcg  54660 

ggacgcggac cagccgctct ggctcggctc cgtcaagacg aacgtgggtc acacgcaggc  54720 

cgcggccggt gttgccggtg tgatcaagat ggtgctcgcg atgcgggccg gtgtgctgcc  54780 

gaagacgctg catgtcaccg agccgtcgcc gcacgtggac tggtccgccg gcgccgtgga  54840 

gctgctgacg gagacgcgcg actggccgga gaccggccgt ccgcgccgcg ccggtgtgtc  54900 

gtcgttcggt gtgagcggca cgaacgcgca cgtcatcgtc gagcaggcac ccgccgtcga  54960 

agaggagccg acgcgcgccc ttccggcact cccggtcccg tggtccatct cggccaagtc  55020 

ggccgacgca ctgcgcggcc aggcccaggc cctgtcgtcg ttcgtctctg ccgccggtga  55080 

tgtgtcggtg gtggatgtgg cgtactcgct gggtgtgtcg cgtgcgggtc ttgagcatcg  55140 

tggtgtggtg gtgggggagt cgcgtgcgga gttgctcgtg gctctggagt cgttggcgtc  55200 

cggggttgag tcgccgggtg tggtgacggg gcgggtcgcc gagggtcggt tggcgttcct  55260 

gttcacgggg cagggtgcgc agcgggtcgg catgggtcgg gaactcgctg ccgaattccc  55320 

ggtgttcgcg gcgtctcttg agcagacgtg tgacttgttg gagcgtgccg gggttgcggt  55380 

gcgtgaggtg ctgttcgctg aggagggttc ggccgaggcc gccctgctga cgcggacggt  55440 

gtatgcgcag gctgcgttgt tcgccgtcga ggtggcgctg ttccggttgg tggagtcgtt  55500 

cggtgtggtg ccggactttg tcgccgggca ttcggtgggt gagatcgccg ccgcgcatgt  55560 

cgcgggcgtg ttctcgcttg aggatgcggt gtccctggtc gcggctcgtg gtcggttgat  55620 

ggatgcgctg ccggagggtg gggcgatggt ggcggtgcag gccaccgagg aggatgtgct  55680 

tgccctgttg gagggggtgg aggacgcctc catcgccgcg atcaacggcc ccgacgccgt  55740 

ggtggtctcc ggcaccgaga ccggtgtcgc ccgcgtagtg gacgtactcc gggagcgggg  55800 

tgcgaagacc aagcggctcg tggtgagtca tgccttccac tcgccgctga tggagccgat  55860 

gctcgccgac ttcgccaccg tcgtggaggg gctctcgtac aaggctcccg ccatcccggt  55920 

cgtgtcggga tcagttgtcg ggagcgagtt gtcgacgccg ggttactggg tgcggcatgt  55980 

tcgtgaggcg gttcgtttcg gtgcaggggt ggagaccctg ctcggcgctg gtgtgtcgtc  56040 

gttcctggag atcggtccgg acggtgtgct gagcgggatg gcccgtacgt ccgtgcctga  56100 

gggtgcggat gtggagtgcg cgccgctgat gcgccgggac cgcgccgagg tgcgggagtt  56160 

cctgaccggt ctctcccgtc tcgccgtacg cggtgtcccg gtcgcctggg agtcgctggt  56220 

cgaaggcggc cggcgggtcg agctgccgac gtacgccttc cagcgtcgcc ggttctggct  56280 

ggaggccggc cgttcggtga cggatgcttc gggtctgggc cagaccgccg cggagcaccc  56340 

cttggtgggt gccgtggtgg gtctggccgg tggcgatggt gtggtgctga ccggtcgggt  56400 

gtcgttgcac acccacccct ggttggcgga tcaccaggtc gcgggggtga cgctgctgcc  56460 

gggtacgggc tttgtggagc tggcggtccg tgccggtgac gaggtcggct gtggccggct  56520 

ggaggaactg acgctggagg ccccgctggt cgtgcccgac cggggcgcgg tgcagctcca  56580 

ggtcgtcgtc ggcgcactgg agacgtccgg tgtccgtacc gtcagcgtct actcccgcgt  56640 

ggaggaagag agcgcggatg acacctgggt ccgccacgcg accggcgcgc tcatggccgc  56700 

cgccgaggag cccggattcg acctcaccgc atggccgccg gctggtgcgc gggcggtcga  56760 

tgtgagtgac gcttacgccg gactggcgag ccagggctac gggtacggac ccgtcttcca  56820 

ggggctgacg gccgcctggc gcaagggccg ggaggtcttc gcggagatca cgctgccgga  56880 

ggccgcgcag gtggacgctt cggcgttcgg gctgcacccc gcgctgctgg acgctgcgct  56940 

gcacgccacc gactacctcg atcaggagag cgccgagggc acgcatctgc cgttcgcgtg  57000 

gagcggtgtc tcgctgcacg ccgccggcgc gtccgcgctg cgggtacgga tcgtcgcgac  57060 

cggcaaggac ggatacgcgc tcgacctcgc cgacagcaca ggccgccccg tggccactgt  57120 

tcagtcgctg gtcacccgtc ccgtcaccgc ggaccaactg tccgaagcct cggccactca  57180 

gcaccagtcg ctcttccgga tggagtggac cgccacgacc gccccggccg cgaccgctga  57240 

tgtccgctgg gcgcttctcg gcgagccggt cgcggaactg ggcgacctcg cgggcttcgg  57300 

ccgtacgacc gcgtacgcct cgctcgccga cctggccgcc gccgacgcgg acaccgttcc  57360 

ggacctcgtc gtcctgccgc tgggcagccg gatggctgag ggaagtgacg taccggaagc  57420 

ggtacgggag aacctcggtc aggtcctggc gacgatccag cagtggaacg acgactcccg  57480 

gttcgacggc tcccggctcg tggtgctgac acacggtgcc gtctcggtct ccgacgatga  57540 

atcgctcacc gcactggatc tggctccggt ctggggtctg gtccgctcgg ccatggccga  57600 

gactcccggc cgcttcctgc tggtggacac cgatgggacc gacccgtcga ccgacgcgct  57660 

gcgtcatctg gccgaactcc aggaggccga gttcgcgctg cgcgagggcg agatacgcgt  57720 

acctcggctc gcgcgcgttc cggtggccgg agctggtgcc gacatcacgg gtggtttggg  57780 

tgatggtgtg gtgttggtga cgggtggtac gggtgggttg ggtgctgtgg tggcgcgtca  57840 

tgcggtggtg gtgcatgggg tgcgtcgttt ggtgttggtg tcgcgtcgtg ggttgggtgc  57900 

tccgggtgcg gtggggttgg tggctgagct tgagagcttg ggtgctgtgg tggaggtggt  57960 

ggcgtgtgat gtgagtgatc gtgtggcgtt ggctggtgtg gtggggggta ttgggtcgga  58020 

tctgtcggct gtggtgcata cggcgggtgt ggtggatgac ggtgtggtgg gttcgttgtc  58080 

ggtggggcgg ttgtcgtcgg tgttgggtcc gaaggcggat gcggcgtggt atttgcatga  58140 

gttgacggtg aggttggatc tgtcggcgtt tgtgttgttc tcgtcggttg ctggtgtggt  58200 

ggatggtgcg ggtcagggga attatgcggc ggcgaatgtg tttttggatg ggttggctgt  58260 

ggtgcggcgt ggtttggggt tgccgggtac gtcggtggcg tgggggttgt gggagggggc  58320 

tggtatgggt gcggtgttgg gtgaggctga tgtgttgcgg atgagtcgtt cgggtgtttt  58380 

ggggttgtcg gtgggtgagg ggttggggtt gtttgatgtg gcgttgggtg aggatgtggc  58440 

ggcgttggtg ccggtgcggt tggatttggg ggctttgcgt tcgcgggttg atggggtgcc  58500 

tgcggtgttc cggtcgttgg tgcgggtgcc ggtgcgtcgt tcggtgggtg tgggtgtttc  58560 

gggtggtggt gaggtgtcgt tggagcggcg tttggcggtg ttggatgcgg gtgagcgtga  58620 

gcgggtgttg ttggagttgg tgcggtcgca tgtggcggct gtgttgggtt atgagggtgc  58680 

ggggtcgatt gagccgggtc gtgcgttcag tgatatcggg ttcgattcgt tgtcggcggt  58740 

tgagctgcgg aatcgtttga atggtgagac ggggctgcgg ctgccggcga cgctgatctt  58800 

cgattacccc accccccaag ccctcgccga tctcatccag gagaagacgc tgggtctggt  58860 

cgacgccgcc gcggccaccg tgtccaccac ggtgtcccgc accgatgacg agcccatcgc  58920 

catcgtcggc atgggctgcc gctacccggg agacgtccgt acccccgagg agctgtggcg  58980 

gctcgtcgcc agcggcacgg acgccgtcag cctcttcccc gaggaccggg gctggaacgt  59040 

cgactccatc tacgacccga cgcccggcct gtccgggaag acgtacaccc gtgagggcgg  59100 

cttcctgcac gacgcggccg agttcgacgc cggcttcttc gggatctcgc cgcgcgaggc  59160 

cctcgccatg gacccgcagc agcgactgct ccttgagacg tcctgggagg cgatggagcg  59220 

ggccggcatc gacccgaaca gcctgcgcgg cacccagacc ggcgtcttcg ccgggatcat  59280 

gtaccacgac tacgggtccc gggtgaccca gccgtcggag gaggtcgagg gctacctcgg  59340 

caacggcagc gcgggcagca tcgcgtccgg ccgggtctcc tacaccttcg ggttcgaggg  59400 

tccggcggtc acggtcgaca ccgcctgttc ctcctcgctc gtcgccctcc actgggcggc  59460 

tcaggccctg cgccagggcg agtgcagcat ggcgctcgcg ggcggtgtga ccgtcatgtc  59520 

gacgccggag accttcgtcg acttcagcct ccagcgcggc cttgccacga acggccggtg  59580 

caaggcgttc tcgtccgacg cggacggaac tggctggggc gagggcgcgg gaatgctcct  59640 

gctggagcgg ttgtcggacg cgcggaagaa cgggcacgaa gtactcgcgg tcatccgtgg  59700 

ttcggcgctg aaccaggacg gtgcgagcaa tggtctgacg gcgccgaacg gtccttcgca  59760 

gcagcgggtg atccgccagg cgctggccaa cgccggtctg tcggccgccg aggtggacgc  59820 

ggtcgaggcg cacggtacgg gtacgaagct gggtgacccg atcgaggcgc aggcgctcct  59880 

ggcgacctac ggccaggagc gggacggcga ccagccgctg ctgctgggct cgatcaagtc  59940 

gaacgtcggc cacacgcagg cggccgccgg tgtcggcggt gtgatcaaga tggtgatggc  60000 

catcaggaac ggtgtgctgc cgaagacgct gcatgtcacc gagccgtcgc cgcacgtgga  60060 

ttggtccgct ggtgcggtgg agctgttggc ggaggctcgg gagtggcctg agacgggtcg  60120 

tccgcgtcgt gcgggtgtgt cgtcgttcgg tatcagtggg acgaatgcgc acgtgatcgt  60180 

ggagcaggcc cccaccgacc agccggcgcc gctgagcgag ccggttggtg atgtgccggg  60240 

tcttccggtg ccgtggatcg tctcggccaa gtccgcggag gcgttgcggg cgcaggcggg  60300 

tcggttgggt tcgttcttgg gtgagaccgg tgttgttgat gtgccggcgg tgggttggtc  60360 

gttggtgcgg ggtcgttcgg tgttcgcgca tcgggcggtt gtggtgggtg gtgagtggga  60420 

tgagctgttg gccggtgtgg ctcgggtcgc tgagggtgtg gatgactcgg ttgtgtcggg  60480 

tgtggcggat gtgtcggggc gtcgggtgtt tgtgttcccg gggcagggtt cgcagtgggt  60540 

tggtatggcg caggggttgt tggattcgtc ggtggtgttc acggagcgga tgacggagtg  60600 

tgctgcggcg ttggatccgt tggtggagtg gtcgttgttg gatgtggtgc ggggtgtgga  60660 

gggtgcggcg tcgttggagc gggtggatgt ggtgcagccg gtgttgtggg cggtgatggt  60720 

gtcgttggcg tcggtgtggc gttcggtggg tgtggtgccg gatgcggtgg tgggtcattc  60780 

gcagggtgag atcgcggctg ctgtggtggg tggttggttg tcgttggtgg atggtgcgcg  60840 

ggtggtggcg ttgcggtcgt tggcgattcg tgaggtgttg gcgggtggtg gtggcatggt  60900 

cgcggtccag gctgccgagg atgaggttgc tgggtggctt gagggtgtgg agggggtggg  60960 

gattgctgcg gtgaatggtc cgcgttcggt ggtgatctcg ggtacgcgtg cgggtttgga  61020 

tgcgtgtgtg gagttgtggt ctgggcgggg gacgtgggtg aagcgggttc cggtggacta  61080 

tgcctcgcat tcggctgagg tggagcgggt gcgtgagcgg gtgctggcgg atctggcgag  61140 

tgtgacgggt ttgtcggggt cggtgccgat gttgtcgacg atgacgggtg actggattgt  61200 

tgagggtcag gtcggggccg ggtattgggt ggagaatctg cgtcgtccgg tgttgttcgc  61260 

ggacgcgacg aggcggttgg cgtcggaggg cttcggtgcg ttcgtcgagg tgagcgcgca  61320 

tccggtcctg gtgatgggca tcgaggagac gatcgaggcg ctgaggtcgg gcgccgccga  61380 

tggtgcgaag tccggtgctg gtgaggagag ttcctccgct gtggtggcgg tggggacgtt  61440 

gcgtcgtggt gagggtggtt gggatcagtt cctgcgttcc ctcgcggggc tcttcgtccg  61500 

gggtgcggtg gcaccggatt gggagtcgtt gttgggtggt gtgcgtcctc gggttgattt  61560 

gccgacgtat gcgttccagc gtgagcggtt gtggctggat gcgggtgtgg tggcggggga  61620 

tgtgtcgggg ttgggtcagg tggtggtggg tcatccgttg ttgggtgctg gtgtgggtgt  61680 

tgctggtgag ggtgggggtg tgttgtttac gggtcgtttg gggttgggtt cgcatccgtg  61740 

gctgggtgat catgcggtgt cgggtgtggt gttgttgccg ggggctgcgt ttgtggagtt  61800 

ggtggtgcgt gcgggtgatg aggtggggtg tggtcggttg gaggagttga cgttggcggc  61860 

tccgttggtg gtgccggagc gtggttcggt gcggattcag gtggtggtgg gtgctggtga  61920 

tgggtcgggt gcgcgttcgg tgggtgtgtg gtcgtcggtg ggggatgagg gtgtgggtgg  61980 

ggagtgggtg tgtcatgcgt cgggtttgtt gacggctgat gtgggtgtgg cgccggtgtt  62040 

gggtggtgtg tggccgccgg tgggtggtgt ggcggtggat gtgtcgggtg tgtatgaggg  62100 

gttggcgttg gaggggtatg agtatgggtc ggtgtttcgg gggttgaggt cggtgtggcg  62160 

tcgtggggat gaggtttttg ctgaggtggc gttgggtgag ggtgtggggg tggaggggtt  62220 

tggtttgcat ccggcgttgt tggatgcggc gttgcaggct gctgggtttg gttcgtttgt  62280 

gccggagtcc gaggcagggt ctgaggcggg ttcgggtggg gtgcggttgc cgttctcgtg  62340 

gtcgggtgtg tcgttgtttg cgtcgggtgc ttcggtgggg cgggtgcggt tgtggccggt  62400 

gggtggggat ggttttggtg tggagttgtt tgatggggtg gggatgccgg tggcgcgggt  62460 

ggatgcgttg gtgacgcggg agattagtgc gggtcagttg ggtgcggctg ctggtgccgg  62520 

gtcgttggtg ggtggggagt cgttgttccg ggtggagtgg gctcctgtgt cgggtgtcgc  62580 

gccggcttct gctggtgtgg gtggttgtgt ggtggtgggt gcggggagtg tgttgtctgg  62640 

ttttggggag gtggttccgg atctggcggc ggtttccgcg ggttctgcgg atggggtggg  62700 

tgtgccgggg tgggtgttgg tggatgtgga tgcgtggttg ggtgcggatc tggctgtggg  62760 

tgtggtgtcg ggtgagggtg ttccggtggt ggcgcgtggt gtggtggcgc gggtgttggg  62820 

gttggtgcgg gagtggttgg gggatgagcg gtgggtgtcg tcgcggttgg tgtgggtgac  62880 

gcgtggtgcg gtgggtgctc gggtgttgga tgaggtgtcg ggtgtggtgt cgtcggggtt  62940 

gtgggggttg gtgcgggctg ctcagtcgga gcatccggac cggttcgcgc ttcttgatct  63000 

ggacagtgcc accgccgtgg atgccgttcg tgatggtgtg ttggggttgc tggcggctgg  63060 

tgagccgcag ttggtggtgc gtgagggtga ggtgctggcc gcacggctga cccccgccca  63120 

caccaccgat gaacccaccg gccaggagtt cggcaaggcg gcgaccggta cggtcctcgt  63180 

caccggtggc accggcggcc tcggtgccgt cgtcgcacgg cacctggtca ccgagcacgg  63240 

cgcacagcgt ctgctcctca ccagccgtcg cggtatcaac gcgccgggag ccgccgaact  63300 

cgtcgcggaa ctcgccgagc tgggtgccag ggccgacgtc gcagcctgcg acgtctcaga  63360 

ccgggcggca ctcaaggaac tgctcgccgg cgtaccgggg gacgcaccgc tcaccgcggt  63420 

cgtccacgcg gccggcgtgc tggacgatgg tgtgatcgag tcgatgacgg ccgatcgcct  63480 

ggacgccgtc atgcggccga aggtcgacgc ggcctggcat ctgcacgagc tgaccgccga  63540 

ccgggaattg gatgcgttcg tcctcttctc ctccgcggcc ggcacgctgg acggtgccgg  63600 

acagtccaac tacgcggcgg cgaatgtgtt cctggacgcg ctcgcgcagt accgccgtgg  63660 

tcagggtctg gcgggtctgt cgctggcctg gggcctgtgg ggcgagagca ccggcatggt  63720 

gggcgcgctg gagggttcgg acctcgaccg catcggccgc tccggcgtcc gggcgctgtc  63780 

gtcggccgag gggctcgcgc tcttcgacgc cgccgccgtg ctgggcgagc cggccgtact  63840 

gccggtcgcg ttggacctcg gcgtactccg gacacagccc cggaaccagg ttccggcgat  63900 

cctgcgcggg ttcgcggcgg gcccgacccg gcgcaccgcg gtcactggtg ggcccgagac  63960 

ggaccaggag gcgctcacgc ggcgcctcgc ttccctctcg cccgccgacc gggaccgctt  64020 

cctgttggat ctggtccgta cgcaggtggc cggggtgctc gggtactccg gtccggacgc  64080 

gatcgatccg cagcgcgggt tccaggagct gggcgtcgac tcgctggccg ccgtacagat  64140 

ccgtaaccgg ctcggcgcgg ccacgggtgt ccggccgccg acgacgctcg tcttcgacta  64200 

tccgaccccc gacgcggtgg ccgggtactt caaggagcac ctcgtcatcg aggaggagga  64260 

ctcgaccgcg gagctgatgc gggagatcgc ccggctggag gccgcggtca cctccgcggc  64320 

ctcatcggcg ggcggcgcgg gcctggcacc cgccgtggac cggctgcggg cgatggcggc  64380 

gaagctggcc gacgcggatg cccagcgggc cgacgaggac gacccgggcc tggagtccgc  64440 

gaccgcggac gaactgttcg acatcctcga cggtgagctg tccacggact ga          64492 

 
           
             2  
             355  
             PRT  
             Streptomyces halstedii sp.HC-34  
           
            2 

Val Lys Ala Leu Val Leu Ser Gly Gly Ser Gly Thr Arg Leu Arg Pro 
1               5                   10                  15 

Ile Thr His Thr Ser Ala Lys Gln Leu Val Pro Val Ala Asn Lys Pro 
            20                  25                  30 

Ile Leu Phe Tyr Val Leu Glu Ser Ile Ala Glu Ala Gly Ile Thr Asp 
        35                  40                  45 

Val Gly Ile Val Val Gly His Thr Ala Pro Glu Val Gln Asp Ala Val 
    50                  55                  60 

Gly Asp Gly Ser Ala Phe Gly Val Asp Val Thr Tyr Ile Ala Gln Asp 
65                  70                  75                  80 

Glu Pro Leu Gly Leu Ala His Ala Val Arg Ile Ser Arg Asp Tyr Leu 
                85                  90                  95 

Gly Asp Asp Asp Phe Val Met Phe Leu Gly Asp Asn Phe Ile Ile Asp 
            100                 105                 110 

Gly Val Thr Gly Leu Val Asp Arg Phe Arg Asp Glu Arg Pro Asp Ala 
        115                 120                 125 

Gln Ile Leu Leu Thr Arg Val Pro Asp Pro Arg Ala Phe Gly Val Ala 
    130                 135                 140 

Val Leu Asp Glu Gln Gly Arg Val Ile Gly Leu Glu Glu Lys Pro Glu 
145                 150                 155                 160 

His Pro Arg Ser Asp Leu Ala Leu Ala Gly Val Tyr Phe Phe Thr Pro 
                165                 170                 175 

Leu Ile His Glu Ala Val Trp Ala Val Lys Pro Ser Trp Arg Gly Glu 
            180                 185                 190 

Leu Glu Ile Thr Asp Ser Ile Gln His Leu Ile Asp Thr Gly Ala Asp 
        195                 200                 205 

Val Arg Ser His Ile Ile Asp Gly Tyr Trp Lys Asp Thr Gly Asn Val 
    210                 215                 220 

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

Ala Ile Asp Gly Asp Val Asp Ala Asp Ser Glu Ile Ile Gly Arg Val 
                245                 250                 255 

Val Ile Glu Lys Gly Ala Thr Val Lys Gly Ser Arg Ile Val Gly Pro 
            260                 265                 270 

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

Phe Thr Ser Val Ala Glu Asn Cys Arg Ile His Asp Ser Glu Leu Glu 
    290                 295                 300 

Phe Ser Ile Met Met Arg Asp Ser Ser Leu Thr Gly Ile Arg Arg Ile 
305                 310                 315                 320 

Glu Ala Ser Leu Ile Gly Arg His Val His Gly Thr Ala Val Pro Arg 
                325                 330                 335 

Val Pro Asn Ala His Arg Leu Val Leu Gly Asp His Ser Thr Phe Gln 
            340                 345                 350 

Ile Ser Ser 
        355 

 
           
             3  
             323  
             PRT  
             Streptomyces halstedii sp.HC-34  
           
            3 

Met Ser Thr Arg Leu Leu Val Thr Gly Ala Ala Gly Phe Ile Gly Ser 
1               5                   10                  15 

Ala Tyr Val Arg Gly Leu Leu Thr Asp Gln Pro Asp Leu Arg Val Thr 
            20                  25                  30 

Val Leu Asp Ser Leu Thr Tyr Ala Gly Asn Arg Ala Asn Leu Asp Leu 
        35                  40                  45 

Thr His Pro Ser Leu Asp Leu Val Glu Gly Asp Ile Cys Asp Thr Glu 
    50                  55                  60 

Leu Val Asp Arg Leu Thr Ala Glu Ala Asp Gln Ile Val His Phe Ala 
65                  70                  75                  80 

Ala Glu Ser His Val Asp Arg Ser Ile Thr Gly Ser Ala Glu Phe Ile 
                85                  90                  95 

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

His Gly Ile Asp Arg Phe Val His Ile Ser Thr Asp Glu Val Tyr Gly 
        115                 120                 125 

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

Ser Pro Tyr Ser Ala Ser Lys Ala Ser Ser Asp Leu Leu Ala Leu Ala 
145                 150                 155                 160 

Tyr His Arg Thr His Gly Leu Asp Val Arg Val Thr Arg Cys Ser Asn 
                165                 170                 175 

Asn Tyr Gly Pro Tyr Gln His Pro Glu Lys Val Ile Pro Leu Phe Val 
            180                 185                 190 

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

Asn Val Arg Asp Trp Leu His Val Glu Asp His Cys Ala Ala Ile Glu 
    210                 215                 220 

Cys Val Arg Thr Arg Gly Gly Ala Gly Glu Ile Tyr Asn Ile Gly Gly 
225                 230                 235                 240 

Gly Thr Glu Leu Ser Asn Arg Glu Leu Thr Gly Leu Leu Leu Glu Ala 
                245                 250                 255 

Cys Gly Ala Asp Trp Asp Ser Val Glu Tyr Val Thr Asp Arg Lys Gly 
            260                 265                 270 

His Asp Leu Arg Tyr Ser Val Asp Trp Ser Lys Val Ala Asp Leu Gly 
        275                 280                 285 

Tyr Thr Pro Ala His Asp Phe Arg Ala Gly Leu Ala Glu Thr Val Asp 
    290                 295                 300 

Trp Tyr Arg Ser Asn Arg Thr Trp Trp Glu Pro Ala Lys Tyr Gly His 
305                 310                 315                 320 

Ser Pro Ala 

 
           
             4  
             419  
             PRT  
             Streptomyces halstedii sp.HC-34  
           
            4 

Met Arg Val Leu Met Thr Val Phe Ala Asn Arg Ser His Leu Tyr Asn 
1               5                   10                  15 

Met Val Pro Leu Ala Trp Ala Leu Thr Thr Ala Gly His Glu Val His 
            20                  25                  30 

Ile Ala Ser His Pro Asp Asn Val Gln Ala Ile Ser Asp Ser Gly Leu 
        35                  40                  45 

Thr Ala Val Pro Val Gly Asn Asp Leu Asn Ile Met Ala Leu Ala Gln 
    50                  55                  60 

Ser Thr Pro Arg Glu Glu Met Val Asn Gly Gly Ala Leu Thr Leu Asn 
65                  70                  75                  80 

Glu Thr Arg Pro Glu Lys Leu Thr Trp Gln Tyr Ile His Asp Val Phe 
                85                  90                  95 

Ala Gln Tyr Ser Gln Ile Tyr Glu Tyr Met Ala Asp Ser Thr Met Thr 
            100                 105                 110 

Ala Asp Leu Val Ala His Ala Arg Gln Trp Gln Pro Asp Leu Val Ile 
        115                 120                 125 

Trp Asp Ala Leu Thr Tyr Ala Gly Pro Ile Ala Ala Glu Ala Val Gly 
    130                 135                 140 

Ala Pro His Val Arg Met Leu Phe Gly Leu Asp Gln Trp Gly Arg Met 
145                 150                 155                 160 

Arg Asp His Phe Asn Arg Leu Thr Gly Glu Arg Ala Ala Asp Asp Arg 
                165                 170                 175 

His Asp Pro Leu Ala Asp Trp Leu Ala Thr Lys Gly Glu Pro His Gly 
            180                 185                 190 

Val Ala Phe Thr Glu Ser Leu Val Thr Gly Thr Thr Thr Leu Ala Val 
        195                 200                 205 

Ala Pro Pro Trp Met Ser Phe Pro Ser Glu Gln Pro Ala Leu Ser Met 
    210                 215                 220 

Arg His Leu Pro Phe Asn Gly Pro Ala Val Leu Pro Asp Trp Leu Arg 
225                 230                 235                 240 

Glu Ala Pro Ser Arg Pro Arg Val Cys Leu Thr Leu Gly Leu Thr Leu 
                245                 250                 255 

Arg Glu Leu Ala Asp Asp Asn Val Thr Leu Ala Asp Phe Val Asn Ala 
            260                 265                 270 

Val Ala Asp Ile Asp Ala Asp Val Val Ala Thr Phe Ser Ala Glu Gln 
        275                 280                 285 

Val Ala Glu Ile Gly Asp Leu Pro Asp Asn Val Arg Ala Val Asp Phe 
    290                 295                 300 

Val Pro Leu His Ala Leu Leu Pro Ser Cys Ala Ala Ile Val His His 
305                 310                 315                 320 

Gly Gly Gly Gly Thr Arg Thr Asn Ala Ile Arg Tyr Gly Val Pro Gln 
                325                 330                 335 

Leu Ile Val Pro Asn Trp Leu Trp Asp Glu Gly Tyr Val Ala Glu Arg 
            340                 345                 350 

Phe Ala Glu Arg Gly Ala Ala Leu Val Thr Glu Val Pro Asp Leu Thr 
        355                 360                 365 

Pro Asp Arg Leu Arg Asp Gln Leu Arg Arg Leu Ile Ala Glu Pro Ser 
    370                 375                 380 

Phe Lys Ala Ala Ala Glu Gln Ile Gln Lys Glu Tyr Asp Ala Leu Pro 
385                 390                 395                 400 

Ser Leu Thr Glu Thr Val Gly Glu Leu Val Arg Val Ala Glu Arg Gly 
                405                 410                 415 

Arg Ser Leu 

 
           
             5  
             2260  
             PRT  
             Streptomyces halstedii sp.HC-34  
           
            5 

Val Glu Asn Glu Lys Lys Leu Leu Asp Tyr Leu Lys Arg Ala Thr Thr 
1               5                   10                  15 

Asp Leu Arg Glu Ala Arg Arg Arg Leu Arg Glu Met Glu Glu Lys Asp 
            20                  25                  30 

Gln Glu Pro Ile Ala Ile Val Gly Ile Gly Cys Arg Phe Pro Arg Gly 
        35                  40                  45 

Val Glu Ser Ala Glu Gln Leu Trp Asp Leu Val Ala Asp Gly Gly Glu 
    50                  55                  60 

Ala Leu Thr Pro Phe Pro Glu Asp Arg Gly Trp Asp Thr Asp Ser Leu 
65                  70                  75                  80 

Tyr His Pro Asp Pro Glu His Leu Gly Thr Ser Tyr Thr Asn Val Gly 
                85                  90                  95 

Ala Phe Leu His Asp Ala Ala Glu Phe Asp Pro Gly Phe Phe Gly Ile 
            100                 105                 110 

Ser Pro Arg Glu Ala Leu Ala Met Asp Pro Gln Gln Arg Leu Leu Leu 
        115                 120                 125 

Glu Thr Ser Trp Glu Ala Met Glu Arg Ala Gly Ile Asp Pro Ala Gly 
    130                 135                 140 

Leu Arg Gly Ser Arg Thr Gly Val Phe Thr Gly Leu Met Tyr Phe Asp 
145                 150                 155                 160 

Tyr Gly Ser Arg Val His Ser Ala Pro Glu Asp Ile Glu Gly Tyr Leu 
                165                 170                 175 

Gly Asn Gly Ser Ala Gly Ser Ile Ala Ser Gly Arg Val Ala Tyr Thr 
            180                 185                 190 

Phe Gly Phe Glu Gly Pro Ala Val Thr Leu Asp Thr Ala Cys Ser Ser 
        195                 200                 205 

Ser Leu Val Ala Ile His Leu Ala Ala Gln Ser Leu Arg Lys Gly Glu 
    210                 215                 220 

Cys Thr Leu Ala Leu Ala Gly Gly Ala Ser Val Met Ser Thr Pro Asp 
225                 230                 235                 240 

Ile Phe Val Asp Phe Ser Arg Gln Arg Gly Leu Ser Ala Asp Gly Arg 
                245                 250                 255 

Cys Lys Ala Phe Ser Ser Asp Ala Asp Gly Thr Gly Trp Gly Glu Gly 
            260                 265                 270 

Val Gly Val Leu Leu Leu Glu Arg Leu Ser Asp Ala Arg Lys Asn Gly 
        275                 280                 285 

His Arg Ile Leu Gly Leu Val Arg Gly Ser Ala Val Asn Gln Asp Gly 
    290                 295                 300 

Ala Ser Ser Gly Leu Thr Ala Pro Asn Gly Pro Ser Gln Gln Arg Val 
305                 310                 315                 320 

Ile Arg Gln Ala Leu Ala Asn Ala Gly Leu Ser Ala Ala Glu Val Asp 
                325                 330                 335 

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

Ala Gln Ala Leu Leu Ala Thr Tyr Gly Gln Glu Arg Glu Glu Gly Arg 
        355                 360                 365 

Pro Leu Trp Leu Gly Ser Ile Lys Ser Asn Val Gly His Thr Gln Ala 
    370                 375                 380 

Ala Ala Gly Val Ala Gly Val Ile Lys Met Val Leu Ala Met Arg Ala 
385                 390                 395                 400 

Gly Val Leu Pro Lys Thr Leu His Val Ser Glu Pro Ser Pro His Val 
                405                 410                 415 

Asp Trp Ser Ala Gly Ala Val Glu Leu Leu Thr Glu Thr Arg Asp Trp 
            420                 425                 430 

Pro Glu Thr Gly Arg Pro Arg Arg Ala Gly Val Ser Ser Phe Gly Ile 
        435                 440                 445 

Ser Gly Thr Asn Ala His Val Ile Val Glu Gln Ala Pro Met Asp Glu 
    450                 455                 460 

Ala Met Asp Glu Val Ala Gly Glu Arg Glu Thr Pro Ala Ala Gly Ser 
465                 470                 475                 480 

Asp Arg Thr Val Pro Trp Val Ile Ser Ala Lys Ser Ala Asp Ala Leu 
                485                 490                 495 

Arg Ala Gln Ala Gly Arg Leu Ser Thr Phe Leu Ala Gly Thr Glu Gly 
            500                 505                 510 

Thr Leu Thr Thr Gly Ile Ser Ser Glu Thr Ser Val Ala Ala Val Ser 
        515                 520                 525 

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

Phe Ala His Arg Ala Val Val Val Gly Gly Glu Trp Asp Ala Leu Leu 
545                 550                 555                 560 

Ala Ser Ile Gly Glu Leu Ala Asp Gly Ala Glu Asp Gly Ser Gly Ala 
                565                 570                 575 

Ala Ser Gly Ser Val Val Ser Gly Val Ala Asp Val Ser Gly Arg Arg 
            580                 585                 590 

Val Phe Val Phe Pro Gly Gln Gly Ser Gln Trp Val Gly Met Ala Gln 
        595                 600                 605 

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

Ala Ala Ala Leu Asp Pro Leu Val Glu Trp Ser Leu Leu Asp Val Val 
625                 630                 635                 640 

Arg Gly Val Glu Gly Ala Ala Ser Leu Glu Arg Val Asp Val Val Gln 
                645                 650                 655 

Pro Val Leu Trp Ala Val Met Val Ser Leu Ala Ser Val Trp Arg Ser 
            660                 665                 670 

Val Gly Val Val Pro Asp Ala Val Val Gly His Ser Gln Gly Glu Ile 
        675                 680                 685 

Ala Ala Ala Val Val Gly Gly Trp Leu Ser Leu Val Asp Gly Ala Arg 
    690                 695                 700 

Val Val Ala Leu Arg Ser Leu Ala Ile Arg Glu Val Leu Ala Gly Gly 
705                 710                 715                 720 

Gly Gly Met Val Ala Val Gln Ala Ala Glu Asp Glu Val Ala Gly Trp 
                725                 730                 735 

Leu Glu Gly Val Glu Gly Val Gly Ile Ala Ala Val Asn Gly Pro Arg 
            740                 745                 750 

Ser Val Val Ile Ser Gly Thr Arg Ala Gly Leu Asp Ala Cys Val Glu 
        755                 760                 765 

Leu Trp Ser Gly Arg Gly Thr Trp Val Lys Arg Val Pro Val Asp Tyr 
    770                 775                 780 

Ala Ser His Ser Ala Glu Val Glu Arg Val Arg Glu Arg Val Leu Ala 
785                 790                 795                 800 

Asp Leu Ala Ser Val Thr Gly Leu Ser Gly Ser Val Pro Met Leu Ser 
                805                 810                 815 

Thr Met Thr Gly Asp Trp Ile Val Glu Gly Gln Val Gly Ala Gly Tyr 
            820                 825                 830 

Trp Val Glu Asn Leu Arg Arg Pro Val Leu Phe Ala Asp Ala Thr Arg 
        835                 840                 845 

Arg Leu Ala Ser Glu Gly Phe Gly Ala Phe Val Glu Val Ser Ala His 
    850                 855                 860 

Pro Val Leu Val Met Gly Ile Glu Glu Thr Ile Glu Ala Leu Arg Ser 
865                 870                 875                 880 

Gly Ala Ala Asp Gly Ala Lys Ser Gly Ala Gly Glu Glu Ser Ser Ser 
                885                 890                 895 

Ala Val Val Ala Val Gly Thr Leu Arg Arg Gly Glu Gly Gly Trp Asp 
            900                 905                 910 

Gln Phe Leu Arg Ser Leu Ala Gly Leu Phe Val Arg Gly Ala Val Thr 
        915                 920                 925 

Pro Asp Trp Glu Ser Leu Leu Gly Gly Val Arg Pro Arg Val Asp Leu 
    930                 935                 940 

Pro Thr Tyr Ala Phe Gln Arg Glu Arg Leu Trp Leu Asp Ala Gly Val 
945                 950                 955                 960 

Val Ala Gly Asp Val Ser Gly Leu Gly Gln Val Val Val Gly His Pro 
                965                 970                 975 

Leu Leu Gly Ala Gly Val Gly Val Ala Gly Glu Gly Gly Gly Val Leu 
            980                 985                 990 

Phe Thr Gly Arg Leu Gly Leu Gly  Ser His Pro Trp Leu  Gly Asp His 
        995                 1000                 1005 

Ala Val  Ser Gly Val Val Leu  Leu Pro Gly Ala Ala  Phe Val Glu 
    1010                 1015                 1020 

Leu Val  Val Arg Ala Gly Asp  Glu Val Gly Cys Gly  Arg Leu Glu 
    1025                 1030                 1035 

Glu Leu  Thr Leu Ala Ala Pro  Leu Val Val Pro Glu  Arg Gly Ser 
    1040                 1045                 1050 

Val Arg  Ile Gln Val Val Val  Gly Ala Gly Asp Gly  Ser Gly Ala 
    1055                 1060                 1065 

Arg Ser  Val Gly Val Trp Ser  Ser Val Gly Asp Glu  Gly Val Gly 
    1070                 1075                 1080 

Gly Glu  Trp Val Cys His Ala  Ser Gly Leu Leu Thr  Ala Asp Val 
    1085                 1090                 1095 

Gly Val  Ala Pro Val Leu Gly  Gly Val Trp Pro Pro  Val Gly Gly 
    1100                 1105                 1110 

Val Ala  Val Asp Val Ser Gly  Val Tyr Glu Gly Leu  Ala Leu Glu 
    1115                 1120                 1125 

Gly Tyr  Glu Tyr Gly Ser Val  Phe Arg Gly Leu Arg  Ser Val Trp 
    1130                 1135                 1140 

Arg Arg  Gly Asp Glu Val Phe  Ala Glu Val Ala Leu  Gly Glu Gly 
    1145                 1150                 1155 

Val Gly  Val Glu Gly Phe Gly  Leu His Pro Ala Leu  Leu Asp Ala 
    1160                 1165                 1170 

Ala Leu  Gln Ala Ala Gly Phe  Gly Ser Phe Val Pro  Glu Ser Glu 
    1175                 1180                 1185 

Ala Gly  Ser Glu Ala Gly Ser  Gly Gly Val Arg Leu  Pro Phe Ser 
    1190                 1195                 1200 

Trp Ser  Gly Val Ser Leu Phe  Ala Ser Gly Ala Ser  Val Gly Arg 
    1205                 1210                 1215 

Val Arg  Leu Trp Pro Val Gly  Gly Asp Gly Phe Gly  Val Glu Leu 
    1220                 1225                 1230 

Phe Asp  Gly Val Gly Met Pro  Val Ala Arg Val Asp  Ala Leu Val 
    1235                 1240                 1245 

Thr Arg  Glu Ile Ser Ala Gly  Gln Leu Gly Ala Ala  Ala Gly Ala 
    1250                 1255                 1260 

Gly Ser  Leu Val Gly Gly Glu  Ser Leu Phe Arg Val  Glu Trp Ala 
    1265                 1270                 1275 

Pro Val  Ser Gly Val Ala Pro  Ala Ser Ala Gly Val  Gly Gly Cys 
    1280                 1285                 1290 

Val Val  Val Gly Ala Gly Ser  Val Leu Ser Gly Phe  Gly Glu Val 
    1295                 1300                 1305 

Val Pro  Asp Leu Ala Ala Val  Ser Ala Gly Ser Ala  Ala Val Pro 
    1310                 1315                 1320 

Gly Trp  Val Leu Val Asp Val  Asp Ala Trp Leu Gly  Ala Asp Leu 
    1325                 1330                 1335 

Ala Val  Gly Val Val Ser Gly  Glu Gly Val Pro Val  Val Ala Arg 
    1340                 1345                 1350 

Gly Val  Val Ala Arg Val Leu  Gly Leu Val Arg Glu  Trp Leu Gly 
    1355                 1360                 1365 

Asp Glu  Arg Trp Val Ser Ser  Arg Leu Val Trp Val  Thr Arg Gly 
    1370                 1375                 1380 

Ala Val  Gly Ala Arg Val Leu  Asp Glu Val Ser Gly  Val Val Ser 
    1385                 1390                 1395 

Ser Gly  Leu Trp Gly Leu Val  Arg Ala Ala Gln Ser  Glu His Pro 
    1400                 1405                 1410 

Asp Arg  Phe Ala Leu Leu Asp  Leu Asp Ser Ala Thr  Ala Val Asp 
    1415                 1420                 1425 

Ala Val  Arg Asp Gly Val Leu  Gly Leu Leu Ala Ala  Gly Glu Pro 
    1430                 1435                 1440 

Gln Leu  Val Val Arg Glu Gly  Glu Val Leu Ala Ala  Arg Leu Thr 
    1445                 1450                 1455 

Pro Ala  His Thr Thr Asp Ala  Leu Ile Pro Leu Ala  Asp His Ala 
    1460                 1465                 1470 

Pro Trp  Arg Leu Ala Lys Asp  Pro Gly Gly Ser Leu  Asp Ala Leu 
    1475                 1480                 1485 

Thr Val  Val Pro Ala Pro Asp  Val Leu Glu Pro Leu  Thr Glu Gly 
    1490                 1495                 1500 

Gln Val  Arg Ile Ala Val Arg  Ala Ala Gly Val Asn  Phe Arg Asp 
    1505                 1510                 1515 

Val Leu  Met Ala Leu Gly Met  Val Pro Ala Arg Gly  Thr Gln Leu 
    1520                 1525                 1530 

Gly Gly  Glu Ala Ala Gly Val  Val Thr Ala Val Gly  Pro Gly Val 
    1535                 1540                 1545 

Thr Gly  Ile Ala Val Gly Asp  Arg Val Met Gly Val  Phe Asp Gly 
    1550                 1555                 1560 

Pro Phe  Gly Pro Val Ala Val  Ala Asp Arg Arg Met  Val Ser Arg 
    1565                 1570                 1575 

Ile Pro  Asp Ala Trp Ser Tyr  Thr Glu Ala Ala Thr  Ile Pro Leu 
    1580                 1585                 1590 

Val Tyr  Leu Thr Ala Tyr Tyr  Gly Leu Val Asp Leu  Ala Ala Leu 
    1595                 1600                 1605 

Gln Gln  Gly Gln Arg Ile Leu  Val His Ala Ala Thr  Gly Gly Val 
    1610                 1615                 1620 

Gly Met  Ala Ala Val Gln Leu  Ala Arg His Phe Gly  Ala Glu Val 
    1625                 1630                 1635 

Tyr Gly  Thr Ala Ser Pro Gly  Lys Trp Asp Thr Leu  Arg Ala Met 
    1640                 1645                 1650 

Gly Phe  Asp Glu Ala His Met  Ala Ser Ser Arg Ser  Leu Asp Phe 
    1655                 1660                 1665 

Glu Asp  His Phe Trp Gln Thr  Thr Gly Gly Glu Gly  Phe Asp Val 
    1670                 1675                 1680 

Val Leu  Asn Ser Leu Ala Gln  Glu Tyr Val Asp Ala  Ser Leu Arg 
    1685                 1690                 1695 

Leu Gln  Pro Arg Gly Gly Arg  Phe Leu Glu Met Gly  Lys Thr Asp 
    1700                 1705                 1710 

Ile Arg  Asp Ala Asp Glu Val  Ala Ala Ala His Glu  Gly Val Arg 
    1715                 1720                 1725 

Tyr Glu  Ala Tyr Asp Leu Thr  Val Phe Thr Ser Val  Asp Gly Pro 
    1730                 1735                 1740 

Gly Ala  Ile Pro Glu Arg Ile  Gln Glu Met Leu Ser  Glu Leu Leu 
    1745                 1750                 1755 

Ala Leu  Phe Asp Lys Gly Val  Leu Thr Pro Leu Pro  Val Thr Thr 
    1760                 1765                 1770 

Trp Asp  Val Arg Arg Ala Ser  Ala Ala Leu Arg His  Met Ser Gln 
    1775                 1780                 1785 

Ala Arg  His Thr Gly Lys Ile  Ala Leu Thr Val Pro  Arg Pro Leu 
    1790                 1795                 1800 

Asp Gln  Asp Gly Thr Val Leu  Val Thr Gly Gly Thr  Gly Val Leu 
    1805                 1810                 1815 

Gly Ser  Leu Leu Ala Arg His  Leu Val Thr Glu His  Gly Val Arg 
    1820                 1825                 1830 

Asn Leu  Leu Leu Val Ser Arg  Arg Gly Gly Asp Ala  Pro Gly Ala 
    1835                 1840                 1845 

Ala Glu  Leu Val Ala Glu Leu  Thr Ala Ala Gly Ala  Glu Val Ser 
    1850                 1855                 1860 

Val Val  Ala Cys Asp Thr Ala  Asp Arg Ala Ala Leu  Glu Lys Leu 
    1865                 1870                 1875 

Leu Ala  Ser Val Pro Gly Asp  Ala Pro Leu Thr Gly  Val Phe His 
    1880                 1885                 1890 

Thr Ala  Gly Val Leu Asp Asp  Gly Ile Val Glu Ala  Met Thr Pro 
    1895                 1900                 1905 

Glu Arg  Val Asp Ala Val Met  Arg Pro Lys Val Asp  Ala Ala Trp 
    1910                 1915                 1920 

His Leu  His Glu Leu Thr Glu  Gly Leu Asp Leu Ala  Ala Phe Val 
    1925                 1930                 1935 

Leu Tyr  Ser Ser Ala Ala Gly  Val Ser Gly Asp Ala  Gly Gln Ser 
    1940                 1945                 1950 

Asn Tyr  Ala Ala Ala Asn Val  Phe Leu Asp Ala Leu  Ala Gln Arg 
    1955                 1960                 1965 

Arg Arg  Ala Ala Gly Leu Pro  Gly Gln Ser Leu Ala  Trp Gly Leu 
    1970                 1975                 1980 

Trp Asp  Asp Arg Ser Glu Met  Thr Gly His Leu Gly  Asp Ala Glu 
    1985                 1990                 1995 

Ile Ala  Arg Met Thr Glu Ala  Gly Val Leu Gly Phe  Thr Ala Ala 
    2000                 2005                 2010 

Asp Gly  Leu Ala Ala Leu Asp  Arg Ala Ala Met Tyr  Asp Asp Ala 
    2015                 2020                 2025 

Val Leu  Val Pro Met Lys Leu  Asp Thr Ala Thr Leu  Gly Ala Gly 
    2030                 2035                 2040 

Ser Ser  Pro Val Pro His Leu  Phe Arg Gly Leu Val  Arg Thr Pro 
    2045                 2050                 2055 

Val Val  Arg Arg Ala Val Ala  Gly Asn Thr Gly Gly  Asp Ser Gly 
    2060                 2065                 2070 

Gly Gly  Leu Glu Gln Arg Leu  Ala Ala Leu Thr Ala  Ala Glu Arg 
    2075                 2080                 2085 

Thr Glu  Thr Val Leu Glu Leu  Val Arg Glu Arg Val  Ala Ala Val 
    2090                 2095                 2100 

Leu Gly  His Ala Ser Ala Asp  Ala Ile Asp Pro Ala  Arg Ala Phe 
    2105                 2110                 2115 

Lys Glu  Ile Gly Phe Asp Ser  Leu Thr Ala Val Glu  Leu Arg Asn 
    2120                 2125                 2130 

Arg Leu  Asn Ala Ala Thr Gly  Leu Arg Leu Pro Ala  Thr Leu Val 
    2135                 2140                 2145 

Phe Asp  Tyr Pro Thr Pro Thr  Val Leu Ser Gln Tyr  Leu Leu Ala 
    2150                 2155                 2160 

Glu Leu  Ala Pro Gly Leu Pro  Ala Glu Asp Pro Val  Gly Thr Arg 
    2165                 2170                 2175 

Leu Leu  Glu Gln Ile Ala Arg  Ile Glu Ala Val Leu  Ser Glu Val 
    2180                 2185                 2190 

Ser Glu  Val Thr Asp Glu Thr  Ser Ser Leu Ser Asp  Met Asp Ala 
    2195                 2200                 2205 

Asp Ala  Arg Ser Gly Ile Thr  Ala Arg Leu Asn Asp  Ile Leu Thr 
    2210                 2215                 2220 

Ala Trp  Asn Arg Ala Gln Arg  Ala Pro Gly His Asp  Ala Val Ala 
    2225                 2230                 2235 

Ala Glu  Leu Asp Asp Ala Ser  Asp Asp Glu Ile Phe  Asp Phe Ile 
    2240                 2245                 2250 

Asp Ser  Thr Phe Gly Lys Ser 
    2255                 2260 

 
           
             6  
             3362  
             PRT  
             Streptomyces halstedii sp.HC-34  
           
            6 

Met Ala Asn Glu Ala Lys Leu Arg Glu Tyr Leu Lys Arg Val Thr Thr 
1               5                   10                  15 

Asp Leu His Glu Thr Asn Glu Arg Leu Arg Glu Val Glu Gly Arg Ala 
            20                  25                  30 

Asn Glu Pro Ile Ala Ile Val Gly Met Ser Cys Arg Phe Pro Gly Gly 
        35                  40                  45 

Val Glu Ser Pro Glu Gln Leu Trp Glu Leu Phe Arg Thr Gly Thr Asp 
    50                  55                  60 

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

Tyr His Pro Asp Pro Asp His Ala Gly Thr Ser Tyr Thr Arg Glu Gly 
                85                  90                  95 

Gly Phe Val His Gly Ala Glu Arg Phe Asp Pro Ser Leu Phe Gly Ile 
            100                 105                 110 

Ser Pro Arg Glu Ala Val Ser Met Asp Pro Gln Gln Arg Leu Leu Leu 
        115                 120                 125 

Glu Thr Ser Trp Glu Ala Leu Glu Ala Ser Gly Leu Asp Pro Leu Arg 
    130                 135                 140 

Leu Lys Gly Ser Arg Thr Gly Val Phe Val Gly Val Met Ser Ser Asp 
145                 150                 155                 160 

Tyr Gly Ile Gln Lys Gly Ser Ala Pro Asp Gly Val Glu Gly Phe Leu 
                165                 170                 175 

Ser Thr Gly Thr His Ser Ser Ile Val Ser Gly Arg Val Ser Tyr Val 
            180                 185                 190 

Leu Gly Leu Glu Gly Pro Ala Val Ser Val Asp Thr Ala Cys Ser Ser 
        195                 200                 205 

Ser Leu Val Ala Leu His Ser Ala Ala His Ala Leu Arg Gln Gly Glu 
    210                 215                 220 

Cys Ser Leu Ala Leu Ala Gly Gly Val Thr Ile Met Ser Thr Pro Glu 
225                 230                 235                 240 

Arg Phe Val Glu Phe Ser Arg Gln Arg Ala Leu Ser Ala Asp Gly Arg 
                245                 250                 255 

Cys Lys Ala Phe Ser Ala Ser Ala Asp Gly Thr Gly Trp Ser Glu Gly 
            260                 265                 270 

Val Gly Met Leu Val Leu Glu Arg Leu Ser Asp Ala Arg Lys Asn Gly 
        275                 280                 285 

His Arg Val Leu Ala Val Ile Arg Gly Ser Ala Leu Asn Gln Asp Gly 
    290                 295                 300 

Ala Ser Asn Gly Leu Thr Ala Pro Asn Gly Pro Ser Gln Gln Arg Val 
305                 310                 315                 320 

Ile Arg Gln Ala Leu Ala Ser Ala Gly Leu Thr Ala Ala Glu Val Asp 
                325                 330                 335 

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

Ala Gln Ala Leu Leu Ala Thr Tyr Gly Lys Glu Arg Glu Asp Gly Arg 
        355                 360                 365 

Pro Leu Leu Leu Gly Ser Ser Lys Ser Asn Leu Gly His Thr Gln Ala 
    370                 375                 380 

Ala Ala Gly Val Ala Gly Val Ile Lys Met Val Leu Ala Met Arg Ala 
385                 390                 395                 400 

Gly Val Leu Pro Lys Thr Leu His Val Ser Glu Pro Ser Pro His Val 
                405                 410                 415 

Asp Trp Ser Ala Gly Ala Val Glu Leu Leu Thr Glu Ala Arg Glu Trp 
            420                 425                 430 

Pro Glu Thr Gly Arg Pro Arg Arg Ala Gly Val Ser Ser Phe Gly Phe 
        435                 440                 445 

Ser Gly Thr Asn Ala His Val Ile Ile Glu Glu Ala Ser Glu Phe Glu 
    450                 455                 460 

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

Val Leu Ser Ala Arg Ser Ala Asp Ala Leu Arg Gly Gln Ala Glu Arg 
                485                 490                 495 

Leu Leu Ser Phe Val Ser Ala Ala Gly Asp Val Ser Val Val Asp Val 
            500                 505                 510 

Ala Tyr Ser Leu Gly Val Ser Arg Ala Gly Leu Glu His Arg Gly Val 
        515                 520                 525 

Val Val Gly Glu Ser Arg Ala Glu Leu Leu Ala Ala Leu Glu Ser Leu 
    530                 535                 540 

Ala Ser Gly Val Glu Ser Pro Gly Val Val Thr Gly Arg Val Ala Glu 
545                 550                 555                 560 

Gly Arg Leu Ala Phe Leu Phe Thr Gly Gln Gly Ala Gln Arg Val Gly 
                565                 570                 575 

Met Gly Arg Glu Leu Ala Ala Ala Phe Pro Leu Phe Ala Ala Ser Leu 
            580                 585                 590 

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

Val Leu Phe Ala Glu Glu Gly Ser Ala Glu Ala Ala Leu Leu Thr Arg 
    610                 615                 620 

Thr Val Tyr Ala Gln Ala Ala Leu Phe Ala Val Glu Val Ala Leu Phe 
625                 630                 635                 640 

Arg Leu Val Glu Ser Phe Gly Val Val Pro Asp Phe Val Ala Gly His 
                645                 650                 655 

Ser Val Gly Glu Ile Ala Ala Ala His Val Ala Gly Val Phe Ser Leu 
            660                 665                 670 

Glu Asp Ala Val Ser Leu Val Ala Ala Arg Gly Arg Leu Met Asp Ala 
        675                 680                 685 

Leu Pro Glu Gly Gly Ala Met Val Ala Val Gln Ala Thr Glu Glu Asp 
    690                 695                 700 

Val Leu Ala Leu Leu Glu Gly Val Glu Asp Ala Ser Ile Ala Ala Ile 
705                 710                 715                 720 

Asn Gly Pro Asp Ala Val Val Val Ser Gly Thr Glu Ala Gly Val Ala 
                725                 730                 735 

Arg Val Val Asp Val Leu Arg Glu Arg Gly Ala Lys Thr Lys Arg Leu 
            740                 745                 750 

Val Val Ser His Ala Phe His Ser Pro Leu Met Glu Pro Met Leu Ala 
        755                 760                 765 

Glu Phe Ala Thr Val Val Glu Gly Leu Ser Phe Ala Ala Pro Thr Ile 
    770                 775                 780 

Pro Val Val Ser Asn Val Ser Gly Ala Val Ala Asp Ala Glu Leu Ser 
785                 790                 795                 800 

Ser Pro Gly Tyr Trp Val Arg His Val Arg Glu Ala Val Arg Phe Gly 
                805                 810                 815 

Ala Gly Val Glu Thr Leu Leu Gly Ala Gly Val Ser Ser Phe Leu Glu 
            820                 825                 830 

Ile Gly Pro Asp Gly Val Leu Ser Gly Met Ala Arg Thr Ser Val Pro 
        835                 840                 845 

Glu Gly Ala Asp Val Glu Cys Ala Pro Leu Met Arg Arg Gly Arg Gly 
    850                 855                 860 

Glu Val Arg Glu Phe Leu Thr Gly Leu Ser Arg Met Val Val Arg Gly 
865                 870                 875                 880 

Val Pro Val Asp Trp Gln Ser Leu Val Glu Gly Gly Arg Leu Ala Gly 
                885                 890                 895 

Leu Pro Thr Tyr Ala Phe Gln Arg Glu Arg Phe Trp Leu Asp Val Pro 
            900                 905                 910 

Ser Ala Val Gly Asp Val Ala Thr Ala Gly Leu Ala Pro Ser Gly His 
        915                 920                 925 

Pro Leu Leu Gly Ala Val Met Arg Arg Ala Asp Val Asp Gly Val Val 
    930                 935                 940 

Phe Thr Gly Arg Trp Ser Leu Arg Ser His Pro Trp Leu Gly Glu His 
945                 950                 955                 960 

Arg Val Gly Ser Ser Val Val Phe Pro Gly Thr Gly Phe Val Glu Leu 
                965                 970                 975 

Leu Met Arg Ala Gly Asp Glu Val Gly Cys Gly Arg Ile Glu Glu Leu 
            980                 985                 990 

Asn Gln Glu Thr Pro Leu Val Val Pro Glu Arg Gly  Ala Leu Gln Leu 
        995                 1000                 1005 

Gln Val Val Val Gly Ala  Pro  Glu Glu Thr Gly Leu  Arg Gly Val 
    1010                 1015                 1020 

Gly Val  Tyr Ser Arg Ala Glu  Asp Ala Asp Ala Asp  Val Pro Trp 
    1025                 1030                 1035 

Thr Arg  His Ala Ser Gly Leu  Leu Ser Pro Ala Val  Val Pro Ala 
    1040                 1045                 1050 

Asp Phe  Glu Leu Thr Gln Trp  Pro Pro Ala Gly Ala  Glu Ala Leu 
    1055                 1060                 1065 

Asn Val  Glu Asp Thr Tyr Gln  Arg Leu Ala Asp Ala  Gly Leu Val 
    1070                 1075                 1080 

Tyr Gly  Glu Arg Phe Gln Gly  Leu Lys Ser Gly Trp  Ile Lys Gly 
    1085                 1090                 1095 

Glu Asp  Ile Tyr Ala Glu Ile  Ala Leu Pro Glu His  Ala Val Ala 
    1100                 1105                 1110 

Glu Ala  Ala Glu Tyr Thr Leu  His Pro Ala Ala Leu  Asp Ala Ala 
    1115                 1120                 1125 

Leu Gln  Ala Ser Gly Leu Asn  Asp Pro Pro Glu Val  Gln Ala Thr 
    1130                 1135                 1140 

Ala Tyr  Val Pro Phe Ser Trp  Ser Gly Val Ser Leu  Phe Ala Ser 
    1145                 1150                 1155 

Gly Ala  Ser Val Leu Arg Val  Cys Val Arg His Val  Ala Arg Asp 
    1160                 1165                 1170 

Arg Val  Ser Leu Leu Val Ala  Asp Gly Val Gly Val  Pro Val Ala 
    1175                 1180                 1185 

Val Val  Glu Ser Leu Val Leu  Arg Ala Ile Ser Ala  Gly Ala Val 
    1190                 1195                 1200 

Ala Val  Ala Gly Val Gly Ser  Gly Val Gly Gly Gly  Leu Phe Glu 
    1205                 1210                 1215 

Val Val  Trp Ser Pro Val Val  Gly Val Arg Gly Val  Asp Val Ser 
    1220                 1225                 1230 

Gly Val  Val Val Leu Glu Ala  Gly Val Gly Val Gly  Gly Asp Gly 
    1235                 1240                 1245 

Val Ser  Val Val Gly Gly Val  Leu Glu Gly Leu Gln  Gly Val Leu 
    1250                 1255                 1260 

Gly Gly  Gly Ser Gly Ser Arg  Val Val Val Val Thr  Arg Gly Ala 
    1265                 1270                 1275 

Val Gly  Ser Gly Gly Val Val  Asp Val Ser Gly Ala  Gly Val Trp 
    1280                 1285                 1290 

Gly Leu  Val Arg Ser Val Gln  Ala Glu His Pro Gly  Arg Leu Val 
    1295                 1300                 1305 

Leu Val  Asp Val Gly Val Glu  Gly Asp Val Gly Val  Gly Val Gly 
    1310                 1315                 1320 

Leu Ala  Leu Gly Ser Gly Glu  Glu Gln Val Val Val  Arg Gly Gly 
    1325                 1330                 1335 

Glu Val  Phe Val Pro Arg Leu  Ala Arg Val Gly Ala  Val Ala Ala 
    1340                 1345                 1350 

Asp Ala  Gly Val Asp Gly Ala  Glu Ile Ala Gly Gly  Leu Gly Asp 
    1355                 1360                 1365 

Gly Val  Val Leu Val Thr Gly  Gly Thr Gly Gly Leu  Gly Ala Leu 
    1370                 1375                 1380 

Val Ala  Arg His Val Val Val  Glu Arg Gly Val Arg  Arg Leu Val 
    1385                 1390                 1395 

Leu Val  Ser Arg Arg Gly Leu  Gly Ala Pro Gly Ala  Val Gly Leu 
    1400                 1405                 1410 

Val Ala  Glu Leu Glu Gly Leu  Gly Ala Val Val Glu  Val Val Ala 
    1415                 1420                 1425 

Cys Asp  Val Ser Asp Arg Val  Ala Leu Ala Gly Val  Val Gly Gly 
    1430                 1435                 1440 

Ile Gly  Ser Asp Leu Ser Ala  Val Val His Thr Ala  Gly Val Val 
    1445                 1450                 1455 

Asp Asp  Gly Val Val Glu Ser  Met Ser Val Gly Arg  Val Ala Ser 
    1460                 1465                 1470 

Val Phe  Gly Pro Lys Ala Asp  Ala Ala Trp Phe Leu  His Glu Leu 
    1475                 1480                 1485 

Thr Arg  Asp Met Gly Leu Ser  Ala Phe Val Leu Phe  Ser Ser Met 
    1490                 1495                 1500 

Ala Gly  Thr Val Gly Gly Gly  Gly Gln Ser Asn Tyr  Ala Ala Ala 
    1505                 1510                 1515 

Asn Ala  Tyr Leu Asp Gly Leu  Ala Glu Tyr Arg Arg  Gly Leu Gly 
    1520                 1525                 1530 

Leu Ala  Ala Thr Ser Leu Ala  Trp Gly Leu Trp Glu  Glu Ser Thr 
    1535                 1540                 1545 

Gly Met  Gly Ser Arg Leu Thr  Asp Ala Asp Leu Asp  Arg Met Ser 
    1550                 1555                 1560 

Arg Ser  Gly Ile Arg Thr Leu  Ser Ile Glu Asp Gly  Leu Ala Leu 
    1565                 1570                 1575 

Phe Asp  Ala Ala Leu Ala Ala  Asp Arg Pro Thr Val  Met Pro Ala 
    1580                 1585                 1590 

His Phe  Asp Ile Pro Ala Leu  Arg Gly Gln Gly Glu  Ser Leu Ala 
    1595                 1600                 1605 

Pro Val  Phe Arg Thr Leu Ala  Gly Pro Pro Ala Arg  Arg Ser Ala 
    1610                 1615                 1620 

Ala Val  Thr Pro Arg Asp Ile  Ala Ala Ala Thr Glu  Ser Ser Leu 
    1625                 1630                 1635 

Thr Asp  Arg Leu Ala Gly Leu  Asp Ala Glu Gly Arg  Arg Ala Leu 
    1640                 1645                 1650 

Val Leu  Gly Val Val Arg Ala  Gln Val Ala Gln Val  Leu Ala Tyr 
    1655                 1660                 1665 

Ala Ser  Pro Asp Leu Val Glu  Pro Glu Arg Ala Phe  Gln Asp Leu 
    1670                 1675                 1680 

Gly Phe  Asp Ser Leu Thr Ala  Val Glu Leu Arg Asn  Gly Leu Thr 
    1685                 1690                 1695 

Ala Ile  Ala Gly Val Arg Leu  Pro Ala Thr Leu Val  Phe Asp Tyr 
    1700                 1705                 1710 

Pro Ser  Thr Asp Ile Leu Thr  Asp Phe Leu Leu Ala  Glu Leu Ser 
    1715                 1720                 1725 

Asp Glu  Ile Pro Ala Ala Val  Ala Thr Leu Pro Ala  Met Gly His 
    1730                 1735                 1740 

Val Val  Asp Asp Asp Pro Ile  Ala Val Ile Gly Met  Gly Cys Arg 
    1745                 1750                 1755 

Tyr Pro  Gly Gly Val Glu Ser  Pro Glu Glu Leu Trp  Lys Leu Met 
    1760                 1765                 1770 

Ala Glu  Gly Arg Asp Ala Ile  Ser Glu Phe Pro Thr  Asp Arg Gly 
    1775                 1780                 1785 

Trp Asp  Leu Asp Ala Ile Tyr  His Pro Asp Pro Met  His Thr Gly 
    1790                 1795                 1800 

Thr Ser  Tyr Thr Arg Glu Gly  Gly Phe Ile His Asn  Ala Gly Asp 
    1805                 1810                 1815 

Phe Asp  Ala Ala Phe Phe Gly  Ile Ser Pro Arg Glu  Ala Met Glu 
    1820                 1825                 1830 

Thr Asp  Pro Gln Gln Arg Leu  Leu Leu Glu Thr Ser  Trp Glu Ala 
    1835                 1840                 1845 

Phe Glu  Gln Ala Gly Ile Val  Pro Thr Asp Leu Lys  Gly Thr Gln 
    1850                 1855                 1860 

Thr Gly  Val Phe Ala Gly Val  Met Tyr His Asp Tyr  Ala Gly Asn 
    1865                 1870                 1875 

Ile Gly  Ser Gly Ser Ile Val  Thr Gly Arg Val Ala  Tyr Thr Leu 
    1880                 1885                 1890 

Gly Leu  Glu Gly Pro Ala Val  Ser Ile Asp Thr Ala  Cys Ser Ser 
    1895                 1900                 1905 

Ser Leu  Val Ala Ile His Leu  Ala Ala Gln Ser Leu  Arg Gln Gly 
    1910                 1915                 1920 

Glu Cys  Ser Met Ala Ile Ala  Gly Gly Val Ala Val  Met Ala Thr 
    1925                 1930                 1935 

Pro Glu  Ser Phe Ile Glu Phe  Ser Arg Gln Arg Ala  Leu Ser Gln 
    1940                 1945                 1950 

Asn Gly  Arg Cys Arg Ala Phe  Ser Ser Asp Ala Asp  Gly Thr Ala 
    1955                 1960                 1965 

Trp Gly  Glu Gly Val Gly Val  Leu Ile Leu Glu Arg  Leu Ser Asp 
    1970                 1975                 1980 

Ala Arg  Lys Asn Gly His Glu  Val Leu Ala Val Ile  Arg Gly Ser 
    1985                 1990                 1995 

Ala Leu  Asn Gln Asp Gly Ala  Ser Asn Gly Leu Thr  Ala Pro Asn 
    2000                 2005                 2010 

Gly Pro  Ser Gln Gln Arg Val  Ile Arg Gln Ala Leu  Ala Asn Ser 
    2015                 2020                 2025 

Gly Leu  Ser Ala Ala Glu Val  Asp Ala Val Glu Ala  His Gly Thr 
    2030                 2035                 2040 

Gly Thr  Thr Leu Gly Asp Pro  Ile Glu Ala Gln Ala  Leu Leu Ala 
    2045                 2050                 2055 

Thr Tyr  Gly Lys Glu Arg Asp  Ala Asp Gln Pro Leu  Trp Leu Gly 
    2060                 2065                 2070 

Ser Ser  Lys Ser Asn Phe Gly  His Thr Lys Ala Ala  Ala Gly Val 
    2075                 2080                 2085 

Ala Gly  Val Ile Lys Met Val  Met Ala Ile Arg Asn  Gly Val Leu 
    2090                 2095                 2100 

Pro Lys  Thr Leu His Val Thr  Glu Pro Ser Pro His  Val Asp Trp 
    2105                 2110                 2115 

Ser Ala  Gly Ala Val Glu Leu  Leu Ala Glu Ala Arg  Glu Trp Pro 
    2120                 2125                 2130 

Glu Thr  Gly Arg Pro Arg Arg  Ala Gly Val Ser Ser  Phe Gly Ile 
    2135                 2140                 2145 

Ser Gly  Thr Asn Ala His Val  Ile Val Glu Gln Ala  Pro Thr Asp 
    2150                 2155                 2160 

Gln Ala  Ala Thr Lys Pro Lys  Ala Ala Asp Ala Val  Pro Gly Leu 
    2165                 2170                 2175 

Pro Val  Pro Trp Val Val Ser  Ala Lys Asn Pro Glu  Ala Leu Arg 
    2180                 2185                 2190 

Ala Gln  Ala Gly Arg Leu Gly  Ser Phe Leu Gly Glu  Thr Gly Val 
    2195                 2200                 2205 

Val Asp  Val Pro Ala Val Gly  Trp Ser Leu Val Arg  Gly Arg Ser 
    2210                 2215                 2220 

Val Phe  Ala His Arg Ala Val  Val Val Gly Gly Glu  Trp Asp Ala 
    2225                 2230                 2235 

Leu Leu  Ala Ser Ile Gly Glu  Leu Ala Asp Gly Ala  Glu Asp Gly 
    2240                 2245                 2250 

Ser Gly  Ala Ala Ser Gly Ser  Val Val Ser Gly Val  Ala Asp Val 
    2255                 2260                 2265 

Ser Gly  Arg Arg Val Phe Val  Phe Pro Gly Gln Gly  Ser Gln Trp 
    2270                 2275                 2280 

Val Gly  Met Ala Gln Gly Leu  Leu Asp Ser Ser Val  Val Phe Thr 
    2285                 2290                 2295 

Glu Arg  Met Thr Glu Cys Ala  Ala Ala Leu Asp Pro  Leu Val Glu 
    2300                 2305                 2310 

Trp Ser  Leu Leu Asp Val Val  Arg Gly Val Glu Gly  Ala Ala Ser 
    2315                 2320                 2325 

Leu Glu  Arg Val Asp Val Val  Gln Pro Val Leu Trp  Ala Val Met 
    2330                 2335                 2340 

Val Ser  Leu Ala Ser Val Trp  Arg Ser Val Gly Val  Val Pro Asp 
    2345                 2350                 2355 

Ala Val  Val Gly His Ser Gln  Gly Glu Ile Ala Ala  Ala Val Val 
    2360                 2365                 2370 

Gly Gly  Trp Leu Ser Leu Val  Asp Gly Ala Arg Val  Val Ala Leu 
    2375                 2380                 2385 

Arg Ser  Leu Ala Ile Arg Glu  Val Leu Ala Gly Gly  Gly Gly Met 
    2390                 2395                 2400 

Val Ala  Val Gln Ala Ala Glu  Asp Glu Val Ala Gly  Trp Leu Glu 
    2405                 2410                 2415 

Gly Val  Glu Gly Val Gly Ile  Ala Ala Val Asn Gly  Pro Arg Ser 
    2420                 2425                 2430 

Val Val  Ile Ser Gly Thr Arg  Ala Gly Leu Asp Ala  Cys Val Glu 
    2435                 2440                 2445 

Leu Trp  Ser Gly Arg Gly Thr  Trp Val Lys Arg Val  Pro Val Asp 
    2450                 2455                 2460 

Tyr Ala  Ser His Ser Ala Glu  Val Glu Arg Val Arg  Glu Arg Val 
    2465                 2470                 2475 

Leu Ala  Asp Leu Ala Ser Val  Thr Gly Leu Ser Gly  Ser Val Pro 
    2480                 2485                 2490 

Met Leu  Ser Thr Met Thr Gly  Asp Trp Ile Val Glu  Gly Gln Val 
    2495                 2500                 2505 

Gly Ala  Gly Tyr Trp Val Glu  Asn Leu Arg Arg Pro  Val Leu Phe 
    2510                 2515                 2520 

Ala Asp  Ala Thr Arg Arg Leu  Ala Ser Glu Gly Phe  Gly Ala Phe 
    2525                 2530                 2535 

Val Glu  Val Ser Ala His Pro  Val Leu Val Met Gly  Ile Glu Glu 
    2540                 2545                 2550 

Thr Leu  Glu Ala His His Thr  Ala Thr Thr Asp Asp  Asp Thr Thr 
    2555                 2560                 2565 

Thr Arg  Thr Pro Val Val Thr  Val Gly Thr Leu Arg  Arg Gly Glu 
    2570                 2575                 2580 

Gly Gly  Trp Asp Gln Phe Leu  Arg Ser Leu Ala Gly  Leu Phe Val 
    2585                 2590                 2595 

Arg Gly  Ala Val Thr Pro Asp  Trp Glu Ser Leu Leu  Gly Gly Thr 
    2600                 2605                 2610 

Arg Pro  Arg Val Asp Leu Pro  Thr Tyr Ala Phe Gln  Arg Arg Arg 
    2615                 2620                 2625 

Phe Trp  Ile Glu Ser Val Arg  Lys Glu Ala Val Thr  Leu Ala Ala 
    2630                 2635                 2640 

Asp Pro  Val Asp Ala Ala Phe  Trp Glu Ala Val Glu  Ser Ala Asp 
    2645                 2650                 2655 

Leu Ala  Lys Leu Ala Asp Ser  Leu Arg Ile Glu Thr  Asp Val Leu 
    2660                 2665                 2670 

Glu Gly  Val Leu Pro Ala Leu  Thr Ser Trp Arg Thr  Arg Ser Arg 
    2675                 2680                 2685 

Glu Gln  Ser Leu Val Asp Gly  Trp Arg Tyr Arg Glu  Glu Trp Lys 
    2690                 2695                 2700 

Pro Val  Pro Ala Pro Thr Pro  Asn Ser Ala Thr Gly  Thr Trp Thr 
    2705                 2710                 2715 

Val Leu  Val Pro Ala Thr His  Gln Gly Asp Ala Thr  Val Thr Gly 
    2720                 2725                 2730 

Val Leu  Asp Gly Leu Arg Arg  Gly Gly Ala Asp Ile  Arg Val Leu 
    2735                 2740                 2745 

Glu Val  Thr Ala Thr Asp Arg  Glu Ala Leu Ala Glu  Gln Leu Arg 
    2750                 2755                 2760 

Ala Glu  Leu Ala Gln Ser Glu  Pro Arg Leu Ile Leu  Ser Leu Leu 
    2765                 2770                 2775 

Ala Leu  Asp Asp Arg Ala His  Pro Arg His Pro Glu  Leu Thr Glu 
    2780                 2785                 2790 

Gly Ile  Thr Ala Thr Ile Ala  Leu Val Gln Ala Leu  Asp Asp Cys 
    2795                 2800                 2805 

Gly Ala  Thr Ala Arg Leu Trp  Cys Ala Thr Ser Leu  Ala Val Ala 
    2810                 2815                 2820 

Val Thr  Glu Ser Ala Glu Val  Leu Asn Pro Val Gln  Thr Thr Ala 
    2825                 2830                 2835 

Trp Gly  Met Gly Ala Ser Phe  Ala Leu Asp His Pro  Glu Thr Trp 
    2840                 2845                 2850 

Gly Gly  Leu Val Asp Leu Pro  Ala Asp Ile Asp Thr  Arg Thr Ala 
    2855                 2860                 2865 

Asp Ile  Leu Cys Ser Val Leu  Ala Ser Asp Leu Gln  Glu Asp Gln 
    2870                 2875                 2880 

Ile Ala  Leu Arg Thr Ala Gly  Leu Phe Ala Arg Arg  Met Val Arg 
    2885                 2890                 2895 

Ala Arg  Leu Asp Glu Ser Ala  Val Ala Thr Glu Gln  Pro Trp Arg 
    2900                 2905                 2910 

Pro Asn  Gly Thr Val Leu Val  Thr Gly Gly Thr Gly  Gly Ile Gly 
    2915                 2920                 2925 

Ser His  Val Ala Arg Trp Leu  Ala Ala Ala Gly Ala  Glu His Leu 
    2930                 2935                 2940 

Val Leu  Thr Ser Arg Arg Gly  Ala Glu Ala Pro Gly  Ala Ala Glu 
    2945                 2950                 2955 

Leu Glu  Ala Glu Leu Ala Leu  Leu Gly Ala Lys Val  Thr Leu Ala 
    2960                 2965                 2970 

Ala Cys  Asp Met Gly Asp Arg  Glu Ser Val Arg Glu  Leu Val Ala 
    2975                 2980                 2985 

Ala Leu  Pro Asp Ala Ala Pro  Leu Thr Ala Val Phe  His Leu Ala 
    2990                 2995                 3000 

Gly Ala  Leu Pro Asp Gly Glu  Arg Arg Leu Ser Ala  Thr Thr Phe 
    3005                 3010                 3015 

Glu Asp  Phe Ser Arg Met Thr  Arg Ala Lys Ile Gly  Gly Ala Val 
    3020                 3025                 3030 

His Leu  Asp Glu Leu Leu Ala  Asp Arg Glu Leu Ala  Ala Phe Val 
    3035                 3040                 3045 

Thr Phe  Ser Ser Gly Ser Ala  Ile Trp Gly Asn Ala  Asn Gln Ala 
    3050                 3055                 3060 

Ala Tyr  Gly Ala Ser Asn Ala  Phe Leu Asp Gly Leu  Val His Asn 
    3065                 3070                 3075 

Arg Arg  Ala Arg Gly Leu Ala  Gly Thr Ser Ile Ala  Trp Gly Leu 
    3080                 3085                 3090 

Trp Gly  Gly Asp Gly Thr Asp  Thr Glu Thr Asp Glu  Gln Leu Ser 
    3095                 3100                 3105 

Arg Ile  Gly Val Arg Ser Met  Asp Pro Arg Leu Ala  Leu Glu Val 
    3110                 3115                 3120 

Leu Arg  Gln Ala Leu Asp Gln  Asp Thr Ser His Leu  Ile Ala Thr 
    3125                 3130                 3135 

Asp Ile  Asp Trp Gln Arg Phe  Ala Pro Val Phe Thr  Ile Ala Arg 
    3140                 3145                 3150 

Pro Arg  Pro Leu Leu Asp Gly  Ile Ala Glu Val Arg  Ala Val Leu 
    3155                 3160                 3165 

Ser Ala  Asp Thr Ala Glu Val  Gly Pro Ala Asp Asp  Asp Thr Pro 
    3170                 3175                 3180 

Lys Glu  Thr Val Val Thr Arg  Leu Ala Gly Leu Ser  Pro Ala Glu 
    3185                 3190                 3195 

Arg Asp  His Ala Leu Leu Glu  Leu Val Arg Thr Gln  Val Ala Ala 
    3200                 3205                 3210 

Val Leu  Arg Tyr Ser Asp Thr  Ser Asp Val Glu Gln  Asp Gln Ser 
    3215                 3220                 3225 

Phe Lys  Asp Leu Gly Phe Asp  Ser Val Thr Ala Val  Glu Leu Arg 
    3230                 3235                 3240 

Asn Lys  Leu Thr Arg Gly Val  Arg Ala Ala Ala Ala  Arg His Gly 
    3245                 3250                 3255 

Val Phe  Asp Tyr Ala Thr Pro  Val Ala Leu Ala Ala  His Leu Arg 
    3260                 3265                 3270 

Ser Glu  Leu Phe Thr Asp Asp  Ala Ala Ala Ser Gly  Glu Val Pro 
    3275                 3280                 3285 

Leu Leu  Ala Glu Leu Asp Arg  Ile Glu Ala Ala Val  Thr Ser Leu 
    3290                 3295                 3300 

Pro Ser  Ala Asp Ile Glu Arg  Met His Leu Thr Ser  Arg Leu Gln 
    3305                 3310                 3315 

Ser Leu  Val Thr Lys Leu Asn  Asp Ile Val Gly Ala  Gly Ala Pro 
    3320                 3325                 3330 

Leu Glu  Ala Glu Ala Ile Ala  Asp Lys Leu Glu Thr  Ala Thr Ala 
    3335                 3340                 3345 
Asp Asp  Ile Phe Ala Phe Ile  Asp Lys Asp Leu Gly  Leu Asn 
    3350                 3355                 3360 

 
           
             7  
             3808  
             PRT  
             Streptomyces halstedii sp.HC-34  
           
            7 

Met Ser Asn Glu Glu Lys Leu Leu Asp Tyr Leu Lys Arg Val Thr Ala 
1               5                   10                  15 

Asp Leu His Ala Thr Arg Gln Arg Leu Arg Glu Ala Glu Ser Asp Glu 
            20                  25                  30 

Gln Glu Pro Ile Ala Val Val Ala Met Gly Cys Arg Tyr Pro Gly Asp 
        35                  40                  45 

Val Arg Thr Pro Glu Asp Leu Trp Gln Leu Val Ala Thr Gly Gly Asp 
    50                  55                  60 

Ala Val Thr Glu Phe Pro Ala Asp Arg Gly Trp Asp Phe Asp Thr Leu 
65                  70                  75                  80 

Leu Gly Gly Asp Ala Gly Ala Ser Gly Ser Thr Tyr Val Ala Arg Gly 
                85                  90                  95 

Gly Phe Val His Asp Ala Ala Asp Phe Asp Ala Asp Phe Phe Gly Ile 
            100                 105                 110 

Ser Pro Arg Glu Ala Leu Ala Met Asp Pro Gln Gln Arg Leu Leu Leu 
        115                 120                 125 

Glu Leu Ala Trp Glu Thr Ser Glu Arg Ala Gly Ile Asp Pro His Ser 
    130                 135                 140 

Leu Arg Gly Ala Ser Val Gly Val Phe Ala Gly Thr Asn Gly Gln Asp 
145                 150                 155                 160 

Tyr Ala Asp Leu Met Asp Arg Ala Pro Glu Asp Thr Glu Ala Tyr Leu 
                165                 170                 175 

Ser Thr Gly Ser Val Ala Ala Val Val Ser Gly Arg Val Ser Tyr Ala 
            180                 185                 190 

Leu Gly Leu Glu Gly Pro Ser Val Ser Val Asp Thr Ala Cys Ser Ser 
        195                 200                 205 

Ser Leu Val Ala Leu His Leu Ala Cys Gln Ala Leu Arg Gln Lys Glu 
    210                 215                 220 

Cys Ser Met Ala Phe Ala Gly Gly Val Thr Ile Met Ser Thr Pro Gly 
225                 230                 235                 240 

Pro Phe Ile Ala Phe Ser Arg Gln Ser Gly Leu Ala Ser Asp Gly Arg 
                245                 250                 255 

Cys Lys Ala Phe Ser Asp Asp Thr Asp Gly Thr Gly Trp Gly Glu Gly 
            260                 265                 270 

Ala Gly Leu Leu Leu Leu Glu Arg Leu Ser Asp Ala Arg Arg Asn Gly 
        275                 280                 285 

His Gln Val Leu Ala Val Val Arg Gly Ser Ala Leu Asn Gln Asp Gly 
    290                 295                 300 

Ala Ser Asn Gly Leu Thr Ala Pro Asn Gly Pro Ser Gln Gln Arg Val 
305                 310                 315                 320 

Ile Arg Gln Ala Leu Ala Asn Ala Gly Leu Thr Ala Ala Glu Val Asp 
                325                 330                 335 

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

Ala Gln Ala Ile Leu Ala Thr Tyr Gly Gln Ser Arg Glu Gln Asp Gln 
        355                 360                 365 

Pro Leu Trp Leu Gly Ser Ile Lys Ser Asn Ile Gly His Thr Gln Ala 
    370                 375                 380 

Ala Ala Gly Val Ser Gly Val Ile Lys Met Val Met Ala Ile Gln Asn 
385                 390                 395                 400 

Gly Val Leu Pro Lys Thr Leu His Val Ser Glu Pro Ser Ser Val Val 
                405                 410                 415 

Asp Trp Ser Ala Gly Ala Val Glu Leu Leu Thr Glu Ala Arg Glu Trp 
            420                 425                 430 

Pro Glu Thr Gly Arg Pro Arg Arg Ala Gly Val Ser Ser Phe Gly Val 
        435                 440                 445 

Ser Gly Thr Asn Ala His Ile Ile Met Glu Gln Ala Pro Val Pro Glu 
    450                 455                 460 

Ala Glu Ser Glu Pro Asp Gly Glu Ala Pro Ala Ala Val Ser Gly Leu 
465                 470                 475                 480 

Pro Val Pro Trp Val Val Ser Gly Lys Thr Ala Asp Ala Leu Arg Ala 
                485                 490                 495 

Gln Ala Glu Arg Leu Leu Ser Phe Val Ser Ala Asp Ala Asp Val Ser 
            500                 505                 510 

Val Val Asp Val Ala Tyr Ser Leu Gly Val Ser Arg Ala Gly Leu Glu 
        515                 520                 525 

His Arg Gly Val Val Val Gly Glu Ser Arg Ala Glu Leu Leu Ala Ala 
    530                 535                 540 

Leu Glu Ser Leu Ala Ser Gly Val Glu Ser Pro Gly Val Val Thr Gly 
545                 550                 555                 560 

Arg Val Ala Glu Gly Arg Leu Ala Phe Leu Phe Thr Gly Gln Gly Ala 
                565                 570                 575 

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

Ala Ala Ser Leu Glu Glu Thr Cys Gly Leu Leu Glu Arg Ala Gly Val 
        595                 600                 605 

Ala Val Arg Glu Val Leu Phe Ala Glu Glu Gly Ser Ala Glu Ala Ala 
    610                 615                 620 

Leu Leu Thr Arg Thr Val Tyr Ala Gln Ala Ala Leu Phe Ala Val Glu 
625                 630                 635                 640 

Val Ala Leu Phe Arg Leu Val Glu Ser Phe Gly Val Val Pro Asp Phe 
                645                 650                 655 

Val Ala Gly His Ser Val Gly Glu Ile Ala Ala Ala His Val Ala Gly 
            660                 665                 670 

Val Phe Ser Leu Glu Asp Ala Val Ser Leu Val Ala Ala Arg Gly Arg 
        675                 680                 685 

Leu Met Asp Ala Leu Pro Glu Gly Gly Ala Met Val Ala Val Gln Ala 
    690                 695                 700 

Thr Glu Glu Asp Val Leu Ala Leu Leu Glu Gly Val Glu Asp Ala Ser 
705                 710                 715                 720 

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

Ala Gly Val Ala Arg Val Val Asp Val Leu Arg Glu Arg Gly Ala Lys 
            740                 745                 750 

Thr Lys Arg Leu Asp Val Ser His Ala Phe His Ser Pro Leu Met Glu 
        755                 760                 765 

Pro Met Leu Ala Glu Phe Ala Thr Val Val Glu Gly Leu Ser Phe Ala 
    770                 775                 780 

Ala Pro Thr Ile Pro Val Val Ser Asn Val Ser Gly Ala Val Ala Asp 
785                 790                 795                 800 

Ala Glu Leu Ser Ser Pro Gly Tyr Trp Val Arg His Val Arg Glu Ala 
                805                 810                 815 

Val Arg Phe Gly Ala Gly Val Glu Thr Leu Leu Gly Ala Gly Val Ser 
            820                 825                 830 

Ser Phe Leu Glu Ile Gly Pro Asp Gly Val Leu Ser Gly Met Ala Arg 
        835                 840                 845 

Gly Ser Ile Ser Asp Gly Ala Asp Val Gly Cys Val Pro Val Met Arg 
    850                 855                 860 

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

Ala Val Arg Gly Val Pro Val Ser Trp Gly Pro Leu Leu Ala Gly Gly 
                885                 890                 895 

Arg Arg Val Glu Leu Pro Thr Tyr Ala Phe Gln Arg Arg Arg Phe Trp 
            900                 905                 910 

Leu Glu Ala Gly His Ser Val Thr Asp Ala Ser Gly Leu Gly Gln Thr 
        915                 920                 925 

Ala Ala Gly His Pro Leu Ile Gly Ala Val Val Ser Leu Ala Gly Gly 
    930                 935                 940 

Asp Gly Ala Val Leu Thr Gly Arg Val Ser Leu Asn Thr His Pro Trp 
945                 950                 955                 960 

Leu Gly Asp His Arg Val Ala Ser Ser Val Val Phe Pro Gly Thr Gly 
                965                 970                 975 

Phe Val Glu Leu Leu Met Arg Ala Gly Asp Glu Val Gly Cys Gly Arg 
            980                 985                 990 

Leu Glu Glu Leu Asn Gln Glu Ala  Pro Leu Val Val Pro  Asp Arg Gly 
        995                 1000                 1005 

Ala Val  Gln Ile Gln Val Thr  Val Glu Ala Pro Asn  Ala Val Gly 
    1010                 1015                 1020 

Glu Arg  Pro Val Ala Val Tyr  Ser Arg Leu Glu Asp  Thr Asp Thr 
    1025                 1030                 1035 

Asp Ala  Pro Trp Thr Arg His  Ala Ser Gly Leu Leu  Ser Pro Thr 
    1040                 1045                 1050 

Thr Ala  Ser Ala Asp Phe Asp  Phe Thr Ala Trp Pro  Pro Ala Gly 
    1055                 1060                 1065 

Ala Asp  Pro Leu Ser Val Asp  Gly Met Tyr Asp Arg  Pro Asp Ser 
    1070                 1075                 1080 

Gly Leu  Val Tyr Gly Pro Leu  Phe Gln Gly Leu Thr  Ala Ala Trp 
    1085                 1090                 1095 

Arg Lys  Gly Asp Glu Val Tyr  Ala Glu Ile Glu Leu  Pro Glu Gly 
    1100                 1105                 1110 

Ala Ala  Val Asp Ala Ala Arg  Phe Gly Met His Pro  Ala Leu Leu 
    1115                 1120                 1125 

Asp Ala  Ala Leu His Ala Leu  Gly Phe Ser Ala Ser  Tyr Glu Asp 
    1130                 1135                 1140 

Gln Glu  Glu Asp Gly Thr Val  Ala Arg Leu Pro Phe  Ser Trp Ser 
    1145                 1150                 1155 

Gly Val  Ser Leu Phe Ala Ser  Gly Ala Ser Val Leu  Arg Val Cys 
    1160                 1165                 1170 

Val Arg  His Val Ala Arg Asp  Arg Val Ser Leu Leu  Val Ala Asp 
    1175                 1180                 1185 

Gly Val  Gly Val Pro Val Ala  Val Val Glu Ser Leu  Val Leu Arg 
    1190                 1195                 1200 

Ala Ile  Ser Ala Gly Ala Val  Ala Val Ala Gly Val  Gly Ser Gly 
    1205                 1210                 1215 

Val Gly  Gly Gly Leu Phe Glu  Val Val Trp Ser Pro  Val Val Gly 
    1220                 1225                 1230 

Val Arg  Gly Val Asp Val Ser  Gly Val Val Val Leu  Glu Ala Gly 
    1235                 1240                 1245 

Val Gly  Val Gly Gly Asp Gly  Val Ser Val Val Gly  Gly Val Leu 
    1250                 1255                 1260 

Glu Gly  Leu Gln Gly Val Leu  Gly Gly Gly Ser Gly  Ser Arg Val 
    1265                 1270                 1275 

Val Val  Val Thr Arg Gly Ala  Val Gly Ser Gly Gly  Val Val Asp 
    1280                 1285                 1290 

Val Ser  Gly Ala Gly Val Trp  Gly Leu Val Arg Ser  Val Gln Ala 
    1295                 1300                 1305 

Glu His  Pro Gly Arg Leu Val  Leu Val Asp Val Gly  Val Glu Gly 
    1310                 1315                 1320 

Asp Val  Gly Val Gly Val Gly  Leu Ala Leu Gly Ser  Gly Glu Glu 
    1325                 1330                 1335 

Gln Val  Val Val Arg Gly Gly  Glu Val Phe Val Pro  Arg Leu Ala 
    1340                 1345                 1350 

Arg Val  Ser Val Val Ala Ala  Asp Val Val Pro Asp  Ala Gly Val 
    1355                 1360                 1365 

Asp Gly  Ala Asp Ile Arg Gly  Gly Leu Gly Asp Gly  Val Val Leu 
    1370                 1375                 1380 

Val Thr  Gly Gly Thr Gly Gly  Leu Gly Ala Leu Val  Ala Arg His 
    1385                 1390                 1395 

Val Val  Val Glu Arg Gly Val  Arg Arg Leu Val Leu  Val Ser Arg 
    1400                 1405                 1410 

Arg Gly  Leu Gly Ala Pro Gly  Ala Val Gly Leu Val  Ala Glu Leu 
    1415                 1420                 1425 

Glu Ser  Leu Gly Ala Val Val  Glu Val Val Ala Cys  Asp Val Ser 
    1430                 1435                 1440 

Asp Arg  Val Ala Leu Ala Gly  Val Val Gly Gly Ile  Gly Ser Asp 
    1445                 1450                 1455 

Leu Ser  Ala Val Val His Thr  Ala Gly Val Val Asp  Asp Gly Val 
    1460                 1465                 1470 

Val Glu  Ser Met Ser Val Gly  Arg Val Ala Ser Val  Phe Gly Pro 
    1475                 1480                 1485 

Lys Ala  Asp Ala Ala Trp Phe  Leu His Glu Leu Thr  Arg Asp Met 
    1490                 1495                 1500 

Gly Leu  Ser Ala Phe Val Leu  Phe Ser Ser Met Ala  Gly Thr Val 
    1505                 1510                 1515 

Gly Gly  Gly Gly Gln Ser Asn  Tyr Ala Ala Ala Asn  Ala Tyr Leu 
    1520                 1525                 1530 

Asp Gly  Leu Ala Glu Tyr Arg  Arg Gly Leu Gly Leu  Ala Ala Thr 
    1535                 1540                 1545 

Ser Leu  Ala Trp Gly Leu Trp  Glu Asp Thr Ala Asn  Gly Gly Met 
    1550                 1555                 1560 

Thr Gly  His Leu Ala Glu Ala  Asp Arg Thr Arg Met  Ala Arg Gly 
    1565                 1570                 1575 

Gly Val  Phe Pro Leu Ala Leu  Asp Glu Gly Leu Ala  Leu Phe Asp 
    1580                 1585                 1590 

Ala Ala  Leu Ala Thr Gly Lys  Ala Thr Leu Val Pro  Val His Leu 
    1595                 1600                 1605 

Asp Thr  Thr Ala Leu Arg Ala  His Ala Asp Glu Leu  Pro Ala Leu 
    1610                 1615                 1620 

Phe Arg  Asp Leu Val Arg Ala  Pro Lys Arg Arg Thr  Ala Ala Glu 
    1625                 1630                 1635 

Gly Arg  Ala Ala Asp Ser Ala  Asp Asp Leu Ala Gly  Arg Leu Ala 
    1640                 1645                 1650 

Gly Leu  Ala Ala Glu Ala Arg  Arg Pro Leu Val Leu  Gly Val Val 
    1655                 1660                 1665 

Arg Ala  Gln Val Ala Gln Val  Leu Gly Tyr Ala Ser  Ala Asp Leu 
    1670                 1675                 1680 

Val Glu  Pro Glu Arg Ala Phe  Gln Asp Leu Gly Phe  Asp Ser Leu 
    1685                 1690                 1695 

Thr Ala  Val Glu Leu Arg Asn  Gly Leu Thr Ala Val  Ala Gly Val 
    1700                 1705                 1710 

Arg Leu  Pro Ala Thr Leu Val  Phe Asp Tyr Pro Ser  Thr Asp Ile 
    1715                 1720                 1725 

Leu Thr  Asp Phe Leu Leu Ala  Glu Leu Ser Gly Lys  Val Ala Val 
    1730                 1735                 1740 

Ala Ala  Pro Leu Ala Pro Leu  Ala Thr Thr Gly Pro  Val His Asp 
    1745                 1750                 1755 

Asp Pro  Ile Val Val Ile Gly  Met Gly Cys Arg Tyr  Pro Gly Gly 
    1760                 1765                 1770 

Val Arg  Ser Pro Glu Asp Leu  Trp Arg Leu Val Ala  Asp Gly Arg 
    1775                 1780                 1785 

Asp Ala  Ile Ser Glu Phe Pro  Thr Asp Arg Gly Trp  Asp Leu Asp 
    1790                 1795                 1800 

Ala Leu  Tyr His Pro Asp Pro  Asp His Ala Gly Thr  Ser Tyr Thr 
    1805                 1810                 1815 

Arg Glu  Gly Gly Phe Leu His  Asp Ala Ala Asp Phe  Asp Ala Asp 
    1820                 1825                 1830 

Phe Phe  Gly Ile Ser Pro Arg  Glu Ala Ile Val Met  Asp Pro Gln 
    1835                 1840                 1845 

Gln Arg  Leu Leu Leu Glu Thr  Ser Trp Glu Ala Phe  Glu Gln Ala 
    1850                 1855                 1860 

Gly Ile  Val Pro Ala Asp Leu  Lys Gly Thr Gln Thr  Gly Val Phe 
    1865                 1870                 1875 

Ala Gly  Val Met Tyr His Asp  Tyr Gly Thr Arg Ile  Val Asp Ile 
    1880                 1885                 1890 

Pro Glu  Gly Ala Glu Gly Tyr  Leu Gly Thr Gly Ile  Ser Gly Ser 
    1895                 1900                 1905 

Val Val  Ser Gly Arg Val Ala  Tyr Thr Leu Gly Leu  Glu Gly Pro 
    1910                 1915                 1920 

Ala Val  Thr Ile Asp Thr Ala  Cys Ser Ser Ser Leu  Val Ala Leu 
    1925                 1930                 1935 

His Ser  Ala Ala His Ala Leu  Arg Gln Gly Glu Cys  Ser Met Ala 
    1940                 1945                 1950 

Ile Ala  Gly Gly Val Thr Val  Met Ala Gly Pro Asp  Thr Phe Ile 
    1955                 1960                 1965 

Asp Phe  Ser Arg Gln Arg Gly  Leu Ala Thr Asn Gly  Arg Cys Lys 
    1970                 1975                 1980 

Ala Phe  Ser Ala Asp Ala Asp  Gly Thr Gly Trp Gly  Glu Gly Val 
    1985                 1990                 1995 

Gly Val  Leu Val Leu Glu Arg  Leu Ser Asp Ala Arg  Lys Asn Gly 
    2000                 2005                 2010 

His Glu  Val Leu Ala Val Ile  Arg Gly Ser Ala Leu  Asn Gln Asp 
    2015                 2020                 2025 

Gly Ala  Ser Asn Gly Leu Thr  Ala Pro Asn Gly Pro  Ser Gln Gln 
    2030                 2035                 2040 

Arg Val  Ile Arg Gln Ala Leu  Ala Ser Ala Gly Leu  Thr Thr Ser 
    2045                 2050                 2055 

Asp Val  Asp Ala Val Glu Ala  His Gly Thr Gly Thr  Thr Leu Gly 
    2060                 2065                 2070 

Asp Pro  Ile Glu Ala Gln Ala  Val Leu Ala Thr Tyr  Gly Gln Asp 
    2075                 2080                 2085 

Arg Ala  Ala Asp Gln Pro Leu  Trp Leu Gly Ser Ala  Lys Ser Asn 
    2090                 2095                 2100 

Phe Gly  His Thr Gln Ala Ala  Ala Gly Val Ala Gly  Val Ile Lys 
    2105                 2110                 2115 

Met Val  Met Ala Ile Arg Asn  Gly Val Leu Pro Lys  Thr Leu His 
    2120                 2125                 2130 

Val Ser  Glu Pro Ser Thr His  Val Asp Trp Ser Ala  Gly Ala Val 
    2135                 2140                 2145 

Glu Leu  Leu Ala Glu Ala Arg  Glu Trp Pro Glu Thr  Gly Arg Pro 
    2150                 2155                 2160 

Arg Arg  Ala Gly Val Ser Ser  Phe Gly Val Ser Gly  Thr Asn Ala 
    2165                 2170                 2175 

His Val  Ile Val Glu Gln Ala  Pro Thr Glu Glu Gln  Ala Pro Ala 
    2180                 2185                 2190 

Asp Ala  Pro Ala Pro Thr Asp  Ala Pro Ala Gly Thr  Pro Val Pro 
    2195                 2200                 2205 

Trp Ile  Val Ser Gly Arg Thr  Ala Asp Ser Leu Arg  Asp Gln Ala 
    2210                 2215                 2220 

Arg Arg  Leu Leu Glu His Leu  Asp Arg Asn Gly Asp  Leu Asp Pro 
    2225                 2230                 2235 

Gln Asp  Val Ala Arg Ala Leu  Leu Thr Thr Arg Thr  Arg Phe His 
    2240                 2245                 2250 

His Arg  Ala Ala Val Val Ala  Thr Glu Arg Gln Asp  Ile Val Ala 
    2255                 2260                 2265 

Ala Leu  Glu Ala Leu Ala Asp  Gly Arg Pro Val Ser  Gly Leu Val 
    2270                 2275                 2280 

Gln Gly  Thr Ala Thr Thr Met  Ala Lys Ser Ala Phe  Leu Phe Thr 
    2285                 2290                 2295 

Gly Gln  Gly Ala Gln Arg Val  Gly Met Gly Arg Glu  Leu Ala Ala 
    2300                 2305                 2310 

Glu Phe  Pro Val Phe Ala Ala  Ser Leu Glu Gln Thr  Cys Gly Leu 
    2315                 2320                 2325 

Leu Glu  Arg Ala Gly Val Ala  Val Arg Glu Val Leu  Phe Ala Glu 
    2330                 2335                 2340 

Glu Gly  Ser Ala Glu Ala Ala  Leu Leu Thr Arg Thr  Val Tyr Ala 
    2345                 2350                 2355 

Gln Ala  Ala Leu Phe Ala Val  Glu Val Ala Leu Phe  Arg Leu Val 
    2360                 2365                 2370 

Glu Ser  Phe Gly Val Val Pro  Asp Phe Val Ala Gly  His Ser Val 
    2375                 2380                 2385 

Gly Glu  Ile Ala Ala Ala His  Val Ala Gly Val Phe  Ser Leu Glu 
    2390                 2395                 2400 

Asp Ala  Val Ser Leu Val Ala  Ala Arg Gly Arg Leu  Met Asp Ala 
    2405                 2410                 2415 

Leu Pro  Glu Gly Gly Ala Met  Val Ala Val Gln Ala  Thr Glu Glu 
    2420                 2425                 2430 

Asp Val  Leu Ala Leu Leu Glu  Gly Val Glu Asp Ala  Ser Ile Ala 
    2435                 2440                 2445 

Ala Ile  Asn Gly Pro Asp Ala  Val Val Val Ser Gly  Thr Glu Thr 
    2450                 2455                 2460 

Gly Val  Ala Arg Val Val Asp  Val Leu Arg Glu Arg  Gly Ala Lys 
    2465                 2470                 2475 

Thr Lys  Arg Leu Asp Val Ser  His Ala Phe His Ser  Pro Leu Met 
    2480                 2485                 2490 

Glu Pro  Met Leu Ala Asp Phe  Ala Arg Val Val Ala  Gly Leu Ser 
    2495                 2500                 2505 

Tyr Glu  Asp Pro Ala Ile Pro  Val Val Ser Asn Val  Ser Gly Ser 
    2510                 2515                 2520 

Met Ala  Asp Gly Glu Leu Ser  Thr Pro Gly Tyr Trp  Val Arg His 
    2525                 2530                 2535 

Val Arg  Glu Ala Val Arg Phe  Gly Ala Gly Val Glu  Thr Leu Leu 
    2540                 2545                 2550 

Gly Ala  Gly Val Ser Ser Phe  Leu Glu Ile Gly Pro  Asp Gly Val 
    2555                 2560                 2565 

Leu Ser  Gly Met Ala Arg Thr  Ser Val Pro Glu Gly  Ala Asp Val 
    2570                 2575                 2580 

Glu Cys  Ala Pro Leu Met Arg  Arg Asp Arg Ala Glu  Val Arg Glu 
    2585                 2590                 2595 

Phe Leu  Thr Gly Leu Ser Arg  Leu Ala Val Arg Gly  Val Pro Val 
    2600                 2605                 2610 

Ser Trp  Ser Pro Leu Val Ala  Gly Gly Arg Arg Val  Glu Leu Pro 
    2615                 2620                 2625 

Thr Tyr  Ala Phe Gln Arg Arg  Arg Phe Trp Leu Asp  Ala Gly His 
    2630                 2635                 2640 

Ser Val  Thr Asp Ala Ser Gly  Leu Gly Gln Thr Ala  Ala Gly His 
    2645                 2650                 2655 

Pro Leu  Ile Gly Ala Val Val  Gly Leu Ala Gly Gly  Asp Gly Val 
    2660                 2665                 2670 

Val Leu  Thr Gly Arg Val Ser  Leu His Thr His Pro  Trp Leu Ala 
    2675                 2680                 2685 

Asp His  Gln Val Ala Gly Val  Thr Leu Leu Pro Gly  Thr Gly Phe 
    2690                 2695                 2700 

Val Glu  Leu Ala Val Arg Ala  Gly Asp Glu Val Gly  Cys Gly Arg 
    2705                 2710                 2715 

Leu Glu  Glu Leu Thr Leu Glu  Ala Pro Leu Val Val  Pro Asp Arg 
    2720                 2725                 2730 

Gly Ala  Val Gln Leu Gln Val  Val Val Gly Gly Leu  Glu Glu Ser 
    2735                 2740                 2745 

Gly Val  Arg Thr Val Ser Val  Tyr Ser Arg Ala Glu  Asp Thr Asp 
    2750                 2755                 2760 

Asn Pro  Asp Thr Pro Trp Thr  Arg His Ala Ser Gly  Ala Leu Gly 
    2765                 2770                 2775 

Thr Ala  Ala Asp Pro Ala Asp  Phe Asp Leu Thr Ala  Trp Pro Pro 
    2780                 2785                 2790 

Ala Gly  Thr Glu Ala Val Glu  Ile Gly Asp Phe Tyr  Gly Glu Leu 
    2795                 2800                 2805 

Ala Ala  Thr Pro Asp Gly Leu  Val Tyr Gly Pro Leu  Phe Gln Gly 
    2810                 2815                 2820 

Leu Thr  Ala Ala Trp Arg Lys  Gly Asp Glu Val Tyr  Ala Glu Ile 
    2825                 2830                 2835 

Glu Leu  Pro Glu Gly Ala Ala  Val Asp Ala Ala Arg  Phe Gly Met 
    2840                 2845                 2850 

His Pro  Ala Leu Leu Asp Ala  Ala Leu His Ala Val  Gly Leu Ser 
    2855                 2860                 2865 

Asn Asp  Ala Asp Ala Asp Ala  Asp Ala Gly Thr Ala  Gln Glu Asp 
    2870                 2875                 2880 

Gly Thr  Val Ala Arg Leu Pro  Phe Ala Trp Ser Gly  Val Thr Leu 
    2885                 2890                 2895 

His Arg  Ser Gly Ala Thr Arg  Leu Arg Leu Ser Val  Arg Pro Thr 
    2900                 2905                 2910 

Gly Gly  Asp Ser Tyr His Leu  Arg Ile Ala Asp Ala  Val Gly Ala 
    2915                 2920                 2925 

Pro Val  Ala Thr Val Gly Glu  Leu Leu Leu Arg Gly  Ile Ser Ala 
    2930                 2935                 2940 

Glu Gln  Leu Ala Arg Ala Gly  Thr Asp Arg Pro Asp  Ala Leu Phe 
    2945                 2950                 2955 

Arg Leu  Glu Trp Glu Ala Leu  Arg Gly Asp Gly Ala  Thr Thr Ala 
    2960                 2965                 2970 

Gly Glu  Trp Ala Leu Leu Gly  Gly Asp Pro Tyr Gly  Leu Ala Pro 
    2975                 2980                 2985 

Ala Arg  Ala Val Pro Tyr Gly  Asp Leu Asp Ala Leu  Ala Ala Glu 
    2990                 2995                 3000 

Ala Glu  Gly Gly Thr Pro Pro  Glu Val Val Leu Leu  Pro Leu Thr 
    3005                 3010                 3015 

Val Pro  Ala Gly Glu Glu Pro  Asp Ala Gly Glu Arg  Ala Ala His 
    3020                 3025                 3030 

Arg Ala  Leu Arg Ala Val Arg  Ser Trp Leu Ala Asp  Asp Arg Phe 
    3035                 3040                 3045 

Ala Ala  Ala Thr Leu Val Leu  Met Thr Arg Gly Ala  Leu Ala Ala 
    3050                 3055                 3060 

Thr Pro  Gly Asp Glu Val Thr  Asp Val Ala Gly Ala  Glu Val Trp 
    3065                 3070                 3075 

Gly Leu  Val Arg Ser Ala Gln  Thr Glu His Pro Gly  Arg Phe Val 
    3080                 3085                 3090 

Leu Val  Asp Ser Asp Gly Ser  Glu Ala Ser Ala Arg  Ala Leu Pro 
    3095                 3100                 3105 

Ala Ala  Val Ala Ser Gly Glu  Pro Gln Leu Ala Leu  Arg Ala Gly 
    3110                 3115                 3120 

Thr Val  Asn Ala Ala Arg Leu  Gly Arg Val Glu Arg  Ala Gly Ala 
    3125                 3130                 3135 

Glu Ala  Val Ala Thr Phe Asp  Pro Glu Arg Thr Val  Leu Ile Thr 
    3140                 3145                 3150 

Gly Gly  Thr Gly Ala Leu Ala  Gly Gln Leu Ala Arg  His Leu Ala 
    3155                 3160                 3165 

Arg Ala  Tyr Gly Val Arg His  Leu Leu Leu Ala Gly  Arg Arg Gly 
    3170                 3175                 3180 

Pro Ser  Ala Pro His Ala Ala  Glu Leu Val Ala Glu  Leu Ala Glu 
    3185                 3190                 3195 

Leu Gly  Ala Leu Ala Glu Val  Val Ala Cys Asp Val  Ala Asp Arg 
    3200                 3205                 3210 

Glu Ala  Leu Thr Ala Leu Leu  Ala Ala Val Pro Ala  Asp Arg Pro 
    3215                 3220                 3225 

Leu Gly  Ala Val Val His Thr  Ala Gly Val Leu Asp  Asp Gly Leu 
    3230                 3235                 3240 

Val Glu  Ser Leu Thr Pro Glu  Arg Leu Asp Ala Val  Leu His Pro 
    3245                 3250                 3255 

Lys Ala  Thr Ala Ala Leu Leu  Leu Asp Glu Leu Thr  Arg Asp Ala 
    3260                 3265                 3270 

Asp Leu  Thr Ala Phe Val Leu  Phe Ser Ser Ala Ala  Gly Thr Leu 
    3275                 3280                 3285 

Gly Ser  Pro Gly Gln Ala Asn  Tyr Ala Ala Ala Asn  Ala Gly Leu 
    3290                 3295                 3300 

Asp Ala  Leu Ala Val Arg Arg  Arg Gly Gln Gly Leu  Pro Gly Leu 
    3305                 3310                 3315 

Ser Leu  Gly Trp Gly Leu Trp  Gln Ala Asp Gly Gly  Met Gly Gly 
    3320                 3325                 3330 

Ala Leu  Ser Gly Gly Asp Gln  Ala Arg Ile Ala Arg  Gly Gly Val 
    3335                 3340                 3345 

Ala Ala  Leu Thr Thr Asp His  Gly Leu Ala Leu Phe  Asp Thr Ala 
    3350                 3355                 3360 

Cys Ala  Gly Pro Asp Ala Val  Val Leu Pro Met Leu  Leu Asp Leu 
    3365                 3370                 3375 

Arg Pro  Gln Asp Asp Val Pro  His Leu Leu Arg Ser  Leu Val Ser 
    3380                 3385                 3390 

Ala Arg  Arg Lys Gly Ala Ser  Ala Gly Ala Arg His  Glu Gly Pro 
    3395                 3400                 3405 

Ala Glu  Leu Arg Arg Arg Leu  Ala Ala Ala Thr Pro  Asp Glu Arg 
    3410                 3415                 3420 

Tyr Glu  His Leu Leu Gly Leu  Val Arg Ser Cys Thr  Ala Val Val 
    3425                 3430                 3435 

Leu Gly  His Arg Gly Pro Gln  Asp Val Asp Pro Gly  Val Gly Phe 
    3440                 3445                 3450 

Leu Glu  Ser Gly Phe Asp Ser  Leu Thr Ala Met Glu  Leu Arg Asn 
    3455                 3460                 3465 

Gln Leu  Asn Glu Ala Thr Gly  Leu Arg Leu Ala Ala  Thr Val Val 
    3470                 3475                 3480 

Phe Asp  His Thr Thr Pro Ala  Asp Leu Ala Arg His  Leu Val Asp 
    3485                 3490                 3495 

Gly Val  Ala Asp Thr Val Ala  Ala Ala Pro Gly Gln  Gln Pro Ala 
    3500                 3505                 3510 

Pro Arg  Ser Asp Asp Asp Ala  Asp Thr Leu Ser Gly  Leu Phe Arg 
    3515                 3520                 3525 

Thr Ala  Val Arg Ala Gly Gln  Val Thr Lys Gly Val  Asp Leu Leu 
    3530                 3535                 3540 

Arg Ala  Val Ala Glu Leu Arg  Pro Ala Phe His Ser  Ala Asp Glu 
    3545                 3550                 3555 

Leu Gly  Asp Asp Leu Pro Val  Pro Val Arg Leu Ala  Gln Gly Pro 
    3560                 3565                 3570 

Ser Ala  Ala Arg Leu Phe Cys  Phe Ala Ser Pro Met  Ala Met Gly 
    3575                 3580                 3585 

Gly Thr  His Gln Tyr Ala Arg  Leu Ala Ala His Phe  Arg Gly Val 
    3590                 3595                 3600 

Arg Glu  Val Ser Ala Leu Pro  Met Pro Gly Phe Ala  Thr Gly Asp 
    3605                 3610                 3615 

Leu Leu  Pro Ala Thr Ala Glu  Ala Val Val Glu Val  Phe Gly Arg 
    3620                 3625                 3630 

Ser Leu  Leu Arg Ala Ala Gly  Asp Glu Pro Phe Val  Leu Leu Gly 
    3635                 3640                 3645 

Tyr Ser  Ala Gly Gly Val Phe  Ala His Ala Val Ala  Ala Trp Leu 
    3650                 3655                 3660 

Glu Ser  Glu Gly Cys Ala Pro  Ala Ala Val Val Leu  Leu Asp Ser 
    3665                 3670                 3675 

Tyr Arg  Ala Asp Gly Gly Thr  Ser Met Asp Gly Asp  Phe Trp Val 
    3680                 3685                 3690 

Ser Met  Val Glu Gly Leu Phe  Ser Arg Glu Glu Val  Phe Gly Arg 
    3695                 3700                 3705 

Phe Thr  Ser Ala Arg Leu Ser  Ala Met Gly Arg Tyr  Ala Arg Leu 
    3710                 3715                 3720 

Val Gly  Glu Val Lys Thr Gly  Glu Val Lys Ala Pro  Val Leu Phe 
    3725                 3730                 3735 

Val Arg  Pro Glu Arg Ser Leu  Ser Ala Ser Ala Asp  Ala Gly Gly 
    3740                 3745                 3750 

Val Gly  Gly Gly Asp Ala Gly  Ala Ala Ala Ala Thr  Asp Asp Trp 
    3755                 3760                 3765 

Arg Ala  Ser Trp Asp Thr Ala  Glu Thr Val Leu Glu  Val Ala Gly 
    3770                 3775                 3780 

Asp His  Phe Asp Ile Ile Glu  Ser Gln Ala Ala Ala  Thr Ala Asp 
    3785                 3790                 3795 

Ala Val  Glu Gly Trp Leu Ala  Asp Arg Val 
    3800                 3805 

 
           
             8  
             236  
             PRT  
             Streptomyces halstedii sp.HC-34  
           
            8 

Met Tyr Glu Glu Asp Phe Ala Arg Val Tyr Asp Asp Ile Tyr Arg Arg 
1               5                   10                  15 

His Lys Asp Tyr Ala Gly Glu Ala Ala Arg Ile Arg Glu Leu Ala Leu 
            20                  25                  30 

Glu Arg Asn Pro Gly Ala Ala Asp Leu Leu Asp Val Gly Cys Gly Thr 
        35                  40                  45 

Gly Glu His Leu Ala Leu Leu Arg Asp Asp Phe Ala Val Thr Gly Val 
    50                  55                  60 

Asp Leu Ser Ala Pro Met Val Arg Val Ala Glu Ala Lys Leu Pro Gly 
65                  70                  75                  80 

Val Pro Val His Glu Gly Asp Met Arg Thr Phe Gly Leu Asp Arg Ser 
                85                  90                  95 

Phe Asp Val Ile Cys Ser Met Tyr Ser Ser Val Gly Tyr Leu Glu Thr 
            100                 105                 110 

Leu Asp Gly Leu Phe Ala Ala Leu Lys Asn Met Ala His His Leu Arg 
        115                 120                 125 

Pro Gly Gly Val Leu Ile Ile Glu Pro Trp Ile Leu Arg Asp Ser Trp 
    130                 135                 140 

Asn Gly Gly Asp Leu Val Glu Ala Ser Phe Glu Asn Glu Gly Gly Lys 
145                 150                 155                 160 

Val Val Arg Met Gly Arg Trp Thr Thr Arg Ala Gly Arg Ser His Val 
                165                 170                 175 

Glu Met His Tyr Leu Val Thr Ser Gly Asp Asp Pro Val Arg His Phe 
            180                 185                 190 

Val Asp Glu Gln Glu Leu Ser Leu Phe Ser Lys Asp Glu Tyr Glu Glu 
        195                 200                 205 

Ala Phe Arg Ala Ala Gly Cys Ser Val Glu Tyr Leu Pro Asp Gly Tyr 
    210                 215                 220 

Val Asp Arg Gly Val Phe Val Gly Val Arg Gln Pro 
225                 230                 235 

 
           
             9  
             397  
             PRT  
             Streptomyces halstedii sp.HC-34  
           
            9 

Leu Arg Leu Gly Ala Gly Glu Arg Asn Asp Glu Gln Val Thr Asp Ser 
1               5                   10                  15 

Pro Val Phe Arg Glu Pro Leu His Val Gly Arg Pro Asn Ile Gly Ser 
            20                  25                  30 

Arg Ala Arg Leu Thr Glu Arg Leu Glu Gly Ala Leu Asp Arg Leu Tyr 
        35                  40                  45 

Leu Thr Asn Gly Pro Leu Val Arg Glu Phe Glu Glu Arg Leu Ala Glu 
    50                  55                  60 

Val Ala Gly Val Asp His Cys Val Ala Val Cys Asn Ala Thr Ile Gly 
65                  70                  75                  80 

Leu Gln Val Ala Ala Lys Ala Ala Gly Ile Arg Gly Gly Asp Glu Val 
                85                  90                  95 

Ile Val Pro Ala Phe Thr Trp Val Ala Thr Ala Ala Ala Leu Asp Trp 
            100                 105                 110 

Ile Gly Ile Val Pro Val Phe Cys Asp Ala Asp Glu Thr Thr Gly Asn 
        115                 120                 125 

Ile Asp Trp Thr Lys Val Glu Ala Leu Ile Gly Pro Arg Thr Arg Gly 
    130                 135                 140 

Ile Met Gly Val His Val Phe Gly Arg Pro Cys Glu Val Asp Glu Leu 
145                 150                 155                 160 

Glu Glu Ile Ala Gly Arg His Gly Leu Pro Leu Leu Phe Asp Ser Ala 
                165                 170                 175 

His Ala Ile Gly Cys Thr Tyr Lys Gly Arg Pro Val Gly Gly Phe Gly 
            180                 185                 190 

Thr Ala Glu Val Tyr Ser Phe His Ala Thr Lys Phe Val Asn Ser Phe 
        195                 200                 205 

Glu Gly Gly Ala Ile Val Thr Arg Asp Ala Glu Phe Ala Glu Arg Cys 
    210                 215                 220 

Arg Glu Leu Arg Asn Phe Gly Ile Thr Ser Ala Gly Glu Ile Arg Ser 
225                 230                 235                 240 

Gly Gly Thr Asn Ala Lys Met Asn Glu Ala Ala Ala Ala Met Gly Leu 
                245                 250                 255 

Thr Ser Leu Glu Val Met Asp Ser Leu Met Glu Ala Asn Arg Ile Asn 
            260                 265                 270 

His Gly Arg Tyr Glu Lys Gly Leu Asp Gly Leu Pro Gly Val Trp Val 
        275                 280                 285 

Arg Gly Gln Ala Glu Gly Glu Arg Ala Asn His Gln Tyr Leu Val Ile 
    290                 295                 300 

Glu Ile Asp Ala Ala Val Ala Gly Ile His Arg Asp Glu Val His Thr 
305                 310                 315                 320 

Ala Leu Ile Ala Gln Asn Val Leu Ser Arg Arg Tyr Phe His Pro Ser 
                325                 330                 335 

Cys His Gln Val Glu Pro Tyr Leu Ser Asp Pro Ala Arg His Ala Pro 
            340                 345                 350 

His Pro Leu Pro His Ala Glu Ala Leu Ala Glu Arg Val Leu Ala Leu 
        355                 360                 365 

Pro Thr Gly Thr Thr Val Gly Pro Ser Glu Ile Asp Gln Val Cys Asp 
    370                 375                 380 

Ile Ile Arg Arg Cys Val Ser Ala Arg Thr Pro Ala Arg 
385                 390                 395 

 
           
             10  
             493  
             PRT  
             Streptomyces halstedii sp.HC-34  
           
            10 

Met Glu Ile Ser Met Thr Glu Thr Leu Ser Thr Leu Pro Pro Thr His 
1               5                   10                  15 

Thr Gly Asp Glu Ser Leu Ala Val Arg Ile Ala Lys Ser Val Ser Val 
            20                  25                  30 

Val Asp Asp Gly Ala Leu His Ser Leu Asp Glu Phe His Asp Trp Phe 
        35                  40                  45 

Thr Ala Arg Gly Gln Arg Thr Ala His Val Glu Arg Val Pro Leu Asp 
    50                  55                  60 

Glu Leu Thr Gly Trp Ser Ser Asp Pro Val Thr Gly Asn Ile Gly His 
65                  70                  75                  80 

Asp Ser Gly Lys Phe Phe Ser Val Gln Gly Leu Ser Val Glu Leu Pro 
                85                  90                  95 

Gly Ala Pro Val Pro Ala Trp Ala Gln Pro Ile Ile Asn Gln Pro Glu 
            100                 105                 110 

Ile Gly Ile Leu Gly Ile Leu Ile Lys Glu Phe Asn Gly Val Leu His 
        115                 120                 125 

Cys Leu Met Gln Ala Lys Leu Glu Pro Gly Asn Arg Asn Gly Leu Gln 
    130                 135                 140 

Leu Ser Pro Thr Val Gln Ala Thr Arg Ser Asn Tyr Thr Arg Val His 
145                 150                 155                 160 

Gln Gly Asn Pro Val Pro Tyr Val Gly Tyr Phe Gln Asp Thr Ser Ala 
                165                 170                 175 

Asn Arg Val Ile Thr Asp Ala Leu Gln Ser Glu Gln Gly Ser Trp Phe 
            180                 185                 190 

Tyr Gln Lys Arg Asn Arg Asn Met Val Val Glu Thr Glu Ala Glu Ile 
        195                 200                 205 

Glu Gln His Glu Ala Phe Met Trp Leu Thr Ile Gly Gln Leu His Arg 
    210                 215                 220 

Leu Leu Ala Ile Asp Asp Leu Ile Asn Met Asp Thr Arg Thr Val Leu 
225                 230                 235                 240 

Ser Cys Leu Pro Phe Ser Gly Ala Gln Leu Ala Glu Gln Leu Pro Gly 
                245                 250                 255 

Thr Gly Gly Asp Leu Arg Met Pro Ile Leu Arg Ser Cys Ser Glu Asp 
            260                 265                 270 

Gln Gly Ser Leu His Thr Thr Gly Asp Leu Leu Ser Trp Ile Thr Asp 
        275                 280                 285 

Ala Arg Thr Arg Asn Glu Val Arg Thr Arg Leu Thr Pro Leu Arg Asp 
    290                 295                 300 

Val Ala Gly Trp Arg Arg Thr Pro Asp Ala Ile Thr His Asp Thr Gly 
305                 310                 315                 320 

Arg Phe Phe Asp Val Met Ala Val Arg Ile Glu Thr Asp Gly Asp Arg 
                325                 330                 335 

Glu Val Arg Gln Trp Thr Gln Pro Met Ile Ala Pro Ala Gly Ile Gly 
            340                 345                 350 

Ile Val Ala Phe Leu Val Lys Arg Ile Asp Gly Val Leu His Val Leu 
        355                 360                 365 

Ala His Ala Arg Val Glu Pro Gly Tyr Leu Asp Val Val Glu Leu Ser 
    370                 375                 380 

Pro Thr Val Met Cys Thr Pro Gly Asn Tyr Glu Gly Leu Pro Ala Ala 
385                 390                 395                 400 

Ala Arg Pro Pro Phe Leu Gly Glu Val Leu Ser Ala Arg Pro Glu Gln 
                405                 410                 415 

Val Arg Phe Glu Thr Ile Leu Ser Glu Glu Gly Gly Arg Phe Tyr His 
            420                 425                 430 

Ala Gln Asn Arg Tyr Ile Ile Val Glu Ser Asp Ile Asp Val Ala Pro 
        435                 440                 445 

Glu Leu Ala Ser Glu Tyr Arg Trp Met Ala Leu His Gln Met Val Gly 
    450                 455                 460 

Leu Leu Arg His Ser His Tyr Val Asn Val Gln Ala Arg Ser Leu Ile 
465                 470                 475                 480 

Ala Cys Leu His Ser Leu Ser Gly Ala Gln Gly Arg Asn 
                485                 490 

 
           
             11  
             330  
             PRT  
             Streptomyces halstedii sp.HC-34  
           
            11 

Val Thr Met Leu Tyr Arg Gln Leu Gly Arg Thr Ala Leu Lys Val Ser 
1               5                   10                  15 

Pro Leu Cys Leu Gly Thr Leu Asn Leu Gly Val Arg Thr Thr Arg Asp 
            20                  25                  30 

Glu Ala Phe Ala Leu Met Asp Glu Ala Leu Glu Gln Gly Ile Asn Phe 
        35                  40                  45 

Phe Asp Thr Ala Asn Gln Tyr Gly Trp Gln Val His Lys Gly Leu Thr 
    50                  55                  60 

Glu Glu Ile Ile Gly Glu Trp Phe Ala Gln Gly Gly Gly Arg Arg Glu 
65                  70                  75                  80 

Arg Val Val Leu Gly Thr Lys Val Cys Asn Pro Met Ser Asp Leu Pro 
                85                  90                  95 

Asn Asp Gln Gly Leu Ser Ala Arg His Ile Ile Ala Ser Cys Glu Asp 
            100                 105                 110 

Ser Leu Arg Arg Leu Arg Thr Asp Trp Ile Asp Val Tyr Gln Leu His 
        115                 120                 125 

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

Thr Leu Val His Gln Gly Lys Ile Arg Tyr Val Gly Ser Ser Asn Phe 
145                 150                 155                 160 

Ala Gly Trp His Leu Ala Asp Ala Gln Ala Ala Ala Ala Arg Arg Asn 
                165                 170                 175 

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

Tyr Val Glu Met Glu Val Val Pro Ala Ala Arg Ala His Gly Ile Gly 
        195                 200                 205 

Val Leu Ala Trp Ser Pro Leu His Gly Gly Leu Leu Ser Gly Ala Leu 
    210                 215                 220 

Arg Lys Leu Asp Glu Gly Thr Ala Val Lys Thr Ala Gln Gly Arg Ala 
225                 230                 235                 240 

Gln Ile Ala Leu Arg Thr Met Arg Asp Thr Val Glu Gln Tyr Glu Lys 
                245                 250                 255 

Leu Cys Glu Ser Ile Ser Ala Asp Pro Ser Gln Val Ala Leu Ala Trp 
            260                 265                 270 

Leu Leu Ser Arg Pro Gly Leu Thr Ala Ala Val Ile Gly Pro Arg Thr 
        275                 280                 285 

Thr Gly His Leu Ala Ser Ala Leu Glu Thr Leu Asp Met Thr Leu Pro 
    290                 295                 300 

Glu Asp Ile Leu Ala Pro Leu Asp Glu Leu Phe Pro Pro Ile Gly Asn 
305                 310                 315                 320 

Gly Gln Pro Ala Pro Ala Thr Trp Leu Ala 
                325                 330 

 
           
             12  
             158  
             PRT  
             Streptomyces halstedii sp.HC-34  
           
            12 

Met Pro Asp Ile Thr Ser Glu Arg Leu Pro Asp Gln Asp His His Leu 
1               5                   10                  15 

Pro Ala Glu Arg Ala Arg Pro Val Leu Ile Ser Ser Val Ala Ser Asp 
            20                  25                  30 

Ser His Thr Trp Asn Leu Val Phe Leu Gln Leu Leu Ile Glu Glu Leu 
        35                  40                  45 

Gly His Glu Val Ile Asn Leu Gly Pro Cys Val Pro Asp Glu Leu Leu 
    50                  55                  60 

Ile Ala Glu Cys Arg Asp Arg Arg Pro Gly Leu Val Val Ile Ser Thr 
65                  70                  75                  80 

Val Asn Gly His Gly Tyr Gln Asp Gly Leu Arg Val Ile Gly Lys Leu 
                85                  90                  95 

Arg Ala Cys Glu Asp Leu Ala Asn Ile Pro Val Val Ile Gly Gly Lys 
            100                 105                 110 

Leu Gly Val Ser Gly Pro Gly Gln Ser Tyr Ala Ala Glu Leu Ala Gly 
        115                 120                 125 

Ala Gly Phe Asp Ala Val Phe Pro Asp Gly Ala Glu Ala Val Ser Ser 
    130                 135                 140 

Phe Thr Arg Tyr Val Glu Lys Leu Pro Gln Arg Val Val Ser 
145                 150                 155 

 
           
             13  
             469  
             PRT  
             Streptomyces halstedii sp.HC-34  
           
            13 

Leu Thr Gly Phe Gly Ala Tyr Val Arg Ser Val His Arg Arg Gly Glu 
1               5                   10                  15 

Leu Val Val Gln Pro Arg Met Gly Phe Ser Gly Thr Val Glu Met Arg 
            20                  25                  30 

Ala Gly Leu Ala Ala Thr Arg Ala Ala Asp Ala Ala Thr Val Gly Thr 
        35                  40                  45 

Ile Thr Leu Asp Ser Tyr Thr Arg Val Gly Glu Leu Ala Ala Ala Glu 
    50                  55                  60 

Glu Ala Leu Arg Ser Gly Ile Ala Leu Asn Gly Tyr Pro Ile Val Thr 
65                  70                  75                  80 

Tyr Asp Glu Ser Thr Thr Arg Glu Leu Leu Ala Gly Ile Ala Gly Glu 
                85                  90                  95 

Asp Phe Pro Val Gln Ile Arg His Gly Ser Ala Thr Pro Leu His Ile 
            100                 105                 110 

Phe Gly Ala Leu Thr Arg Ala Gly Leu Asp Ala Thr Glu Gly Gly Pro 
        115                 120                 125 

Val Ser Tyr Cys Leu Pro Tyr Gly Arg Ile Pro Leu Glu Gln Ser Val 
    130                 135                 140 

Thr Asn Trp Thr Arg Cys Cys Glu Glu Phe Ala Arg Leu Arg Gly Leu 
145                 150                 155                 160 

Gly Arg Glu Pro His Leu Glu Thr Phe Gly Gly Cys Met Leu Gly Gln 
                165                 170                 175 

Leu Cys Pro Pro Ser Gln Leu Val Ala Ile Ser Met Leu Glu Ala Leu 
            180                 185                 190 

Phe Phe His Gln His Gly Ile Arg Ser Ile Ser Leu Ser Tyr Ala Gln 
        195                 200                 205 

Gln Thr His Gln Gly Gln Asp Glu Glu Ala Val Leu Ala Leu Arg Arg 
    210                 215                 220 

Leu His Arg Glu Leu Leu Pro Asp Ala Asp Cys His Ile Val Ile Tyr 
225                 230                 235                 240 

Ala Tyr Met Gly Val Tyr Pro Thr Thr Pro Glu Gly Ala His Ala Leu 
                245                 250                 255 

Leu Gly Arg Ala Ala Glu Leu Ala Val Ala Thr Gly Ala Glu Arg Leu 
            260                 265                 270 

Ile Val Lys Thr Ala Ala Glu Ala His Arg Ile Pro Thr Ile Gly Glu 
        275                 280                 285 

Asn Val Ala Ala Leu Glu His Ala Ala Thr Val Ser Arg Ala Ala Arg 
    290                 295                 300 

Arg Ala Thr Ala Leu Pro Ala Gly His Ser Ala Ala Pro Ala Ala Thr 
305                 310                 315                 320 

Asp Pro Thr Ala Ala Leu Thr Ala Arg Pro Gly Thr Tyr Ala Asp Gly 
                325                 330                 335 

Ser Ala Ala Leu Thr Ala Gly Pro Gly Ala Ala Arg Asp Gly Ser Thr 
            340                 345                 350 

Asp Ser Ala Val Tyr Ala Glu Ala Arg Ala Leu Ile Glu Ala Val Met 
        355                 360                 365 

Asn Cys Gly Pro Asp Val Gly Thr Ala Leu Phe Arg Ala Phe Lys Arg 
    370                 375                 380 

Gly Tyr Leu Asp Ile Pro Tyr Cys Leu His Pro Asp Asn Met Gly Arg 
385                 390                 395                 400 

Ser Arg Ser Tyr Ile Asp Asp Thr Gly Arg Leu Gln Trp Ala Glu Thr 
                405                 410                 415 

Gly Met Leu Pro Leu Gly Asn Ala Arg Lys Ser Gly Thr Gly Arg Ser 
            420                 425                 430 

Val Ser Ser Thr Asp Leu Ile Ser Ala Leu Ser Phe Val Gln Arg Thr 
        435                 440                 445 

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

Arg Gln Gln Arg Pro 
465 

 
           
             14  
             299  
             PRT  
             Streptomyces halstedii sp.HC-34  
           
            14 

Met Ser Lys Pro Pro Ser Ala Lys Gly Thr Val Pro Phe Gly Gln Tyr 
1               5                   10                  15 

Arg Thr Trp Tyr Arg Val Thr Gly Asp Leu His Ser Gly Lys Pro Pro 
            20                  25                  30 

Val Val Leu Leu His Gly Gly Pro Gly Ser Thr His Asp Tyr Leu Leu 
        35                  40                  45 

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

Gln Leu Gly Asn Gly Gly Ser Thr His Leu Pro Glu Lys Gly Glu Asp 
65                  70                  75                  80 

Phe Trp Thr Val Gln Leu Phe Glu Asp Glu Leu Asp Asn Leu Leu Asn 
                85                  90                  95 

Gln Leu Gly Ile Ala Gly Asp Tyr Val Leu Phe Gly Gln Ser Trp Gly 
            100                 105                 110 

Gly Met Leu Gly Ser Val His Ala Ala Arg Arg Pro Ala Gly Leu Arg 
        115                 120                 125 

Gly Leu Val Val Ala Asn Ala Pro Ala Ser Met Lys Ile Trp Leu Gln 
    130                 135                 140 

Glu Met Ala Arg Leu Arg Ala Leu Leu Pro Pro Asp Val Gln Glu Thr 
145                 150                 155                 160 

Leu Leu Lys His Glu Ala Ala Arg Thr Thr Asp Thr Glu Glu Tyr Phe 
                165                 170                 175 

His Ala Met Arg Ala Phe Tyr Asp Arg His Val Cys Arg Ile Val Pro 
            180                 185                 190 

Trp Pro Arg Asp Phe Ala Ala Thr Phe Met Glu Ile Tyr Asn Asp Pro 
        195                 200                 205 

Thr Val Tyr Thr Thr Met Asn Gly Pro Asn Glu Phe His Val Ile Gly 
    210                 215                 220 

Thr Leu Arg Asp Trp Ser Val Glu Asp Cys Leu Pro Asp Ile Gln Val 
225                 230                 235                 240 

Pro Thr Met Val Leu Ile Gly Arg His Asp Glu Ala Thr Pro Ala Thr 
                245                 250                 255 

Val Lys Pro Phe Leu Asp Leu Val Pro Asp Val Arg Tyr Glu Val Leu 
            260                 265                 270 

Glu Asn Ser Ser His Val Pro His Leu Glu Glu Pro Glu Arg Phe His 
        275                 280                 285 

Glu Val Met Ile Asp Tyr Leu Glu Ser Leu Val 
    290                 295 

 
           
             15  
             327  
             PRT  
             Streptomyces halstedii sp.HC-34  
           
            15 

Val Asn Ala Thr Val Glu Thr Thr Gln His Asp Val Glu Gly Thr Gly 
1               5                   10                  15 

Ala Ala Gly Ala Thr Ala Met Leu Phe Pro Gly Met Gly Pro Ala Ala 
            20                  25                  30 

Phe Ser Asp Val Gly Arg Phe Met Val Thr Asn Arg Tyr Thr Arg Glu 
        35                  40                  45 

Leu Leu Ala Glu Ala Asp Asp Thr Leu Gly Tyr Ser Leu Val Asp Arg 
    50                  55                  60 

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

Leu Val Asn Cys Val Ala Leu Ala Arg Trp Ala Glu Gln Thr Met Asp 
                85                  90                  95 

Leu Thr Pro Arg Ile Cys Ala Gly Ala Ser Phe Gly Glu Lys Ser Val 
            100                 105                 110 

Ala Ala Tyr Ser Gly Ala Leu Thr Phe Ala Asp Ala Val Arg Met Thr 
        115                 120                 125 

Ala Gly Leu Ala Arg Cys Met Asp Glu Tyr Phe Arg Thr Glu His Leu 
    130                 135                 140 

Gly Val Val Thr His Ser Phe Val Arg Ala Pro Arg Glu Arg Leu Asp 
145                 150                 155                 160 

Glu Ile Leu Ala Glu Leu Asp Glu Arg Gly Glu Trp His Glu Ile Ser 
                165                 170                 175 

Cys His Ile Asp His Asp Phe Phe Met Leu Thr Leu His Glu Arg Asn 
            180                 185                 190 

Ser Val Trp Leu Glu Gly Arg Leu Arg Ser Val Gly Ala Met Pro Leu 
        195                 200                 205 

Tyr Ala Met Arg Pro Pro Met His Ala Ala Ala Phe Gly Gly Leu Arg 
    210                 215                 220 

Asp Lys Ala Glu Glu Glu Val Ile Ala Pro Leu Thr Phe His Asp Pro 
225                 230                 235                 240 

Thr Leu Pro Val Val Ala Asp Gln Asp Gly Lys Val Leu Thr Thr Gly 
                245                 250                 255 

Asp Glu Val Arg Thr Met Leu Leu Glu Ser Phe Val Arg Pro Leu Arg 
            260                 265                 270 

Trp Pro Asp Val Ile Ser Ser Leu Gln Asp Gln Gly Val Thr Arg Val 
        275                 280                 285 

Cys Val Ala Gly Pro Asp Ser Leu Phe Gly Arg Val Gly Thr Thr Thr 
    290                 295                 300 

Arg Ala Phe Glu Val Ile Ala Ala Thr Pro Arg Leu Ala Leu Gln Pro 
305                 310                 315                 320 

Arg Ala Arg Thr Thr Ser Arg 
                325 

 
           
             16  
             82  
             PRT  
             Streptomyces halstedii sp.HC-34  
           
            16 

Met Trp Asp Ala Gln Phe Glu Asn Leu Leu Arg Arg Tyr Leu Pro Phe 
1               5                   10                  15 

Leu Ser Ala Asp Gln Pro Leu Glu Gln Asp Ile Asn Leu Arg Asp Ile 
            20                  25                  30 

Gly Leu Asp Ser Leu Gly Thr Val Glu Leu Leu Ser Glu Leu Glu Asn 
        35                  40                  45 

Thr Tyr Asp Val His Phe Gln Asp Glu Ala Leu Thr Lys Glu Thr Phe 
    50                  55                  60 

Glu Thr Pro Gly Val Leu Trp Lys Thr Leu Ser Gln Met Val Glu Pro 
65                  70                  75                  80 

Arg His 

 
           
             17  
             524  
             PRT  
             Streptomyces halstedii sp.HC-34  
           
            17 

Met His Ala Ala Asp His Ala Leu His Ala Arg Phe Leu Arg Gly Leu 
1               5                   10                  15 

Ala Cys Ala Pro Asp Arg Pro Ala Val Arg Phe Gly Gly Arg Thr Leu 
            20                  25                  30 

Thr Tyr Ala Gln Ala His Arg Thr Ala Leu Thr Trp Ala Gly Ser Leu 
        35                  40                  45 

Leu Arg Ala Thr Pro Glu Pro Pro Ala Ala Val Gly Val Leu Ala Asp 
    50                  55                  60 

Lys Gly Ile Pro Ala Tyr Leu Gly Ile Leu Thr Ala Leu Tyr Ala Gly 
65                  70                  75                  80 

Ala Ala Val Val Pro Leu Arg Pro Asp Phe Pro Ala Ala Arg Thr Ala 
                85                  90                  95 

Glu Met Met Arg Ala Ala Gly Val Thr Ala Val Ile Ala Asp Gly Arg 
            100                 105                 110 

Gly Arg Arg Leu Leu Pro Glu Leu Leu Ala Asp Arg Arg Asp Thr Ala 
        115                 120                 125 

Val Leu Ala Ala Asp Glu Glu Gly Ala Pro Ala Asp Glu Ser Pro Ala 
    130                 135                 140 

Asp Gly Ser Ala Pro Gly Arg Arg Val Ala Ile Asp Glu Gly Tyr Ala 
145                 150                 155                 160 

Leu Thr Ala Pro Arg Asp Val Val Pro Asp Asp Thr Ala Tyr Val Leu 
                165                 170                 175 

Phe Thr Ser Gly Ser Thr Gly Arg Pro Lys Gly Val Pro Leu Ser His 
            180                 185                 190 

Gly Asn Ile Ala His Tyr Phe Glu Val Leu Asp Ala Arg Tyr Asp Phe 
        195                 200                 205 

Thr Ala Asp Asp Val Phe Thr Gln Thr Phe Asp Leu Asn Phe Asp Cys 
    210                 215                 220 

Ser Leu Phe Asp Leu Phe Cys Ala Trp Gly Ala Gly Ala Ser Val Ile 
225                 230                 235                 240 

Gln Ile Pro Pro Gln Ala Tyr Arg Asp Leu Pro Ser His Leu Ala Glu 
                245                 250                 255 

Gln Gly Val Thr Val Trp Phe Ser Thr Pro Ser Ser Ile Ala Leu Val 
            260                 265                 270 

Arg Arg Leu Gly Gly Leu Ala Pro Gly Ser Leu Pro Thr Leu Arg Trp 
        275                 280                 285 

Ser Phe Phe Ala Gly Glu Ala Leu Lys Cys Ala Asp Thr Glu Asp Trp 
    290                 295                 300 

Gln Arg Ala Ala Pro Ala Ser Phe Val Glu Asn Leu Tyr Gly Pro Thr 
305                 310                 315                 320 

Glu Leu Thr Val Thr Val Thr Ala His Arg Trp Ser Pro Glu Val Ser 
                325                 330                 335 

Pro Val Val Gly Ala Asn Gly Val Val Pro Ile Gly Pro Leu His Lys 
            340                 345                 350 

Gly Leu Asp His Val Leu Ile Asp Ala Gly Gly Leu Pro His Pro Asp 
        355                 360                 365 

Thr Gly Glu Leu Cys Val Thr Gly Pro Gln Met Ala Gly Arg Tyr Leu 
    370                 375                 380 

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

Trp Tyr Arg Thr Gly Asp Arg Val Arg Leu Ala Pro Gly Gly Glu Leu 
                405                 410                 415 

Val Tyr Leu Gly Arg Met Asp Ala Gln Val Gln Ile Gln Gly Trp Arg 
            420                 425                 430 

Val Glu Leu Ala Glu Val Asp His Ala Leu Gln Gly Cys Glu Gly Val 
        435                 440                 445 

Gly Glu Ala Val Thr Val Gly Ala Ala Thr Asp Ala Gly Thr Glu Leu 
    450                 455                 460 

Val Val Phe Tyr Thr Ala Pro Ala Pro Val Pro Pro Val Arg Phe Ala 
465                 470                 475                 480 

Ala Val Leu Arg Ala Thr Leu Pro Asp Gly Val Val Pro Arg His Tyr 
                485                 490                 495 

Arg His Val Ala Glu Leu Pro Leu Asn Ser Asn Arg Lys Ile Asp Arg 
            500                 505                 510 

Arg Ala Leu Thr Ala Arg Ala Glu Glu Leu Leu Gly 
        515                 520 

 
           
             18  
             478  
             PRT  
             Streptomyces halstedii sp.HC-34  
           
            18 

Met Glu Asp Ala Phe Gly Thr Trp Thr Tyr Gln Glu Leu Leu Asn His 
1               5                   10                  15 

Ser Gln Ala Phe Ser Ala Trp Leu Asp Gly Lys Gly Val Ala Arg Gly 
            20                  25                  30 

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

Phe Tyr Gly Ala Cys Arg Arg Gly Val Val Phe Val Pro Leu Asn Pro 
    50                  55                  60 

Gly Met Lys Pro Phe His Leu Arg Ser Val Ile Ala Asp Ala Asp Pro 
65                  70                  75                  80 

Arg Leu Val Ile Ala Glu Asp Glu Thr Ala Ala Asp Arg Leu Arg Asp 
                85                  90                  95 

Val Thr Asp Leu Pro Val Tyr Ser Ile Asp Ser Leu Trp Ala Asp Val 
            100                 105                 110 

Glu Arg Leu Arg Asp Ala Gly Ala Gly Ala Glu Ala Val Glu Val Ser 
        115                 120                 125 

Pro Glu Asp Leu Ala Val Leu Ile Tyr Thr Ser Gly Ser Thr Ala Ala 
    130                 135                 140 

Pro Lys Ala Val Ala Cys Pro His Gln Gln Ile Val Phe Ala Ala Ser 
145                 150                 155                 160 

Ser Ile Asn Ala Val Leu Gly Tyr His Ala Glu Asp Ile Val Phe Cys 
                165                 170                 175 

Arg Met Ser Val Ser Trp Asp Phe Gly Leu Tyr Lys Val Leu Ile Ser 
            180                 185                 190 

Thr Leu Thr Gly Ala Lys Leu Val Leu Ala Gly Gly Glu Pro Asp Ile 
        195                 200                 205 

Ala Leu Val Lys Ser Leu Arg Glu Ser Gly Ala Thr Met Met Pro Ile 
    210                 215                 220 

Val Pro Ser Leu Ala Ser Met Leu Thr Thr Leu Ile Arg Arg Asp Pro 
225                 230                 235                 240 

Glu Gly Ala Pro Thr Leu Arg Met Phe Thr Asn Ser Ala Ala Ala Leu 
                245                 250                 255 

Pro Gln Val Thr Ile Asp Ala Leu Arg Ser Ala Phe Pro Gly Ala Gln 
            260                 265                 270 

Val Val Arg Met Tyr Gly Gln Thr Glu Cys Lys Arg Ile Ser Ile Met 
        275                 280                 285 

Pro Pro His Leu Glu His Glu Arg Pro Asp Ser Val Gly Leu Pro Leu 
    290                 295                 300 

Pro Gly Thr Thr Ile Glu Ile Leu Asp Glu Asp Gly Thr Leu Leu Pro 
305                 310                 315                 320 

Pro Gly Glu Pro Gly Glu Ile Thr Val Thr Gly Pro His Val Met Ala 
                325                 330                 335 

Gly Tyr Trp Arg Ala Pro Glu Ile Thr Ala Arg Ala Tyr Arg Arg Asp 
            340                 345                 350 

Glu Thr Thr Gly Ala Met Arg Leu His Thr Gly Asp Tyr Gly His Leu 
        355                 360                 365 

Asp Glu Asp Gly Phe Leu Tyr Phe Gly Gly Arg Arg Asp Asp Met Phe 
    370                 375                 380 

Lys Arg Lys Gly Thr Arg Met Ser Thr Val Glu Ile Glu Ala Ala Ala 
385                 390                 395                 400 

Leu Asp Ile Pro Gly Val Thr Ala Ala Val Ala Leu Pro Pro Thr Ala 
                405                 410                 415 

Thr Arg Asp Leu Ala Leu Cys Val Ala Ser Asp Leu Glu Pro His Asp 
            420                 425                 430 

Val Leu Arg Ser Leu Ala Glu Arg Leu Glu Pro Ala Lys Val Pro Ala 
        435                 440                 445 

Thr Cys Arg Ile Val Asn Asp Phe Pro Leu Thr Leu Asn Gly Lys Ser 
    450                 455                 460 

Glu Arg Lys Gln Leu Ala Arg Leu Leu Asp Gly Ser Asp Lys 
465                 470                 475 

 
           
             19  
             414  
             PRT  
             Streptomyces halstedii sp.HC-34  
           
            19 

Val Asn Gln Tyr Glu Glu Leu Ala Asp Gln Tyr Gly Thr Pro Leu Tyr 
1               5                   10                  15 

Val Tyr Asp Leu Asp Arg Val Ala Glu Ala Arg His Asp Leu Arg Thr 
            20                  25                  30 

Ser Leu Pro Asp Glu Val Glu Ile Tyr Tyr Ala Leu Lys Ala Asn Pro 
        35                  40                  45 

His Pro Gln Val Ala Gly Ala Leu Arg Ser Gly Glu Gly Arg Glu Cys 
    50                  55                  60 

Arg Ala Glu Ile Ser Ser Val Gly Glu Leu Ala Ala Ala Leu Thr Ala 
65                  70                  75                  80 

Gly Phe Arg Ala Ser Glu Ile Leu Tyr Thr Gly Pro Gly Lys Thr Asp 
                85                  90                  95 

Gly Glu Leu Asp Glu Ala Ile Gly Lys Gly Val Lys Thr Phe Cys Val 
            100                 105                 110 

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

Gly Val Val Ala Asp Cys Leu Leu Arg Ile Asn Ser Ala Thr Ala Ser 
    130                 135                 140 

Ala Thr Thr Ser Ile Arg Met Thr Gly Thr Pro Ser Gln Phe Gly Ile 
145                 150                 155                 160 

Asp Ser Glu Thr Leu Val Asp Ala Met Pro Glu Leu Arg Ala Val Pro 
                165                 170                 175 

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

Asp Glu Ala Ser Leu Ile Gly Glu Phe Arg His Thr Ile Ala Tyr Ala 
        195                 200                 205 

Ala Gly Leu Ala Glu Glu Thr Gly Leu Thr Leu Glu Phe Leu Asp Ile 
    210                 215                 220 

Gly Gly Gly Phe Ala His Pro Tyr Gly Ala Pro Gly Glu Arg Pro Val 
225                 230                 235                 240 

Tyr Arg Glu Leu Arg Thr Glu Leu Ala Ala Ala Leu Asp Glu His Phe 
                245                 250                 255 

Pro His Trp Arg Glu Gly Ala Pro Arg Ile Ala Val Glu Thr Gly Arg 
            260                 265                 270 

Tyr Gln Thr Ser Gly Ala Gly Thr Leu Leu Thr Arg Val Val Asn Ile 
        275                 280                 285 

Lys Val Ser Arg Gly Arg Lys Phe Val Val Ile Asp Ala Gly Ile Asn 
    290                 295                 300 

Thr Phe Gly Gly Met Ser Gly Leu Gly Arg Leu Leu Pro Val Ala Val 
305                 310                 315                 320 

Glu Pro Glu Tyr Thr Gly Ser Ala Glu Ala Thr Glu Leu Thr Asp Val 
                325                 330                 335 

Ala Ser Leu Ala Gly Pro Leu Cys Thr Pro Gly Asp Ile Leu Gly Arg 
            340                 345                 350 

Glu Ile Arg Leu Pro Glu Leu Ala Pro Gly Asp Leu Val Thr Ile Pro 
        355                 360                 365 

Asn Ala Gly Ala Tyr Gly Val Thr Ala Ser Leu Leu Met Phe Leu Gly 
    370                 375                 380 

Arg Pro Ala Pro Val Glu Val Val Leu Lys Gly Gly Lys Val Val Ser 
385                 390                 395                 400 

Ala Ser Arg Leu Glu His His Arg Thr Pro Ala Thr Pro Gly 
                405                 410 

 
           
             20  
             5836  
             PRT  
             Streptomyces halstedii sp.HC-34  
           
            20 

Met Ser Pro Ala Leu Ala Arg Ser Lys Arg Met Ser Glu Ser Glu Asn 
1               5                   10                  15 

Pro Val Ser Ala Thr Thr Ala Gly Ala Asp Glu Thr Pro Asp Thr Arg 
            20                  25                  30 

Thr Ala Leu Ala Arg Arg Leu Ala Gly Leu Ser Pro Ala Glu Gln Glu 
        35                  40                  45 

Gln His Leu Val Asp Met Val His Arg His Thr Val Ala Ala Leu Gln 
    50                  55                  60 

Ala Val Ala Pro Leu Thr Pro Asp Gln Val Asp Val Gln Arg Pro Phe 
65                  70                  75                  80 

Leu Glu Leu Gly Phe Asp Ser Leu Ala Ala Val Asp Leu His Lys Arg 
                85                  90                  95 

Leu Thr Gly Glu Thr Gly Leu Glu Leu Pro Val Thr Val Ala Phe Asp 
            100                 105                 110 

Phe Pro Thr Pro Val Leu Val Ala Glu Glu Ile Arg Arg Ile Ala Phe 
        115                 120                 125 

Gly Ile Arg Pro Ala Pro Leu Ala Pro Val Val Ala Thr Gly Asn Leu 
    130                 135                 140 

Asp Asp Asp Pro Ile Ala Ile Ile Gly Ile Gly Cys Arg Phe Pro Gly 
145                 150                 155                 160 

Gly Ile Asn Ser Ala Glu Glu Leu Trp Gln Leu Val Met Asp Glu Ala 
                165                 170                 175 

Glu Val Leu Ser Gly Phe Pro Thr Asn Arg Gly Trp Asp Val Glu Gly 
            180                 185                 190 

Ile Tyr Asp Pro Asp Pro Gly Lys Pro Gly Lys Ser Tyr Val Arg Glu 
        195                 200                 205 

Gly Gly Phe Leu Gln Asp Ala Gly Asp Phe Asp Ala Asp Phe Phe Gly 
    210                 215                 220 

Ile Ser Pro Arg Glu Ala Leu Ala Met Asp Pro Gln Gln Arg Leu Val 
225                 230                 235                 240 

Leu Glu Thr Ala Trp Glu Ala Phe Glu Arg Ala Gly Ile Asp Pro Gly 
                245                 250                 255 

Ser Leu His Gly Ser Lys Ala Gly Val Phe Ile Gly Ala Glu Val His 
            260                 265                 270 

Glu Tyr Gly Thr Arg Val His Glu Ala Pro Glu Gly Leu Asp Gly Tyr 
        275                 280                 285 

Leu Met Thr Gly Asn Ala Pro Ser Val Ala Ser Gly Arg Ile Ala Tyr 
    290                 295                 300 

Ser Leu Gly Leu Glu Gly Pro Ala Val Thr Ile Asp Thr Ala Cys Ser 
305                 310                 315                 320 

Gly Ser Leu Val Ala Leu His Leu Ala Ala His Ser Leu Arg Gln Gly 
                325                 330                 335 

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

Gly Met Phe Ala Ala Phe Ser Arg Gln Arg Gly Leu Ala Ala Asp Gly 
        355                 360                 365 

Arg Cys Lys Pro Phe Ala Ala Ala Ala Asp Gly Thr Gly Phe Ser Glu 
    370                 375                 380 

Gly Val Gly Val Phe Val Val Glu Arg Leu Ala Asp Ala Arg Arg Asn 
385                 390                 395                 400 

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

Gly Ala Ser Asn Gly Leu Thr Ala Pro Asn Gly Pro Ser Gln Gln Arg 
            420                 425                 430 

Leu Ile Leu Gln Ala Leu Ala Asn Ala Gly Leu Lys Pro Ala Asp Val 
        435                 440                 445 

Asp Thr Met Glu Ala His Gly Thr Gly Thr Lys Leu Gly Asp Pro Ile 
    450                 455                 460 

Glu Ala Gln Ala Ile Leu Ala Thr Tyr Gly Gln Glu Arg Glu Glu Gly 
465                 470                 475                 480 

Arg Pro Leu Trp Leu Gly Ser Ile Lys Ser Asn Leu Gly His Thr Gln 
                485                 490                 495 

Ala Ala Gly Gly Ala Ala Ser Leu Ile Lys Met Leu Met Gly Met Arg 
            500                 505                 510 

His Gly Lys Leu Pro Arg Ser Leu His Ile Asp Ala Pro Thr Pro His 
        515                 520                 525 

Val Asp Trp Thr Thr Gly Asp Val Ala Leu Leu Thr Glu Thr Arg Asp 
    530                 535                 540 

Trp Asp Ala Pro Asp Arg Pro Arg Arg Ala Gly Val Ser Ala Phe Gly 
545                 550                 555                 560 

Ile Ser Gly Thr Asn Ala His Val Ile Ile Glu Glu Ala Pro Glu Phe 
                565                 570                 575 

Glu Pro Ser Ala Val Glu Pro Val Ala Gly Ser Gly Val Thr Pro Pro 
            580                 585                 590 

Trp Val Leu Ser Ala Arg Ser Ala Asp Ala Leu Arg Gly Gln Ala Glu 
        595                 600                 605 

Arg Leu Leu Ser Phe Val Ser Thr Asp Ala Asp Val Ser Val Val Asp 
    610                 615                 620 

Val Ala Tyr Ser Leu Gly Val Ser Arg Ala Gly Leu Glu His Arg Gly 
625                 630                 635                 640 

Val Val Leu Gly Glu Ser Arg Glu Glu Leu Ile Ala Ala Leu Glu Ser 
                645                 650                 655 

Leu Ala Ser Gly Ala Glu Ala Pro Gly Val Val Thr Gly Arg Val Ala 
            660                 665                 670 

Glu Gly Arg Leu Ala Phe Leu Phe Thr Gly Gln Gly Ala Gln Arg Val 
        675                 680                 685 

Gly Met Gly Arg Glu Leu Ala Ala Glu Phe Pro Val Phe Ala Ala Ser 
    690                 695                 700 

Leu Glu Glu Thr Cys Asp Leu Leu Asp Val Gly Leu Glu Asp Gln Asp 
705                 710                 715                 720 

His Ser Leu Arg Glu Val Leu Phe Ala Glu Glu Gly Ser Ala Glu Ala 
                725                 730                 735 

Ala Leu Leu Thr Arg Thr Val Tyr Ala Gln Ala Ala Leu Phe Ala Val 
            740                 745                 750 

Glu Val Ala Leu Phe Arg Leu Val Glu Ser Phe Gly Val Val Pro Asp 
        755                 760                 765 

Phe Val Ala Gly His Ser Val Gly Glu Ile Ala Ala Ala His Val Ala 
    770                 775                 780 

Gly Val Phe Ser Leu Glu Asp Ala Thr Met Leu Val Ala Ala Arg Gly 
785                 790                 795                 800 

Arg Leu Met Asp Ala Leu Pro Glu Gly Gly Thr Met Val Ala Val Gln 
                805                 810                 815 

Ala Thr Glu Glu Asp Val Leu Ala Leu Leu Glu Gly Val Glu Asp Ala 
            820                 825                 830 

Ser Ile Ala Ala Ile Asn Gly Pro Asp Ala Val Val Val Ser Gly Thr 
        835                 840                 845 

Glu Thr Gly Val Ala Arg Val Val Asp Val Leu Arg Asp Arg Gly Ala 
    850                 855                 860 

Lys Thr Lys Arg Leu Asp Val Ser His Ala Phe His Ser Pro Leu Met 
865                 870                 875                 880 

Glu Pro Met Leu Thr Glu Phe Arg Arg Val Ala Glu Val Leu Glu Tyr 
                885                 890                 895 

Gln Ala Pro Arg Ile Ala Val Val Ser Asn Val Ser Gly Ser Val Ala 
            900                 905                 910 

Gly Thr Glu Leu Ala Thr Pro Glu Tyr Trp Val Thr His Val Arg Glu 
        915                 920                 925 

Ala Val Arg Phe Ser Ala Gly Val Arg Thr Leu Leu Gly Ala Gly Val 
    930                 935                 940 

Ser Ser Phe Leu Glu Ile Gly Pro Asp Gly Val Leu Ser Gly Met Ala 
945                 950                 955                 960 

Arg Gly Ser Val Ser Asp Gly Ala Asp Val Gly Cys Val Pro Val Met 
                965                 970                 975 

Arg Arg Gly Arg Gly Glu Val Arg Glu Phe Leu Thr Gly Leu Ser Arg 
            980                 985                 990 

Ile Ala Val Arg Gly Val Pro Val  Thr Trp Glu Pro Leu  Ile Glu Gly 
        995                 1000                 1005 

Ala Arg  Arg Val Glu Leu Pro  Thr Tyr Ala Phe Gln  Arg Arg Trp 
    1010                 1015                 1020 

Phe Trp  Leu Glu Ala Gly Arg  Ser Thr Thr Asp Ala  Leu Gly Leu 
    1025                 1030                 1035 

Gly Gln  Thr Ala Ala Glu His  Pro Leu Val Gly Ala  Val Val Gly 
    1040                 1045                 1050 

Leu Ala  Gly Gly Asp Gly Val  Val Leu Thr Gly Arg  Val Ser Leu 
    1055                 1060                 1065 

His Thr  His Pro Trp Leu Ala  Asp His Gln Val Ala  Gly Val Thr 
    1070                 1075                 1080 

Leu Leu  Pro Gly Thr Gly Phe  Val Glu Leu Ala Val  Arg Ala Gly 
    1085                 1090                 1095 

Asp Glu  Val Gly Cys Gly Arg  Leu Glu Glu Leu Thr  Leu Glu Ala 
    1100                 1105                 1110 

Pro Leu  Val Val Pro Asp Arg  Gly Ala Val Gln Leu  Gln Val Val 
    1115                 1120                 1125 

Val Gly  Ala Leu Glu Glu Ser  Asp Val Arg Thr Val  Ser Val Tyr 
    1130                 1135                 1140 

Ser Arg  Ala Glu Glu Asp Asp  Val Trp Thr Arg His  Ala Thr Gly 
    1145                 1150                 1155 

Phe Val  Gly Ala Ala Val Asp  Gly Gly Leu Asn Leu  Glu Ala Trp 
    1160                 1165                 1170 

Pro Pro  Pro Gly Ala Arg Ala  Val Asp Val Ser Asp  Val Tyr Ala 
    1175                 1180                 1185 

Gly Leu  Ala Asp Gln Gly Tyr  Gly Tyr Gly Pro Val  Phe Gln Gly 
    1190                 1195                 1200 

Leu Arg  Ser Val Trp Arg Gly  Asp Gly Glu Val Phe  Ala Glu Val 
    1205                 1210                 1215 

Val Leu  Pro Glu Gly Ala Gln  Ala Asp Ala Ser Ala  Phe Gly Leu 
    1220                 1225                 1230 

His Pro  Ala Leu Leu Asp Ala  Ala Leu His Ala Thr  Asp Tyr Leu 
    1235                 1240                 1245 

Asp Pro  Glu Ser Ala Val Glu  Gly Thr His Leu Pro  Phe Ala Trp 
    1250                 1255                 1260 

Thr Gly  Val Ser Leu His Ala  Thr Gly Ala Ser Glu  Leu Arg Val 
    1265                 1270                 1275 

Arg Ile  Thr Ala Thr Gly Asn  Asp Gly Tyr Ala Leu  Asp Leu Ala 
    1280                 1285                 1290 

Asp Thr  Thr Gly Arg Pro Val  Ala Thr Val Gln Ser  Leu Val Leu 
    1295                 1300                 1305 

Arg Pro  Val Thr Glu Glu Gln  Leu Arg Ser Ala Gln  Gly Gly Asn 
    1310                 1315                 1320 

Gly Pro  Asp Ser Leu Phe Arg  Val Glu Trp Ala Pro  Val Thr Ala 
    1325                 1330                 1335 

Asp Leu  Thr Ala Ser Gly Ala  Gly Trp Ala Val Leu  Gly Ala Gly 
    1340                 1345                 1350 

Ala Pro  Glu Leu Ala Ala Ala  Leu Thr Ala Ala Gly  Thr Pro Gly 
    1355                 1360                 1365 

Thr Ala  Tyr His Gly Thr Ala  Glu Leu Ser Ala Ala  Val Asp Gly 
    1370                 1375                 1380 

Gly Thr  Thr Pro Asp Val Val  Ala Val Gln Leu Pro  Ser Ala Gly 
    1385                 1390                 1395 

Ala Ala  Asp Ala Asp Leu Pro  Asp Ala Val Arg Ala  Thr Leu Asn 
    1400                 1405                 1410 

Thr Ala  Leu Glu Phe Val Gln  Asn Trp Leu Ala Asp  Glu Arg Leu 
    1415                 1420                 1425 

Ala Glu  Thr Arg Leu Val Val  Val Thr Arg Asp Ala  Val Thr Val 
    1430                 1435                 1440 

Asp Thr  Ala Ala Gly Gly Pro  Asp Leu Thr Val Ala  Pro Val Trp 
    1445                 1450                 1455 

Gly Leu  Ile Arg Ser Ala Gln  Ala Glu Asn Pro Gly  Arg Ile Leu 
    1460                 1465                 1470 

Leu Ala  Asp Ile Asp Gly Thr  Asp Gln Ser Arg Thr  Ala Leu Ala 
    1475                 1480                 1485 

Ala Ile  Thr Ala Ala Asp Glu  Pro Glu Leu Ala Phe  Arg Asn Gly 
    1490                 1495                 1500 

Asn Ala  Tyr Ala Pro Arg Leu  Val Arg Ser Val Ser  Glu Gly Gly 
    1505                 1510                 1515 

Leu Val  Pro Pro Ser Asp Ala  Ala Ser Trp Arg Leu  Asp Val Leu 
    1520                 1525                 1530 

Ser Gln  Gly Thr Leu Glu Asn  Leu Ala Leu Ile Pro  Ser Asp Ala 
    1535                 1540                 1545 

Asp Glu  Arg Thr Leu Ala Pro  Gly Glu Val Arg Ile  Ala Val Arg 
    1550                 1555                 1560 

Ala Ala  Gly Val Asn Phe Arg  Asp Val Leu Val Ala  Leu Gly Met 
    1565                 1570                 1575 

Tyr Pro  Thr Lys Ala Asp Ile  Gly Gly Glu Ala Ala  Gly Leu Val 
    1580                 1585                 1590 

Leu Glu  Val Gly Pro Gly Val  Thr Asp Phe Thr Pro  Gly Asp Arg 
    1595                 1600                 1605 

Val Met  Gly Leu Phe Asp Thr  Ala Phe Gly Pro His  Ala Ile Thr 
    1610                 1615                 1620 

Asp His  Arg Thr Leu Val Pro  Met Pro Thr Gly Trp  Thr Tyr Ala 
    1625                 1630                 1635 

Gln Ala  Ala Thr Ala Pro Leu  Val Phe Ala Thr Ala  Tyr Tyr Gly 
    1640                 1645                 1650 

Leu Val  Asp Leu Ala Glu Leu  Arg Ser Gly Glu Ser  Ala Leu Ile 
    1655                 1660                 1665 

His Ala  Ala Ala Gly Gly Val  Gly Met Ala Ala Val  Gln Ile Ala 
    1670                 1675                 1680 

Arg His  Leu Gly Ala Glu Val  Tyr Gly Thr Ala Ser  Pro Gly Lys 
    1685                 1690                 1695 

Trp Asn  Ala Leu Arg Ala Ala  Gly Leu Asp Asp Asn  His Ile Ala 
    1700                 1705                 1710 

Ser Ser  Arg Asp Thr Thr Phe  Glu Gln Lys Phe Leu  Ala Asn Ser 
    1715                 1720                 1725 

Gly Gly  Arg Gly Val Asp Val  Val Leu Asp Ala Leu  Thr Gly Glu 
    1730                 1735                 1740 

Phe Ile  Asp Ala Ser Leu Arg  Leu Leu Pro Arg Gly  Gly Arg Phe 
    1745                 1750                 1755 

Ala Glu  Met Gly Lys Thr Asp  Val Arg Asp Pro Glu  Arg Val Ala 
    1760                 1765                 1770 

Ala Glu  Tyr Pro Gly Val Arg  Tyr Arg Ala Phe Asp  Leu Phe Glu 
    1775                 1780                 1785 

Ala Asp  Leu Asp Arg Leu Arg  Glu Ile Leu Arg Glu  Leu Leu Ala 
    1790                 1795                 1800 

Leu Phe  Glu Ser Gly Ala Leu  Arg Pro Leu Pro Val  Arg Ala Trp 
    1805                 1810                 1815 

Asp Ile  Arg Lys Ser Lys Asp  Ala Phe Arg His Ile  Ala Gln Ala 
    1820                 1825                 1830 

Arg His  Ile Gly Lys Val Ala  Leu Thr Met Pro Thr  Gly Gly Leu 
    1835                 1840                 1845 

Gly Asp  Gly Val Val Leu Val  Thr Gly Gly Thr Gly  Gly Leu Gly 
    1850                 1855                 1860 

Ala Leu  Val Ala Arg His Val  Val Val Val His Gly  Val Arg Arg 
    1865                 1870                 1875 

Leu Val  Leu Val Ser Arg Arg  Gly Leu Gly Ala Pro  Gly Ala Val 
    1880                 1885                 1890 

Gly Leu  Val Ala Glu Leu Glu  Gly Leu Gly Ala Val  Val Glu Val 
    1895                 1900                 1905 

Val Ala  Cys Asp Val Ser Asp  Arg Val Ala Leu Ala  Gly Val Val 
    1910                 1915                 1920 

Gly Gly  Ile Gly Ser Asp Leu  Ser Ala Val Val His  Thr Ala Gly 
    1925                 1930                 1935 

Val Val  Asp Asp Gly Val Val  Gly Ser Leu Ser Val  Gly Arg Leu 
    1940                 1945                 1950 

Ser Ser  Val Leu Gly Pro Lys  Ala Asp Ala Ala Trp  Tyr Leu His 
    1955                 1960                 1965 

Glu Leu  Thr Val Gly Leu Asp  Leu Ser Ala Phe Val  Leu Phe Ser 
    1970                 1975                 1980 

Ser Val  Ala Gly Val Val Asp  Gly Ala Gly Gln Gly  Asn Tyr Ala 
    1985                 1990                 1995 

Ala Ala  Asn Val Phe Leu Asp  Gly Leu Ala Val Val  Arg Arg Gly 
    2000                 2005                 2010 

Leu Gly  Leu Pro Gly Thr Ser  Val Ala Trp Gly Leu  Trp Glu Gly 
    2015                 2020                 2025 

Ala Gly  Met Gly Ala Val Leu  Gly Glu Ala Asp Val  Leu Arg Met 
    2030                 2035                 2040 

Ser Arg  Ser Gly Val Leu Gly  Leu Ser Val Gly Glu  Gly Leu Gly 
    2045                 2050                 2055 

Leu Phe  Asp Val Ala Leu Gly  Glu Asp Val Ala Ala  Leu Val Pro 
    2060                 2065                 2070 

Val Arg  Leu Asp Leu Gly Ala  Leu Arg Ser Arg Val  Asp Gly Val 
    2075                 2080                 2085 

Pro Ala  Val Phe Arg Ser Leu  Val Arg Val Pro Val  Arg Arg Ser 
    2090                 2095                 2100 

Val Gly  Val Gly Val Ser Gly  Gly Gly Glu Val Ser  Leu Glu Arg 
    2105                 2110                 2115 

Arg Leu  Val Val Leu Asp Ala  Gly Glu Arg Glu Arg  Val Leu Leu 
    2120                 2125                 2130 

Glu Leu  Val Arg Ser His Val  Ala Ala Val Leu Gly  Tyr Glu Gly 
    2135                 2140                 2145 

Ala Gly  Ser Ile Glu Pro Gly  Arg Ala Phe Ser Asp  Ile Gly Phe 
    2150                 2155                 2160 

Asp Ser  Leu Ser Ala Val Glu  Leu Arg Asn Arg Leu  Asn Gly Glu 
    2165                 2170                 2175 

Thr Gly  Leu Arg Leu Pro Ala  Thr Leu Ile Phe Asp  Tyr Pro Thr 
    2180                 2185                 2190 

Pro Gln  Ala Leu Ala Glu Tyr  Val Ile Val Ala Leu  Leu Gly Glu 
    2195                 2200                 2205 

Glu Ala  Ala Asn Ala Pro Ala  Leu Pro Pro Thr Glu  Ala Pro Thr 
    2210                 2215                 2220 

Val Thr  Gly Thr Asp Asp Asp  Pro Val Val Ile Val  Gly Met Gly 
    2225                 2230                 2235 

Cys Arg  Phe Pro Gly Asp Val  Arg Thr Pro Glu Asp  Leu Trp Arg 
    2240                 2245                 2250 

Leu Val  Ser Asn Gly Ser Asp  Ala Val Thr Pro Phe  Pro Asp Asn 
    2255                 2260                 2265 

Arg Ala  Trp Asp Ile Glu Gly  Ile Tyr Asp Pro Leu  Pro Gly Val 
    2270                 2275                 2280 

Ser Gly  Lys Thr Tyr Ala Arg  Glu Gly Gly Phe Leu  His Asp Ala 
    2285                 2290                 2295 

Ala Glu  Phe Asp Pro Glu Phe  Phe Gly Ile Ser Pro  Arg Glu Ala 
    2300                 2305                 2310 

Leu Ala  Met Asp Pro Gln Gln  Arg Leu Leu Leu Glu  Thr Ser Trp 
    2315                 2320                 2325 

Glu Ala  Ile Glu Arg Ala Gly  Ile Asp Pro Asn Ser  Leu Arg Gly 
    2330                 2335                 2340 

Thr Gln  Thr Gly Val Phe Ala  Gly Val Met Gln Thr  Asp Tyr Gly 
    2345                 2350                 2355 

Asn Gly  Gly Ala Arg Leu Ala  Glu Asp Val Glu Gly  Tyr Ile Ala 
    2360                 2365                 2370 

Asn Gly  Thr Leu Gly Ser Ile  Val Ser Gly Arg Val  Ser Tyr Ala 
    2375                 2380                 2385 

Leu Gly  Leu Glu Gly Pro Ala  Val Thr Ile Asp Thr  Ala Cys Ser 
    2390                 2395                 2400 

Ser Ser  Leu Val Ala Met His  Trp Ala Ala His Ala  Leu Arg Gln 
    2405                 2410                 2415 

Gly Glu  Cys Ser Leu Ala Leu  Ala Gly Gly Val Thr  Val Met Ser 
    2420                 2425                 2430 

Thr Pro  Glu Thr Phe Val Asp  Phe Ser Leu Gln Arg  Gly Leu Ala 
    2435                 2440                 2445 

Pro Asn  Gly Arg Cys Lys Ala  Phe Ser Ala Asp Ala  Asp Gly Thr 
    2450                 2455                 2460 

Gly Trp  Gly Glu Gly Val Gly  Val Leu Val Leu Glu  Arg Leu Ser 
    2465                 2470                 2475 

Asp Ala  Arg Arg Asn Gly His  Gln Val Leu Ala Val  Ile Arg Gly 
    2480                 2485                 2490 

Ser Ala  Leu Asn Gln Asp Gly  Ala Ser Asn Gly Leu  Thr Ala Pro 
    2495                 2500                 2505 

Asn Gly  Pro Ser Gln Gln Arg  Val Ile Arg Gln Ala  Leu Val Ser 
    2510                 2515                 2520 

Ala Gly  Leu Thr Thr Ser Asp  Val Asp Ala Val Glu  Ala His Gly 
    2525                 2530                 2535 

Thr Gly  Thr Thr Leu Gly Asp  Pro Ile Glu Ala Gln  Ala Leu Leu 
    2540                 2545                 2550 

Ala Thr  Tyr Gly Gln Glu Arg  Asp Ala Asp Gln Pro  Leu Trp Leu 
    2555                 2560                 2565 

Gly Ser  Val Lys Thr Asn Val  Gly His Thr Gln Ala  Ala Ala Gly 
    2570                 2575                 2580 

Val Ala  Gly Val Ile Lys Met  Val Leu Ala Met Arg  Ala Gly Val 
    2585                 2590                 2595 

Leu Pro  Lys Thr Leu His Val  Thr Glu Pro Ser Pro  His Val Asp 
    2600                 2605                 2610 

Trp Ser  Ala Gly Ala Val Glu  Leu Leu Thr Glu Thr  Arg Asp Trp 
    2615                 2620                 2625 

Pro Glu  Thr Gly Arg Pro Arg  Arg Ala Gly Val Ser  Ser Phe Gly 
    2630                 2635                 2640 

Val Ser  Gly Thr Asn Ala His  Val Ile Val Glu Gln  Ala Pro Ala 
    2645                 2650                 2655 

Val Glu  Glu Glu Pro Thr Arg  Ala Leu Pro Ala Leu  Pro Val Pro 
    2660                 2665                 2670 

Trp Ser  Ile Ser Ala Lys Ser  Ala Asp Ala Leu Arg  Gly Gln Ala 
    2675                 2680                 2685 

Gln Ala  Leu Ser Ser Phe Val  Ser Ala Ala Gly Asp  Val Ser Val 
    2690                 2695                 2700 

Val Asp  Val Ala Tyr Ser Leu  Gly Val Ser Arg Ala  Gly Leu Glu 
    2705                 2710                 2715 

His Arg  Gly Val Val Val Gly  Glu Ser Arg Ala Glu  Leu Leu Val 
    2720                 2725                 2730 

Ala Leu  Glu Ser Leu Ala Ser  Gly Val Glu Ser Pro  Gly Val Val 
    2735                 2740                 2745 

Thr Gly  Arg Val Ala Glu Gly  Arg Leu Ala Phe Leu  Phe Thr Gly 
    2750                 2755                 2760 

Gln Gly  Ala Gln Arg Val Gly  Met Gly Arg Glu Leu  Ala Ala Glu 
    2765                 2770                 2775 

Phe Pro  Val Phe Ala Ala Ser  Leu Glu Gln Thr Cys  Asp Leu Leu 
    2780                 2785                 2790 

Glu Arg  Ala Gly Val Ala Val  Arg Glu Val Leu Phe  Ala Glu Glu 
    2795                 2800                 2805 

Gly Ser  Ala Glu Ala Ala Leu  Leu Thr Arg Thr Val  Tyr Ala Gln 
    2810                 2815                 2820 

Ala Ala  Leu Phe Ala Val Glu  Val Ala Leu Phe Arg  Leu Val Glu 
    2825                 2830                 2835 

Ser Phe  Gly Val Val Pro Asp  Phe Val Ala Gly His  Ser Val Gly 
    2840                 2845                 2850 

Glu Ile  Ala Ala Ala His Val  Ala Gly Val Phe Ser  Leu Glu Asp 
    2855                 2860                 2865 

Ala Val  Ser Leu Val Ala Ala  Arg Gly Arg Leu Met  Asp Ala Leu 
    2870                 2875                 2880 

Pro Glu  Gly Gly Ala Met Val  Ala Val Gln Ala Thr  Glu Glu Asp 
    2885                 2890                 2895 

Val Leu  Ala Leu Leu Glu Gly  Val Glu Asp Ala Ser  Ile Ala Ala 
    2900                 2905                 2910 

Ile Asn  Gly Pro Asp Ala Val  Val Val Ser Gly Thr  Glu Thr Gly 
    2915                 2920                 2925 

Val Ala  Arg Val Val Asp Val  Leu Arg Glu Arg Gly  Ala Lys Thr 
    2930                 2935                 2940 

Lys Arg  Leu Val Val Ser His  Ala Phe His Ser Pro  Leu Met Glu 
    2945                 2950                 2955 

Pro Met  Leu Ala Asp Phe Ala  Thr Val Val Glu Gly  Leu Ser Tyr 
    2960                 2965                 2970 

Lys Ala  Pro Ala Ile Pro Val  Val Ser Gly Ser Val  Val Gly Ser 
    2975                 2980                 2985 

Glu Leu  Ser Thr Pro Gly Tyr  Trp Val Arg His Val  Arg Glu Ala 
    2990                 2995                 3000 

Val Arg  Phe Gly Ala Gly Val  Glu Thr Leu Leu Gly  Ala Gly Val 
    3005                 3010                 3015 

Ser Ser  Phe Leu Glu Ile Gly  Pro Asp Gly Val Leu  Ser Gly Met 
    3020                 3025                 3030 

Ala Arg  Thr Ser Val Pro Glu  Gly Ala Asp Val Glu  Cys Ala Pro 
    3035                 3040                 3045 

Leu Met  Arg Arg Asp Arg Ala  Glu Val Arg Glu Phe  Leu Thr Gly 
    3050                 3055                 3060 

Leu Ser  Arg Leu Ala Val Arg  Gly Val Pro Val Ala  Trp Glu Ser 
    3065                 3070                 3075 

Leu Val  Glu Gly Gly Arg Arg  Val Glu Leu Pro Thr  Tyr Ala Phe 
    3080                 3085                 3090 

Gln Arg  Arg Arg Phe Trp Leu  Glu Ala Gly Arg Ser  Val Thr Asp 
    3095                 3100                 3105 

Ala Ser  Gly Leu Gly Gln Thr  Ala Ala Glu His Pro  Leu Val Gly 
    3110                 3115                 3120 

Ala Val  Val Gly Leu Ala Gly  Gly Asp Gly Val Val  Leu Thr Gly 
    3125                 3130                 3135 

Arg Val  Ser Leu His Thr His  Pro Trp Leu Ala Asp  His Gln Val 
    3140                 3145                 3150 

Ala Gly  Val Thr Leu Leu Pro  Gly Thr Gly Phe Val  Glu Leu Ala 
    3155                 3160                 3165 

Val Arg  Ala Gly Asp Glu Val  Gly Cys Gly Arg Leu  Glu Glu Leu 
    3170                 3175                 3180 

Thr Leu  Glu Ala Pro Leu Val  Val Pro Asp Arg Gly  Ala Val Gln 
    3185                 3190                 3195 

Leu Gln  Val Val Val Gly Ala  Leu Glu Thr Ser Gly  Val Arg Thr 
    3200                 3205                 3210 

Val Ser  Val Tyr Ser Arg Val  Glu Glu Glu Ser Ala  Asp Asp Thr 
    3215                 3220                 3225 

Trp Val  Arg His Ala Thr Gly  Ala Leu Met Ala Ala  Ala Glu Glu 
    3230                 3235                 3240 

Pro Gly  Phe Asp Leu Thr Ala  Trp Pro Pro Ala Gly  Ala Arg Ala 
    3245                 3250                 3255 

Val Asp  Val Ser Asp Ala Tyr  Ala Gly Leu Ala Ser  Gln Gly Tyr 
    3260                 3265                 3270 

Gly Tyr  Gly Pro Val Phe Gln  Gly Leu Thr Ala Ala  Trp Arg Lys 
    3275                 3280                 3285 

Gly Arg  Glu Val Phe Ala Glu  Ile Thr Leu Pro Glu  Ala Ala Gln 
    3290                 3295                 3300 

Val Asp  Ala Ser Ala Phe Gly  Leu His Pro Ala Leu  Leu Asp Ala 
    3305                 3310                 3315 

Ala Leu  His Ala Thr Asp Tyr  Leu Asp Gln Glu Ser  Ala Glu Gly 
    3320                 3325                 3330 

Thr His  Leu Pro Phe Ala Trp  Ser Gly Val Ser Leu  His Ala Ala 
    3335                 3340                 3345 

Gly Ala  Ser Ala Leu Arg Val  Arg Ile Val Ala Thr  Gly Lys Asp 
    3350                 3355                 3360 

Gly Tyr  Ala Leu Asp Leu Ala  Asp Ser Thr Gly Arg  Pro Val Ala 
    3365                 3370                 3375 

Thr Val  Gln Ser Leu Val Thr  Arg Pro Val Thr Ala  Asp Gln Leu 
    3380                 3385                 3390 

Ser Glu  Ala Ser Ala Thr Gln  His Gln Ser Leu Phe  Arg Met Glu 
    3395                 3400                 3405 

Trp Thr  Ala Thr Thr Ala Pro  Ala Ala Thr Ala Asp  Val Arg Trp 
    3410                 3415                 3420 

Ala Leu  Leu Gly Glu Pro Val  Ala Glu Leu Gly Asp  Leu Ala Gly 
    3425                 3430                 3435 

Phe Gly  Arg Thr Thr Ala Tyr  Ala Ser Leu Ala Asp  Leu Ala Ala 
    3440                 3445                 3450 

Ala Asp  Ala Asp Thr Val Pro  Asp Leu Val Val Leu  Pro Leu Gly 
    3455                 3460                 3465 

Ser Arg  Met Ala Glu Gly Ser  Asp Val Pro Glu Ala  Val Arg Glu 
    3470                 3475                 3480 

Asn Leu  Gly Gln Val Leu Ala  Thr Ile Gln Gln Trp  Asn Asp Asp 
    3485                 3490                 3495 

Ser Arg  Phe Asp Gly Ser Arg  Leu Val Val Leu Thr  His Gly Ala 
    3500                 3505                 3510 

Val Ser  Val Ser Asp Asp Glu  Ser Leu Thr Ala Leu  Asp Leu Ala 
    3515                 3520                 3525 

Pro Val  Trp Gly Leu Val Arg  Ser Ala Met Ala Glu  Thr Pro Gly 
    3530                 3535                 3540 

Arg Phe  Leu Leu Val Asp Thr  Asp Gly Thr Asp Pro  Ser Thr Asp 
    3545                 3550                 3555 

Ala Leu  Arg His Leu Ala Glu  Leu Gln Glu Ala Glu  Phe Ala Leu 
    3560                 3565                 3570 

Arg Glu  Gly Glu Ile Arg Val  Pro Arg Leu Ala Arg  Val Pro Val 
    3575                 3580                 3585 

Ala Gly  Ala Gly Ala Asp Ile  Thr Gly Gly Leu Gly  Asp Gly Val 
    3590                 3595                 3600 

Val Leu  Val Thr Gly Gly Thr  Gly Gly Leu Gly Ala  Val Val Ala 
    3605                 3610                 3615 

Arg His  Ala Val Val Val His  Gly Val Arg Arg Leu  Val Leu Val 
    3620                 3625                 3630 

Ser Arg  Arg Gly Leu Gly Ala  Pro Gly Ala Val Gly  Leu Val Ala 
    3635                 3640                 3645 

Glu Leu  Glu Ser Leu Gly Ala  Val Val Glu Val Val  Ala Cys Asp 
    3650                 3655                 3660 

Val Ser  Asp Arg Val Ala Leu  Ala Gly Val Val Gly  Gly Ile Gly 
    3665                 3670                 3675 

Ser Asp  Leu Ser Ala Val Val  His Thr Ala Gly Val  Val Asp Asp 
    3680                 3685                 3690 

Gly Val  Val Gly Ser Leu Ser  Val Gly Arg Leu Ser  Ser Val Leu 
    3695                 3700                 3705 

Gly Pro  Lys Ala Asp Ala Ala  Trp Tyr Leu His Glu  Leu Thr Val 
    3710                 3715                 3720 

Arg Leu  Asp Leu Ser Ala Phe  Val Leu Phe Ser Ser  Val Ala Gly 
    3725                 3730                 3735 

Val Val  Asp Gly Ala Gly Gln  Gly Asn Tyr Ala Ala  Ala Asn Val 
    3740                 3745                 3750 

Phe Leu  Asp Gly Leu Ala Val  Val Arg Arg Gly Leu  Gly Leu Pro 
    3755                 3760                 3765 

Gly Thr  Ser Val Ala Trp Gly  Leu Trp Glu Gly Ala  Gly Met Gly 
    3770                 3775                 3780 

Ala Val  Leu Gly Glu Ala Asp  Val Leu Arg Met Ser  Arg Ser Gly 
    3785                 3790                 3795 

Val Leu  Gly Leu Ser Val Gly  Glu Gly Leu Gly Leu  Phe Asp Val 
    3800                 3805                 3810 

Ala Leu  Gly Glu Asp Val Ala  Ala Leu Val Pro Val  Arg Leu Asp 
    3815                 3820                 3825 

Leu Gly  Ala Leu Arg Ser Arg  Val Asp Gly Val Pro  Ala Val Phe 
    3830                 3835                 3840 

Arg Ser  Leu Val Arg Val Pro  Val Arg Arg Ser Val  Gly Val Gly 
    3845                 3850                 3855 

Val Ser  Gly Gly Gly Glu Val  Ser Leu Glu Arg Arg  Leu Ala Val 
    3860                 3865                 3870 

Leu Asp  Ala Gly Glu Arg Glu  Arg Val Leu Leu Glu  Leu Val Arg 
    3875                 3880                 3885 

Ser His  Val Ala Ala Val Leu  Gly Tyr Glu Gly Ala  Gly Ser Ile 
    3890                 3895                 3900 

Glu Pro  Gly Arg Ala Phe Ser  Asp Ile Gly Phe Asp  Ser Leu Ser 
    3905                 3910                 3915 

Ala Val  Glu Leu Arg Asn Arg  Leu Asn Gly Glu Thr  Gly Leu Arg 
    3920                 3925                 3930 

Leu Pro  Ala Thr Leu Ile Phe  Asp Tyr Pro Thr Pro  Gln Ala Leu 
    3935                 3940                 3945 

Ala Asp  Leu Ile Gln Glu Lys  Thr Leu Gly Leu Val  Asp Ala Ala 
    3950                 3955                 3960 

Ala Ala  Thr Val Ser Thr Thr  Val Ser Arg Thr Asp  Asp Glu Pro 
    3965                 3970                 3975 

Ile Ala  Ile Val Gly Met Gly  Cys Arg Tyr Pro Gly  Asp Val Arg 
    3980                 3985                 3990 

Thr Pro  Glu Glu Leu Trp Arg  Leu Val Ala Ser Gly  Thr Asp Ala 
    3995                 4000                 4005 

Val Ser  Leu Phe Pro Glu Asp  Arg Gly Trp Asn Val  Asp Ser Ile 
    4010                 4015                 4020 

Tyr Asp  Pro Thr Pro Gly Leu  Ser Gly Lys Thr Tyr  Thr Arg Glu 
    4025                 4030                 4035 

Gly Gly  Phe Leu His Asp Ala  Ala Glu Phe Asp Ala  Gly Phe Phe 
    4040                 4045                 4050 

Gly Ile  Ser Pro Arg Glu Ala  Leu Ala Met Asp Pro  Gln Gln Arg 
    4055                 4060                 4065 

Leu Leu  Leu Glu Thr Ser Trp  Glu Ala Met Glu Arg  Ala Gly Ile 
    4070                 4075                 4080 

Asp Pro  Asn Ser Leu Arg Gly  Thr Gln Thr Gly Val  Phe Ala Gly 
    4085                 4090                 4095 

Ile Met  Tyr His Asp Tyr Gly  Ser Arg Val Thr Gln  Pro Ser Glu 
    4100                 4105                 4110 

Glu Val  Glu Gly Tyr Leu Gly  Asn Gly Ser Ala Gly  Ser Ile Ala 
    4115                 4120                 4125 

Ser Gly  Arg Val Ser Tyr Thr  Phe Gly Phe Glu Gly  Pro Ala Val 
    4130                 4135                 4140 

Thr Val  Asp Thr Ala Cys Ser  Ser Ser Leu Val Ala  Leu His Trp 
    4145                 4150                 4155 

Ala Ala  Gln Ala Leu Arg Gln  Gly Glu Cys Ser Met  Ala Leu Ala 
    4160                 4165                 4170 

Gly Gly  Val Thr Val Met Ser  Thr Pro Glu Thr Phe  Val Asp Phe 
    4175                 4180                 4185 

Ser Leu  Gln Arg Gly Leu Ala  Thr Asn Gly Arg Cys  Lys Ala Phe 
    4190                 4195                 4200 

Ser Ser  Asp Ala Asp Gly Thr  Gly Trp Gly Glu Gly  Ala Gly Met 
    4205                 4210                 4215 

Leu Leu  Leu Glu Arg Leu Ser  Asp Ala Arg Lys Asn  Gly His Glu 
    4220                 4225                 4230 

Val Leu  Ala Val Ile Arg Gly  Ser Ala Leu Asn Gln  Asp Gly Ala 
    4235                 4240                 4245 

Ser Asn  Gly Leu Thr Ala Pro  Asn Gly Pro Ser Gln  Gln Arg Val 
    4250                 4255                 4260 

Ile Arg  Gln Ala Leu Ala Asn  Ala Gly Leu Ser Ala  Ala Glu Val 
    4265                 4270                 4275 

Asp Ala  Val Glu Ala His Gly  Thr Gly Thr Lys Leu  Gly Asp Pro 
    4280                 4285                 4290 

Ile Glu  Ala Gln Ala Leu Leu  Ala Thr Tyr Gly Gln  Glu Arg Asp 
    4295                 4300                 4305 

Gly Asp  Gln Pro Leu Leu Leu  Gly Ser Ile Lys Ser  Asn Val Gly 
    4310                 4315                 4320 

His Thr  Gln Ala Ala Ala Gly  Val Gly Gly Val Ile  Lys Met Val 
    4325                 4330                 4335 

Met Ala  Ile Arg Asn Gly Val  Leu Pro Lys Thr Leu  His Val Thr 
    4340                 4345                 4350 

Glu Pro  Ser Pro His Val Asp  Trp Ser Ala Gly Ala  Val Glu Leu 
    4355                 4360                 4365 

Leu Ala  Glu Ala Arg Glu Trp  Pro Glu Thr Gly Arg  Pro Arg Arg 
    4370                 4375                 4380 

Ala Gly  Val Ser Ser Phe Gly  Ile Ser Gly Thr Asn  Ala His Val 
    4385                 4390                 4395 

Ile Val  Glu Gln Ala Pro Thr  Asp Gln Pro Ala Pro  Leu Ser Glu 
    4400                 4405                 4410 

Pro Val  Gly Asp Val Pro Gly  Leu Pro Val Pro Trp  Ile Val Ser 
    4415                 4420                 4425 

Ala Lys  Ser Ala Glu Ala Leu  Arg Ala Gln Ala Gly  Arg Leu Gly 
    4430                 4435                 4440 

Ser Phe  Leu Gly Glu Thr Gly  Val Val Asp Val Pro  Ala Val Gly 
    4445                 4450                 4455 

Trp Ser  Leu Val Arg Gly Arg  Ser Val Phe Ala His  Arg Ala Val 
    4460                 4465                 4470 

Val Val  Gly Gly Glu Trp Asp  Glu Leu Leu Ala Gly  Val Ala Arg 
    4475                 4480                 4485 

Val Ala  Glu Gly Val Asp Asp  Ser Val Val Ser Gly  Val Ala Asp 
    4490                 4495                 4500 

Val Ser  Gly Arg Arg Val Phe  Val Phe Pro Gly Gln  Gly Ser Gln 
    4505                 4510                 4515 

Trp Val  Gly Met Ala Gln Gly  Leu Leu Asp Ser Ser  Val Val Phe 
    4520                 4525                 4530 

Thr Glu  Arg Met Thr Glu Cys  Ala Ala Ala Leu Asp  Pro Leu Val 
    4535                 4540                 4545 

Glu Trp  Ser Leu Leu Asp Val  Val Arg Gly Val Glu  Gly Ala Ala 
    4550                 4555                 4560 

Ser Leu  Glu Arg Val Asp Val  Val Gln Pro Val Leu  Trp Ala Val 
    4565                 4570                 4575 

Met Val  Ser Leu Ala Ser Val  Trp Arg Ser Val Gly  Val Val Pro 
    4580                 4585                 4590 

Asp Ala  Val Val Gly His Ser  Gln Gly Glu Ile Ala  Ala Ala Val 
    4595                 4600                 4605 

Val Gly  Gly Trp Leu Ser Leu  Val Asp Gly Ala Arg  Val Val Ala 
    4610                 4615                 4620 

Leu Arg  Ser Leu Ala Ile Arg  Glu Val Leu Ala Gly  Gly Gly Gly 
    4625                 4630                 4635 

Met Val  Ala Val Gln Ala Ala  Glu Asp Glu Val Ala  Gly Trp Leu 
    4640                 4645                 4650 

Glu Gly  Val Glu Gly Val Gly  Ile Ala Ala Val Asn  Gly Pro Arg 
    4655                 4660                 4665 

Ser Val  Val Ile Ser Gly Thr  Arg Ala Gly Leu Asp  Ala Cys Val 
    4670                 4675                 4680 

Glu Leu  Trp Ser Gly Arg Gly  Thr Trp Val Lys Arg  Val Pro Val 
    4685                 4690                 4695 

Asp Tyr  Ala Ser His Ser Ala  Glu Val Glu Arg Val  Arg Glu Arg 
    4700                 4705                 4710 

Val Leu  Ala Asp Leu Ala Ser  Val Thr Gly Leu Ser  Gly Ser Val 
    4715                 4720                 4725 

Pro Met  Leu Ser Thr Met Thr  Gly Asp Trp Ile Val  Glu Gly Gln 
    4730                 4735                 4740 

Val Gly  Ala Gly Tyr Trp Val  Glu Asn Leu Arg Arg  Pro Val Leu 
    4745                 4750                 4755 

Phe Ala  Asp Ala Thr Arg Arg  Leu Ala Ser Glu Gly  Phe Gly Ala 
    4760                 4765                 4770 

Phe Val  Glu Val Ser Ala His  Pro Val Leu Val Met  Gly Ile Glu 
    4775                 4780                 4785 

Glu Thr  Ile Glu Ala Leu Arg  Ser Gly Ala Ala Asp  Gly Ala Lys 
    4790                 4795                 4800 

Ser Gly  Ala Gly Glu Glu Ser  Ser Ser Ala Val Val  Ala Val Gly 
    4805                 4810                 4815 

Thr Leu  Arg Arg Gly Glu Gly  Gly Trp Asp Gln Phe  Leu Arg Ser 
    4820                 4825                 4830 

Leu Ala  Gly Leu Phe Val Arg  Gly Ala Val Ala Pro  Asp Trp Glu 
    4835                 4840                 4845 

Ser Leu  Leu Gly Gly Val Arg  Pro Arg Val Asp Leu  Pro Thr Tyr 
    4850                 4855                 4860 

Ala Phe  Gln Arg Glu Arg Leu  Trp Leu Asp Ala Gly  Val Val Ala 
    4865                 4870                 4875 

Gly Asp  Val Ser Gly Leu Gly  Gln Val Val Val Gly  His Pro Leu 
    4880                 4885                 4890 

Leu Gly  Ala Gly Val Gly Val  Ala Gly Glu Gly Gly  Gly Val Leu 
    4895                 4900                 4905 

Phe Thr  Gly Arg Leu Gly Leu  Gly Ser His Pro Trp  Leu Gly Asp 
    4910                 4915                 4920 

His Ala  Val Ser Gly Val Val  Leu Leu Pro Gly Ala  Ala Phe Val 
    4925                 4930                 4935 

Glu Leu  Val Val Arg Ala Gly  Asp Glu Val Gly Cys  Gly Arg Leu 
    4940                 4945                 4950 

Glu Glu  Leu Thr Leu Ala Ala  Pro Leu Val Val Pro  Glu Arg Gly 
    4955                 4960                 4965 

Ser Val  Arg Ile Gln Val Val  Val Gly Ala Gly Asp  Gly Ser Gly 
    4970                 4975                 4980 

Ala Arg  Ser Val Gly Val Trp  Ser Ser Val Gly Asp  Glu Gly Val 
    4985                 4990                 4995 

Gly Gly  Glu Trp Val Cys His  Ala Ser Gly Leu Leu  Thr Ala Asp 
    5000                 5005                 5010 

Val Gly  Val Ala Pro Val Leu  Gly Gly Val Trp Pro  Pro Val Gly 
    5015                 5020                 5025 

Gly Val  Ala Val Asp Val Ser  Gly Val Tyr Glu Gly  Leu Ala Leu 
    5030                 5035                 5040 

Glu Gly  Tyr Glu Tyr Gly Ser  Val Phe Arg Gly Leu  Arg Ser Val 
    5045                 5050                 5055 

Trp Arg  Arg Gly Asp Glu Val  Phe Ala Glu Val Ala  Leu Gly Glu 
    5060                 5065                 5070 

Gly Val  Gly Val Glu Gly Phe  Gly Leu His Pro Ala  Leu Leu Asp 
    5075                 5080                 5085 

Ala Ala  Leu Gln Ala Ala Gly  Phe Gly Ser Phe Val  Pro Glu Ser 
    5090                 5095                 5100 

Glu Ala  Gly Ser Glu Ala Gly  Ser Gly Gly Val Arg  Leu Pro Phe 
    5105                 5110                 5115 

Ser Trp  Ser Gly Val Ser Leu  Phe Ala Ser Gly Ala  Ser Val Gly 
    5120                 5125                 5130 

Arg Val  Arg Leu Trp Pro Val  Gly Gly Asp Gly Phe  Gly Val Glu 
    5135                 5140                 5145 

Leu Phe  Asp Gly Val Gly Met  Pro Val Ala Arg Val  Asp Ala Leu 
    5150                 5155                 5160 

Val Thr  Arg Glu Ile Ser Ala  Gly Gln Leu Gly Ala  Ala Ala Gly 
    5165                 5170                 5175 

Ala Gly  Ser Leu Val Gly Gly  Glu Ser Leu Phe Arg  Val Glu Trp 
    5180                 5185                 5190 

Ala Pro  Val Ser Gly Val Ala  Pro Ala Ser Ala Gly  Val Gly Gly 
    5195                 5200                 5205 

Cys Val  Val Val Gly Ala Gly  Ser Val Leu Ser Gly  Phe Gly Glu 
    5210                 5215                 5220 

Val Val  Pro Asp Leu Ala Ala  Val Ser Ala Gly Ser  Ala Asp Gly 
    5225                 5230                 5235 

Val Gly  Val Pro Gly Trp Val  Leu Val Asp Val Asp  Ala Trp Leu 
    5240                 5245                 5250 

Gly Ala  Asp Leu Ala Val Gly  Val Val Ser Gly Glu  Gly Val Pro 
    5255                 5260                 5265 

Val Val  Ala Arg Gly Val Val  Ala Arg Val Leu Gly  Leu Val Arg 
    5270                 5275                 5280 

Glu Trp  Leu Gly Asp Glu Arg  Trp Val Ser Ser Arg  Leu Val Trp 
    5285                 5290                 5295 

Val Thr  Arg Gly Ala Val Gly  Ala Arg Val Leu Asp  Glu Val Ser 
    5300                 5305                 5310 

Gly Val  Val Ser Ser Gly Leu  Trp Gly Leu Val Arg  Ala Ala Gln 
    5315                 5320                 5325 

Ser Glu  His Pro Asp Arg Phe  Ala Leu Leu Asp Leu  Asp Ser Ala 
    5330                 5335                 5340 

Thr Ala  Val Asp Ala Val Arg  Asp Gly Val Leu Gly  Leu Leu Ala 
    5345                 5350                 5355 

Ala Gly  Glu Pro Gln Leu Val  Val Arg Glu Gly Glu  Val Leu Ala 
    5360                 5365                 5370 

Ala Arg  Leu Thr Pro Ala His  Thr Thr Asp Glu Pro  Thr Gly Gln 
    5375                 5380                 5385 

Glu Phe  Gly Lys Ala Ala Thr  Gly Thr Val Leu Val  Thr Gly Gly 
    5390                 5395                 5400 

Thr Gly  Gly Leu Gly Ala Val  Val Ala Arg His Leu  Val Thr Glu 
    5405                 5410                 5415 

His Gly  Ala Gln Arg Leu Leu  Leu Thr Ser Arg Arg  Gly Ile Asn 
    5420                 5425                 5430 

Ala Pro  Gly Ala Ala Glu Leu  Val Ala Glu Leu Ala  Glu Leu Gly 
    5435                 5440                 5445 

Ala Arg  Ala Asp Val Ala Ala  Cys Asp Val Ser Asp  Arg Ala Ala 
    5450                 5455                 5460 

Leu Lys  Glu Leu Leu Ala Gly  Val Pro Gly Asp Ala  Pro Leu Thr 
    5465                 5470                 5475 

Ala Val  Val His Ala Ala Gly  Val Leu Asp Asp Gly  Val Ile Glu 
    5480                 5485                 5490 

Ser Met  Thr Ala Asp Arg Leu  Asp Ala Val Met Arg  Pro Lys Val 
    5495                 5500                 5505 

Asp Ala  Ala Trp His Leu His  Glu Leu Thr Ala Asp  Arg Glu Leu 
    5510                 5515                 5520 

Asp Ala  Phe Val Leu Phe Ser  Ser Ala Ala Gly Thr  Leu Asp Gly 
    5525                 5530                 5535 

Ala Gly  Gln Ser Asn Tyr Ala  Ala Ala Asn Val Phe  Leu Asp Ala 
    5540                 5545                 5550 

Leu Ala  Gln Tyr Arg Arg Gly  Gln Gly Leu Ala Gly  Leu Ser Leu 
    5555                 5560                 5565 

Ala Trp  Gly Leu Trp Gly Glu  Ser Thr Gly Met Val  Gly Ala Leu 
    5570                 5575                 5580 

Glu Gly  Ser Asp Leu Asp Arg  Ile Gly Arg Ser Gly  Val Arg Ala 
    5585                 5590                 5595 

Leu Ser  Ser Ala Glu Gly Leu  Ala Leu Phe Asp Ala  Ala Ala Val 
    5600                 5605                 5610 

Leu Gly  Glu Pro Ala Val Leu  Pro Val Ala Leu Asp  Leu Gly Val 
    5615                 5620                 5625 

Leu Arg  Thr Gln Pro Arg Asn  Gln Val Pro Ala Ile  Leu Arg Gly 
    5630                 5635                 5640 

Phe Ala  Ala Gly Pro Thr Arg  Arg Thr Ala Val Thr  Gly Gly Pro 
    5645                 5650                 5655 

Glu Thr  Asp Gln Glu Ala Leu  Thr Arg Arg Leu Ala  Ser Leu Ser 
    5660                 5665                 5670 

Pro Ala  Asp Arg Asp Arg Phe  Leu Leu Asp Leu Val  Arg Thr Gln 
    5675                 5680                 5685 

Val Ala  Gly Val Leu Gly Tyr  Ser Gly Pro Asp Ala  Ile Asp Pro 
    5690                 5695                 5700 

Gln Arg  Gly Phe Gln Glu Leu  Gly Val Asp Ser Leu  Ala Ala Val 
    5705                 5710                 5715 

Gln Ile  Arg Asn Arg Leu Gly  Ala Ala Thr Gly Val  Arg Pro Pro 
    5720                 5725                 5730 

Thr Thr  Leu Val Phe Asp Tyr  Pro Thr Pro Asp Ala  Val Ala Gly 
    5735                 5740                 5745 

Tyr Phe  Lys Glu His Leu Val  Ile Glu Glu Glu Asp  Ser Thr Ala 
    5750                 5755                 5760 

Glu Leu  Met Arg Glu Ile Ala  Arg Leu Glu Ala Ala  Val Thr Ser 
    5765                 5770                 5775 

Ala Ala  Ser Ser Ala Gly Gly  Ala Gly Leu Ala Pro  Ala Val Asp 
    5780                 5785                 5790 

Arg Leu  Arg Ala Met Ala Ala  Lys Leu Ala Asp Ala  Asp Ala Gln 
    5795                 5800                 5805 

Arg Ala  Asp Glu Asp Asp Pro  Gly Leu Glu Ser Ala  Thr Ala Asp 
    5810                 5815                 5820 

Glu Leu  Phe Asp Ile Leu Asp  Gly Glu Leu Ser Thr  Asp 
    5825                 5830                 5835 

 
           
             21  
             23  
             DNA  
             Artificial Sequence  
             
               Primer for PCR (46DH-1)  
             
           
            21 

acsggycsbg ccgchttcat cgg                                             23 

 
           
             22  
             24  
             DNA  
             Artificial Sequence  
             
               Primer for PCR (46DH-2)  
             
           
            22 

grwrctgrtr sggccgtagt tgtt                                            24 

 
           
             23  
             22  
             DNA  
             Artificial Sequence  
             
               Primer for PCR (23DH-1)  
             
           
            23 

aggccacccg sagcaactac ac                                              22 

 
           
             24  
             21  
             DNA  
             Artificial Sequence  
             
               Primer for PCR (23DH-2)  
             
           
            24 

gaascgsccg ccctcctcsg a                                               21 

 
           
             25  
             26  
             DNA  
             Artificial Sequence  
             
               Primer for PCR (vinC-Nterm)  
             
           
            25 

aaggtaccat atgcgcgtcc tgatga                                          26 

 
           
             26  
             26  
             DNA  
             Artificial Sequence  
             
               Primer for PCR (vinC-Cterm)  
             
           
            26 

cccggatccg ctgggcggag tgctac                                          26